data_8JE6
# 
_entry.id   8JE6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8JE6         pdb_00008je6 10.2210/pdb8je6/pdb 
WWPDB D_1300037707 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-27 
# 
_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                        8JE6 
_pdbx_database_status.recvd_initial_deposition_date   2023-05-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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                 3 
_pdbx_contact_author.email              amit.icgeb@gmail.com 
_pdbx_contact_author.name_first         Amit 
_pdbx_contact_author.name_last          Sharma 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3305-0034 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Goswami, R.'       1 ?                   
'Manickam, Y.'      2 0000-0002-2119-062X 
'Gupta, S.'         3 ?                   
'Chhibber-Goel, J.' 4 0000-0003-4654-5463 
'Harlos, K.'        5 ?                   
'Sharma, A.'        6 0000-0002-3305-0034 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Targeting Prolyl-tRNA synthetase of Anopheles culicifacies for the development of new larvicide' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Goswami, R.'       1 ?                   
primary 'Chhibber-Goel, J.' 2 0000-0003-4654-5463 
primary 'Manickam, Y.'      3 0000-0002-2119-062X 
primary 'Gupta, S.'         4 ?                   
primary 'Harlos, K.'        5 ?                   
primary 'Laleu, B.'         6 ?                   
primary 'Sharma, A.'        7 0000-0002-3305-0034 
# 
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 'PROLYL-TRNA SYNTHETASE'                                                                   58101.004 2 ? ? ? ? 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'                                              506.196   2 ? ? ? ? 
3 non-polymer syn '7-bromo-6-chloro-3-{3-[(2R,3S)-3-hydroxypiperidin-2-yl]-2-oxopropyl}quinazolin-4(3H)-one' 414.681   2 ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                                                            24.305    2 ? ? ? ? 
5 non-polymer syn 'ZINC ION'                                                                                 65.409    2 ? ? ? ? 
# 
_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       
;MTRLGLEATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRHWSFAIWKAIRNWFDAEITRLGVKECYFPIFVSRAALERE
KTHIADFAPEVAWVTKSGDSELAEPIAVRPTSETVMYPAYAKWIQSYRDLPIRLNQWNNVVRWEFKHPQPFLRTREFLWQ
EGHTAFATQKEADEEVLTILDLYAKVYTDLLAIPVVKGRKTEKEKFAGGDYTTTVEAYISASGRAIQGATSHHLGQNFSR
MFDIVYEHPETKEKEYVFQNSWGITTRTIGVMIMVHADNQGLVLPPRVACIQVVIVPCGITATTTDDERRRLYESCRELE
QTFVKAGIRCEGDYRDNYSPGWKYNHWELKGVPVRIELGFKDLQNDQFVAVRRDNGAKQTIKRAQATVEMPKLLETIHTS
MYERAERDLQSHTKLTKQWAEFLQFLETKNIIMAPFCGEISCEDRIKAESARDDAEAEAGAPAMGAKSLCIPFEQPAKID
PKVDKCVHPACGRVAKFYTLFGRSY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTRLGLEATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRHWSFAIWKAIRNWFDAEITRLGVKECYFPIFVSRAALERE
KTHIADFAPEVAWVTKSGDSELAEPIAVRPTSETVMYPAYAKWIQSYRDLPIRLNQWNNVVRWEFKHPQPFLRTREFLWQ
EGHTAFATQKEADEEVLTILDLYAKVYTDLLAIPVVKGRKTEKEKFAGGDYTTTVEAYISASGRAIQGATSHHLGQNFSR
MFDIVYEHPETKEKEYVFQNSWGITTRTIGVMIMVHADNQGLVLPPRVACIQVVIVPCGITATTTDDERRRLYESCRELE
QTFVKAGIRCEGDYRDNYSPGWKYNHWELKGVPVRIELGFKDLQNDQFVAVRRDNGAKQTIKRAQATVEMPKLLETIHTS
MYERAERDLQSHTKLTKQWAEFLQFLETKNIIMAPFCGEISCEDRIKAESARDDAEAEAGAPAMGAKSLCIPFEQPAKID
PKVDKCVHPACGRVAKFYTLFGRSY
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'                                              ANP 
3 '7-bromo-6-chloro-3-{3-[(2R,3S)-3-hydroxypiperidin-2-yl]-2-oxopropyl}quinazolin-4(3H)-one' HFG 
4 'MAGNESIUM ION'                                                                            MG  
5 'ZINC ION'                                                                                 ZN  
# 
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   THR n 
1 3   ARG n 
1 4   LEU n 
1 5   GLY n 
1 6   LEU n 
1 7   GLU n 
1 8   ALA n 
1 9   THR n 
1 10  LYS n 
1 11  GLU n 
1 12  ASP n 
1 13  ASN n 
1 14  LEU n 
1 15  PRO n 
1 16  ASP n 
1 17  TRP n 
1 18  TYR n 
1 19  SER n 
1 20  GLN n 
1 21  VAL n 
1 22  ILE n 
1 23  THR n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  MET n 
1 28  ILE n 
1 29  GLU n 
1 30  TYR n 
1 31  TYR n 
1 32  ASP n 
1 33  VAL n 
1 34  SER n 
1 35  GLY n 
1 36  CYS n 
1 37  TYR n 
1 38  ILE n 
1 39  LEU n 
1 40  ARG n 
1 41  HIS n 
1 42  TRP n 
1 43  SER n 
1 44  PHE n 
1 45  ALA n 
1 46  ILE n 
1 47  TRP n 
1 48  LYS n 
1 49  ALA n 
1 50  ILE n 
1 51  ARG n 
1 52  ASN n 
1 53  TRP n 
1 54  PHE n 
1 55  ASP n 
1 56  ALA n 
1 57  GLU n 
1 58  ILE n 
1 59  THR n 
1 60  ARG n 
1 61  LEU n 
1 62  GLY n 
1 63  VAL n 
1 64  LYS n 
1 65  GLU n 
1 66  CYS n 
1 67  TYR n 
1 68  PHE n 
1 69  PRO n 
1 70  ILE n 
1 71  PHE n 
1 72  VAL n 
1 73  SER n 
1 74  ARG n 
1 75  ALA n 
1 76  ALA n 
1 77  LEU n 
1 78  GLU n 
1 79  ARG n 
1 80  GLU n 
1 81  LYS n 
1 82  THR n 
1 83  HIS n 
1 84  ILE n 
1 85  ALA n 
1 86  ASP n 
1 87  PHE n 
1 88  ALA n 
1 89  PRO n 
1 90  GLU n 
1 91  VAL n 
1 92  ALA n 
1 93  TRP n 
1 94  VAL n 
1 95  THR n 
1 96  LYS n 
1 97  SER n 
1 98  GLY n 
1 99  ASP n 
1 100 SER n 
1 101 GLU n 
1 102 LEU n 
1 103 ALA n 
1 104 GLU n 
1 105 PRO n 
1 106 ILE n 
1 107 ALA n 
1 108 VAL n 
1 109 ARG n 
1 110 PRO n 
1 111 THR n 
1 112 SER n 
1 113 GLU n 
1 114 THR n 
1 115 VAL n 
1 116 MET n 
1 117 TYR n 
1 118 PRO n 
1 119 ALA n 
1 120 TYR n 
1 121 ALA n 
1 122 LYS n 
1 123 TRP n 
1 124 ILE n 
1 125 GLN n 
1 126 SER n 
1 127 TYR n 
1 128 ARG n 
1 129 ASP n 
1 130 LEU n 
1 131 PRO n 
1 132 ILE n 
1 133 ARG n 
1 134 LEU n 
1 135 ASN n 
1 136 GLN n 
1 137 TRP n 
1 138 ASN n 
1 139 ASN n 
1 140 VAL n 
1 141 VAL n 
1 142 ARG n 
1 143 TRP n 
1 144 GLU n 
1 145 PHE n 
1 146 LYS n 
1 147 HIS n 
1 148 PRO n 
1 149 GLN n 
1 150 PRO n 
1 151 PHE n 
1 152 LEU n 
1 153 ARG n 
1 154 THR n 
1 155 ARG n 
1 156 GLU n 
1 157 PHE n 
1 158 LEU n 
1 159 TRP n 
1 160 GLN n 
1 161 GLU n 
1 162 GLY n 
1 163 HIS n 
1 164 THR n 
1 165 ALA n 
1 166 PHE n 
1 167 ALA n 
1 168 THR n 
1 169 GLN n 
1 170 LYS n 
1 171 GLU n 
1 172 ALA n 
1 173 ASP n 
1 174 GLU n 
1 175 GLU n 
1 176 VAL n 
1 177 LEU n 
1 178 THR n 
1 179 ILE n 
1 180 LEU n 
1 181 ASP n 
1 182 LEU n 
1 183 TYR n 
1 184 ALA n 
1 185 LYS n 
1 186 VAL n 
1 187 TYR n 
1 188 THR n 
1 189 ASP n 
1 190 LEU n 
1 191 LEU n 
1 192 ALA n 
1 193 ILE n 
1 194 PRO n 
1 195 VAL n 
1 196 VAL n 
1 197 LYS n 
1 198 GLY n 
1 199 ARG n 
1 200 LYS n 
1 201 THR n 
1 202 GLU n 
1 203 LYS n 
1 204 GLU n 
1 205 LYS n 
1 206 PHE n 
1 207 ALA n 
1 208 GLY n 
1 209 GLY n 
1 210 ASP n 
1 211 TYR n 
1 212 THR n 
1 213 THR n 
1 214 THR n 
1 215 VAL n 
1 216 GLU n 
1 217 ALA n 
1 218 TYR n 
1 219 ILE n 
1 220 SER n 
1 221 ALA n 
1 222 SER n 
1 223 GLY n 
1 224 ARG n 
1 225 ALA n 
1 226 ILE n 
1 227 GLN n 
1 228 GLY n 
1 229 ALA n 
1 230 THR n 
1 231 SER n 
1 232 HIS n 
1 233 HIS n 
1 234 LEU n 
1 235 GLY n 
1 236 GLN n 
1 237 ASN n 
1 238 PHE n 
1 239 SER n 
1 240 ARG n 
1 241 MET n 
1 242 PHE n 
1 243 ASP n 
1 244 ILE n 
1 245 VAL n 
1 246 TYR n 
1 247 GLU n 
1 248 HIS n 
1 249 PRO n 
1 250 GLU n 
1 251 THR n 
1 252 LYS n 
1 253 GLU n 
1 254 LYS n 
1 255 GLU n 
1 256 TYR n 
1 257 VAL n 
1 258 PHE n 
1 259 GLN n 
1 260 ASN n 
1 261 SER n 
1 262 TRP n 
1 263 GLY n 
1 264 ILE n 
1 265 THR n 
1 266 THR n 
1 267 ARG n 
1 268 THR n 
1 269 ILE n 
1 270 GLY n 
1 271 VAL n 
1 272 MET n 
1 273 ILE n 
1 274 MET n 
1 275 VAL n 
1 276 HIS n 
1 277 ALA n 
1 278 ASP n 
1 279 ASN n 
1 280 GLN n 
1 281 GLY n 
1 282 LEU n 
1 283 VAL n 
1 284 LEU n 
1 285 PRO n 
1 286 PRO n 
1 287 ARG n 
1 288 VAL n 
1 289 ALA n 
1 290 CYS n 
1 291 ILE n 
1 292 GLN n 
1 293 VAL n 
1 294 VAL n 
1 295 ILE n 
1 296 VAL n 
1 297 PRO n 
1 298 CYS n 
1 299 GLY n 
1 300 ILE n 
1 301 THR n 
1 302 ALA n 
1 303 THR n 
1 304 THR n 
1 305 THR n 
1 306 ASP n 
1 307 ASP n 
1 308 GLU n 
1 309 ARG n 
1 310 ARG n 
1 311 ARG n 
1 312 LEU n 
1 313 TYR n 
1 314 GLU n 
1 315 SER n 
1 316 CYS n 
1 317 ARG n 
1 318 GLU n 
1 319 LEU n 
1 320 GLU n 
1 321 GLN n 
1 322 THR n 
1 323 PHE n 
1 324 VAL n 
1 325 LYS n 
1 326 ALA n 
1 327 GLY n 
1 328 ILE n 
1 329 ARG n 
1 330 CYS n 
1 331 GLU n 
1 332 GLY n 
1 333 ASP n 
1 334 TYR n 
1 335 ARG n 
1 336 ASP n 
1 337 ASN n 
1 338 TYR n 
1 339 SER n 
1 340 PRO n 
1 341 GLY n 
1 342 TRP n 
1 343 LYS n 
1 344 TYR n 
1 345 ASN n 
1 346 HIS n 
1 347 TRP n 
1 348 GLU n 
1 349 LEU n 
1 350 LYS n 
1 351 GLY n 
1 352 VAL n 
1 353 PRO n 
1 354 VAL n 
1 355 ARG n 
1 356 ILE n 
1 357 GLU n 
1 358 LEU n 
1 359 GLY n 
1 360 PHE n 
1 361 LYS n 
1 362 ASP n 
1 363 LEU n 
1 364 GLN n 
1 365 ASN n 
1 366 ASP n 
1 367 GLN n 
1 368 PHE n 
1 369 VAL n 
1 370 ALA n 
1 371 VAL n 
1 372 ARG n 
1 373 ARG n 
1 374 ASP n 
1 375 ASN n 
1 376 GLY n 
1 377 ALA n 
1 378 LYS n 
1 379 GLN n 
1 380 THR n 
1 381 ILE n 
1 382 LYS n 
1 383 ARG n 
1 384 ALA n 
1 385 GLN n 
1 386 ALA n 
1 387 THR n 
1 388 VAL n 
1 389 GLU n 
1 390 MET n 
1 391 PRO n 
1 392 LYS n 
1 393 LEU n 
1 394 LEU n 
1 395 GLU n 
1 396 THR n 
1 397 ILE n 
1 398 HIS n 
1 399 THR n 
1 400 SER n 
1 401 MET n 
1 402 TYR n 
1 403 GLU n 
1 404 ARG n 
1 405 ALA n 
1 406 GLU n 
1 407 ARG n 
1 408 ASP n 
1 409 LEU n 
1 410 GLN n 
1 411 SER n 
1 412 HIS n 
1 413 THR n 
1 414 LYS n 
1 415 LEU n 
1 416 THR n 
1 417 LYS n 
1 418 GLN n 
1 419 TRP n 
1 420 ALA n 
1 421 GLU n 
1 422 PHE n 
1 423 LEU n 
1 424 GLN n 
1 425 PHE n 
1 426 LEU n 
1 427 GLU n 
1 428 THR n 
1 429 LYS n 
1 430 ASN n 
1 431 ILE n 
1 432 ILE n 
1 433 MET n 
1 434 ALA n 
1 435 PRO n 
1 436 PHE n 
1 437 CYS n 
1 438 GLY n 
1 439 GLU n 
1 440 ILE n 
1 441 SER n 
1 442 CYS n 
1 443 GLU n 
1 444 ASP n 
1 445 ARG n 
1 446 ILE n 
1 447 LYS n 
1 448 ALA n 
1 449 GLU n 
1 450 SER n 
1 451 ALA n 
1 452 ARG n 
1 453 ASP n 
1 454 ASP n 
1 455 ALA n 
1 456 GLU n 
1 457 ALA n 
1 458 GLU n 
1 459 ALA n 
1 460 GLY n 
1 461 ALA n 
1 462 PRO n 
1 463 ALA n 
1 464 MET n 
1 465 GLY n 
1 466 ALA n 
1 467 LYS n 
1 468 SER n 
1 469 LEU n 
1 470 CYS n 
1 471 ILE n 
1 472 PRO n 
1 473 PHE n 
1 474 GLU n 
1 475 GLN n 
1 476 PRO n 
1 477 ALA n 
1 478 LYS n 
1 479 ILE n 
1 480 ASP n 
1 481 PRO n 
1 482 LYS n 
1 483 VAL n 
1 484 ASP n 
1 485 LYS n 
1 486 CYS n 
1 487 VAL n 
1 488 HIS n 
1 489 PRO n 
1 490 ALA n 
1 491 CYS n 
1 492 GLY n 
1 493 ARG n 
1 494 VAL n 
1 495 ALA n 
1 496 LYS n 
1 497 PHE n 
1 498 TYR n 
1 499 THR n 
1 500 LEU n 
1 501 PHE n 
1 502 GLY n 
1 503 ARG n 
1 504 SER n 
1 505 TYR 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                   505 
_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      'Anopheles culicifacies' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     139723 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pETM11 
_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  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'                                              ?            
'C10 H17 N6 O12 P3'   506.196 
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  
HFG non-polymer         . '7-bromo-6-chloro-3-{3-[(2R,3S)-3-hydroxypiperidin-2-yl]-2-oxopropyl}quinazolin-4(3H)-one' Halofuginone 
'C16 H17 Br Cl N3 O3' 414.681 
HIS 'L-peptide linking' y HISTIDINE                                                                                  ?            
'C6 H10 N3 O2 1'      156.162 
ILE 'L-peptide linking' y ISOLEUCINE                                                                                 ?            
'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                    ?            
'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                                                     ?            
'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                                                 ?            
'C5 H11 N O2 S'       149.211 
MG  non-polymer         . 'MAGNESIUM ION'                                                                            ?            
'Mg 2'                24.305  
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 
ZN  non-polymer         . 'ZINC ION'                                                                                 ?            
'Zn 2'                65.409  
# 
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   1218 ?    ?   ?   A . n 
A 1 2   THR 2   1219 ?    ?   ?   A . n 
A 1 3   ARG 3   1220 ?    ?   ?   A . n 
A 1 4   LEU 4   1221 ?    ?   ?   A . n 
A 1 5   GLY 5   1222 ?    ?   ?   A . n 
A 1 6   LEU 6   1223 1223 LEU LEU A . n 
A 1 7   GLU 7   1224 1224 GLU GLU A . n 
A 1 8   ALA 8   1225 1225 ALA ALA A . n 
A 1 9   THR 9   1226 1226 THR THR A . n 
A 1 10  LYS 10  1227 1227 LYS LYS A . n 
A 1 11  GLU 11  1228 1228 GLU GLU A . n 
A 1 12  ASP 12  1229 1229 ASP ASP A . n 
A 1 13  ASN 13  1230 1230 ASN ASN A . n 
A 1 14  LEU 14  1231 1231 LEU LEU A . n 
A 1 15  PRO 15  1232 1232 PRO PRO A . n 
A 1 16  ASP 16  1233 1233 ASP ASP A . n 
A 1 17  TRP 17  1234 1234 TRP TRP A . n 
A 1 18  TYR 18  1235 1235 TYR TYR A . n 
A 1 19  SER 19  1236 1236 SER SER A . n 
A 1 20  GLN 20  1237 1237 GLN GLN A . n 
A 1 21  VAL 21  1238 1238 VAL VAL A . n 
A 1 22  ILE 22  1239 1239 ILE ILE A . n 
A 1 23  THR 23  1240 1240 THR THR A . n 
A 1 24  LYS 24  1241 1241 LYS LYS A . n 
A 1 25  GLY 25  1242 1242 GLY GLY A . n 
A 1 26  GLU 26  1243 1243 GLU GLU A . n 
A 1 27  MET 27  1244 1244 MET MET A . n 
A 1 28  ILE 28  1245 1245 ILE ILE A . n 
A 1 29  GLU 29  1246 1246 GLU GLU A . n 
A 1 30  TYR 30  1247 1247 TYR TYR A . n 
A 1 31  TYR 31  1248 1248 TYR TYR A . n 
A 1 32  ASP 32  1249 1249 ASP ASP A . n 
A 1 33  VAL 33  1250 1250 VAL VAL A . n 
A 1 34  SER 34  1251 1251 SER SER A . n 
A 1 35  GLY 35  1252 1252 GLY GLY A . n 
A 1 36  CYS 36  1253 1253 CYS CYS A . n 
A 1 37  TYR 37  1254 1254 TYR TYR A . n 
A 1 38  ILE 38  1255 1255 ILE ILE A . n 
A 1 39  LEU 39  1256 1256 LEU LEU A . n 
A 1 40  ARG 40  1257 1257 ARG ARG A . n 
A 1 41  HIS 41  1258 1258 HIS HIS A . n 
A 1 42  TRP 42  1259 1259 TRP TRP A . n 
A 1 43  SER 43  1260 1260 SER SER A . n 
A 1 44  PHE 44  1261 1261 PHE PHE A . n 
A 1 45  ALA 45  1262 1262 ALA ALA A . n 
A 1 46  ILE 46  1263 1263 ILE ILE A . n 
A 1 47  TRP 47  1264 1264 TRP TRP A . n 
A 1 48  LYS 48  1265 1265 LYS LYS A . n 
A 1 49  ALA 49  1266 1266 ALA ALA A . n 
A 1 50  ILE 50  1267 1267 ILE ILE A . n 
A 1 51  ARG 51  1268 1268 ARG ARG A . n 
A 1 52  ASN 52  1269 1269 ASN ASN A . n 
A 1 53  TRP 53  1270 1270 TRP TRP A . n 
A 1 54  PHE 54  1271 1271 PHE PHE A . n 
A 1 55  ASP 55  1272 1272 ASP ASP A . n 
A 1 56  ALA 56  1273 1273 ALA ALA A . n 
A 1 57  GLU 57  1274 1274 GLU GLU A . n 
A 1 58  ILE 58  1275 1275 ILE ILE A . n 
A 1 59  THR 59  1276 1276 THR THR A . n 
A 1 60  ARG 60  1277 1277 ARG ARG A . n 
A 1 61  LEU 61  1278 1278 LEU LEU A . n 
A 1 62  GLY 62  1279 1279 GLY GLY A . n 
A 1 63  VAL 63  1280 1280 VAL VAL A . n 
A 1 64  LYS 64  1281 1281 LYS LYS A . n 
A 1 65  GLU 65  1282 1282 GLU GLU A . n 
A 1 66  CYS 66  1283 1283 CYS CYS A . n 
A 1 67  TYR 67  1284 1284 TYR TYR A . n 
A 1 68  PHE 68  1285 1285 PHE PHE A . n 
A 1 69  PRO 69  1286 1286 PRO PRO A . n 
A 1 70  ILE 70  1287 1287 ILE ILE A . n 
A 1 71  PHE 71  1288 1288 PHE PHE A . n 
A 1 72  VAL 72  1289 1289 VAL VAL A . n 
A 1 73  SER 73  1290 1290 SER SER A . n 
A 1 74  ARG 74  1291 1291 ARG ARG A . n 
A 1 75  ALA 75  1292 1292 ALA ALA A . n 
A 1 76  ALA 76  1293 1293 ALA ALA A . n 
A 1 77  LEU 77  1294 1294 LEU LEU A . n 
A 1 78  GLU 78  1295 1295 GLU GLU A . n 
A 1 79  ARG 79  1296 1296 ARG ARG A . n 
A 1 80  GLU 80  1297 ?    ?   ?   A . n 
A 1 81  LYS 81  1298 ?    ?   ?   A . n 
A 1 82  THR 82  1299 ?    ?   ?   A . n 
A 1 83  HIS 83  1300 ?    ?   ?   A . n 
A 1 84  ILE 84  1301 ?    ?   ?   A . n 
A 1 85  ALA 85  1302 ?    ?   ?   A . n 
A 1 86  ASP 86  1303 1303 ASP ASP A . n 
A 1 87  PHE 87  1304 1304 PHE PHE A . n 
A 1 88  ALA 88  1305 1305 ALA ALA A . n 
A 1 89  PRO 89  1306 1306 PRO PRO A . n 
A 1 90  GLU 90  1307 1307 GLU GLU A . n 
A 1 91  VAL 91  1308 1308 VAL VAL A . n 
A 1 92  ALA 92  1309 1309 ALA ALA A . n 
A 1 93  TRP 93  1310 1310 TRP TRP A . n 
A 1 94  VAL 94  1311 1311 VAL VAL A . n 
A 1 95  THR 95  1312 1312 THR THR A . n 
A 1 96  LYS 96  1313 1313 LYS LYS A . n 
A 1 97  SER 97  1314 1314 SER SER A . n 
A 1 98  GLY 98  1315 1315 GLY GLY A . n 
A 1 99  ASP 99  1316 1316 ASP ASP A . n 
A 1 100 SER 100 1317 1317 SER SER A . n 
A 1 101 GLU 101 1318 1318 GLU GLU A . n 
A 1 102 LEU 102 1319 1319 LEU LEU A . n 
A 1 103 ALA 103 1320 1320 ALA ALA A . n 
A 1 104 GLU 104 1321 1321 GLU GLU A . n 
A 1 105 PRO 105 1322 1322 PRO PRO A . n 
A 1 106 ILE 106 1323 1323 ILE ILE A . n 
A 1 107 ALA 107 1324 1324 ALA ALA A . n 
A 1 108 VAL 108 1325 1325 VAL VAL A . n 
A 1 109 ARG 109 1326 1326 ARG ARG A . n 
A 1 110 PRO 110 1327 1327 PRO PRO A . n 
A 1 111 THR 111 1328 1328 THR THR A . n 
A 1 112 SER 112 1329 1329 SER SER A . n 
A 1 113 GLU 113 1330 1330 GLU GLU A . n 
A 1 114 THR 114 1331 1331 THR THR A . n 
A 1 115 VAL 115 1332 1332 VAL VAL A . n 
A 1 116 MET 116 1333 1333 MET MET A . n 
A 1 117 TYR 117 1334 1334 TYR TYR A . n 
A 1 118 PRO 118 1335 1335 PRO PRO A . n 
A 1 119 ALA 119 1336 1336 ALA ALA A . n 
A 1 120 TYR 120 1337 1337 TYR TYR A . n 
A 1 121 ALA 121 1338 1338 ALA ALA A . n 
A 1 122 LYS 122 1339 1339 LYS LYS A . n 
A 1 123 TRP 123 1340 1340 TRP TRP A . n 
A 1 124 ILE 124 1341 1341 ILE ILE A . n 
A 1 125 GLN 125 1342 1342 GLN GLN A . n 
A 1 126 SER 126 1343 1343 SER SER A . n 
A 1 127 TYR 127 1344 1344 TYR TYR A . n 
A 1 128 ARG 128 1345 1345 ARG ARG A . n 
A 1 129 ASP 129 1346 1346 ASP ASP A . n 
A 1 130 LEU 130 1347 1347 LEU LEU A . n 
A 1 131 PRO 131 1348 1348 PRO PRO A . n 
A 1 132 ILE 132 1349 1349 ILE ILE A . n 
A 1 133 ARG 133 1350 1350 ARG ARG A . n 
A 1 134 LEU 134 1351 1351 LEU LEU A . n 
A 1 135 ASN 135 1352 1352 ASN ASN A . n 
A 1 136 GLN 136 1353 1353 GLN GLN A . n 
A 1 137 TRP 137 1354 1354 TRP TRP A . n 
A 1 138 ASN 138 1355 1355 ASN ASN A . n 
A 1 139 ASN 139 1356 1356 ASN ASN A . n 
A 1 140 VAL 140 1357 1357 VAL VAL A . n 
A 1 141 VAL 141 1358 1358 VAL VAL A . n 
A 1 142 ARG 142 1359 1359 ARG ARG A . n 
A 1 143 TRP 143 1360 1360 TRP TRP A . n 
A 1 144 GLU 144 1361 1361 GLU GLU A . n 
A 1 145 PHE 145 1362 1362 PHE PHE A . n 
A 1 146 LYS 146 1363 1363 LYS LYS A . n 
A 1 147 HIS 147 1364 1364 HIS HIS A . n 
A 1 148 PRO 148 1365 1365 PRO PRO A . n 
A 1 149 GLN 149 1366 1366 GLN GLN A . n 
A 1 150 PRO 150 1367 1367 PRO PRO A . n 
A 1 151 PHE 151 1368 1368 PHE PHE A . n 
A 1 152 LEU 152 1369 1369 LEU LEU A . n 
A 1 153 ARG 153 1370 1370 ARG ARG A . n 
A 1 154 THR 154 1371 1371 THR THR A . n 
A 1 155 ARG 155 1372 1372 ARG ARG A . n 
A 1 156 GLU 156 1373 1373 GLU GLU A . n 
A 1 157 PHE 157 1374 1374 PHE PHE A . n 
A 1 158 LEU 158 1375 1375 LEU LEU A . n 
A 1 159 TRP 159 1376 1376 TRP TRP A . n 
A 1 160 GLN 160 1377 1377 GLN GLN A . n 
A 1 161 GLU 161 1378 1378 GLU GLU A . n 
A 1 162 GLY 162 1379 1379 GLY GLY A . n 
A 1 163 HIS 163 1380 1380 HIS HIS A . n 
A 1 164 THR 164 1381 1381 THR THR A . n 
A 1 165 ALA 165 1382 1382 ALA ALA A . n 
A 1 166 PHE 166 1383 1383 PHE PHE A . n 
A 1 167 ALA 167 1384 1384 ALA ALA A . n 
A 1 168 THR 168 1385 1385 THR THR A . n 
A 1 169 GLN 169 1386 1386 GLN GLN A . n 
A 1 170 LYS 170 1387 1387 LYS LYS A . n 
A 1 171 GLU 171 1388 1388 GLU GLU A . n 
A 1 172 ALA 172 1389 1389 ALA ALA A . n 
A 1 173 ASP 173 1390 1390 ASP ASP A . n 
A 1 174 GLU 174 1391 1391 GLU GLU A . n 
A 1 175 GLU 175 1392 1392 GLU GLU A . n 
A 1 176 VAL 176 1393 1393 VAL VAL A . n 
A 1 177 LEU 177 1394 1394 LEU LEU A . n 
A 1 178 THR 178 1395 1395 THR THR A . n 
A 1 179 ILE 179 1396 1396 ILE ILE A . n 
A 1 180 LEU 180 1397 1397 LEU LEU A . n 
A 1 181 ASP 181 1398 1398 ASP ASP A . n 
A 1 182 LEU 182 1399 1399 LEU LEU A . n 
A 1 183 TYR 183 1400 1400 TYR TYR A . n 
A 1 184 ALA 184 1401 1401 ALA ALA A . n 
A 1 185 LYS 185 1402 1402 LYS LYS A . n 
A 1 186 VAL 186 1403 1403 VAL VAL A . n 
A 1 187 TYR 187 1404 1404 TYR TYR A . n 
A 1 188 THR 188 1405 1405 THR THR A . n 
A 1 189 ASP 189 1406 1406 ASP ASP A . n 
A 1 190 LEU 190 1407 1407 LEU LEU A . n 
A 1 191 LEU 191 1408 1408 LEU LEU A . n 
A 1 192 ALA 192 1409 1409 ALA ALA A . n 
A 1 193 ILE 193 1410 1410 ILE ILE A . n 
A 1 194 PRO 194 1411 1411 PRO PRO A . n 
A 1 195 VAL 195 1412 1412 VAL VAL A . n 
A 1 196 VAL 196 1413 1413 VAL VAL A . n 
A 1 197 LYS 197 1414 1414 LYS LYS A . n 
A 1 198 GLY 198 1415 1415 GLY GLY A . n 
A 1 199 ARG 199 1416 1416 ARG ARG A . n 
A 1 200 LYS 200 1417 1417 LYS LYS A . n 
A 1 201 THR 201 1418 1418 THR THR A . n 
A 1 202 GLU 202 1419 1419 GLU GLU A . n 
A 1 203 LYS 203 1420 1420 LYS LYS A . n 
A 1 204 GLU 204 1421 1421 GLU GLU A . n 
A 1 205 LYS 205 1422 1422 LYS LYS A . n 
A 1 206 PHE 206 1423 1423 PHE PHE A . n 
A 1 207 ALA 207 1424 1424 ALA ALA A . n 
A 1 208 GLY 208 1425 1425 GLY GLY A . n 
A 1 209 GLY 209 1426 1426 GLY GLY A . n 
A 1 210 ASP 210 1427 1427 ASP ASP A . n 
A 1 211 TYR 211 1428 1428 TYR TYR A . n 
A 1 212 THR 212 1429 1429 THR THR A . n 
A 1 213 THR 213 1430 1430 THR THR A . n 
A 1 214 THR 214 1431 1431 THR THR A . n 
A 1 215 VAL 215 1432 1432 VAL VAL A . n 
A 1 216 GLU 216 1433 1433 GLU GLU A . n 
A 1 217 ALA 217 1434 1434 ALA ALA A . n 
A 1 218 TYR 218 1435 1435 TYR TYR A . n 
A 1 219 ILE 219 1436 1436 ILE ILE A . n 
A 1 220 SER 220 1437 1437 SER SER A . n 
A 1 221 ALA 221 1438 1438 ALA ALA A . n 
A 1 222 SER 222 1439 1439 SER SER A . n 
A 1 223 GLY 223 1440 1440 GLY GLY A . n 
A 1 224 ARG 224 1441 1441 ARG ARG A . n 
A 1 225 ALA 225 1442 1442 ALA ALA A . n 
A 1 226 ILE 226 1443 1443 ILE ILE A . n 
A 1 227 GLN 227 1444 1444 GLN GLN A . n 
A 1 228 GLY 228 1445 1445 GLY GLY A . n 
A 1 229 ALA 229 1446 1446 ALA ALA A . n 
A 1 230 THR 230 1447 1447 THR THR A . n 
A 1 231 SER 231 1448 1448 SER SER A . n 
A 1 232 HIS 232 1449 1449 HIS HIS A . n 
A 1 233 HIS 233 1450 1450 HIS HIS A . n 
A 1 234 LEU 234 1451 1451 LEU LEU A . n 
A 1 235 GLY 235 1452 1452 GLY GLY A . n 
A 1 236 GLN 236 1453 1453 GLN GLN A . n 
A 1 237 ASN 237 1454 1454 ASN ASN A . n 
A 1 238 PHE 238 1455 1455 PHE PHE A . n 
A 1 239 SER 239 1456 1456 SER SER A . n 
A 1 240 ARG 240 1457 1457 ARG ARG A . n 
A 1 241 MET 241 1458 1458 MET MET A . n 
A 1 242 PHE 242 1459 1459 PHE PHE A . n 
A 1 243 ASP 243 1460 1460 ASP ASP A . n 
A 1 244 ILE 244 1461 1461 ILE ILE A . n 
A 1 245 VAL 245 1462 1462 VAL VAL A . n 
A 1 246 TYR 246 1463 1463 TYR TYR A . n 
A 1 247 GLU 247 1464 1464 GLU GLU A . n 
A 1 248 HIS 248 1465 1465 HIS HIS A . n 
A 1 249 PRO 249 1466 1466 PRO PRO A . n 
A 1 250 GLU 250 1467 1467 GLU GLU A . n 
A 1 251 THR 251 1468 1468 THR THR A . n 
A 1 252 LYS 252 1469 1469 LYS LYS A . n 
A 1 253 GLU 253 1470 1470 GLU GLU A . n 
A 1 254 LYS 254 1471 1471 LYS LYS A . n 
A 1 255 GLU 255 1472 1472 GLU GLU A . n 
A 1 256 TYR 256 1473 1473 TYR TYR A . n 
A 1 257 VAL 257 1474 1474 VAL VAL A . n 
A 1 258 PHE 258 1475 1475 PHE PHE A . n 
A 1 259 GLN 259 1476 1476 GLN GLN A . n 
A 1 260 ASN 260 1477 1477 ASN ASN A . n 
A 1 261 SER 261 1478 1478 SER SER A . n 
A 1 262 TRP 262 1479 1479 TRP TRP A . n 
A 1 263 GLY 263 1480 1480 GLY GLY A . n 
A 1 264 ILE 264 1481 1481 ILE ILE A . n 
A 1 265 THR 265 1482 1482 THR THR A . n 
A 1 266 THR 266 1483 1483 THR THR A . n 
A 1 267 ARG 267 1484 1484 ARG ARG A . n 
A 1 268 THR 268 1485 1485 THR THR A . n 
A 1 269 ILE 269 1486 1486 ILE ILE A . n 
A 1 270 GLY 270 1487 1487 GLY GLY A . n 
A 1 271 VAL 271 1488 1488 VAL VAL A . n 
A 1 272 MET 272 1489 1489 MET MET A . n 
A 1 273 ILE 273 1490 1490 ILE ILE A . n 
A 1 274 MET 274 1491 1491 MET MET A . n 
A 1 275 VAL 275 1492 1492 VAL VAL A . n 
A 1 276 HIS 276 1493 1493 HIS HIS A . n 
A 1 277 ALA 277 1494 1494 ALA ALA A . n 
A 1 278 ASP 278 1495 1495 ASP ASP A . n 
A 1 279 ASN 279 1496 1496 ASN ASN A . n 
A 1 280 GLN 280 1497 1497 GLN GLN A . n 
A 1 281 GLY 281 1498 1498 GLY GLY A . n 
A 1 282 LEU 282 1499 1499 LEU LEU A . n 
A 1 283 VAL 283 1500 1500 VAL VAL A . n 
A 1 284 LEU 284 1501 1501 LEU LEU A . n 
A 1 285 PRO 285 1502 1502 PRO PRO A . n 
A 1 286 PRO 286 1503 1503 PRO PRO A . n 
A 1 287 ARG 287 1504 1504 ARG ARG A . n 
A 1 288 VAL 288 1505 1505 VAL VAL A . n 
A 1 289 ALA 289 1506 1506 ALA ALA A . n 
A 1 290 CYS 290 1507 1507 CYS CYS A . n 
A 1 291 ILE 291 1508 1508 ILE ILE A . n 
A 1 292 GLN 292 1509 1509 GLN GLN A . n 
A 1 293 VAL 293 1510 1510 VAL VAL A . n 
A 1 294 VAL 294 1511 1511 VAL VAL A . n 
A 1 295 ILE 295 1512 1512 ILE ILE A . n 
A 1 296 VAL 296 1513 1513 VAL VAL A . n 
A 1 297 PRO 297 1514 1514 PRO PRO A . n 
A 1 298 CYS 298 1515 1515 CYS CYS A . n 
A 1 299 GLY 299 1516 1516 GLY GLY A . n 
A 1 300 ILE 300 1517 1517 ILE ILE A . n 
A 1 301 THR 301 1518 1518 THR THR A . n 
A 1 302 ALA 302 1519 1519 ALA ALA A . n 
A 1 303 THR 303 1520 1520 THR THR A . n 
A 1 304 THR 304 1521 1521 THR THR A . n 
A 1 305 THR 305 1522 1522 THR THR A . n 
A 1 306 ASP 306 1523 1523 ASP ASP A . n 
A 1 307 ASP 307 1524 1524 ASP ASP A . n 
A 1 308 GLU 308 1525 1525 GLU GLU A . n 
A 1 309 ARG 309 1526 1526 ARG ARG A . n 
A 1 310 ARG 310 1527 1527 ARG ARG A . n 
A 1 311 ARG 311 1528 1528 ARG ARG A . n 
A 1 312 LEU 312 1529 1529 LEU LEU A . n 
A 1 313 TYR 313 1530 1530 TYR TYR A . n 
A 1 314 GLU 314 1531 1531 GLU GLU A . n 
A 1 315 SER 315 1532 1532 SER SER A . n 
A 1 316 CYS 316 1533 1533 CYS CYS A . n 
A 1 317 ARG 317 1534 1534 ARG ARG A . n 
A 1 318 GLU 318 1535 1535 GLU GLU A . n 
A 1 319 LEU 319 1536 1536 LEU LEU A . n 
A 1 320 GLU 320 1537 1537 GLU GLU A . n 
A 1 321 GLN 321 1538 1538 GLN GLN A . n 
A 1 322 THR 322 1539 1539 THR THR A . n 
A 1 323 PHE 323 1540 1540 PHE PHE A . n 
A 1 324 VAL 324 1541 1541 VAL VAL A . n 
A 1 325 LYS 325 1542 1542 LYS LYS A . n 
A 1 326 ALA 326 1543 1543 ALA ALA A . n 
A 1 327 GLY 327 1544 1544 GLY GLY A . n 
A 1 328 ILE 328 1545 1545 ILE ILE A . n 
A 1 329 ARG 329 1546 1546 ARG ARG A . n 
A 1 330 CYS 330 1547 1547 CYS CYS A . n 
A 1 331 GLU 331 1548 1548 GLU GLU A . n 
A 1 332 GLY 332 1549 1549 GLY GLY A . n 
A 1 333 ASP 333 1550 1550 ASP ASP A . n 
A 1 334 TYR 334 1551 1551 TYR TYR A . n 
A 1 335 ARG 335 1552 1552 ARG ARG A . n 
A 1 336 ASP 336 1553 1553 ASP ASP A . n 
A 1 337 ASN 337 1554 1554 ASN ASN A . n 
A 1 338 TYR 338 1555 1555 TYR TYR A . n 
A 1 339 SER 339 1556 1556 SER SER A . n 
A 1 340 PRO 340 1557 1557 PRO PRO A . n 
A 1 341 GLY 341 1558 1558 GLY GLY A . n 
A 1 342 TRP 342 1559 1559 TRP TRP A . n 
A 1 343 LYS 343 1560 1560 LYS LYS A . n 
A 1 344 TYR 344 1561 1561 TYR TYR A . n 
A 1 345 ASN 345 1562 1562 ASN ASN A . n 
A 1 346 HIS 346 1563 1563 HIS HIS A . n 
A 1 347 TRP 347 1564 1564 TRP TRP A . n 
A 1 348 GLU 348 1565 1565 GLU GLU A . n 
A 1 349 LEU 349 1566 1566 LEU LEU A . n 
A 1 350 LYS 350 1567 1567 LYS LYS A . n 
A 1 351 GLY 351 1568 1568 GLY GLY A . n 
A 1 352 VAL 352 1569 1569 VAL VAL A . n 
A 1 353 PRO 353 1570 1570 PRO PRO A . n 
A 1 354 VAL 354 1571 1571 VAL VAL A . n 
A 1 355 ARG 355 1572 1572 ARG ARG A . n 
A 1 356 ILE 356 1573 1573 ILE ILE A . n 
A 1 357 GLU 357 1574 1574 GLU GLU A . n 
A 1 358 LEU 358 1575 1575 LEU LEU A . n 
A 1 359 GLY 359 1576 1576 GLY GLY A . n 
A 1 360 PHE 360 1577 1577 PHE PHE A . n 
A 1 361 LYS 361 1578 1578 LYS LYS A . n 
A 1 362 ASP 362 1579 1579 ASP ASP A . n 
A 1 363 LEU 363 1580 1580 LEU LEU A . n 
A 1 364 GLN 364 1581 1581 GLN GLN A . n 
A 1 365 ASN 365 1582 1582 ASN ASN A . n 
A 1 366 ASP 366 1583 1583 ASP ASP A . n 
A 1 367 GLN 367 1584 1584 GLN GLN A . n 
A 1 368 PHE 368 1585 1585 PHE PHE A . n 
A 1 369 VAL 369 1586 1586 VAL VAL A . n 
A 1 370 ALA 370 1587 1587 ALA ALA A . n 
A 1 371 VAL 371 1588 1588 VAL VAL A . n 
A 1 372 ARG 372 1589 1589 ARG ARG A . n 
A 1 373 ARG 373 1590 1590 ARG ARG A . n 
A 1 374 ASP 374 1591 1591 ASP ASP A . n 
A 1 375 ASN 375 1592 1592 ASN ASN A . n 
A 1 376 GLY 376 1593 1593 GLY GLY A . n 
A 1 377 ALA 377 1594 1594 ALA ALA A . n 
A 1 378 LYS 378 1595 1595 LYS LYS A . n 
A 1 379 GLN 379 1596 1596 GLN GLN A . n 
A 1 380 THR 380 1597 1597 THR THR A . n 
A 1 381 ILE 381 1598 1598 ILE ILE A . n 
A 1 382 LYS 382 1599 1599 LYS LYS A . n 
A 1 383 ARG 383 1600 1600 ARG ARG A . n 
A 1 384 ALA 384 1601 1601 ALA ALA A . n 
A 1 385 GLN 385 1602 1602 GLN GLN A . n 
A 1 386 ALA 386 1603 1603 ALA ALA A . n 
A 1 387 THR 387 1604 1604 THR THR A . n 
A 1 388 VAL 388 1605 1605 VAL VAL A . n 
A 1 389 GLU 389 1606 1606 GLU GLU A . n 
A 1 390 MET 390 1607 1607 MET MET A . n 
A 1 391 PRO 391 1608 1608 PRO PRO A . n 
A 1 392 LYS 392 1609 1609 LYS LYS A . n 
A 1 393 LEU 393 1610 1610 LEU LEU A . n 
A 1 394 LEU 394 1611 1611 LEU LEU A . n 
A 1 395 GLU 395 1612 1612 GLU GLU A . n 
A 1 396 THR 396 1613 1613 THR THR A . n 
A 1 397 ILE 397 1614 1614 ILE ILE A . n 
A 1 398 HIS 398 1615 1615 HIS HIS A . n 
A 1 399 THR 399 1616 1616 THR THR A . n 
A 1 400 SER 400 1617 1617 SER SER A . n 
A 1 401 MET 401 1618 1618 MET MET A . n 
A 1 402 TYR 402 1619 1619 TYR TYR A . n 
A 1 403 GLU 403 1620 1620 GLU GLU A . n 
A 1 404 ARG 404 1621 1621 ARG ARG A . n 
A 1 405 ALA 405 1622 1622 ALA ALA A . n 
A 1 406 GLU 406 1623 1623 GLU GLU A . n 
A 1 407 ARG 407 1624 1624 ARG ARG A . n 
A 1 408 ASP 408 1625 1625 ASP ASP A . n 
A 1 409 LEU 409 1626 1626 LEU LEU A . n 
A 1 410 GLN 410 1627 1627 GLN GLN A . n 
A 1 411 SER 411 1628 1628 SER SER A . n 
A 1 412 HIS 412 1629 1629 HIS HIS A . n 
A 1 413 THR 413 1630 1630 THR THR A . n 
A 1 414 LYS 414 1631 1631 LYS LYS A . n 
A 1 415 LEU 415 1632 1632 LEU LEU A . n 
A 1 416 THR 416 1633 1633 THR THR A . n 
A 1 417 LYS 417 1634 1634 LYS LYS A . n 
A 1 418 GLN 418 1635 1635 GLN GLN A . n 
A 1 419 TRP 419 1636 1636 TRP TRP A . n 
A 1 420 ALA 420 1637 1637 ALA ALA A . n 
A 1 421 GLU 421 1638 1638 GLU GLU A . n 
A 1 422 PHE 422 1639 1639 PHE PHE A . n 
A 1 423 LEU 423 1640 1640 LEU LEU A . n 
A 1 424 GLN 424 1641 1641 GLN GLN A . n 
A 1 425 PHE 425 1642 1642 PHE PHE A . n 
A 1 426 LEU 426 1643 1643 LEU LEU A . n 
A 1 427 GLU 427 1644 1644 GLU GLU A . n 
A 1 428 THR 428 1645 1645 THR THR A . n 
A 1 429 LYS 429 1646 1646 LYS LYS A . n 
A 1 430 ASN 430 1647 1647 ASN ASN A . n 
A 1 431 ILE 431 1648 1648 ILE ILE A . n 
A 1 432 ILE 432 1649 1649 ILE ILE A . n 
A 1 433 MET 433 1650 1650 MET MET A . n 
A 1 434 ALA 434 1651 1651 ALA ALA A . n 
A 1 435 PRO 435 1652 1652 PRO PRO A . n 
A 1 436 PHE 436 1653 1653 PHE PHE A . n 
A 1 437 CYS 437 1654 1654 CYS CYS A . n 
A 1 438 GLY 438 1655 1655 GLY GLY A . n 
A 1 439 GLU 439 1656 1656 GLU GLU A . n 
A 1 440 ILE 440 1657 1657 ILE ILE A . n 
A 1 441 SER 441 1658 1658 SER SER A . n 
A 1 442 CYS 442 1659 1659 CYS CYS A . n 
A 1 443 GLU 443 1660 1660 GLU GLU A . n 
A 1 444 ASP 444 1661 1661 ASP ASP A . n 
A 1 445 ARG 445 1662 1662 ARG ARG A . n 
A 1 446 ILE 446 1663 1663 ILE ILE A . n 
A 1 447 LYS 447 1664 1664 LYS LYS A . n 
A 1 448 ALA 448 1665 1665 ALA ALA A . n 
A 1 449 GLU 449 1666 1666 GLU GLU A . n 
A 1 450 SER 450 1667 1667 SER SER A . n 
A 1 451 ALA 451 1668 1668 ALA ALA A . n 
A 1 452 ARG 452 1669 ?    ?   ?   A . n 
A 1 453 ASP 453 1670 ?    ?   ?   A . n 
A 1 454 ASP 454 1671 ?    ?   ?   A . n 
A 1 455 ALA 455 1672 ?    ?   ?   A . n 
A 1 456 GLU 456 1673 ?    ?   ?   A . n 
A 1 457 ALA 457 1674 ?    ?   ?   A . n 
A 1 458 GLU 458 1675 ?    ?   ?   A . n 
A 1 459 ALA 459 1676 ?    ?   ?   A . n 
A 1 460 GLY 460 1677 ?    ?   ?   A . n 
A 1 461 ALA 461 1678 ?    ?   ?   A . n 
A 1 462 PRO 462 1679 1679 PRO PRO A . n 
A 1 463 ALA 463 1680 1680 ALA ALA A . n 
A 1 464 MET 464 1681 1681 MET MET A . n 
A 1 465 GLY 465 1682 1682 GLY GLY A . n 
A 1 466 ALA 466 1683 1683 ALA ALA A . n 
A 1 467 LYS 467 1684 1684 LYS LYS A . n 
A 1 468 SER 468 1685 1685 SER SER A . n 
A 1 469 LEU 469 1686 1686 LEU LEU A . n 
A 1 470 CYS 470 1687 1687 CYS CYS A . n 
A 1 471 ILE 471 1688 1688 ILE ILE A . n 
A 1 472 PRO 472 1689 1689 PRO PRO A . n 
A 1 473 PHE 473 1690 1690 PHE PHE A . n 
A 1 474 GLU 474 1691 1691 GLU GLU A . n 
A 1 475 GLN 475 1692 1692 GLN GLN A . n 
A 1 476 PRO 476 1693 1693 PRO PRO A . n 
A 1 477 ALA 477 1694 1694 ALA ALA A . n 
A 1 478 LYS 478 1695 1695 LYS LYS A . n 
A 1 479 ILE 479 1696 1696 ILE ILE A . n 
A 1 480 ASP 480 1697 1697 ASP ASP A . n 
A 1 481 PRO 481 1698 1698 PRO PRO A . n 
A 1 482 LYS 482 1699 1699 LYS LYS A . n 
A 1 483 VAL 483 1700 1700 VAL VAL A . n 
A 1 484 ASP 484 1701 1701 ASP ASP A . n 
A 1 485 LYS 485 1702 1702 LYS LYS A . n 
A 1 486 CYS 486 1703 1703 CYS CYS A . n 
A 1 487 VAL 487 1704 1704 VAL VAL A . n 
A 1 488 HIS 488 1705 1705 HIS HIS A . n 
A 1 489 PRO 489 1706 1706 PRO PRO A . n 
A 1 490 ALA 490 1707 1707 ALA ALA A . n 
A 1 491 CYS 491 1708 1708 CYS CYS A . n 
A 1 492 GLY 492 1709 1709 GLY GLY A . n 
A 1 493 ARG 493 1710 1710 ARG ARG A . n 
A 1 494 VAL 494 1711 1711 VAL VAL A . n 
A 1 495 ALA 495 1712 1712 ALA ALA A . n 
A 1 496 LYS 496 1713 1713 LYS LYS A . n 
A 1 497 PHE 497 1714 1714 PHE PHE A . n 
A 1 498 TYR 498 1715 1715 TYR TYR A . n 
A 1 499 THR 499 1716 1716 THR THR A . n 
A 1 500 LEU 500 1717 1717 LEU LEU A . n 
A 1 501 PHE 501 1718 1718 PHE PHE A . n 
A 1 502 GLY 502 1719 1719 GLY GLY A . n 
A 1 503 ARG 503 1720 1720 ARG ARG A . n 
A 1 504 SER 504 1721 1721 SER SER A . n 
A 1 505 TYR 505 1722 1722 TYR TYR A . n 
B 1 1   MET 1   1218 ?    ?   ?   B . n 
B 1 2   THR 2   1219 ?    ?   ?   B . n 
B 1 3   ARG 3   1220 ?    ?   ?   B . n 
B 1 4   LEU 4   1221 ?    ?   ?   B . n 
B 1 5   GLY 5   1222 ?    ?   ?   B . n 
B 1 6   LEU 6   1223 1223 LEU LEU B . n 
B 1 7   GLU 7   1224 1224 GLU GLU B . n 
B 1 8   ALA 8   1225 1225 ALA ALA B . n 
B 1 9   THR 9   1226 1226 THR THR B . n 
B 1 10  LYS 10  1227 1227 LYS LYS B . n 
B 1 11  GLU 11  1228 1228 GLU GLU B . n 
B 1 12  ASP 12  1229 1229 ASP ASP B . n 
B 1 13  ASN 13  1230 1230 ASN ASN B . n 
B 1 14  LEU 14  1231 1231 LEU LEU B . n 
B 1 15  PRO 15  1232 1232 PRO PRO B . n 
B 1 16  ASP 16  1233 1233 ASP ASP B . n 
B 1 17  TRP 17  1234 1234 TRP TRP B . n 
B 1 18  TYR 18  1235 1235 TYR TYR B . n 
B 1 19  SER 19  1236 1236 SER SER B . n 
B 1 20  GLN 20  1237 1237 GLN GLN B . n 
B 1 21  VAL 21  1238 1238 VAL VAL B . n 
B 1 22  ILE 22  1239 1239 ILE ILE B . n 
B 1 23  THR 23  1240 1240 THR THR B . n 
B 1 24  LYS 24  1241 1241 LYS LYS B . n 
B 1 25  GLY 25  1242 1242 GLY GLY B . n 
B 1 26  GLU 26  1243 1243 GLU GLU B . n 
B 1 27  MET 27  1244 1244 MET MET B . n 
B 1 28  ILE 28  1245 1245 ILE ILE B . n 
B 1 29  GLU 29  1246 1246 GLU GLU B . n 
B 1 30  TYR 30  1247 1247 TYR TYR B . n 
B 1 31  TYR 31  1248 1248 TYR TYR B . n 
B 1 32  ASP 32  1249 1249 ASP ASP B . n 
B 1 33  VAL 33  1250 1250 VAL VAL B . n 
B 1 34  SER 34  1251 1251 SER SER B . n 
B 1 35  GLY 35  1252 1252 GLY GLY B . n 
B 1 36  CYS 36  1253 1253 CYS CYS B . n 
B 1 37  TYR 37  1254 1254 TYR TYR B . n 
B 1 38  ILE 38  1255 1255 ILE ILE B . n 
B 1 39  LEU 39  1256 1256 LEU LEU B . n 
B 1 40  ARG 40  1257 1257 ARG ARG B . n 
B 1 41  HIS 41  1258 1258 HIS HIS B . n 
B 1 42  TRP 42  1259 1259 TRP TRP B . n 
B 1 43  SER 43  1260 1260 SER SER B . n 
B 1 44  PHE 44  1261 1261 PHE PHE B . n 
B 1 45  ALA 45  1262 1262 ALA ALA B . n 
B 1 46  ILE 46  1263 1263 ILE ILE B . n 
B 1 47  TRP 47  1264 1264 TRP TRP B . n 
B 1 48  LYS 48  1265 1265 LYS LYS B . n 
B 1 49  ALA 49  1266 1266 ALA ALA B . n 
B 1 50  ILE 50  1267 1267 ILE ILE B . n 
B 1 51  ARG 51  1268 1268 ARG ARG B . n 
B 1 52  ASN 52  1269 1269 ASN ASN B . n 
B 1 53  TRP 53  1270 1270 TRP TRP B . n 
B 1 54  PHE 54  1271 1271 PHE PHE B . n 
B 1 55  ASP 55  1272 1272 ASP ASP B . n 
B 1 56  ALA 56  1273 1273 ALA ALA B . n 
B 1 57  GLU 57  1274 1274 GLU GLU B . n 
B 1 58  ILE 58  1275 1275 ILE ILE B . n 
B 1 59  THR 59  1276 1276 THR THR B . n 
B 1 60  ARG 60  1277 1277 ARG ARG B . n 
B 1 61  LEU 61  1278 1278 LEU LEU B . n 
B 1 62  GLY 62  1279 1279 GLY GLY B . n 
B 1 63  VAL 63  1280 1280 VAL VAL B . n 
B 1 64  LYS 64  1281 1281 LYS LYS B . n 
B 1 65  GLU 65  1282 1282 GLU GLU B . n 
B 1 66  CYS 66  1283 1283 CYS CYS B . n 
B 1 67  TYR 67  1284 1284 TYR TYR B . n 
B 1 68  PHE 68  1285 1285 PHE PHE B . n 
B 1 69  PRO 69  1286 1286 PRO PRO B . n 
B 1 70  ILE 70  1287 1287 ILE ILE B . n 
B 1 71  PHE 71  1288 1288 PHE PHE B . n 
B 1 72  VAL 72  1289 1289 VAL VAL B . n 
B 1 73  SER 73  1290 1290 SER SER B . n 
B 1 74  ARG 74  1291 1291 ARG ARG B . n 
B 1 75  ALA 75  1292 1292 ALA ALA B . n 
B 1 76  ALA 76  1293 1293 ALA ALA B . n 
B 1 77  LEU 77  1294 1294 LEU LEU B . n 
B 1 78  GLU 78  1295 1295 GLU GLU B . n 
B 1 79  ARG 79  1296 1296 ARG ARG B . n 
B 1 80  GLU 80  1297 ?    ?   ?   B . n 
B 1 81  LYS 81  1298 ?    ?   ?   B . n 
B 1 82  THR 82  1299 ?    ?   ?   B . n 
B 1 83  HIS 83  1300 ?    ?   ?   B . n 
B 1 84  ILE 84  1301 ?    ?   ?   B . n 
B 1 85  ALA 85  1302 ?    ?   ?   B . n 
B 1 86  ASP 86  1303 1303 ASP ASP B . n 
B 1 87  PHE 87  1304 1304 PHE PHE B . n 
B 1 88  ALA 88  1305 1305 ALA ALA B . n 
B 1 89  PRO 89  1306 1306 PRO PRO B . n 
B 1 90  GLU 90  1307 1307 GLU GLU B . n 
B 1 91  VAL 91  1308 1308 VAL VAL B . n 
B 1 92  ALA 92  1309 1309 ALA ALA B . n 
B 1 93  TRP 93  1310 1310 TRP TRP B . n 
B 1 94  VAL 94  1311 1311 VAL VAL B . n 
B 1 95  THR 95  1312 1312 THR THR B . n 
B 1 96  LYS 96  1313 1313 LYS LYS B . n 
B 1 97  SER 97  1314 1314 SER SER B . n 
B 1 98  GLY 98  1315 1315 GLY GLY B . n 
B 1 99  ASP 99  1316 1316 ASP ASP B . n 
B 1 100 SER 100 1317 1317 SER SER B . n 
B 1 101 GLU 101 1318 1318 GLU GLU B . n 
B 1 102 LEU 102 1319 1319 LEU LEU B . n 
B 1 103 ALA 103 1320 1320 ALA ALA B . n 
B 1 104 GLU 104 1321 1321 GLU GLU B . n 
B 1 105 PRO 105 1322 1322 PRO PRO B . n 
B 1 106 ILE 106 1323 1323 ILE ILE B . n 
B 1 107 ALA 107 1324 1324 ALA ALA B . n 
B 1 108 VAL 108 1325 1325 VAL VAL B . n 
B 1 109 ARG 109 1326 1326 ARG ARG B . n 
B 1 110 PRO 110 1327 1327 PRO PRO B . n 
B 1 111 THR 111 1328 1328 THR THR B . n 
B 1 112 SER 112 1329 1329 SER SER B . n 
B 1 113 GLU 113 1330 1330 GLU GLU B . n 
B 1 114 THR 114 1331 1331 THR THR B . n 
B 1 115 VAL 115 1332 1332 VAL VAL B . n 
B 1 116 MET 116 1333 1333 MET MET B . n 
B 1 117 TYR 117 1334 1334 TYR TYR B . n 
B 1 118 PRO 118 1335 1335 PRO PRO B . n 
B 1 119 ALA 119 1336 1336 ALA ALA B . n 
B 1 120 TYR 120 1337 1337 TYR TYR B . n 
B 1 121 ALA 121 1338 1338 ALA ALA B . n 
B 1 122 LYS 122 1339 1339 LYS LYS B . n 
B 1 123 TRP 123 1340 1340 TRP TRP B . n 
B 1 124 ILE 124 1341 1341 ILE ILE B . n 
B 1 125 GLN 125 1342 1342 GLN GLN B . n 
B 1 126 SER 126 1343 1343 SER SER B . n 
B 1 127 TYR 127 1344 1344 TYR TYR B . n 
B 1 128 ARG 128 1345 1345 ARG ARG B . n 
B 1 129 ASP 129 1346 1346 ASP ASP B . n 
B 1 130 LEU 130 1347 1347 LEU LEU B . n 
B 1 131 PRO 131 1348 1348 PRO PRO B . n 
B 1 132 ILE 132 1349 1349 ILE ILE B . n 
B 1 133 ARG 133 1350 1350 ARG ARG B . n 
B 1 134 LEU 134 1351 1351 LEU LEU B . n 
B 1 135 ASN 135 1352 1352 ASN ASN B . n 
B 1 136 GLN 136 1353 1353 GLN GLN B . n 
B 1 137 TRP 137 1354 1354 TRP TRP B . n 
B 1 138 ASN 138 1355 1355 ASN ASN B . n 
B 1 139 ASN 139 1356 1356 ASN ASN B . n 
B 1 140 VAL 140 1357 1357 VAL VAL B . n 
B 1 141 VAL 141 1358 1358 VAL VAL B . n 
B 1 142 ARG 142 1359 1359 ARG ARG B . n 
B 1 143 TRP 143 1360 1360 TRP TRP B . n 
B 1 144 GLU 144 1361 1361 GLU GLU B . n 
B 1 145 PHE 145 1362 1362 PHE PHE B . n 
B 1 146 LYS 146 1363 1363 LYS LYS B . n 
B 1 147 HIS 147 1364 1364 HIS HIS B . n 
B 1 148 PRO 148 1365 1365 PRO PRO B . n 
B 1 149 GLN 149 1366 1366 GLN GLN B . n 
B 1 150 PRO 150 1367 1367 PRO PRO B . n 
B 1 151 PHE 151 1368 1368 PHE PHE B . n 
B 1 152 LEU 152 1369 1369 LEU LEU B . n 
B 1 153 ARG 153 1370 1370 ARG ARG B . n 
B 1 154 THR 154 1371 1371 THR THR B . n 
B 1 155 ARG 155 1372 1372 ARG ARG B . n 
B 1 156 GLU 156 1373 1373 GLU GLU B . n 
B 1 157 PHE 157 1374 1374 PHE PHE B . n 
B 1 158 LEU 158 1375 1375 LEU LEU B . n 
B 1 159 TRP 159 1376 1376 TRP TRP B . n 
B 1 160 GLN 160 1377 1377 GLN GLN B . n 
B 1 161 GLU 161 1378 1378 GLU GLU B . n 
B 1 162 GLY 162 1379 1379 GLY GLY B . n 
B 1 163 HIS 163 1380 1380 HIS HIS B . n 
B 1 164 THR 164 1381 1381 THR THR B . n 
B 1 165 ALA 165 1382 1382 ALA ALA B . n 
B 1 166 PHE 166 1383 1383 PHE PHE B . n 
B 1 167 ALA 167 1384 1384 ALA ALA B . n 
B 1 168 THR 168 1385 1385 THR THR B . n 
B 1 169 GLN 169 1386 1386 GLN GLN B . n 
B 1 170 LYS 170 1387 1387 LYS LYS B . n 
B 1 171 GLU 171 1388 1388 GLU GLU B . n 
B 1 172 ALA 172 1389 1389 ALA ALA B . n 
B 1 173 ASP 173 1390 1390 ASP ASP B . n 
B 1 174 GLU 174 1391 1391 GLU GLU B . n 
B 1 175 GLU 175 1392 1392 GLU GLU B . n 
B 1 176 VAL 176 1393 1393 VAL VAL B . n 
B 1 177 LEU 177 1394 1394 LEU LEU B . n 
B 1 178 THR 178 1395 1395 THR THR B . n 
B 1 179 ILE 179 1396 1396 ILE ILE B . n 
B 1 180 LEU 180 1397 1397 LEU LEU B . n 
B 1 181 ASP 181 1398 1398 ASP ASP B . n 
B 1 182 LEU 182 1399 1399 LEU LEU B . n 
B 1 183 TYR 183 1400 1400 TYR TYR B . n 
B 1 184 ALA 184 1401 1401 ALA ALA B . n 
B 1 185 LYS 185 1402 1402 LYS LYS B . n 
B 1 186 VAL 186 1403 1403 VAL VAL B . n 
B 1 187 TYR 187 1404 1404 TYR TYR B . n 
B 1 188 THR 188 1405 1405 THR THR B . n 
B 1 189 ASP 189 1406 1406 ASP ASP B . n 
B 1 190 LEU 190 1407 1407 LEU LEU B . n 
B 1 191 LEU 191 1408 1408 LEU LEU B . n 
B 1 192 ALA 192 1409 1409 ALA ALA B . n 
B 1 193 ILE 193 1410 1410 ILE ILE B . n 
B 1 194 PRO 194 1411 1411 PRO PRO B . n 
B 1 195 VAL 195 1412 1412 VAL VAL B . n 
B 1 196 VAL 196 1413 1413 VAL VAL B . n 
B 1 197 LYS 197 1414 1414 LYS LYS B . n 
B 1 198 GLY 198 1415 1415 GLY GLY B . n 
B 1 199 ARG 199 1416 1416 ARG ARG B . n 
B 1 200 LYS 200 1417 1417 LYS LYS B . n 
B 1 201 THR 201 1418 1418 THR THR B . n 
B 1 202 GLU 202 1419 1419 GLU GLU B . n 
B 1 203 LYS 203 1420 1420 LYS LYS B . n 
B 1 204 GLU 204 1421 1421 GLU GLU B . n 
B 1 205 LYS 205 1422 1422 LYS LYS B . n 
B 1 206 PHE 206 1423 1423 PHE PHE B . n 
B 1 207 ALA 207 1424 1424 ALA ALA B . n 
B 1 208 GLY 208 1425 1425 GLY GLY B . n 
B 1 209 GLY 209 1426 1426 GLY GLY B . n 
B 1 210 ASP 210 1427 1427 ASP ASP B . n 
B 1 211 TYR 211 1428 1428 TYR TYR B . n 
B 1 212 THR 212 1429 1429 THR THR B . n 
B 1 213 THR 213 1430 1430 THR THR B . n 
B 1 214 THR 214 1431 1431 THR THR B . n 
B 1 215 VAL 215 1432 1432 VAL VAL B . n 
B 1 216 GLU 216 1433 1433 GLU GLU B . n 
B 1 217 ALA 217 1434 1434 ALA ALA B . n 
B 1 218 TYR 218 1435 1435 TYR TYR B . n 
B 1 219 ILE 219 1436 1436 ILE ILE B . n 
B 1 220 SER 220 1437 1437 SER SER B . n 
B 1 221 ALA 221 1438 1438 ALA ALA B . n 
B 1 222 SER 222 1439 1439 SER SER B . n 
B 1 223 GLY 223 1440 1440 GLY GLY B . n 
B 1 224 ARG 224 1441 1441 ARG ARG B . n 
B 1 225 ALA 225 1442 1442 ALA ALA B . n 
B 1 226 ILE 226 1443 1443 ILE ILE B . n 
B 1 227 GLN 227 1444 1444 GLN GLN B . n 
B 1 228 GLY 228 1445 1445 GLY GLY B . n 
B 1 229 ALA 229 1446 1446 ALA ALA B . n 
B 1 230 THR 230 1447 1447 THR THR B . n 
B 1 231 SER 231 1448 1448 SER SER B . n 
B 1 232 HIS 232 1449 1449 HIS HIS B . n 
B 1 233 HIS 233 1450 1450 HIS HIS B . n 
B 1 234 LEU 234 1451 1451 LEU LEU B . n 
B 1 235 GLY 235 1452 1452 GLY GLY B . n 
B 1 236 GLN 236 1453 1453 GLN GLN B . n 
B 1 237 ASN 237 1454 1454 ASN ASN B . n 
B 1 238 PHE 238 1455 1455 PHE PHE B . n 
B 1 239 SER 239 1456 1456 SER SER B . n 
B 1 240 ARG 240 1457 1457 ARG ARG B . n 
B 1 241 MET 241 1458 1458 MET MET B . n 
B 1 242 PHE 242 1459 1459 PHE PHE B . n 
B 1 243 ASP 243 1460 1460 ASP ASP B . n 
B 1 244 ILE 244 1461 1461 ILE ILE B . n 
B 1 245 VAL 245 1462 1462 VAL VAL B . n 
B 1 246 TYR 246 1463 1463 TYR TYR B . n 
B 1 247 GLU 247 1464 1464 GLU GLU B . n 
B 1 248 HIS 248 1465 1465 HIS HIS B . n 
B 1 249 PRO 249 1466 1466 PRO PRO B . n 
B 1 250 GLU 250 1467 1467 GLU GLU B . n 
B 1 251 THR 251 1468 1468 THR THR B . n 
B 1 252 LYS 252 1469 1469 LYS LYS B . n 
B 1 253 GLU 253 1470 1470 GLU GLU B . n 
B 1 254 LYS 254 1471 1471 LYS LYS B . n 
B 1 255 GLU 255 1472 1472 GLU GLU B . n 
B 1 256 TYR 256 1473 1473 TYR TYR B . n 
B 1 257 VAL 257 1474 1474 VAL VAL B . n 
B 1 258 PHE 258 1475 1475 PHE PHE B . n 
B 1 259 GLN 259 1476 1476 GLN GLN B . n 
B 1 260 ASN 260 1477 1477 ASN ASN B . n 
B 1 261 SER 261 1478 1478 SER SER B . n 
B 1 262 TRP 262 1479 1479 TRP TRP B . n 
B 1 263 GLY 263 1480 1480 GLY GLY B . n 
B 1 264 ILE 264 1481 1481 ILE ILE B . n 
B 1 265 THR 265 1482 1482 THR THR B . n 
B 1 266 THR 266 1483 1483 THR THR B . n 
B 1 267 ARG 267 1484 1484 ARG ARG B . n 
B 1 268 THR 268 1485 1485 THR THR B . n 
B 1 269 ILE 269 1486 1486 ILE ILE B . n 
B 1 270 GLY 270 1487 1487 GLY GLY B . n 
B 1 271 VAL 271 1488 1488 VAL VAL B . n 
B 1 272 MET 272 1489 1489 MET MET B . n 
B 1 273 ILE 273 1490 1490 ILE ILE B . n 
B 1 274 MET 274 1491 1491 MET MET B . n 
B 1 275 VAL 275 1492 1492 VAL VAL B . n 
B 1 276 HIS 276 1493 1493 HIS HIS B . n 
B 1 277 ALA 277 1494 1494 ALA ALA B . n 
B 1 278 ASP 278 1495 1495 ASP ASP B . n 
B 1 279 ASN 279 1496 1496 ASN ASN B . n 
B 1 280 GLN 280 1497 1497 GLN GLN B . n 
B 1 281 GLY 281 1498 1498 GLY GLY B . n 
B 1 282 LEU 282 1499 1499 LEU LEU B . n 
B 1 283 VAL 283 1500 1500 VAL VAL B . n 
B 1 284 LEU 284 1501 1501 LEU LEU B . n 
B 1 285 PRO 285 1502 1502 PRO PRO B . n 
B 1 286 PRO 286 1503 1503 PRO PRO B . n 
B 1 287 ARG 287 1504 1504 ARG ARG B . n 
B 1 288 VAL 288 1505 1505 VAL VAL B . n 
B 1 289 ALA 289 1506 1506 ALA ALA B . n 
B 1 290 CYS 290 1507 1507 CYS CYS B . n 
B 1 291 ILE 291 1508 1508 ILE ILE B . n 
B 1 292 GLN 292 1509 1509 GLN GLN B . n 
B 1 293 VAL 293 1510 1510 VAL VAL B . n 
B 1 294 VAL 294 1511 1511 VAL VAL B . n 
B 1 295 ILE 295 1512 1512 ILE ILE B . n 
B 1 296 VAL 296 1513 1513 VAL VAL B . n 
B 1 297 PRO 297 1514 1514 PRO PRO B . n 
B 1 298 CYS 298 1515 1515 CYS CYS B . n 
B 1 299 GLY 299 1516 1516 GLY GLY B . n 
B 1 300 ILE 300 1517 1517 ILE ILE B . n 
B 1 301 THR 301 1518 1518 THR THR B . n 
B 1 302 ALA 302 1519 1519 ALA ALA B . n 
B 1 303 THR 303 1520 1520 THR THR B . n 
B 1 304 THR 304 1521 1521 THR THR B . n 
B 1 305 THR 305 1522 1522 THR THR B . n 
B 1 306 ASP 306 1523 1523 ASP ASP B . n 
B 1 307 ASP 307 1524 1524 ASP ASP B . n 
B 1 308 GLU 308 1525 1525 GLU GLU B . n 
B 1 309 ARG 309 1526 1526 ARG ARG B . n 
B 1 310 ARG 310 1527 1527 ARG ARG B . n 
B 1 311 ARG 311 1528 1528 ARG ARG B . n 
B 1 312 LEU 312 1529 1529 LEU LEU B . n 
B 1 313 TYR 313 1530 1530 TYR TYR B . n 
B 1 314 GLU 314 1531 1531 GLU GLU B . n 
B 1 315 SER 315 1532 1532 SER SER B . n 
B 1 316 CYS 316 1533 1533 CYS CYS B . n 
B 1 317 ARG 317 1534 1534 ARG ARG B . n 
B 1 318 GLU 318 1535 1535 GLU GLU B . n 
B 1 319 LEU 319 1536 1536 LEU LEU B . n 
B 1 320 GLU 320 1537 1537 GLU GLU B . n 
B 1 321 GLN 321 1538 1538 GLN GLN B . n 
B 1 322 THR 322 1539 1539 THR THR B . n 
B 1 323 PHE 323 1540 1540 PHE PHE B . n 
B 1 324 VAL 324 1541 1541 VAL VAL B . n 
B 1 325 LYS 325 1542 1542 LYS LYS B . n 
B 1 326 ALA 326 1543 1543 ALA ALA B . n 
B 1 327 GLY 327 1544 1544 GLY GLY B . n 
B 1 328 ILE 328 1545 1545 ILE ILE B . n 
B 1 329 ARG 329 1546 1546 ARG ARG B . n 
B 1 330 CYS 330 1547 1547 CYS CYS B . n 
B 1 331 GLU 331 1548 1548 GLU GLU B . n 
B 1 332 GLY 332 1549 1549 GLY GLY B . n 
B 1 333 ASP 333 1550 1550 ASP ASP B . n 
B 1 334 TYR 334 1551 1551 TYR TYR B . n 
B 1 335 ARG 335 1552 1552 ARG ARG B . n 
B 1 336 ASP 336 1553 1553 ASP ASP B . n 
B 1 337 ASN 337 1554 1554 ASN ASN B . n 
B 1 338 TYR 338 1555 1555 TYR TYR B . n 
B 1 339 SER 339 1556 1556 SER SER B . n 
B 1 340 PRO 340 1557 1557 PRO PRO B . n 
B 1 341 GLY 341 1558 1558 GLY GLY B . n 
B 1 342 TRP 342 1559 1559 TRP TRP B . n 
B 1 343 LYS 343 1560 1560 LYS LYS B . n 
B 1 344 TYR 344 1561 1561 TYR TYR B . n 
B 1 345 ASN 345 1562 1562 ASN ASN B . n 
B 1 346 HIS 346 1563 1563 HIS HIS B . n 
B 1 347 TRP 347 1564 1564 TRP TRP B . n 
B 1 348 GLU 348 1565 1565 GLU GLU B . n 
B 1 349 LEU 349 1566 1566 LEU LEU B . n 
B 1 350 LYS 350 1567 1567 LYS LYS B . n 
B 1 351 GLY 351 1568 1568 GLY GLY B . n 
B 1 352 VAL 352 1569 1569 VAL VAL B . n 
B 1 353 PRO 353 1570 1570 PRO PRO B . n 
B 1 354 VAL 354 1571 1571 VAL VAL B . n 
B 1 355 ARG 355 1572 1572 ARG ARG B . n 
B 1 356 ILE 356 1573 1573 ILE ILE B . n 
B 1 357 GLU 357 1574 1574 GLU GLU B . n 
B 1 358 LEU 358 1575 1575 LEU LEU B . n 
B 1 359 GLY 359 1576 1576 GLY GLY B . n 
B 1 360 PHE 360 1577 1577 PHE PHE B . n 
B 1 361 LYS 361 1578 1578 LYS LYS B . n 
B 1 362 ASP 362 1579 1579 ASP ASP B . n 
B 1 363 LEU 363 1580 1580 LEU LEU B . n 
B 1 364 GLN 364 1581 1581 GLN GLN B . n 
B 1 365 ASN 365 1582 1582 ASN ASN B . n 
B 1 366 ASP 366 1583 1583 ASP ASP B . n 
B 1 367 GLN 367 1584 1584 GLN GLN B . n 
B 1 368 PHE 368 1585 1585 PHE PHE B . n 
B 1 369 VAL 369 1586 1586 VAL VAL B . n 
B 1 370 ALA 370 1587 1587 ALA ALA B . n 
B 1 371 VAL 371 1588 1588 VAL VAL B . n 
B 1 372 ARG 372 1589 1589 ARG ARG B . n 
B 1 373 ARG 373 1590 1590 ARG ARG B . n 
B 1 374 ASP 374 1591 1591 ASP ASP B . n 
B 1 375 ASN 375 1592 1592 ASN ASN B . n 
B 1 376 GLY 376 1593 1593 GLY GLY B . n 
B 1 377 ALA 377 1594 1594 ALA ALA B . n 
B 1 378 LYS 378 1595 1595 LYS LYS B . n 
B 1 379 GLN 379 1596 1596 GLN GLN B . n 
B 1 380 THR 380 1597 1597 THR THR B . n 
B 1 381 ILE 381 1598 1598 ILE ILE B . n 
B 1 382 LYS 382 1599 1599 LYS LYS B . n 
B 1 383 ARG 383 1600 1600 ARG ARG B . n 
B 1 384 ALA 384 1601 1601 ALA ALA B . n 
B 1 385 GLN 385 1602 1602 GLN GLN B . n 
B 1 386 ALA 386 1603 1603 ALA ALA B . n 
B 1 387 THR 387 1604 1604 THR THR B . n 
B 1 388 VAL 388 1605 1605 VAL VAL B . n 
B 1 389 GLU 389 1606 1606 GLU GLU B . n 
B 1 390 MET 390 1607 1607 MET MET B . n 
B 1 391 PRO 391 1608 1608 PRO PRO B . n 
B 1 392 LYS 392 1609 1609 LYS LYS B . n 
B 1 393 LEU 393 1610 1610 LEU LEU B . n 
B 1 394 LEU 394 1611 1611 LEU LEU B . n 
B 1 395 GLU 395 1612 1612 GLU GLU B . n 
B 1 396 THR 396 1613 1613 THR THR B . n 
B 1 397 ILE 397 1614 1614 ILE ILE B . n 
B 1 398 HIS 398 1615 1615 HIS HIS B . n 
B 1 399 THR 399 1616 1616 THR THR B . n 
B 1 400 SER 400 1617 1617 SER SER B . n 
B 1 401 MET 401 1618 1618 MET MET B . n 
B 1 402 TYR 402 1619 1619 TYR TYR B . n 
B 1 403 GLU 403 1620 1620 GLU GLU B . n 
B 1 404 ARG 404 1621 1621 ARG ARG B . n 
B 1 405 ALA 405 1622 1622 ALA ALA B . n 
B 1 406 GLU 406 1623 1623 GLU GLU B . n 
B 1 407 ARG 407 1624 1624 ARG ARG B . n 
B 1 408 ASP 408 1625 1625 ASP ASP B . n 
B 1 409 LEU 409 1626 1626 LEU LEU B . n 
B 1 410 GLN 410 1627 1627 GLN GLN B . n 
B 1 411 SER 411 1628 1628 SER SER B . n 
B 1 412 HIS 412 1629 1629 HIS HIS B . n 
B 1 413 THR 413 1630 1630 THR THR B . n 
B 1 414 LYS 414 1631 1631 LYS LYS B . n 
B 1 415 LEU 415 1632 1632 LEU LEU B . n 
B 1 416 THR 416 1633 1633 THR THR B . n 
B 1 417 LYS 417 1634 1634 LYS LYS B . n 
B 1 418 GLN 418 1635 1635 GLN GLN B . n 
B 1 419 TRP 419 1636 1636 TRP TRP B . n 
B 1 420 ALA 420 1637 1637 ALA ALA B . n 
B 1 421 GLU 421 1638 1638 GLU GLU B . n 
B 1 422 PHE 422 1639 1639 PHE PHE B . n 
B 1 423 LEU 423 1640 1640 LEU LEU B . n 
B 1 424 GLN 424 1641 1641 GLN GLN B . n 
B 1 425 PHE 425 1642 1642 PHE PHE B . n 
B 1 426 LEU 426 1643 1643 LEU LEU B . n 
B 1 427 GLU 427 1644 1644 GLU GLU B . n 
B 1 428 THR 428 1645 1645 THR THR B . n 
B 1 429 LYS 429 1646 1646 LYS LYS B . n 
B 1 430 ASN 430 1647 1647 ASN ASN B . n 
B 1 431 ILE 431 1648 1648 ILE ILE B . n 
B 1 432 ILE 432 1649 1649 ILE ILE B . n 
B 1 433 MET 433 1650 1650 MET MET B . n 
B 1 434 ALA 434 1651 1651 ALA ALA B . n 
B 1 435 PRO 435 1652 1652 PRO PRO B . n 
B 1 436 PHE 436 1653 1653 PHE PHE B . n 
B 1 437 CYS 437 1654 1654 CYS CYS B . n 
B 1 438 GLY 438 1655 1655 GLY GLY B . n 
B 1 439 GLU 439 1656 1656 GLU GLU B . n 
B 1 440 ILE 440 1657 1657 ILE ILE B . n 
B 1 441 SER 441 1658 1658 SER SER B . n 
B 1 442 CYS 442 1659 1659 CYS CYS B . n 
B 1 443 GLU 443 1660 1660 GLU GLU B . n 
B 1 444 ASP 444 1661 1661 ASP ASP B . n 
B 1 445 ARG 445 1662 1662 ARG ARG B . n 
B 1 446 ILE 446 1663 1663 ILE ILE B . n 
B 1 447 LYS 447 1664 1664 LYS LYS B . n 
B 1 448 ALA 448 1665 1665 ALA ALA B . n 
B 1 449 GLU 449 1666 1666 GLU GLU B . n 
B 1 450 SER 450 1667 1667 SER SER B . n 
B 1 451 ALA 451 1668 1668 ALA ALA B . n 
B 1 452 ARG 452 1669 ?    ?   ?   B . n 
B 1 453 ASP 453 1670 ?    ?   ?   B . n 
B 1 454 ASP 454 1671 ?    ?   ?   B . n 
B 1 455 ALA 455 1672 ?    ?   ?   B . n 
B 1 456 GLU 456 1673 ?    ?   ?   B . n 
B 1 457 ALA 457 1674 ?    ?   ?   B . n 
B 1 458 GLU 458 1675 ?    ?   ?   B . n 
B 1 459 ALA 459 1676 ?    ?   ?   B . n 
B 1 460 GLY 460 1677 ?    ?   ?   B . n 
B 1 461 ALA 461 1678 ?    ?   ?   B . n 
B 1 462 PRO 462 1679 ?    ?   ?   B . n 
B 1 463 ALA 463 1680 ?    ?   ?   B . n 
B 1 464 MET 464 1681 1681 MET MET B . n 
B 1 465 GLY 465 1682 1682 GLY GLY B . n 
B 1 466 ALA 466 1683 1683 ALA ALA B . n 
B 1 467 LYS 467 1684 1684 LYS LYS B . n 
B 1 468 SER 468 1685 1685 SER SER B . n 
B 1 469 LEU 469 1686 1686 LEU LEU B . n 
B 1 470 CYS 470 1687 1687 CYS CYS B . n 
B 1 471 ILE 471 1688 1688 ILE ILE B . n 
B 1 472 PRO 472 1689 1689 PRO PRO B . n 
B 1 473 PHE 473 1690 1690 PHE PHE B . n 
B 1 474 GLU 474 1691 1691 GLU GLU B . n 
B 1 475 GLN 475 1692 1692 GLN GLN B . n 
B 1 476 PRO 476 1693 1693 PRO PRO B . n 
B 1 477 ALA 477 1694 1694 ALA ALA B . n 
B 1 478 LYS 478 1695 1695 LYS LYS B . n 
B 1 479 ILE 479 1696 1696 ILE ILE B . n 
B 1 480 ASP 480 1697 1697 ASP ASP B . n 
B 1 481 PRO 481 1698 1698 PRO PRO B . n 
B 1 482 LYS 482 1699 1699 LYS LYS B . n 
B 1 483 VAL 483 1700 1700 VAL VAL B . n 
B 1 484 ASP 484 1701 1701 ASP ASP B . n 
B 1 485 LYS 485 1702 1702 LYS LYS B . n 
B 1 486 CYS 486 1703 1703 CYS CYS B . n 
B 1 487 VAL 487 1704 1704 VAL VAL B . n 
B 1 488 HIS 488 1705 1705 HIS HIS B . n 
B 1 489 PRO 489 1706 1706 PRO PRO B . n 
B 1 490 ALA 490 1707 1707 ALA ALA B . n 
B 1 491 CYS 491 1708 1708 CYS CYS B . n 
B 1 492 GLY 492 1709 1709 GLY GLY B . n 
B 1 493 ARG 493 1710 1710 ARG ARG B . n 
B 1 494 VAL 494 1711 1711 VAL VAL B . n 
B 1 495 ALA 495 1712 1712 ALA ALA B . n 
B 1 496 LYS 496 1713 1713 LYS LYS B . n 
B 1 497 PHE 497 1714 1714 PHE PHE B . n 
B 1 498 TYR 498 1715 1715 TYR TYR B . n 
B 1 499 THR 499 1716 1716 THR THR B . n 
B 1 500 LEU 500 1717 1717 LEU LEU B . n 
B 1 501 PHE 501 1718 1718 PHE PHE B . n 
B 1 502 GLY 502 1719 1719 GLY GLY B . n 
B 1 503 ARG 503 1720 1720 ARG ARG B . n 
B 1 504 SER 504 1721 1721 SER SER B . n 
B 1 505 TYR 505 1722 1722 TYR TYR B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HFG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HFG 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ANP 1 1801 1801 ANP ANP A . 
D 3 HFG 1 1802 1802 HFG HFG A . 
E 4 MG  1 1803 1803 MG  MG  A . 
F 5 ZN  1 1804 1804 ZN  ZN  A . 
G 2 ANP 1 1801 1801 ANP ANP B . 
H 3 HFG 1 1802 1802 HFG HFG B . 
I 4 MG  1 1803 1803 MG  MG  B . 
J 5 ZN  1 1804 1804 ZN  ZN  B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 1224 ? CG  ? A GLU 7   CG  
2   1 Y 1 A GLU 1224 ? CD  ? A GLU 7   CD  
3   1 Y 1 A GLU 1224 ? OE1 ? A GLU 7   OE1 
4   1 Y 1 A GLU 1224 ? OE2 ? A GLU 7   OE2 
5   1 Y 1 A ARG 1291 ? CG  ? A ARG 74  CG  
6   1 Y 1 A ARG 1291 ? CD  ? A ARG 74  CD  
7   1 Y 1 A ARG 1291 ? NE  ? A ARG 74  NE  
8   1 Y 1 A ARG 1291 ? CZ  ? A ARG 74  CZ  
9   1 Y 1 A ARG 1291 ? NH1 ? A ARG 74  NH1 
10  1 Y 1 A ARG 1291 ? NH2 ? A ARG 74  NH2 
11  1 Y 1 A ASP 1303 ? CG  ? A ASP 86  CG  
12  1 Y 1 A ASP 1303 ? OD1 ? A ASP 86  OD1 
13  1 Y 1 A ASP 1303 ? OD2 ? A ASP 86  OD2 
14  1 Y 1 A GLU 1318 ? CG  ? A GLU 101 CG  
15  1 Y 1 A GLU 1318 ? CD  ? A GLU 101 CD  
16  1 Y 1 A GLU 1318 ? OE1 ? A GLU 101 OE1 
17  1 Y 1 A GLU 1318 ? OE2 ? A GLU 101 OE2 
18  1 Y 1 A GLU 1321 ? CG  ? A GLU 104 CG  
19  1 Y 1 A GLU 1321 ? CD  ? A GLU 104 CD  
20  1 Y 1 A GLU 1321 ? OE1 ? A GLU 104 OE1 
21  1 Y 1 A GLU 1321 ? OE2 ? A GLU 104 OE2 
22  1 Y 1 A GLN 1342 ? CG  ? A GLN 125 CG  
23  1 Y 1 A GLN 1342 ? CD  ? A GLN 125 CD  
24  1 Y 1 A GLN 1342 ? OE1 ? A GLN 125 OE1 
25  1 Y 1 A GLN 1342 ? NE2 ? A GLN 125 NE2 
26  1 Y 1 A TYR 1344 ? CG  ? A TYR 127 CG  
27  1 Y 1 A TYR 1344 ? CD1 ? A TYR 127 CD1 
28  1 Y 1 A TYR 1344 ? CD2 ? A TYR 127 CD2 
29  1 Y 1 A TYR 1344 ? CE1 ? A TYR 127 CE1 
30  1 Y 1 A TYR 1344 ? CE2 ? A TYR 127 CE2 
31  1 Y 1 A TYR 1344 ? CZ  ? A TYR 127 CZ  
32  1 Y 1 A TYR 1344 ? OH  ? A TYR 127 OH  
33  1 Y 1 A ARG 1345 ? CG  ? A ARG 128 CG  
34  1 Y 1 A ARG 1345 ? CD  ? A ARG 128 CD  
35  1 Y 1 A ARG 1345 ? NE  ? A ARG 128 NE  
36  1 Y 1 A ARG 1345 ? CZ  ? A ARG 128 CZ  
37  1 Y 1 A ARG 1345 ? NH1 ? A ARG 128 NH1 
38  1 Y 1 A ARG 1345 ? NH2 ? A ARG 128 NH2 
39  1 Y 1 A LYS 1387 ? CG  ? A LYS 170 CG  
40  1 Y 1 A LYS 1387 ? CD  ? A LYS 170 CD  
41  1 Y 1 A LYS 1387 ? CE  ? A LYS 170 CE  
42  1 Y 1 A LYS 1387 ? NZ  ? A LYS 170 NZ  
43  1 Y 1 A GLU 1467 ? CG  ? A GLU 250 CG  
44  1 Y 1 A GLU 1467 ? CD  ? A GLU 250 CD  
45  1 Y 1 A GLU 1467 ? OE1 ? A GLU 250 OE1 
46  1 Y 1 A GLU 1467 ? OE2 ? A GLU 250 OE2 
47  1 Y 1 A LYS 1469 ? CG  ? A LYS 252 CG  
48  1 Y 1 A LYS 1469 ? CD  ? A LYS 252 CD  
49  1 Y 1 A LYS 1469 ? CE  ? A LYS 252 CE  
50  1 Y 1 A LYS 1469 ? NZ  ? A LYS 252 NZ  
51  1 Y 1 A LYS 1471 ? CG  ? A LYS 254 CG  
52  1 Y 1 A LYS 1471 ? CD  ? A LYS 254 CD  
53  1 Y 1 A LYS 1471 ? CE  ? A LYS 254 CE  
54  1 Y 1 A LYS 1471 ? NZ  ? A LYS 254 NZ  
55  1 Y 1 A ILE 1517 ? CG1 ? A ILE 300 CG1 
56  1 Y 1 A ILE 1517 ? CG2 ? A ILE 300 CG2 
57  1 Y 1 A ILE 1517 ? CD1 ? A ILE 300 CD1 
58  1 Y 1 A THR 1518 ? OG1 ? A THR 301 OG1 
59  1 Y 1 A THR 1518 ? CG2 ? A THR 301 CG2 
60  1 Y 1 A THR 1520 ? OG1 ? A THR 303 OG1 
61  1 Y 1 A THR 1520 ? CG2 ? A THR 303 CG2 
62  1 Y 1 A THR 1521 ? OG1 ? A THR 304 OG1 
63  1 Y 1 A THR 1521 ? CG2 ? A THR 304 CG2 
64  1 Y 1 A THR 1522 ? OG1 ? A THR 305 OG1 
65  1 Y 1 A THR 1522 ? CG2 ? A THR 305 CG2 
66  1 Y 1 A GLU 1525 ? CG  ? A GLU 308 CG  
67  1 Y 1 A GLU 1525 ? CD  ? A GLU 308 CD  
68  1 Y 1 A GLU 1525 ? OE1 ? A GLU 308 OE1 
69  1 Y 1 A GLU 1525 ? OE2 ? A GLU 308 OE2 
70  1 Y 1 A ARG 1526 ? CG  ? A ARG 309 CG  
71  1 Y 1 A ARG 1526 ? CD  ? A ARG 309 CD  
72  1 Y 1 A ARG 1526 ? NE  ? A ARG 309 NE  
73  1 Y 1 A ARG 1526 ? CZ  ? A ARG 309 CZ  
74  1 Y 1 A ARG 1526 ? NH1 ? A ARG 309 NH1 
75  1 Y 1 A ARG 1526 ? NH2 ? A ARG 309 NH2 
76  1 Y 1 A ARG 1527 ? CG  ? A ARG 310 CG  
77  1 Y 1 A ARG 1527 ? CD  ? A ARG 310 CD  
78  1 Y 1 A ARG 1527 ? NE  ? A ARG 310 NE  
79  1 Y 1 A ARG 1527 ? CZ  ? A ARG 310 CZ  
80  1 Y 1 A ARG 1527 ? NH1 ? A ARG 310 NH1 
81  1 Y 1 A ARG 1527 ? NH2 ? A ARG 310 NH2 
82  1 Y 1 A ARG 1528 ? CG  ? A ARG 311 CG  
83  1 Y 1 A ARG 1528 ? CD  ? A ARG 311 CD  
84  1 Y 1 A ARG 1528 ? NE  ? A ARG 311 NE  
85  1 Y 1 A ARG 1528 ? CZ  ? A ARG 311 CZ  
86  1 Y 1 A ARG 1528 ? NH1 ? A ARG 311 NH1 
87  1 Y 1 A ARG 1528 ? NH2 ? A ARG 311 NH2 
88  1 Y 1 A TYR 1530 ? CG  ? A TYR 313 CG  
89  1 Y 1 A TYR 1530 ? CD1 ? A TYR 313 CD1 
90  1 Y 1 A TYR 1530 ? CD2 ? A TYR 313 CD2 
91  1 Y 1 A TYR 1530 ? CE1 ? A TYR 313 CE1 
92  1 Y 1 A TYR 1530 ? CE2 ? A TYR 313 CE2 
93  1 Y 1 A TYR 1530 ? CZ  ? A TYR 313 CZ  
94  1 Y 1 A TYR 1530 ? OH  ? A TYR 313 OH  
95  1 Y 1 A GLU 1548 ? CG  ? A GLU 331 CG  
96  1 Y 1 A GLU 1548 ? CD  ? A GLU 331 CD  
97  1 Y 1 A GLU 1548 ? OE1 ? A GLU 331 OE1 
98  1 Y 1 A GLU 1548 ? OE2 ? A GLU 331 OE2 
99  1 Y 1 A LYS 1578 ? CG  ? A LYS 361 CG  
100 1 Y 1 A LYS 1578 ? CD  ? A LYS 361 CD  
101 1 Y 1 A LYS 1578 ? CE  ? A LYS 361 CE  
102 1 Y 1 A LYS 1578 ? NZ  ? A LYS 361 NZ  
103 1 Y 1 A GLN 1581 ? CG  ? A GLN 364 CG  
104 1 Y 1 A GLN 1581 ? CD  ? A GLN 364 CD  
105 1 Y 1 A GLN 1581 ? OE1 ? A GLN 364 OE1 
106 1 Y 1 A GLN 1581 ? NE2 ? A GLN 364 NE2 
107 1 Y 1 A LYS 1595 ? CG  ? A LYS 378 CG  
108 1 Y 1 A LYS 1595 ? CD  ? A LYS 378 CD  
109 1 Y 1 A LYS 1595 ? CE  ? A LYS 378 CE  
110 1 Y 1 A LYS 1595 ? NZ  ? A LYS 378 NZ  
111 1 Y 1 A LYS 1599 ? CG  ? A LYS 382 CG  
112 1 Y 1 A LYS 1599 ? CD  ? A LYS 382 CD  
113 1 Y 1 A LYS 1599 ? CE  ? A LYS 382 CE  
114 1 Y 1 A LYS 1599 ? NZ  ? A LYS 382 NZ  
115 1 Y 1 A LYS 1609 ? CG  ? A LYS 392 CG  
116 1 Y 1 A LYS 1609 ? CD  ? A LYS 392 CD  
117 1 Y 1 A LYS 1609 ? CE  ? A LYS 392 CE  
118 1 Y 1 A LYS 1609 ? NZ  ? A LYS 392 NZ  
119 1 Y 1 A GLU 1612 ? OE1 ? A GLU 395 OE1 
120 1 Y 1 A GLU 1612 ? OE2 ? A GLU 395 OE2 
121 1 Y 1 A ARG 1624 ? CG  ? A ARG 407 CG  
122 1 Y 1 A ARG 1624 ? CD  ? A ARG 407 CD  
123 1 Y 1 A ARG 1624 ? NE  ? A ARG 407 NE  
124 1 Y 1 A ARG 1624 ? CZ  ? A ARG 407 CZ  
125 1 Y 1 A ARG 1624 ? NH1 ? A ARG 407 NH1 
126 1 Y 1 A ARG 1624 ? NH2 ? A ARG 407 NH2 
127 1 Y 1 A LYS 1631 ? CG  ? A LYS 414 CG  
128 1 Y 1 A LYS 1631 ? CD  ? A LYS 414 CD  
129 1 Y 1 A LYS 1631 ? CE  ? A LYS 414 CE  
130 1 Y 1 A LYS 1631 ? NZ  ? A LYS 414 NZ  
131 1 Y 1 A GLN 1641 ? CG  ? A GLN 424 CG  
132 1 Y 1 A GLN 1641 ? CD  ? A GLN 424 CD  
133 1 Y 1 A GLN 1641 ? OE1 ? A GLN 424 OE1 
134 1 Y 1 A GLN 1641 ? NE2 ? A GLN 424 NE2 
135 1 Y 1 A GLU 1644 ? CG  ? A GLU 427 CG  
136 1 Y 1 A GLU 1644 ? CD  ? A GLU 427 CD  
137 1 Y 1 A GLU 1644 ? OE1 ? A GLU 427 OE1 
138 1 Y 1 A GLU 1644 ? OE2 ? A GLU 427 OE2 
139 1 Y 1 A ARG 1662 ? CG  ? A ARG 445 CG  
140 1 Y 1 A ARG 1662 ? CD  ? A ARG 445 CD  
141 1 Y 1 A ARG 1662 ? NE  ? A ARG 445 NE  
142 1 Y 1 A ARG 1662 ? CZ  ? A ARG 445 CZ  
143 1 Y 1 A ARG 1662 ? NH1 ? A ARG 445 NH1 
144 1 Y 1 A ARG 1662 ? NH2 ? A ARG 445 NH2 
145 1 Y 1 A LYS 1664 ? CG  ? A LYS 447 CG  
146 1 Y 1 A LYS 1664 ? CD  ? A LYS 447 CD  
147 1 Y 1 A LYS 1664 ? CE  ? A LYS 447 CE  
148 1 Y 1 A LYS 1664 ? NZ  ? A LYS 447 NZ  
149 1 Y 1 A GLU 1666 ? CG  ? A GLU 449 CG  
150 1 Y 1 A GLU 1666 ? CD  ? A GLU 449 CD  
151 1 Y 1 A GLU 1666 ? OE1 ? A GLU 449 OE1 
152 1 Y 1 A GLU 1666 ? OE2 ? A GLU 449 OE2 
153 1 Y 1 A LYS 1684 ? CG  ? A LYS 467 CG  
154 1 Y 1 A LYS 1684 ? CD  ? A LYS 467 CD  
155 1 Y 1 A LYS 1684 ? CE  ? A LYS 467 CE  
156 1 Y 1 A LYS 1684 ? NZ  ? A LYS 467 NZ  
157 1 Y 1 A LYS 1695 ? CG  ? A LYS 478 CG  
158 1 Y 1 A LYS 1695 ? CD  ? A LYS 478 CD  
159 1 Y 1 A LYS 1695 ? CE  ? A LYS 478 CE  
160 1 Y 1 A LYS 1695 ? NZ  ? A LYS 478 NZ  
161 1 Y 1 A ILE 1696 ? CG1 ? A ILE 479 CG1 
162 1 Y 1 A ILE 1696 ? CG2 ? A ILE 479 CG2 
163 1 Y 1 A ILE 1696 ? CD1 ? A ILE 479 CD1 
164 1 Y 1 A ASP 1697 ? CG  ? A ASP 480 CG  
165 1 Y 1 A ASP 1697 ? OD1 ? A ASP 480 OD1 
166 1 Y 1 A ASP 1697 ? OD2 ? A ASP 480 OD2 
167 1 Y 1 A LYS 1699 ? CG  ? A LYS 482 CG  
168 1 Y 1 A LYS 1699 ? CD  ? A LYS 482 CD  
169 1 Y 1 A LYS 1699 ? CE  ? A LYS 482 CE  
170 1 Y 1 A LYS 1699 ? NZ  ? A LYS 482 NZ  
171 1 Y 1 A VAL 1700 ? CG1 ? A VAL 483 CG1 
172 1 Y 1 A VAL 1700 ? CG2 ? A VAL 483 CG2 
173 1 Y 1 A LYS 1702 ? CG  ? A LYS 485 CG  
174 1 Y 1 A LYS 1702 ? CD  ? A LYS 485 CD  
175 1 Y 1 A LYS 1702 ? CE  ? A LYS 485 CE  
176 1 Y 1 A LYS 1702 ? NZ  ? A LYS 485 NZ  
177 1 Y 1 A ARG 1710 ? CG  ? A ARG 493 CG  
178 1 Y 1 A ARG 1710 ? CD  ? A ARG 493 CD  
179 1 Y 1 A ARG 1710 ? NE  ? A ARG 493 NE  
180 1 Y 1 A ARG 1710 ? CZ  ? A ARG 493 CZ  
181 1 Y 1 A ARG 1710 ? NH1 ? A ARG 493 NH1 
182 1 Y 1 A ARG 1710 ? NH2 ? A ARG 493 NH2 
183 1 Y 1 A VAL 1711 ? CG1 ? A VAL 494 CG1 
184 1 Y 1 A VAL 1711 ? CG2 ? A VAL 494 CG2 
185 1 Y 1 A LYS 1713 ? CG  ? A LYS 496 CG  
186 1 Y 1 A LYS 1713 ? CD  ? A LYS 496 CD  
187 1 Y 1 A LYS 1713 ? CE  ? A LYS 496 CE  
188 1 Y 1 A LYS 1713 ? NZ  ? A LYS 496 NZ  
189 1 Y 1 B ARG 1291 ? CG  ? B ARG 74  CG  
190 1 Y 1 B ARG 1291 ? CD  ? B ARG 74  CD  
191 1 Y 1 B ARG 1291 ? NE  ? B ARG 74  NE  
192 1 Y 1 B ARG 1291 ? CZ  ? B ARG 74  CZ  
193 1 Y 1 B ARG 1291 ? NH1 ? B ARG 74  NH1 
194 1 Y 1 B ARG 1291 ? NH2 ? B ARG 74  NH2 
195 1 Y 1 B ASP 1303 ? CG  ? B ASP 86  CG  
196 1 Y 1 B ASP 1303 ? OD1 ? B ASP 86  OD1 
197 1 Y 1 B ASP 1303 ? OD2 ? B ASP 86  OD2 
198 1 Y 1 B GLU 1321 ? CG  ? B GLU 104 CG  
199 1 Y 1 B GLU 1321 ? CD  ? B GLU 104 CD  
200 1 Y 1 B GLU 1321 ? OE1 ? B GLU 104 OE1 
201 1 Y 1 B GLU 1321 ? OE2 ? B GLU 104 OE2 
202 1 Y 1 B LYS 1339 ? CG  ? B LYS 122 CG  
203 1 Y 1 B LYS 1339 ? CD  ? B LYS 122 CD  
204 1 Y 1 B LYS 1339 ? CE  ? B LYS 122 CE  
205 1 Y 1 B LYS 1339 ? NZ  ? B LYS 122 NZ  
206 1 Y 1 B GLN 1342 ? CG  ? B GLN 125 CG  
207 1 Y 1 B GLN 1342 ? CD  ? B GLN 125 CD  
208 1 Y 1 B GLN 1342 ? OE1 ? B GLN 125 OE1 
209 1 Y 1 B GLN 1342 ? NE2 ? B GLN 125 NE2 
210 1 Y 1 B ARG 1345 ? CG  ? B ARG 128 CG  
211 1 Y 1 B ARG 1345 ? CD  ? B ARG 128 CD  
212 1 Y 1 B ARG 1345 ? NE  ? B ARG 128 NE  
213 1 Y 1 B ARG 1345 ? CZ  ? B ARG 128 CZ  
214 1 Y 1 B ARG 1345 ? NH1 ? B ARG 128 NH1 
215 1 Y 1 B ARG 1345 ? NH2 ? B ARG 128 NH2 
216 1 Y 1 B GLU 1464 ? CG  ? B GLU 247 CG  
217 1 Y 1 B GLU 1464 ? CD  ? B GLU 247 CD  
218 1 Y 1 B GLU 1464 ? OE1 ? B GLU 247 OE1 
219 1 Y 1 B GLU 1464 ? OE2 ? B GLU 247 OE2 
220 1 Y 1 B GLU 1467 ? CG  ? B GLU 250 CG  
221 1 Y 1 B GLU 1467 ? CD  ? B GLU 250 CD  
222 1 Y 1 B GLU 1467 ? OE1 ? B GLU 250 OE1 
223 1 Y 1 B GLU 1467 ? OE2 ? B GLU 250 OE2 
224 1 Y 1 B THR 1468 ? OG1 ? B THR 251 OG1 
225 1 Y 1 B THR 1468 ? CG2 ? B THR 251 CG2 
226 1 Y 1 B GLU 1470 ? CG  ? B GLU 253 CG  
227 1 Y 1 B GLU 1470 ? CD  ? B GLU 253 CD  
228 1 Y 1 B GLU 1470 ? OE1 ? B GLU 253 OE1 
229 1 Y 1 B GLU 1470 ? OE2 ? B GLU 253 OE2 
230 1 Y 1 B ILE 1517 ? CG1 ? B ILE 300 CG1 
231 1 Y 1 B ILE 1517 ? CG2 ? B ILE 300 CG2 
232 1 Y 1 B ILE 1517 ? CD1 ? B ILE 300 CD1 
233 1 Y 1 B THR 1518 ? OG1 ? B THR 301 OG1 
234 1 Y 1 B THR 1518 ? CG2 ? B THR 301 CG2 
235 1 Y 1 B THR 1520 ? OG1 ? B THR 303 OG1 
236 1 Y 1 B THR 1520 ? CG2 ? B THR 303 CG2 
237 1 Y 1 B THR 1521 ? OG1 ? B THR 304 OG1 
238 1 Y 1 B THR 1521 ? CG2 ? B THR 304 CG2 
239 1 Y 1 B GLU 1525 ? CG  ? B GLU 308 CG  
240 1 Y 1 B GLU 1525 ? CD  ? B GLU 308 CD  
241 1 Y 1 B GLU 1525 ? OE1 ? B GLU 308 OE1 
242 1 Y 1 B GLU 1525 ? OE2 ? B GLU 308 OE2 
243 1 Y 1 B ARG 1526 ? CG  ? B ARG 309 CG  
244 1 Y 1 B ARG 1526 ? CD  ? B ARG 309 CD  
245 1 Y 1 B ARG 1526 ? NE  ? B ARG 309 NE  
246 1 Y 1 B ARG 1526 ? CZ  ? B ARG 309 CZ  
247 1 Y 1 B ARG 1526 ? NH1 ? B ARG 309 NH1 
248 1 Y 1 B ARG 1526 ? NH2 ? B ARG 309 NH2 
249 1 Y 1 B TYR 1530 ? CG  ? B TYR 313 CG  
250 1 Y 1 B TYR 1530 ? CD1 ? B TYR 313 CD1 
251 1 Y 1 B TYR 1530 ? CD2 ? B TYR 313 CD2 
252 1 Y 1 B TYR 1530 ? CE1 ? B TYR 313 CE1 
253 1 Y 1 B TYR 1530 ? CE2 ? B TYR 313 CE2 
254 1 Y 1 B TYR 1530 ? CZ  ? B TYR 313 CZ  
255 1 Y 1 B TYR 1530 ? OH  ? B TYR 313 OH  
256 1 Y 1 B LYS 1542 ? CG  ? B LYS 325 CG  
257 1 Y 1 B LYS 1542 ? CD  ? B LYS 325 CD  
258 1 Y 1 B LYS 1542 ? CE  ? B LYS 325 CE  
259 1 Y 1 B LYS 1542 ? NZ  ? B LYS 325 NZ  
260 1 Y 1 B LYS 1560 ? CG  ? B LYS 343 CG  
261 1 Y 1 B LYS 1560 ? CD  ? B LYS 343 CD  
262 1 Y 1 B LYS 1560 ? CE  ? B LYS 343 CE  
263 1 Y 1 B LYS 1560 ? NZ  ? B LYS 343 NZ  
264 1 Y 1 B LYS 1578 ? CG  ? B LYS 361 CG  
265 1 Y 1 B LYS 1578 ? CD  ? B LYS 361 CD  
266 1 Y 1 B LYS 1578 ? CE  ? B LYS 361 CE  
267 1 Y 1 B LYS 1578 ? NZ  ? B LYS 361 NZ  
268 1 Y 1 B LYS 1599 ? CG  ? B LYS 382 CG  
269 1 Y 1 B LYS 1599 ? CD  ? B LYS 382 CD  
270 1 Y 1 B LYS 1599 ? CE  ? B LYS 382 CE  
271 1 Y 1 B LYS 1599 ? NZ  ? B LYS 382 NZ  
272 1 Y 1 B GLN 1602 ? CG  ? B GLN 385 CG  
273 1 Y 1 B GLN 1602 ? CD  ? B GLN 385 CD  
274 1 Y 1 B GLN 1602 ? OE1 ? B GLN 385 OE1 
275 1 Y 1 B GLN 1602 ? NE2 ? B GLN 385 NE2 
276 1 Y 1 B LYS 1609 ? CG  ? B LYS 392 CG  
277 1 Y 1 B LYS 1609 ? CD  ? B LYS 392 CD  
278 1 Y 1 B LYS 1609 ? CE  ? B LYS 392 CE  
279 1 Y 1 B LYS 1609 ? NZ  ? B LYS 392 NZ  
280 1 Y 1 B GLU 1612 ? OE1 ? B GLU 395 OE1 
281 1 Y 1 B GLU 1612 ? OE2 ? B GLU 395 OE2 
282 1 Y 1 B LYS 1634 ? CG  ? B LYS 417 CG  
283 1 Y 1 B LYS 1634 ? CD  ? B LYS 417 CD  
284 1 Y 1 B LYS 1634 ? CE  ? B LYS 417 CE  
285 1 Y 1 B LYS 1634 ? NZ  ? B LYS 417 NZ  
286 1 Y 1 B GLN 1641 ? CG  ? B GLN 424 CG  
287 1 Y 1 B GLN 1641 ? CD  ? B GLN 424 CD  
288 1 Y 1 B GLN 1641 ? OE1 ? B GLN 424 OE1 
289 1 Y 1 B GLN 1641 ? NE2 ? B GLN 424 NE2 
290 1 Y 1 B GLU 1644 ? CG  ? B GLU 427 CG  
291 1 Y 1 B GLU 1644 ? CD  ? B GLU 427 CD  
292 1 Y 1 B GLU 1644 ? OE1 ? B GLU 427 OE1 
293 1 Y 1 B GLU 1644 ? OE2 ? B GLU 427 OE2 
294 1 Y 1 B ARG 1662 ? CG  ? B ARG 445 CG  
295 1 Y 1 B ARG 1662 ? CD  ? B ARG 445 CD  
296 1 Y 1 B ARG 1662 ? NE  ? B ARG 445 NE  
297 1 Y 1 B ARG 1662 ? CZ  ? B ARG 445 CZ  
298 1 Y 1 B ARG 1662 ? NH1 ? B ARG 445 NH1 
299 1 Y 1 B ARG 1662 ? NH2 ? B ARG 445 NH2 
300 1 Y 1 B LYS 1684 ? CG  ? B LYS 467 CG  
301 1 Y 1 B LYS 1684 ? CD  ? B LYS 467 CD  
302 1 Y 1 B LYS 1684 ? CE  ? B LYS 467 CE  
303 1 Y 1 B LYS 1684 ? NZ  ? B LYS 467 NZ  
304 1 Y 1 B LYS 1695 ? CG  ? B LYS 478 CG  
305 1 Y 1 B LYS 1695 ? CD  ? B LYS 478 CD  
306 1 Y 1 B LYS 1695 ? CE  ? B LYS 478 CE  
307 1 Y 1 B LYS 1695 ? NZ  ? B LYS 478 NZ  
308 1 Y 1 B ILE 1696 ? CG1 ? B ILE 479 CG1 
309 1 Y 1 B ILE 1696 ? CG2 ? B ILE 479 CG2 
310 1 Y 1 B ILE 1696 ? CD1 ? B ILE 479 CD1 
311 1 Y 1 B LYS 1702 ? CG  ? B LYS 485 CG  
312 1 Y 1 B LYS 1702 ? CD  ? B LYS 485 CD  
313 1 Y 1 B LYS 1702 ? CE  ? B LYS 485 CE  
314 1 Y 1 B LYS 1702 ? NZ  ? B LYS 485 NZ  
315 1 Y 1 B ARG 1710 ? CG  ? B ARG 493 CG  
316 1 Y 1 B ARG 1710 ? CD  ? B ARG 493 CD  
317 1 Y 1 B ARG 1710 ? NE  ? B ARG 493 NE  
318 1 Y 1 B ARG 1710 ? CZ  ? B ARG 493 CZ  
319 1 Y 1 B ARG 1710 ? NH1 ? B ARG 493 NH1 
320 1 Y 1 B ARG 1710 ? NH2 ? B ARG 493 NH2 
321 1 Y 1 B VAL 1711 ? CG1 ? B VAL 494 CG1 
322 1 Y 1 B VAL 1711 ? CG2 ? B VAL 494 CG2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.15rc1_3423: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                     2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                     3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                     4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   105.39 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8JE6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     80.978 
_cell.length_a_esd                 ? 
_cell.length_b                     69.798 
_cell.length_b_esd                 ? 
_cell.length_c                     106.839 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8JE6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8JE6 
_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             2.51 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.90 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Morpheus III-C12:
1% Nucleosides mix, 0.1 M Buffer System 3  and 37.5% Precipitant Mix 4.
;
_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         2022-02-18 
_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   0.9763 
_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        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8JE6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.88 
_reflns.d_resolution_low                               78.072 
_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                                     26195 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.0 
_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                                2.625 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.88 
_reflns_shell.d_res_low                                     2.93 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1271 
_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                               6.3 
_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                               0.342 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.4 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8JE6 
_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                            2.883 
_refine.ls_d_res_low                             78.072 
_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                     26150 
_refine.ls_number_reflns_R_free                  1210 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.81 
_refine.ls_percent_reflns_R_free                 4.63 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2020 
_refine.ls_R_factor_R_free                       0.2789 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1983 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      7F9A 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_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                 32.11 
_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                            0.51 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        7536 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         114 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               7650 
_refine_hist.d_res_high                       2.883 
_refine_hist.d_res_low                        78.072 
# 
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' ? 0.010 ? 7867  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.297 ? 10728 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.110 ? 4629  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.070 ? 1174  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010 ? 1397  ? 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' 2.8832 2.9987 . . 140 2695 99.00  . . . . 0.3037 . . . . . . . . . . . 0.3820 
'X-RAY DIFFRACTION' 2.9987 3.1351 . . 125 2777 100.00 . . . . 0.2852 . . . . . . . . . . . 0.3529 
'X-RAY DIFFRACTION' 3.1351 3.3004 . . 116 2754 100.00 . . . . 0.2688 . . . . . . . . . . . 0.3619 
'X-RAY DIFFRACTION' 3.3004 3.5072 . . 135 2762 100.00 . . . . 0.2210 . . . . . . . . . . . 0.3062 
'X-RAY DIFFRACTION' 3.5072 3.7780 . . 135 2759 100.00 . . . . 0.1959 . . . . . . . . . . . 0.3030 
'X-RAY DIFFRACTION' 3.7780 4.1582 . . 152 2750 100.00 . . . . 0.1740 . . . . . . . . . . . 0.2893 
'X-RAY DIFFRACTION' 4.1582 4.7598 . . 136 2796 100.00 . . . . 0.1486 . . . . . . . . . . . 0.2323 
'X-RAY DIFFRACTION' 4.7598 5.9965 . . 122 2796 100.00 . . . . 0.1735 . . . . . . . . . . . 0.2084 
'X-RAY DIFFRACTION' 5.9965 78.072 . . 149 2851 100.00 . . . . 0.1918 . . . . . . . . . . . 0.2656 
# 
_struct.entry_id                     8JE6 
_struct.title                        
'Crystal Structure of Anopheles culicifacies Prolyl-tRNA Synthetase (AcPRS) in complex with Halofuginone and ATP analogue' 
_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        8JE6 
_struct_keywords.text            
'Malaria, Vector, Anopheles, Mosquito, Larvicidal, Aminoacyl-tRNA synthetase, LIGASE, LIGASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   LIGASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A182M1F8_9DIPT 
_struct_ref.pdbx_db_accession          A0A182M1F8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TRLGLEATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRHWSFAIWKAIRNWFDAEITRLGVKECYFPIFVSRAALEREK
THIADFAPEVAWVTKSGDSELAEPIAVRPTSETVMYPAYAKWIQSYRDLPIRLNQWNNVVRWEFKHPQPFLRTREFLWQE
GHTAFATQKEADEEVLTILDLYAKVYTDLLAIPVVKGRKTEKEKFAGGDYTTTVEAYISASGRAIQGATSHHLGQNFSRM
FDIVYEHPETKEKEYVFQNSWGITTRTIGVMIMVHADNQGLVLPPRVACIQVVIVPCGITATTTDDERRRLYESCRELEQ
TFVKAGIRCEGDYRDNYSPGWKYNHWELKGVPVRIELGFKDLQNDQFVAVRRDNGAKQTIKRAQATVEMPKLLETIHTSM
YERAERDLQSHTKLTKQWAEFLQFLETKNIIMAPFCGEISCEDRIKAESARDDAEAEAGAPAMGAKSLCIPFEQPAKIDP
KVDKCVHPACGRVAKFYTLFGRSY
;
_struct_ref.pdbx_align_begin           1219 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8JE6 A 2 ? 505 ? A0A182M1F8 1219 ? 1722 ? 1219 1722 
2 1 8JE6 B 2 ? 505 ? A0A182M1F8 1219 ? 1722 ? 1219 1722 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8JE6 MET A 1 ? UNP A0A182M1F8 ? ? 'initiating methionine' 1218 1 
2 8JE6 MET B 1 ? UNP A0A182M1F8 ? ? 'initiating methionine' 1218 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 6050  ? 
1 MORE         -45   ? 
1 'SSA (A^2)'  37980 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_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 ASN A 13  ? GLY A 25  ? ASN A 1230 GLY A 1242 1 ? 13 
HELX_P HELX_P2  AA2 ARG A 40  ? GLY A 62  ? ARG A 1257 GLY A 1279 1 ? 23 
HELX_P HELX_P3  AA3 ARG A 74  ? GLU A 78  ? ARG A 1291 GLU A 1295 1 ? 5  
HELX_P HELX_P4  AA4 PHE A 87  ? GLU A 90  ? PHE A 1304 GLU A 1307 5 ? 4  
HELX_P HELX_P5  AA5 SER A 112 ? ILE A 124 ? SER A 1329 ILE A 1341 1 ? 13 
HELX_P HELX_P6  AA6 SER A 126 ? LEU A 130 ? SER A 1343 LEU A 1347 5 ? 5  
HELX_P HELX_P7  AA7 THR A 168 ? LEU A 190 ? THR A 1385 LEU A 1407 1 ? 23 
HELX_P HELX_P8  AA8 GLN A 236 ? PHE A 242 ? GLN A 1453 PHE A 1459 1 ? 7  
HELX_P HELX_P9  AA9 THR A 266 ? ALA A 277 ? THR A 1483 ALA A 1494 1 ? 12 
HELX_P HELX_P10 AB1 THR A 305 ? ALA A 326 ? THR A 1522 ALA A 1543 1 ? 22 
HELX_P HELX_P11 AB2 SER A 339 ? LYS A 350 ? SER A 1556 LYS A 1567 1 ? 12 
HELX_P HELX_P12 AB3 GLY A 359 ? ASN A 365 ? GLY A 1576 ASN A 1582 1 ? 7  
HELX_P HELX_P13 AB4 GLN A 385 ? HIS A 412 ? GLN A 1602 HIS A 1629 1 ? 28 
HELX_P HELX_P14 AB5 GLN A 418 ? THR A 428 ? GLN A 1635 THR A 1645 1 ? 11 
HELX_P HELX_P15 AB6 GLU A 439 ? ALA A 451 ? GLU A 1656 ALA A 1668 1 ? 13 
HELX_P HELX_P16 AB7 ASN B 13  ? GLY B 25  ? ASN B 1230 GLY B 1242 1 ? 13 
HELX_P HELX_P17 AB8 ARG B 40  ? LEU B 61  ? ARG B 1257 LEU B 1278 1 ? 22 
HELX_P HELX_P18 AB9 ARG B 74  ? GLU B 78  ? ARG B 1291 GLU B 1295 1 ? 5  
HELX_P HELX_P19 AC1 PHE B 87  ? GLU B 90  ? PHE B 1304 GLU B 1307 5 ? 4  
HELX_P HELX_P20 AC2 SER B 112 ? ILE B 124 ? SER B 1329 ILE B 1341 1 ? 13 
HELX_P HELX_P21 AC3 SER B 126 ? LEU B 130 ? SER B 1343 LEU B 1347 5 ? 5  
HELX_P HELX_P22 AC4 THR B 168 ? LEU B 190 ? THR B 1385 LEU B 1407 1 ? 23 
HELX_P HELX_P23 AC5 GLN B 236 ? ASP B 243 ? GLN B 1453 ASP B 1460 1 ? 8  
HELX_P HELX_P24 AC6 THR B 266 ? ALA B 277 ? THR B 1483 ALA B 1494 1 ? 12 
HELX_P HELX_P25 AC7 THR B 305 ? ALA B 326 ? THR B 1522 ALA B 1543 1 ? 22 
HELX_P HELX_P26 AC8 SER B 339 ? GLY B 351 ? SER B 1556 GLY B 1568 1 ? 13 
HELX_P HELX_P27 AC9 GLY B 359 ? ASN B 365 ? GLY B 1576 ASN B 1582 1 ? 7  
HELX_P HELX_P28 AD1 GLN B 385 ? HIS B 412 ? GLN B 1602 HIS B 1629 1 ? 28 
HELX_P HELX_P29 AD2 GLN B 418 ? THR B 428 ? GLN B 1635 THR B 1645 1 ? 11 
HELX_P HELX_P30 AD3 GLU B 439 ? ALA B 451 ? GLU B 1656 ALA B 1668 1 ? 13 
# 
_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 
metalc1  metalc ? ? A CYS 437 SG  ? ? ? 1_555 F ZN . ZN ? ? A CYS 1654 A ZN 1804 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc2  metalc ? ? A CYS 442 SG  ? ? ? 1_555 F ZN . ZN ? ? A CYS 1659 A ZN 1804 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc3  metalc ? ? A CYS 486 SG  ? ? ? 1_555 F ZN . ZN ? ? A CYS 1703 A ZN 1804 1_555 ? ? ? ? ? ? ? 2.445 ? ? 
metalc4  metalc ? ? A CYS 491 SG  ? ? ? 1_555 F ZN . ZN ? ? A CYS 1708 A ZN 1804 1_555 ? ? ? ? ? ? ? 2.121 ? ? 
metalc5  metalc ? ? C ANP .   O2G ? ? ? 1_555 E MG . MG ? ? A ANP 1801 A MG 1803 1_555 ? ? ? ? ? ? ? 2.154 ? ? 
metalc6  metalc ? ? C ANP .   O2B ? ? ? 1_555 E MG . MG ? ? A ANP 1801 A MG 1803 1_555 ? ? ? ? ? ? ? 2.580 ? ? 
metalc7  metalc ? ? B CYS 437 SG  ? ? ? 1_555 J ZN . ZN ? ? B CYS 1654 B ZN 1804 1_555 ? ? ? ? ? ? ? 2.371 ? ? 
metalc8  metalc ? ? B CYS 442 SG  ? ? ? 1_555 J ZN . ZN ? ? B CYS 1659 B ZN 1804 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc9  metalc ? ? B CYS 486 SG  ? ? ? 1_555 J ZN . ZN ? ? B CYS 1703 B ZN 1804 1_555 ? ? ? ? ? ? ? 2.723 ? ? 
metalc10 metalc ? ? B CYS 491 SG  ? ? ? 1_555 J ZN . ZN ? ? B CYS 1708 B ZN 1804 1_555 ? ? ? ? ? ? ? 2.658 ? ? 
metalc11 metalc ? ? G ANP .   O2G ? ? ? 1_555 I MG . MG ? ? B ANP 1801 B MG 1803 1_555 ? ? ? ? ? ? ? 2.636 ? ? 
metalc12 metalc ? ? G ANP .   O2B ? ? ? 1_555 I MG . MG ? ? B ANP 1801 B MG 1803 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 437 ? A CYS 1654 ? 1_555 ZN ? F ZN . ? A ZN 1804 ? 1_555 SG  ? A CYS 442 ? A CYS 1659 ? 1_555 112.9 ? 
2  SG  ? A CYS 437 ? A CYS 1654 ? 1_555 ZN ? F ZN . ? A ZN 1804 ? 1_555 SG  ? A CYS 486 ? A CYS 1703 ? 1_555 124.5 ? 
3  SG  ? A CYS 442 ? A CYS 1659 ? 1_555 ZN ? F ZN . ? A ZN 1804 ? 1_555 SG  ? A CYS 486 ? A CYS 1703 ? 1_555 111.1 ? 
4  SG  ? A CYS 437 ? A CYS 1654 ? 1_555 ZN ? F ZN . ? A ZN 1804 ? 1_555 SG  ? A CYS 491 ? A CYS 1708 ? 1_555 93.2  ? 
5  SG  ? A CYS 442 ? A CYS 1659 ? 1_555 ZN ? F ZN . ? A ZN 1804 ? 1_555 SG  ? A CYS 491 ? A CYS 1708 ? 1_555 108.4 ? 
6  SG  ? A CYS 486 ? A CYS 1703 ? 1_555 ZN ? F ZN . ? A ZN 1804 ? 1_555 SG  ? A CYS 491 ? A CYS 1708 ? 1_555 103.3 ? 
7  O2G ? C ANP .   ? A ANP 1801 ? 1_555 MG ? E MG . ? A MG 1803 ? 1_555 O2B ? C ANP .   ? A ANP 1801 ? 1_555 60.5  ? 
8  SG  ? B CYS 437 ? B CYS 1654 ? 1_555 ZN ? J ZN . ? B ZN 1804 ? 1_555 SG  ? B CYS 442 ? B CYS 1659 ? 1_555 114.0 ? 
9  SG  ? B CYS 437 ? B CYS 1654 ? 1_555 ZN ? J ZN . ? B ZN 1804 ? 1_555 SG  ? B CYS 486 ? B CYS 1703 ? 1_555 109.8 ? 
10 SG  ? B CYS 442 ? B CYS 1659 ? 1_555 ZN ? J ZN . ? B ZN 1804 ? 1_555 SG  ? B CYS 486 ? B CYS 1703 ? 1_555 95.9  ? 
11 SG  ? B CYS 437 ? B CYS 1654 ? 1_555 ZN ? J ZN . ? B ZN 1804 ? 1_555 SG  ? B CYS 491 ? B CYS 1708 ? 1_555 150.2 ? 
12 SG  ? B CYS 442 ? B CYS 1659 ? 1_555 ZN ? J ZN . ? B ZN 1804 ? 1_555 SG  ? B CYS 491 ? B CYS 1708 ? 1_555 93.0  ? 
13 SG  ? B CYS 486 ? B CYS 1703 ? 1_555 ZN ? J ZN . ? B ZN 1804 ? 1_555 SG  ? B CYS 491 ? B CYS 1708 ? 1_555 78.0  ? 
14 O2G ? G ANP .   ? B ANP 1801 ? 1_555 MG ? I MG . ? B MG 1803 ? 1_555 O2B ? G ANP .   ? B ANP 1801 ? 1_555 63.7  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 130 A . ? LEU 1347 A PRO 131 A ? PRO 1348 A 1 6.04  
2 LEU 130 B . ? LEU 1347 B PRO 131 B ? PRO 1348 B 1 10.00 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 11 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 5  ? 
AA6 ? 2  ? 
AA7 ? 11 ? 
AA8 ? 2  ? 
AA9 ? 5  ? 
# 
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 
AA2 1  2  ? parallel      
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? anti-parallel 
AA2 8  9  ? anti-parallel 
AA2 9  10 ? anti-parallel 
AA2 10 11 ? parallel      
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? anti-parallel 
AA3 4  5  ? anti-parallel 
AA3 5  6  ? anti-parallel 
AA4 1  2  ? anti-parallel 
AA5 1  2  ? parallel      
AA5 2  3  ? parallel      
AA5 3  4  ? anti-parallel 
AA5 4  5  ? anti-parallel 
AA6 1  2  ? anti-parallel 
AA7 1  2  ? parallel      
AA7 2  3  ? anti-parallel 
AA7 3  4  ? anti-parallel 
AA7 4  5  ? anti-parallel 
AA7 5  6  ? anti-parallel 
AA7 6  7  ? anti-parallel 
AA7 7  8  ? anti-parallel 
AA7 8  9  ? anti-parallel 
AA7 9  10 ? anti-parallel 
AA7 10 11 ? parallel      
AA8 1  2  ? anti-parallel 
AA9 1  2  ? parallel      
AA9 2  3  ? parallel      
AA9 3  4  ? anti-parallel 
AA9 4  5  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ILE A 28  ? GLU A 29  ? ILE A 1245 GLU A 1246 
AA1 2  ILE A 38  ? LEU A 39  ? ILE A 1255 LEU A 1256 
AA2 1  LYS A 64  ? GLU A 65  ? LYS A 1281 GLU A 1282 
AA2 2  ILE A 132 ? VAL A 141 ? ILE A 1349 VAL A 1358 
AA2 3  GLU A 156 ? PHE A 166 ? GLU A 1373 PHE A 1383 
AA2 4  PHE A 258 ? THR A 265 ? PHE A 1475 THR A 1482 
AA2 5  ARG A 224 ? GLY A 235 ? ARG A 1441 GLY A 1452 
AA2 6  TYR A 211 ? ILE A 219 ? TYR A 1428 ILE A 1436 
AA2 7  VAL A 196 ? ARG A 199 ? VAL A 1413 ARG A 1416 
AA2 8  LYS A 467 ? PRO A 472 ? LYS A 1684 PRO A 1689 
AA2 9  PHE A 497 ? GLY A 502 ? PHE A 1714 GLY A 1719 
AA2 10 ILE A 431 ? PHE A 436 ? ILE A 1648 PHE A 1653 
AA2 11 THR A 413 ? LEU A 415 ? THR A 1630 LEU A 1632 
AA3 1  PHE A 71  ? SER A 73  ? PHE A 1288 SER A 1290 
AA3 2  SER A 100 ? VAL A 108 ? SER A 1317 VAL A 1325 
AA3 3  ALA A 92  ? SER A 97  ? ALA A 1309 SER A 1314 
AA3 4  ALA B 92  ? SER B 97  ? ALA B 1309 SER B 1314 
AA3 5  SER B 100 ? VAL B 108 ? SER B 1317 VAL B 1325 
AA3 6  PHE B 71  ? SER B 73  ? PHE B 1288 SER B 1290 
AA4 1  VAL A 245 ? GLU A 247 ? VAL A 1462 GLU A 1464 
AA4 2  LYS A 254 ? TYR A 256 ? LYS A 1471 TYR A 1473 
AA5 1  CYS A 330 ? GLY A 332 ? CYS A 1547 GLY A 1549 
AA5 2  VAL A 293 ? PRO A 297 ? VAL A 1510 PRO A 1514 
AA5 3  VAL A 354 ? LEU A 358 ? VAL A 1571 LEU A 1575 
AA5 4  GLN A 367 ? ARG A 372 ? GLN A 1584 ARG A 1589 
AA5 5  LYS A 378 ? LYS A 382 ? LYS A 1595 LYS A 1599 
AA6 1  ILE B 28  ? TYR B 30  ? ILE B 1245 TYR B 1247 
AA6 2  TYR B 37  ? LEU B 39  ? TYR B 1254 LEU B 1256 
AA7 1  LYS B 64  ? GLU B 65  ? LYS B 1281 GLU B 1282 
AA7 2  ILE B 132 ? VAL B 141 ? ILE B 1349 VAL B 1358 
AA7 3  GLU B 156 ? PHE B 166 ? GLU B 1373 PHE B 1383 
AA7 4  PHE B 258 ? THR B 265 ? PHE B 1475 THR B 1482 
AA7 5  ARG B 224 ? GLY B 235 ? ARG B 1441 GLY B 1452 
AA7 6  TYR B 211 ? ILE B 219 ? TYR B 1428 ILE B 1436 
AA7 7  VAL B 196 ? ARG B 199 ? VAL B 1413 ARG B 1416 
AA7 8  LYS B 467 ? PRO B 472 ? LYS B 1684 PRO B 1689 
AA7 9  PHE B 497 ? GLY B 502 ? PHE B 1714 GLY B 1719 
AA7 10 ILE B 431 ? PHE B 436 ? ILE B 1648 PHE B 1653 
AA7 11 THR B 413 ? LEU B 415 ? THR B 1630 LEU B 1632 
AA8 1  VAL B 245 ? GLU B 247 ? VAL B 1462 GLU B 1464 
AA8 2  LYS B 254 ? TYR B 256 ? LYS B 1471 TYR B 1473 
AA9 1  CYS B 330 ? GLY B 332 ? CYS B 1547 GLY B 1549 
AA9 2  VAL B 293 ? PRO B 297 ? VAL B 1510 PRO B 1514 
AA9 3  VAL B 354 ? LEU B 358 ? VAL B 1571 LEU B 1575 
AA9 4  GLN B 367 ? ARG B 372 ? GLN B 1584 ARG B 1589 
AA9 5  LYS B 378 ? LYS B 382 ? LYS B 1595 LYS B 1599 
# 
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 GLU A 29  ? N GLU A 1246 O ILE A 38  ? O ILE A 1255 
AA2 1  2  N LYS A 64  ? N LYS A 1281 O ARG A 133 ? O ARG A 1350 
AA2 2  3  N ASN A 138 ? N ASN A 1355 O TRP A 159 ? O TRP A 1376 
AA2 3  4  N PHE A 166 ? N PHE A 1383 O PHE A 258 ? O PHE A 1475 
AA2 4  5  O SER A 261 ? O SER A 1478 N HIS A 232 ? N HIS A 1449 
AA2 5  6  O ARG A 224 ? O ARG A 1441 N ILE A 219 ? N ILE A 1436 
AA2 6  7  O GLU A 216 ? O GLU A 1433 N VAL A 196 ? N VAL A 1413 
AA2 7  8  N ARG A 199 ? N ARG A 1416 O ILE A 471 ? O ILE A 1688 
AA2 8  9  N LEU A 469 ? N LEU A 1686 O LEU A 500 ? O LEU A 1717 
AA2 9  10 O PHE A 497 ? O PHE A 1714 N PHE A 436 ? N PHE A 1653 
AA2 10 11 O ILE A 431 ? O ILE A 1648 N LYS A 414 ? N LYS A 1631 
AA3 1  2  N VAL A 72  ? N VAL A 1289 O ALA A 107 ? O ALA A 1324 
AA3 2  3  O SER A 100 ? O SER A 1317 N SER A 97  ? N SER A 1314 
AA3 3  4  N LYS A 96  ? N LYS A 1313 O TRP B 93  ? O TRP B 1310 
AA3 4  5  N SER B 97  ? N SER B 1314 O SER B 100 ? O SER B 1317 
AA3 5  6  O ALA B 107 ? O ALA B 1324 N VAL B 72  ? N VAL B 1289 
AA4 1  2  N TYR A 246 ? N TYR A 1463 O GLU A 255 ? O GLU A 1472 
AA5 1  2  O GLU A 331 ? O GLU A 1548 N VAL A 293 ? N VAL A 1510 
AA5 2  3  N VAL A 294 ? N VAL A 1511 O ILE A 356 ? O ILE A 1573 
AA5 3  4  N ARG A 355 ? N ARG A 1572 O VAL A 371 ? O VAL A 1588 
AA5 4  5  N PHE A 368 ? N PHE A 1585 O ILE A 381 ? O ILE A 1598 
AA6 1  2  N GLU B 29  ? N GLU B 1246 O ILE B 38  ? O ILE B 1255 
AA7 1  2  N LYS B 64  ? N LYS B 1281 O ARG B 133 ? O ARG B 1350 
AA7 2  3  N ASN B 138 ? N ASN B 1355 O TRP B 159 ? O TRP B 1376 
AA7 3  4  N PHE B 166 ? N PHE B 1383 O PHE B 258 ? O PHE B 1475 
AA7 4  5  O SER B 261 ? O SER B 1478 N HIS B 232 ? N HIS B 1449 
AA7 5  6  O ARG B 224 ? O ARG B 1441 N ILE B 219 ? N ILE B 1436 
AA7 6  7  O GLU B 216 ? O GLU B 1433 N VAL B 196 ? N VAL B 1413 
AA7 7  8  N ARG B 199 ? N ARG B 1416 O ILE B 471 ? O ILE B 1688 
AA7 8  9  N LEU B 469 ? N LEU B 1686 O LEU B 500 ? O LEU B 1717 
AA7 9  10 O THR B 499 ? O THR B 1716 N ALA B 434 ? N ALA B 1651 
AA7 10 11 O MET B 433 ? O MET B 1650 N LYS B 414 ? N LYS B 1631 
AA8 1  2  N TYR B 246 ? N TYR B 1463 O GLU B 255 ? O GLU B 1472 
AA9 1  2  O GLU B 331 ? O GLU B 1548 N VAL B 293 ? N VAL B 1510 
AA9 2  3  N VAL B 294 ? N VAL B 1511 O ILE B 356 ? O ILE B 1573 
AA9 3  4  N GLU B 357 ? N GLU B 1574 O VAL B 369 ? O VAL B 1586 
AA9 4  5  N ALA B 370 ? N ALA B 1587 O GLN B 379 ? O GLN B 1596 
# 
_pdbx_entry_details.entry_id                   8JE6 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ILE 1649 ? ? CA A ILE 1649 ? ? C  A ILE 1649 ? ? 98.64  111.60 -12.96 2.00 N 
2 1 C  B ARG 1326 ? ? N  B PRO 1327 ? ? CA B PRO 1327 ? ? 133.71 119.30 14.41  1.50 Y 
3 1 C  B ARG 1326 ? ? N  B PRO 1327 ? ? CD B PRO 1327 ? ? 110.64 128.40 -17.76 2.10 Y 
4 1 C  B HIS 1705 ? ? N  B PRO 1706 ? ? CA B PRO 1706 ? ? 129.86 119.30 10.56  1.50 Y 
5 1 C  B HIS 1705 ? ? N  B PRO 1706 ? ? CD B PRO 1706 ? ? 111.67 128.40 -16.73 2.10 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 ASN A 1230 ? ? 64.79   74.52   
2  1 THR A 1328 ? ? 177.24  168.00  
3  1 ASP A 1427 ? ? -94.86  -71.92  
4  1 ASP A 1495 ? ? -104.03 -160.16 
5  1 THR A 1518 ? ? 69.34   -125.22 
6  1 THR A 1645 ? ? -95.88  44.93   
7  1 LYS A 1646 ? ? 70.77   37.21   
8  1 ALA A 1694 ? ? 78.58   147.69  
9  1 ARG A 1710 ? ? -64.78  69.45   
10 1 PHE A 1714 ? ? -170.19 -173.09 
11 1 ASN B 1230 ? ? 64.32   73.89   
12 1 ASP B 1495 ? ? -104.27 -162.71 
13 1 THR B 1518 ? ? -76.08  -166.72 
14 1 THR B 1520 ? ? -85.15  31.59   
15 1 TYR B 1551 ? ? -114.91 62.77   
16 1 ASN B 1592 ? ? 67.28   -8.51   
17 1 THR B 1645 ? ? -81.69  34.68   
18 1 LEU B 1686 ? ? -92.40  -63.34  
19 1 ALA B 1707 ? ? -98.27  -69.56  
20 1 CYS B 1708 ? ? 52.95   -159.46 
21 1 ARG B 1710 ? ? 55.32   -66.27  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.3878 
_pdbx_refine_tls.origin_y         -12.0956 
_pdbx_refine_tls.origin_z         26.5060 
_pdbx_refine_tls.T[1][1]          0.3539 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0087 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0039 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2708 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0191 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.3080 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.1004 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.1477 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0970 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.6624 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.1226 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.7730 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0277 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0235 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.1004 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0071 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0842 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0336 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0321 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0758 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0367 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
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 1218 ? A MET 1   
2  1 Y 1 A THR 1219 ? A THR 2   
3  1 Y 1 A ARG 1220 ? A ARG 3   
4  1 Y 1 A LEU 1221 ? A LEU 4   
5  1 Y 1 A GLY 1222 ? A GLY 5   
6  1 Y 1 A GLU 1297 ? A GLU 80  
7  1 Y 1 A LYS 1298 ? A LYS 81  
8  1 Y 1 A THR 1299 ? A THR 82  
9  1 Y 1 A HIS 1300 ? A HIS 83  
10 1 Y 1 A ILE 1301 ? A ILE 84  
11 1 Y 1 A ALA 1302 ? A ALA 85  
12 1 Y 1 A ARG 1669 ? A ARG 452 
13 1 Y 1 A ASP 1670 ? A ASP 453 
14 1 Y 1 A ASP 1671 ? A ASP 454 
15 1 Y 1 A ALA 1672 ? A ALA 455 
16 1 Y 1 A GLU 1673 ? A GLU 456 
17 1 Y 1 A ALA 1674 ? A ALA 457 
18 1 Y 1 A GLU 1675 ? A GLU 458 
19 1 Y 1 A ALA 1676 ? A ALA 459 
20 1 Y 1 A GLY 1677 ? A GLY 460 
21 1 Y 1 A ALA 1678 ? A ALA 461 
22 1 Y 1 B MET 1218 ? B MET 1   
23 1 Y 1 B THR 1219 ? B THR 2   
24 1 Y 1 B ARG 1220 ? B ARG 3   
25 1 Y 1 B LEU 1221 ? B LEU 4   
26 1 Y 1 B GLY 1222 ? B GLY 5   
27 1 Y 1 B GLU 1297 ? B GLU 80  
28 1 Y 1 B LYS 1298 ? B LYS 81  
29 1 Y 1 B THR 1299 ? B THR 82  
30 1 Y 1 B HIS 1300 ? B HIS 83  
31 1 Y 1 B ILE 1301 ? B ILE 84  
32 1 Y 1 B ALA 1302 ? B ALA 85  
33 1 Y 1 B ARG 1669 ? B ARG 452 
34 1 Y 1 B ASP 1670 ? B ASP 453 
35 1 Y 1 B ASP 1671 ? B ASP 454 
36 1 Y 1 B ALA 1672 ? B ALA 455 
37 1 Y 1 B GLU 1673 ? B GLU 456 
38 1 Y 1 B ALA 1674 ? B ALA 457 
39 1 Y 1 B GLU 1675 ? B GLU 458 
40 1 Y 1 B ALA 1676 ? B ALA 459 
41 1 Y 1 B GLY 1677 ? B GLY 460 
42 1 Y 1 B ALA 1678 ? B ALA 461 
43 1 Y 1 B PRO 1679 ? B PRO 462 
44 1 Y 1 B ALA 1680 ? B ALA 463 
# 
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  
ANP PG     P  N N 14  
ANP O1G    O  N N 15  
ANP O2G    O  N N 16  
ANP O3G    O  N N 17  
ANP PB     P  N N 18  
ANP O1B    O  N N 19  
ANP O2B    O  N N 20  
ANP N3B    N  N N 21  
ANP PA     P  N N 22  
ANP O1A    O  N N 23  
ANP O2A    O  N N 24  
ANP O3A    O  N N 25  
ANP "O5'"  O  N N 26  
ANP "C5'"  C  N N 27  
ANP "C4'"  C  N R 28  
ANP "O4'"  O  N N 29  
ANP "C3'"  C  N S 30  
ANP "O3'"  O  N N 31  
ANP "C2'"  C  N R 32  
ANP "O2'"  O  N N 33  
ANP "C1'"  C  N R 34  
ANP N9     N  Y N 35  
ANP C8     C  Y N 36  
ANP N7     N  Y N 37  
ANP C5     C  Y N 38  
ANP C6     C  Y N 39  
ANP N6     N  N N 40  
ANP N1     N  Y N 41  
ANP C2     C  Y N 42  
ANP N3     N  Y N 43  
ANP C4     C  Y N 44  
ANP HOG2   H  N N 45  
ANP HOG3   H  N N 46  
ANP HOB2   H  N N 47  
ANP HNB1   H  N N 48  
ANP HOA2   H  N N 49  
ANP "H5'1" H  N N 50  
ANP "H5'2" H  N N 51  
ANP "H4'"  H  N N 52  
ANP "H3'"  H  N N 53  
ANP "HO3'" H  N N 54  
ANP "H2'"  H  N N 55  
ANP "HO2'" H  N N 56  
ANP "H1'"  H  N N 57  
ANP H8     H  N N 58  
ANP HN61   H  N N 59  
ANP HN62   H  N N 60  
ANP H2     H  N N 61  
ARG N      N  N N 62  
ARG CA     C  N S 63  
ARG C      C  N N 64  
ARG O      O  N N 65  
ARG CB     C  N N 66  
ARG CG     C  N N 67  
ARG CD     C  N N 68  
ARG NE     N  N N 69  
ARG CZ     C  N N 70  
ARG NH1    N  N N 71  
ARG NH2    N  N N 72  
ARG OXT    O  N N 73  
ARG H      H  N N 74  
ARG H2     H  N N 75  
ARG HA     H  N N 76  
ARG HB2    H  N N 77  
ARG HB3    H  N N 78  
ARG HG2    H  N N 79  
ARG HG3    H  N N 80  
ARG HD2    H  N N 81  
ARG HD3    H  N N 82  
ARG HE     H  N N 83  
ARG HH11   H  N N 84  
ARG HH12   H  N N 85  
ARG HH21   H  N N 86  
ARG HH22   H  N N 87  
ARG HXT    H  N N 88  
ASN N      N  N N 89  
ASN CA     C  N S 90  
ASN C      C  N N 91  
ASN O      O  N N 92  
ASN CB     C  N N 93  
ASN CG     C  N N 94  
ASN OD1    O  N N 95  
ASN ND2    N  N N 96  
ASN OXT    O  N N 97  
ASN H      H  N N 98  
ASN H2     H  N N 99  
ASN HA     H  N N 100 
ASN HB2    H  N N 101 
ASN HB3    H  N N 102 
ASN HD21   H  N N 103 
ASN HD22   H  N N 104 
ASN HXT    H  N N 105 
ASP N      N  N N 106 
ASP CA     C  N S 107 
ASP C      C  N N 108 
ASP O      O  N N 109 
ASP CB     C  N N 110 
ASP CG     C  N N 111 
ASP OD1    O  N N 112 
ASP OD2    O  N N 113 
ASP OXT    O  N N 114 
ASP H      H  N N 115 
ASP H2     H  N N 116 
ASP HA     H  N N 117 
ASP HB2    H  N N 118 
ASP HB3    H  N N 119 
ASP HD2    H  N N 120 
ASP HXT    H  N N 121 
CYS N      N  N N 122 
CYS CA     C  N R 123 
CYS C      C  N N 124 
CYS O      O  N N 125 
CYS CB     C  N N 126 
CYS SG     S  N N 127 
CYS OXT    O  N N 128 
CYS H      H  N N 129 
CYS H2     H  N N 130 
CYS HA     H  N N 131 
CYS HB2    H  N N 132 
CYS HB3    H  N N 133 
CYS HG     H  N N 134 
CYS HXT    H  N N 135 
GLN N      N  N N 136 
GLN CA     C  N S 137 
GLN C      C  N N 138 
GLN O      O  N N 139 
GLN CB     C  N N 140 
GLN CG     C  N N 141 
GLN CD     C  N N 142 
GLN OE1    O  N N 143 
GLN NE2    N  N N 144 
GLN OXT    O  N N 145 
GLN H      H  N N 146 
GLN H2     H  N N 147 
GLN HA     H  N N 148 
GLN HB2    H  N N 149 
GLN HB3    H  N N 150 
GLN HG2    H  N N 151 
GLN HG3    H  N N 152 
GLN HE21   H  N N 153 
GLN HE22   H  N N 154 
GLN HXT    H  N N 155 
GLU N      N  N N 156 
GLU CA     C  N S 157 
GLU C      C  N N 158 
GLU O      O  N N 159 
GLU CB     C  N N 160 
GLU CG     C  N N 161 
GLU CD     C  N N 162 
GLU OE1    O  N N 163 
GLU OE2    O  N N 164 
GLU OXT    O  N N 165 
GLU H      H  N N 166 
GLU H2     H  N N 167 
GLU HA     H  N N 168 
GLU HB2    H  N N 169 
GLU HB3    H  N N 170 
GLU HG2    H  N N 171 
GLU HG3    H  N N 172 
GLU HE2    H  N N 173 
GLU HXT    H  N N 174 
GLY N      N  N N 175 
GLY CA     C  N N 176 
GLY C      C  N N 177 
GLY O      O  N N 178 
GLY OXT    O  N N 179 
GLY H      H  N N 180 
GLY H2     H  N N 181 
GLY HA2    H  N N 182 
GLY HA3    H  N N 183 
GLY HXT    H  N N 184 
HFG "O4'"  O  N N 185 
HFG C21    C  N N 186 
HFG "C3'"  C  N N 187 
HFG "C2'"  C  N R 188 
HFG "N1'"  N  N N 189 
HFG "C6'"  C  N N 190 
HFG "C5'"  C  N N 191 
HFG "C4'"  C  N N 192 
HFG C39    C  N S 193 
HFG "O7'"  O  N N 194 
HFG "C1'"  C  N N 195 
HFG N3     N  N N 196 
HFG C4     C  N N 197 
HFG O11    O  N N 198 
HFG C10    C  Y N 199 
HFG C5     C  Y N 200 
HFG C2     C  N N 201 
HFG N1     N  N N 202 
HFG C9     C  Y N 203 
HFG C8     C  Y N 204 
HFG C7     C  Y N 205 
HFG BR1    BR N N 206 
HFG C6     C  Y N 207 
HFG CL1    CL N N 208 
HFG H1     H  N N 209 
HFG H2     H  N N 210 
HFG H3     H  N N 211 
HFG H4     H  N N 212 
HFG H6     H  N N 213 
HFG H7     H  N N 214 
HFG H8     H  N N 215 
HFG H9     H  N N 216 
HFG H10    H  N N 217 
HFG H11    H  N N 218 
HFG H12    H  N N 219 
HFG H13    H  N N 220 
HFG H14    H  N N 221 
HFG H15    H  N N 222 
HFG H16    H  N N 223 
HFG H17    H  N N 224 
HFG H18    H  N N 225 
HIS N      N  N N 226 
HIS CA     C  N S 227 
HIS C      C  N N 228 
HIS O      O  N N 229 
HIS CB     C  N N 230 
HIS CG     C  Y N 231 
HIS ND1    N  Y N 232 
HIS CD2    C  Y N 233 
HIS CE1    C  Y N 234 
HIS NE2    N  Y N 235 
HIS OXT    O  N N 236 
HIS H      H  N N 237 
HIS H2     H  N N 238 
HIS HA     H  N N 239 
HIS HB2    H  N N 240 
HIS HB3    H  N N 241 
HIS HD1    H  N N 242 
HIS HD2    H  N N 243 
HIS HE1    H  N N 244 
HIS HE2    H  N N 245 
HIS HXT    H  N N 246 
ILE N      N  N N 247 
ILE CA     C  N S 248 
ILE C      C  N N 249 
ILE O      O  N N 250 
ILE CB     C  N S 251 
ILE CG1    C  N N 252 
ILE CG2    C  N N 253 
ILE CD1    C  N N 254 
ILE OXT    O  N N 255 
ILE H      H  N N 256 
ILE H2     H  N N 257 
ILE HA     H  N N 258 
ILE HB     H  N N 259 
ILE HG12   H  N N 260 
ILE HG13   H  N N 261 
ILE HG21   H  N N 262 
ILE HG22   H  N N 263 
ILE HG23   H  N N 264 
ILE HD11   H  N N 265 
ILE HD12   H  N N 266 
ILE HD13   H  N N 267 
ILE HXT    H  N N 268 
LEU N      N  N N 269 
LEU CA     C  N S 270 
LEU C      C  N N 271 
LEU O      O  N N 272 
LEU CB     C  N N 273 
LEU CG     C  N N 274 
LEU CD1    C  N N 275 
LEU CD2    C  N N 276 
LEU OXT    O  N N 277 
LEU H      H  N N 278 
LEU H2     H  N N 279 
LEU HA     H  N N 280 
LEU HB2    H  N N 281 
LEU HB3    H  N N 282 
LEU HG     H  N N 283 
LEU HD11   H  N N 284 
LEU HD12   H  N N 285 
LEU HD13   H  N N 286 
LEU HD21   H  N N 287 
LEU HD22   H  N N 288 
LEU HD23   H  N N 289 
LEU HXT    H  N N 290 
LYS N      N  N N 291 
LYS CA     C  N S 292 
LYS C      C  N N 293 
LYS O      O  N N 294 
LYS CB     C  N N 295 
LYS CG     C  N N 296 
LYS CD     C  N N 297 
LYS CE     C  N N 298 
LYS NZ     N  N N 299 
LYS OXT    O  N N 300 
LYS H      H  N N 301 
LYS H2     H  N N 302 
LYS HA     H  N N 303 
LYS HB2    H  N N 304 
LYS HB3    H  N N 305 
LYS HG2    H  N N 306 
LYS HG3    H  N N 307 
LYS HD2    H  N N 308 
LYS HD3    H  N N 309 
LYS HE2    H  N N 310 
LYS HE3    H  N N 311 
LYS HZ1    H  N N 312 
LYS HZ2    H  N N 313 
LYS HZ3    H  N N 314 
LYS HXT    H  N N 315 
MET N      N  N N 316 
MET CA     C  N S 317 
MET C      C  N N 318 
MET O      O  N N 319 
MET CB     C  N N 320 
MET CG     C  N N 321 
MET SD     S  N N 322 
MET CE     C  N N 323 
MET OXT    O  N N 324 
MET H      H  N N 325 
MET H2     H  N N 326 
MET HA     H  N N 327 
MET HB2    H  N N 328 
MET HB3    H  N N 329 
MET HG2    H  N N 330 
MET HG3    H  N N 331 
MET HE1    H  N N 332 
MET HE2    H  N N 333 
MET HE3    H  N N 334 
MET HXT    H  N N 335 
MG  MG     MG N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TYR N      N  N N 435 
TYR CA     C  N S 436 
TYR C      C  N N 437 
TYR O      O  N N 438 
TYR CB     C  N N 439 
TYR CG     C  Y N 440 
TYR CD1    C  Y N 441 
TYR CD2    C  Y N 442 
TYR CE1    C  Y N 443 
TYR CE2    C  Y N 444 
TYR CZ     C  Y N 445 
TYR OH     O  N N 446 
TYR OXT    O  N N 447 
TYR H      H  N N 448 
TYR H2     H  N N 449 
TYR HA     H  N N 450 
TYR HB2    H  N N 451 
TYR HB3    H  N N 452 
TYR HD1    H  N N 453 
TYR HD2    H  N N 454 
TYR HE1    H  N N 455 
TYR HE2    H  N N 456 
TYR HH     H  N N 457 
TYR HXT    H  N N 458 
VAL N      N  N N 459 
VAL CA     C  N S 460 
VAL C      C  N N 461 
VAL O      O  N N 462 
VAL CB     C  N N 463 
VAL CG1    C  N N 464 
VAL CG2    C  N N 465 
VAL OXT    O  N N 466 
VAL H      H  N N 467 
VAL H2     H  N N 468 
VAL HA     H  N N 469 
VAL HB     H  N N 470 
VAL HG11   H  N N 471 
VAL HG12   H  N N 472 
VAL HG13   H  N N 473 
VAL HG21   H  N N 474 
VAL HG22   H  N N 475 
VAL HG23   H  N N 476 
VAL HXT    H  N N 477 
ZN  ZN     ZN N N 478 
# 
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  
ANP PG    O1G    doub N N 13  
ANP PG    O2G    sing N N 14  
ANP PG    O3G    sing N N 15  
ANP PG    N3B    sing N N 16  
ANP O2G   HOG2   sing N N 17  
ANP O3G   HOG3   sing N N 18  
ANP PB    O1B    doub N N 19  
ANP PB    O2B    sing N N 20  
ANP PB    N3B    sing N N 21  
ANP PB    O3A    sing N N 22  
ANP O2B   HOB2   sing N N 23  
ANP N3B   HNB1   sing N N 24  
ANP PA    O1A    doub N N 25  
ANP PA    O2A    sing N N 26  
ANP PA    O3A    sing N N 27  
ANP PA    "O5'"  sing N N 28  
ANP O2A   HOA2   sing N N 29  
ANP "O5'" "C5'"  sing N N 30  
ANP "C5'" "C4'"  sing N N 31  
ANP "C5'" "H5'1" sing N N 32  
ANP "C5'" "H5'2" sing N N 33  
ANP "C4'" "O4'"  sing N N 34  
ANP "C4'" "C3'"  sing N N 35  
ANP "C4'" "H4'"  sing N N 36  
ANP "O4'" "C1'"  sing N N 37  
ANP "C3'" "O3'"  sing N N 38  
ANP "C3'" "C2'"  sing N N 39  
ANP "C3'" "H3'"  sing N N 40  
ANP "O3'" "HO3'" sing N N 41  
ANP "C2'" "O2'"  sing N N 42  
ANP "C2'" "C1'"  sing N N 43  
ANP "C2'" "H2'"  sing N N 44  
ANP "O2'" "HO2'" sing N N 45  
ANP "C1'" N9     sing N N 46  
ANP "C1'" "H1'"  sing N N 47  
ANP N9    C8     sing Y N 48  
ANP N9    C4     sing Y N 49  
ANP C8    N7     doub Y N 50  
ANP C8    H8     sing N N 51  
ANP N7    C5     sing Y N 52  
ANP C5    C6     sing Y N 53  
ANP C5    C4     doub Y N 54  
ANP C6    N6     sing N N 55  
ANP C6    N1     doub Y N 56  
ANP N6    HN61   sing N N 57  
ANP N6    HN62   sing N N 58  
ANP N1    C2     sing Y N 59  
ANP C2    N3     doub Y N 60  
ANP C2    H2     sing N N 61  
ANP N3    C4     sing Y N 62  
ARG N     CA     sing N N 63  
ARG N     H      sing N N 64  
ARG N     H2     sing N N 65  
ARG CA    C      sing N N 66  
ARG CA    CB     sing N N 67  
ARG CA    HA     sing N N 68  
ARG C     O      doub N N 69  
ARG C     OXT    sing N N 70  
ARG CB    CG     sing N N 71  
ARG CB    HB2    sing N N 72  
ARG CB    HB3    sing N N 73  
ARG CG    CD     sing N N 74  
ARG CG    HG2    sing N N 75  
ARG CG    HG3    sing N N 76  
ARG CD    NE     sing N N 77  
ARG CD    HD2    sing N N 78  
ARG CD    HD3    sing N N 79  
ARG NE    CZ     sing N N 80  
ARG NE    HE     sing N N 81  
ARG CZ    NH1    sing N N 82  
ARG CZ    NH2    doub N N 83  
ARG NH1   HH11   sing N N 84  
ARG NH1   HH12   sing N N 85  
ARG NH2   HH21   sing N N 86  
ARG NH2   HH22   sing N N 87  
ARG OXT   HXT    sing N N 88  
ASN N     CA     sing N N 89  
ASN N     H      sing N N 90  
ASN N     H2     sing N N 91  
ASN CA    C      sing N N 92  
ASN CA    CB     sing N N 93  
ASN CA    HA     sing N N 94  
ASN C     O      doub N N 95  
ASN C     OXT    sing N N 96  
ASN CB    CG     sing N N 97  
ASN CB    HB2    sing N N 98  
ASN CB    HB3    sing N N 99  
ASN CG    OD1    doub N N 100 
ASN CG    ND2    sing N N 101 
ASN ND2   HD21   sing N N 102 
ASN ND2   HD22   sing N N 103 
ASN OXT   HXT    sing N N 104 
ASP N     CA     sing N N 105 
ASP N     H      sing N N 106 
ASP N     H2     sing N N 107 
ASP CA    C      sing N N 108 
ASP CA    CB     sing N N 109 
ASP CA    HA     sing N N 110 
ASP C     O      doub N N 111 
ASP C     OXT    sing N N 112 
ASP CB    CG     sing N N 113 
ASP CB    HB2    sing N N 114 
ASP CB    HB3    sing N N 115 
ASP CG    OD1    doub N N 116 
ASP CG    OD2    sing N N 117 
ASP OD2   HD2    sing N N 118 
ASP OXT   HXT    sing N N 119 
CYS N     CA     sing N N 120 
CYS N     H      sing N N 121 
CYS N     H2     sing N N 122 
CYS CA    C      sing N N 123 
CYS CA    CB     sing N N 124 
CYS CA    HA     sing N N 125 
CYS C     O      doub N N 126 
CYS C     OXT    sing N N 127 
CYS CB    SG     sing N N 128 
CYS CB    HB2    sing N N 129 
CYS CB    HB3    sing N N 130 
CYS SG    HG     sing N N 131 
CYS OXT   HXT    sing N N 132 
GLN N     CA     sing N N 133 
GLN N     H      sing N N 134 
GLN N     H2     sing N N 135 
GLN CA    C      sing N N 136 
GLN CA    CB     sing N N 137 
GLN CA    HA     sing N N 138 
GLN C     O      doub N N 139 
GLN C     OXT    sing N N 140 
GLN CB    CG     sing N N 141 
GLN CB    HB2    sing N N 142 
GLN CB    HB3    sing N N 143 
GLN CG    CD     sing N N 144 
GLN CG    HG2    sing N N 145 
GLN CG    HG3    sing N N 146 
GLN CD    OE1    doub N N 147 
GLN CD    NE2    sing N N 148 
GLN NE2   HE21   sing N N 149 
GLN NE2   HE22   sing N N 150 
GLN OXT   HXT    sing N N 151 
GLU N     CA     sing N N 152 
GLU N     H      sing N N 153 
GLU N     H2     sing N N 154 
GLU CA    C      sing N N 155 
GLU CA    CB     sing N N 156 
GLU CA    HA     sing N N 157 
GLU C     O      doub N N 158 
GLU C     OXT    sing N N 159 
GLU CB    CG     sing N N 160 
GLU CB    HB2    sing N N 161 
GLU CB    HB3    sing N N 162 
GLU CG    CD     sing N N 163 
GLU CG    HG2    sing N N 164 
GLU CG    HG3    sing N N 165 
GLU CD    OE1    doub N N 166 
GLU CD    OE2    sing N N 167 
GLU OE2   HE2    sing N N 168 
GLU OXT   HXT    sing N N 169 
GLY N     CA     sing N N 170 
GLY N     H      sing N N 171 
GLY N     H2     sing N N 172 
GLY CA    C      sing N N 173 
GLY CA    HA2    sing N N 174 
GLY CA    HA3    sing N N 175 
GLY C     O      doub N N 176 
GLY C     OXT    sing N N 177 
GLY OXT   HXT    sing N N 178 
HFG CL1   C6     sing N N 179 
HFG C6    C5     doub Y N 180 
HFG C6    C7     sing Y N 181 
HFG BR1   C7     sing N N 182 
HFG C5    C10    sing Y N 183 
HFG C7    C8     doub Y N 184 
HFG O11   C4     doub N N 185 
HFG C10   C4     sing N N 186 
HFG C10   C9     doub Y N 187 
HFG C8    C9     sing Y N 188 
HFG C4    N3     sing N N 189 
HFG C9    N1     sing N N 190 
HFG "N1'" "C6'"  sing N N 191 
HFG "N1'" "C2'"  sing N N 192 
HFG "C6'" "C5'"  sing N N 193 
HFG "O4'" C21    doub N N 194 
HFG N3    "C1'"  sing N N 195 
HFG N3    C2     sing N N 196 
HFG N1    C2     doub N N 197 
HFG C21   "C3'"  sing N N 198 
HFG C21   "C1'"  sing N N 199 
HFG "C3'" "C2'"  sing N N 200 
HFG "C2'" C39    sing N N 201 
HFG "C5'" "C4'"  sing N N 202 
HFG C39   "C4'"  sing N N 203 
HFG C39   "O7'"  sing N N 204 
HFG "C3'" H1     sing N N 205 
HFG "C3'" H2     sing N N 206 
HFG "C2'" H3     sing N N 207 
HFG "N1'" H4     sing N N 208 
HFG "C6'" H6     sing N N 209 
HFG "C6'" H7     sing N N 210 
HFG "C5'" H8     sing N N 211 
HFG "C5'" H9     sing N N 212 
HFG "C4'" H10    sing N N 213 
HFG "C4'" H11    sing N N 214 
HFG C39   H12    sing N N 215 
HFG "O7'" H13    sing N N 216 
HFG "C1'" H14    sing N N 217 
HFG "C1'" H15    sing N N 218 
HFG C5    H16    sing N N 219 
HFG C2    H17    sing N N 220 
HFG C8    H18    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
_pdbx_audit_support.funding_organization   'Department of Biotechnology (DBT, India)' 
_pdbx_audit_support.country                India 
_pdbx_audit_support.grant_number           PR32713 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7F9A 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8JE6 
_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.fract_transf_matrix[1][1]   0.012349 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003400 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014327 
_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]   0.009708 
_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 
BR 
C  
CL 
MG 
N  
O  
P  
S  
ZN 
# 
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     . LEU A 1 6   ? 13.548  -28.737 -2.127 1.00 68.90  ? 1223 LEU A N     1 
ATOM   2    C  CA    . LEU A 1 6   ? 14.846  -28.091 -2.301 1.00 69.23  ? 1223 LEU A CA    1 
ATOM   3    C  C     . LEU A 1 6   ? 15.308  -28.190 -3.736 1.00 83.59  ? 1223 LEU A C     1 
ATOM   4    O  O     . LEU A 1 6   ? 15.447  -29.286 -4.275 1.00 95.59  ? 1223 LEU A O     1 
ATOM   5    C  CB    . LEU A 1 6   ? 15.906  -28.706 -1.374 1.00 60.43  ? 1223 LEU A CB    1 
ATOM   6    C  CG    . LEU A 1 6   ? 16.361  -27.854 -0.170 1.00 57.81  ? 1223 LEU A CG    1 
ATOM   7    C  CD1   . LEU A 1 6   ? 15.280  -27.754 0.900  1.00 53.36  ? 1223 LEU A CD1   1 
ATOM   8    C  CD2   . LEU A 1 6   ? 17.665  -28.365 0.437  1.00 48.91  ? 1223 LEU A CD2   1 
ATOM   9    N  N     . GLU A 1 7   ? 15.552  -27.036 -4.356 1.00 86.94  ? 1224 GLU A N     1 
ATOM   10   C  CA    . GLU A 1 7   ? 15.902  -27.020 -5.771 1.00 93.00  ? 1224 GLU A CA    1 
ATOM   11   C  C     . GLU A 1 7   ? 17.395  -27.266 -5.956 1.00 94.04  ? 1224 GLU A C     1 
ATOM   12   O  O     . GLU A 1 7   ? 17.796  -28.135 -6.738 1.00 108.45 ? 1224 GLU A O     1 
ATOM   13   C  CB    . GLU A 1 7   ? 15.481  -25.694 -6.407 1.00 92.11  ? 1224 GLU A CB    1 
ATOM   14   N  N     . ALA A 1 8   ? 18.222  -26.562 -5.198 1.00 86.40  ? 1225 ALA A N     1 
ATOM   15   C  CA    . ALA A 1 8   ? 19.667  -26.642 -5.328 1.00 87.33  ? 1225 ALA A CA    1 
ATOM   16   C  C     . ALA A 1 8   ? 20.233  -27.664 -4.349 1.00 86.49  ? 1225 ALA A C     1 
ATOM   17   O  O     . ALA A 1 8   ? 19.606  -28.013 -3.344 1.00 86.25  ? 1225 ALA A O     1 
ATOM   18   C  CB    . ALA A 1 8   ? 20.302  -25.275 -5.077 1.00 88.25  ? 1225 ALA A CB    1 
ATOM   19   N  N     . THR A 1 9   ? 21.448  -28.125 -4.641 1.00 81.19  ? 1226 THR A N     1 
ATOM   20   C  CA    . THR A 1 9   ? 22.104  -29.138 -3.828 1.00 72.75  ? 1226 THR A CA    1 
ATOM   21   C  C     . THR A 1 9   ? 23.213  -28.531 -2.988 1.00 71.08  ? 1226 THR A C     1 
ATOM   22   O  O     . THR A 1 9   ? 23.783  -27.494 -3.328 1.00 70.97  ? 1226 THR A O     1 
ATOM   23   C  CB    . THR A 1 9   ? 22.710  -30.258 -4.668 1.00 66.46  ? 1226 THR A CB    1 
ATOM   24   O  OG1   . THR A 1 9   ? 24.040  -29.888 -5.044 1.00 63.79  ? 1226 THR A OG1   1 
ATOM   25   C  CG2   . THR A 1 9   ? 21.880  -30.520 -5.909 1.00 74.15  ? 1226 THR A CG2   1 
ATOM   26   N  N     . LYS A 1 10  ? 23.507  -29.196 -1.873 1.00 68.16  ? 1227 LYS A N     1 
ATOM   27   C  CA    . LYS A 1 10  ? 24.540  -28.701 -0.985 1.00 42.37  ? 1227 LYS A CA    1 
ATOM   28   C  C     . LYS A 1 10  ? 25.889  -28.717 -1.671 1.00 66.67  ? 1227 LYS A C     1 
ATOM   29   O  O     . LYS A 1 10  ? 26.697  -27.813 -1.471 1.00 73.64  ? 1227 LYS A O     1 
ATOM   30   C  CB    . LYS A 1 10  ? 24.567  -29.540 0.287  1.00 41.92  ? 1227 LYS A CB    1 
ATOM   31   C  CG    . LYS A 1 10  ? 25.330  -28.901 1.440  1.00 59.40  ? 1227 LYS A CG    1 
ATOM   32   C  CD    . LYS A 1 10  ? 25.243  -29.720 2.729  1.00 62.32  ? 1227 LYS A CD    1 
ATOM   33   C  CE    . LYS A 1 10  ? 26.180  -29.196 3.812  1.00 57.26  ? 1227 LYS A CE    1 
ATOM   34   N  NZ    . LYS A 1 10  ? 26.141  -30.092 5.001  1.00 64.72  ? 1227 LYS A NZ    1 
ATOM   35   N  N     . GLU A 1 11  ? 26.114  -29.687 -2.549 1.00 77.03  ? 1228 GLU A N     1 
ATOM   36   C  CA    . GLU A 1 11  ? 27.436  -29.922 -3.121 1.00 82.89  ? 1228 GLU A CA    1 
ATOM   37   C  C     . GLU A 1 11  ? 27.758  -28.923 -4.226 1.00 84.46  ? 1228 GLU A C     1 
ATOM   38   O  O     . GLU A 1 11  ? 28.834  -28.319 -4.235 1.00 83.65  ? 1228 GLU A O     1 
ATOM   39   C  CB    . GLU A 1 11  ? 27.506  -31.359 -3.648 1.00 80.37  ? 1228 GLU A CB    1 
ATOM   40   C  CG    . GLU A 1 11  ? 26.533  -32.344 -2.969 1.00 79.74  ? 1228 GLU A CG    1 
ATOM   41   C  CD    . GLU A 1 11  ? 26.698  -32.426 -1.449 1.00 91.62  ? 1228 GLU A CD    1 
ATOM   42   O  OE1   . GLU A 1 11  ? 27.763  -32.022 -0.926 1.00 96.20  ? 1228 GLU A OE1   1 
ATOM   43   O  OE2   . GLU A 1 11  ? 25.756  -32.898 -0.773 1.00 94.67  ? 1228 GLU A OE2   1 
ATOM   44   N  N     . ASP A 1 12  ? 26.846  -28.753 -5.170 1.00 91.08  ? 1229 ASP A N     1 
ATOM   45   C  CA    . ASP A 1 12  ? 26.928  -27.696 -6.165 1.00 99.76  ? 1229 ASP A CA    1 
ATOM   46   C  C     . ASP A 1 12  ? 26.088  -26.513 -5.700 1.00 106.51 ? 1229 ASP A C     1 
ATOM   47   O  O     . ASP A 1 12  ? 24.920  -26.688 -5.343 1.00 114.10 ? 1229 ASP A O     1 
ATOM   48   C  CB    . ASP A 1 12  ? 26.418  -28.179 -7.515 1.00 106.56 ? 1229 ASP A CB    1 
ATOM   49   C  CG    . ASP A 1 12  ? 26.915  -29.546 -7.853 1.00 120.53 ? 1229 ASP A CG    1 
ATOM   50   O  OD1   . ASP A 1 12  ? 28.046  -29.638 -8.377 1.00 129.10 ? 1229 ASP A OD1   1 
ATOM   51   O  OD2   . ASP A 1 12  ? 26.182  -30.526 -7.581 1.00 122.02 ? 1229 ASP A OD2   1 
ATOM   52   N  N     . ASN A 1 13  ? 26.679  -25.319 -5.687 1.00 96.58  ? 1230 ASN A N     1 
ATOM   53   C  CA    . ASN A 1 13  ? 25.967  -24.105 -5.288 1.00 84.17  ? 1230 ASN A CA    1 
ATOM   54   C  C     . ASN A 1 13  ? 25.557  -24.174 -3.808 1.00 71.10  ? 1230 ASN A C     1 
ATOM   55   O  O     . ASN A 1 13  ? 24.402  -24.390 -3.440 1.00 67.92  ? 1230 ASN A O     1 
ATOM   56   C  CB    . ASN A 1 13  ? 24.761  -23.866 -6.210 1.00 79.17  ? 1230 ASN A CB    1 
ATOM   57   C  CG    . ASN A 1 13  ? 24.321  -22.421 -6.242 1.00 86.10  ? 1230 ASN A CG    1 
ATOM   58   O  OD1   . ASN A 1 13  ? 24.785  -21.598 -5.451 1.00 86.86  ? 1230 ASN A OD1   1 
ATOM   59   N  ND2   . ASN A 1 13  ? 23.409  -22.103 -7.152 1.00 94.39  ? 1230 ASN A ND2   1 
ATOM   60   N  N     . LEU A 1 14  ? 26.576  -23.994 -2.974 1.00 61.98  ? 1231 LEU A N     1 
ATOM   61   C  CA    . LEU A 1 14  ? 26.361  -23.947 -1.535 1.00 51.87  ? 1231 LEU A CA    1 
ATOM   62   C  C     . LEU A 1 14  ? 25.533  -22.752 -1.088 1.00 55.41  ? 1231 LEU A C     1 
ATOM   63   O  O     . LEU A 1 14  ? 24.629  -22.952 -0.258 1.00 54.32  ? 1231 LEU A O     1 
ATOM   64   C  CB    . LEU A 1 14  ? 27.717  -23.946 -0.817 1.00 40.94  ? 1231 LEU A CB    1 
ATOM   65   C  CG    . LEU A 1 14  ? 27.488  -24.150 0.662  1.00 48.84  ? 1231 LEU A CG    1 
ATOM   66   C  CD1   . LEU A 1 14  ? 26.959  -25.546 0.790  1.00 42.94  ? 1231 LEU A CD1   1 
ATOM   67   C  CD2   . LEU A 1 14  ? 28.749  -23.952 1.471  1.00 52.57  ? 1231 LEU A CD2   1 
ATOM   68   N  N     . PRO A 1 15  ? 25.776  -21.519 -1.561 1.00 58.61  ? 1232 PRO A N     1 
ATOM   69   C  CA    . PRO A 1 15  ? 25.036  -20.368 -1.012 1.00 55.10  ? 1232 PRO A CA    1 
ATOM   70   C  C     . PRO A 1 15  ? 23.554  -20.447 -1.287 1.00 58.96  ? 1232 PRO A C     1 
ATOM   71   O  O     . PRO A 1 15  ? 22.704  -20.118 -0.445 1.00 55.58  ? 1232 PRO A O     1 
ATOM   72   C  CB    . PRO A 1 15  ? 25.681  -19.176 -1.741 1.00 49.19  ? 1232 PRO A CB    1 
ATOM   73   C  CG    . PRO A 1 15  ? 26.239  -19.742 -2.975 1.00 40.77  ? 1232 PRO A CG    1 
ATOM   74   C  CD    . PRO A 1 15  ? 26.709  -21.090 -2.618 1.00 56.91  ? 1232 PRO A CD    1 
ATOM   75   N  N     . ASP A 1 16  ? 23.235  -21.019 -2.428 1.00 70.87  ? 1233 ASP A N     1 
ATOM   76   C  CA    . ASP A 1 16  ? 21.877  -21.053 -2.915 1.00 82.54  ? 1233 ASP A CA    1 
ATOM   77   C  C     . ASP A 1 16  ? 21.152  -22.237 -2.302 1.00 84.94  ? 1233 ASP A C     1 
ATOM   78   O  O     . ASP A 1 16  ? 19.973  -22.136 -1.973 1.00 96.82  ? 1233 ASP A O     1 
ATOM   79   C  CB    . ASP A 1 16  ? 21.941  -21.162 -4.435 1.00 96.71  ? 1233 ASP A CB    1 
ATOM   80   C  CG    . ASP A 1 16  ? 20.636  -20.924 -5.145 1.00 109.88 ? 1233 ASP A CG    1 
ATOM   81   O  OD1   . ASP A 1 16  ? 20.715  -20.316 -6.247 1.00 118.91 ? 1233 ASP A OD1   1 
ATOM   82   O  OD2   . ASP A 1 16  ? 19.612  -21.477 -4.686 1.00 112.08 ? 1233 ASP A OD2   1 
ATOM   83   N  N     . TRP A 1 17  ? 21.902  -23.290 -1.984 1.00 65.28  ? 1234 TRP A N     1 
ATOM   84   C  CA    . TRP A 1 17  ? 21.394  -24.331 -1.097 1.00 58.70  ? 1234 TRP A CA    1 
ATOM   85   C  C     . TRP A 1 17  ? 21.077  -23.810 0.304  1.00 60.26  ? 1234 TRP A C     1 
ATOM   86   O  O     . TRP A 1 17  ? 20.034  -24.143 0.871  1.00 55.47  ? 1234 TRP A O     1 
ATOM   87   C  CB    . TRP A 1 17  ? 22.425  -25.455 -1.023 1.00 63.84  ? 1234 TRP A CB    1 
ATOM   88   C  CG    . TRP A 1 17  ? 22.099  -26.435 0.079  1.00 60.75  ? 1234 TRP A CG    1 
ATOM   89   C  CD1   . TRP A 1 17  ? 21.237  -27.500 0.017  1.00 61.93  ? 1234 TRP A CD1   1 
ATOM   90   C  CD2   . TRP A 1 17  ? 22.604  -26.409 1.412  1.00 54.45  ? 1234 TRP A CD2   1 
ATOM   91   N  NE1   . TRP A 1 17  ? 21.189  -28.143 1.235  1.00 64.07  ? 1234 TRP A NE1   1 
ATOM   92   C  CE2   . TRP A 1 17  ? 22.017  -27.489 2.109  1.00 59.20  ? 1234 TRP A CE2   1 
ATOM   93   C  CE3   . TRP A 1 17  ? 23.505  -25.584 2.083  1.00 51.90  ? 1234 TRP A CE3   1 
ATOM   94   C  CZ2   . TRP A 1 17  ? 22.309  -27.762 3.440  1.00 62.14  ? 1234 TRP A CZ2   1 
ATOM   95   C  CZ3   . TRP A 1 17  ? 23.789  -25.850 3.394  1.00 58.32  ? 1234 TRP A CZ3   1 
ATOM   96   C  CH2   . TRP A 1 17  ? 23.197  -26.935 4.065  1.00 60.49  ? 1234 TRP A CH2   1 
ATOM   97   N  N     . TYR A 1 18  ? 22.021  -23.084 0.915  1.00 62.13  ? 1235 TYR A N     1 
ATOM   98   C  CA    . TYR A 1 18  ? 21.818  -22.509 2.247  1.00 56.24  ? 1235 TYR A CA    1 
ATOM   99   C  C     . TYR A 1 18  ? 20.581  -21.627 2.285  1.00 50.71  ? 1235 TYR A C     1 
ATOM   100  O  O     . TYR A 1 18  ? 19.778  -21.697 3.226  1.00 45.60  ? 1235 TYR A O     1 
ATOM   101  C  CB    . TYR A 1 18  ? 23.041  -21.701 2.648  1.00 51.99  ? 1235 TYR A CB    1 
ATOM   102  C  CG    . TYR A 1 18  ? 23.086  -21.207 4.078  1.00 44.53  ? 1235 TYR A CG    1 
ATOM   103  C  CD1   . TYR A 1 18  ? 23.466  -22.034 5.134  1.00 48.21  ? 1235 TYR A CD1   1 
ATOM   104  C  CD2   . TYR A 1 18  ? 22.799  -19.900 4.369  1.00 34.64  ? 1235 TYR A CD2   1 
ATOM   105  C  CE1   . TYR A 1 18  ? 23.549  -21.538 6.467  1.00 41.14  ? 1235 TYR A CE1   1 
ATOM   106  C  CE2   . TYR A 1 18  ? 22.874  -19.407 5.665  1.00 35.36  ? 1235 TYR A CE2   1 
ATOM   107  C  CZ    . TYR A 1 18  ? 23.242  -20.213 6.708  1.00 35.87  ? 1235 TYR A CZ    1 
ATOM   108  O  OH    . TYR A 1 18  ? 23.290  -19.637 7.964  1.00 38.57  ? 1235 TYR A OH    1 
ATOM   109  N  N     . SER A 1 19  ? 20.409  -20.786 1.263  1.00 48.01  ? 1236 SER A N     1 
ATOM   110  C  CA    . SER A 1 19  ? 19.220  -19.943 1.211  1.00 51.38  ? 1236 SER A CA    1 
ATOM   111  C  C     . SER A 1 19  ? 17.962  -20.796 1.141  1.00 67.50  ? 1236 SER A C     1 
ATOM   112  O  O     . SER A 1 19  ? 17.002  -20.573 1.895  1.00 63.82  ? 1236 SER A O     1 
ATOM   113  C  CB    . SER A 1 19  ? 19.290  -19.010 0.004  1.00 48.87  ? 1236 SER A CB    1 
ATOM   114  O  OG    . SER A 1 19  ? 18.220  -18.081 0.017  1.00 51.44  ? 1236 SER A OG    1 
ATOM   115  N  N     . GLN A 1 20  ? 17.967  -21.812 0.265  1.00 80.56  ? 1237 GLN A N     1 
ATOM   116  C  CA    . GLN A 1 20  ? 16.804  -22.690 0.149  1.00 78.57  ? 1237 GLN A CA    1 
ATOM   117  C  C     . GLN A 1 20  ? 16.487  -23.410 1.465  1.00 64.38  ? 1237 GLN A C     1 
ATOM   118  O  O     . GLN A 1 20  ? 15.333  -23.422 1.907  1.00 54.54  ? 1237 GLN A O     1 
ATOM   119  C  CB    . GLN A 1 20  ? 17.010  -23.675 -0.995 1.00 82.77  ? 1237 GLN A CB    1 
ATOM   120  C  CG    . GLN A 1 20  ? 17.113  -22.956 -2.310 1.00 85.68  ? 1237 GLN A CG    1 
ATOM   121  C  CD    . GLN A 1 20  ? 16.197  -23.508 -3.356 1.00 99.22  ? 1237 GLN A CD    1 
ATOM   122  O  OE1   . GLN A 1 20  ? 15.606  -24.574 -3.190 1.00 98.23  ? 1237 GLN A OE1   1 
ATOM   123  N  NE2   . GLN A 1 20  ? 16.066  -22.781 -4.456 1.00 113.74 ? 1237 GLN A NE2   1 
ATOM   124  N  N     . VAL A 1 21  ? 17.482  -23.992 2.133  1.00 55.78  ? 1238 VAL A N     1 
ATOM   125  C  CA    . VAL A 1 21  ? 17.133  -24.710 3.355  1.00 51.78  ? 1238 VAL A CA    1 
ATOM   126  C  C     . VAL A 1 21  ? 16.601  -23.734 4.396  1.00 48.10  ? 1238 VAL A C     1 
ATOM   127  O  O     . VAL A 1 21  ? 15.461  -23.878 4.854  1.00 39.93  ? 1238 VAL A O     1 
ATOM   128  C  CB    . VAL A 1 21  ? 18.311  -25.542 3.898  1.00 52.65  ? 1238 VAL A CB    1 
ATOM   129  C  CG1   . VAL A 1 21  ? 19.575  -24.748 3.926  1.00 55.77  ? 1238 VAL A CG1   1 
ATOM   130  C  CG2   . VAL A 1 21  ? 17.981  -26.053 5.317  1.00 35.73  ? 1238 VAL A CG2   1 
ATOM   131  N  N     . ILE A 1 22  ? 17.344  -22.653 4.681  1.00 41.84  ? 1239 ILE A N     1 
ATOM   132  C  CA    . ILE A 1 22  ? 16.918  -21.751 5.755  1.00 40.70  ? 1239 ILE A CA    1 
ATOM   133  C  C     . ILE A 1 22  ? 15.589  -21.043 5.463  1.00 43.40  ? 1239 ILE A C     1 
ATOM   134  O  O     . ILE A 1 22  ? 14.908  -20.601 6.407  1.00 33.82  ? 1239 ILE A O     1 
ATOM   135  C  CB    . ILE A 1 22  ? 17.974  -20.671 6.039  1.00 43.57  ? 1239 ILE A CB    1 
ATOM   136  C  CG1   . ILE A 1 22  ? 18.024  -19.699 4.858  1.00 36.85  ? 1239 ILE A CG1   1 
ATOM   137  C  CG2   . ILE A 1 22  ? 19.334  -21.277 6.363  1.00 37.13  ? 1239 ILE A CG2   1 
ATOM   138  C  CD1   . ILE A 1 22  ? 18.924  -18.538 5.080  1.00 36.45  ? 1239 ILE A CD1   1 
ATOM   139  N  N     . THR A 1 23  ? 15.168  -20.942 4.198  1.00 38.83  ? 1240 THR A N     1 
ATOM   140  C  CA    . THR A 1 23  ? 13.851  -20.358 3.988  1.00 36.24  ? 1240 THR A CA    1 
ATOM   141  C  C     . THR A 1 23  ? 12.783  -21.437 3.988  1.00 51.42  ? 1240 THR A C     1 
ATOM   142  O  O     . THR A 1 23  ? 11.848  -21.373 4.786  1.00 72.18  ? 1240 THR A O     1 
ATOM   143  C  CB    . THR A 1 23  ? 13.748  -19.576 2.671  1.00 34.49  ? 1240 THR A CB    1 
ATOM   144  O  OG1   . THR A 1 23  ? 13.682  -20.506 1.587  1.00 42.00  ? 1240 THR A OG1   1 
ATOM   145  C  CG2   . THR A 1 23  ? 14.882  -18.599 2.455  1.00 38.79  ? 1240 THR A CG2   1 
ATOM   146  N  N     . LYS A 1 24  ? 12.942  -22.465 3.146  1.00 39.70  ? 1241 LYS A N     1 
ATOM   147  C  CA    . LYS A 1 24  ? 11.914  -23.497 3.091  1.00 37.16  ? 1241 LYS A CA    1 
ATOM   148  C  C     . LYS A 1 24  ? 11.842  -24.309 4.370  1.00 49.19  ? 1241 LYS A C     1 
ATOM   149  O  O     . LYS A 1 24  ? 10.820  -24.964 4.604  1.00 54.45  ? 1241 LYS A O     1 
ATOM   150  C  CB    . LYS A 1 24  ? 12.119  -24.432 1.895  1.00 38.95  ? 1241 LYS A CB    1 
ATOM   151  C  CG    . LYS A 1 24  ? 12.252  -23.747 0.541  1.00 48.61  ? 1241 LYS A CG    1 
ATOM   152  C  CD    . LYS A 1 24  ? 12.196  -24.733 -0.626 1.00 56.85  ? 1241 LYS A CD    1 
ATOM   153  C  CE    . LYS A 1 24  ? 12.671  -24.059 -1.916 1.00 71.27  ? 1241 LYS A CE    1 
ATOM   154  N  NZ    . LYS A 1 24  ? 12.392  -24.830 -3.174 1.00 74.83  ? 1241 LYS A NZ    1 
ATOM   155  N  N     . GLY A 1 25  ? 12.856  -24.224 5.224  1.00 34.71  ? 1242 GLY A N     1 
ATOM   156  C  CA    . GLY A 1 25  ? 12.802  -24.833 6.532  1.00 34.28  ? 1242 GLY A CA    1 
ATOM   157  C  C     . GLY A 1 25  ? 12.161  -23.957 7.555  1.00 63.01  ? 1242 GLY A C     1 
ATOM   158  O  O     . GLY A 1 25  ? 12.014  -24.370 8.708  1.00 66.00  ? 1242 GLY A O     1 
ATOM   159  N  N     . GLU A 1 26  ? 11.785  -22.739 7.141  1.00 64.82  ? 1243 GLU A N     1 
ATOM   160  C  CA    . GLU A 1 26  ? 10.962  -21.807 7.917  1.00 54.33  ? 1243 GLU A CA    1 
ATOM   161  C  C     . GLU A 1 26  ? 11.681  -21.250 9.152  1.00 47.48  ? 1243 GLU A C     1 
ATOM   162  O  O     . GLU A 1 26  ? 11.107  -21.142 10.238 1.00 45.39  ? 1243 GLU A O     1 
ATOM   163  C  CB    . GLU A 1 26  ? 9.637   -22.466 8.287  1.00 40.19  ? 1243 GLU A CB    1 
ATOM   164  C  CG    . GLU A 1 26  ? 8.852   -22.814 7.055  1.00 35.23  ? 1243 GLU A CG    1 
ATOM   165  C  CD    . GLU A 1 26  ? 7.449   -23.207 7.398  1.00 55.27  ? 1243 GLU A CD    1 
ATOM   166  O  OE1   . GLU A 1 26  ? 6.726   -23.667 6.491  1.00 75.05  ? 1243 GLU A OE1   1 
ATOM   167  O  OE2   . GLU A 1 26  ? 7.072   -23.057 8.582  1.00 51.32  ? 1243 GLU A OE2   1 
ATOM   168  N  N     . MET A 1 27  ? 12.932  -20.859 8.986  1.00 44.20  ? 1244 MET A N     1 
ATOM   169  C  CA    . MET A 1 27  ? 13.633  -20.202 10.074 1.00 57.30  ? 1244 MET A CA    1 
ATOM   170  C  C     . MET A 1 27  ? 13.991  -18.755 9.793  1.00 59.82  ? 1244 MET A C     1 
ATOM   171  O  O     . MET A 1 27  ? 14.015  -17.940 10.715 1.00 46.90  ? 1244 MET A O     1 
ATOM   172  C  CB    . MET A 1 27  ? 14.903  -20.976 10.396 1.00 65.02  ? 1244 MET A CB    1 
ATOM   173  C  CG    . MET A 1 27  ? 14.649  -22.440 10.555 1.00 56.35  ? 1244 MET A CG    1 
ATOM   174  S  SD    . MET A 1 27  ? 16.248  -23.183 10.507 1.00 54.88  ? 1244 MET A SD    1 
ATOM   175  C  CE    . MET A 1 27  ? 16.757  -23.037 12.192 1.00 35.53  ? 1244 MET A CE    1 
ATOM   176  N  N     . ILE A 1 28  ? 14.193  -18.409 8.540  1.00 64.13  ? 1245 ILE A N     1 
ATOM   177  C  CA    . ILE A 1 28  ? 14.647  -17.097 8.132  1.00 50.95  ? 1245 ILE A CA    1 
ATOM   178  C  C     . ILE A 1 28  ? 13.490  -16.464 7.386  1.00 51.04  ? 1245 ILE A C     1 
ATOM   179  O  O     . ILE A 1 28  ? 12.644  -17.151 6.792  1.00 52.62  ? 1245 ILE A O     1 
ATOM   180  C  CB    . ILE A 1 28  ? 15.925  -17.227 7.257  1.00 49.73  ? 1245 ILE A CB    1 
ATOM   181  C  CG1   . ILE A 1 28  ? 17.122  -17.535 8.135  1.00 52.30  ? 1245 ILE A CG1   1 
ATOM   182  C  CG2   . ILE A 1 28  ? 16.235  -16.008 6.418  1.00 38.73  ? 1245 ILE A CG2   1 
ATOM   183  C  CD1   . ILE A 1 28  ? 17.104  -16.749 9.385  1.00 57.61  ? 1245 ILE A CD1   1 
ATOM   184  N  N     . GLU A 1 29  ? 13.401  -15.150 7.488  1.00 51.17  ? 1246 GLU A N     1 
ATOM   185  C  CA    . GLU A 1 29  ? 12.696  -14.371 6.487  1.00 52.32  ? 1246 GLU A CA    1 
ATOM   186  C  C     . GLU A 1 29  ? 13.593  -13.209 6.090  1.00 51.90  ? 1246 GLU A C     1 
ATOM   187  O  O     . GLU A 1 29  ? 13.979  -12.394 6.936  1.00 43.35  ? 1246 GLU A O     1 
ATOM   188  C  CB    . GLU A 1 29  ? 11.348  -13.906 7.022  1.00 52.60  ? 1246 GLU A CB    1 
ATOM   189  C  CG    . GLU A 1 29  ? 10.425  -13.532 5.939  1.00 51.48  ? 1246 GLU A CG    1 
ATOM   190  C  CD    . GLU A 1 29  ? 10.322  -14.597 4.897  1.00 49.15  ? 1246 GLU A CD    1 
ATOM   191  O  OE1   . GLU A 1 29  ? 9.490   -15.510 5.111  1.00 52.15  ? 1246 GLU A OE1   1 
ATOM   192  O  OE2   . GLU A 1 29  ? 11.062  -14.512 3.875  1.00 43.41  ? 1246 GLU A OE2   1 
ATOM   193  N  N     . TYR A 1 30  ? 13.912  -13.119 4.805  1.00 51.59  ? 1247 TYR A N     1 
ATOM   194  C  CA    . TYR A 1 30  ? 14.814  -12.061 4.395  1.00 49.83  ? 1247 TYR A CA    1 
ATOM   195  C  C     . TYR A 1 30  ? 14.184  -10.701 4.673  1.00 47.95  ? 1247 TYR A C     1 
ATOM   196  O  O     . TYR A 1 30  ? 12.987  -10.580 4.916  1.00 31.54  ? 1247 TYR A O     1 
ATOM   197  C  CB    . TYR A 1 30  ? 15.185  -12.207 2.932  1.00 52.27  ? 1247 TYR A CB    1 
ATOM   198  C  CG    . TYR A 1 30  ? 16.107  -13.359 2.700  1.00 48.12  ? 1247 TYR A CG    1 
ATOM   199  C  CD1   . TYR A 1 30  ? 17.412  -13.317 3.147  1.00 43.70  ? 1247 TYR A CD1   1 
ATOM   200  C  CD2   . TYR A 1 30  ? 15.679  -14.496 2.033  1.00 57.30  ? 1247 TYR A CD2   1 
ATOM   201  C  CE1   . TYR A 1 30  ? 18.284  -14.386 2.925  1.00 55.74  ? 1247 TYR A CE1   1 
ATOM   202  C  CE2   . TYR A 1 30  ? 16.546  -15.578 1.806  1.00 59.49  ? 1247 TYR A CE2   1 
ATOM   203  C  CZ    . TYR A 1 30  ? 17.845  -15.514 2.257  1.00 56.09  ? 1247 TYR A CZ    1 
ATOM   204  O  OH    . TYR A 1 30  ? 18.712  -16.564 2.048  1.00 51.35  ? 1247 TYR A OH    1 
ATOM   205  N  N     . TYR A 1 31  ? 15.029  -9.684  4.745  1.00 50.26  ? 1248 TYR A N     1 
ATOM   206  C  CA    . TYR A 1 31  ? 14.616  -8.427  5.335  1.00 38.91  ? 1248 TYR A CA    1 
ATOM   207  C  C     . TYR A 1 31  ? 15.178  -7.271  4.530  1.00 55.37  ? 1248 TYR A C     1 
ATOM   208  O  O     . TYR A 1 31  ? 16.239  -7.386  3.913  1.00 74.44  ? 1248 TYR A O     1 
ATOM   209  C  CB    . TYR A 1 31  ? 15.085  -8.387  6.768  1.00 35.23  ? 1248 TYR A CB    1 
ATOM   210  C  CG    . TYR A 1 31  ? 14.463  -7.329  7.585  1.00 37.77  ? 1248 TYR A CG    1 
ATOM   211  C  CD1   . TYR A 1 31  ? 13.108  -7.293  7.763  1.00 37.39  ? 1248 TYR A CD1   1 
ATOM   212  C  CD2   . TYR A 1 31  ? 15.246  -6.371  8.214  1.00 48.68  ? 1248 TYR A CD2   1 
ATOM   213  C  CE1   . TYR A 1 31  ? 12.534  -6.309  8.518  1.00 43.29  ? 1248 TYR A CE1   1 
ATOM   214  C  CE2   . TYR A 1 31  ? 14.677  -5.387  8.972  1.00 46.67  ? 1248 TYR A CE2   1 
ATOM   215  C  CZ    . TYR A 1 31  ? 13.317  -5.367  9.118  1.00 41.86  ? 1248 TYR A CZ    1 
ATOM   216  O  OH    . TYR A 1 31  ? 12.713  -4.409  9.866  1.00 48.42  ? 1248 TYR A OH    1 
ATOM   217  N  N     . ASP A 1 32  ? 14.468  -6.150  4.544  1.00 54.41  ? 1249 ASP A N     1 
ATOM   218  C  CA    . ASP A 1 32  ? 14.815  -5.065  3.642  1.00 48.95  ? 1249 ASP A CA    1 
ATOM   219  C  C     . ASP A 1 32  ? 15.852  -4.116  4.219  1.00 42.81  ? 1249 ASP A C     1 
ATOM   220  O  O     . ASP A 1 32  ? 16.189  -3.130  3.563  1.00 46.11  ? 1249 ASP A O     1 
ATOM   221  C  CB    . ASP A 1 32  ? 13.558  -4.292  3.219  1.00 52.47  ? 1249 ASP A CB    1 
ATOM   222  C  CG    . ASP A 1 32  ? 13.012  -3.355  4.311  1.00 58.18  ? 1249 ASP A CG    1 
ATOM   223  O  OD1   . ASP A 1 32  ? 13.147  -3.658  5.528  1.00 60.42  ? 1249 ASP A OD1   1 
ATOM   224  O  OD2   . ASP A 1 32  ? 12.418  -2.309  3.927  1.00 44.86  ? 1249 ASP A OD2   1 
ATOM   225  N  N     . VAL A 1 33  ? 16.403  -4.413  5.392  1.00 39.24  ? 1250 VAL A N     1 
ATOM   226  C  CA    . VAL A 1 33  ? 17.590  -3.740  5.922  1.00 43.10  ? 1250 VAL A CA    1 
ATOM   227  C  C     . VAL A 1 33  ? 18.747  -4.730  5.841  1.00 54.52  ? 1250 VAL A C     1 
ATOM   228  O  O     . VAL A 1 33  ? 18.812  -5.678  6.636  1.00 52.13  ? 1250 VAL A O     1 
ATOM   229  C  CB    . VAL A 1 33  ? 17.361  -3.268  7.368  1.00 37.66  ? 1250 VAL A CB    1 
ATOM   230  C  CG1   . VAL A 1 33  ? 18.673  -2.908  8.045  1.00 43.41  ? 1250 VAL A CG1   1 
ATOM   231  C  CG2   . VAL A 1 33  ? 16.420  -2.106  7.386  1.00 46.70  ? 1250 VAL A CG2   1 
ATOM   232  N  N     . SER A 1 34  ? 19.686  -4.480  4.928  1.00 54.81  ? 1251 SER A N     1 
ATOM   233  C  CA    . SER A 1 34  ? 20.729  -5.432  4.556  1.00 52.21  ? 1251 SER A CA    1 
ATOM   234  C  C     . SER A 1 34  ? 21.437  -5.994  5.785  1.00 46.07  ? 1251 SER A C     1 
ATOM   235  O  O     . SER A 1 34  ? 21.959  -5.241  6.607  1.00 48.32  ? 1251 SER A O     1 
ATOM   236  C  CB    . SER A 1 34  ? 21.727  -4.785  3.617  1.00 53.77  ? 1251 SER A CB    1 
ATOM   237  O  OG    . SER A 1 34  ? 22.408  -3.722  4.273  1.00 68.68  ? 1251 SER A OG    1 
ATOM   238  N  N     . GLY A 1 35  ? 21.519  -7.332  5.888  1.00 47.55  ? 1252 GLY A N     1 
ATOM   239  C  CA    . GLY A 1 35  ? 22.260  -8.010  6.926  1.00 41.05  ? 1252 GLY A CA    1 
ATOM   240  C  C     . GLY A 1 35  ? 21.495  -8.310  8.197  1.00 45.25  ? 1252 GLY A C     1 
ATOM   241  O  O     . GLY A 1 35  ? 22.084  -8.828  9.157  1.00 65.32  ? 1252 GLY A O     1 
ATOM   242  N  N     . CYS A 1 36  ? 20.199  -8.045  8.229  1.00 35.84  ? 1253 CYS A N     1 
ATOM   243  C  CA    . CYS A 1 36  ? 19.297  -8.465  9.288  1.00 31.41  ? 1253 CYS A CA    1 
ATOM   244  C  C     . CYS A 1 36  ? 18.281  -9.404  8.674  1.00 41.88  ? 1253 CYS A C     1 
ATOM   245  O  O     . CYS A 1 36  ? 17.993  -9.327  7.467  1.00 30.47  ? 1253 CYS A O     1 
ATOM   246  C  CB    . CYS A 1 36  ? 18.566  -7.287  9.937  1.00 32.21  ? 1253 CYS A CB    1 
ATOM   247  S  SG    . CYS A 1 36  ? 19.610  -5.785  10.232 1.00 50.07  ? 1253 CYS A SG    1 
ATOM   248  N  N     . TYR A 1 37  ? 17.784  -10.329 9.502  1.00 29.44  ? 1254 TYR A N     1 
ATOM   249  C  CA    . TYR A 1 37  ? 17.006  -11.462 9.034  1.00 29.87  ? 1254 TYR A CA    1 
ATOM   250  C  C     . TYR A 1 37  ? 15.955  -11.758 10.080 1.00 35.95  ? 1254 TYR A C     1 
ATOM   251  O  O     . TYR A 1 37  ? 16.253  -11.777 11.274 1.00 41.67  ? 1254 TYR A O     1 
ATOM   252  C  CB    . TYR A 1 37  ? 17.897  -12.694 8.770  1.00 35.41  ? 1254 TYR A CB    1 
ATOM   253  C  CG    . TYR A 1 37  ? 19.088  -12.428 7.866  1.00 30.55  ? 1254 TYR A CG    1 
ATOM   254  C  CD1   . TYR A 1 37  ? 18.988  -12.584 6.500  1.00 31.28  ? 1254 TYR A CD1   1 
ATOM   255  C  CD2   . TYR A 1 37  ? 20.302  -12.003 8.380  1.00 30.45  ? 1254 TYR A CD2   1 
ATOM   256  C  CE1   . TYR A 1 37  ? 20.059  -12.329 5.667  1.00 31.91  ? 1254 TYR A CE1   1 
ATOM   257  C  CE2   . TYR A 1 37  ? 21.383  -11.734 7.552  1.00 31.07  ? 1254 TYR A CE2   1 
ATOM   258  C  CZ    . TYR A 1 37  ? 21.250  -11.907 6.193  1.00 34.32  ? 1254 TYR A CZ    1 
ATOM   259  O  OH    . TYR A 1 37  ? 22.288  -11.659 5.325  1.00 45.31  ? 1254 TYR A OH    1 
ATOM   260  N  N     . ILE A 1 38  ? 14.722  -11.950 9.636  1.00 42.80  ? 1255 ILE A N     1 
ATOM   261  C  CA    . ILE A 1 38  ? 13.644  -12.259 10.565 1.00 48.71  ? 1255 ILE A CA    1 
ATOM   262  C  C     . ILE A 1 38  ? 13.832  -13.675 11.097 1.00 46.18  ? 1255 ILE A C     1 
ATOM   263  O  O     . ILE A 1 38  ? 13.830  -14.637 10.325 1.00 68.32  ? 1255 ILE A O     1 
ATOM   264  C  CB    . ILE A 1 38  ? 12.276  -12.087 9.892  1.00 42.78  ? 1255 ILE A CB    1 
ATOM   265  C  CG1   . ILE A 1 38  ? 12.176  -10.705 9.266  1.00 53.36  ? 1255 ILE A CG1   1 
ATOM   266  C  CG2   . ILE A 1 38  ? 11.191  -12.175 10.907 1.00 43.96  ? 1255 ILE A CG2   1 
ATOM   267  C  CD1   . ILE A 1 38  ? 11.012  -10.532 8.323  1.00 52.86  ? 1255 ILE A CD1   1 
ATOM   268  N  N     . LEU A 1 39  ? 13.961  -13.810 12.414 1.00 31.06  ? 1256 LEU A N     1 
ATOM   269  C  CA    . LEU A 1 39  ? 14.027  -15.110 13.074 1.00 28.20  ? 1256 LEU A CA    1 
ATOM   270  C  C     . LEU A 1 39  ? 12.616  -15.617 13.315 1.00 43.28  ? 1256 LEU A C     1 
ATOM   271  O  O     . LEU A 1 39  ? 11.917  -15.130 14.220 1.00 30.61  ? 1256 LEU A O     1 
ATOM   272  C  CB    . LEU A 1 39  ? 14.739  -15.023 14.415 1.00 27.75  ? 1256 LEU A CB    1 
ATOM   273  C  CG    . LEU A 1 39  ? 16.130  -14.465 14.349 1.00 31.38  ? 1256 LEU A CG    1 
ATOM   274  C  CD1   . LEU A 1 39  ? 16.835  -14.829 15.666 1.00 27.46  ? 1256 LEU A CD1   1 
ATOM   275  C  CD2   . LEU A 1 39  ? 16.792  -14.997 13.096 1.00 28.32  ? 1256 LEU A CD2   1 
ATOM   276  N  N     . ARG A 1 40  ? 12.225  -16.640 12.558 1.00 40.79  ? 1257 ARG A N     1 
ATOM   277  C  CA    . ARG A 1 40  ? 10.913  -17.236 12.721 1.00 39.09  ? 1257 ARG A CA    1 
ATOM   278  C  C     . ARG A 1 40  ? 10.890  -18.106 13.973 1.00 43.74  ? 1257 ARG A C     1 
ATOM   279  O  O     . ARG A 1 40  ? 11.909  -18.332 14.638 1.00 44.19  ? 1257 ARG A O     1 
ATOM   280  C  CB    . ARG A 1 40  ? 10.542  -18.017 11.469 1.00 34.55  ? 1257 ARG A CB    1 
ATOM   281  C  CG    . ARG A 1 40  ? 10.839  -17.200 10.215 1.00 34.51  ? 1257 ARG A CG    1 
ATOM   282  C  CD    . ARG A 1 40  ? 10.259  -17.804 8.949  1.00 31.36  ? 1257 ARG A CD    1 
ATOM   283  N  NE    . ARG A 1 40  ? 8.838   -18.134 9.040  1.00 33.44  ? 1257 ARG A NE    1 
ATOM   284  C  CZ    . ARG A 1 40  ? 8.200   -18.851 8.123  1.00 35.71  ? 1257 ARG A CZ    1 
ATOM   285  N  NH1   . ARG A 1 40  ? 8.874   -19.298 7.084  1.00 39.25  ? 1257 ARG A NH1   1 
ATOM   286  N  NH2   . ARG A 1 40  ? 6.909   -19.130 8.241  1.00 41.29  ? 1257 ARG A NH2   1 
ATOM   287  N  N     . HIS A 1 41  ? 9.696   -18.591 14.290 1.00 45.95  ? 1258 HIS A N     1 
ATOM   288  C  CA    . HIS A 1 41  ? 9.492   -19.315 15.538 1.00 52.05  ? 1258 HIS A CA    1 
ATOM   289  C  C     . HIS A 1 41  ? 10.444  -20.511 15.659 1.00 59.12  ? 1258 HIS A C     1 
ATOM   290  O  O     . HIS A 1 41  ? 10.963  -20.789 16.748 1.00 60.55  ? 1258 HIS A O     1 
ATOM   291  C  CB    . HIS A 1 41  ? 8.029   -19.736 15.616 1.00 49.70  ? 1258 HIS A CB    1 
ATOM   292  C  CG    . HIS A 1 41  ? 7.804   -20.970 16.409 1.00 70.91  ? 1258 HIS A CG    1 
ATOM   293  N  ND1   . HIS A 1 41  ? 8.044   -21.031 17.765 1.00 81.32  ? 1258 HIS A ND1   1 
ATOM   294  C  CD2   . HIS A 1 41  ? 7.387   -22.203 16.039 1.00 77.33  ? 1258 HIS A CD2   1 
ATOM   295  C  CE1   . HIS A 1 41  ? 7.762   -22.246 18.202 1.00 82.97  ? 1258 HIS A CE1   1 
ATOM   296  N  NE2   . HIS A 1 41  ? 7.363   -22.976 17.174 1.00 79.93  ? 1258 HIS A NE2   1 
ATOM   297  N  N     . TRP A 1 42  ? 10.694  -21.212 14.542 1.00 50.35  ? 1259 TRP A N     1 
ATOM   298  C  CA    . TRP A 1 42  ? 11.502  -22.430 14.527 1.00 50.39  ? 1259 TRP A CA    1 
ATOM   299  C  C     . TRP A 1 42  ? 12.941  -22.168 14.986 1.00 52.45  ? 1259 TRP A C     1 
ATOM   300  O  O     . TRP A 1 42  ? 13.412  -22.718 16.003 1.00 69.67  ? 1259 TRP A O     1 
ATOM   301  C  CB    . TRP A 1 42  ? 11.472  -22.999 13.105 1.00 50.57  ? 1259 TRP A CB    1 
ATOM   302  C  CG    . TRP A 1 42  ? 11.644  -24.503 12.920 1.00 56.75  ? 1259 TRP A CG    1 
ATOM   303  C  CD1   . TRP A 1 42  ? 12.621  -25.122 12.193 1.00 64.03  ? 1259 TRP A CD1   1 
ATOM   304  C  CD2   . TRP A 1 42  ? 10.806  -25.555 13.424 1.00 53.03  ? 1259 TRP A CD2   1 
ATOM   305  N  NE1   . TRP A 1 42  ? 12.462  -26.485 12.230 1.00 56.71  ? 1259 TRP A NE1   1 
ATOM   306  C  CE2   . TRP A 1 42  ? 11.353  -26.779 12.976 1.00 55.71  ? 1259 TRP A CE2   1 
ATOM   307  C  CE3   . TRP A 1 42  ? 9.662   -25.585 14.227 1.00 56.99  ? 1259 TRP A CE3   1 
ATOM   308  C  CZ2   . TRP A 1 42  ? 10.787  -28.022 13.295 1.00 58.93  ? 1259 TRP A CZ2   1 
ATOM   309  C  CZ3   . TRP A 1 42  ? 9.098   -26.831 14.547 1.00 61.64  ? 1259 TRP A CZ3   1 
ATOM   310  C  CH2   . TRP A 1 42  ? 9.662   -28.027 14.077 1.00 55.72  ? 1259 TRP A CH2   1 
ATOM   311  N  N     . SER A 1 43  ? 13.646  -21.285 14.275 1.00 45.66  ? 1260 SER A N     1 
ATOM   312  C  CA    . SER A 1 43  ? 15.024  -20.991 14.664 1.00 35.37  ? 1260 SER A CA    1 
ATOM   313  C  C     . SER A 1 43  ? 15.044  -20.409 16.059 1.00 28.74  ? 1260 SER A C     1 
ATOM   314  O  O     . SER A 1 43  ? 15.902  -20.754 16.886 1.00 29.18  ? 1260 SER A O     1 
ATOM   315  C  CB    . SER A 1 43  ? 15.683  -20.023 13.685 1.00 29.33  ? 1260 SER A CB    1 
ATOM   316  O  OG    . SER A 1 43  ? 14.815  -18.957 13.384 1.00 33.65  ? 1260 SER A OG    1 
ATOM   317  N  N     . PHE A 1 44  ? 14.097  -19.532 16.356 1.00 28.35  ? 1261 PHE A N     1 
ATOM   318  C  CA    . PHE A 1 44  ? 14.158  -18.905 17.656 1.00 45.25  ? 1261 PHE A CA    1 
ATOM   319  C  C     . PHE A 1 44  ? 13.982  -19.938 18.767 1.00 41.04  ? 1261 PHE A C     1 
ATOM   320  O  O     . PHE A 1 44  ? 14.541  -19.773 19.854 1.00 33.18  ? 1261 PHE A O     1 
ATOM   321  C  CB    . PHE A 1 44  ? 13.133  -17.773 17.767 1.00 27.48  ? 1261 PHE A CB    1 
ATOM   322  C  CG    . PHE A 1 44  ? 13.500  -16.774 18.825 1.00 29.34  ? 1261 PHE A CG    1 
ATOM   323  C  CD1   . PHE A 1 44  ? 14.576  -15.932 18.639 1.00 33.36  ? 1261 PHE A CD1   1 
ATOM   324  C  CD2   . PHE A 1 44  ? 12.825  -16.733 20.015 1.00 33.40  ? 1261 PHE A CD2   1 
ATOM   325  C  CE1   . PHE A 1 44  ? 14.939  -15.055 19.589 1.00 33.60  ? 1261 PHE A CE1   1 
ATOM   326  C  CE2   . PHE A 1 44  ? 13.186  -15.858 20.965 1.00 38.96  ? 1261 PHE A CE2   1 
ATOM   327  C  CZ    . PHE A 1 44  ? 14.248  -15.012 20.757 1.00 37.48  ? 1261 PHE A CZ    1 
ATOM   328  N  N     . ALA A 1 45  ? 13.228  -21.013 18.516 1.00 38.41  ? 1262 ALA A N     1 
ATOM   329  C  CA    . ALA A 1 45  ? 13.114  -22.057 19.526 1.00 41.87  ? 1262 ALA A CA    1 
ATOM   330  C  C     . ALA A 1 45  ? 14.463  -22.695 19.758 1.00 41.22  ? 1262 ALA A C     1 
ATOM   331  O  O     . ALA A 1 45  ? 14.834  -22.990 20.908 1.00 38.39  ? 1262 ALA A O     1 
ATOM   332  C  CB    . ALA A 1 45  ? 12.086  -23.113 19.108 1.00 46.17  ? 1262 ALA A CB    1 
ATOM   333  N  N     . ILE A 1 46  ? 15.225  -22.882 18.670 1.00 41.06  ? 1263 ILE A N     1 
ATOM   334  C  CA    . ILE A 1 46  ? 16.585  -23.426 18.802 1.00 43.32  ? 1263 ILE A CA    1 
ATOM   335  C  C     . ILE A 1 46  ? 17.442  -22.517 19.686 1.00 48.28  ? 1263 ILE A C     1 
ATOM   336  O  O     . ILE A 1 46  ? 18.152  -22.968 20.615 1.00 55.53  ? 1263 ILE A O     1 
ATOM   337  C  CB    . ILE A 1 46  ? 17.234  -23.609 17.416 1.00 35.62  ? 1263 ILE A CB    1 
ATOM   338  C  CG1   . ILE A 1 46  ? 16.466  -24.636 16.570 1.00 30.41  ? 1263 ILE A CG1   1 
ATOM   339  C  CG2   . ILE A 1 46  ? 18.734  -23.932 17.571 1.00 30.02  ? 1263 ILE A CG2   1 
ATOM   340  C  CD1   . ILE A 1 46  ? 17.032  -24.859 15.185 1.00 30.91  ? 1263 ILE A CD1   1 
ATOM   341  N  N     . TRP A 1 47  ? 17.394  -21.215 19.388 1.00 29.24  ? 1264 TRP A N     1 
ATOM   342  C  CA    . TRP A 1 47  ? 18.143  -20.246 20.178 1.00 51.32  ? 1264 TRP A CA    1 
ATOM   343  C  C     . TRP A 1 47  ? 17.703  -20.271 21.638 1.00 53.90  ? 1264 TRP A C     1 
ATOM   344  O  O     . TRP A 1 47  ? 18.534  -20.195 22.548 1.00 61.37  ? 1264 TRP A O     1 
ATOM   345  C  CB    . TRP A 1 47  ? 17.977  -18.839 19.584 1.00 56.33  ? 1264 TRP A CB    1 
ATOM   346  C  CG    . TRP A 1 47  ? 18.594  -17.763 20.433 1.00 53.62  ? 1264 TRP A CG    1 
ATOM   347  C  CD1   . TRP A 1 47  ? 17.941  -16.793 21.156 1.00 59.43  ? 1264 TRP A CD1   1 
ATOM   348  C  CD2   . TRP A 1 47  ? 19.984  -17.561 20.666 1.00 50.95  ? 1264 TRP A CD2   1 
ATOM   349  N  NE1   . TRP A 1 47  ? 18.847  -15.999 21.819 1.00 52.17  ? 1264 TRP A NE1   1 
ATOM   350  C  CE2   . TRP A 1 47  ? 20.109  -16.454 21.536 1.00 49.73  ? 1264 TRP A CE2   1 
ATOM   351  C  CE3   . TRP A 1 47  ? 21.138  -18.211 20.230 1.00 51.23  ? 1264 TRP A CE3   1 
ATOM   352  C  CZ2   . TRP A 1 47  ? 21.344  -15.987 21.970 1.00 51.65  ? 1264 TRP A CZ2   1 
ATOM   353  C  CZ3   . TRP A 1 47  ? 22.359  -17.741 20.659 1.00 54.96  ? 1264 TRP A CZ3   1 
ATOM   354  C  CH2   . TRP A 1 47  ? 22.454  -16.641 21.523 1.00 53.46  ? 1264 TRP A CH2   1 
ATOM   355  N  N     . LYS A 1 48  ? 16.399  -20.386 21.872 1.00 48.81  ? 1265 LYS A N     1 
ATOM   356  C  CA    . LYS A 1 48  ? 15.855  -20.355 23.222 1.00 45.03  ? 1265 LYS A CA    1 
ATOM   357  C  C     . LYS A 1 48  ? 16.396  -21.507 24.051 1.00 54.83  ? 1265 LYS A C     1 
ATOM   358  O  O     . LYS A 1 48  ? 16.773  -21.331 25.215 1.00 58.32  ? 1265 LYS A O     1 
ATOM   359  C  CB    . LYS A 1 48  ? 14.326  -20.388 23.149 1.00 42.23  ? 1265 LYS A CB    1 
ATOM   360  C  CG    . LYS A 1 48  ? 13.616  -19.854 24.371 1.00 48.11  ? 1265 LYS A CG    1 
ATOM   361  C  CD    . LYS A 1 48  ? 12.127  -20.185 24.357 1.00 61.94  ? 1265 LYS A CD    1 
ATOM   362  C  CE    . LYS A 1 48  ? 11.366  -19.457 23.241 1.00 64.39  ? 1265 LYS A CE    1 
ATOM   363  N  NZ    . LYS A 1 48  ? 9.890   -19.777 23.334 1.00 57.00  ? 1265 LYS A NZ    1 
ATOM   364  N  N     . ALA A 1 49  ? 16.425  -22.704 23.467 1.00 54.86  ? 1266 ALA A N     1 
ATOM   365  C  CA    . ALA A 1 49  ? 16.998  -23.842 24.177 1.00 49.37  ? 1266 ALA A CA    1 
ATOM   366  C  C     . ALA A 1 49  ? 18.461  -23.592 24.527 1.00 51.12  ? 1266 ALA A C     1 
ATOM   367  O  O     . ALA A 1 49  ? 18.877  -23.789 25.679 1.00 60.42  ? 1266 ALA A O     1 
ATOM   368  C  CB    . ALA A 1 49  ? 16.839  -25.123 23.351 1.00 52.29  ? 1266 ALA A CB    1 
ATOM   369  N  N     . ILE A 1 50  ? 19.266  -23.163 23.548 1.00 44.59  ? 1267 ILE A N     1 
ATOM   370  C  CA    . ILE A 1 50  ? 20.680  -22.906 23.846 1.00 43.12  ? 1267 ILE A CA    1 
ATOM   371  C  C     . ILE A 1 50  ? 20.814  -21.895 24.985 1.00 42.55  ? 1267 ILE A C     1 
ATOM   372  O  O     . ILE A 1 50  ? 21.634  -22.049 25.907 1.00 29.70  ? 1267 ILE A O     1 
ATOM   373  C  CB    . ILE A 1 50  ? 21.414  -22.410 22.593 1.00 39.90  ? 1267 ILE A CB    1 
ATOM   374  C  CG1   . ILE A 1 50  ? 21.239  -23.376 21.428 1.00 41.20  ? 1267 ILE A CG1   1 
ATOM   375  C  CG2   . ILE A 1 50  ? 22.874  -22.147 22.924 1.00 31.94  ? 1267 ILE A CG2   1 
ATOM   376  C  CD1   . ILE A 1 50  ? 21.961  -22.896 20.190 1.00 45.80  ? 1267 ILE A CD1   1 
ATOM   377  N  N     . ARG A 1 51  ? 20.035  -20.815 24.901 1.00 37.09  ? 1268 ARG A N     1 
ATOM   378  C  CA    . ARG A 1 51  ? 20.088  -19.758 25.895 1.00 39.14  ? 1268 ARG A CA    1 
ATOM   379  C  C     . ARG A 1 51  ? 19.723  -20.278 27.282 1.00 42.79  ? 1268 ARG A C     1 
ATOM   380  O  O     . ARG A 1 51  ? 20.406  -19.983 28.268 1.00 39.00  ? 1268 ARG A O     1 
ATOM   381  C  CB    . ARG A 1 51  ? 19.149  -18.630 25.483 1.00 45.89  ? 1268 ARG A CB    1 
ATOM   382  C  CG    . ARG A 1 51  ? 19.041  -17.513 26.513 1.00 50.00  ? 1268 ARG A CG    1 
ATOM   383  C  CD    . ARG A 1 51  ? 17.621  -17.015 26.640 1.00 64.65  ? 1268 ARG A CD    1 
ATOM   384  N  NE    . ARG A 1 51  ? 17.495  -16.140 27.801 1.00 87.81  ? 1268 ARG A NE    1 
ATOM   385  C  CZ    . ARG A 1 51  ? 16.940  -14.930 27.775 1.00 92.90  ? 1268 ARG A CZ    1 
ATOM   386  N  NH1   . ARG A 1 51  ? 16.444  -14.453 26.639 1.00 100.04 ? 1268 ARG A NH1   1 
ATOM   387  N  NH2   . ARG A 1 51  ? 16.878  -14.197 28.886 1.00 81.38  ? 1268 ARG A NH2   1 
ATOM   388  N  N     . ASN A 1 52  ? 18.636  -21.036 27.387 1.00 27.98  ? 1269 ASN A N     1 
ATOM   389  C  CA    . ASN A 1 52  ? 18.210  -21.479 28.708 1.00 42.02  ? 1269 ASN A CA    1 
ATOM   390  C  C     . ASN A 1 52  ? 19.224  -22.429 29.313 1.00 43.79  ? 1269 ASN A C     1 
ATOM   391  O  O     . ASN A 1 52  ? 19.481  -22.392 30.523 1.00 38.94  ? 1269 ASN A O     1 
ATOM   392  C  CB    . ASN A 1 52  ? 16.837  -22.119 28.629 1.00 57.73  ? 1269 ASN A CB    1 
ATOM   393  C  CG    . ASN A 1 52  ? 15.842  -21.221 27.960 1.00 64.44  ? 1269 ASN A CG    1 
ATOM   394  O  OD1   . ASN A 1 52  ? 14.981  -21.678 27.221 1.00 81.56  ? 1269 ASN A OD1   1 
ATOM   395  N  ND2   . ASN A 1 52  ? 15.969  -19.925 28.190 1.00 58.21  ? 1269 ASN A ND2   1 
ATOM   396  N  N     . TRP A 1 53  ? 19.774  -23.321 28.490 1.00 46.51  ? 1270 TRP A N     1 
ATOM   397  C  CA    . TRP A 1 53  ? 20.835  -24.194 28.970 1.00 48.28  ? 1270 TRP A CA    1 
ATOM   398  C  C     . TRP A 1 53  ? 21.981  -23.386 29.541 1.00 50.46  ? 1270 TRP A C     1 
ATOM   399  O  O     . TRP A 1 53  ? 22.341  -23.537 30.718 1.00 65.48  ? 1270 TRP A O     1 
ATOM   400  C  CB    . TRP A 1 53  ? 21.334  -25.101 27.841 1.00 59.96  ? 1270 TRP A CB    1 
ATOM   401  C  CG    . TRP A 1 53  ? 22.228  -26.176 28.362 1.00 57.07  ? 1270 TRP A CG    1 
ATOM   402  C  CD1   . TRP A 1 53  ? 21.844  -27.372 28.893 1.00 49.57  ? 1270 TRP A CD1   1 
ATOM   403  C  CD2   . TRP A 1 53  ? 23.655  -26.137 28.447 1.00 54.27  ? 1270 TRP A CD2   1 
ATOM   404  N  NE1   . TRP A 1 53  ? 22.941  -28.077 29.300 1.00 40.18  ? 1270 TRP A NE1   1 
ATOM   405  C  CE2   . TRP A 1 53  ? 24.068  -27.347 29.035 1.00 39.65  ? 1270 TRP A CE2   1 
ATOM   406  C  CE3   . TRP A 1 53  ? 24.628  -25.196 28.083 1.00 57.74  ? 1270 TRP A CE3   1 
ATOM   407  C  CZ2   . TRP A 1 53  ? 25.414  -27.650 29.264 1.00 33.14  ? 1270 TRP A CZ2   1 
ATOM   408  C  CZ3   . TRP A 1 53  ? 25.970  -25.500 28.317 1.00 55.09  ? 1270 TRP A CZ3   1 
ATOM   409  C  CH2   . TRP A 1 53  ? 26.346  -26.724 28.896 1.00 38.73  ? 1270 TRP A CH2   1 
ATOM   410  N  N     . PHE A 1 54  ? 22.557  -22.501 28.719 1.00 48.53  ? 1271 PHE A N     1 
ATOM   411  C  CA    . PHE A 1 54  ? 23.725  -21.747 29.166 1.00 54.11  ? 1271 PHE A CA    1 
ATOM   412  C  C     . PHE A 1 54  ? 23.393  -20.849 30.347 1.00 54.38  ? 1271 PHE A C     1 
ATOM   413  O  O     . PHE A 1 54  ? 24.247  -20.623 31.215 1.00 58.04  ? 1271 PHE A O     1 
ATOM   414  C  CB    . PHE A 1 54  ? 24.305  -20.922 28.025 1.00 48.53  ? 1271 PHE A CB    1 
ATOM   415  C  CG    . PHE A 1 54  ? 25.681  -20.365 28.304 1.00 34.13  ? 1271 PHE A CG    1 
ATOM   416  C  CD1   . PHE A 1 54  ? 26.813  -21.094 28.017 1.00 36.40  ? 1271 PHE A CD1   1 
ATOM   417  C  CD2   . PHE A 1 54  ? 25.833  -19.110 28.835 1.00 33.13  ? 1271 PHE A CD2   1 
ATOM   418  C  CE1   . PHE A 1 54  ? 28.061  -20.567 28.258 1.00 41.89  ? 1271 PHE A CE1   1 
ATOM   419  C  CE2   . PHE A 1 54  ? 27.088  -18.582 29.075 1.00 28.87  ? 1271 PHE A CE2   1 
ATOM   420  C  CZ    . PHE A 1 54  ? 28.188  -19.297 28.796 1.00 33.26  ? 1271 PHE A CZ    1 
ATOM   421  N  N     . ASP A 1 55  ? 22.171  -20.331 30.412 1.00 28.46  ? 1272 ASP A N     1 
ATOM   422  C  CA    . ASP A 1 55  ? 21.868  -19.464 31.533 1.00 28.27  ? 1272 ASP A CA    1 
ATOM   423  C  C     . ASP A 1 55  ? 21.704  -20.258 32.811 1.00 35.36  ? 1272 ASP A C     1 
ATOM   424  O  O     . ASP A 1 55  ? 22.147  -19.813 33.876 1.00 36.89  ? 1272 ASP A O     1 
ATOM   425  C  CB    . ASP A 1 55  ? 20.631  -18.616 31.296 1.00 31.47  ? 1272 ASP A CB    1 
ATOM   426  C  CG    . ASP A 1 55  ? 20.524  -17.504 32.329 1.00 49.04  ? 1272 ASP A CG    1 
ATOM   427  O  OD1   . ASP A 1 55  ? 21.368  -16.565 32.278 1.00 46.20  ? 1272 ASP A OD1   1 
ATOM   428  O  OD2   . ASP A 1 55  ? 19.643  -17.601 33.221 1.00 56.65  ? 1272 ASP A OD2   1 
ATOM   429  N  N     . ALA A 1 56  ? 21.069  -21.429 32.735 1.00 39.25  ? 1273 ALA A N     1 
ATOM   430  C  CA    . ALA A 1 56  ? 21.017  -22.297 33.904 1.00 46.29  ? 1273 ALA A CA    1 
ATOM   431  C  C     . ALA A 1 56  ? 22.419  -22.550 34.427 1.00 33.08  ? 1273 ALA A C     1 
ATOM   432  O  O     . ALA A 1 56  ? 22.692  -22.400 35.628 1.00 30.44  ? 1273 ALA A O     1 
ATOM   433  C  CB    . ALA A 1 56  ? 20.323  -23.612 33.557 1.00 51.67  ? 1273 ALA A CB    1 
ATOM   434  N  N     . GLU A 1 57  ? 23.338  -22.846 33.503 1.00 30.22  ? 1274 GLU A N     1 
ATOM   435  C  CA    . GLU A 1 57  ? 24.714  -23.153 33.875 1.00 33.40  ? 1274 GLU A CA    1 
ATOM   436  C  C     . GLU A 1 57  ? 25.385  -21.976 34.566 1.00 41.43  ? 1274 GLU A C     1 
ATOM   437  O  O     . GLU A 1 57  ? 25.923  -22.116 35.677 1.00 38.65  ? 1274 GLU A O     1 
ATOM   438  C  CB    . GLU A 1 57  ? 25.506  -23.578 32.637 1.00 30.82  ? 1274 GLU A CB    1 
ATOM   439  C  CG    . GLU A 1 57  ? 25.365  -25.055 32.326 1.00 52.48  ? 1274 GLU A CG    1 
ATOM   440  C  CD    . GLU A 1 57  ? 25.277  -25.910 33.602 1.00 70.01  ? 1274 GLU A CD    1 
ATOM   441  O  OE1   . GLU A 1 57  ? 26.245  -25.915 34.392 1.00 76.89  ? 1274 GLU A OE1   1 
ATOM   442  O  OE2   . GLU A 1 57  ? 24.229  -26.555 33.836 1.00 75.67  ? 1274 GLU A OE2   1 
ATOM   443  N  N     . ILE A 1 58  ? 25.319  -20.791 33.950 1.00 49.50  ? 1275 ILE A N     1 
ATOM   444  C  CA    . ILE A 1 58  ? 26.120  -19.690 34.479 1.00 50.15  ? 1275 ILE A CA    1 
ATOM   445  C  C     . ILE A 1 58  ? 25.488  -19.077 35.715 1.00 48.69  ? 1275 ILE A C     1 
ATOM   446  O  O     . ILE A 1 58  ? 26.202  -18.538 36.569 1.00 55.65  ? 1275 ILE A O     1 
ATOM   447  C  CB    . ILE A 1 58  ? 26.356  -18.616 33.414 1.00 50.38  ? 1275 ILE A CB    1 
ATOM   448  C  CG1   . ILE A 1 58  ? 25.015  -18.064 32.922 1.00 47.90  ? 1275 ILE A CG1   1 
ATOM   449  C  CG2   . ILE A 1 58  ? 27.227  -19.170 32.310 1.00 53.20  ? 1275 ILE A CG2   1 
ATOM   450  C  CD1   . ILE A 1 58  ? 25.029  -16.610 32.637 1.00 43.97  ? 1275 ILE A CD1   1 
ATOM   451  N  N     . THR A 1 59  ? 24.169  -19.163 35.879 1.00 36.09  ? 1276 THR A N     1 
ATOM   452  C  CA    . THR A 1 59  ? 23.664  -18.663 37.143 1.00 38.12  ? 1276 THR A CA    1 
ATOM   453  C  C     . THR A 1 59  ? 23.872  -19.687 38.243 1.00 48.22  ? 1276 THR A C     1 
ATOM   454  O  O     . THR A 1 59  ? 23.992  -19.302 39.408 1.00 48.64  ? 1276 THR A O     1 
ATOM   455  C  CB    . THR A 1 59  ? 22.198  -18.210 37.045 1.00 36.37  ? 1276 THR A CB    1 
ATOM   456  O  OG1   . THR A 1 59  ? 21.327  -19.314 37.188 1.00 50.34  ? 1276 THR A OG1   1 
ATOM   457  C  CG2   . THR A 1 59  ? 21.892  -17.497 35.731 1.00 37.49  ? 1276 THR A CG2   1 
ATOM   458  N  N     . ARG A 1 60  ? 23.939  -20.983 37.897 1.00 54.97  ? 1277 ARG A N     1 
ATOM   459  C  CA    . ARG A 1 60  ? 24.362  -21.978 38.878 1.00 62.95  ? 1277 ARG A CA    1 
ATOM   460  C  C     . ARG A 1 60  ? 25.786  -21.739 39.353 1.00 58.29  ? 1277 ARG A C     1 
ATOM   461  O  O     . ARG A 1 60  ? 26.101  -21.985 40.523 1.00 71.03  ? 1277 ARG A O     1 
ATOM   462  C  CB    . ARG A 1 60  ? 24.243  -23.387 38.308 1.00 77.37  ? 1277 ARG A CB    1 
ATOM   463  C  CG    . ARG A 1 60  ? 24.344  -24.464 39.380 1.00 82.77  ? 1277 ARG A CG    1 
ATOM   464  C  CD    . ARG A 1 60  ? 24.687  -25.823 38.794 1.00 90.29  ? 1277 ARG A CD    1 
ATOM   465  N  NE    . ARG A 1 60  ? 26.104  -26.159 38.924 1.00 94.44  ? 1277 ARG A NE    1 
ATOM   466  C  CZ    . ARG A 1 60  ? 26.988  -26.082 37.934 1.00 93.41  ? 1277 ARG A CZ    1 
ATOM   467  N  NH1   . ARG A 1 60  ? 26.612  -25.678 36.728 1.00 89.22  ? 1277 ARG A NH1   1 
ATOM   468  N  NH2   . ARG A 1 60  ? 28.251  -26.420 38.151 1.00 97.06  ? 1277 ARG A NH2   1 
ATOM   469  N  N     . LEU A 1 61  ? 26.674  -21.292 38.464 1.00 36.13  ? 1278 LEU A N     1 
ATOM   470  C  CA    . LEU A 1 61  ? 28.027  -21.010 38.938 1.00 42.44  ? 1278 LEU A CA    1 
ATOM   471  C  C     . LEU A 1 61  ? 28.064  -19.754 39.806 1.00 50.16  ? 1278 LEU A C     1 
ATOM   472  O  O     . LEU A 1 61  ? 28.910  -19.644 40.697 1.00 49.83  ? 1278 LEU A O     1 
ATOM   473  C  CB    . LEU A 1 61  ? 28.982  -20.839 37.764 1.00 44.11  ? 1278 LEU A CB    1 
ATOM   474  C  CG    . LEU A 1 61  ? 29.110  -21.939 36.721 1.00 42.14  ? 1278 LEU A CG    1 
ATOM   475  C  CD1   . LEU A 1 61  ? 29.969  -21.450 35.567 1.00 32.65  ? 1278 LEU A CD1   1 
ATOM   476  C  CD2   . LEU A 1 61  ? 29.721  -23.182 37.345 1.00 39.58  ? 1278 LEU A CD2   1 
ATOM   477  N  N     . GLY A 1 62  ? 27.104  -18.848 39.618 1.00 59.69  ? 1279 GLY A N     1 
ATOM   478  C  CA    . GLY A 1 62  ? 26.980  -17.606 40.366 1.00 56.06  ? 1279 GLY A CA    1 
ATOM   479  C  C     . GLY A 1 62  ? 26.990  -16.312 39.564 1.00 43.04  ? 1279 GLY A C     1 
ATOM   480  O  O     . GLY A 1 62  ? 26.867  -15.228 40.130 1.00 35.44  ? 1279 GLY A O     1 
ATOM   481  N  N     . VAL A 1 63  ? 26.978  -16.388 38.243 1.00 43.60  ? 1280 VAL A N     1 
ATOM   482  C  CA    . VAL A 1 63  ? 26.970  -15.155 37.482 1.00 29.64  ? 1280 VAL A CA    1 
ATOM   483  C  C     . VAL A 1 63  ? 25.581  -14.556 37.531 1.00 46.23  ? 1280 VAL A C     1 
ATOM   484  O  O     . VAL A 1 63  ? 24.570  -15.264 37.395 1.00 31.02  ? 1280 VAL A O     1 
ATOM   485  C  CB    . VAL A 1 63  ? 27.406  -15.385 36.029 1.00 34.77  ? 1280 VAL A CB    1 
ATOM   486  C  CG1   . VAL A 1 63  ? 27.485  -14.052 35.307 1.00 35.06  ? 1280 VAL A CG1   1 
ATOM   487  C  CG2   . VAL A 1 63  ? 28.728  -16.088 35.978 1.00 29.93  ? 1280 VAL A CG2   1 
ATOM   488  N  N     . LYS A 1 64  ? 25.526  -13.248 37.782 1.00 46.61  ? 1281 LYS A N     1 
ATOM   489  C  CA    . LYS A 1 64  ? 24.278  -12.503 37.795 1.00 47.03  ? 1281 LYS A CA    1 
ATOM   490  C  C     . LYS A 1 64  ? 24.033  -11.791 36.469 1.00 46.70  ? 1281 LYS A C     1 
ATOM   491  O  O     . LYS A 1 64  ? 24.952  -11.514 35.692 1.00 49.81  ? 1281 LYS A O     1 
ATOM   492  C  CB    . LYS A 1 64  ? 24.278  -11.490 38.929 1.00 38.68  ? 1281 LYS A CB    1 
ATOM   493  C  CG    . LYS A 1 64  ? 23.916  -12.092 40.229 1.00 29.34  ? 1281 LYS A CG    1 
ATOM   494  C  CD    . LYS A 1 64  ? 24.851  -11.615 41.269 1.00 32.75  ? 1281 LYS A CD    1 
ATOM   495  C  CE    . LYS A 1 64  ? 24.478  -12.168 42.601 1.00 42.08  ? 1281 LYS A CE    1 
ATOM   496  N  NZ    . LYS A 1 64  ? 25.200  -11.383 43.620 1.00 64.45  ? 1281 LYS A NZ    1 
ATOM   497  N  N     . GLU A 1 65  ? 22.773  -11.443 36.255 1.00 42.54  ? 1282 GLU A N     1 
ATOM   498  C  CA    . GLU A 1 65  ? 22.302  -10.905 34.990 1.00 44.69  ? 1282 GLU A CA    1 
ATOM   499  C  C     . GLU A 1 65  ? 21.785  -9.488  35.186 1.00 40.48  ? 1282 GLU A C     1 
ATOM   500  O  O     . GLU A 1 65  ? 21.143  -9.194  36.198 1.00 40.33  ? 1282 GLU A O     1 
ATOM   501  C  CB    . GLU A 1 65  ? 21.208  -11.792 34.410 1.00 47.52  ? 1282 GLU A CB    1 
ATOM   502  C  CG    . GLU A 1 65  ? 20.502  -11.182 33.250 1.00 48.52  ? 1282 GLU A CG    1 
ATOM   503  C  CD    . GLU A 1 65  ? 19.851  -12.231 32.424 1.00 60.05  ? 1282 GLU A CD    1 
ATOM   504  O  OE1   . GLU A 1 65  ? 20.111  -13.422 32.713 1.00 68.39  ? 1282 GLU A OE1   1 
ATOM   505  O  OE2   . GLU A 1 65  ? 19.080  -11.875 31.508 1.00 65.18  ? 1282 GLU A OE2   1 
ATOM   506  N  N     . CYS A 1 66  ? 22.121  -8.599  34.253 1.00 47.73  ? 1283 CYS A N     1 
ATOM   507  C  CA    . CYS A 1 66  ? 21.710  -7.188  34.295 1.00 53.68  ? 1283 CYS A CA    1 
ATOM   508  C  C     . CYS A 1 66  ? 21.403  -6.753  32.872 1.00 54.12  ? 1283 CYS A C     1 
ATOM   509  O  O     . CYS A 1 66  ? 21.417  -7.568  31.946 1.00 67.79  ? 1283 CYS A O     1 
ATOM   510  C  CB    . CYS A 1 66  ? 22.782  -6.293  34.920 1.00 50.53  ? 1283 CYS A CB    1 
ATOM   511  S  SG    . CYS A 1 66  ? 24.314  -6.385  33.984 1.00 52.37  ? 1283 CYS A SG    1 
ATOM   512  N  N     . TYR A 1 67  ? 21.138  -5.462  32.684 1.00 41.15  ? 1284 TYR A N     1 
ATOM   513  C  CA    . TYR A 1 67  ? 20.849  -4.971  31.338 1.00 36.89  ? 1284 TYR A CA    1 
ATOM   514  C  C     . TYR A 1 67  ? 21.149  -3.478  31.261 1.00 38.98  ? 1284 TYR A C     1 
ATOM   515  O  O     . TYR A 1 67  ? 20.405  -2.656  31.813 1.00 46.52  ? 1284 TYR A O     1 
ATOM   516  C  CB    . TYR A 1 67  ? 19.392  -5.272  30.954 1.00 26.02  ? 1284 TYR A CB    1 
ATOM   517  C  CG    . TYR A 1 67  ? 19.084  -4.824  29.552 1.00 44.85  ? 1284 TYR A CG    1 
ATOM   518  C  CD1   . TYR A 1 67  ? 19.587  -5.520  28.464 1.00 39.12  ? 1284 TYR A CD1   1 
ATOM   519  C  CD2   . TYR A 1 67  ? 18.353  -3.657  29.308 1.00 47.09  ? 1284 TYR A CD2   1 
ATOM   520  C  CE1   . TYR A 1 67  ? 19.345  -5.104  27.181 1.00 40.24  ? 1284 TYR A CE1   1 
ATOM   521  C  CE2   . TYR A 1 67  ? 18.113  -3.226  28.013 1.00 39.18  ? 1284 TYR A CE2   1 
ATOM   522  C  CZ    . TYR A 1 67  ? 18.614  -3.959  26.961 1.00 36.02  ? 1284 TYR A CZ    1 
ATOM   523  O  OH    . TYR A 1 67  ? 18.410  -3.557  25.680 1.00 32.50  ? 1284 TYR A OH    1 
ATOM   524  N  N     . PHE A 1 68  ? 22.181  -3.139  30.535 1.00 33.55  ? 1285 PHE A N     1 
ATOM   525  C  CA    . PHE A 1 68  ? 22.579  -1.776  30.236 1.00 40.89  ? 1285 PHE A CA    1 
ATOM   526  C  C     . PHE A 1 68  ? 21.848  -1.289  28.992 1.00 47.91  ? 1285 PHE A C     1 
ATOM   527  O  O     . PHE A 1 68  ? 21.381  -2.095  28.188 1.00 51.15  ? 1285 PHE A O     1 
ATOM   528  C  CB    . PHE A 1 68  ? 24.092  -1.718  30.012 1.00 48.32  ? 1285 PHE A CB    1 
ATOM   529  C  CG    . PHE A 1 68  ? 24.914  -1.793  31.288 1.00 47.36  ? 1285 PHE A CG    1 
ATOM   530  C  CD1   . PHE A 1 68  ? 24.918  -2.935  32.069 1.00 41.84  ? 1285 PHE A CD1   1 
ATOM   531  C  CD2   . PHE A 1 68  ? 25.682  -0.713  31.699 1.00 46.17  ? 1285 PHE A CD2   1 
ATOM   532  C  CE1   . PHE A 1 68  ? 25.666  -3.008  33.227 1.00 40.86  ? 1285 PHE A CE1   1 
ATOM   533  C  CE2   . PHE A 1 68  ? 26.429  -0.772  32.854 1.00 43.00  ? 1285 PHE A CE2   1 
ATOM   534  C  CZ    . PHE A 1 68  ? 26.420  -1.922  33.623 1.00 46.38  ? 1285 PHE A CZ    1 
ATOM   535  N  N     . PRO A 1 69  ? 21.724  0.025   28.792 1.00 51.70  ? 1286 PRO A N     1 
ATOM   536  C  CA    . PRO A 1 69  ? 20.983  0.523   27.619 1.00 49.47  ? 1286 PRO A CA    1 
ATOM   537  C  C     . PRO A 1 69  ? 21.643  0.103   26.309 1.00 47.86  ? 1286 PRO A C     1 
ATOM   538  O  O     . PRO A 1 69  ? 22.849  -0.147  26.240 1.00 57.89  ? 1286 PRO A O     1 
ATOM   539  C  CB    . PRO A 1 69  ? 21.029  2.044   27.786 1.00 47.21  ? 1286 PRO A CB    1 
ATOM   540  C  CG    . PRO A 1 69  ? 21.399  2.268   29.231 1.00 47.81  ? 1286 PRO A CG    1 
ATOM   541  C  CD    . PRO A 1 69  ? 22.192  1.108   29.675 1.00 48.53  ? 1286 PRO A CD    1 
ATOM   542  N  N     . ILE A 1 70  ? 20.837  0.030   25.247 1.00 32.75  ? 1287 ILE A N     1 
ATOM   543  C  CA    . ILE A 1 70  ? 21.390  -0.285  23.933 1.00 40.10  ? 1287 ILE A CA    1 
ATOM   544  C  C     . ILE A 1 70  ? 22.244  0.826   23.384 1.00 44.24  ? 1287 ILE A C     1 
ATOM   545  O  O     . ILE A 1 70  ? 22.947  0.616   22.387 1.00 49.62  ? 1287 ILE A O     1 
ATOM   546  C  CB    . ILE A 1 70  ? 20.322  -0.471  22.850 1.00 43.92  ? 1287 ILE A CB    1 
ATOM   547  C  CG1   . ILE A 1 70  ? 19.347  0.685   22.937 1.00 27.07  ? 1287 ILE A CG1   1 
ATOM   548  C  CG2   . ILE A 1 70  ? 19.727  -1.889  22.790 1.00 34.25  ? 1287 ILE A CG2   1 
ATOM   549  C  CD1   . ILE A 1 70  ? 18.382  0.567   21.931 1.00 40.13  ? 1287 ILE A CD1   1 
ATOM   550  N  N     . PHE A 1 71  ? 22.104  2.031   23.929 1.00 43.18  ? 1288 PHE A N     1 
ATOM   551  C  CA    . PHE A 1 71  ? 22.763  3.220   23.416 1.00 28.54  ? 1288 PHE A CA    1 
ATOM   552  C  C     . PHE A 1 71  ? 24.017  3.530   24.225 1.00 28.90  ? 1288 PHE A C     1 
ATOM   553  O  O     . PHE A 1 71  ? 24.040  3.356   25.445 1.00 28.75  ? 1288 PHE A O     1 
ATOM   554  C  CB    . PHE A 1 71  ? 21.821  4.415   23.460 1.00 46.86  ? 1288 PHE A CB    1 
ATOM   555  C  CG    . PHE A 1 71  ? 20.747  4.387   22.426 1.00 40.14  ? 1288 PHE A CG    1 
ATOM   556  C  CD1   . PHE A 1 71  ? 21.052  4.199   21.082 1.00 37.65  ? 1288 PHE A CD1   1 
ATOM   557  C  CD2   . PHE A 1 71  ? 19.425  4.589   22.801 1.00 28.42  ? 1288 PHE A CD2   1 
ATOM   558  C  CE1   . PHE A 1 71  ? 20.056  4.206   20.137 1.00 28.83  ? 1288 PHE A CE1   1 
ATOM   559  C  CE2   . PHE A 1 71  ? 18.429  4.571   21.871 1.00 28.38  ? 1288 PHE A CE2   1 
ATOM   560  C  CZ    . PHE A 1 71  ? 18.733  4.394   20.541 1.00 29.65  ? 1288 PHE A CZ    1 
ATOM   561  N  N     . VAL A 1 72  ? 25.044  4.010   23.524 1.00 45.17  ? 1289 VAL A N     1 
ATOM   562  C  CA    . VAL A 1 72  ? 26.353  4.367   24.065 1.00 41.20  ? 1289 VAL A CA    1 
ATOM   563  C  C     . VAL A 1 72  ? 26.662  5.834   23.741 1.00 46.87  ? 1289 VAL A C     1 
ATOM   564  O  O     . VAL A 1 72  ? 26.603  6.234   22.576 1.00 51.02  ? 1289 VAL A O     1 
ATOM   565  C  CB    . VAL A 1 72  ? 27.438  3.449   23.487 1.00 43.12  ? 1289 VAL A CB    1 
ATOM   566  C  CG1   . VAL A 1 72  ? 28.776  3.735   24.136 1.00 37.01  ? 1289 VAL A CG1   1 
ATOM   567  C  CG2   . VAL A 1 72  ? 26.993  1.993   23.677 1.00 29.34  ? 1289 VAL A CG2   1 
ATOM   568  N  N     . SER A 1 73  ? 26.965  6.629   24.784 1.00 53.54  ? 1290 SER A N     1 
ATOM   569  C  CA    . SER A 1 73  ? 27.552  7.967   24.618 1.00 31.97  ? 1290 SER A CA    1 
ATOM   570  C  C     . SER A 1 73  ? 28.767  7.918   23.692 1.00 50.16  ? 1290 SER A C     1 
ATOM   571  O  O     . SER A 1 73  ? 29.569  6.985   23.744 1.00 62.91  ? 1290 SER A O     1 
ATOM   572  C  CB    . SER A 1 73  ? 27.984  8.512   25.992 1.00 32.31  ? 1290 SER A CB    1 
ATOM   573  O  OG    . SER A 1 73  ? 28.765  9.690   25.864 1.00 84.29  ? 1290 SER A OG    1 
ATOM   574  N  N     . ARG A 1 74  ? 28.922  8.944   22.855 1.00 52.11  ? 1291 ARG A N     1 
ATOM   575  C  CA    . ARG A 1 74  ? 30.150  9.055   22.075 1.00 43.98  ? 1291 ARG A CA    1 
ATOM   576  C  C     . ARG A 1 74  ? 31.358  9.019   22.991 1.00 40.70  ? 1291 ARG A C     1 
ATOM   577  O  O     . ARG A 1 74  ? 32.279  8.223   22.789 1.00 41.88  ? 1291 ARG A O     1 
ATOM   578  C  CB    . ARG A 1 74  ? 30.150  10.343  21.247 1.00 34.84  ? 1291 ARG A CB    1 
ATOM   579  N  N     . ALA A 1 75  ? 31.347  9.840   24.044 1.00 47.75  ? 1292 ALA A N     1 
ATOM   580  C  CA    . ALA A 1 75  ? 32.527  9.937   24.900 1.00 60.44  ? 1292 ALA A CA    1 
ATOM   581  C  C     . ALA A 1 75  ? 32.837  8.601   25.564 1.00 58.15  ? 1292 ALA A C     1 
ATOM   582  O  O     . ALA A 1 75  ? 33.997  8.181   25.614 1.00 63.80  ? 1292 ALA A O     1 
ATOM   583  C  CB    . ALA A 1 75  ? 32.352  11.043  25.944 1.00 61.44  ? 1292 ALA A CB    1 
ATOM   584  N  N     . ALA A 1 76  ? 31.809  7.914   26.065 1.00 51.17  ? 1293 ALA A N     1 
ATOM   585  C  CA    . ALA A 1 76  ? 32.005  6.592   26.654 1.00 53.49  ? 1293 ALA A CA    1 
ATOM   586  C  C     . ALA A 1 76  ? 32.741  5.682   25.691 1.00 58.88  ? 1293 ALA A C     1 
ATOM   587  O  O     . ALA A 1 76  ? 33.739  5.039   26.049 1.00 57.89  ? 1293 ALA A O     1 
ATOM   588  C  CB    . ALA A 1 76  ? 30.653  5.982   27.025 1.00 54.14  ? 1293 ALA A CB    1 
ATOM   589  N  N     . LEU A 1 77  ? 32.228  5.605   24.463 1.00 59.52  ? 1294 LEU A N     1 
ATOM   590  C  CA    . LEU A 1 77  ? 32.814  4.769   23.428 1.00 45.58  ? 1294 LEU A CA    1 
ATOM   591  C  C     . LEU A 1 77  ? 34.206  5.262   23.047 1.00 46.26  ? 1294 LEU A C     1 
ATOM   592  O  O     . LEU A 1 77  ? 35.096  4.450   22.778 1.00 50.56  ? 1294 LEU A O     1 
ATOM   593  C  CB    . LEU A 1 77  ? 31.867  4.755   22.229 1.00 39.27  ? 1294 LEU A CB    1 
ATOM   594  C  CG    . LEU A 1 77  ? 31.981  3.811   21.031 1.00 41.61  ? 1294 LEU A CG    1 
ATOM   595  C  CD1   . LEU A 1 77  ? 31.969  2.354   21.443 1.00 39.20  ? 1294 LEU A CD1   1 
ATOM   596  C  CD2   . LEU A 1 77  ? 30.880  4.112   20.019 1.00 32.27  ? 1294 LEU A CD2   1 
ATOM   597  N  N     . GLU A 1 78  ? 34.442  6.572   23.065 1.00 45.34  ? 1295 GLU A N     1 
ATOM   598  C  CA    . GLU A 1 78  ? 35.760  7.091   22.701 1.00 56.60  ? 1295 GLU A CA    1 
ATOM   599  C  C     . GLU A 1 78  ? 36.600  7.308   23.966 1.00 63.94  ? 1295 GLU A C     1 
ATOM   600  O  O     . GLU A 1 78  ? 36.970  8.419   24.325 1.00 72.84  ? 1295 GLU A O     1 
ATOM   601  C  CB    . GLU A 1 78  ? 35.610  8.394   21.919 1.00 67.63  ? 1295 GLU A CB    1 
ATOM   602  C  CG    . GLU A 1 78  ? 34.569  8.402   20.788 1.00 75.37  ? 1295 GLU A CG    1 
ATOM   603  C  CD    . GLU A 1 78  ? 34.303  9.825   20.252 1.00 82.25  ? 1295 GLU A CD    1 
ATOM   604  O  OE1   . GLU A 1 78  ? 34.915  10.784  20.788 1.00 85.43  ? 1295 GLU A OE1   1 
ATOM   605  O  OE2   . GLU A 1 78  ? 33.478  9.988   19.313 1.00 76.75  ? 1295 GLU A OE2   1 
ATOM   606  N  N     . ARG A 1 79  ? 36.975  6.209   24.604 1.00 73.28  ? 1296 ARG A N     1 
ATOM   607  C  CA    . ARG A 1 79  ? 37.733  6.300   25.848 1.00 74.15  ? 1296 ARG A CA    1 
ATOM   608  C  C     . ARG A 1 79  ? 38.382  4.944   26.182 1.00 88.22  ? 1296 ARG A C     1 
ATOM   609  O  O     . ARG A 1 79  ? 39.595  4.749   26.004 1.00 90.81  ? 1296 ARG A O     1 
ATOM   610  C  CB    . ARG A 1 79  ? 36.814  6.777   26.999 1.00 54.95  ? 1296 ARG A CB    1 
ATOM   611  C  CG    . ARG A 1 79  ? 37.444  6.679   28.379 1.00 50.09  ? 1296 ARG A CG    1 
ATOM   612  C  CD    . ARG A 1 79  ? 36.492  6.795   29.562 1.00 48.49  ? 1296 ARG A CD    1 
ATOM   613  N  NE    . ARG A 1 79  ? 37.198  6.392   30.785 1.00 61.67  ? 1296 ARG A NE    1 
ATOM   614  C  CZ    . ARG A 1 79  ? 36.634  6.191   31.978 1.00 70.71  ? 1296 ARG A CZ    1 
ATOM   615  N  NH1   . ARG A 1 79  ? 35.332  6.381   32.149 1.00 70.21  ? 1296 ARG A NH1   1 
ATOM   616  N  NH2   . ARG A 1 79  ? 37.381  5.819   33.014 1.00 70.80  ? 1296 ARG A NH2   1 
ATOM   617  N  N     . ASP A 1 86  ? 39.862  1.808   14.796 1.00 43.82  ? 1303 ASP A N     1 
ATOM   618  C  CA    . ASP A 1 86  ? 40.017  0.352   14.690 1.00 65.39  ? 1303 ASP A CA    1 
ATOM   619  C  C     . ASP A 1 86  ? 38.705  -0.338  14.212 1.00 79.97  ? 1303 ASP A C     1 
ATOM   620  O  O     . ASP A 1 86  ? 38.601  -0.776  13.055 1.00 70.84  ? 1303 ASP A O     1 
ATOM   621  C  CB    . ASP A 1 86  ? 40.488  -0.231  16.033 1.00 52.07  ? 1303 ASP A CB    1 
ATOM   622  N  N     . PHE A 1 87  ? 37.693  -0.392  15.081 1.00 84.00  ? 1304 PHE A N     1 
ATOM   623  C  CA    . PHE A 1 87  ? 36.362  -0.825  14.677 1.00 80.43  ? 1304 PHE A CA    1 
ATOM   624  C  C     . PHE A 1 87  ? 35.437  0.341   14.335 1.00 76.52  ? 1304 PHE A C     1 
ATOM   625  O  O     . PHE A 1 87  ? 34.228  0.140   14.208 1.00 75.87  ? 1304 PHE A O     1 
ATOM   626  C  CB    . PHE A 1 87  ? 35.691  -1.628  15.794 1.00 83.19  ? 1304 PHE A CB    1 
ATOM   627  C  CG    . PHE A 1 87  ? 36.493  -2.769  16.334 1.00 84.81  ? 1304 PHE A CG    1 
ATOM   628  C  CD1   . PHE A 1 87  ? 36.772  -2.837  17.686 1.00 85.57  ? 1304 PHE A CD1   1 
ATOM   629  C  CD2   . PHE A 1 87  ? 36.905  -3.805  15.523 1.00 84.85  ? 1304 PHE A CD2   1 
ATOM   630  C  CE1   . PHE A 1 87  ? 37.480  -3.902  18.223 1.00 82.76  ? 1304 PHE A CE1   1 
ATOM   631  C  CE2   . PHE A 1 87  ? 37.615  -4.873  16.053 1.00 87.18  ? 1304 PHE A CE2   1 
ATOM   632  C  CZ    . PHE A 1 87  ? 37.899  -4.918  17.407 1.00 82.71  ? 1304 PHE A CZ    1 
ATOM   633  N  N     . ALA A 1 88  ? 35.964  1.551   14.203 1.00 78.05  ? 1305 ALA A N     1 
ATOM   634  C  CA    . ALA A 1 88  ? 35.108  2.721   14.007 1.00 79.28  ? 1305 ALA A CA    1 
ATOM   635  C  C     . ALA A 1 88  ? 34.099  2.599   12.866 1.00 74.52  ? 1305 ALA A C     1 
ATOM   636  O  O     . ALA A 1 88  ? 32.950  3.032   13.055 1.00 67.17  ? 1305 ALA A O     1 
ATOM   637  C  CB    . ALA A 1 88  ? 35.980  3.973   13.811 1.00 81.47  ? 1305 ALA A CB    1 
ATOM   638  N  N     . PRO A 1 89  ? 34.434  2.049   11.688 1.00 76.58  ? 1306 PRO A N     1 
ATOM   639  C  CA    . PRO A 1 89  ? 33.453  2.007   10.587 1.00 71.68  ? 1306 PRO A CA    1 
ATOM   640  C  C     . PRO A 1 89  ? 32.251  1.101   10.819 1.00 69.38  ? 1306 PRO A C     1 
ATOM   641  O  O     . PRO A 1 89  ? 31.340  1.117   9.978  1.00 70.53  ? 1306 PRO A O     1 
ATOM   642  C  CB    . PRO A 1 89  ? 34.291  1.512   9.403  1.00 65.91  ? 1306 PRO A CB    1 
ATOM   643  C  CG    . PRO A 1 89  ? 35.684  1.942   9.746  1.00 63.96  ? 1306 PRO A CG    1 
ATOM   644  C  CD    . PRO A 1 89  ? 35.772  1.657   11.202 1.00 72.09  ? 1306 PRO A CD    1 
ATOM   645  N  N     . GLU A 1 90  ? 32.218  0.325   11.907 1.00 65.19  ? 1307 GLU A N     1 
ATOM   646  C  CA    . GLU A 1 90  ? 31.136  -0.606  12.204 1.00 58.64  ? 1307 GLU A CA    1 
ATOM   647  C  C     . GLU A 1 90  ? 30.105  -0.048  13.185 1.00 54.02  ? 1307 GLU A C     1 
ATOM   648  O  O     . GLU A 1 90  ? 29.183  -0.773  13.566 1.00 61.31  ? 1307 GLU A O     1 
ATOM   649  C  CB    . GLU A 1 90  ? 31.712  -1.915  12.761 1.00 65.42  ? 1307 GLU A CB    1 
ATOM   650  C  CG    . GLU A 1 90  ? 32.420  -2.787  11.733 1.00 70.56  ? 1307 GLU A CG    1 
ATOM   651  C  CD    . GLU A 1 90  ? 32.836  -4.158  12.274 1.00 70.68  ? 1307 GLU A CD    1 
ATOM   652  O  OE1   . GLU A 1 90  ? 32.887  -4.362  13.519 1.00 69.37  ? 1307 GLU A OE1   1 
ATOM   653  O  OE2   . GLU A 1 90  ? 33.115  -5.036  11.433 1.00 64.04  ? 1307 GLU A OE2   1 
ATOM   654  N  N     . VAL A 1 91  ? 30.238  1.208   13.611 1.00 50.38  ? 1308 VAL A N     1 
ATOM   655  C  CA    . VAL A 1 91  ? 29.373  1.803   14.632 1.00 43.01  ? 1308 VAL A CA    1 
ATOM   656  C  C     . VAL A 1 91  ? 28.187  2.517   13.993 1.00 44.81  ? 1308 VAL A C     1 
ATOM   657  O  O     . VAL A 1 91  ? 28.363  3.391   13.134 1.00 33.12  ? 1308 VAL A O     1 
ATOM   658  C  CB    . VAL A 1 91  ? 30.172  2.781   15.493 1.00 44.30  ? 1308 VAL A CB    1 
ATOM   659  C  CG1   . VAL A 1 91  ? 29.260  3.476   16.498 1.00 36.87  ? 1308 VAL A CG1   1 
ATOM   660  C  CG2   . VAL A 1 91  ? 31.345  2.051   16.125 1.00 46.34  ? 1308 VAL A CG2   1 
ATOM   661  N  N     . ALA A 1 92  ? 26.975  2.152   14.418 1.00 44.99  ? 1309 ALA A N     1 
ATOM   662  C  CA    . ALA A 1 92  ? 25.753  2.809   13.962 1.00 41.20  ? 1309 ALA A CA    1 
ATOM   663  C  C     . ALA A 1 92  ? 25.377  3.935   14.915 1.00 47.35  ? 1309 ALA A C     1 
ATOM   664  O  O     . ALA A 1 92  ? 25.265  3.715   16.129 1.00 53.19  ? 1309 ALA A O     1 
ATOM   665  C  CB    . ALA A 1 92  ? 24.594  1.819   13.852 1.00 39.81  ? 1309 ALA A CB    1 
ATOM   666  N  N     . TRP A 1 93  ? 25.155  5.128   14.357 1.00 50.13  ? 1310 TRP A N     1 
ATOM   667  C  CA    . TRP A 1 93  ? 24.963  6.358   15.123 1.00 42.83  ? 1310 TRP A CA    1 
ATOM   668  C  C     . TRP A 1 93  ? 23.527  6.822   14.972 1.00 46.58  ? 1310 TRP A C     1 
ATOM   669  O  O     . TRP A 1 93  ? 23.084  7.128   13.861 1.00 50.50  ? 1310 TRP A O     1 
ATOM   670  C  CB    . TRP A 1 93  ? 25.921  7.454   14.647 1.00 36.67  ? 1310 TRP A CB    1 
ATOM   671  C  CG    . TRP A 1 93  ? 27.354  7.188   15.046 1.00 42.81  ? 1310 TRP A CG    1 
ATOM   672  C  CD1   . TRP A 1 93  ? 28.375  6.751   14.239 1.00 34.19  ? 1310 TRP A CD1   1 
ATOM   673  C  CD2   . TRP A 1 93  ? 27.915  7.332   16.358 1.00 33.54  ? 1310 TRP A CD2   1 
ATOM   674  N  NE1   . TRP A 1 93  ? 29.526  6.614   14.978 1.00 34.32  ? 1310 TRP A NE1   1 
ATOM   675  C  CE2   . TRP A 1 93  ? 29.267  6.973   16.275 1.00 33.93  ? 1310 TRP A CE2   1 
ATOM   676  C  CE3   . TRP A 1 93  ? 27.398  7.735   17.593 1.00 33.17  ? 1310 TRP A CE3   1 
ATOM   677  C  CZ2   . TRP A 1 93  ? 30.103  7.009   17.366 1.00 33.96  ? 1310 TRP A CZ2   1 
ATOM   678  C  CZ3   . TRP A 1 93  ? 28.234  7.772   18.678 1.00 34.20  ? 1310 TRP A CZ3   1 
ATOM   679  C  CH2   . TRP A 1 93  ? 29.572  7.407   18.560 1.00 34.77  ? 1310 TRP A CH2   1 
ATOM   680  N  N     . VAL A 1 94  ? 22.802  6.881   16.081 1.00 49.12  ? 1311 VAL A N     1 
ATOM   681  C  CA    . VAL A 1 94  ? 21.556  7.636   16.074 1.00 53.97  ? 1311 VAL A CA    1 
ATOM   682  C  C     . VAL A 1 94  ? 21.921  9.111   16.185 1.00 49.59  ? 1311 VAL A C     1 
ATOM   683  O  O     . VAL A 1 94  ? 22.592  9.536   17.131 1.00 47.63  ? 1311 VAL A O     1 
ATOM   684  C  CB    . VAL A 1 94  ? 20.601  7.197   17.199 1.00 48.43  ? 1311 VAL A CB    1 
ATOM   685  C  CG1   . VAL A 1 94  ? 19.377  8.109   17.244 1.00 43.62  ? 1311 VAL A CG1   1 
ATOM   686  C  CG2   . VAL A 1 94  ? 20.124  5.776   16.969 1.00 46.54  ? 1311 VAL A CG2   1 
ATOM   687  N  N     . THR A 1 95  ? 21.494  9.891   15.206 1.00 46.27  ? 1312 THR A N     1 
ATOM   688  C  CA    . THR A 1 95  ? 21.747  11.312  15.215 1.00 48.79  ? 1312 THR A CA    1 
ATOM   689  C  C     . THR A 1 95  ? 20.474  12.144  15.325 1.00 56.18  ? 1312 THR A C     1 
ATOM   690  O  O     . THR A 1 95  ? 20.555  13.317  15.695 1.00 71.92  ? 1312 THR A O     1 
ATOM   691  C  CB    . THR A 1 95  ? 22.510  11.712  13.953 1.00 39.08  ? 1312 THR A CB    1 
ATOM   692  O  OG1   . THR A 1 95  ? 21.599  11.722  12.856 1.00 47.79  ? 1312 THR A OG1   1 
ATOM   693  C  CG2   . THR A 1 95  ? 23.600  10.731  13.677 1.00 34.94  ? 1312 THR A CG2   1 
ATOM   694  N  N     . LYS A 1 96  ? 19.303  11.558  15.108 1.00 42.34  ? 1313 LYS A N     1 
ATOM   695  C  CA    . LYS A 1 96  ? 18.085  12.323  14.909 1.00 39.28  ? 1313 LYS A CA    1 
ATOM   696  C  C     . LYS A 1 96  ? 16.960  11.699  15.694 1.00 33.29  ? 1313 LYS A C     1 
ATOM   697  O  O     . LYS A 1 96  ? 16.822  10.479  15.709 1.00 53.97  ? 1313 LYS A O     1 
ATOM   698  C  CB    . LYS A 1 96  ? 17.666  12.363  13.434 1.00 36.74  ? 1313 LYS A CB    1 
ATOM   699  C  CG    . LYS A 1 96  ? 17.940  13.691  12.796 1.00 48.86  ? 1313 LYS A CG    1 
ATOM   700  C  CD    . LYS A 1 96  ? 17.260  13.818  11.455 1.00 51.36  ? 1313 LYS A CD    1 
ATOM   701  C  CE    . LYS A 1 96  ? 17.919  12.961  10.408 1.00 52.11  ? 1313 LYS A CE    1 
ATOM   702  N  NZ    . LYS A 1 96  ? 16.924  12.675  9.350  1.00 59.74  ? 1313 LYS A NZ    1 
ATOM   703  N  N     . SER A 1 97  ? 16.151  12.534  16.334 1.00 34.93  ? 1314 SER A N     1 
ATOM   704  C  CA    . SER A 1 97  ? 14.906  12.083  16.945 1.00 40.98  ? 1314 SER A CA    1 
ATOM   705  C  C     . SER A 1 97  ? 13.783  12.620  16.066 1.00 45.38  ? 1314 SER A C     1 
ATOM   706  O  O     . SER A 1 97  ? 13.131  13.611  16.384 1.00 46.43  ? 1314 SER A O     1 
ATOM   707  C  CB    . SER A 1 97  ? 14.781  12.575  18.348 1.00 43.28  ? 1314 SER A CB    1 
ATOM   708  O  OG    . SER A 1 97  ? 14.305  13.912  18.365 1.00 36.49  ? 1314 SER A OG    1 
ATOM   709  N  N     . GLY A 1 98  ? 13.539  11.925  14.962 1.00 55.43  ? 1315 GLY A N     1 
ATOM   710  C  CA    . GLY A 1 98  ? 12.479  12.320  14.070 1.00 58.29  ? 1315 GLY A CA    1 
ATOM   711  C  C     . GLY A 1 98  ? 12.923  13.401  13.121 1.00 63.24  ? 1315 GLY A C     1 
ATOM   712  O  O     . GLY A 1 98  ? 13.575  13.136  12.108 1.00 63.24  ? 1315 GLY A O     1 
ATOM   713  N  N     . ASP A 1 99  ? 12.558  14.636  13.470 1.00 69.69  ? 1316 ASP A N     1 
ATOM   714  C  CA    . ASP A 1 99  ? 12.964  15.863  12.802 1.00 60.95  ? 1316 ASP A CA    1 
ATOM   715  C  C     . ASP A 1 99  ? 14.211  16.440  13.439 1.00 61.65  ? 1316 ASP A C     1 
ATOM   716  O  O     . ASP A 1 99  ? 15.211  16.713  12.766 1.00 54.89  ? 1316 ASP A O     1 
ATOM   717  C  CB    . ASP A 1 99  ? 11.858  16.901  12.978 1.00 58.02  ? 1316 ASP A CB    1 
ATOM   718  C  CG    . ASP A 1 99  ? 11.170  17.231  11.717 1.00 77.73  ? 1316 ASP A CG    1 
ATOM   719  O  OD1   . ASP A 1 99  ? 11.537  16.649  10.676 1.00 89.47  ? 1316 ASP A OD1   1 
ATOM   720  O  OD2   . ASP A 1 99  ? 10.291  18.118  11.768 1.00 77.84  ? 1316 ASP A OD2   1 
ATOM   721  N  N     . SER A 1 100 ? 14.170  16.501  14.758 1.00 61.63  ? 1317 SER A N     1 
ATOM   722  C  CA    . SER A 1 100 ? 15.148  17.191  15.570 1.00 67.78  ? 1317 SER A CA    1 
ATOM   723  C  C     . SER A 1 100 ? 16.429  16.373  15.713 1.00 68.26  ? 1317 SER A C     1 
ATOM   724  O  O     . SER A 1 100 ? 16.400  15.239  16.192 1.00 65.15  ? 1317 SER A O     1 
ATOM   725  C  CB    . SER A 1 100 ? 14.490  17.473  16.918 1.00 76.31  ? 1317 SER A CB    1 
ATOM   726  O  OG    . SER A 1 100 ? 13.625  16.380  17.243 1.00 82.41  ? 1317 SER A OG    1 
ATOM   727  N  N     . GLU A 1 101 ? 17.562  16.981  15.426 1.00 75.34  ? 1318 GLU A N     1 
ATOM   728  C  CA    . GLU A 1 101 ? 18.845  16.347  15.597 1.00 80.49  ? 1318 GLU A CA    1 
ATOM   729  C  C     . GLU A 1 101 ? 19.163  16.471  17.041 1.00 84.03  ? 1318 GLU A C     1 
ATOM   730  O  O     . GLU A 1 101 ? 18.868  17.457  17.656 1.00 78.68  ? 1318 GLU A O     1 
ATOM   731  C  CB    . GLU A 1 101 ? 19.915  17.012  14.794 1.00 88.56  ? 1318 GLU A CB    1 
ATOM   732  N  N     . LEU A 1 102 ? 19.891  15.499  17.545 1.00 100.66 ? 1319 LEU A N     1 
ATOM   733  C  CA    . LEU A 1 102 ? 20.144  15.326  18.972 1.00 72.37  ? 1319 LEU A CA    1 
ATOM   734  C  C     . LEU A 1 102 ? 21.390  16.064  19.430 1.00 59.40  ? 1319 LEU A C     1 
ATOM   735  O  O     . LEU A 1 102 ? 22.363  16.204  18.682 1.00 58.81  ? 1319 LEU A O     1 
ATOM   736  C  CB    . LEU A 1 102 ? 20.303  13.843  19.313 1.00 69.15  ? 1319 LEU A CB    1 
ATOM   737  C  CG    . LEU A 1 102 ? 18.999  13.052  19.390 1.00 72.51  ? 1319 LEU A CG    1 
ATOM   738  C  CD1   . LEU A 1 102 ? 19.293  11.662  19.862 1.00 76.46  ? 1319 LEU A CD1   1 
ATOM   739  C  CD2   . LEU A 1 102 ? 17.969  13.718  20.303 1.00 75.87  ? 1319 LEU A CD2   1 
ATOM   740  N  N     . ALA A 1 103 ? 21.361  16.521  20.691 1.00 55.49  ? 1320 ALA A N     1 
ATOM   741  C  CA    . ALA A 1 103 ? 22.492  17.241  21.281 1.00 61.91  ? 1320 ALA A CA    1 
ATOM   742  C  C     . ALA A 1 103 ? 23.808  16.516  21.027 1.00 59.86  ? 1320 ALA A C     1 
ATOM   743  O  O     . ALA A 1 103 ? 24.631  16.942  20.210 1.00 51.16  ? 1320 ALA A O     1 
ATOM   744  C  CB    . ALA A 1 103 ? 22.280  17.416  22.782 1.00 64.76  ? 1320 ALA A CB    1 
ATOM   745  N  N     . GLU A 1 104 ? 23.970  15.391  21.658 1.00 59.51  ? 1321 GLU A N     1 
ATOM   746  C  CA    . GLU A 1 104 ? 25.067  14.548  21.273 1.00 43.14  ? 1321 GLU A CA    1 
ATOM   747  C  C     . GLU A 1 104 ? 24.519  13.374  20.477 1.00 46.26  ? 1321 GLU A C     1 
ATOM   748  O  O     . GLU A 1 104 ? 23.377  12.961  20.700 1.00 34.13  ? 1321 GLU A O     1 
ATOM   749  C  CB    . GLU A 1 104 ? 25.814  14.040  22.508 1.00 35.30  ? 1321 GLU A CB    1 
ATOM   750  N  N     . PRO A 1 105 ? 25.253  12.883  19.478 1.00 49.72  ? 1322 PRO A N     1 
ATOM   751  C  CA    . PRO A 1 105 ? 24.845  11.636  18.812 1.00 54.51  ? 1322 PRO A CA    1 
ATOM   752  C  C     . PRO A 1 105 ? 25.085  10.439  19.718 1.00 47.70  ? 1322 PRO A C     1 
ATOM   753  O  O     . PRO A 1 105 ? 25.982  10.435  20.568 1.00 53.24  ? 1322 PRO A O     1 
ATOM   754  C  CB    . PRO A 1 105 ? 25.743  11.570  17.570 1.00 54.49  ? 1322 PRO A CB    1 
ATOM   755  C  CG    . PRO A 1 105 ? 26.408  12.907  17.485 1.00 56.99  ? 1322 PRO A CG    1 
ATOM   756  C  CD    . PRO A 1 105 ? 26.457  13.461  18.875 1.00 49.36  ? 1322 PRO A CD    1 
ATOM   757  N  N     . ILE A 1 106 ? 24.269  9.417   19.533 1.00 38.18  ? 1323 ILE A N     1 
ATOM   758  C  CA    . ILE A 1 106 ? 24.408  8.201   20.317 1.00 39.99  ? 1323 ILE A CA    1 
ATOM   759  C  C     . ILE A 1 106 ? 24.671  7.028   19.391 1.00 43.35  ? 1323 ILE A C     1 
ATOM   760  O  O     . ILE A 1 106 ? 24.231  7.006   18.238 1.00 45.16  ? 1323 ILE A O     1 
ATOM   761  C  CB    . ILE A 1 106 ? 23.169  7.950   21.207 1.00 36.88  ? 1323 ILE A CB    1 
ATOM   762  C  CG1   . ILE A 1 106 ? 21.938  7.672   20.371 1.00 38.08  ? 1323 ILE A CG1   1 
ATOM   763  C  CG2   . ILE A 1 106 ? 22.873  9.179   22.014 1.00 40.63  ? 1323 ILE A CG2   1 
ATOM   764  C  CD1   . ILE A 1 106 ? 20.664  7.859   21.133 1.00 44.28  ? 1323 ILE A CD1   1 
ATOM   765  N  N     . ALA A 1 107 ? 25.383  6.038   19.913 1.00 49.49  ? 1324 ALA A N     1 
ATOM   766  C  CA    . ALA A 1 107 ? 25.794  4.869   19.155 1.00 52.79  ? 1324 ALA A CA    1 
ATOM   767  C  C     . ALA A 1 107 ? 25.009  3.668   19.638 1.00 47.07  ? 1324 ALA A C     1 
ATOM   768  O  O     . ALA A 1 107 ? 24.689  3.577   20.820 1.00 42.65  ? 1324 ALA A O     1 
ATOM   769  C  CB    . ALA A 1 107 ? 27.287  4.592   19.317 1.00 55.58  ? 1324 ALA A CB    1 
ATOM   770  N  N     . VAL A 1 108 ? 24.649  2.779   18.722 1.00 45.85  ? 1325 VAL A N     1 
ATOM   771  C  CA    . VAL A 1 108 ? 24.065  1.503   19.126 1.00 45.28  ? 1325 VAL A CA    1 
ATOM   772  C  C     . VAL A 1 108 ? 25.184  0.584   19.580 1.00 42.30  ? 1325 VAL A C     1 
ATOM   773  O  O     . VAL A 1 108 ? 26.195  0.463   18.880 1.00 45.80  ? 1325 VAL A O     1 
ATOM   774  C  CB    . VAL A 1 108 ? 23.287  0.864   17.973 1.00 43.46  ? 1325 VAL A CB    1 
ATOM   775  C  CG1   . VAL A 1 108 ? 22.302  -0.150  18.526 1.00 43.57  ? 1325 VAL A CG1   1 
ATOM   776  C  CG2   . VAL A 1 108 ? 22.634  1.921   17.123 1.00 35.93  ? 1325 VAL A CG2   1 
ATOM   777  N  N     . ARG A 1 109 ? 25.012  -0.041  20.725 1.00 38.49  ? 1326 ARG A N     1 
ATOM   778  C  CA    . ARG A 1 109 ? 26.018  -0.901  21.290 1.00 40.40  ? 1326 ARG A CA    1 
ATOM   779  C  C     . ARG A 1 109 ? 26.525  -1.955  20.397 1.00 44.05  ? 1326 ARG A C     1 
ATOM   780  O  O     . ARG A 1 109 ? 25.801  -2.555  19.710 1.00 42.49  ? 1326 ARG A O     1 
ATOM   781  C  CB    . ARG A 1 109 ? 25.551  -1.521  22.596 1.00 28.03  ? 1326 ARG A CB    1 
ATOM   782  C  CG    . ARG A 1 109 ? 24.821  -2.807  22.505 1.00 27.53  ? 1326 ARG A CG    1 
ATOM   783  C  CD    . ARG A 1 109 ? 24.245  -3.201  23.811 1.00 31.85  ? 1326 ARG A CD    1 
ATOM   784  N  NE    . ARG A 1 109 ? 22.845  -3.553  23.716 1.00 41.37  ? 1326 ARG A NE    1 
ATOM   785  C  CZ    . ARG A 1 109 ? 22.062  -3.709  24.758 1.00 51.27  ? 1326 ARG A CZ    1 
ATOM   786  N  NH1   . ARG A 1 109 ? 22.553  -3.578  25.930 1.00 53.60  ? 1326 ARG A NH1   1 
ATOM   787  N  NH2   . ARG A 1 109 ? 20.807  -4.002  24.641 1.00 26.19  ? 1326 ARG A NH2   1 
ATOM   788  N  N     . PRO A 1 110 ? 27.822  -2.127  20.356 1.00 46.44  ? 1327 PRO A N     1 
ATOM   789  C  CA    . PRO A 1 110 ? 28.454  -3.161  19.580 1.00 58.25  ? 1327 PRO A CA    1 
ATOM   790  C  C     . PRO A 1 110 ? 29.069  -4.277  20.432 1.00 63.19  ? 1327 PRO A C     1 
ATOM   791  O  O     . PRO A 1 110 ? 29.380  -5.331  19.948 1.00 64.81  ? 1327 PRO A O     1 
ATOM   792  C  CB    . PRO A 1 110 ? 29.511  -2.388  18.884 1.00 50.27  ? 1327 PRO A CB    1 
ATOM   793  C  CG    . PRO A 1 110 ? 29.899  -1.396  19.852 1.00 30.20  ? 1327 PRO A CG    1 
ATOM   794  C  CD    . PRO A 1 110 ? 28.704  -0.990  20.550 1.00 29.63  ? 1327 PRO A CD    1 
ATOM   795  N  N     . THR A 1 111 ? 29.201  -3.968  21.703 1.00 54.84  ? 1328 THR A N     1 
ATOM   796  C  CA    . THR A 1 111 ? 29.735  -4.674  22.841 1.00 47.40  ? 1328 THR A CA    1 
ATOM   797  C  C     . THR A 1 111 ? 29.654  -3.721  24.025 1.00 43.67  ? 1328 THR A C     1 
ATOM   798  O  O     . THR A 1 111 ? 29.466  -2.557  23.855 1.00 58.91  ? 1328 THR A O     1 
ATOM   799  C  CB    . THR A 1 111 ? 31.115  -5.209  22.634 1.00 40.83  ? 1328 THR A CB    1 
ATOM   800  O  OG1   . THR A 1 111 ? 31.569  -5.718  23.854 1.00 39.31  ? 1328 THR A OG1   1 
ATOM   801  C  CG2   . THR A 1 111 ? 31.982  -4.174  22.220 1.00 40.15  ? 1328 THR A CG2   1 
ATOM   802  N  N     . SER A 1 112 ? 29.852  -4.177  25.237 1.00 28.75  ? 1329 SER A N     1 
ATOM   803  C  CA    . SER A 1 112 ? 29.579  -3.284  26.361 1.00 28.74  ? 1329 SER A CA    1 
ATOM   804  C  C     . SER A 1 112 ? 30.762  -3.000  27.279 1.00 39.28  ? 1329 SER A C     1 
ATOM   805  O  O     . SER A 1 112 ? 30.563  -2.364  28.321 1.00 32.13  ? 1329 SER A O     1 
ATOM   806  C  CB    . SER A 1 112 ? 28.457  -3.854  27.220 1.00 28.22  ? 1329 SER A CB    1 
ATOM   807  O  OG    . SER A 1 112 ? 27.520  -4.497  26.411 1.00 35.34  ? 1329 SER A OG    1 
ATOM   808  N  N     . GLU A 1 113 ? 31.991  -3.327  26.879 1.00 37.36  ? 1330 GLU A N     1 
ATOM   809  C  CA    . GLU A 1 113 ? 33.134  -3.031  27.734 1.00 45.74  ? 1330 GLU A CA    1 
ATOM   810  C  C     . GLU A 1 113 ? 33.200  -1.549  28.106 1.00 50.38  ? 1330 GLU A C     1 
ATOM   811  O  O     . GLU A 1 113 ? 33.316  -1.198  29.293 1.00 46.52  ? 1330 GLU A O     1 
ATOM   812  C  CB    . GLU A 1 113 ? 34.407  -3.483  27.042 1.00 50.20  ? 1330 GLU A CB    1 
ATOM   813  C  CG    . GLU A 1 113 ? 34.689  -4.954  27.253 1.00 62.81  ? 1330 GLU A CG    1 
ATOM   814  C  CD    . GLU A 1 113 ? 34.278  -5.788  26.091 1.00 57.98  ? 1330 GLU A CD    1 
ATOM   815  O  OE1   . GLU A 1 113 ? 34.800  -6.926  25.965 1.00 53.95  ? 1330 GLU A OE1   1 
ATOM   816  O  OE2   . GLU A 1 113 ? 33.435  -5.286  25.317 1.00 54.46  ? 1330 GLU A OE2   1 
ATOM   817  N  N     . THR A 1 114 ? 33.090  -0.674  27.095 1.00 52.02  ? 1331 THR A N     1 
ATOM   818  C  CA    . THR A 1 114 ? 33.143  0.781   27.235 1.00 54.49  ? 1331 THR A CA    1 
ATOM   819  C  C     . THR A 1 114 ? 32.170  1.332   28.258 1.00 56.58  ? 1331 THR A C     1 
ATOM   820  O  O     . THR A 1 114 ? 32.353  2.455   28.747 1.00 52.28  ? 1331 THR A O     1 
ATOM   821  C  CB    . THR A 1 114 ? 32.794  1.411   25.898 1.00 55.49  ? 1331 THR A CB    1 
ATOM   822  O  OG1   . THR A 1 114 ? 31.669  0.697   25.351 1.00 66.53  ? 1331 THR A OG1   1 
ATOM   823  C  CG2   . THR A 1 114 ? 33.970  1.324   24.960 1.00 47.07  ? 1331 THR A CG2   1 
ATOM   824  N  N     . VAL A 1 115 ? 31.131  0.574   28.576 1.00 55.43  ? 1332 VAL A N     1 
ATOM   825  C  CA    . VAL A 1 115 ? 30.034  1.047   29.394 1.00 44.66  ? 1332 VAL A CA    1 
ATOM   826  C  C     . VAL A 1 115 ? 29.952  0.309   30.719 1.00 45.78  ? 1332 VAL A C     1 
ATOM   827  O  O     . VAL A 1 115 ? 29.649  0.909   31.759 1.00 47.47  ? 1332 VAL A O     1 
ATOM   828  C  CB    . VAL A 1 115 ? 28.729  0.903   28.600 1.00 39.07  ? 1332 VAL A CB    1 
ATOM   829  C  CG1   . VAL A 1 115 ? 27.540  1.044   29.493 1.00 37.45  ? 1332 VAL A CG1   1 
ATOM   830  C  CG2   . VAL A 1 115 ? 28.752  1.927   27.458 1.00 30.44  ? 1332 VAL A CG2   1 
ATOM   831  N  N     . MET A 1 116 ? 30.209  -0.994  30.703 1.00 40.89  ? 1333 MET A N     1 
ATOM   832  C  CA    . MET A 1 116 ? 30.165  -1.780  31.920 1.00 34.22  ? 1333 MET A CA    1 
ATOM   833  C  C     . MET A 1 116 ? 31.390  -1.548  32.796 1.00 43.52  ? 1333 MET A C     1 
ATOM   834  O  O     . MET A 1 116 ? 31.276  -1.631  34.025 1.00 42.22  ? 1333 MET A O     1 
ATOM   835  C  CB    . MET A 1 116 ? 30.035  -3.256  31.572 1.00 34.51  ? 1333 MET A CB    1 
ATOM   836  C  CG    . MET A 1 116 ? 28.698  -3.669  30.978 1.00 47.75  ? 1333 MET A CG    1 
ATOM   837  S  SD    . MET A 1 116 ? 28.576  -5.478  30.756 1.00 57.40  ? 1333 MET A SD    1 
ATOM   838  C  CE    . MET A 1 116 ? 28.589  -5.997  32.464 1.00 56.97  ? 1333 MET A CE    1 
ATOM   839  N  N     . TYR A 1 117 ? 32.566  -1.246  32.198 1.00 44.36  ? 1334 TYR A N     1 
ATOM   840  C  CA    . TYR A 1 117 ? 33.769  -1.155  33.028 1.00 49.40  ? 1334 TYR A CA    1 
ATOM   841  C  C     . TYR A 1 117 ? 33.817  0.128   33.852 1.00 55.36  ? 1334 TYR A C     1 
ATOM   842  O  O     . TYR A 1 117 ? 34.344  0.104   34.972 1.00 64.44  ? 1334 TYR A O     1 
ATOM   843  C  CB    . TYR A 1 117 ? 35.039  -1.307  32.189 1.00 45.79  ? 1334 TYR A CB    1 
ATOM   844  C  CG    . TYR A 1 117 ? 35.123  -2.678  31.582 1.00 43.81  ? 1334 TYR A CG    1 
ATOM   845  C  CD1   . TYR A 1 117 ? 34.230  -3.669  31.968 1.00 54.13  ? 1334 TYR A CD1   1 
ATOM   846  C  CD2   . TYR A 1 117 ? 36.084  -2.997  30.640 1.00 40.33  ? 1334 TYR A CD2   1 
ATOM   847  C  CE1   . TYR A 1 117 ? 34.268  -4.918  31.427 1.00 53.35  ? 1334 TYR A CE1   1 
ATOM   848  C  CE2   . TYR A 1 117 ? 36.143  -4.262  30.098 1.00 39.99  ? 1334 TYR A CE2   1 
ATOM   849  C  CZ    . TYR A 1 117 ? 35.217  -5.213  30.493 1.00 48.13  ? 1334 TYR A CZ    1 
ATOM   850  O  OH    . TYR A 1 117 ? 35.213  -6.470  29.954 1.00 50.51  ? 1334 TYR A OH    1 
ATOM   851  N  N     . PRO A 1 118 ? 33.319  1.265   33.349 1.00 52.56  ? 1335 PRO A N     1 
ATOM   852  C  CA    . PRO A 1 118 ? 33.114  2.418   34.247 1.00 53.10  ? 1335 PRO A CA    1 
ATOM   853  C  C     . PRO A 1 118 ? 32.190  2.123   35.421 1.00 53.57  ? 1335 PRO A C     1 
ATOM   854  O  O     . PRO A 1 118 ? 32.465  2.556   36.550 1.00 54.95  ? 1335 PRO A O     1 
ATOM   855  C  CB    . PRO A 1 118 ? 32.522  3.467   33.309 1.00 49.68  ? 1335 PRO A CB    1 
ATOM   856  C  CG    . PRO A 1 118 ? 33.097  3.126   31.994 1.00 46.30  ? 1335 PRO A CG    1 
ATOM   857  C  CD    . PRO A 1 118 ? 33.160  1.650   31.936 1.00 46.43  ? 1335 PRO A CD    1 
ATOM   858  N  N     . ALA A 1 119 ? 31.076  1.423   35.178 1.00 49.88  ? 1336 ALA A N     1 
ATOM   859  C  CA    . ALA A 1 119 ? 30.229  0.961   36.277 1.00 47.36  ? 1336 ALA A CA    1 
ATOM   860  C  C     . ALA A 1 119 ? 31.002  0.068   37.236 1.00 52.61  ? 1336 ALA A C     1 
ATOM   861  O  O     . ALA A 1 119 ? 30.765  0.092   38.446 1.00 50.55  ? 1336 ALA A O     1 
ATOM   862  C  CB    . ALA A 1 119 ? 29.016  0.216   35.743 1.00 41.64  ? 1336 ALA A CB    1 
ATOM   863  N  N     . TYR A 1 120 ? 31.868  -0.790  36.703 1.00 53.07  ? 1337 TYR A N     1 
ATOM   864  C  CA    . TYR A 1 120 ? 32.693  -1.631  37.560 1.00 48.46  ? 1337 TYR A CA    1 
ATOM   865  C  C     . TYR A 1 120 ? 33.599  -0.793  38.452 1.00 48.81  ? 1337 TYR A C     1 
ATOM   866  O  O     . TYR A 1 120 ? 33.712  -1.048  39.659 1.00 36.08  ? 1337 TYR A O     1 
ATOM   867  C  CB    . TYR A 1 120 ? 33.519  -2.573  36.693 1.00 46.82  ? 1337 TYR A CB    1 
ATOM   868  C  CG    . TYR A 1 120 ? 32.735  -3.783  36.238 1.00 50.24  ? 1337 TYR A CG    1 
ATOM   869  C  CD1   . TYR A 1 120 ? 31.355  -3.807  36.343 1.00 45.27  ? 1337 TYR A CD1   1 
ATOM   870  C  CD2   . TYR A 1 120 ? 33.374  -4.896  35.700 1.00 42.69  ? 1337 TYR A CD2   1 
ATOM   871  C  CE1   . TYR A 1 120 ? 30.640  -4.893  35.948 1.00 44.40  ? 1337 TYR A CE1   1 
ATOM   872  C  CE2   . TYR A 1 120 ? 32.666  -5.974  35.302 1.00 35.47  ? 1337 TYR A CE2   1 
ATOM   873  C  CZ    . TYR A 1 120 ? 31.295  -5.972  35.425 1.00 43.21  ? 1337 TYR A CZ    1 
ATOM   874  O  OH    . TYR A 1 120 ? 30.555  -7.059  35.021 1.00 51.57  ? 1337 TYR A OH    1 
ATOM   875  N  N     . ALA A 1 121 ? 34.228  0.231   37.872 1.00 48.00  ? 1338 ALA A N     1 
ATOM   876  C  CA    . ALA A 1 121 ? 35.064  1.134   38.647 1.00 37.93  ? 1338 ALA A CA    1 
ATOM   877  C  C     . ALA A 1 121 ? 34.251  1.817   39.738 1.00 34.07  ? 1338 ALA A C     1 
ATOM   878  O  O     . ALA A 1 121 ? 34.716  1.971   40.877 1.00 34.74  ? 1338 ALA A O     1 
ATOM   879  C  CB    . ALA A 1 121 ? 35.703  2.147   37.707 1.00 37.40  ? 1338 ALA A CB    1 
ATOM   880  N  N     . LYS A 1 122 ? 33.005  2.160   39.432 1.00 45.73  ? 1339 LYS A N     1 
ATOM   881  C  CA    . LYS A 1 122 ? 32.147  2.754   40.453 1.00 53.16  ? 1339 LYS A CA    1 
ATOM   882  C  C     . LYS A 1 122 ? 31.720  1.717   41.486 1.00 51.28  ? 1339 LYS A C     1 
ATOM   883  O  O     . LYS A 1 122 ? 31.549  2.048   42.658 1.00 64.65  ? 1339 LYS A O     1 
ATOM   884  C  CB    . LYS A 1 122 ? 30.916  3.406   39.810 1.00 55.41  ? 1339 LYS A CB    1 
ATOM   885  C  CG    . LYS A 1 122 ? 31.238  4.621   38.934 1.00 69.54  ? 1339 LYS A CG    1 
ATOM   886  C  CD    . LYS A 1 122 ? 30.031  5.577   38.773 1.00 74.42  ? 1339 LYS A CD    1 
ATOM   887  C  CE    . LYS A 1 122 ? 30.422  7.069   38.989 1.00 68.90  ? 1339 LYS A CE    1 
ATOM   888  N  NZ    . LYS A 1 122 ? 29.620  7.835   40.004 1.00 54.90  ? 1339 LYS A NZ    1 
ATOM   889  N  N     . TRP A 1 123 ? 31.591  0.460   41.088 1.00 43.26  ? 1340 TRP A N     1 
ATOM   890  C  CA    . TRP A 1 123 ? 30.996  -0.544  41.952 1.00 44.98  ? 1340 TRP A CA    1 
ATOM   891  C  C     . TRP A 1 123 ? 31.988  -1.214  42.892 1.00 38.60  ? 1340 TRP A C     1 
ATOM   892  O  O     . TRP A 1 123 ? 31.587  -1.596  43.997 1.00 40.77  ? 1340 TRP A O     1 
ATOM   893  C  CB    . TRP A 1 123 ? 30.301  -1.610  41.096 1.00 46.79  ? 1340 TRP A CB    1 
ATOM   894  C  CG    . TRP A 1 123 ? 28.909  -1.237  40.666 1.00 40.91  ? 1340 TRP A CG    1 
ATOM   895  C  CD1   . TRP A 1 123 ? 28.027  -0.450  41.337 1.00 44.28  ? 1340 TRP A CD1   1 
ATOM   896  C  CD2   . TRP A 1 123 ? 28.250  -1.641  39.469 1.00 39.76  ? 1340 TRP A CD2   1 
ATOM   897  N  NE1   . TRP A 1 123 ? 26.856  -0.343  40.636 1.00 37.25  ? 1340 TRP A NE1   1 
ATOM   898  C  CE2   . TRP A 1 123 ? 26.973  -1.071  39.483 1.00 43.19  ? 1340 TRP A CE2   1 
ATOM   899  C  CE3   . TRP A 1 123 ? 28.615  -2.443  38.386 1.00 46.28  ? 1340 TRP A CE3   1 
ATOM   900  C  CZ2   . TRP A 1 123 ? 26.060  -1.282  38.459 1.00 52.35  ? 1340 TRP A CZ2   1 
ATOM   901  C  CZ3   . TRP A 1 123 ? 27.709  -2.646  37.370 1.00 40.44  ? 1340 TRP A CZ3   1 
ATOM   902  C  CH2   . TRP A 1 123 ? 26.455  -2.070  37.410 1.00 47.34  ? 1340 TRP A CH2   1 
ATOM   903  N  N     . ILE A 1 124 ? 33.267  -1.335  42.523 1.00 36.54  ? 1341 ILE A N     1 
ATOM   904  C  CA    . ILE A 1 124 ? 34.271  -1.939  43.420 1.00 43.23  ? 1341 ILE A CA    1 
ATOM   905  C  C     . ILE A 1 124 ? 34.780  -0.814  44.311 1.00 62.35  ? 1341 ILE A C     1 
ATOM   906  O  O     . ILE A 1 124 ? 35.728  -0.093  43.975 1.00 68.48  ? 1341 ILE A O     1 
ATOM   907  C  CB    . ILE A 1 124 ? 35.424  -2.611  42.683 1.00 37.08  ? 1341 ILE A CB    1 
ATOM   908  C  CG1   . ILE A 1 124 ? 35.011  -3.229  41.367 1.00 39.27  ? 1341 ILE A CG1   1 
ATOM   909  C  CG2   . ILE A 1 124 ? 36.044  -3.658  43.570 1.00 35.19  ? 1341 ILE A CG2   1 
ATOM   910  C  CD1   . ILE A 1 124 ? 34.223  -4.427  41.528 1.00 41.61  ? 1341 ILE A CD1   1 
ATOM   911  N  N     . GLN A 1 125 ? 34.141  -0.660  45.457 1.00 59.07  ? 1342 GLN A N     1 
ATOM   912  C  CA    . GLN A 1 125 ? 34.633  0.284   46.430 1.00 62.66  ? 1342 GLN A CA    1 
ATOM   913  C  C     . GLN A 1 125 ? 35.688  -0.347  47.329 1.00 72.93  ? 1342 GLN A C     1 
ATOM   914  O  O     . GLN A 1 125 ? 36.522  0.368   47.900 1.00 78.81  ? 1342 GLN A O     1 
ATOM   915  C  CB    . GLN A 1 125 ? 33.449  0.821   47.239 1.00 67.65  ? 1342 GLN A CB    1 
ATOM   916  N  N     . SER A 1 126 ? 35.713  -1.675  47.405 1.00 71.04  ? 1343 SER A N     1 
ATOM   917  C  CA    . SER A 1 126 ? 36.605  -2.379  48.306 1.00 59.47  ? 1343 SER A CA    1 
ATOM   918  C  C     . SER A 1 126 ? 36.980  -3.736  47.722 1.00 64.28  ? 1343 SER A C     1 
ATOM   919  O  O     . SER A 1 126 ? 36.381  -4.219  46.756 1.00 67.27  ? 1343 SER A O     1 
ATOM   920  C  CB    . SER A 1 126 ? 35.943  -2.576  49.663 1.00 58.69  ? 1343 SER A CB    1 
ATOM   921  O  OG    . SER A 1 126 ? 36.409  -3.781  50.228 1.00 66.56  ? 1343 SER A OG    1 
ATOM   922  N  N     . TYR A 1 127 ? 37.983  -4.358  48.338 1.00 65.30  ? 1344 TYR A N     1 
ATOM   923  C  CA    . TYR A 1 127 ? 38.237  -5.760  48.039 1.00 55.66  ? 1344 TYR A CA    1 
ATOM   924  C  C     . TYR A 1 127 ? 37.026  -6.618  48.396 1.00 52.57  ? 1344 TYR A C     1 
ATOM   925  O  O     . TYR A 1 127 ? 36.821  -7.681  47.804 1.00 67.40  ? 1344 TYR A O     1 
ATOM   926  C  CB    . TYR A 1 127 ? 39.492  -6.230  48.779 1.00 49.55  ? 1344 TYR A CB    1 
ATOM   927  N  N     . ARG A 1 128 ? 36.206  -6.173  49.348 1.00 45.00  ? 1345 ARG A N     1 
ATOM   928  C  CA    . ARG A 1 128 ? 35.073  -6.974  49.790 1.00 50.70  ? 1345 ARG A CA    1 
ATOM   929  C  C     . ARG A 1 128 ? 34.012  -7.138  48.717 1.00 46.64  ? 1345 ARG A C     1 
ATOM   930  O  O     . ARG A 1 128 ? 33.278  -8.134  48.744 1.00 41.86  ? 1345 ARG A O     1 
ATOM   931  C  CB    . ARG A 1 128 ? 34.444  -6.353  51.038 1.00 62.19  ? 1345 ARG A CB    1 
ATOM   932  N  N     . ASP A 1 129 ? 33.937  -6.224  47.752 1.00 53.59  ? 1346 ASP A N     1 
ATOM   933  C  CA    . ASP A 1 129 ? 32.915  -6.353  46.715 1.00 59.62  ? 1346 ASP A CA    1 
ATOM   934  C  C     . ASP A 1 129 ? 33.305  -7.376  45.660 1.00 48.98  ? 1346 ASP A C     1 
ATOM   935  O  O     . ASP A 1 129 ? 32.602  -7.525  44.658 1.00 36.13  ? 1346 ASP A O     1 
ATOM   936  C  CB    . ASP A 1 129 ? 32.620  -5.020  45.985 1.00 68.23  ? 1346 ASP A CB    1 
ATOM   937  C  CG    . ASP A 1 129 ? 32.529  -3.815  46.897 1.00 70.68  ? 1346 ASP A CG    1 
ATOM   938  O  OD1   . ASP A 1 129 ? 31.906  -3.919  47.969 1.00 78.27  ? 1346 ASP A OD1   1 
ATOM   939  O  OD2   . ASP A 1 129 ? 33.016  -2.733  46.484 1.00 66.98  ? 1346 ASP A OD2   1 
ATOM   940  N  N     . LEU A 1 130 ? 34.412  -8.044  45.838 1.00 51.97  ? 1347 LEU A N     1 
ATOM   941  C  CA    . LEU A 1 130 ? 34.856  -8.910  44.766 1.00 60.12  ? 1347 LEU A CA    1 
ATOM   942  C  C     . LEU A 1 130 ? 34.503  -10.371 45.032 1.00 61.66  ? 1347 LEU A C     1 
ATOM   943  O  O     . LEU A 1 130 ? 34.529  -10.825 46.184 1.00 71.29  ? 1347 LEU A O     1 
ATOM   944  C  CB    . LEU A 1 130 ? 36.366  -8.761  44.578 1.00 64.75  ? 1347 LEU A CB    1 
ATOM   945  C  CG    . LEU A 1 130 ? 36.704  -7.438  43.897 1.00 60.51  ? 1347 LEU A CG    1 
ATOM   946  C  CD1   . LEU A 1 130 ? 38.035  -7.508  43.214 1.00 58.81  ? 1347 LEU A CD1   1 
ATOM   947  C  CD2   . LEU A 1 130 ? 35.622  -7.154  42.896 1.00 61.29  ? 1347 LEU A CD2   1 
ATOM   948  N  N     . PRO A 1 131 ? 34.165  -11.134 43.989 1.00 50.78  ? 1348 PRO A N     1 
ATOM   949  C  CA    . PRO A 1 131 ? 34.192  -10.804 42.557 1.00 50.75  ? 1348 PRO A CA    1 
ATOM   950  C  C     . PRO A 1 131 ? 32.886  -10.240 42.006 1.00 56.58  ? 1348 PRO A C     1 
ATOM   951  O  O     . PRO A 1 131 ? 31.817  -10.534 42.554 1.00 65.73  ? 1348 PRO A O     1 
ATOM   952  C  CB    . PRO A 1 131 ? 34.491  -12.151 41.908 1.00 49.40  ? 1348 PRO A CB    1 
ATOM   953  C  CG    . PRO A 1 131 ? 33.843  -13.131 42.815 1.00 53.84  ? 1348 PRO A CG    1 
ATOM   954  C  CD    . PRO A 1 131 ? 33.946  -12.570 44.214 1.00 51.42  ? 1348 PRO A CD    1 
ATOM   955  N  N     . ILE A 1 132 ? 32.956  -9.464  40.924 1.00 52.34  ? 1349 ILE A N     1 
ATOM   956  C  CA    . ILE A 1 132 ? 31.756  -9.055  40.190 1.00 51.42  ? 1349 ILE A CA    1 
ATOM   957  C  C     . ILE A 1 132 ? 31.673  -9.929  38.959 1.00 47.69  ? 1349 ILE A C     1 
ATOM   958  O  O     . ILE A 1 132 ? 32.592  -9.923  38.130 1.00 42.14  ? 1349 ILE A O     1 
ATOM   959  C  CB    . ILE A 1 132 ? 31.782  -7.561  39.809 1.00 53.48  ? 1349 ILE A CB    1 
ATOM   960  C  CG1   . ILE A 1 132 ? 31.799  -6.686  41.056 1.00 50.95  ? 1349 ILE A CG1   1 
ATOM   961  C  CG2   . ILE A 1 132 ? 30.554  -7.170  39.000 1.00 50.97  ? 1349 ILE A CG2   1 
ATOM   962  C  CD1   . ILE A 1 132 ? 30.430  -6.502  41.707 1.00 48.31  ? 1349 ILE A CD1   1 
ATOM   963  N  N     . ARG A 1 133 ? 30.562  -10.649 38.808 1.00 42.65  ? 1350 ARG A N     1 
ATOM   964  C  CA    . ARG A 1 133 ? 30.438  -11.641 37.739 1.00 35.08  ? 1350 ARG A CA    1 
ATOM   965  C  C     . ARG A 1 133 ? 29.063  -11.431 37.122 1.00 40.92  ? 1350 ARG A C     1 
ATOM   966  O  O     . ARG A 1 133 ? 28.046  -11.899 37.637 1.00 40.54  ? 1350 ARG A O     1 
ATOM   967  C  CB    . ARG A 1 133 ? 30.631  -13.055 38.263 1.00 38.43  ? 1350 ARG A CB    1 
ATOM   968  C  CG    . ARG A 1 133 ? 31.746  -13.195 39.283 1.00 52.73  ? 1350 ARG A CG    1 
ATOM   969  C  CD    . ARG A 1 133 ? 31.800  -14.601 39.807 1.00 64.88  ? 1350 ARG A CD    1 
ATOM   970  N  NE    . ARG A 1 133 ? 32.378  -15.452 38.780 1.00 68.35  ? 1350 ARG A NE    1 
ATOM   971  C  CZ    . ARG A 1 133 ? 31.885  -16.630 38.432 1.00 66.19  ? 1350 ARG A CZ    1 
ATOM   972  N  NH1   . ARG A 1 133 ? 30.793  -17.092 39.031 1.00 67.84  ? 1350 ARG A NH1   1 
ATOM   973  N  NH2   . ARG A 1 133 ? 32.464  -17.328 37.468 1.00 62.48  ? 1350 ARG A NH2   1 
ATOM   974  N  N     . LEU A 1 134 ? 29.034  -10.674 36.042 1.00 52.48  ? 1351 LEU A N     1 
ATOM   975  C  CA    . LEU A 1 134 ? 27.786  -10.235 35.465 1.00 46.76  ? 1351 LEU A CA    1 
ATOM   976  C  C     . LEU A 1 134 ? 27.632  -10.793 34.060 1.00 45.39  ? 1351 LEU A C     1 
ATOM   977  O  O     . LEU A 1 134 ? 28.616  -11.084 33.365 1.00 41.78  ? 1351 LEU A O     1 
ATOM   978  C  CB    . LEU A 1 134 ? 27.722  -8.714  35.477 1.00 33.11  ? 1351 LEU A CB    1 
ATOM   979  C  CG    . LEU A 1 134 ? 27.548  -8.198  36.900 1.00 31.21  ? 1351 LEU A CG    1 
ATOM   980  C  CD1   . LEU A 1 134 ? 27.731  -6.681  36.982 1.00 37.94  ? 1351 LEU A CD1   1 
ATOM   981  C  CD2   . LEU A 1 134 ? 26.173  -8.619  37.388 1.00 28.67  ? 1351 LEU A CD2   1 
ATOM   982  N  N     . ASN A 1 135 ? 26.379  -10.980 33.675 1.00 36.33  ? 1352 ASN A N     1 
ATOM   983  C  CA    . ASN A 1 135 ? 26.056  -11.441 32.342 1.00 36.42  ? 1352 ASN A CA    1 
ATOM   984  C  C     . ASN A 1 135 ? 24.860  -10.652 31.841 1.00 34.51  ? 1352 ASN A C     1 
ATOM   985  O  O     . ASN A 1 135 ? 23.984  -10.263 32.621 1.00 27.05  ? 1352 ASN A O     1 
ATOM   986  C  CB    . ASN A 1 135 ? 25.763  -12.955 32.355 1.00 34.22  ? 1352 ASN A CB    1 
ATOM   987  C  CG    . ASN A 1 135 ? 24.905  -13.406 31.191 1.00 30.21  ? 1352 ASN A CG    1 
ATOM   988  O  OD1   . ASN A 1 135 ? 25.360  -13.422 30.051 1.00 29.80  ? 1352 ASN A OD1   1 
ATOM   989  N  ND2   . ASN A 1 135 ? 23.658  -13.788 31.481 1.00 27.18  ? 1352 ASN A ND2   1 
ATOM   990  N  N     . GLN A 1 136 ? 24.856  -10.354 30.553 1.00 29.81  ? 1353 GLN A N     1 
ATOM   991  C  CA    . GLN A 1 136 ? 23.644  -9.855  29.940 1.00 39.50  ? 1353 GLN A CA    1 
ATOM   992  C  C     . GLN A 1 136 ? 23.388  -10.595 28.642 1.00 48.35  ? 1353 GLN A C     1 
ATOM   993  O  O     . GLN A 1 136 ? 24.308  -10.810 27.838 1.00 56.18  ? 1353 GLN A O     1 
ATOM   994  C  CB    . GLN A 1 136 ? 23.643  -8.342  29.732 1.00 44.36  ? 1353 GLN A CB    1 
ATOM   995  C  CG    . GLN A 1 136 ? 24.879  -7.616  29.308 1.00 47.22  ? 1353 GLN A CG    1 
ATOM   996  C  CD    . GLN A 1 136 ? 24.589  -6.114  29.217 1.00 42.16  ? 1353 GLN A CD    1 
ATOM   997  O  OE1   . GLN A 1 136 ? 23.539  -5.655  29.679 1.00 32.77  ? 1353 GLN A OE1   1 
ATOM   998  N  NE2   . GLN A 1 136 ? 25.491  -5.355  28.592 1.00 41.48  ? 1353 GLN A NE2   1 
ATOM   999  N  N     . TRP A 1 137 ? 22.138  -11.010 28.475 1.00 42.42  ? 1354 TRP A N     1 
ATOM   1000 C  CA    . TRP A 1 137 ? 21.613  -11.454 27.193 1.00 48.22  ? 1354 TRP A CA    1 
ATOM   1001 C  C     . TRP A 1 137 ? 21.078  -10.225 26.481 1.00 44.05  ? 1354 TRP A C     1 
ATOM   1002 O  O     . TRP A 1 137 ? 20.128  -9.598  26.955 1.00 54.46  ? 1354 TRP A O     1 
ATOM   1003 C  CB    . TRP A 1 137 ? 20.488  -12.471 27.370 1.00 47.94  ? 1354 TRP A CB    1 
ATOM   1004 C  CG    . TRP A 1 137 ? 20.853  -13.716 28.051 1.00 43.39  ? 1354 TRP A CG    1 
ATOM   1005 C  CD1   . TRP A 1 137 ? 20.668  -14.023 29.369 1.00 43.52  ? 1354 TRP A CD1   1 
ATOM   1006 C  CD2   . TRP A 1 137 ? 21.441  -14.856 27.448 1.00 44.65  ? 1354 TRP A CD2   1 
ATOM   1007 N  NE1   . TRP A 1 137 ? 21.131  -15.289 29.628 1.00 47.60  ? 1354 TRP A NE1   1 
ATOM   1008 C  CE2   . TRP A 1 137 ? 21.613  -15.823 28.462 1.00 48.28  ? 1354 TRP A CE2   1 
ATOM   1009 C  CE3   . TRP A 1 137 ? 21.844  -15.157 26.149 1.00 43.70  ? 1354 TRP A CE3   1 
ATOM   1010 C  CZ2   . TRP A 1 137 ? 22.172  -17.060 28.215 1.00 50.62  ? 1354 TRP A CZ2   1 
ATOM   1011 C  CZ3   . TRP A 1 137 ? 22.393  -16.391 25.905 1.00 51.01  ? 1354 TRP A CZ3   1 
ATOM   1012 C  CH2   . TRP A 1 137 ? 22.555  -17.329 26.934 1.00 52.37  ? 1354 TRP A CH2   1 
ATOM   1013 N  N     . ASN A 1 138 ? 21.702  -9.845  25.377 1.00 33.10  ? 1355 ASN A N     1 
ATOM   1014 C  CA    . ASN A 1 138 ? 21.202  -8.668  24.681 1.00 31.08  ? 1355 ASN A CA    1 
ATOM   1015 C  C     . ASN A 1 138 ? 21.528  -8.784  23.201 1.00 35.30  ? 1355 ASN A C     1 
ATOM   1016 O  O     . ASN A 1 138 ? 22.132  -9.759  22.751 1.00 57.93  ? 1355 ASN A O     1 
ATOM   1017 C  CB    . ASN A 1 138 ? 21.727  -7.370  25.336 1.00 34.83  ? 1355 ASN A CB    1 
ATOM   1018 C  CG    . ASN A 1 138 ? 23.248  -7.222  25.282 1.00 40.42  ? 1355 ASN A CG    1 
ATOM   1019 O  OD1   . ASN A 1 138 ? 23.881  -7.411  24.249 1.00 35.88  ? 1355 ASN A OD1   1 
ATOM   1020 N  ND2   . ASN A 1 138 ? 23.831  -6.860  26.411 1.00 38.53  ? 1355 ASN A ND2   1 
ATOM   1021 N  N     . ASN A 1 139 ? 21.136  -7.764  22.447 1.00 26.14  ? 1356 ASN A N     1 
ATOM   1022 C  CA    . ASN A 1 139 ? 21.368  -7.686  21.010 1.00 34.53  ? 1356 ASN A CA    1 
ATOM   1023 C  C     . ASN A 1 139 ? 22.377  -6.586  20.734 1.00 40.03  ? 1356 ASN A C     1 
ATOM   1024 O  O     . ASN A 1 139 ? 22.457  -5.604  21.477 1.00 28.71  ? 1356 ASN A O     1 
ATOM   1025 C  CB    . ASN A 1 139 ? 20.102  -7.341  20.254 1.00 28.29  ? 1356 ASN A CB    1 
ATOM   1026 C  CG    . ASN A 1 139 ? 19.556  -6.029  20.693 1.00 32.86  ? 1356 ASN A CG    1 
ATOM   1027 O  OD1   . ASN A 1 139 ? 19.655  -5.679  21.876 1.00 37.29  ? 1356 ASN A OD1   1 
ATOM   1028 N  ND2   . ASN A 1 139 ? 19.017  -5.265  19.755 1.00 32.31  ? 1356 ASN A ND2   1 
ATOM   1029 N  N     . VAL A 1 140 ? 23.191  -6.787  19.699 1.00 38.54  ? 1357 VAL A N     1 
ATOM   1030 C  CA    . VAL A 1 140 ? 24.211  -5.823  19.330 1.00 27.49  ? 1357 VAL A CA    1 
ATOM   1031 C  C     . VAL A 1 140 ? 24.240  -5.697  17.813 1.00 45.50  ? 1357 VAL A C     1 
ATOM   1032 O  O     . VAL A 1 140 ? 23.747  -6.560  17.079 1.00 48.53  ? 1357 VAL A O     1 
ATOM   1033 C  CB    . VAL A 1 140 ? 25.595  -6.179  19.898 1.00 27.73  ? 1357 VAL A CB    1 
ATOM   1034 C  CG1   . VAL A 1 140 ? 25.499  -6.398  21.395 1.00 27.41  ? 1357 VAL A CG1   1 
ATOM   1035 C  CG2   . VAL A 1 140 ? 26.158  -7.395  19.216 1.00 31.38  ? 1357 VAL A CG2   1 
ATOM   1036 N  N     . VAL A 1 141 ? 24.769  -4.554  17.366 1.00 36.36  ? 1358 VAL A N     1 
ATOM   1037 C  CA    . VAL A 1 141 ? 24.808  -4.146  15.967 1.00 38.50  ? 1358 VAL A CA    1 
ATOM   1038 C  C     . VAL A 1 141 ? 26.259  -3.859  15.591 1.00 35.29  ? 1358 VAL A C     1 
ATOM   1039 O  O     . VAL A 1 141 ? 26.992  -3.240  16.360 1.00 41.83  ? 1358 VAL A O     1 
ATOM   1040 C  CB    . VAL A 1 141 ? 23.933  -2.906  15.711 1.00 52.43  ? 1358 VAL A CB    1 
ATOM   1041 C  CG1   . VAL A 1 141 ? 24.111  -2.437  14.272 1.00 61.00  ? 1358 VAL A CG1   1 
ATOM   1042 C  CG2   . VAL A 1 141 ? 22.474  -3.208  15.990 1.00 28.29  ? 1358 VAL A CG2   1 
ATOM   1043 N  N     . ARG A 1 142 ? 26.709  -4.421  14.480 1.00 29.81  ? 1359 ARG A N     1 
ATOM   1044 C  CA    . ARG A 1 142 ? 27.987  -4.024  13.904 1.00 32.19  ? 1359 ARG A CA    1 
ATOM   1045 C  C     . ARG A 1 142 ? 27.846  -3.983  12.392 1.00 44.28  ? 1359 ARG A C     1 
ATOM   1046 O  O     . ARG A 1 142 ? 27.460  -4.983  11.784 1.00 44.87  ? 1359 ARG A O     1 
ATOM   1047 C  CB    . ARG A 1 142 ? 29.083  -4.970  14.328 1.00 43.22  ? 1359 ARG A CB    1 
ATOM   1048 C  CG    . ARG A 1 142 ? 29.034  -5.340  15.792 1.00 43.37  ? 1359 ARG A CG    1 
ATOM   1049 C  CD    . ARG A 1 142 ? 29.966  -6.463  15.992 1.00 46.00  ? 1359 ARG A CD    1 
ATOM   1050 N  NE    . ARG A 1 142 ? 30.234  -6.731  17.377 1.00 42.55  ? 1359 ARG A NE    1 
ATOM   1051 C  CZ    . ARG A 1 142 ? 31.177  -7.568  17.737 1.00 54.99  ? 1359 ARG A CZ    1 
ATOM   1052 N  NH1   . ARG A 1 142 ? 31.888  -8.154  16.784 1.00 59.65  ? 1359 ARG A NH1   1 
ATOM   1053 N  NH2   . ARG A 1 142 ? 31.416  -7.800  19.017 1.00 67.30  ? 1359 ARG A NH2   1 
ATOM   1054 N  N     . TRP A 1 143 ? 28.167  -2.839  11.781 1.00 60.70  ? 1360 TRP A N     1 
ATOM   1055 C  CA    . TRP A 1 143 ? 28.025  -2.652  10.334 1.00 59.31  ? 1360 TRP A CA    1 
ATOM   1056 C  C     . TRP A 1 143 ? 29.212  -3.285  9.617  1.00 69.26  ? 1360 TRP A C     1 
ATOM   1057 O  O     . TRP A 1 143 ? 30.069  -2.612  9.042  1.00 77.47  ? 1360 TRP A O     1 
ATOM   1058 C  CB    . TRP A 1 143 ? 27.909  -1.176  10.000 1.00 55.67  ? 1360 TRP A CB    1 
ATOM   1059 C  CG    . TRP A 1 143 ? 26.878  -0.913  8.999  1.00 62.02  ? 1360 TRP A CG    1 
ATOM   1060 C  CD1   . TRP A 1 143 ? 27.067  -0.608  7.683  1.00 68.81  ? 1360 TRP A CD1   1 
ATOM   1061 C  CD2   . TRP A 1 143 ? 25.469  -0.932  9.210  1.00 59.58  ? 1360 TRP A CD2   1 
ATOM   1062 N  NE1   . TRP A 1 143 ? 25.851  -0.428  7.058  1.00 66.58  ? 1360 TRP A NE1   1 
ATOM   1063 C  CE2   . TRP A 1 143 ? 24.856  -0.623  7.979  1.00 64.01  ? 1360 TRP A CE2   1 
ATOM   1064 C  CE3   . TRP A 1 143 ? 24.664  -1.172  10.323 1.00 59.27  ? 1360 TRP A CE3   1 
ATOM   1065 C  CZ2   . TRP A 1 143 ? 23.490  -0.549  7.835  1.00 68.00  ? 1360 TRP A CZ2   1 
ATOM   1066 C  CZ3   . TRP A 1 143 ? 23.313  -1.105  10.175 1.00 66.54  ? 1360 TRP A CZ3   1 
ATOM   1067 C  CH2   . TRP A 1 143 ? 22.737  -0.802  8.940  1.00 72.10  ? 1360 TRP A CH2   1 
ATOM   1068 N  N     . GLU A 1 144 ? 29.216  -4.616  9.621  1.00 72.04  ? 1361 GLU A N     1 
ATOM   1069 C  CA    . GLU A 1 144 ? 30.402  -5.347  9.197  1.00 74.64  ? 1361 GLU A CA    1 
ATOM   1070 C  C     . GLU A 1 144 ? 30.736  -5.015  7.752  1.00 60.74  ? 1361 GLU A C     1 
ATOM   1071 O  O     . GLU A 1 144 ? 29.851  -4.795  6.923  1.00 46.15  ? 1361 GLU A O     1 
ATOM   1072 C  CB    . GLU A 1 144 ? 30.233  -6.869  9.393  1.00 81.45  ? 1361 GLU A CB    1 
ATOM   1073 C  CG    . GLU A 1 144 ? 29.727  -7.290  10.794 1.00 78.88  ? 1361 GLU A CG    1 
ATOM   1074 C  CD    . GLU A 1 144 ? 30.746  -8.122  11.603 1.00 83.29  ? 1361 GLU A CD    1 
ATOM   1075 O  OE1   . GLU A 1 144 ? 30.394  -8.611  12.709 1.00 85.09  ? 1361 GLU A OE1   1 
ATOM   1076 O  OE2   . GLU A 1 144 ? 31.904  -8.273  11.146 1.00 84.35  ? 1361 GLU A OE2   1 
ATOM   1077 N  N     . PHE A 1 145 ? 32.029  -4.907  7.490  1.00 72.18  ? 1362 PHE A N     1 
ATOM   1078 C  CA    . PHE A 1 145 ? 32.608  -4.680  6.178  1.00 80.03  ? 1362 PHE A CA    1 
ATOM   1079 C  C     . PHE A 1 145 ? 32.670  -5.956  5.352  1.00 79.55  ? 1362 PHE A C     1 
ATOM   1080 O  O     . PHE A 1 145 ? 33.339  -5.974  4.322  1.00 87.82  ? 1362 PHE A O     1 
ATOM   1081 C  CB    . PHE A 1 145 ? 34.009  -4.048  6.310  1.00 95.53  ? 1362 PHE A CB    1 
ATOM   1082 C  CG    . PHE A 1 145 ? 34.891  -4.663  7.397  1.00 119.47 ? 1362 PHE A CG    1 
ATOM   1083 C  CD1   . PHE A 1 145 ? 35.999  -5.435  7.053  1.00 132.77 ? 1362 PHE A CD1   1 
ATOM   1084 C  CD2   . PHE A 1 145 ? 34.644  -4.439  8.750  1.00 128.58 ? 1362 PHE A CD2   1 
ATOM   1085 C  CE1   . PHE A 1 145 ? 36.831  -5.996  8.039  1.00 132.24 ? 1362 PHE A CE1   1 
ATOM   1086 C  CE2   . PHE A 1 145 ? 35.470  -4.998  9.738  1.00 132.82 ? 1362 PHE A CE2   1 
ATOM   1087 C  CZ    . PHE A 1 145 ? 36.563  -5.776  9.380  1.00 131.65 ? 1362 PHE A CZ    1 
ATOM   1088 N  N     . LYS A 1 146 ? 32.110  -7.052  5.851  1.00 75.66  ? 1363 LYS A N     1 
ATOM   1089 C  CA    . LYS A 1 146 ? 32.092  -8.324  5.150  1.00 69.69  ? 1363 LYS A CA    1 
ATOM   1090 C  C     . LYS A 1 146 ? 30.683  -8.697  4.722  1.00 77.25  ? 1363 LYS A C     1 
ATOM   1091 O  O     . LYS A 1 146 ? 29.705  -8.390  5.413  1.00 76.43  ? 1363 LYS A O     1 
ATOM   1092 C  CB    . LYS A 1 146 ? 32.632  -9.432  6.030  1.00 68.59  ? 1363 LYS A CB    1 
ATOM   1093 C  CG    . LYS A 1 146 ? 33.889  -9.061  6.786  1.00 72.27  ? 1363 LYS A CG    1 
ATOM   1094 C  CD    . LYS A 1 146 ? 34.653  -10.314 7.226  1.00 73.52  ? 1363 LYS A CD    1 
ATOM   1095 C  CE    . LYS A 1 146 ? 35.471  -10.059 8.492  1.00 77.80  ? 1363 LYS A CE    1 
ATOM   1096 N  NZ    . LYS A 1 146 ? 35.880  -11.326 9.184  1.00 77.47  ? 1363 LYS A NZ    1 
ATOM   1097 N  N     . HIS A 1 147 ? 30.595  -9.398  3.592  1.00 78.97  ? 1364 HIS A N     1 
ATOM   1098 C  CA    . HIS A 1 147 ? 29.326  -9.925  3.123  1.00 67.21  ? 1364 HIS A CA    1 
ATOM   1099 C  C     . HIS A 1 147 ? 28.672  -10.692 4.265  1.00 60.28  ? 1364 HIS A C     1 
ATOM   1100 O  O     . HIS A 1 147 ? 29.301  -11.598 4.831  1.00 68.55  ? 1364 HIS A O     1 
ATOM   1101 C  CB    . HIS A 1 147 ? 29.511  -10.844 1.921  1.00 71.33  ? 1364 HIS A CB    1 
ATOM   1102 C  CG    . HIS A 1 147 ? 30.162  -10.186 0.746  1.00 81.53  ? 1364 HIS A CG    1 
ATOM   1103 N  ND1   . HIS A 1 147 ? 30.675  -10.900 -0.316 1.00 86.53  ? 1364 HIS A ND1   1 
ATOM   1104 C  CD2   . HIS A 1 147 ? 30.389  -8.881  0.467  1.00 85.23  ? 1364 HIS A CD2   1 
ATOM   1105 C  CE1   . HIS A 1 147 ? 31.190  -10.063 -1.199 1.00 89.96  ? 1364 HIS A CE1   1 
ATOM   1106 N  NE2   . HIS A 1 147 ? 31.029  -8.831  -0.747 1.00 86.93  ? 1364 HIS A NE2   1 
ATOM   1107 N  N     . PRO A 1 148 ? 27.463  -10.328 4.667  1.00 53.56  ? 1365 PRO A N     1 
ATOM   1108 C  CA    . PRO A 1 148 ? 26.775  -11.060 5.729  1.00 45.69  ? 1365 PRO A CA    1 
ATOM   1109 C  C     . PRO A 1 148 ? 26.068  -12.291 5.203  1.00 48.08  ? 1365 PRO A C     1 
ATOM   1110 O  O     . PRO A 1 148 ? 25.636  -12.350 4.051  1.00 50.00  ? 1365 PRO A O     1 
ATOM   1111 C  CB    . PRO A 1 148 ? 25.773  -10.036 6.262  1.00 42.56  ? 1365 PRO A CB    1 
ATOM   1112 C  CG    . PRO A 1 148 ? 25.466  -9.184  5.098  1.00 46.43  ? 1365 PRO A CG    1 
ATOM   1113 C  CD    . PRO A 1 148 ? 26.708  -9.141  4.239  1.00 55.61  ? 1365 PRO A CD    1 
ATOM   1114 N  N     . GLN A 1 149 ? 26.025  -13.308 6.051  1.00 50.97  ? 1366 GLN A N     1 
ATOM   1115 C  CA    . GLN A 1 149 ? 25.308  -14.535 5.782  1.00 57.31  ? 1366 GLN A CA    1 
ATOM   1116 C  C     . GLN A 1 149 ? 24.444  -14.803 7.009  1.00 52.11  ? 1366 GLN A C     1 
ATOM   1117 O  O     . GLN A 1 149 ? 24.863  -14.518 8.136  1.00 46.68  ? 1366 GLN A O     1 
ATOM   1118 C  CB    . GLN A 1 149 ? 26.282  -15.695 5.474  1.00 69.44  ? 1366 GLN A CB    1 
ATOM   1119 C  CG    . GLN A 1 149 ? 25.636  -16.933 4.809  1.00 90.18  ? 1366 GLN A CG    1 
ATOM   1120 C  CD    . GLN A 1 149 ? 26.300  -17.404 3.488  1.00 105.47 ? 1366 GLN A CD    1 
ATOM   1121 O  OE1   . GLN A 1 149 ? 26.313  -16.669 2.493  1.00 110.73 ? 1366 GLN A OE1   1 
ATOM   1122 N  NE2   . GLN A 1 149 ? 26.804  -18.655 3.470  1.00 102.22 ? 1366 GLN A NE2   1 
ATOM   1123 N  N     . PRO A 1 150 ? 23.232  -15.331 6.813  1.00 47.04  ? 1367 PRO A N     1 
ATOM   1124 C  CA    . PRO A 1 150 ? 22.158  -15.200 7.815  1.00 54.52  ? 1367 PRO A CA    1 
ATOM   1125 C  C     . PRO A 1 150 ? 22.381  -15.645 9.253  1.00 61.09  ? 1367 PRO A C     1 
ATOM   1126 O  O     . PRO A 1 150 ? 21.676  -15.117 10.123 1.00 65.03  ? 1367 PRO A O     1 
ATOM   1127 C  CB    . PRO A 1 150 ? 21.005  -15.967 7.160  1.00 52.32  ? 1367 PRO A CB    1 
ATOM   1128 C  CG    . PRO A 1 150 ? 21.469  -16.251 5.745  1.00 54.24  ? 1367 PRO A CG    1 
ATOM   1129 C  CD    . PRO A 1 150 ? 22.625  -15.356 5.486  1.00 43.86  ? 1367 PRO A CD    1 
ATOM   1130 N  N     . PHE A 1 151 ? 23.197  -16.609 9.578  1.00 55.93  ? 1368 PHE A N     1 
ATOM   1131 C  CA    . PHE A 1 151 ? 23.410  -16.700 11.018 1.00 43.03  ? 1368 PHE A CA    1 
ATOM   1132 C  C     . PHE A 1 151 ? 24.845  -16.462 11.420 1.00 45.70  ? 1368 PHE A C     1 
ATOM   1133 O  O     . PHE A 1 151 ? 25.109  -15.937 12.516 1.00 30.21  ? 1368 PHE A O     1 
ATOM   1134 C  CB    . PHE A 1 151 ? 22.968  -18.061 11.544 1.00 34.85  ? 1368 PHE A CB    1 
ATOM   1135 C  CG    . PHE A 1 151 ? 21.473  -18.257 11.588 1.00 35.34  ? 1368 PHE A CG    1 
ATOM   1136 C  CD1   . PHE A 1 151 ? 20.759  -17.957 12.728 1.00 32.07  ? 1368 PHE A CD1   1 
ATOM   1137 C  CD2   . PHE A 1 151 ? 20.790  -18.789 10.498 1.00 33.83  ? 1368 PHE A CD2   1 
ATOM   1138 C  CE1   . PHE A 1 151 ? 19.390  -18.172 12.787 1.00 32.25  ? 1368 PHE A CE1   1 
ATOM   1139 C  CE2   . PHE A 1 151 ? 19.421  -19.010 10.552 1.00 33.44  ? 1368 PHE A CE2   1 
ATOM   1140 C  CZ    . PHE A 1 151 ? 18.721  -18.695 11.705 1.00 33.67  ? 1368 PHE A CZ    1 
ATOM   1141 N  N     . LEU A 1 152 ? 25.765  -16.780 10.515 1.00 52.41  ? 1369 LEU A N     1 
ATOM   1142 C  CA    . LEU A 1 152 ? 27.191  -16.730 10.788 1.00 47.57  ? 1369 LEU A CA    1 
ATOM   1143 C  C     . LEU A 1 152 ? 27.660  -15.305 11.039 1.00 46.74  ? 1369 LEU A C     1 
ATOM   1144 O  O     . LEU A 1 152 ? 28.456  -15.054 11.953 1.00 48.34  ? 1369 LEU A O     1 
ATOM   1145 C  CB    . LEU A 1 152 ? 27.919  -17.382 9.613  1.00 43.14  ? 1369 LEU A CB    1 
ATOM   1146 C  CG    . LEU A 1 152 ? 27.246  -18.741 9.322  1.00 36.08  ? 1369 LEU A CG    1 
ATOM   1147 C  CD1   . LEU A 1 152 ? 27.732  -19.443 8.041  1.00 33.83  ? 1369 LEU A CD1   1 
ATOM   1148 C  CD2   . LEU A 1 152 ? 27.407  -19.634 10.532 1.00 32.60  ? 1369 LEU A CD2   1 
ATOM   1149 N  N     . ARG A 1 153 ? 27.172  -14.358 10.248 1.00 42.70  ? 1370 ARG A N     1 
ATOM   1150 C  CA    . ARG A 1 153 ? 27.577  -12.963 10.401 1.00 40.87  ? 1370 ARG A CA    1 
ATOM   1151 C  C     . ARG A 1 153 ? 26.386  -12.100 10.019 1.00 40.50  ? 1370 ARG A C     1 
ATOM   1152 O  O     . ARG A 1 153 ? 26.098  -11.922 8.831  1.00 48.02  ? 1370 ARG A O     1 
ATOM   1153 C  CB    . ARG A 1 153 ? 28.781  -12.610 9.553  1.00 43.71  ? 1370 ARG A CB    1 
ATOM   1154 C  CG    . ARG A 1 153 ? 29.179  -11.180 9.753  1.00 54.60  ? 1370 ARG A CG    1 
ATOM   1155 C  CD    . ARG A 1 153 ? 30.386  -10.813 8.927  1.00 67.10  ? 1370 ARG A CD    1 
ATOM   1156 N  NE    . ARG A 1 153 ? 31.339  -11.906 8.861  1.00 70.07  ? 1370 ARG A NE    1 
ATOM   1157 C  CZ    . ARG A 1 153 ? 32.173  -12.212 9.846  1.00 80.65  ? 1370 ARG A CZ    1 
ATOM   1158 N  NH1   . ARG A 1 153 ? 33.009  -13.224 9.705  1.00 88.78  ? 1370 ARG A NH1   1 
ATOM   1159 N  NH2   . ARG A 1 153 ? 32.162  -11.521 10.979 1.00 81.16  ? 1370 ARG A NH2   1 
ATOM   1160 N  N     . THR A 1 154 ? 25.677  -11.624 11.023 1.00 31.25  ? 1371 THR A N     1 
ATOM   1161 C  CA    . THR A 1 154 ? 24.569  -10.720 10.805 1.00 37.57  ? 1371 THR A CA    1 
ATOM   1162 C  C     . THR A 1 154 ? 24.889  -9.367  11.432 1.00 46.82  ? 1371 THR A C     1 
ATOM   1163 O  O     . THR A 1 154 ? 25.719  -9.270  12.345 1.00 31.38  ? 1371 THR A O     1 
ATOM   1164 C  CB    . THR A 1 154 ? 23.274  -11.342 11.330 1.00 35.26  ? 1371 THR A CB    1 
ATOM   1165 O  OG1   . THR A 1 154 ? 23.393  -11.688 12.723 1.00 32.96  ? 1371 THR A OG1   1 
ATOM   1166 C  CG2   . THR A 1 154 ? 23.071  -12.581 10.572 1.00 30.04  ? 1371 THR A CG2   1 
ATOM   1167 N  N     . ARG A 1 155 ? 24.268  -8.314  10.875 1.00 49.13  ? 1372 ARG A N     1 
ATOM   1168 C  CA    . ARG A 1 155 ? 24.576  -6.942  11.265 1.00 46.19  ? 1372 ARG A CA    1 
ATOM   1169 C  C     . ARG A 1 155 ? 23.949  -6.583  12.605 1.00 42.10  ? 1372 ARG A C     1 
ATOM   1170 O  O     . ARG A 1 155 ? 24.535  -5.820  13.380 1.00 37.43  ? 1372 ARG A O     1 
ATOM   1171 C  CB    . ARG A 1 155 ? 24.164  -5.973  10.156 1.00 45.24  ? 1372 ARG A CB    1 
ATOM   1172 C  CG    . ARG A 1 155 ? 25.310  -5.816  9.153  1.00 56.49  ? 1372 ARG A CG    1 
ATOM   1173 C  CD    . ARG A 1 155 ? 25.196  -4.655  8.174  1.00 61.13  ? 1372 ARG A CD    1 
ATOM   1174 N  NE    . ARG A 1 155 ? 26.247  -4.769  7.165  1.00 65.31  ? 1372 ARG A NE    1 
ATOM   1175 C  CZ    . ARG A 1 155 ? 26.112  -4.377  5.907  1.00 80.03  ? 1372 ARG A CZ    1 
ATOM   1176 N  NH1   . ARG A 1 155 ? 24.968  -3.846  5.514  1.00 90.30  ? 1372 ARG A NH1   1 
ATOM   1177 N  NH2   . ARG A 1 155 ? 27.110  -4.519  5.047  1.00 81.61  ? 1372 ARG A NH2   1 
ATOM   1178 N  N     . GLU A 1 156 ? 22.781  -7.109  12.906 1.00 28.95  ? 1373 GLU A N     1 
ATOM   1179 C  CA    . GLU A 1 156 ? 22.355  -7.231  14.283 1.00 28.33  ? 1373 GLU A CA    1 
ATOM   1180 C  C     . GLU A 1 156 ? 22.441  -8.712  14.604 1.00 32.88  ? 1373 GLU A C     1 
ATOM   1181 O  O     . GLU A 1 156 ? 22.187  -9.554  13.732 1.00 29.75  ? 1373 GLU A O     1 
ATOM   1182 C  CB    . GLU A 1 156 ? 20.936  -6.693  14.514 1.00 27.99  ? 1373 GLU A CB    1 
ATOM   1183 C  CG    . GLU A 1 156 ? 20.506  -6.850  15.963 1.00 27.43  ? 1373 GLU A CG    1 
ATOM   1184 C  CD    . GLU A 1 156 ? 19.000  -6.842  16.168 1.00 42.35  ? 1373 GLU A CD    1 
ATOM   1185 O  OE1   . GLU A 1 156 ? 18.263  -6.858  15.158 1.00 48.13  ? 1373 GLU A OE1   1 
ATOM   1186 O  OE2   . GLU A 1 156 ? 18.546  -6.853  17.341 1.00 26.72  ? 1373 GLU A OE2   1 
ATOM   1187 N  N     . PHE A 1 157 ? 22.909  -9.027  15.806 1.00 32.38  ? 1374 PHE A N     1 
ATOM   1188 C  CA    . PHE A 1 157 ? 22.838  -10.397 16.286 1.00 29.21  ? 1374 PHE A CA    1 
ATOM   1189 C  C     . PHE A 1 157 ? 22.626  -10.402 17.786 1.00 38.47  ? 1374 PHE A C     1 
ATOM   1190 O  O     . PHE A 1 157 ? 22.989  -9.452  18.484 1.00 60.37  ? 1374 PHE A O     1 
ATOM   1191 C  CB    . PHE A 1 157 ? 24.069  -11.209 15.908 1.00 28.20  ? 1374 PHE A CB    1 
ATOM   1192 C  CG    . PHE A 1 157 ? 25.348  -10.712 16.472 1.00 30.75  ? 1374 PHE A CG    1 
ATOM   1193 C  CD1   . PHE A 1 157 ? 25.694  -10.972 17.779 1.00 40.72  ? 1374 PHE A CD1   1 
ATOM   1194 C  CD2   . PHE A 1 157 ? 26.254  -10.071 15.664 1.00 36.36  ? 1374 PHE A CD2   1 
ATOM   1195 C  CE1   . PHE A 1 157 ? 26.910  -10.548 18.281 1.00 40.51  ? 1374 PHE A CE1   1 
ATOM   1196 C  CE2   . PHE A 1 157 ? 27.463  -9.648  16.153 1.00 35.17  ? 1374 PHE A CE2   1 
ATOM   1197 C  CZ    . PHE A 1 157 ? 27.798  -9.886  17.456 1.00 35.61  ? 1374 PHE A CZ    1 
ATOM   1198 N  N     . LEU A 1 158 ? 21.996  -11.458 18.267 1.00 33.38  ? 1375 LEU A N     1 
ATOM   1199 C  CA    . LEU A 1 158 ? 21.770  -11.636 19.691 1.00 38.21  ? 1375 LEU A CA    1 
ATOM   1200 C  C     . LEU A 1 158 ? 22.871  -12.503 20.309 1.00 42.66  ? 1375 LEU A C     1 
ATOM   1201 O  O     . LEU A 1 158 ? 23.438  -13.400 19.668 1.00 43.16  ? 1375 LEU A O     1 
ATOM   1202 C  CB    . LEU A 1 158 ? 20.404  -12.251 19.947 1.00 32.31  ? 1375 LEU A CB    1 
ATOM   1203 C  CG    . LEU A 1 158 ? 19.225  -11.687 19.172 1.00 34.53  ? 1375 LEU A CG    1 
ATOM   1204 C  CD1   . LEU A 1 158 ? 18.152  -12.765 19.140 1.00 37.70  ? 1375 LEU A CD1   1 
ATOM   1205 C  CD2   . LEU A 1 158 ? 18.691  -10.406 19.800 1.00 34.06  ? 1375 LEU A CD2   1 
ATOM   1206 N  N     . TRP A 1 159 ? 23.197  -12.213 21.560 1.00 34.55  ? 1376 TRP A N     1 
ATOM   1207 C  CA    . TRP A 1 159 ? 24.235  -12.986 22.207 1.00 39.95  ? 1376 TRP A CA    1 
ATOM   1208 C  C     . TRP A 1 159 ? 24.036  -12.940 23.712 1.00 44.92  ? 1376 TRP A C     1 
ATOM   1209 O  O     . TRP A 1 159 ? 23.060  -12.377 24.232 1.00 52.17  ? 1376 TRP A O     1 
ATOM   1210 C  CB    . TRP A 1 159 ? 25.624  -12.485 21.788 1.00 42.12  ? 1376 TRP A CB    1 
ATOM   1211 C  CG    . TRP A 1 159 ? 26.077  -11.192 22.356 1.00 56.61  ? 1376 TRP A CG    1 
ATOM   1212 C  CD1   . TRP A 1 159 ? 25.394  -10.362 23.204 1.00 59.15  ? 1376 TRP A CD1   1 
ATOM   1213 C  CD2   . TRP A 1 159 ? 27.334  -10.551 22.101 1.00 66.13  ? 1376 TRP A CD2   1 
ATOM   1214 N  NE1   . TRP A 1 159 ? 26.160  -9.256  23.509 1.00 53.66  ? 1376 TRP A NE1   1 
ATOM   1215 C  CE2   . TRP A 1 159 ? 27.349  -9.342  22.837 1.00 50.08  ? 1376 TRP A CE2   1 
ATOM   1216 C  CE3   . TRP A 1 159 ? 28.453  -10.885 21.325 1.00 69.03  ? 1376 TRP A CE3   1 
ATOM   1217 C  CZ2   . TRP A 1 159 ? 28.426  -8.473  22.814 1.00 38.18  ? 1376 TRP A CZ2   1 
ATOM   1218 C  CZ3   . TRP A 1 159 ? 29.530  -10.013 21.306 1.00 59.44  ? 1376 TRP A CZ3   1 
ATOM   1219 C  CH2   . TRP A 1 159 ? 29.504  -8.818  22.044 1.00 50.87  ? 1376 TRP A CH2   1 
ATOM   1220 N  N     . GLN A 1 160 ? 25.055  -13.412 24.401 1.00 41.55  ? 1377 GLN A N     1 
ATOM   1221 C  CA    . GLN A 1 160 ? 25.216  -13.263 25.799 1.00 43.17  ? 1377 GLN A CA    1 
ATOM   1222 C  C     . GLN A 1 160 ? 26.639  -12.819 25.969 1.00 40.99  ? 1377 GLN A C     1 
ATOM   1223 O  O     . GLN A 1 160 ? 27.479  -13.403 25.432 1.00 57.21  ? 1377 GLN A O     1 
ATOM   1224 C  CB    . GLN A 1 160 ? 25.015  -14.578 26.538 1.00 50.18  ? 1377 GLN A CB    1 
ATOM   1225 C  CG    . GLN A 1 160 ? 25.991  -15.694 26.274 1.00 34.57  ? 1377 GLN A CG    1 
ATOM   1226 C  CD    . GLN A 1 160 ? 27.254  -15.581 27.008 1.00 43.71  ? 1377 GLN A CD    1 
ATOM   1227 O  OE1   . GLN A 1 160 ? 28.283  -15.840 26.492 1.00 48.70  ? 1377 GLN A OE1   1 
ATOM   1228 N  NE2   . GLN A 1 160 ? 27.181  -15.205 28.196 1.00 51.22  ? 1377 GLN A NE2   1 
ATOM   1229 N  N     . GLU A 1 161 ? 26.896  -11.728 26.651 1.00 45.67  ? 1378 GLU A N     1 
ATOM   1230 C  CA    . GLU A 1 161 ? 28.228  -11.279 27.039 1.00 49.17  ? 1378 GLU A CA    1 
ATOM   1231 C  C     . GLU A 1 161 ? 28.312  -11.326 28.550 1.00 47.78  ? 1378 GLU A C     1 
ATOM   1232 O  O     . GLU A 1 161 ? 27.435  -10.799 29.241 1.00 51.38  ? 1378 GLU A O     1 
ATOM   1233 C  CB    . GLU A 1 161 ? 28.582  -9.871  26.528 1.00 45.89  ? 1378 GLU A CB    1 
ATOM   1234 C  CG    . GLU A 1 161 ? 27.565  -8.772  26.783 1.00 48.28  ? 1378 GLU A CG    1 
ATOM   1235 C  CD    . GLU A 1 161 ? 27.952  -7.432  26.140 1.00 44.60  ? 1378 GLU A CD    1 
ATOM   1236 O  OE1   . GLU A 1 161 ? 29.148  -7.057  26.144 1.00 37.32  ? 1378 GLU A OE1   1 
ATOM   1237 O  OE2   . GLU A 1 161 ? 27.044  -6.744  25.643 1.00 38.02  ? 1378 GLU A OE2   1 
ATOM   1238 N  N     . GLY A 1 162 ? 29.324  -12.018 29.051 1.00 44.81  ? 1379 GLY A N     1 
ATOM   1239 C  CA    . GLY A 1 162 ? 29.610  -12.068 30.475 1.00 38.83  ? 1379 GLY A CA    1 
ATOM   1240 C  C     . GLY A 1 162 ? 30.934  -11.375 30.731 1.00 40.98  ? 1379 GLY A C     1 
ATOM   1241 O  O     . GLY A 1 162 ? 31.903  -11.585 30.000 1.00 39.83  ? 1379 GLY A O     1 
ATOM   1242 N  N     . HIS A 1 163 ? 30.959  -10.545 31.768 1.00 46.09  ? 1380 HIS A N     1 
ATOM   1243 C  CA    . HIS A 1 163 ? 32.131  -9.755  32.119 1.00 50.12  ? 1380 HIS A CA    1 
ATOM   1244 C  C     . HIS A 1 163 ? 32.367  -9.920  33.603 1.00 47.41  ? 1380 HIS A C     1 
ATOM   1245 O  O     . HIS A 1 163 ? 31.422  -9.806  34.395 1.00 43.30  ? 1380 HIS A O     1 
ATOM   1246 C  CB    . HIS A 1 163 ? 31.960  -8.266  31.782 1.00 48.63  ? 1380 HIS A CB    1 
ATOM   1247 C  CG    . HIS A 1 163 ? 31.634  -8.002  30.350 1.00 40.27  ? 1380 HIS A CG    1 
ATOM   1248 N  ND1   . HIS A 1 163 ? 32.589  -7.639  29.430 1.00 41.38  ? 1380 HIS A ND1   1 
ATOM   1249 C  CD2   . HIS A 1 163 ? 30.457  -8.038  29.681 1.00 41.04  ? 1380 HIS A CD2   1 
ATOM   1250 C  CE1   . HIS A 1 163 ? 32.016  -7.476  28.249 1.00 43.06  ? 1380 HIS A CE1   1 
ATOM   1251 N  NE2   . HIS A 1 163 ? 30.723  -7.715  28.374 1.00 42.99  ? 1380 HIS A NE2   1 
ATOM   1252 N  N     . THR A 1 164 ? 33.623  -10.166 33.975 1.00 51.87  ? 1381 THR A N     1 
ATOM   1253 C  CA    . THR A 1 164 ? 33.939  -10.621 35.322 1.00 47.05  ? 1381 THR A CA    1 
ATOM   1254 C  C     . THR A 1 164 ? 35.238  -9.994  35.807 1.00 47.55  ? 1381 THR A C     1 
ATOM   1255 O  O     . THR A 1 164 ? 36.170  -9.762  35.029 1.00 56.68  ? 1381 THR A O     1 
ATOM   1256 C  CB    . THR A 1 164 ? 34.052  -12.151 35.385 1.00 43.06  ? 1381 THR A CB    1 
ATOM   1257 O  OG1   . THR A 1 164 ? 34.989  -12.591 34.402 1.00 41.53  ? 1381 THR A OG1   1 
ATOM   1258 C  CG2   . THR A 1 164 ? 32.720  -12.807 35.108 1.00 47.54  ? 1381 THR A CG2   1 
ATOM   1259 N  N     . ALA A 1 165 ? 35.276  -9.736  37.116 1.00 36.66  ? 1382 ALA A N     1 
ATOM   1260 C  CA    . ALA A 1 165 ? 36.404  -9.103  37.792 1.00 42.10  ? 1382 ALA A CA    1 
ATOM   1261 C  C     . ALA A 1 165 ? 36.675  -9.791  39.121 1.00 38.13  ? 1382 ALA A C     1 
ATOM   1262 O  O     . ALA A 1 165 ? 35.754  -9.990  39.926 1.00 33.22  ? 1382 ALA A O     1 
ATOM   1263 C  CB    . ALA A 1 165 ? 36.145  -7.609  38.030 1.00 50.93  ? 1382 ALA A CB    1 
ATOM   1264 N  N     . PHE A 1 166 ? 37.960  -10.072 39.356 1.00 41.32  ? 1383 PHE A N     1 
ATOM   1265 C  CA    . PHE A 1 166 ? 38.451  -10.973 40.383 1.00 50.01  ? 1383 PHE A CA    1 
ATOM   1266 C  C     . PHE A 1 166 ? 39.683  -10.372 41.035 1.00 56.96  ? 1383 PHE A C     1 
ATOM   1267 O  O     . PHE A 1 166 ? 40.541  -9.800  40.352 1.00 47.05  ? 1383 PHE A O     1 
ATOM   1268 C  CB    . PHE A 1 166 ? 38.865  -12.339 39.800 1.00 48.11  ? 1383 PHE A CB    1 
ATOM   1269 C  CG    . PHE A 1 166 ? 37.742  -13.132 39.193 1.00 42.51  ? 1383 PHE A CG    1 
ATOM   1270 C  CD1   . PHE A 1 166 ? 37.601  -13.204 37.812 1.00 34.95  ? 1383 PHE A CD1   1 
ATOM   1271 C  CD2   . PHE A 1 166 ? 36.862  -13.840 39.994 1.00 46.98  ? 1383 PHE A CD2   1 
ATOM   1272 C  CE1   . PHE A 1 166 ? 36.592  -13.937 37.232 1.00 37.18  ? 1383 PHE A CE1   1 
ATOM   1273 C  CE2   . PHE A 1 166 ? 35.841  -14.577 39.430 1.00 54.67  ? 1383 PHE A CE2   1 
ATOM   1274 C  CZ    . PHE A 1 166 ? 35.704  -14.628 38.038 1.00 52.02  ? 1383 PHE A CZ    1 
ATOM   1275 N  N     . ALA A 1 167 ? 39.820  -10.626 42.343 1.00 60.66  ? 1384 ALA A N     1 
ATOM   1276 C  CA    . ALA A 1 167 ? 41.015  -10.207 43.075 1.00 45.00  ? 1384 ALA A CA    1 
ATOM   1277 C  C     . ALA A 1 167 ? 42.260  -10.904 42.548 1.00 42.25  ? 1384 ALA A C     1 
ATOM   1278 O  O     . ALA A 1 167 ? 43.245  -10.249 42.217 1.00 43.87  ? 1384 ALA A O     1 
ATOM   1279 C  CB    . ALA A 1 167 ? 40.860  -10.474 44.568 1.00 37.98  ? 1384 ALA A CB    1 
ATOM   1280 N  N     . THR A 1 168 ? 42.239  -12.228 42.449 1.00 51.67  ? 1385 THR A N     1 
ATOM   1281 C  CA    . THR A 1 168 ? 43.428  -12.953 42.028 1.00 64.29  ? 1385 THR A CA    1 
ATOM   1282 C  C     . THR A 1 168 ? 43.322  -13.458 40.597 1.00 69.38  ? 1385 THR A C     1 
ATOM   1283 O  O     . THR A 1 168 ? 42.239  -13.755 40.088 1.00 68.43  ? 1385 THR A O     1 
ATOM   1284 C  CB    . THR A 1 168 ? 43.687  -14.157 42.937 1.00 66.99  ? 1385 THR A CB    1 
ATOM   1285 O  OG1   . THR A 1 168 ? 42.682  -15.156 42.711 1.00 68.29  ? 1385 THR A OG1   1 
ATOM   1286 C  CG2   . THR A 1 168 ? 43.655  -13.742 44.377 1.00 67.71  ? 1385 THR A CG2   1 
ATOM   1287 N  N     . GLN A 1 169 ? 44.487  -13.583 39.964 1.00 71.01  ? 1386 GLN A N     1 
ATOM   1288 C  CA    . GLN A 1 169 ? 44.556  -14.025 38.578 1.00 69.09  ? 1386 GLN A CA    1 
ATOM   1289 C  C     . GLN A 1 169 ? 44.120  -15.481 38.425 1.00 67.06  ? 1386 GLN A C     1 
ATOM   1290 O  O     . GLN A 1 169 ? 43.609  -15.868 37.361 1.00 67.61  ? 1386 GLN A O     1 
ATOM   1291 C  CB    . GLN A 1 169 ? 45.982  -13.820 38.070 1.00 71.29  ? 1386 GLN A CB    1 
ATOM   1292 C  CG    . GLN A 1 169 ? 46.254  -14.313 36.678 1.00 73.31  ? 1386 GLN A CG    1 
ATOM   1293 C  CD    . GLN A 1 169 ? 47.411  -13.574 36.045 1.00 80.56  ? 1386 GLN A CD    1 
ATOM   1294 O  OE1   . GLN A 1 169 ? 47.319  -13.118 34.902 1.00 82.07  ? 1386 GLN A OE1   1 
ATOM   1295 N  NE2   . GLN A 1 169 ? 48.509  -13.440 36.789 1.00 81.23  ? 1386 GLN A NE2   1 
ATOM   1296 N  N     . LYS A 1 170 ? 44.312  -16.297 39.470 1.00 59.99  ? 1387 LYS A N     1 
ATOM   1297 C  CA    . LYS A 1 170 ? 43.923  -17.702 39.397 1.00 54.29  ? 1387 LYS A CA    1 
ATOM   1298 C  C     . LYS A 1 170 ? 42.433  -17.844 39.097 1.00 59.47  ? 1387 LYS A C     1 
ATOM   1299 O  O     . LYS A 1 170 ? 42.051  -18.522 38.131 1.00 61.81  ? 1387 LYS A O     1 
ATOM   1300 C  CB    . LYS A 1 170 ? 44.295  -18.424 40.699 1.00 41.60  ? 1387 LYS A CB    1 
ATOM   1301 N  N     . GLU A 1 171 ? 41.584  -17.176 39.899 1.00 56.16  ? 1388 GLU A N     1 
ATOM   1302 C  CA    . GLU A 1 171 ? 40.136  -17.232 39.702 1.00 55.47  ? 1388 GLU A CA    1 
ATOM   1303 C  C     . GLU A 1 171 ? 39.767  -16.921 38.265 1.00 54.70  ? 1388 GLU A C     1 
ATOM   1304 O  O     . GLU A 1 171 ? 38.902  -17.585 37.672 1.00 57.65  ? 1388 GLU A O     1 
ATOM   1305 C  CB    . GLU A 1 171 ? 39.429  -16.251 40.638 1.00 55.14  ? 1388 GLU A CB    1 
ATOM   1306 C  CG    . GLU A 1 171 ? 39.874  -16.308 42.080 1.00 60.53  ? 1388 GLU A CG    1 
ATOM   1307 C  CD    . GLU A 1 171 ? 39.408  -15.099 42.884 1.00 72.78  ? 1388 GLU A CD    1 
ATOM   1308 O  OE1   . GLU A 1 171 ? 38.179  -14.953 43.096 1.00 76.18  ? 1388 GLU A OE1   1 
ATOM   1309 O  OE2   . GLU A 1 171 ? 40.272  -14.295 43.309 1.00 72.33  ? 1388 GLU A OE2   1 
ATOM   1310 N  N     . ALA A 1 172 ? 40.431  -15.920 37.689 1.00 46.37  ? 1389 ALA A N     1 
ATOM   1311 C  CA    . ALA A 1 172 ? 40.139  -15.513 36.326 1.00 59.07  ? 1389 ALA A CA    1 
ATOM   1312 C  C     . ALA A 1 172 ? 40.493  -16.612 35.336 1.00 66.77  ? 1389 ALA A C     1 
ATOM   1313 O  O     . ALA A 1 172 ? 39.674  -16.960 34.475 1.00 70.05  ? 1389 ALA A O     1 
ATOM   1314 C  CB    . ALA A 1 172 ? 40.891  -14.225 36.000 1.00 66.76  ? 1389 ALA A CB    1 
ATOM   1315 N  N     . ASP A 1 173 ? 41.710  -17.172 35.446 1.00 60.60  ? 1390 ASP A N     1 
ATOM   1316 C  CA    . ASP A 1 173 ? 42.117  -18.255 34.548 1.00 50.40  ? 1390 ASP A CA    1 
ATOM   1317 C  C     . ASP A 1 173 ? 41.115  -19.405 34.598 1.00 49.43  ? 1390 ASP A C     1 
ATOM   1318 O  O     . ASP A 1 173 ? 40.742  -19.996 33.557 1.00 44.43  ? 1390 ASP A O     1 
ATOM   1319 C  CB    . ASP A 1 173 ? 43.509  -18.757 34.938 1.00 52.29  ? 1390 ASP A CB    1 
ATOM   1320 C  CG    . ASP A 1 173 ? 44.607  -17.722 34.722 1.00 57.26  ? 1390 ASP A CG    1 
ATOM   1321 O  OD1   . ASP A 1 173 ? 44.597  -17.032 33.675 1.00 51.12  ? 1390 ASP A OD1   1 
ATOM   1322 O  OD2   . ASP A 1 173 ? 45.493  -17.611 35.604 1.00 62.33  ? 1390 ASP A OD2   1 
ATOM   1323 N  N     . GLU A 1 174 ? 40.654  -19.721 35.813 1.00 40.88  ? 1391 GLU A N     1 
ATOM   1324 C  CA    . GLU A 1 174 ? 39.752  -20.851 35.981 1.00 46.14  ? 1391 GLU A CA    1 
ATOM   1325 C  C     . GLU A 1 174 ? 38.408  -20.589 35.334 1.00 47.79  ? 1391 GLU A C     1 
ATOM   1326 O  O     . GLU A 1 174 ? 37.860  -21.459 34.646 1.00 50.11  ? 1391 GLU A O     1 
ATOM   1327 C  CB    . GLU A 1 174 ? 39.593  -21.179 37.456 1.00 38.28  ? 1391 GLU A CB    1 
ATOM   1328 C  CG    . GLU A 1 174 ? 40.877  -21.726 38.017 1.00 47.67  ? 1391 GLU A CG    1 
ATOM   1329 C  CD    . GLU A 1 174 ? 40.856  -21.729 39.497 1.00 62.10  ? 1391 GLU A CD    1 
ATOM   1330 O  OE1   . GLU A 1 174 ? 39.738  -21.590 40.050 1.00 60.06  ? 1391 GLU A OE1   1 
ATOM   1331 O  OE2   . GLU A 1 174 ? 41.950  -21.830 40.092 1.00 70.28  ? 1391 GLU A OE2   1 
ATOM   1332 N  N     . GLU A 1 175 ? 37.869  -19.397 35.524 1.00 46.01  ? 1392 GLU A N     1 
ATOM   1333 C  CA    . GLU A 1 175 ? 36.575  -19.148 34.922 1.00 46.93  ? 1392 GLU A CA    1 
ATOM   1334 C  C     . GLU A 1 175 ? 36.686  -19.134 33.415 1.00 48.57  ? 1392 GLU A C     1 
ATOM   1335 O  O     . GLU A 1 175 ? 35.779  -19.609 32.724 1.00 53.27  ? 1392 GLU A O     1 
ATOM   1336 C  CB    . GLU A 1 175 ? 35.995  -17.844 35.421 1.00 42.85  ? 1392 GLU A CB    1 
ATOM   1337 C  CG    . GLU A 1 175 ? 34.668  -17.575 34.828 1.00 39.15  ? 1392 GLU A CG    1 
ATOM   1338 C  CD    . GLU A 1 175 ? 34.332  -16.147 34.941 1.00 49.88  ? 1392 GLU A CD    1 
ATOM   1339 O  OE1   . GLU A 1 175 ? 33.652  -15.798 35.925 1.00 61.67  ? 1392 GLU A OE1   1 
ATOM   1340 O  OE2   . GLU A 1 175 ? 34.768  -15.377 34.065 1.00 40.74  ? 1392 GLU A OE2   1 
ATOM   1341 N  N     . VAL A 1 176 ? 37.787  -18.582 32.894 1.00 44.40  ? 1393 VAL A N     1 
ATOM   1342 C  CA    . VAL A 1 176 ? 38.019  -18.613 31.451 1.00 40.40  ? 1393 VAL A CA    1 
ATOM   1343 C  C     . VAL A 1 176 ? 37.829  -20.030 30.929 1.00 47.87  ? 1393 VAL A C     1 
ATOM   1344 O  O     . VAL A 1 176 ? 37.045  -20.271 29.991 1.00 45.24  ? 1393 VAL A O     1 
ATOM   1345 C  CB    . VAL A 1 176 ? 39.430  -18.095 31.115 1.00 34.25  ? 1393 VAL A CB    1 
ATOM   1346 C  CG1   . VAL A 1 176 ? 39.629  -18.115 29.633 1.00 37.23  ? 1393 VAL A CG1   1 
ATOM   1347 C  CG2   . VAL A 1 176 ? 39.647  -16.738 31.635 1.00 34.12  ? 1393 VAL A CG2   1 
ATOM   1348 N  N     . LEU A 1 177 ? 38.521  -21.002 31.564 1.00 45.40  ? 1394 LEU A N     1 
ATOM   1349 C  CA    . LEU A 1 177 ? 38.474  -22.375 31.043 1.00 46.10  ? 1394 LEU A CA    1 
ATOM   1350 C  C     . LEU A 1 177 ? 37.118  -23.047 31.298 1.00 54.72  ? 1394 LEU A C     1 
ATOM   1351 O  O     . LEU A 1 177 ? 36.601  -23.768 30.433 1.00 53.77  ? 1394 LEU A O     1 
ATOM   1352 C  CB    . LEU A 1 177 ? 39.616  -23.203 31.627 1.00 39.58  ? 1394 LEU A CB    1 
ATOM   1353 C  CG    . LEU A 1 177 ? 41.048  -22.977 31.112 1.00 42.32  ? 1394 LEU A CG    1 
ATOM   1354 C  CD1   . LEU A 1 177 ? 42.007  -23.981 31.719 1.00 37.86  ? 1394 LEU A CD1   1 
ATOM   1355 C  CD2   . LEU A 1 177 ? 41.178  -22.989 29.581 1.00 36.70  ? 1394 LEU A CD2   1 
ATOM   1356 N  N     . THR A 1 178 ? 36.514  -22.799 32.462 1.00 50.17  ? 1395 THR A N     1 
ATOM   1357 C  CA    . THR A 1 178 ? 35.180  -23.316 32.759 1.00 44.28  ? 1395 THR A CA    1 
ATOM   1358 C  C     . THR A 1 178 ? 34.168  -22.876 31.706 1.00 54.98  ? 1395 THR A C     1 
ATOM   1359 O  O     . THR A 1 178 ? 33.420  -23.697 31.146 1.00 57.08  ? 1395 THR A O     1 
ATOM   1360 C  CB    . THR A 1 178 ? 34.754  -22.803 34.134 1.00 38.51  ? 1395 THR A CB    1 
ATOM   1361 O  OG1   . THR A 1 178 ? 35.546  -23.431 35.141 1.00 47.97  ? 1395 THR A OG1   1 
ATOM   1362 C  CG2   . THR A 1 178 ? 33.295  -23.057 34.395 1.00 33.49  ? 1395 THR A CG2   1 
ATOM   1363 N  N     . ILE A 1 179 ? 34.122  -21.562 31.449 1.00 48.85  ? 1396 ILE A N     1 
ATOM   1364 C  CA    . ILE A 1 179 ? 33.222  -20.995 30.455 1.00 34.42  ? 1396 ILE A CA    1 
ATOM   1365 C  C     . ILE A 1 179 ? 33.491  -21.601 29.091 1.00 38.26  ? 1396 ILE A C     1 
ATOM   1366 O  O     . ILE A 1 179 ? 32.554  -21.977 28.371 1.00 32.37  ? 1396 ILE A O     1 
ATOM   1367 C  CB    . ILE A 1 179 ? 33.376  -19.461 30.444 1.00 38.01  ? 1396 ILE A CB    1 
ATOM   1368 C  CG1   . ILE A 1 179 ? 32.854  -18.913 31.747 1.00 36.24  ? 1396 ILE A CG1   1 
ATOM   1369 C  CG2   . ILE A 1 179 ? 32.629  -18.812 29.269 1.00 30.90  ? 1396 ILE A CG2   1 
ATOM   1370 C  CD1   . ILE A 1 179 ? 31.381  -19.087 31.828 1.00 35.05  ? 1396 ILE A CD1   1 
ATOM   1371 N  N     . LEU A 1 180 ? 34.776  -21.744 28.728 1.00 36.79  ? 1397 LEU A N     1 
ATOM   1372 C  CA    . LEU A 1 180 ? 35.096  -22.318 27.422 1.00 44.09  ? 1397 LEU A CA    1 
ATOM   1373 C  C     . LEU A 1 180 ? 34.559  -23.750 27.308 1.00 48.80  ? 1397 LEU A C     1 
ATOM   1374 O  O     . LEU A 1 180 ? 34.084  -24.175 26.240 1.00 43.70  ? 1397 LEU A O     1 
ATOM   1375 C  CB    . LEU A 1 180 ? 36.612  -22.265 27.190 1.00 37.41  ? 1397 LEU A CB    1 
ATOM   1376 C  CG    . LEU A 1 180 ? 37.048  -22.588 25.755 1.00 45.09  ? 1397 LEU A CG    1 
ATOM   1377 C  CD1   . LEU A 1 180 ? 36.703  -21.478 24.756 1.00 46.40  ? 1397 LEU A CD1   1 
ATOM   1378 C  CD2   . LEU A 1 180 ? 38.520  -22.930 25.690 1.00 41.07  ? 1397 LEU A CD2   1 
ATOM   1379 N  N     . ASP A 1 181 ? 34.638  -24.507 28.404 1.00 45.48  ? 1398 ASP A N     1 
ATOM   1380 C  CA    . ASP A 1 181 ? 34.074  -25.846 28.424 1.00 53.05  ? 1398 ASP A CA    1 
ATOM   1381 C  C     . ASP A 1 181 ? 32.560  -25.824 28.233 1.00 58.27  ? 1398 ASP A C     1 
ATOM   1382 O  O     . ASP A 1 181 ? 32.007  -26.676 27.524 1.00 51.98  ? 1398 ASP A O     1 
ATOM   1383 C  CB    . ASP A 1 181 ? 34.452  -26.533 29.729 1.00 61.70  ? 1398 ASP A CB    1 
ATOM   1384 C  CG    . ASP A 1 181 ? 33.879  -27.913 29.830 1.00 65.90  ? 1398 ASP A CG    1 
ATOM   1385 O  OD1   . ASP A 1 181 ? 33.196  -28.178 30.840 1.00 67.46  ? 1398 ASP A OD1   1 
ATOM   1386 O  OD2   . ASP A 1 181 ? 34.086  -28.714 28.889 1.00 65.16  ? 1398 ASP A OD2   1 
ATOM   1387 N  N     . LEU A 1 182 ? 31.872  -24.862 28.867 1.00 60.20  ? 1399 LEU A N     1 
ATOM   1388 C  CA    . LEU A 1 182 ? 30.423  -24.704 28.661 1.00 61.85  ? 1399 LEU A CA    1 
ATOM   1389 C  C     . LEU A 1 182 ? 30.068  -24.378 27.199 1.00 61.56  ? 1399 LEU A C     1 
ATOM   1390 O  O     . LEU A 1 182 ? 29.048  -24.844 26.678 1.00 58.91  ? 1399 LEU A O     1 
ATOM   1391 C  CB    . LEU A 1 182 ? 29.874  -23.627 29.588 1.00 61.15  ? 1399 LEU A CB    1 
ATOM   1392 C  CG    . LEU A 1 182 ? 29.736  -23.967 31.064 1.00 56.61  ? 1399 LEU A CG    1 
ATOM   1393 C  CD1   . LEU A 1 182 ? 29.220  -22.750 31.809 1.00 56.90  ? 1399 LEU A CD1   1 
ATOM   1394 C  CD2   . LEU A 1 182 ? 28.779  -25.104 31.224 1.00 50.16  ? 1399 LEU A CD2   1 
ATOM   1395 N  N     . TYR A 1 183 ? 30.844  -23.503 26.554 1.00 50.00  ? 1400 TYR A N     1 
ATOM   1396 C  CA    . TYR A 1 183 ? 30.646  -23.233 25.130 1.00 37.74  ? 1400 TYR A CA    1 
ATOM   1397 C  C     . TYR A 1 183 ? 30.764  -24.514 24.311 1.00 42.21  ? 1400 TYR A C     1 
ATOM   1398 O  O     . TYR A 1 183 ? 29.867  -24.868 23.520 1.00 37.37  ? 1400 TYR A O     1 
ATOM   1399 C  CB    . TYR A 1 183 ? 31.675  -22.200 24.647 1.00 36.12  ? 1400 TYR A CB    1 
ATOM   1400 C  CG    . TYR A 1 183 ? 31.395  -20.773 25.109 1.00 48.51  ? 1400 TYR A CG    1 
ATOM   1401 C  CD1   . TYR A 1 183 ? 30.105  -20.382 25.440 1.00 43.79  ? 1400 TYR A CD1   1 
ATOM   1402 C  CD2   . TYR A 1 183 ? 32.419  -19.823 25.216 1.00 41.67  ? 1400 TYR A CD2   1 
ATOM   1403 C  CE1   . TYR A 1 183 ? 29.831  -19.116 25.854 1.00 41.25  ? 1400 TYR A CE1   1 
ATOM   1404 C  CE2   . TYR A 1 183 ? 32.150  -18.546 25.641 1.00 38.05  ? 1400 TYR A CE2   1 
ATOM   1405 C  CZ    . TYR A 1 183 ? 30.839  -18.195 25.961 1.00 44.11  ? 1400 TYR A CZ    1 
ATOM   1406 O  OH    . TYR A 1 183 ? 30.482  -16.924 26.378 1.00 48.39  ? 1400 TYR A OH    1 
ATOM   1407 N  N     . ALA A 1 184 ? 31.881  -25.228 24.495 1.00 53.14  ? 1401 ALA A N     1 
ATOM   1408 C  CA    . ALA A 1 184 ? 32.091  -26.486 23.784 1.00 44.87  ? 1401 ALA A CA    1 
ATOM   1409 C  C     . ALA A 1 184 ? 30.975  -27.480 24.068 1.00 43.47  ? 1401 ALA A C     1 
ATOM   1410 O  O     . ALA A 1 184 ? 30.597  -28.254 23.186 1.00 34.12  ? 1401 ALA A O     1 
ATOM   1411 C  CB    . ALA A 1 184 ? 33.452  -27.065 24.148 1.00 38.60  ? 1401 ALA A CB    1 
ATOM   1412 N  N     . LYS A 1 185 ? 30.418  -27.465 25.278 1.00 40.02  ? 1402 LYS A N     1 
ATOM   1413 C  CA    . LYS A 1 185 ? 29.301  -28.356 25.573 1.00 38.54  ? 1402 LYS A CA    1 
ATOM   1414 C  C     . LYS A 1 185 ? 28.051  -27.946 24.810 1.00 43.32  ? 1402 LYS A C     1 
ATOM   1415 O  O     . LYS A 1 185 ? 27.321  -28.794 24.305 1.00 57.49  ? 1402 LYS A O     1 
ATOM   1416 C  CB    . LYS A 1 185 ? 29.001  -28.349 27.064 1.00 33.58  ? 1402 LYS A CB    1 
ATOM   1417 C  CG    . LYS A 1 185 ? 29.901  -29.243 27.841 1.00 53.74  ? 1402 LYS A CG    1 
ATOM   1418 C  CD    . LYS A 1 185 ? 29.467  -29.330 29.275 1.00 53.65  ? 1402 LYS A CD    1 
ATOM   1419 C  CE    . LYS A 1 185 ? 29.897  -30.634 29.854 1.00 59.84  ? 1402 LYS A CE    1 
ATOM   1420 N  NZ    . LYS A 1 185 ? 30.988  -30.419 30.830 1.00 74.74  ? 1402 LYS A NZ    1 
ATOM   1421 N  N     . VAL A 1 186 ? 27.783  -26.653 24.699 1.00 38.41  ? 1403 VAL A N     1 
ATOM   1422 C  CA    . VAL A 1 186 ? 26.675  -26.229 23.859 1.00 43.83  ? 1403 VAL A CA    1 
ATOM   1423 C  C     . VAL A 1 186 ? 26.839  -26.825 22.479 1.00 51.43  ? 1403 VAL A C     1 
ATOM   1424 O  O     . VAL A 1 186 ? 25.874  -27.245 21.841 1.00 50.08  ? 1403 VAL A O     1 
ATOM   1425 C  CB    . VAL A 1 186 ? 26.604  -24.693 23.797 1.00 52.43  ? 1403 VAL A CB    1 
ATOM   1426 C  CG1   . VAL A 1 186 ? 25.864  -24.248 22.559 1.00 48.28  ? 1403 VAL A CG1   1 
ATOM   1427 C  CG2   . VAL A 1 186 ? 25.963  -24.128 25.034 1.00 56.51  ? 1403 VAL A CG2   1 
ATOM   1428 N  N     . TYR A 1 187 ? 28.071  -26.870 22.014 1.00 62.47  ? 1404 TYR A N     1 
ATOM   1429 C  CA    . TYR A 1 187 ? 28.270  -27.369 20.659 1.00 64.99  ? 1404 TYR A CA    1 
ATOM   1430 C  C     . TYR A 1 187 ? 28.147  -28.890 20.565 1.00 62.69  ? 1404 TYR A C     1 
ATOM   1431 O  O     . TYR A 1 187 ? 27.481  -29.392 19.652 1.00 60.16  ? 1404 TYR A O     1 
ATOM   1432 C  CB    . TYR A 1 187 ? 29.609  -26.876 20.118 1.00 63.17  ? 1404 TYR A CB    1 
ATOM   1433 C  CG    . TYR A 1 187 ? 29.438  -25.514 19.492 1.00 50.86  ? 1404 TYR A CG    1 
ATOM   1434 C  CD1   . TYR A 1 187 ? 29.658  -24.352 20.229 1.00 51.24  ? 1404 TYR A CD1   1 
ATOM   1435 C  CD2   . TYR A 1 187 ? 29.016  -25.393 18.172 1.00 39.85  ? 1404 TYR A CD2   1 
ATOM   1436 C  CE1   . TYR A 1 187 ? 29.490  -23.106 19.654 1.00 53.18  ? 1404 TYR A CE1   1 
ATOM   1437 C  CE2   . TYR A 1 187 ? 28.844  -24.156 17.588 1.00 34.80  ? 1404 TYR A CE2   1 
ATOM   1438 C  CZ    . TYR A 1 187 ? 29.079  -23.017 18.333 1.00 47.75  ? 1404 TYR A CZ    1 
ATOM   1439 O  OH    . TYR A 1 187 ? 28.902  -21.792 17.751 1.00 52.13  ? 1404 TYR A OH    1 
ATOM   1440 N  N     . THR A 1 188 ? 28.732  -29.642 21.506 1.00 63.47  ? 1405 THR A N     1 
ATOM   1441 C  CA    . THR A 1 188 ? 28.779  -31.106 21.366 1.00 53.33  ? 1405 THR A CA    1 
ATOM   1442 C  C     . THR A 1 188 ? 27.603  -31.830 22.007 1.00 39.12  ? 1405 THR A C     1 
ATOM   1443 O  O     . THR A 1 188 ? 27.191  -32.858 21.481 1.00 49.98  ? 1405 THR A O     1 
ATOM   1444 C  CB    . THR A 1 188 ? 30.085  -31.697 21.924 1.00 51.57  ? 1405 THR A CB    1 
ATOM   1445 O  OG1   . THR A 1 188 ? 30.203  -31.479 23.338 1.00 35.95  ? 1405 THR A OG1   1 
ATOM   1446 C  CG2   . THR A 1 188 ? 31.280  -31.098 21.223 1.00 62.49  ? 1405 THR A CG2   1 
ATOM   1447 N  N     . ASP A 1 189 ? 27.058  -31.329 23.121 1.00 41.76  ? 1406 ASP A N     1 
ATOM   1448 C  CA    . ASP A 1 189 ? 25.911  -31.893 23.838 1.00 46.66  ? 1406 ASP A CA    1 
ATOM   1449 C  C     . ASP A 1 189 ? 24.568  -31.343 23.371 1.00 51.80  ? 1406 ASP A C     1 
ATOM   1450 O  O     . ASP A 1 189 ? 23.551  -32.036 23.477 1.00 54.78  ? 1406 ASP A O     1 
ATOM   1451 C  CB    . ASP A 1 189 ? 25.978  -31.573 25.336 1.00 41.51  ? 1406 ASP A CB    1 
ATOM   1452 C  CG    . ASP A 1 189 ? 27.253  -32.001 25.966 1.00 56.95  ? 1406 ASP A CG    1 
ATOM   1453 O  OD1   . ASP A 1 189 ? 28.096  -32.568 25.250 1.00 55.90  ? 1406 ASP A OD1   1 
ATOM   1454 O  OD2   . ASP A 1 189 ? 27.404  -31.780 27.187 1.00 73.47  ? 1406 ASP A OD2   1 
ATOM   1455 N  N     . LEU A 1 190 ? 24.527  -30.096 22.909 1.00 51.31  ? 1407 LEU A N     1 
ATOM   1456 C  CA    . LEU A 1 190 ? 23.298  -29.505 22.406 1.00 47.80  ? 1407 LEU A CA    1 
ATOM   1457 C  C     . LEU A 1 190 ? 23.204  -29.579 20.888 1.00 49.22  ? 1407 LEU A C     1 
ATOM   1458 O  O     . LEU A 1 190 ? 22.182  -30.010 20.358 1.00 43.50  ? 1407 LEU A O     1 
ATOM   1459 C  CB    . LEU A 1 190 ? 23.169  -28.052 22.902 1.00 38.61  ? 1407 LEU A CB    1 
ATOM   1460 C  CG    . LEU A 1 190 ? 22.772  -27.947 24.385 1.00 37.64  ? 1407 LEU A CG    1 
ATOM   1461 C  CD1   . LEU A 1 190 ? 22.668  -26.526 24.919 1.00 38.51  ? 1407 LEU A CD1   1 
ATOM   1462 C  CD2   . LEU A 1 190 ? 21.447  -28.654 24.587 1.00 35.37  ? 1407 LEU A CD2   1 
ATOM   1463 N  N     . LEU A 1 191 ? 24.246  -29.176 20.169 1.00 60.61  ? 1408 LEU A N     1 
ATOM   1464 C  CA    . LEU A 1 191 ? 24.132  -29.084 18.721 1.00 56.77  ? 1408 LEU A CA    1 
ATOM   1465 C  C     . LEU A 1 191 ? 24.755  -30.256 17.994 1.00 50.09  ? 1408 LEU A C     1 
ATOM   1466 O  O     . LEU A 1 191 ? 24.579  -30.355 16.776 1.00 42.41  ? 1408 LEU A O     1 
ATOM   1467 C  CB    . LEU A 1 191 ? 24.771  -27.782 18.206 1.00 55.25  ? 1408 LEU A CB    1 
ATOM   1468 C  CG    . LEU A 1 191 ? 24.219  -26.505 18.828 1.00 51.33  ? 1408 LEU A CG    1 
ATOM   1469 C  CD1   . LEU A 1 191 ? 24.562  -25.312 17.953 1.00 55.39  ? 1408 LEU A CD1   1 
ATOM   1470 C  CD2   . LEU A 1 191 ? 22.703  -26.595 19.098 1.00 36.96  ? 1408 LEU A CD2   1 
ATOM   1471 N  N     . ALA A 1 192 ? 25.419  -31.166 18.712 1.00 50.75  ? 1409 ALA A N     1 
ATOM   1472 C  CA    . ALA A 1 192 ? 26.021  -32.353 18.113 1.00 42.73  ? 1409 ALA A CA    1 
ATOM   1473 C  C     . ALA A 1 192 ? 27.045  -31.987 17.038 1.00 53.26  ? 1409 ALA A C     1 
ATOM   1474 O  O     . ALA A 1 192 ? 27.081  -32.584 15.966 1.00 55.37  ? 1409 ALA A O     1 
ATOM   1475 C  CB    . ALA A 1 192 ? 24.942  -33.275 17.551 1.00 36.50  ? 1409 ALA A CB    1 
ATOM   1476 N  N     . ILE A 1 193 ? 27.890  -31.002 17.328 1.00 63.80  ? 1410 ILE A N     1 
ATOM   1477 C  CA    . ILE A 1 193 ? 28.973  -30.581 16.444 1.00 71.68  ? 1410 ILE A CA    1 
ATOM   1478 C  C     . ILE A 1 193 ? 30.288  -30.797 17.183 1.00 70.24  ? 1410 ILE A C     1 
ATOM   1479 O  O     . ILE A 1 193 ? 30.415  -30.368 18.331 1.00 75.49  ? 1410 ILE A O     1 
ATOM   1480 C  CB    . ILE A 1 193 ? 28.847  -29.107 16.015 1.00 75.28  ? 1410 ILE A CB    1 
ATOM   1481 C  CG1   . ILE A 1 193 ? 27.406  -28.756 15.643 1.00 78.63  ? 1410 ILE A CG1   1 
ATOM   1482 C  CG2   . ILE A 1 193 ? 29.743  -28.820 14.833 1.00 75.58  ? 1410 ILE A CG2   1 
ATOM   1483 C  CD1   . ILE A 1 193 ? 27.158  -27.252 15.431 1.00 70.26  ? 1410 ILE A CD1   1 
ATOM   1484 N  N     . PRO A 1 194 ? 31.306  -31.406 16.564 1.00 54.44  ? 1411 PRO A N     1 
ATOM   1485 C  CA    . PRO A 1 194 ? 32.614  -31.515 17.224 1.00 55.51  ? 1411 PRO A CA    1 
ATOM   1486 C  C     . PRO A 1 194 ? 33.423  -30.233 17.083 1.00 51.26  ? 1411 PRO A C     1 
ATOM   1487 O  O     . PRO A 1 194 ? 33.472  -29.621 16.011 1.00 49.15  ? 1411 PRO A O     1 
ATOM   1488 C  CB    . PRO A 1 194 ? 33.283  -32.672 16.473 1.00 47.16  ? 1411 PRO A CB    1 
ATOM   1489 C  CG    . PRO A 1 194 ? 32.760  -32.533 15.093 1.00 48.71  ? 1411 PRO A CG    1 
ATOM   1490 C  CD    . PRO A 1 194 ? 31.309  -32.074 15.253 1.00 51.30  ? 1411 PRO A CD    1 
ATOM   1491 N  N     . VAL A 1 195 ? 34.105  -29.851 18.167 1.00 37.16  ? 1412 VAL A N     1 
ATOM   1492 C  CA    . VAL A 1 195 ? 34.791  -28.565 18.214 1.00 42.41  ? 1412 VAL A CA    1 
ATOM   1493 C  C     . VAL A 1 195 ? 36.176  -28.715 18.811 1.00 40.76  ? 1412 VAL A C     1 
ATOM   1494 O  O     . VAL A 1 195 ? 36.377  -29.443 19.784 1.00 54.87  ? 1412 VAL A O     1 
ATOM   1495 C  CB    . VAL A 1 195 ? 34.012  -27.514 19.035 1.00 45.03  ? 1412 VAL A CB    1 
ATOM   1496 C  CG1   . VAL A 1 195 ? 32.765  -26.977 18.256 1.00 37.99  ? 1412 VAL A CG1   1 
ATOM   1497 C  CG2   . VAL A 1 195 ? 33.681  -28.061 20.435 1.00 35.53  ? 1412 VAL A CG2   1 
ATOM   1498 N  N     . VAL A 1 196 ? 37.105  -27.919 18.298 1.00 39.44  ? 1413 VAL A N     1 
ATOM   1499 C  CA    . VAL A 1 196 ? 38.493  -27.924 18.746 1.00 49.20  ? 1413 VAL A CA    1 
ATOM   1500 C  C     . VAL A 1 196 ? 38.675  -26.785 19.737 1.00 50.91  ? 1413 VAL A C     1 
ATOM   1501 O  O     . VAL A 1 196 ? 38.494  -25.615 19.377 1.00 55.14  ? 1413 VAL A O     1 
ATOM   1502 C  CB    . VAL A 1 196 ? 39.464  -27.763 17.567 1.00 38.84  ? 1413 VAL A CB    1 
ATOM   1503 C  CG1   . VAL A 1 196 ? 40.883  -27.956 18.019 1.00 39.66  ? 1413 VAL A CG1   1 
ATOM   1504 C  CG2   . VAL A 1 196 ? 39.111  -28.687 16.457 1.00 39.42  ? 1413 VAL A CG2   1 
ATOM   1505 N  N     . LYS A 1 197 ? 39.029  -27.128 20.980 1.00 47.91  ? 1414 LYS A N     1 
ATOM   1506 C  CA    . LYS A 1 197 ? 39.387  -26.131 21.979 1.00 52.83  ? 1414 LYS A CA    1 
ATOM   1507 C  C     . LYS A 1 197 ? 40.801  -25.641 21.715 1.00 59.94  ? 1414 LYS A C     1 
ATOM   1508 O  O     . LYS A 1 197 ? 41.699  -26.433 21.399 1.00 62.05  ? 1414 LYS A O     1 
ATOM   1509 C  CB    . LYS A 1 197 ? 39.310  -26.706 23.392 1.00 52.08  ? 1414 LYS A CB    1 
ATOM   1510 C  CG    . LYS A 1 197 ? 37.914  -26.858 23.966 1.00 56.25  ? 1414 LYS A CG    1 
ATOM   1511 C  CD    . LYS A 1 197 ? 37.977  -27.671 25.252 1.00 59.96  ? 1414 LYS A CD    1 
ATOM   1512 C  CE    . LYS A 1 197 ? 36.657  -27.705 25.987 1.00 61.97  ? 1414 LYS A CE    1 
ATOM   1513 N  NZ    . LYS A 1 197 ? 36.830  -27.851 27.464 1.00 62.07  ? 1414 LYS A NZ    1 
ATOM   1514 N  N     . GLY A 1 198 ? 40.995  -24.326 21.825 1.00 58.28  ? 1415 GLY A N     1 
ATOM   1515 C  CA    . GLY A 1 198 ? 42.342  -23.830 21.627 1.00 61.55  ? 1415 GLY A CA    1 
ATOM   1516 C  C     . GLY A 1 198 ? 42.566  -22.431 22.155 1.00 57.22  ? 1415 GLY A C     1 
ATOM   1517 O  O     . GLY A 1 198 ? 41.653  -21.766 22.640 1.00 53.92  ? 1415 GLY A O     1 
ATOM   1518 N  N     . ARG A 1 199 ? 43.817  -22.000 22.051 1.00 59.71  ? 1416 ARG A N     1 
ATOM   1519 C  CA    . ARG A 1 199 ? 44.236  -20.629 22.296 1.00 55.68  ? 1416 ARG A CA    1 
ATOM   1520 C  C     . ARG A 1 199 ? 44.404  -19.887 20.979 1.00 54.64  ? 1416 ARG A C     1 
ATOM   1521 O  O     . ARG A 1 199 ? 44.934  -20.430 20.005 1.00 53.13  ? 1416 ARG A O     1 
ATOM   1522 C  CB    . ARG A 1 199 ? 45.555  -20.610 23.065 1.00 55.76  ? 1416 ARG A CB    1 
ATOM   1523 C  CG    . ARG A 1 199 ? 46.002  -19.246 23.501 1.00 56.52  ? 1416 ARG A CG    1 
ATOM   1524 C  CD    . ARG A 1 199 ? 47.344  -19.333 24.173 1.00 51.80  ? 1416 ARG A CD    1 
ATOM   1525 N  NE    . ARG A 1 199 ? 47.936  -18.011 24.318 1.00 56.34  ? 1416 ARG A NE    1 
ATOM   1526 C  CZ    . ARG A 1 199 ? 48.307  -17.472 25.476 1.00 53.77  ? 1416 ARG A CZ    1 
ATOM   1527 N  NH1   . ARG A 1 199 ? 48.160  -18.142 26.611 1.00 41.48  ? 1416 ARG A NH1   1 
ATOM   1528 N  NH2   . ARG A 1 199 ? 48.823  -16.251 25.492 1.00 62.35  ? 1416 ARG A NH2   1 
ATOM   1529 N  N     . LYS A 1 200 ? 43.990  -18.633 20.957 1.00 57.48  ? 1417 LYS A N     1 
ATOM   1530 C  CA    . LYS A 1 200 ? 44.176  -17.859 19.744 1.00 62.64  ? 1417 LYS A CA    1 
ATOM   1531 C  C     . LYS A 1 200 ? 45.599  -17.315 19.693 1.00 64.16  ? 1417 LYS A C     1 
ATOM   1532 O  O     . LYS A 1 200 ? 46.196  -16.981 20.723 1.00 69.35  ? 1417 LYS A O     1 
ATOM   1533 C  CB    . LYS A 1 200 ? 43.139  -16.730 19.673 1.00 56.78  ? 1417 LYS A CB    1 
ATOM   1534 C  CG    . LYS A 1 200 ? 41.727  -17.204 19.276 1.00 50.56  ? 1417 LYS A CG    1 
ATOM   1535 C  CD    . LYS A 1 200 ? 41.649  -17.321 17.750 1.00 55.71  ? 1417 LYS A CD    1 
ATOM   1536 C  CE    . LYS A 1 200 ? 40.238  -17.566 17.227 1.00 52.38  ? 1417 LYS A CE    1 
ATOM   1537 N  NZ    . LYS A 1 200 ? 40.045  -17.189 15.773 1.00 49.57  ? 1417 LYS A NZ    1 
ATOM   1538 N  N     . THR A 1 201 ? 46.145  -17.235 18.480 1.00 58.41  ? 1418 THR A N     1 
ATOM   1539 C  CA    . THR A 1 201 ? 47.479  -16.682 18.310 1.00 65.49  ? 1418 THR A CA    1 
ATOM   1540 C  C     . THR A 1 201 ? 47.498  -15.217 18.744 1.00 68.56  ? 1418 THR A C     1 
ATOM   1541 O  O     . THR A 1 201 ? 46.462  -14.586 18.982 1.00 69.81  ? 1418 THR A O     1 
ATOM   1542 C  CB    . THR A 1 201 ? 47.943  -16.799 16.856 1.00 71.74  ? 1418 THR A CB    1 
ATOM   1543 O  OG1   . THR A 1 201 ? 46.962  -16.214 15.985 1.00 76.77  ? 1418 THR A OG1   1 
ATOM   1544 C  CG2   . THR A 1 201 ? 48.173  -18.254 16.463 1.00 66.13  ? 1418 THR A CG2   1 
ATOM   1545 N  N     . GLU A 1 202 ? 48.707  -14.673 18.857 1.00 66.85  ? 1419 GLU A N     1 
ATOM   1546 C  CA    . GLU A 1 202 ? 48.811  -13.255 19.157 1.00 66.64  ? 1419 GLU A CA    1 
ATOM   1547 C  C     . GLU A 1 202 ? 48.103  -12.412 18.104 1.00 68.66  ? 1419 GLU A C     1 
ATOM   1548 O  O     . GLU A 1 202 ? 47.498  -11.383 18.437 1.00 76.36  ? 1419 GLU A O     1 
ATOM   1549 C  CB    . GLU A 1 202 ? 50.282  -12.861 19.275 1.00 65.72  ? 1419 GLU A CB    1 
ATOM   1550 C  CG    . GLU A 1 202 ? 50.961  -13.448 20.490 1.00 68.74  ? 1419 GLU A CG    1 
ATOM   1551 C  CD    . GLU A 1 202 ? 50.135  -13.280 21.746 1.00 75.34  ? 1419 GLU A CD    1 
ATOM   1552 O  OE1   . GLU A 1 202 ? 49.380  -14.212 22.108 1.00 81.14  ? 1419 GLU A OE1   1 
ATOM   1553 O  OE2   . GLU A 1 202 ? 50.245  -12.211 22.374 1.00 76.13  ? 1419 GLU A OE2   1 
ATOM   1554 N  N     . LYS A 1 203 ? 48.093  -12.872 16.850 1.00 63.54  ? 1420 LYS A N     1 
ATOM   1555 C  CA    . LYS A 1 203 ? 47.446  -12.108 15.788 1.00 59.02  ? 1420 LYS A CA    1 
ATOM   1556 C  C     . LYS A 1 203 ? 45.932  -12.164 15.895 1.00 56.92  ? 1420 LYS A C     1 
ATOM   1557 O  O     . LYS A 1 203 ? 45.254  -11.156 15.670 1.00 66.67  ? 1420 LYS A O     1 
ATOM   1558 C  CB    . LYS A 1 203 ? 47.880  -12.611 14.407 1.00 55.29  ? 1420 LYS A CB    1 
ATOM   1559 C  CG    . LYS A 1 203 ? 46.968  -12.084 13.323 1.00 57.19  ? 1420 LYS A CG    1 
ATOM   1560 C  CD    . LYS A 1 203 ? 47.540  -12.211 11.947 1.00 58.41  ? 1420 LYS A CD    1 
ATOM   1561 C  CE    . LYS A 1 203 ? 46.541  -11.623 10.963 1.00 61.99  ? 1420 LYS A CE    1 
ATOM   1562 N  NZ    . LYS A 1 203 ? 46.940  -11.737 9.530  1.00 68.53  ? 1420 LYS A NZ    1 
ATOM   1563 N  N     . GLU A 1 204 ? 45.383  -13.303 16.283 1.00 56.31  ? 1421 GLU A N     1 
ATOM   1564 C  CA    . GLU A 1 204 ? 43.946  -13.464 16.227 1.00 57.76  ? 1421 GLU A CA    1 
ATOM   1565 C  C     . GLU A 1 204 ? 43.276  -13.333 17.578 1.00 49.20  ? 1421 GLU A C     1 
ATOM   1566 O  O     . GLU A 1 204 ? 42.043  -13.341 17.636 1.00 55.01  ? 1421 GLU A O     1 
ATOM   1567 C  CB    . GLU A 1 204 ? 43.600  -14.814 15.592 1.00 69.52  ? 1421 GLU A CB    1 
ATOM   1568 C  CG    . GLU A 1 204 ? 44.327  -15.049 14.285 1.00 73.38  ? 1421 GLU A CG    1 
ATOM   1569 C  CD    . GLU A 1 204 ? 43.514  -14.581 13.103 1.00 75.85  ? 1421 GLU A CD    1 
ATOM   1570 O  OE1   . GLU A 1 204 ? 44.043  -14.617 11.972 1.00 79.20  ? 1421 GLU A OE1   1 
ATOM   1571 O  OE2   . GLU A 1 204 ? 42.348  -14.169 13.314 1.00 71.89  ? 1421 GLU A OE2   1 
ATOM   1572 N  N     . LYS A 1 205 ? 44.042  -13.163 18.650 1.00 40.61  ? 1422 LYS A N     1 
ATOM   1573 C  CA    . LYS A 1 205 ? 43.425  -12.959 19.948 1.00 43.66  ? 1422 LYS A CA    1 
ATOM   1574 C  C     . LYS A 1 205 ? 42.727  -11.590 19.995 1.00 52.45  ? 1422 LYS A C     1 
ATOM   1575 O  O     . LYS A 1 205 ? 42.928  -10.726 19.137 1.00 66.71  ? 1422 LYS A O     1 
ATOM   1576 C  CB    . LYS A 1 205 ? 44.469  -13.108 21.047 1.00 44.74  ? 1422 LYS A CB    1 
ATOM   1577 C  CG    . LYS A 1 205 ? 45.437  -11.952 21.182 1.00 52.38  ? 1422 LYS A CG    1 
ATOM   1578 C  CD    . LYS A 1 205 ? 46.199  -12.066 22.501 1.00 61.41  ? 1422 LYS A CD    1 
ATOM   1579 C  CE    . LYS A 1 205 ? 47.377  -11.103 22.557 1.00 61.70  ? 1422 LYS A CE    1 
ATOM   1580 N  NZ    . LYS A 1 205 ? 47.487  -10.382 23.859 1.00 58.52  ? 1422 LYS A NZ    1 
ATOM   1581 N  N     . PHE A 1 206 ? 41.890  -11.393 21.014 1.00 45.57  ? 1423 PHE A N     1 
ATOM   1582 C  CA    . PHE A 1 206 ? 41.204  -10.114 21.179 1.00 39.56  ? 1423 PHE A CA    1 
ATOM   1583 C  C     . PHE A 1 206 ? 42.212  -9.077  21.661 1.00 50.22  ? 1423 PHE A C     1 
ATOM   1584 O  O     . PHE A 1 206 ? 42.916  -9.304  22.651 1.00 64.16  ? 1423 PHE A O     1 
ATOM   1585 C  CB    . PHE A 1 206 ? 40.020  -10.284 22.156 1.00 33.74  ? 1423 PHE A CB    1 
ATOM   1586 C  CG    . PHE A 1 206 ? 39.436  -8.993  22.678 1.00 45.49  ? 1423 PHE A CG    1 
ATOM   1587 C  CD1   . PHE A 1 206 ? 39.181  -7.916  21.840 1.00 52.84  ? 1423 PHE A CD1   1 
ATOM   1588 C  CD2   . PHE A 1 206 ? 39.127  -8.858  24.018 1.00 46.19  ? 1423 PHE A CD2   1 
ATOM   1589 C  CE1   . PHE A 1 206 ? 38.637  -6.732  22.347 1.00 48.09  ? 1423 PHE A CE1   1 
ATOM   1590 C  CE2   . PHE A 1 206 ? 38.580  -7.658  24.521 1.00 41.52  ? 1423 PHE A CE2   1 
ATOM   1591 C  CZ    . PHE A 1 206 ? 38.338  -6.613  23.691 1.00 32.72  ? 1423 PHE A CZ    1 
ATOM   1592 N  N     . ALA A 1 207 ? 42.277  -7.936  20.956 1.00 52.09  ? 1424 ALA A N     1 
ATOM   1593 C  CA    . ALA A 1 207 ? 43.382  -6.983  21.130 1.00 41.81  ? 1424 ALA A CA    1 
ATOM   1594 C  C     . ALA A 1 207 ? 43.497  -6.509  22.567 1.00 41.98  ? 1424 ALA A C     1 
ATOM   1595 O  O     . ALA A 1 207 ? 44.599  -6.424  23.120 1.00 39.31  ? 1424 ALA A O     1 
ATOM   1596 C  CB    . ALA A 1 207 ? 43.205  -5.779  20.219 1.00 36.53  ? 1424 ALA A CB    1 
ATOM   1597 N  N     . GLY A 1 208 ? 42.382  -6.157  23.176 1.00 54.47  ? 1425 GLY A N     1 
ATOM   1598 C  CA    . GLY A 1 208 ? 42.546  -5.664  24.517 1.00 71.56  ? 1425 GLY A CA    1 
ATOM   1599 C  C     . GLY A 1 208 ? 42.824  -6.711  25.553 1.00 75.57  ? 1425 GLY A C     1 
ATOM   1600 O  O     . GLY A 1 208 ? 43.054  -6.373  26.714 1.00 72.11  ? 1425 GLY A O     1 
ATOM   1601 N  N     . GLY A 1 209 ? 42.860  -7.979  25.166 1.00 86.99  ? 1426 GLY A N     1 
ATOM   1602 C  CA    . GLY A 1 209 ? 43.025  -9.046  26.124 1.00 92.84  ? 1426 GLY A CA    1 
ATOM   1603 C  C     . GLY A 1 209 ? 44.470  -9.437  26.399 1.00 89.88  ? 1426 GLY A C     1 
ATOM   1604 O  O     . GLY A 1 209 ? 45.434  -8.867  25.885 1.00 92.93  ? 1426 GLY A O     1 
ATOM   1605 N  N     . ASP A 1 210 ? 44.590  -10.467 27.229 1.00 73.62  ? 1427 ASP A N     1 
ATOM   1606 C  CA    . ASP A 1 210 ? 45.868  -11.112 27.524 1.00 69.80  ? 1427 ASP A CA    1 
ATOM   1607 C  C     . ASP A 1 210 ? 46.010  -12.308 26.590 1.00 69.45  ? 1427 ASP A C     1 
ATOM   1608 O  O     . ASP A 1 210 ? 46.807  -12.291 25.646 1.00 75.57  ? 1427 ASP A O     1 
ATOM   1609 C  CB    . ASP A 1 210 ? 45.903  -11.536 28.992 1.00 72.15  ? 1427 ASP A CB    1 
ATOM   1610 C  CG    . ASP A 1 210 ? 47.247  -11.356 29.615 1.00 71.01  ? 1427 ASP A CG    1 
ATOM   1611 O  OD1   . ASP A 1 210 ? 47.791  -10.237 29.481 1.00 67.71  ? 1427 ASP A OD1   1 
ATOM   1612 O  OD2   . ASP A 1 210 ? 47.743  -12.331 30.233 1.00 70.25  ? 1427 ASP A OD2   1 
ATOM   1613 N  N     . TYR A 1 211 ? 45.234  -13.349 26.838 1.00 60.94  ? 1428 TYR A N     1 
ATOM   1614 C  CA    . TYR A 1 211 ? 45.094  -14.430 25.887 1.00 59.79  ? 1428 TYR A CA    1 
ATOM   1615 C  C     . TYR A 1 211 ? 43.617  -14.596 25.565 1.00 61.00  ? 1428 TYR A C     1 
ATOM   1616 O  O     . TYR A 1 211 ? 42.737  -14.119 26.294 1.00 35.33  ? 1428 TYR A O     1 
ATOM   1617 C  CB    . TYR A 1 211 ? 45.684  -15.730 26.438 1.00 52.53  ? 1428 TYR A CB    1 
ATOM   1618 C  CG    . TYR A 1 211 ? 45.075  -16.178 27.757 1.00 51.95  ? 1428 TYR A CG    1 
ATOM   1619 C  CD1   . TYR A 1 211 ? 43.838  -16.816 27.798 1.00 49.06  ? 1428 TYR A CD1   1 
ATOM   1620 C  CD2   . TYR A 1 211 ? 45.736  -15.977 28.959 1.00 49.38  ? 1428 TYR A CD2   1 
ATOM   1621 C  CE1   . TYR A 1 211 ? 43.273  -17.232 29.006 1.00 43.18  ? 1428 TYR A CE1   1 
ATOM   1622 C  CE2   . TYR A 1 211 ? 45.178  -16.399 30.176 1.00 47.39  ? 1428 TYR A CE2   1 
ATOM   1623 C  CZ    . TYR A 1 211 ? 43.949  -17.029 30.188 1.00 46.88  ? 1428 TYR A CZ    1 
ATOM   1624 O  OH    . TYR A 1 211 ? 43.380  -17.453 31.373 1.00 51.16  ? 1428 TYR A OH    1 
ATOM   1625 N  N     . THR A 1 212 ? 43.356  -15.335 24.493 1.00 64.72  ? 1429 THR A N     1 
ATOM   1626 C  CA    . THR A 1 212 ? 41.999  -15.594 24.048 1.00 67.38  ? 1429 THR A CA    1 
ATOM   1627 C  C     . THR A 1 212 ? 41.875  -17.078 23.791 1.00 59.70  ? 1429 THR A C     1 
ATOM   1628 O  O     . THR A 1 212 ? 42.648  -17.652 23.017 1.00 52.53  ? 1429 THR A O     1 
ATOM   1629 C  CB    . THR A 1 212 ? 41.655  -14.815 22.777 1.00 73.04  ? 1429 THR A CB    1 
ATOM   1630 O  OG1   . THR A 1 212 ? 41.407  -13.441 23.104 1.00 77.87  ? 1429 THR A OG1   1 
ATOM   1631 C  CG2   . THR A 1 212 ? 40.436  -15.406 22.097 1.00 72.25  ? 1429 THR A CG2   1 
ATOM   1632 N  N     . THR A 1 213 ? 40.910  -17.683 24.450 1.00 55.67  ? 1430 THR A N     1 
ATOM   1633 C  CA    . THR A 1 213 ? 40.504  -19.038 24.145 1.00 54.86  ? 1430 THR A CA    1 
ATOM   1634 C  C     . THR A 1 213 ? 39.448  -19.002 23.060 1.00 63.48  ? 1430 THR A C     1 
ATOM   1635 O  O     . THR A 1 213 ? 38.778  -17.996 22.858 1.00 76.02  ? 1430 THR A O     1 
ATOM   1636 C  CB    . THR A 1 213 ? 39.873  -19.699 25.343 1.00 46.55  ? 1430 THR A CB    1 
ATOM   1637 O  OG1   . THR A 1 213 ? 38.703  -18.952 25.668 1.00 60.53  ? 1430 THR A OG1   1 
ATOM   1638 C  CG2   . THR A 1 213 ? 40.864  -19.716 26.467 1.00 45.53  ? 1430 THR A CG2   1 
ATOM   1639 N  N     . THR A 1 214 ? 39.311  -20.135 22.384 1.00 57.21  ? 1431 THR A N     1 
ATOM   1640 C  CA    . THR A 1 214 ? 38.257  -20.307 21.393 1.00 49.31  ? 1431 THR A CA    1 
ATOM   1641 C  C     . THR A 1 214 ? 37.873  -21.777 21.260 1.00 51.50  ? 1431 THR A C     1 
ATOM   1642 O  O     . THR A 1 214 ? 38.513  -22.690 21.802 1.00 55.72  ? 1431 THR A O     1 
ATOM   1643 C  CB    . THR A 1 214 ? 38.658  -19.742 20.022 1.00 51.84  ? 1431 THR A CB    1 
ATOM   1644 O  OG1   . THR A 1 214 ? 37.579  -19.902 19.107 1.00 63.07  ? 1431 THR A OG1   1 
ATOM   1645 C  CG2   . THR A 1 214 ? 39.884  -20.437 19.450 1.00 38.36  ? 1431 THR A CG2   1 
ATOM   1646 N  N     . VAL A 1 215 ? 36.761  -21.964 20.561 1.00 50.82  ? 1432 VAL A N     1 
ATOM   1647 C  CA    . VAL A 1 215 ? 36.183  -23.253 20.228 1.00 34.47  ? 1432 VAL A CA    1 
ATOM   1648 C  C     . VAL A 1 215 ? 35.855  -23.173 18.737 1.00 45.59  ? 1432 VAL A C     1 
ATOM   1649 O  O     . VAL A 1 215 ? 34.890  -22.501 18.339 1.00 45.69  ? 1432 VAL A O     1 
ATOM   1650 C  CB    . VAL A 1 215 ? 34.959  -23.550 21.084 1.00 33.86  ? 1432 VAL A CB    1 
ATOM   1651 C  CG1   . VAL A 1 215 ? 34.020  -24.448 20.399 1.00 48.80  ? 1432 VAL A CG1   1 
ATOM   1652 C  CG2   . VAL A 1 215 ? 35.407  -24.144 22.409 1.00 37.37  ? 1432 VAL A CG2   1 
ATOM   1653 N  N     . GLU A 1 216 ? 36.690  -23.800 17.903 1.00 46.01  ? 1433 GLU A N     1 
ATOM   1654 C  CA    . GLU A 1 216 ? 36.543  -23.728 16.455 1.00 48.05  ? 1433 GLU A CA    1 
ATOM   1655 C  C     . GLU A 1 216 ? 35.803  -24.958 15.942 1.00 50.41  ? 1433 GLU A C     1 
ATOM   1656 O  O     . GLU A 1 216 ? 35.845  -26.024 16.555 1.00 45.13  ? 1433 GLU A O     1 
ATOM   1657 C  CB    . GLU A 1 216 ? 37.897  -23.615 15.751 1.00 57.98  ? 1433 GLU A CB    1 
ATOM   1658 C  CG    . GLU A 1 216 ? 38.831  -22.554 16.308 1.00 75.04  ? 1433 GLU A CG    1 
ATOM   1659 C  CD    . GLU A 1 216 ? 38.372  -21.119 16.031 1.00 84.90  ? 1433 GLU A CD    1 
ATOM   1660 O  OE1   . GLU A 1 216 ? 37.831  -20.485 16.961 1.00 89.25  ? 1433 GLU A OE1   1 
ATOM   1661 O  OE2   . GLU A 1 216 ? 38.564  -20.617 14.901 1.00 85.36  ? 1433 GLU A OE2   1 
ATOM   1662 N  N     . ALA A 1 217 ? 35.078  -24.783 14.837 1.00 54.25  ? 1434 ALA A N     1 
ATOM   1663 C  CA    . ALA A 1 217 ? 34.353  -25.874 14.200 1.00 43.96  ? 1434 ALA A CA    1 
ATOM   1664 C  C     . ALA A 1 217 ? 34.565  -25.791 12.695 1.00 44.00  ? 1434 ALA A C     1 
ATOM   1665 O  O     . ALA A 1 217 ? 34.909  -24.742 12.160 1.00 48.13  ? 1434 ALA A O     1 
ATOM   1666 C  CB    . ALA A 1 217 ? 32.863  -25.821 14.551 1.00 37.75  ? 1434 ALA A CB    1 
ATOM   1667 N  N     . TYR A 1 218 ? 34.365  -26.897 11.999 1.00 50.68  ? 1435 TYR A N     1 
ATOM   1668 C  CA    . TYR A 1 218 ? 34.715  -26.956 10.586 1.00 60.96  ? 1435 TYR A CA    1 
ATOM   1669 C  C     . TYR A 1 218 ? 33.502  -27.317 9.749  1.00 53.47  ? 1435 TYR A C     1 
ATOM   1670 O  O     . TYR A 1 218 ? 32.787  -28.266 10.071 1.00 62.91  ? 1435 TYR A O     1 
ATOM   1671 C  CB    . TYR A 1 218 ? 35.821  -27.976 10.336 1.00 70.43  ? 1435 TYR A CB    1 
ATOM   1672 C  CG    . TYR A 1 218 ? 36.324  -27.958 8.921  1.00 77.38  ? 1435 TYR A CG    1 
ATOM   1673 C  CD1   . TYR A 1 218 ? 36.895  -26.812 8.388  1.00 86.97  ? 1435 TYR A CD1   1 
ATOM   1674 C  CD2   . TYR A 1 218 ? 36.238  -29.080 8.119  1.00 83.61  ? 1435 TYR A CD2   1 
ATOM   1675 C  CE1   . TYR A 1 218 ? 37.356  -26.775 7.092  1.00 93.17  ? 1435 TYR A CE1   1 
ATOM   1676 C  CE2   . TYR A 1 218 ? 36.708  -29.062 6.816  1.00 96.38  ? 1435 TYR A CE2   1 
ATOM   1677 C  CZ    . TYR A 1 218 ? 37.272  -27.903 6.309  1.00 103.79 ? 1435 TYR A CZ    1 
ATOM   1678 O  OH    . TYR A 1 218 ? 37.752  -27.868 5.017  1.00 109.94 ? 1435 TYR A OH    1 
ATOM   1679 N  N     . ILE A 1 219 ? 33.250  -26.554 8.698  1.00 48.24  ? 1436 ILE A N     1 
ATOM   1680 C  CA    . ILE A 1 219 ? 32.202  -26.884 7.741  1.00 70.86  ? 1436 ILE A CA    1 
ATOM   1681 C  C     . ILE A 1 219 ? 32.874  -27.307 6.435  1.00 73.79  ? 1436 ILE A C     1 
ATOM   1682 O  O     . ILE A 1 219 ? 33.529  -26.509 5.745  1.00 70.96  ? 1436 ILE A O     1 
ATOM   1683 C  CB    . ILE A 1 219 ? 31.194  -25.734 7.564  1.00 81.00  ? 1436 ILE A CB    1 
ATOM   1684 C  CG1   . ILE A 1 219 ? 31.718  -24.618 6.672  1.00 85.89  ? 1436 ILE A CG1   1 
ATOM   1685 C  CG2   . ILE A 1 219 ? 30.814  -25.132 8.927  1.00 75.81  ? 1436 ILE A CG2   1 
ATOM   1686 C  CD1   . ILE A 1 219 ? 30.666  -23.718 6.226  1.00 87.50  ? 1436 ILE A CD1   1 
ATOM   1687 N  N     . SER A 1 220 ? 32.728  -28.585 6.103  1.00 67.14  ? 1437 SER A N     1 
ATOM   1688 C  CA    . SER A 1 220 ? 33.389  -29.117 4.920  1.00 51.78  ? 1437 SER A CA    1 
ATOM   1689 C  C     . SER A 1 220 ? 32.754  -28.625 3.625  1.00 49.89  ? 1437 SER A C     1 
ATOM   1690 O  O     . SER A 1 220 ? 33.455  -28.481 2.618  1.00 57.26  ? 1437 SER A O     1 
ATOM   1691 C  CB    . SER A 1 220 ? 33.393  -30.635 4.983  1.00 51.59  ? 1437 SER A CB    1 
ATOM   1692 O  OG    . SER A 1 220 ? 32.200  -31.098 5.566  1.00 53.49  ? 1437 SER A OG    1 
ATOM   1693 N  N     . ALA A 1 221 ? 31.441  -28.389 3.616  1.00 47.18  ? 1438 ALA A N     1 
ATOM   1694 C  CA    . ALA A 1 221 ? 30.779  -27.898 2.411  1.00 53.02  ? 1438 ALA A CA    1 
ATOM   1695 C  C     . ALA A 1 221 ? 31.547  -26.732 1.795  1.00 57.07  ? 1438 ALA A C     1 
ATOM   1696 O  O     . ALA A 1 221 ? 32.000  -26.799 0.645  1.00 59.68  ? 1438 ALA A O     1 
ATOM   1697 C  CB    . ALA A 1 221 ? 29.338  -27.497 2.747  1.00 51.25  ? 1438 ALA A CB    1 
ATOM   1698 N  N     . SER A 1 222 ? 31.708  -25.652 2.560  1.00 51.74  ? 1439 SER A N     1 
ATOM   1699 C  CA    . SER A 1 222 ? 32.532  -24.525 2.153  1.00 54.51  ? 1439 SER A CA    1 
ATOM   1700 C  C     . SER A 1 222 ? 34.015  -24.770 2.400  1.00 63.94  ? 1439 SER A C     1 
ATOM   1701 O  O     . SER A 1 222 ? 34.837  -23.928 2.017  1.00 61.83  ? 1439 SER A O     1 
ATOM   1702 C  CB    . SER A 1 222 ? 32.083  -23.260 2.850  1.00 59.32  ? 1439 SER A CB    1 
ATOM   1703 O  OG    . SER A 1 222 ? 32.830  -23.103 4.029  1.00 70.42  ? 1439 SER A OG    1 
ATOM   1704 N  N     . GLY A 1 223 ? 34.368  -25.872 3.067  1.00 70.07  ? 1440 GLY A N     1 
ATOM   1705 C  CA    . GLY A 1 223 ? 35.754  -26.158 3.389  1.00 66.01  ? 1440 GLY A CA    1 
ATOM   1706 C  C     . GLY A 1 223 ? 36.403  -25.192 4.348  1.00 72.54  ? 1440 GLY A C     1 
ATOM   1707 O  O     . GLY A 1 223 ? 37.622  -25.033 4.313  1.00 77.90  ? 1440 GLY A O     1 
ATOM   1708 N  N     . ARG A 1 224 ? 35.627  -24.555 5.222  1.00 70.55  ? 1441 ARG A N     1 
ATOM   1709 C  CA    . ARG A 1 224 ? 36.107  -23.438 6.026  1.00 60.37  ? 1441 ARG A CA    1 
ATOM   1710 C  C     . ARG A 1 224 ? 35.818  -23.683 7.498  1.00 48.75  ? 1441 ARG A C     1 
ATOM   1711 O  O     . ARG A 1 224 ? 34.862  -24.366 7.855  1.00 44.05  ? 1441 ARG A O     1 
ATOM   1712 C  CB    . ARG A 1 224 ? 35.446  -22.100 5.609  1.00 57.51  ? 1441 ARG A CB    1 
ATOM   1713 C  CG    . ARG A 1 224 ? 35.813  -21.626 4.218  1.00 71.31  ? 1441 ARG A CG    1 
ATOM   1714 C  CD    . ARG A 1 224 ? 35.328  -20.200 3.959  1.00 75.47  ? 1441 ARG A CD    1 
ATOM   1715 N  NE    . ARG A 1 224 ? 36.287  -19.449 3.148  1.00 76.47  ? 1441 ARG A NE    1 
ATOM   1716 C  CZ    . ARG A 1 224 ? 36.221  -19.347 1.828  1.00 74.69  ? 1441 ARG A CZ    1 
ATOM   1717 N  NH1   . ARG A 1 224 ? 35.230  -19.946 1.162  1.00 75.74  ? 1441 ARG A NH1   1 
ATOM   1718 N  NH2   . ARG A 1 224 ? 37.148  -18.650 1.181  1.00 62.53  ? 1441 ARG A NH2   1 
ATOM   1719 N  N     . ALA A 1 225 ? 36.637  -23.102 8.358  1.00 48.67  ? 1442 ALA A N     1 
ATOM   1720 C  CA    . ALA A 1 225 ? 36.394  -23.191 9.785  1.00 47.27  ? 1442 ALA A CA    1 
ATOM   1721 C  C     . ALA A 1 225 ? 35.683  -21.926 10.249 1.00 64.24  ? 1442 ALA A C     1 
ATOM   1722 O  O     . ALA A 1 225 ? 35.596  -20.933 9.526  1.00 76.17  ? 1442 ALA A O     1 
ATOM   1723 C  CB    . ALA A 1 225 ? 37.706  -23.391 10.539 1.00 38.34  ? 1442 ALA A CB    1 
ATOM   1724 N  N     . ILE A 1 226 ? 35.135  -21.981 11.458 1.00 63.80  ? 1443 ILE A N     1 
ATOM   1725 C  CA    . ILE A 1 226 ? 34.414  -20.842 12.008 1.00 58.79  ? 1443 ILE A CA    1 
ATOM   1726 C  C     . ILE A 1 226 ? 34.551  -20.864 13.522 1.00 57.64  ? 1443 ILE A C     1 
ATOM   1727 O  O     . ILE A 1 226 ? 34.584  -21.928 14.153 1.00 57.71  ? 1443 ILE A O     1 
ATOM   1728 C  CB    . ILE A 1 226 ? 32.937  -20.832 11.571 1.00 57.93  ? 1443 ILE A CB    1 
ATOM   1729 C  CG1   . ILE A 1 226 ? 32.253  -19.549 12.079 1.00 60.70  ? 1443 ILE A CG1   1 
ATOM   1730 C  CG2   . ILE A 1 226 ? 32.249  -22.083 12.072 1.00 55.84  ? 1443 ILE A CG2   1 
ATOM   1731 C  CD1   . ILE A 1 226 ? 31.193  -18.971 11.156 1.00 56.66  ? 1443 ILE A CD1   1 
ATOM   1732 N  N     . GLN A 1 227 ? 34.678  -19.674 14.092 1.00 51.95  ? 1444 GLN A N     1 
ATOM   1733 C  CA    . GLN A 1 227 ? 34.749  -19.504 15.530 1.00 51.01  ? 1444 GLN A CA    1 
ATOM   1734 C  C     . GLN A 1 227 ? 33.353  -19.592 16.121 1.00 47.30  ? 1444 GLN A C     1 
ATOM   1735 O  O     . GLN A 1 227 ? 32.491  -18.792 15.768 1.00 45.17  ? 1444 GLN A O     1 
ATOM   1736 C  CB    . GLN A 1 227 ? 35.370  -18.151 15.812 1.00 59.39  ? 1444 GLN A CB    1 
ATOM   1737 C  CG    . GLN A 1 227 ? 35.779  -17.900 17.214 1.00 64.88  ? 1444 GLN A CG    1 
ATOM   1738 C  CD    . GLN A 1 227 ? 36.528  -16.602 17.297 1.00 71.55  ? 1444 GLN A CD    1 
ATOM   1739 O  OE1   . GLN A 1 227 ? 37.486  -16.471 18.065 1.00 89.34  ? 1444 GLN A OE1   1 
ATOM   1740 N  NE2   . GLN A 1 227 ? 36.083  -15.625 16.543 1.00 68.59  ? 1444 GLN A NE2   1 
ATOM   1741 N  N     . GLY A 1 228 ? 33.128  -20.535 17.034 1.00 51.60  ? 1445 GLY A N     1 
ATOM   1742 C  CA    . GLY A 1 228 ? 31.809  -20.739 17.598 1.00 40.20  ? 1445 GLY A CA    1 
ATOM   1743 C  C     . GLY A 1 228 ? 31.538  -19.929 18.850 1.00 40.54  ? 1445 GLY A C     1 
ATOM   1744 O  O     . GLY A 1 228 ? 30.376  -19.726 19.212 1.00 44.92  ? 1445 GLY A O     1 
ATOM   1745 N  N     . ALA A 1 229 ? 32.591  -19.500 19.546 1.00 34.63  ? 1446 ALA A N     1 
ATOM   1746 C  CA    . ALA A 1 229 ? 32.451  -18.681 20.748 1.00 35.72  ? 1446 ALA A CA    1 
ATOM   1747 C  C     . ALA A 1 229 ? 33.842  -18.223 21.149 1.00 37.91  ? 1446 ALA A C     1 
ATOM   1748 O  O     . ALA A 1 229 ? 34.842  -18.631 20.547 1.00 33.85  ? 1446 ALA A O     1 
ATOM   1749 C  CB    . ALA A 1 229 ? 31.774  -19.430 21.901 1.00 30.90  ? 1446 ALA A CB    1 
ATOM   1750 N  N     . THR A 1 230 ? 33.894  -17.330 22.140 1.00 35.72  ? 1447 THR A N     1 
ATOM   1751 C  CA    . THR A 1 230 ? 35.169  -16.886 22.697 1.00 53.10  ? 1447 THR A CA    1 
ATOM   1752 C  C     . THR A 1 230 ? 35.059  -16.672 24.194 1.00 55.79  ? 1447 THR A C     1 
ATOM   1753 O  O     . THR A 1 230 ? 34.026  -16.222 24.704 1.00 61.67  ? 1447 THR A O     1 
ATOM   1754 C  CB    . THR A 1 230 ? 35.703  -15.558 22.113 1.00 59.08  ? 1447 THR A CB    1 
ATOM   1755 O  OG1   . THR A 1 230 ? 34.627  -14.640 21.900 1.00 64.46  ? 1447 THR A OG1   1 
ATOM   1756 C  CG2   . THR A 1 230 ? 36.477  -15.775 20.847 1.00 64.30  ? 1447 THR A CG2   1 
ATOM   1757 N  N     . SER A 1 231 ? 36.174  -16.949 24.871 1.00 40.30  ? 1448 SER A N     1 
ATOM   1758 C  CA    . SER A 1 231 ? 36.374  -16.688 26.293 1.00 44.08  ? 1448 SER A CA    1 
ATOM   1759 C  C     . SER A 1 231 ? 37.747  -16.036 26.370 1.00 46.89  ? 1448 SER A C     1 
ATOM   1760 O  O     . SER A 1 231 ? 38.741  -16.653 25.980 1.00 41.35  ? 1448 SER A O     1 
ATOM   1761 C  CB    . SER A 1 231 ? 36.327  -17.969 27.136 1.00 34.04  ? 1448 SER A CB    1 
ATOM   1762 O  OG    . SER A 1 231 ? 36.029  -17.683 28.484 1.00 44.39  ? 1448 SER A OG    1 
ATOM   1763 N  N     . HIS A 1 232 ? 37.787  -14.766 26.760 1.00 46.60  ? 1449 HIS A N     1 
ATOM   1764 C  CA    . HIS A 1 232 ? 39.033  -14.030 26.846 1.00 44.82  ? 1449 HIS A CA    1 
ATOM   1765 C  C     . HIS A 1 232 ? 39.460  -13.902 28.299 1.00 48.04  ? 1449 HIS A C     1 
ATOM   1766 O  O     . HIS A 1 232 ? 38.627  -13.886 29.210 1.00 54.09  ? 1449 HIS A O     1 
ATOM   1767 C  CB    . HIS A 1 232 ? 38.904  -12.629 26.236 1.00 51.74  ? 1449 HIS A CB    1 
ATOM   1768 C  CG    . HIS A 1 232 ? 38.054  -12.566 25.006 1.00 60.31  ? 1449 HIS A CG    1 
ATOM   1769 N  ND1   . HIS A 1 232 ? 38.510  -12.935 23.759 1.00 66.92  ? 1449 HIS A ND1   1 
ATOM   1770 C  CD2   . HIS A 1 232 ? 36.789  -12.122 24.824 1.00 65.08  ? 1449 HIS A CD2   1 
ATOM   1771 C  CE1   . HIS A 1 232 ? 37.554  -12.747 22.866 1.00 67.63  ? 1449 HIS A CE1   1 
ATOM   1772 N  NE2   . HIS A 1 232 ? 36.498  -12.254 23.487 1.00 64.20  ? 1449 HIS A NE2   1 
ATOM   1773 N  N     . HIS A 1 233 ? 40.771  -13.810 28.516 1.00 46.23  ? 1450 HIS A N     1 
ATOM   1774 C  CA    . HIS A 1 233 ? 41.296  -13.322 29.788 1.00 49.32  ? 1450 HIS A CA    1 
ATOM   1775 C  C     . HIS A 1 233 ? 41.845  -11.925 29.564 1.00 58.95  ? 1450 HIS A C     1 
ATOM   1776 O  O     . HIS A 1 233 ? 42.865  -11.750 28.887 1.00 63.36  ? 1450 HIS A O     1 
ATOM   1777 C  CB    . HIS A 1 233 ? 42.388  -14.213 30.361 1.00 45.24  ? 1450 HIS A CB    1 
ATOM   1778 C  CG    . HIS A 1 233 ? 42.919  -13.716 31.666 1.00 42.65  ? 1450 HIS A CG    1 
ATOM   1779 N  ND1   . HIS A 1 233 ? 42.094  -13.362 32.714 1.00 45.69  ? 1450 HIS A ND1   1 
ATOM   1780 C  CD2   . HIS A 1 233 ? 44.182  -13.479 32.086 1.00 42.71  ? 1450 HIS A CD2   1 
ATOM   1781 C  CE1   . HIS A 1 233 ? 42.830  -12.942 33.729 1.00 41.35  ? 1450 HIS A CE1   1 
ATOM   1782 N  NE2   . HIS A 1 233 ? 44.101  -13.005 33.374 1.00 41.10  ? 1450 HIS A NE2   1 
ATOM   1783 N  N     . LEU A 1 234 ? 41.183  -10.937 30.144 1.00 58.14  ? 1451 LEU A N     1 
ATOM   1784 C  CA    . LEU A 1 234 ? 41.634  -9.571  29.962 1.00 57.24  ? 1451 LEU A CA    1 
ATOM   1785 C  C     . LEU A 1 234 ? 42.774  -9.228  30.902 1.00 56.23  ? 1451 LEU A C     1 
ATOM   1786 O  O     . LEU A 1 234 ? 43.468  -8.228  30.677 1.00 57.31  ? 1451 LEU A O     1 
ATOM   1787 C  CB    . LEU A 1 234 ? 40.458  -8.612  30.139 1.00 47.20  ? 1451 LEU A CB    1 
ATOM   1788 C  CG    . LEU A 1 234 ? 39.366  -9.067  29.175 1.00 46.72  ? 1451 LEU A CG    1 
ATOM   1789 C  CD1   . LEU A 1 234 ? 38.112  -8.225  29.306 1.00 32.30  ? 1451 LEU A CD1   1 
ATOM   1790 C  CD2   . LEU A 1 234 ? 39.899  -9.121  27.726 1.00 33.28  ? 1451 LEU A CD2   1 
ATOM   1791 N  N     . GLY A 1 235 ? 42.949  -10.000 31.969 1.00 38.23  ? 1452 GLY A N     1 
ATOM   1792 C  CA    . GLY A 1 235 ? 44.019  -9.661  32.882 1.00 38.83  ? 1452 GLY A CA    1 
ATOM   1793 C  C     . GLY A 1 235 ? 43.745  -8.317  33.516 1.00 47.46  ? 1452 GLY A C     1 
ATOM   1794 O  O     . GLY A 1 235 ? 42.639  -8.033  33.990 1.00 60.31  ? 1452 GLY A O     1 
ATOM   1795 N  N     . GLN A 1 236 ? 44.755  -7.462  33.513 1.00 43.46  ? 1453 GLN A N     1 
ATOM   1796 C  CA    . GLN A 1 236 ? 44.639  -6.130  34.090 1.00 48.42  ? 1453 GLN A CA    1 
ATOM   1797 C  C     . GLN A 1 236 ? 44.668  -5.007  33.064 1.00 54.65  ? 1453 GLN A C     1 
ATOM   1798 O  O     . GLN A 1 236 ? 44.783  -3.842  33.460 1.00 50.92  ? 1453 GLN A O     1 
ATOM   1799 C  CB    . GLN A 1 236 ? 45.762  -5.881  35.081 1.00 42.12  ? 1453 GLN A CB    1 
ATOM   1800 C  CG    . GLN A 1 236 ? 45.515  -6.310  36.468 1.00 38.28  ? 1453 GLN A CG    1 
ATOM   1801 C  CD    . GLN A 1 236 ? 46.775  -6.139  37.230 1.00 51.72  ? 1453 GLN A CD    1 
ATOM   1802 O  OE1   . GLN A 1 236 ? 47.850  -6.113  36.619 1.00 40.10  ? 1453 GLN A OE1   1 
ATOM   1803 N  NE2   . GLN A 1 236 ? 46.685  -6.045  38.559 1.00 56.79  ? 1453 GLN A NE2   1 
ATOM   1804 N  N     . ASN A 1 237 ? 44.531  -5.291  31.800 1.00 56.79  ? 1454 ASN A N     1 
ATOM   1805 C  CA    . ASN A 1 237 ? 44.578  -4.243  30.841 1.00 50.02  ? 1454 ASN A CA    1 
ATOM   1806 C  C     . ASN A 1 237 ? 43.426  -3.342  30.912 1.00 55.63  ? 1454 ASN A C     1 
ATOM   1807 O  O     . ASN A 1 237 ? 43.596  -2.196  30.787 1.00 61.43  ? 1454 ASN A O     1 
ATOM   1808 C  CB    . ASN A 1 237 ? 44.552  -4.798  29.472 1.00 48.49  ? 1454 ASN A CB    1 
ATOM   1809 C  CG    . ASN A 1 237 ? 45.531  -5.862  29.277 1.00 56.50  ? 1454 ASN A CG    1 
ATOM   1810 O  OD1   . ASN A 1 237 ? 46.694  -5.637  29.201 1.00 60.05  ? 1454 ASN A OD1   1 
ATOM   1811 N  ND2   . ASN A 1 237 ? 45.063  -7.014  29.140 1.00 57.86  ? 1454 ASN A ND2   1 
ATOM   1812 N  N     . PHE A 1 238 ? 42.228  -3.859  31.016 1.00 51.15  ? 1455 PHE A N     1 
ATOM   1813 C  CA    . PHE A 1 238 ? 41.046  -3.022  31.095 1.00 54.01  ? 1455 PHE A CA    1 
ATOM   1814 C  C     . PHE A 1 238 ? 40.884  -2.421  32.488 1.00 49.66  ? 1455 PHE A C     1 
ATOM   1815 O  O     . PHE A 1 238 ? 40.427  -1.282  32.625 1.00 48.79  ? 1455 PHE A O     1 
ATOM   1816 C  CB    . PHE A 1 238 ? 39.827  -3.828  30.661 1.00 55.78  ? 1455 PHE A CB    1 
ATOM   1817 C  CG    . PHE A 1 238 ? 39.668  -3.922  29.155 1.00 49.44  ? 1455 PHE A CG    1 
ATOM   1818 C  CD1   . PHE A 1 238 ? 40.248  -4.974  28.446 1.00 45.23  ? 1455 PHE A CD1   1 
ATOM   1819 C  CD2   . PHE A 1 238 ? 38.926  -2.975  28.455 1.00 35.17  ? 1455 PHE A CD2   1 
ATOM   1820 C  CE1   . PHE A 1 238 ? 40.094  -5.083  27.067 1.00 39.45  ? 1455 PHE A CE1   1 
ATOM   1821 C  CE2   . PHE A 1 238 ? 38.768  -3.073  27.090 1.00 33.29  ? 1455 PHE A CE2   1 
ATOM   1822 C  CZ    . PHE A 1 238 ? 39.361  -4.127  26.389 1.00 42.61  ? 1455 PHE A CZ    1 
ATOM   1823 N  N     . SER A 1 239 ? 41.243  -3.164  33.536 1.00 49.43  ? 1456 SER A N     1 
ATOM   1824 C  CA    . SER A 1 239 ? 41.185  -2.589  34.879 1.00 45.14  ? 1456 SER A CA    1 
ATOM   1825 C  C     . SER A 1 239 ? 42.093  -1.378  35.007 1.00 42.85  ? 1456 SER A C     1 
ATOM   1826 O  O     . SER A 1 239 ? 41.860  -0.513  35.854 1.00 37.19  ? 1456 SER A O     1 
ATOM   1827 C  CB    . SER A 1 239 ? 41.593  -3.623  35.921 1.00 48.14  ? 1456 SER A CB    1 
ATOM   1828 O  OG    . SER A 1 239 ? 42.916  -4.064  35.666 1.00 52.21  ? 1456 SER A OG    1 
ATOM   1829 N  N     . ARG A 1 240 ? 43.143  -1.318  34.194 1.00 40.33  ? 1457 ARG A N     1 
ATOM   1830 C  CA    . ARG A 1 240 ? 44.040  -0.177  34.181 1.00 47.53  ? 1457 ARG A CA    1 
ATOM   1831 C  C     . ARG A 1 240 ? 43.488  0.984   33.357 1.00 60.32  ? 1457 ARG A C     1 
ATOM   1832 O  O     . ARG A 1 240 ? 43.602  2.145   33.770 1.00 72.81  ? 1457 ARG A O     1 
ATOM   1833 C  CB    . ARG A 1 240 ? 45.411  -0.634  33.682 1.00 44.63  ? 1457 ARG A CB    1 
ATOM   1834 C  CG    . ARG A 1 240 ? 46.214  -1.307  34.781 1.00 47.35  ? 1457 ARG A CG    1 
ATOM   1835 C  CD    . ARG A 1 240 ? 47.704  -1.356  34.502 1.00 61.46  ? 1457 ARG A CD    1 
ATOM   1836 N  NE    . ARG A 1 240 ? 48.505  -1.461  35.734 1.00 73.32  ? 1457 ARG A NE    1 
ATOM   1837 C  CZ    . ARG A 1 240 ? 49.028  -2.591  36.204 1.00 73.58  ? 1457 ARG A CZ    1 
ATOM   1838 N  NH1   . ARG A 1 240 ? 48.834  -3.729  35.550 1.00 83.78  ? 1457 ARG A NH1   1 
ATOM   1839 N  NH2   . ARG A 1 240 ? 49.747  -2.589  37.323 1.00 64.91  ? 1457 ARG A NH2   1 
ATOM   1840 N  N     . MET A 1 241 ? 42.916  0.699   32.183 1.00 63.41  ? 1458 MET A N     1 
ATOM   1841 C  CA    . MET A 1 241 ? 42.307  1.759   31.378 1.00 55.29  ? 1458 MET A CA    1 
ATOM   1842 C  C     . MET A 1 241 ? 41.281  2.525   32.186 1.00 66.56  ? 1458 MET A C     1 
ATOM   1843 O  O     . MET A 1 241 ? 41.317  3.760   32.258 1.00 80.71  ? 1458 MET A O     1 
ATOM   1844 C  CB    . MET A 1 241 ? 41.630  1.177   30.144 1.00 54.00  ? 1458 MET A CB    1 
ATOM   1845 C  CG    . MET A 1 241 ? 42.563  0.907   29.009 1.00 72.01  ? 1458 MET A CG    1 
ATOM   1846 S  SD    . MET A 1 241 ? 41.702  0.369   27.530 1.00 80.18  ? 1458 MET A SD    1 
ATOM   1847 C  CE    . MET A 1 241 ? 41.085  1.924   26.888 1.00 83.11  ? 1458 MET A CE    1 
ATOM   1848 N  N     . PHE A 1 242 ? 40.369  1.802   32.822 1.00 57.27  ? 1459 PHE A N     1 
ATOM   1849 C  CA    . PHE A 1 242 ? 39.237  2.392   33.512 1.00 51.44  ? 1459 PHE A CA    1 
ATOM   1850 C  C     . PHE A 1 242 ? 39.464  2.475   35.005 1.00 59.43  ? 1459 PHE A C     1 
ATOM   1851 O  O     . PHE A 1 242 ? 38.547  2.855   35.742 1.00 68.33  ? 1459 PHE A O     1 
ATOM   1852 C  CB    . PHE A 1 242 ? 37.970  1.579   33.222 1.00 44.82  ? 1459 PHE A CB    1 
ATOM   1853 C  CG    . PHE A 1 242 ? 37.567  1.605   31.791 1.00 37.39  ? 1459 PHE A CG    1 
ATOM   1854 C  CD1   . PHE A 1 242 ? 36.592  2.483   31.349 1.00 33.73  ? 1459 PHE A CD1   1 
ATOM   1855 C  CD2   . PHE A 1 242 ? 38.196  0.784   30.880 1.00 34.04  ? 1459 PHE A CD2   1 
ATOM   1856 C  CE1   . PHE A 1 242 ? 36.230  2.520   30.043 1.00 40.93  ? 1459 PHE A CE1   1 
ATOM   1857 C  CE2   . PHE A 1 242 ? 37.844  0.810   29.563 1.00 42.27  ? 1459 PHE A CE2   1 
ATOM   1858 C  CZ    . PHE A 1 242 ? 36.855  1.677   29.138 1.00 49.44  ? 1459 PHE A CZ    1 
ATOM   1859 N  N     . ASP A 1 243 ? 40.665  2.132   35.458 1.00 62.15  ? 1460 ASP A N     1 
ATOM   1860 C  CA    . ASP A 1 243 ? 41.066  2.337   36.842 1.00 65.55  ? 1460 ASP A CA    1 
ATOM   1861 C  C     . ASP A 1 243 ? 40.096  1.618   37.777 1.00 58.69  ? 1460 ASP A C     1 
ATOM   1862 O  O     . ASP A 1 243 ? 39.581  2.176   38.749 1.00 61.23  ? 1460 ASP A O     1 
ATOM   1863 C  CB    . ASP A 1 243 ? 41.193  3.827   37.150 1.00 71.16  ? 1460 ASP A CB    1 
ATOM   1864 C  CG    . ASP A 1 243 ? 42.459  4.427   36.545 1.00 74.79  ? 1460 ASP A CG    1 
ATOM   1865 O  OD1   . ASP A 1 243 ? 42.361  5.272   35.625 1.00 75.73  ? 1460 ASP A OD1   1 
ATOM   1866 O  OD2   . ASP A 1 243 ? 43.561  4.044   36.993 1.00 76.64  ? 1460 ASP A OD2   1 
ATOM   1867 N  N     . ILE A 1 244 ? 39.852  0.351   37.450 1.00 48.25  ? 1461 ILE A N     1 
ATOM   1868 C  CA    . ILE A 1 244 ? 39.065  -0.551  38.279 1.00 48.21  ? 1461 ILE A CA    1 
ATOM   1869 C  C     . ILE A 1 244 ? 40.011  -1.097  39.339 1.00 54.28  ? 1461 ILE A C     1 
ATOM   1870 O  O     . ILE A 1 244 ? 40.795  -2.013  39.088 1.00 60.29  ? 1461 ILE A O     1 
ATOM   1871 C  CB    . ILE A 1 244 ? 38.415  -1.653  37.451 1.00 41.56  ? 1461 ILE A CB    1 
ATOM   1872 C  CG1   . ILE A 1 244 ? 37.939  -1.037  36.137 1.00 34.20  ? 1461 ILE A CG1   1 
ATOM   1873 C  CG2   . ILE A 1 244 ? 37.272  -2.283  38.241 1.00 36.36  ? 1461 ILE A CG2   1 
ATOM   1874 C  CD1   . ILE A 1 244 ? 37.379  -2.011  35.144 1.00 39.73  ? 1461 ILE A CD1   1 
ATOM   1875 N  N     . VAL A 1 245 ? 39.960  -0.494  40.525 1.00 56.88  ? 1462 VAL A N     1 
ATOM   1876 C  CA    . VAL A 1 245 ? 40.977  -0.665  41.547 1.00 49.63  ? 1462 VAL A CA    1 
ATOM   1877 C  C     . VAL A 1 245 ? 40.330  -0.944  42.903 1.00 42.15  ? 1462 VAL A C     1 
ATOM   1878 O  O     . VAL A 1 245 ? 39.145  -0.698  43.126 1.00 42.84  ? 1462 VAL A O     1 
ATOM   1879 C  CB    . VAL A 1 245 ? 41.880  0.581   41.627 1.00 40.57  ? 1462 VAL A CB    1 
ATOM   1880 C  CG1   . VAL A 1 245 ? 42.714  0.715   40.369 1.00 40.91  ? 1462 VAL A CG1   1 
ATOM   1881 C  CG2   . VAL A 1 245 ? 41.015  1.801   41.758 1.00 38.58  ? 1462 VAL A CG2   1 
ATOM   1882 N  N     . TYR A 1 246 ? 41.153  -1.432  43.825 1.00 38.62  ? 1463 TYR A N     1 
ATOM   1883 C  CA    . TYR A 1 246 ? 40.757  -1.631  45.212 1.00 49.78  ? 1463 TYR A CA    1 
ATOM   1884 C  C     . TYR A 1 246 ? 42.008  -1.496  46.059 1.00 50.24  ? 1463 TYR A C     1 
ATOM   1885 O  O     . TYR A 1 246 ? 43.134  -1.540  45.552 1.00 40.69  ? 1463 TYR A O     1 
ATOM   1886 C  CB    . TYR A 1 246 ? 40.093  -2.999  45.454 1.00 58.02  ? 1463 TYR A CB    1 
ATOM   1887 C  CG    . TYR A 1 246 ? 40.994  -4.169  45.085 1.00 66.54  ? 1463 TYR A CG    1 
ATOM   1888 C  CD1   . TYR A 1 246 ? 41.658  -4.923  46.062 1.00 65.79  ? 1463 TYR A CD1   1 
ATOM   1889 C  CD2   . TYR A 1 246 ? 41.191  -4.505  43.755 1.00 63.93  ? 1463 TYR A CD2   1 
ATOM   1890 C  CE1   . TYR A 1 246 ? 42.491  -5.973  45.704 1.00 66.97  ? 1463 TYR A CE1   1 
ATOM   1891 C  CE2   . TYR A 1 246 ? 42.011  -5.542  43.395 1.00 70.83  ? 1463 TYR A CE2   1 
ATOM   1892 C  CZ    . TYR A 1 246 ? 42.659  -6.274  44.361 1.00 68.57  ? 1463 TYR A CZ    1 
ATOM   1893 O  OH    . TYR A 1 246 ? 43.478  -7.291  43.942 1.00 60.98  ? 1463 TYR A OH    1 
ATOM   1894 N  N     . GLU A 1 247 ? 41.835  -1.326  47.342 1.00 62.21  ? 1464 GLU A N     1 
ATOM   1895 C  CA    . GLU A 1 247 ? 42.981  -1.178  48.180 1.00 70.09  ? 1464 GLU A CA    1 
ATOM   1896 C  C     . GLU A 1 247 ? 43.267  -2.499  48.704 1.00 74.17  ? 1464 GLU A C     1 
ATOM   1897 O  O     . GLU A 1 247 ? 42.433  -3.078  49.297 1.00 84.39  ? 1464 GLU A O     1 
ATOM   1898 C  CB    . GLU A 1 247 ? 42.692  -0.263  49.340 1.00 77.34  ? 1464 GLU A CB    1 
ATOM   1899 C  CG    . GLU A 1 247 ? 43.883  -0.093  50.258 1.00 88.26  ? 1464 GLU A CG    1 
ATOM   1900 C  CD    . GLU A 1 247 ? 43.545  0.668   51.507 1.00 92.73  ? 1464 GLU A CD    1 
ATOM   1901 O  OE1   . GLU A 1 247 ? 43.509  1.903   51.431 1.00 96.76  ? 1464 GLU A OE1   1 
ATOM   1902 O  OE2   . GLU A 1 247 ? 43.318  0.038   52.549 1.00 87.18  ? 1464 GLU A OE2   1 
ATOM   1903 N  N     . HIS A 1 248 ? 44.497  -2.943  48.596 1.00 75.02  ? 1465 HIS A N     1 
ATOM   1904 C  CA    . HIS A 1 248 ? 44.854  -4.267  49.051 1.00 81.11  ? 1465 HIS A CA    1 
ATOM   1905 C  C     . HIS A 1 248 ? 44.640  -4.386  50.502 1.00 78.36  ? 1465 HIS A C     1 
ATOM   1906 O  O     . HIS A 1 248 ? 44.941  -3.498  51.230 1.00 80.74  ? 1465 HIS A O     1 
ATOM   1907 C  CB    . HIS A 1 248 ? 46.284  -4.589  48.665 1.00 84.26  ? 1465 HIS A CB    1 
ATOM   1908 C  CG    . HIS A 1 248 ? 46.709  -5.978  48.986 1.00 81.38  ? 1465 HIS A CG    1 
ATOM   1909 N  ND1   . HIS A 1 248 ? 47.344  -6.299  50.153 1.00 80.70  ? 1465 HIS A ND1   1 
ATOM   1910 C  CD2   . HIS A 1 248 ? 46.622  -7.121  48.277 1.00 78.63  ? 1465 HIS A CD2   1 
ATOM   1911 C  CE1   . HIS A 1 248 ? 47.611  -7.587  50.161 1.00 80.88  ? 1465 HIS A CE1   1 
ATOM   1912 N  NE2   . HIS A 1 248 ? 47.190  -8.105  49.030 1.00 79.48  ? 1465 HIS A NE2   1 
ATOM   1913 N  N     . PRO A 1 249 ? 44.149  -5.522  50.930 1.00 78.78  ? 1466 PRO A N     1 
ATOM   1914 C  CA    . PRO A 1 249 ? 43.805  -5.593  52.330 1.00 88.69  ? 1466 PRO A CA    1 
ATOM   1915 C  C     . PRO A 1 249 ? 44.935  -5.432  53.282 1.00 95.70  ? 1466 PRO A C     1 
ATOM   1916 O  O     . PRO A 1 249 ? 44.885  -4.528  54.083 1.00 89.97  ? 1466 PRO A O     1 
ATOM   1917 C  CB    . PRO A 1 249 ? 43.303  -7.026  52.471 1.00 85.03  ? 1466 PRO A CB    1 
ATOM   1918 C  CG    . PRO A 1 249 ? 43.509  -7.687  51.162 1.00 74.10  ? 1466 PRO A CG    1 
ATOM   1919 C  CD    . PRO A 1 249 ? 44.391  -6.833  50.357 1.00 70.95  ? 1466 PRO A CD    1 
ATOM   1920 N  N     . GLU A 1 250 ? 45.989  -6.204  53.123 1.00 102.42 ? 1467 GLU A N     1 
ATOM   1921 C  CA    . GLU A 1 250 ? 47.078  -6.076  54.048 1.00 106.34 ? 1467 GLU A CA    1 
ATOM   1922 C  C     . GLU A 1 250 ? 47.812  -4.811  53.877 1.00 107.98 ? 1467 GLU A C     1 
ATOM   1923 O  O     . GLU A 1 250 ? 48.120  -4.153  54.818 1.00 108.84 ? 1467 GLU A O     1 
ATOM   1924 C  CB    . GLU A 1 250 ? 48.050  -7.232  53.955 1.00 105.27 ? 1467 GLU A CB    1 
ATOM   1925 N  N     . THR A 1 251 ? 48.056  -4.442  52.654 1.00 106.98 ? 1468 THR A N     1 
ATOM   1926 C  CA    . THR A 1 251 ? 48.852  -3.300  52.431 1.00 108.47 ? 1468 THR A CA    1 
ATOM   1927 C  C     . THR A 1 251 ? 48.042  -2.293  51.740 1.00 108.50 ? 1468 THR A C     1 
ATOM   1928 O  O     . THR A 1 251 ? 47.723  -2.506  50.615 1.00 104.46 ? 1468 THR A O     1 
ATOM   1929 C  CB    . THR A 1 251 ? 49.891  -3.724  51.426 1.00 113.14 ? 1468 THR A CB    1 
ATOM   1930 O  OG1   . THR A 1 251 ? 49.210  -4.113  50.240 1.00 119.21 ? 1468 THR A OG1   1 
ATOM   1931 C  CG2   . THR A 1 251 ? 50.582  -4.917  51.909 1.00 110.27 ? 1468 THR A CG2   1 
ATOM   1932 N  N     . LYS A 1 252 ? 47.902  -1.091  52.256 1.00 111.65 ? 1469 LYS A N     1 
ATOM   1933 C  CA    . LYS A 1 252 ? 47.056  -0.149  51.553 1.00 111.19 ? 1469 LYS A CA    1 
ATOM   1934 C  C     . LYS A 1 252 ? 47.843  0.309   50.366 1.00 111.76 ? 1469 LYS A C     1 
ATOM   1935 O  O     . LYS A 1 252 ? 48.641  1.204   50.442 1.00 111.96 ? 1469 LYS A O     1 
ATOM   1936 C  CB    . LYS A 1 252 ? 46.819  1.061   52.424 1.00 105.80 ? 1469 LYS A CB    1 
ATOM   1937 N  N     . GLU A 1 253 ? 47.565  -0.313  49.242 1.00 92.22  ? 1470 GLU A N     1 
ATOM   1938 C  CA    . GLU A 1 253 ? 48.231  -0.038  48.020 1.00 79.63  ? 1470 GLU A CA    1 
ATOM   1939 C  C     . GLU A 1 253 ? 47.303  -0.486  46.977 1.00 74.78  ? 1470 GLU A C     1 
ATOM   1940 O  O     . GLU A 1 253 ? 46.685  -1.501  47.083 1.00 67.38  ? 1470 GLU A O     1 
ATOM   1941 C  CB    . GLU A 1 253 ? 49.503  -0.822  47.918 1.00 88.37  ? 1470 GLU A CB    1 
ATOM   1942 C  CG    . GLU A 1 253 ? 50.437  -0.289  46.859 1.00 94.66  ? 1470 GLU A CG    1 
ATOM   1943 C  CD    . GLU A 1 253 ? 51.850  -0.728  47.078 1.00 101.94 ? 1470 GLU A CD    1 
ATOM   1944 O  OE1   . GLU A 1 253 ? 52.093  -1.887  47.430 1.00 103.23 ? 1470 GLU A OE1   1 
ATOM   1945 O  OE2   . GLU A 1 253 ? 52.724  0.105   46.897 1.00 104.57 ? 1470 GLU A OE2   1 
ATOM   1946 N  N     . LYS A 1 254 ? 47.276  0.300   45.930 1.00 86.58  ? 1471 LYS A N     1 
ATOM   1947 C  CA    . LYS A 1 254 ? 46.380  0.142   44.798 1.00 73.36  ? 1471 LYS A CA    1 
ATOM   1948 C  C     . LYS A 1 254 ? 46.619  -1.050  44.034 1.00 62.19  ? 1471 LYS A C     1 
ATOM   1949 O  O     . LYS A 1 254 ? 47.623  -1.223  43.467 1.00 60.24  ? 1471 LYS A O     1 
ATOM   1950 C  CB    . LYS A 1 254 ? 46.471  1.302   43.817 1.00 61.92  ? 1471 LYS A CB    1 
ATOM   1951 N  N     . GLU A 1 255 ? 45.622  -1.871  44.012 1.00 58.43  ? 1472 GLU A N     1 
ATOM   1952 C  CA    . GLU A 1 255 ? 45.683  -3.092  43.245 1.00 56.54  ? 1472 GLU A CA    1 
ATOM   1953 C  C     . GLU A 1 255 ? 44.606  -3.025  42.178 1.00 58.05  ? 1472 GLU A C     1 
ATOM   1954 O  O     . GLU A 1 255 ? 43.502  -2.528  42.419 1.00 57.39  ? 1472 GLU A O     1 
ATOM   1955 C  CB    . GLU A 1 255 ? 45.508  -4.325  44.133 1.00 60.34  ? 1472 GLU A CB    1 
ATOM   1956 C  CG    . GLU A 1 255 ? 46.759  -4.687  44.929 1.00 69.58  ? 1472 GLU A CG    1 
ATOM   1957 C  CD    . GLU A 1 255 ? 48.032  -4.731  44.075 1.00 78.95  ? 1472 GLU A CD    1 
ATOM   1958 O  OE1   . GLU A 1 255 ? 47.962  -5.081  42.866 1.00 80.19  ? 1472 GLU A OE1   1 
ATOM   1959 O  OE2   . GLU A 1 255 ? 49.116  -4.437  44.630 1.00 75.49  ? 1472 GLU A OE2   1 
ATOM   1960 N  N     . TYR A 1 256 ? 44.959  -3.462  40.981 1.00 67.64  ? 1473 TYR A N     1 
ATOM   1961 C  CA    . TYR A 1 256 ? 44.033  -3.525  39.864 1.00 67.10  ? 1473 TYR A CA    1 
ATOM   1962 C  C     . TYR A 1 256 ? 43.456  -4.940  39.758 1.00 66.25  ? 1473 TYR A C     1 
ATOM   1963 O  O     . TYR A 1 256 ? 44.142  -5.941  40.016 1.00 61.35  ? 1473 TYR A O     1 
ATOM   1964 C  CB    . TYR A 1 256 ? 44.724  -3.109  38.561 1.00 60.20  ? 1473 TYR A CB    1 
ATOM   1965 C  CG    . TYR A 1 256 ? 45.153  -1.651  38.492 1.00 58.37  ? 1473 TYR A CG    1 
ATOM   1966 C  CD1   . TYR A 1 256 ? 44.514  -0.757  37.640 1.00 49.19  ? 1473 TYR A CD1   1 
ATOM   1967 C  CD2   . TYR A 1 256 ? 46.207  -1.173  39.262 1.00 62.33  ? 1473 TYR A CD2   1 
ATOM   1968 C  CE1   . TYR A 1 256 ? 44.908  0.562   37.559 1.00 58.61  ? 1473 TYR A CE1   1 
ATOM   1969 C  CE2   . TYR A 1 256 ? 46.611  0.167   39.192 1.00 59.88  ? 1473 TYR A CE2   1 
ATOM   1970 C  CZ    . TYR A 1 256 ? 45.959  1.024   38.339 1.00 65.65  ? 1473 TYR A CZ    1 
ATOM   1971 O  OH    . TYR A 1 256 ? 46.356  2.344   38.259 1.00 73.59  ? 1473 TYR A OH    1 
ATOM   1972 N  N     . VAL A 1 257 ? 42.174  -5.010  39.431 1.00 57.84  ? 1474 VAL A N     1 
ATOM   1973 C  CA    . VAL A 1 257 ? 41.495  -6.290  39.372 1.00 46.74  ? 1474 VAL A CA    1 
ATOM   1974 C  C     . VAL A 1 257 ? 41.867  -7.018  38.092 1.00 44.03  ? 1474 VAL A C     1 
ATOM   1975 O  O     . VAL A 1 257 ? 42.394  -6.445  37.140 1.00 42.80  ? 1474 VAL A O     1 
ATOM   1976 C  CB    . VAL A 1 257 ? 39.977  -6.118  39.458 1.00 43.29  ? 1474 VAL A CB    1 
ATOM   1977 C  CG1   . VAL A 1 257 ? 39.582  -5.352  40.703 1.00 48.36  ? 1474 VAL A CG1   1 
ATOM   1978 C  CG2   . VAL A 1 257 ? 39.510  -5.436  38.213 1.00 42.51  ? 1474 VAL A CG2   1 
ATOM   1979 N  N     . PHE A 1 258 ? 41.582  -8.310  38.081 1.00 47.84  ? 1475 PHE A N     1 
ATOM   1980 C  CA    . PHE A 1 258 ? 41.787  -9.145  36.913 1.00 48.59  ? 1475 PHE A CA    1 
ATOM   1981 C  C     . PHE A 1 258 ? 40.432  -9.452  36.314 1.00 47.04  ? 1475 PHE A C     1 
ATOM   1982 O  O     . PHE A 1 258 ? 39.465  -9.661  37.040 1.00 48.48  ? 1475 PHE A O     1 
ATOM   1983 C  CB    . PHE A 1 258 ? 42.533  -10.417 37.275 1.00 46.59  ? 1475 PHE A CB    1 
ATOM   1984 C  CG    . PHE A 1 258 ? 43.909  -10.155 37.763 1.00 42.91  ? 1475 PHE A CG    1 
ATOM   1985 C  CD1   . PHE A 1 258 ? 44.990  -10.191 36.890 1.00 37.83  ? 1475 PHE A CD1   1 
ATOM   1986 C  CD2   . PHE A 1 258 ? 44.115  -9.804  39.091 1.00 39.43  ? 1475 PHE A CD2   1 
ATOM   1987 C  CE1   . PHE A 1 258 ? 46.261  -9.927  37.356 1.00 38.87  ? 1475 PHE A CE1   1 
ATOM   1988 C  CE2   . PHE A 1 258 ? 45.371  -9.528  39.557 1.00 39.25  ? 1475 PHE A CE2   1 
ATOM   1989 C  CZ    . PHE A 1 258 ? 46.452  -9.589  38.697 1.00 39.40  ? 1475 PHE A CZ    1 
ATOM   1990 N  N     . GLN A 1 259 ? 40.340  -9.386  35.000 1.00 34.33  ? 1476 GLN A N     1 
ATOM   1991 C  CA    . GLN A 1 259 ? 39.049  -9.467  34.349 1.00 39.32  ? 1476 GLN A CA    1 
ATOM   1992 C  C     . GLN A 1 259 ? 39.069  -10.506 33.246 1.00 40.32  ? 1476 GLN A C     1 
ATOM   1993 O  O     . GLN A 1 259 ? 40.097  -10.722 32.586 1.00 35.65  ? 1476 GLN A O     1 
ATOM   1994 C  CB    . GLN A 1 259 ? 38.629  -8.121  33.740 1.00 37.32  ? 1476 GLN A CB    1 
ATOM   1995 C  CG    . GLN A 1 259 ? 38.279  -7.056  34.729 1.00 36.54  ? 1476 GLN A CG    1 
ATOM   1996 C  CD    . GLN A 1 259 ? 38.233  -5.691  34.081 1.00 46.50  ? 1476 GLN A CD    1 
ATOM   1997 O  OE1   . GLN A 1 259 ? 39.270  -5.067  33.854 1.00 39.06  ? 1476 GLN A OE1   1 
ATOM   1998 N  NE2   . GLN A 1 259 ? 37.025  -5.227  33.757 1.00 60.22  ? 1476 GLN A NE2   1 
ATOM   1999 N  N     . ASN A 1 260 ? 37.891  -11.089 33.028 1.00 32.59  ? 1477 ASN A N     1 
ATOM   2000 C  CA    . ASN A 1 260 ? 37.562  -11.799 31.799 1.00 46.39  ? 1477 ASN A CA    1 
ATOM   2001 C  C     . ASN A 1 260 ? 36.319  -11.179 31.165 1.00 47.22  ? 1477 ASN A C     1 
ATOM   2002 O  O     . ASN A 1 260 ? 35.596  -10.379 31.772 1.00 52.47  ? 1477 ASN A O     1 
ATOM   2003 C  CB    . ASN A 1 260 ? 37.319  -13.302 32.028 1.00 36.58  ? 1477 ASN A CB    1 
ATOM   2004 C  CG    . ASN A 1 260 ? 38.245  -13.899 33.059 1.00 48.83  ? 1477 ASN A CG    1 
ATOM   2005 O  OD1   . ASN A 1 260 ? 39.440  -13.593 33.103 1.00 57.37  ? 1477 ASN A OD1   1 
ATOM   2006 N  ND2   . ASN A 1 260 ? 37.700  -14.769 33.894 1.00 47.77  ? 1477 ASN A ND2   1 
ATOM   2007 N  N     . SER A 1 261 ? 36.116  -11.531 29.901 1.00 43.29  ? 1478 SER A N     1 
ATOM   2008 C  CA    . SER A 1 261 ? 34.847  -11.356 29.221 1.00 46.77  ? 1478 SER A CA    1 
ATOM   2009 C  C     . SER A 1 261 ? 34.732  -12.491 28.212 1.00 58.03  ? 1478 SER A C     1 
ATOM   2010 O  O     . SER A 1 261 ? 35.737  -13.012 27.723 1.00 60.75  ? 1478 SER A O     1 
ATOM   2011 C  CB    . SER A 1 261 ? 34.709  -9.970  28.561 1.00 49.42  ? 1478 SER A CB    1 
ATOM   2012 O  OG    . SER A 1 261 ? 35.649  -9.720  27.518 1.00 53.01  ? 1478 SER A OG    1 
ATOM   2013 N  N     . TRP A 1 262 ? 33.500  -12.904 27.948 1.00 63.21  ? 1479 TRP A N     1 
ATOM   2014 C  CA    . TRP A 1 262 ? 33.255  -14.018 27.041 1.00 62.48  ? 1479 TRP A CA    1 
ATOM   2015 C  C     . TRP A 1 262 ? 31.882  -13.825 26.418 1.00 67.73  ? 1479 TRP A C     1 
ATOM   2016 O  O     . TRP A 1 262 ? 31.015  -13.148 26.981 1.00 61.57  ? 1479 TRP A O     1 
ATOM   2017 C  CB    . TRP A 1 262 ? 33.344  -15.373 27.766 1.00 41.49  ? 1479 TRP A CB    1 
ATOM   2018 C  CG    . TRP A 1 262 ? 33.092  -15.258 29.239 1.00 35.85  ? 1479 TRP A CG    1 
ATOM   2019 C  CD1   . TRP A 1 262 ? 34.029  -15.067 30.192 1.00 34.26  ? 1479 TRP A CD1   1 
ATOM   2020 C  CD2   . TRP A 1 262 ? 31.820  -15.299 29.930 1.00 33.92  ? 1479 TRP A CD2   1 
ATOM   2021 N  NE1   . TRP A 1 262 ? 33.442  -14.996 31.438 1.00 40.83  ? 1479 TRP A NE1   1 
ATOM   2022 C  CE2   . TRP A 1 262 ? 32.087  -15.133 31.304 1.00 39.22  ? 1479 TRP A CE2   1 
ATOM   2023 C  CE3   . TRP A 1 262 ? 30.500  -15.461 29.524 1.00 34.04  ? 1479 TRP A CE3   1 
ATOM   2024 C  CZ2   . TRP A 1 262 ? 31.079  -15.123 32.274 1.00 38.72  ? 1479 TRP A CZ2   1 
ATOM   2025 C  CZ3   . TRP A 1 262 ? 29.497  -15.457 30.492 1.00 42.38  ? 1479 TRP A CZ3   1 
ATOM   2026 C  CH2   . TRP A 1 262 ? 29.795  -15.294 31.846 1.00 44.52  ? 1479 TRP A CH2   1 
ATOM   2027 N  N     . GLY A 1 263 ? 31.665  -14.469 25.279 1.00 59.37  ? 1480 GLY A N     1 
ATOM   2028 C  CA    . GLY A 1 263 ? 30.396  -14.287 24.612 1.00 51.23  ? 1480 GLY A CA    1 
ATOM   2029 C  C     . GLY A 1 263 ? 30.121  -15.357 23.586 1.00 51.48  ? 1480 GLY A C     1 
ATOM   2030 O  O     . GLY A 1 263 ? 31.038  -15.961 23.021 1.00 62.63  ? 1480 GLY A O     1 
ATOM   2031 N  N     . ILE A 1 264 ? 28.831  -15.573 23.340 1.00 46.38  ? 1481 ILE A N     1 
ATOM   2032 C  CA    . ILE A 1 264 ? 28.415  -16.492 22.281 1.00 46.95  ? 1481 ILE A CA    1 
ATOM   2033 C  C     . ILE A 1 264 ? 27.150  -15.941 21.648 1.00 49.26  ? 1481 ILE A C     1 
ATOM   2034 O  O     . ILE A 1 264 ? 26.315  -15.330 22.325 1.00 63.92  ? 1481 ILE A O     1 
ATOM   2035 C  CB    . ILE A 1 264 ? 28.213  -17.958 22.769 1.00 46.86  ? 1481 ILE A CB    1 
ATOM   2036 C  CG1   . ILE A 1 264 ? 28.353  -18.900 21.576 1.00 47.96  ? 1481 ILE A CG1   1 
ATOM   2037 C  CG2   . ILE A 1 264 ? 26.865  -18.181 23.403 1.00 28.68  ? 1481 ILE A CG2   1 
ATOM   2038 C  CD1   . ILE A 1 264 ? 28.097  -20.370 21.844 1.00 41.33  ? 1481 ILE A CD1   1 
ATOM   2039 N  N     . THR A 1 265 ? 27.017  -16.162 20.337 1.00 37.73  ? 1482 THR A N     1 
ATOM   2040 C  CA    . THR A 1 265 ? 26.025  -15.461 19.534 1.00 41.94  ? 1482 THR A CA    1 
ATOM   2041 C  C     . THR A 1 265 ? 25.133  -16.432 18.766 1.00 52.82  ? 1482 THR A C     1 
ATOM   2042 O  O     . THR A 1 265 ? 25.217  -17.654 18.904 1.00 49.12  ? 1482 THR A O     1 
ATOM   2043 C  CB    . THR A 1 265 ? 26.697  -14.485 18.562 1.00 41.13  ? 1482 THR A CB    1 
ATOM   2044 O  OG1   . THR A 1 265 ? 27.219  -15.191 17.439 1.00 41.57  ? 1482 THR A OG1   1 
ATOM   2045 C  CG2   . THR A 1 265 ? 27.823  -13.746 19.242 1.00 42.14  ? 1482 THR A CG2   1 
ATOM   2046 N  N     . THR A 1 266 ? 24.294  -15.862 17.906 1.00 65.11  ? 1483 THR A N     1 
ATOM   2047 C  CA    . THR A 1 266 ? 23.397  -16.670 17.092 1.00 67.74  ? 1483 THR A CA    1 
ATOM   2048 C  C     . THR A 1 266 ? 24.122  -17.462 16.010 1.00 68.66  ? 1483 THR A C     1 
ATOM   2049 O  O     . THR A 1 266 ? 23.490  -18.307 15.359 1.00 68.84  ? 1483 THR A O     1 
ATOM   2050 C  CB    . THR A 1 266 ? 22.339  -15.757 16.471 1.00 59.61  ? 1483 THR A CB    1 
ATOM   2051 O  OG1   . THR A 1 266 ? 22.983  -14.748 15.676 1.00 52.61  ? 1483 THR A OG1   1 
ATOM   2052 C  CG2   . THR A 1 266 ? 21.580  -15.070 17.567 1.00 53.38  ? 1483 THR A CG2   1 
ATOM   2053 N  N     . ARG A 1 267 ? 25.431  -17.237 15.835 1.00 58.50  ? 1484 ARG A N     1 
ATOM   2054 C  CA    . ARG A 1 267 ? 26.208  -17.991 14.855 1.00 50.11  ? 1484 ARG A CA    1 
ATOM   2055 C  C     . ARG A 1 267 ? 26.092  -19.496 15.084 1.00 51.23  ? 1484 ARG A C     1 
ATOM   2056 O  O     . ARG A 1 267 ? 26.211  -20.278 14.134 1.00 54.18  ? 1484 ARG A O     1 
ATOM   2057 C  CB    . ARG A 1 267 ? 27.669  -17.551 14.905 1.00 34.75  ? 1484 ARG A CB    1 
ATOM   2058 C  CG    . ARG A 1 267 ? 28.546  -18.152 13.846 1.00 31.27  ? 1484 ARG A CG    1 
ATOM   2059 C  CD    . ARG A 1 267 ? 29.965  -17.723 14.074 1.00 33.23  ? 1484 ARG A CD    1 
ATOM   2060 N  NE    . ARG A 1 267 ? 30.284  -16.512 13.337 1.00 52.24  ? 1484 ARG A NE    1 
ATOM   2061 C  CZ    . ARG A 1 267 ? 31.486  -15.941 13.304 1.00 71.04  ? 1484 ARG A CZ    1 
ATOM   2062 N  NH1   . ARG A 1 267 ? 32.511  -16.472 13.967 1.00 75.17  ? 1484 ARG A NH1   1 
ATOM   2063 N  NH2   . ARG A 1 267 ? 31.664  -14.830 12.601 1.00 73.50  ? 1484 ARG A NH2   1 
ATOM   2064 N  N     . THR A 1 268 ? 25.847  -19.913 16.330 1.00 43.15  ? 1485 THR A N     1 
ATOM   2065 C  CA    . THR A 1 268 ? 25.612  -21.317 16.625 1.00 47.58  ? 1485 THR A CA    1 
ATOM   2066 C  C     . THR A 1 268 ? 24.655  -21.930 15.623 1.00 56.23  ? 1485 THR A C     1 
ATOM   2067 O  O     . THR A 1 268 ? 24.960  -22.942 14.977 1.00 62.06  ? 1485 THR A O     1 
ATOM   2068 C  CB    . THR A 1 268 ? 25.034  -21.461 18.026 1.00 45.12  ? 1485 THR A CB    1 
ATOM   2069 O  OG1   . THR A 1 268 ? 23.830  -20.700 18.087 1.00 29.46  ? 1485 THR A OG1   1 
ATOM   2070 C  CG2   . THR A 1 268 ? 25.999  -20.958 19.053 1.00 43.29  ? 1485 THR A CG2   1 
ATOM   2071 N  N     . ILE A 1 269 ? 23.502  -21.297 15.441 1.00 30.27  ? 1486 ILE A N     1 
ATOM   2072 C  CA    . ILE A 1 269 ? 22.502  -21.905 14.570 1.00 39.14  ? 1486 ILE A CA    1 
ATOM   2073 C  C     . ILE A 1 269 ? 23.053  -22.097 13.161 1.00 38.31  ? 1486 ILE A C     1 
ATOM   2074 O  O     . ILE A 1 269 ? 22.896  -23.166 12.555 1.00 33.94  ? 1486 ILE A O     1 
ATOM   2075 C  CB    . ILE A 1 269 ? 21.213  -21.080 14.592 1.00 38.05  ? 1486 ILE A CB    1 
ATOM   2076 C  CG1   . ILE A 1 269 ? 20.714  -21.038 16.039 1.00 29.49  ? 1486 ILE A CG1   1 
ATOM   2077 C  CG2   . ILE A 1 269 ? 20.218  -21.677 13.630 1.00 30.38  ? 1486 ILE A CG2   1 
ATOM   2078 C  CD1   . ILE A 1 269 ? 19.375  -20.433 16.194 1.00 31.77  ? 1486 ILE A CD1   1 
ATOM   2079 N  N     . GLY A 1 270 ? 23.775  -21.101 12.657 1.00 31.19  ? 1487 GLY A N     1 
ATOM   2080 C  CA    . GLY A 1 270 ? 24.355  -21.223 11.336 1.00 34.81  ? 1487 GLY A CA    1 
ATOM   2081 C  C     . GLY A 1 270 ? 25.259  -22.432 11.208 1.00 39.40  ? 1487 GLY A C     1 
ATOM   2082 O  O     . GLY A 1 270 ? 25.139  -23.207 10.244 1.00 37.06  ? 1487 GLY A O     1 
ATOM   2083 N  N     . VAL A 1 271 ? 26.145  -22.647 12.196 1.00 32.54  ? 1488 VAL A N     1 
ATOM   2084 C  CA    . VAL A 1 271 ? 27.047  -23.791 12.074 1.00 53.47  ? 1488 VAL A CA    1 
ATOM   2085 C  C     . VAL A 1 271 ? 26.248  -25.094 12.135 1.00 55.77  ? 1488 VAL A C     1 
ATOM   2086 O  O     . VAL A 1 271 ? 26.494  -26.036 11.355 1.00 38.93  ? 1488 VAL A O     1 
ATOM   2087 C  CB    . VAL A 1 271 ? 28.202  -23.733 13.099 1.00 55.89  ? 1488 VAL A CB    1 
ATOM   2088 C  CG1   . VAL A 1 271 ? 27.737  -23.405 14.471 1.00 63.23  ? 1488 VAL A CG1   1 
ATOM   2089 C  CG2   . VAL A 1 271 ? 28.998  -25.053 13.104 1.00 58.02  ? 1488 VAL A CG2   1 
ATOM   2090 N  N     . MET A 1 272 ? 25.213  -25.125 12.988 1.00 58.02  ? 1489 MET A N     1 
ATOM   2091 C  CA    . MET A 1 272 ? 24.298  -26.255 12.975 1.00 50.58  ? 1489 MET A CA    1 
ATOM   2092 C  C     . MET A 1 272 ? 23.813  -26.517 11.556 1.00 56.77  ? 1489 MET A C     1 
ATOM   2093 O  O     . MET A 1 272 ? 24.060  -27.590 10.984 1.00 60.81  ? 1489 MET A O     1 
ATOM   2094 C  CB    . MET A 1 272 ? 23.122  -25.970 13.905 1.00 45.09  ? 1489 MET A CB    1 
ATOM   2095 C  CG    . MET A 1 272 ? 22.141  -27.108 13.996 1.00 50.16  ? 1489 MET A CG    1 
ATOM   2096 S  SD    . MET A 1 272 ? 20.539  -26.602 14.612 1.00 49.79  ? 1489 MET A SD    1 
ATOM   2097 C  CE    . MET A 1 272 ? 19.875  -25.819 13.155 1.00 32.29  ? 1489 MET A CE    1 
ATOM   2098 N  N     . ILE A 1 273 ? 23.228  -25.490 10.928 1.00 62.84  ? 1490 ILE A N     1 
ATOM   2099 C  CA    . ILE A 1 273 ? 22.719  -25.659 9.571  1.00 62.95  ? 1490 ILE A CA    1 
ATOM   2100 C  C     . ILE A 1 273 ? 23.820  -26.191 8.668  1.00 55.28  ? 1490 ILE A C     1 
ATOM   2101 O  O     . ILE A 1 273 ? 23.626  -27.190 7.965  1.00 35.81  ? 1490 ILE A O     1 
ATOM   2102 C  CB    . ILE A 1 273 ? 22.104  -24.349 9.045  1.00 49.94  ? 1490 ILE A CB    1 
ATOM   2103 C  CG1   . ILE A 1 273 ? 20.930  -23.978 9.943  1.00 56.10  ? 1490 ILE A CG1   1 
ATOM   2104 C  CG2   . ILE A 1 273 ? 21.603  -24.523 7.601  1.00 34.31  ? 1490 ILE A CG2   1 
ATOM   2105 C  CD1   . ILE A 1 273 ? 20.355  -22.592 9.691  1.00 67.53  ? 1490 ILE A CD1   1 
ATOM   2106 N  N     . MET A 1 274 ? 25.005  -25.553 8.713  1.00 43.39  ? 1491 MET A N     1 
ATOM   2107 C  CA    . MET A 1 274 ? 26.061  -25.881 7.763  1.00 47.89  ? 1491 MET A CA    1 
ATOM   2108 C  C     . MET A 1 274 ? 26.550  -27.294 7.950  1.00 50.80  ? 1491 MET A C     1 
ATOM   2109 O  O     . MET A 1 274 ? 26.927  -27.947 6.965  1.00 57.04  ? 1491 MET A O     1 
ATOM   2110 C  CB    . MET A 1 274 ? 27.268  -24.947 7.900  1.00 62.43  ? 1491 MET A CB    1 
ATOM   2111 C  CG    . MET A 1 274 ? 27.076  -23.488 7.536  1.00 61.71  ? 1491 MET A CG    1 
ATOM   2112 S  SD    . MET A 1 274 ? 26.374  -23.220 5.910  1.00 68.27  ? 1491 MET A SD    1 
ATOM   2113 C  CE    . MET A 1 274 ? 27.653  -23.749 4.786  1.00 65.63  ? 1491 MET A CE    1 
ATOM   2114 N  N     . VAL A 1 275 ? 26.536  -27.795 9.189  1.00 46.38  ? 1492 VAL A N     1 
ATOM   2115 C  CA    . VAL A 1 275 ? 27.158  -29.096 9.435  1.00 52.50  ? 1492 VAL A CA    1 
ATOM   2116 C  C     . VAL A 1 275 ? 26.187  -30.259 9.210  1.00 51.29  ? 1492 VAL A C     1 
ATOM   2117 O  O     . VAL A 1 275 ? 26.576  -31.277 8.636  1.00 42.65  ? 1492 VAL A O     1 
ATOM   2118 C  CB    . VAL A 1 275 ? 27.768  -29.113 10.853 1.00 50.67  ? 1492 VAL A CB    1 
ATOM   2119 C  CG1   . VAL A 1 275 ? 28.028  -30.535 11.321 1.00 48.13  ? 1492 VAL A CG1   1 
ATOM   2120 C  CG2   . VAL A 1 275 ? 29.074  -28.293 10.870 1.00 42.17  ? 1492 VAL A CG2   1 
ATOM   2121 N  N     . HIS A 1 276 ? 24.895  -30.098 9.524  1.00 51.00  ? 1493 HIS A N     1 
ATOM   2122 C  CA    . HIS A 1 276 ? 23.967  -31.218 9.623  1.00 46.35  ? 1493 HIS A CA    1 
ATOM   2123 C  C     . HIS A 1 276 ? 22.969  -31.339 8.479  1.00 55.83  ? 1493 HIS A C     1 
ATOM   2124 O  O     . HIS A 1 276 ? 22.609  -32.460 8.111  1.00 53.08  ? 1493 HIS A O     1 
ATOM   2125 C  CB    . HIS A 1 276 ? 23.166  -31.116 10.921 1.00 45.45  ? 1493 HIS A CB    1 
ATOM   2126 C  CG    . HIS A 1 276 ? 23.963  -31.407 12.146 1.00 54.08  ? 1493 HIS A CG    1 
ATOM   2127 N  ND1   . HIS A 1 276 ? 24.892  -32.422 12.199 1.00 60.89  ? 1493 HIS A ND1   1 
ATOM   2128 C  CD2   . HIS A 1 276 ? 23.969  -30.824 13.366 1.00 54.69  ? 1493 HIS A CD2   1 
ATOM   2129 C  CE1   . HIS A 1 276 ? 25.440  -32.448 13.400 1.00 61.55  ? 1493 HIS A CE1   1 
ATOM   2130 N  NE2   . HIS A 1 276 ? 24.898  -31.488 14.127 1.00 57.06  ? 1493 HIS A NE2   1 
ATOM   2131 N  N     . ALA A 1 277 ? 22.495  -30.235 7.919  1.00 55.52  ? 1494 ALA A N     1 
ATOM   2132 C  CA    . ALA A 1 277 ? 21.435  -30.328 6.930  1.00 53.36  ? 1494 ALA A CA    1 
ATOM   2133 C  C     . ALA A 1 277 ? 21.952  -31.001 5.670  1.00 55.15  ? 1494 ALA A C     1 
ATOM   2134 O  O     . ALA A 1 277 ? 23.112  -30.831 5.290  1.00 54.30  ? 1494 ALA A O     1 
ATOM   2135 C  CB    . ALA A 1 277 ? 20.884  -28.947 6.603  1.00 54.87  ? 1494 ALA A CB    1 
ATOM   2136 N  N     . ASP A 1 278 ? 21.096  -31.804 5.048  1.00 59.48  ? 1495 ASP A N     1 
ATOM   2137 C  CA    . ASP A 1 278 ? 21.410  -32.487 3.803  1.00 59.76  ? 1495 ASP A CA    1 
ATOM   2138 C  C     . ASP A 1 278 ? 20.708  -31.785 2.646  1.00 54.08  ? 1495 ASP A C     1 
ATOM   2139 O  O     . ASP A 1 278 ? 20.332  -30.611 2.749  1.00 50.61  ? 1495 ASP A O     1 
ATOM   2140 C  CB    . ASP A 1 278 ? 21.031  -33.973 3.894  1.00 58.08  ? 1495 ASP A CB    1 
ATOM   2141 C  CG    . ASP A 1 278 ? 19.626  -34.193 4.402  1.00 56.25  ? 1495 ASP A CG    1 
ATOM   2142 O  OD1   . ASP A 1 278 ? 18.698  -33.511 3.924  1.00 58.95  ? 1495 ASP A OD1   1 
ATOM   2143 O  OD2   . ASP A 1 278 ? 19.455  -35.055 5.288  1.00 60.67  ? 1495 ASP A OD2   1 
ATOM   2144 N  N     . ASN A 1 279 ? 20.551  -32.489 1.529  1.00 43.72  ? 1496 ASN A N     1 
ATOM   2145 C  CA    . ASN A 1 279 ? 19.942  -31.917 0.343  1.00 45.05  ? 1496 ASN A CA    1 
ATOM   2146 C  C     . ASN A 1 279 ? 18.440  -32.090 0.335  1.00 57.34  ? 1496 ASN A C     1 
ATOM   2147 O  O     . ASN A 1 279 ? 17.815  -31.977 -0.724 1.00 69.26  ? 1496 ASN A O     1 
ATOM   2148 C  CB    . ASN A 1 279 ? 20.565  -32.508 -0.905 1.00 43.81  ? 1496 ASN A CB    1 
ATOM   2149 C  CG    . ASN A 1 279 ? 22.062  -32.371 -0.902 1.00 66.96  ? 1496 ASN A CG    1 
ATOM   2150 O  OD1   . ASN A 1 279 ? 22.611  -31.441 -1.491 1.00 65.60  ? 1496 ASN A OD1   1 
ATOM   2151 N  ND2   . ASN A 1 279 ? 22.740  -33.285 -0.209 1.00 70.70  ? 1496 ASN A ND2   1 
ATOM   2152 N  N     . GLN A 1 280 ? 17.859  -32.420 1.481  1.00 55.06  ? 1497 GLN A N     1 
ATOM   2153 C  CA    . GLN A 1 280 ? 16.422  -32.468 1.637  1.00 55.57  ? 1497 GLN A CA    1 
ATOM   2154 C  C     . GLN A 1 280 ? 15.953  -31.518 2.721  1.00 56.84  ? 1497 GLN A C     1 
ATOM   2155 O  O     . GLN A 1 280 ? 14.751  -31.454 3.005  1.00 57.58  ? 1497 GLN A O     1 
ATOM   2156 C  CB    . GLN A 1 280 ? 15.969  -33.890 1.967  1.00 54.89  ? 1497 GLN A CB    1 
ATOM   2157 C  CG    . GLN A 1 280 ? 16.046  -34.808 0.793  1.00 73.44  ? 1497 GLN A CG    1 
ATOM   2158 C  CD    . GLN A 1 280 ? 17.400  -35.470 0.694  1.00 96.44  ? 1497 GLN A CD    1 
ATOM   2159 O  OE1   . GLN A 1 280 ? 18.060  -35.401 -0.343 1.00 108.98 ? 1497 GLN A OE1   1 
ATOM   2160 N  NE2   . GLN A 1 280 ? 17.828  -36.118 1.777  1.00 99.63  ? 1497 GLN A NE2   1 
ATOM   2161 N  N     . GLY A 1 281 ? 16.856  -30.774 3.319  1.00 57.69  ? 1498 GLY A N     1 
ATOM   2162 C  CA    . GLY A 1 281 ? 16.455  -29.789 4.282  1.00 63.09  ? 1498 GLY A CA    1 
ATOM   2163 C  C     . GLY A 1 281 ? 17.277  -29.933 5.532  1.00 71.88  ? 1498 GLY A C     1 
ATOM   2164 O  O     . GLY A 1 281 ? 18.328  -30.583 5.540  1.00 74.07  ? 1498 GLY A O     1 
ATOM   2165 N  N     . LEU A 1 282 ? 16.761  -29.331 6.596  1.00 70.03  ? 1499 LEU A N     1 
ATOM   2166 C  CA    . LEU A 1 282 ? 17.394  -29.372 7.900  1.00 62.35  ? 1499 LEU A CA    1 
ATOM   2167 C  C     . LEU A 1 282 ? 17.514  -30.802 8.417  1.00 60.30  ? 1499 LEU A C     1 
ATOM   2168 O  O     . LEU A 1 282 ? 16.897  -31.737 7.899  1.00 53.79  ? 1499 LEU A O     1 
ATOM   2169 C  CB    . LEU A 1 282 ? 16.587  -28.542 8.902  1.00 58.39  ? 1499 LEU A CB    1 
ATOM   2170 C  CG    . LEU A 1 282 ? 16.411  -27.030 8.754  1.00 48.43  ? 1499 LEU A CG    1 
ATOM   2171 C  CD1   . LEU A 1 282 ? 15.145  -26.690 9.489  1.00 41.29  ? 1499 LEU A CD1   1 
ATOM   2172 C  CD2   . LEU A 1 282 ? 17.605  -26.258 9.324  1.00 33.78  ? 1499 LEU A CD2   1 
ATOM   2173 N  N     . VAL A 1 283 ? 18.374  -30.961 9.429  1.00 59.92  ? 1500 VAL A N     1 
ATOM   2174 C  CA    . VAL A 1 283 ? 18.430  -32.129 10.300 1.00 51.21  ? 1500 VAL A CA    1 
ATOM   2175 C  C     . VAL A 1 283 ? 18.706  -31.624 11.711 1.00 49.42  ? 1500 VAL A C     1 
ATOM   2176 O  O     . VAL A 1 283 ? 19.867  -31.452 12.097 1.00 49.93  ? 1500 VAL A O     1 
ATOM   2177 C  CB    . VAL A 1 283 ? 19.518  -33.127 9.868  1.00 53.49  ? 1500 VAL A CB    1 
ATOM   2178 C  CG1   . VAL A 1 283 ? 19.365  -34.418 10.639 1.00 55.20  ? 1500 VAL A CG1   1 
ATOM   2179 C  CG2   . VAL A 1 283 ? 19.468  -33.391 8.380  1.00 55.38  ? 1500 VAL A CG2   1 
ATOM   2180 N  N     . LEU A 1 284 ? 17.643  -31.400 12.507 1.00 49.07  ? 1501 LEU A N     1 
ATOM   2181 C  CA    . LEU A 1 284 ? 17.869  -30.742 13.792 1.00 48.82  ? 1501 LEU A CA    1 
ATOM   2182 C  C     . LEU A 1 284 ? 18.357  -31.744 14.836 1.00 56.55  ? 1501 LEU A C     1 
ATOM   2183 O  O     . LEU A 1 284 ? 17.859  -32.874 14.906 1.00 57.74  ? 1501 LEU A O     1 
ATOM   2184 C  CB    . LEU A 1 284 ? 16.596  -30.037 14.299 1.00 46.74  ? 1501 LEU A CB    1 
ATOM   2185 C  CG    . LEU A 1 284 ? 15.630  -29.239 13.390 1.00 50.58  ? 1501 LEU A CG    1 
ATOM   2186 C  CD1   . LEU A 1 284 ? 14.513  -28.620 14.223 1.00 60.91  ? 1501 LEU A CD1   1 
ATOM   2187 C  CD2   . LEU A 1 284 ? 16.275  -28.148 12.521 1.00 39.14  ? 1501 LEU A CD2   1 
ATOM   2188 N  N     . PRO A 1 285 ? 19.317  -31.350 15.664 1.00 64.89  ? 1502 PRO A N     1 
ATOM   2189 C  CA    . PRO A 1 285 ? 19.737  -32.198 16.774 1.00 77.35  ? 1502 PRO A CA    1 
ATOM   2190 C  C     . PRO A 1 285 ? 18.614  -32.368 17.778 1.00 83.16  ? 1502 PRO A C     1 
ATOM   2191 O  O     . PRO A 1 285 ? 17.890  -31.410 18.081 1.00 95.46  ? 1502 PRO A O     1 
ATOM   2192 C  CB    . PRO A 1 285 ? 20.922  -31.428 17.382 1.00 75.37  ? 1502 PRO A CB    1 
ATOM   2193 C  CG    . PRO A 1 285 ? 21.372  -30.514 16.307 1.00 67.80  ? 1502 PRO A CG    1 
ATOM   2194 C  CD    . PRO A 1 285 ? 20.118  -30.124 15.586 1.00 65.86  ? 1502 PRO A CD    1 
ATOM   2195 N  N     . PRO A 1 286 ? 18.426  -33.577 18.297 1.00 71.56  ? 1503 PRO A N     1 
ATOM   2196 C  CA    . PRO A 1 286 ? 17.234  -33.838 19.121 1.00 62.91  ? 1503 PRO A CA    1 
ATOM   2197 C  C     . PRO A 1 286 ? 17.115  -32.946 20.341 1.00 45.41  ? 1503 PRO A C     1 
ATOM   2198 O  O     . PRO A 1 286 ? 15.998  -32.628 20.742 1.00 41.40  ? 1503 PRO A O     1 
ATOM   2199 C  CB    . PRO A 1 286 ? 17.396  -35.316 19.527 1.00 66.00  ? 1503 PRO A CB    1 
ATOM   2200 C  CG    . PRO A 1 286 ? 18.388  -35.889 18.580 1.00 68.46  ? 1503 PRO A CG    1 
ATOM   2201 C  CD    . PRO A 1 286 ? 19.278  -34.766 18.134 1.00 71.51  ? 1503 PRO A CD    1 
ATOM   2202 N  N     . ARG A 1 287 ? 18.223  -32.536 20.957 1.00 52.09  ? 1504 ARG A N     1 
ATOM   2203 C  CA    . ARG A 1 287 ? 18.115  -31.908 22.269 1.00 50.78  ? 1504 ARG A CA    1 
ATOM   2204 C  C     . ARG A 1 287 ? 17.754  -30.442 22.205 1.00 52.90  ? 1504 ARG A C     1 
ATOM   2205 O  O     . ARG A 1 287 ? 17.361  -29.877 23.224 1.00 61.52  ? 1504 ARG A O     1 
ATOM   2206 C  CB    . ARG A 1 287 ? 19.401  -32.095 23.055 1.00 55.73  ? 1504 ARG A CB    1 
ATOM   2207 C  CG    . ARG A 1 287 ? 19.689  -33.542 23.332 1.00 54.56  ? 1504 ARG A CG    1 
ATOM   2208 C  CD    . ARG A 1 287 ? 20.654  -33.674 24.476 1.00 63.61  ? 1504 ARG A CD    1 
ATOM   2209 N  NE    . ARG A 1 287 ? 21.777  -34.510 24.083 1.00 78.22  ? 1504 ARG A NE    1 
ATOM   2210 C  CZ    . ARG A 1 287 ? 21.700  -35.820 23.876 1.00 94.80  ? 1504 ARG A CZ    1 
ATOM   2211 N  NH1   . ARG A 1 287 ? 20.545  -36.457 24.031 1.00 102.31 ? 1504 ARG A NH1   1 
ATOM   2212 N  NH2   . ARG A 1 287 ? 22.786  -36.483 23.506 1.00 95.60  ? 1504 ARG A NH2   1 
ATOM   2213 N  N     . VAL A 1 288 ? 17.813  -29.855 21.014 1.00 51.36  ? 1505 VAL A N     1 
ATOM   2214 C  CA    . VAL A 1 288 ? 17.382  -28.483 20.760 1.00 37.44  ? 1505 VAL A CA    1 
ATOM   2215 C  C     . VAL A 1 288 ? 16.234  -28.405 19.765 1.00 49.59  ? 1505 VAL A C     1 
ATOM   2216 O  O     . VAL A 1 288 ? 15.759  -27.285 19.474 1.00 43.39  ? 1505 VAL A O     1 
ATOM   2217 C  CB    . VAL A 1 288 ? 18.548  -27.627 20.241 1.00 31.42  ? 1505 VAL A CB    1 
ATOM   2218 C  CG1   . VAL A 1 288 ? 19.792  -27.819 21.121 1.00 47.84  ? 1505 VAL A CG1   1 
ATOM   2219 C  CG2   . VAL A 1 288 ? 18.804  -27.938 18.765 1.00 31.85  ? 1505 VAL A CG2   1 
ATOM   2220 N  N     . ALA A 1 289 ? 15.844  -29.536 19.160 1.00 58.30  ? 1506 ALA A N     1 
ATOM   2221 C  CA    . ALA A 1 289 ? 14.759  -29.561 18.187 1.00 58.90  ? 1506 ALA A CA    1 
ATOM   2222 C  C     . ALA A 1 289 ? 13.484  -29.042 18.829 1.00 70.28  ? 1506 ALA A C     1 
ATOM   2223 O  O     . ALA A 1 289 ? 13.136  -29.439 19.946 1.00 85.79  ? 1506 ALA A O     1 
ATOM   2224 C  CB    . ALA A 1 289 ? 14.560  -30.975 17.657 1.00 47.67  ? 1506 ALA A CB    1 
ATOM   2225 N  N     . CYS A 1 290 ? 12.784  -28.148 18.127 1.00 57.21  ? 1507 CYS A N     1 
ATOM   2226 C  CA    . CYS A 1 290 ? 11.606  -27.535 18.723 1.00 45.06  ? 1507 CYS A CA    1 
ATOM   2227 C  C     . CYS A 1 290 ? 10.469  -28.542 18.832 1.00 44.18  ? 1507 CYS A C     1 
ATOM   2228 O  O     . CYS A 1 290 ? 9.899   -28.731 19.913 1.00 48.78  ? 1507 CYS A O     1 
ATOM   2229 C  CB    . CYS A 1 290 ? 11.176  -26.337 17.881 1.00 48.47  ? 1507 CYS A CB    1 
ATOM   2230 S  SG    . CYS A 1 290 ? 9.599   -25.660 18.387 1.00 62.15  ? 1507 CYS A SG    1 
ATOM   2231 N  N     . ILE A 1 291 ? 10.196  -29.267 17.751 1.00 50.43  ? 1508 ILE A N     1 
ATOM   2232 C  CA    . ILE A 1 291 ? 9.414   -30.504 17.782 1.00 58.55  ? 1508 ILE A CA    1 
ATOM   2233 C  C     . ILE A 1 291 ? 10.395  -31.665 17.640 1.00 51.52  ? 1508 ILE A C     1 
ATOM   2234 O  O     . ILE A 1 291 ? 11.152  -31.730 16.662 1.00 52.33  ? 1508 ILE A O     1 
ATOM   2235 C  CB    . ILE A 1 291 ? 8.362   -30.536 16.654 1.00 59.82  ? 1508 ILE A CB    1 
ATOM   2236 C  CG1   . ILE A 1 291 ? 7.484   -29.286 16.661 1.00 51.91  ? 1508 ILE A CG1   1 
ATOM   2237 C  CG2   . ILE A 1 291 ? 7.488   -31.769 16.742 1.00 56.73  ? 1508 ILE A CG2   1 
ATOM   2238 C  CD1   . ILE A 1 291 ? 6.382   -29.286 15.600 1.00 35.73  ? 1508 ILE A CD1   1 
ATOM   2239 N  N     . GLN A 1 292 ? 10.397  -32.589 18.601 1.00 41.07  ? 1509 GLN A N     1 
ATOM   2240 C  CA    . GLN A 1 292 ? 11.301  -33.729 18.459 1.00 43.74  ? 1509 GLN A CA    1 
ATOM   2241 C  C     . GLN A 1 292 ? 10.663  -34.836 17.633 1.00 50.37  ? 1509 GLN A C     1 
ATOM   2242 O  O     . GLN A 1 292 ? 11.331  -35.479 16.814 1.00 59.44  ? 1509 GLN A O     1 
ATOM   2243 C  CB    . GLN A 1 292 ? 11.681  -34.299 19.827 1.00 40.55  ? 1509 GLN A CB    1 
ATOM   2244 C  CG    . GLN A 1 292 ? 12.555  -33.445 20.688 1.00 50.66  ? 1509 GLN A CG    1 
ATOM   2245 C  CD    . GLN A 1 292 ? 12.711  -34.052 22.062 1.00 58.94  ? 1509 GLN A CD    1 
ATOM   2246 O  OE1   . GLN A 1 292 ? 11.735  -34.500 22.662 1.00 61.16  ? 1509 GLN A OE1   1 
ATOM   2247 N  NE2   . GLN A 1 292 ? 13.940  -34.094 22.561 1.00 60.06  ? 1509 GLN A NE2   1 
ATOM   2248 N  N     . VAL A 1 293 ? 9.373   -35.064 17.846 1.00 50.45  ? 1510 VAL A N     1 
ATOM   2249 C  CA    . VAL A 1 293 ? 8.612   -36.082 17.145 1.00 52.99  ? 1510 VAL A CA    1 
ATOM   2250 C  C     . VAL A 1 293 ? 7.382   -35.419 16.540 1.00 69.23  ? 1510 VAL A C     1 
ATOM   2251 O  O     . VAL A 1 293 ? 6.664   -34.692 17.235 1.00 76.61  ? 1510 VAL A O     1 
ATOM   2252 C  CB    . VAL A 1 293 ? 8.201   -37.234 18.078 1.00 39.14  ? 1510 VAL A CB    1 
ATOM   2253 C  CG1   . VAL A 1 293 ? 7.692   -38.358 17.253 1.00 40.38  ? 1510 VAL A CG1   1 
ATOM   2254 C  CG2   . VAL A 1 293 ? 9.355   -37.688 18.920 1.00 39.23  ? 1510 VAL A CG2   1 
ATOM   2255 N  N     . VAL A 1 294 ? 7.109   -35.700 15.266 1.00 66.31  ? 1511 VAL A N     1 
ATOM   2256 C  CA    . VAL A 1 294 ? 5.847   -35.309 14.648 1.00 61.76  ? 1511 VAL A CA    1 
ATOM   2257 C  C     . VAL A 1 294 ? 5.114   -36.578 14.229 1.00 64.32  ? 1511 VAL A C     1 
ATOM   2258 O  O     . VAL A 1 294 ? 5.698   -37.480 13.614 1.00 60.95  ? 1511 VAL A O     1 
ATOM   2259 C  CB    . VAL A 1 294 ? 6.033   -34.336 13.460 1.00 50.73  ? 1511 VAL A CB    1 
ATOM   2260 C  CG1   . VAL A 1 294 ? 7.102   -34.834 12.470 1.00 45.35  ? 1511 VAL A CG1   1 
ATOM   2261 C  CG2   . VAL A 1 294 ? 4.691   -34.084 12.746 1.00 38.53  ? 1511 VAL A CG2   1 
ATOM   2262 N  N     . ILE A 1 295 ? 3.854   -36.652 14.632 1.00 62.78  ? 1512 ILE A N     1 
ATOM   2263 C  CA    . ILE A 1 295 ? 2.944   -37.752 14.351 1.00 56.70  ? 1512 ILE A CA    1 
ATOM   2264 C  C     . ILE A 1 295 ? 2.171   -37.439 13.067 1.00 61.23  ? 1512 ILE A C     1 
ATOM   2265 O  O     . ILE A 1 295 ? 1.582   -36.363 12.942 1.00 74.13  ? 1512 ILE A O     1 
ATOM   2266 C  CB    . ILE A 1 295 ? 2.000   -37.941 15.554 1.00 46.07  ? 1512 ILE A CB    1 
ATOM   2267 C  CG1   . ILE A 1 295 ? 2.772   -38.556 16.727 1.00 41.86  ? 1512 ILE A CG1   1 
ATOM   2268 C  CG2   . ILE A 1 295 ? 0.744   -38.701 15.194 1.00 43.80  ? 1512 ILE A CG2   1 
ATOM   2269 C  CD1   . ILE A 1 295 ? 1.932   -38.824 17.965 1.00 42.15  ? 1512 ILE A CD1   1 
ATOM   2270 N  N     . VAL A 1 296 ? 2.160   -38.375 12.117 1.00 57.79  ? 1513 VAL A N     1 
ATOM   2271 C  CA    . VAL A 1 296 ? 1.516   -38.212 10.810 1.00 54.89  ? 1513 VAL A CA    1 
ATOM   2272 C  C     . VAL A 1 296 ? 0.591   -39.382 10.468 1.00 64.02  ? 1513 VAL A C     1 
ATOM   2273 O  O     . VAL A 1 296 ? 1.091   -40.443 10.087 1.00 71.41  ? 1513 VAL A O     1 
ATOM   2274 C  CB    . VAL A 1 296 ? 2.579   -38.060 9.708  1.00 60.59  ? 1513 VAL A CB    1 
ATOM   2275 C  CG1   . VAL A 1 296 ? 1.922   -37.873 8.346  1.00 67.81  ? 1513 VAL A CG1   1 
ATOM   2276 C  CG2   . VAL A 1 296 ? 3.520   -36.912 10.024 1.00 57.27  ? 1513 VAL A CG2   1 
ATOM   2277 N  N     . PRO A 1 297 ? -0.736  -39.242 10.549 1.00 66.84  ? 1514 PRO A N     1 
ATOM   2278 C  CA    . PRO A 1 297 ? -1.653  -40.365 10.231 1.00 58.88  ? 1514 PRO A CA    1 
ATOM   2279 C  C     . PRO A 1 297 ? -1.620  -40.769 8.754  1.00 70.30  ? 1514 PRO A C     1 
ATOM   2280 O  O     . PRO A 1 297 ? -1.048  -40.073 7.916  1.00 86.58  ? 1514 PRO A O     1 
ATOM   2281 C  CB    . PRO A 1 297 ? -3.029  -39.830 10.649 1.00 48.20  ? 1514 PRO A CB    1 
ATOM   2282 C  CG    . PRO A 1 297 ? -2.860  -38.358 10.798 1.00 48.96  ? 1514 PRO A CG    1 
ATOM   2283 C  CD    . PRO A 1 297 ? -1.437  -38.121 11.197 1.00 59.33  ? 1514 PRO A CD    1 
ATOM   2284 N  N     . CYS A 1 298 ? -2.208  -41.954 8.431  1.00 74.64  ? 1515 CYS A N     1 
ATOM   2285 C  CA    . CYS A 1 298 ? -1.981  -42.543 7.104  1.00 79.50  ? 1515 CYS A CA    1 
ATOM   2286 C  C     . CYS A 1 298 ? -3.219  -43.153 6.424  1.00 90.48  ? 1515 CYS A C     1 
ATOM   2287 O  O     . CYS A 1 298 ? -3.090  -44.127 5.673  1.00 73.33  ? 1515 CYS A O     1 
ATOM   2288 C  CB    . CYS A 1 298 ? -0.914  -43.637 7.206  1.00 85.97  ? 1515 CYS A CB    1 
ATOM   2289 S  SG    . CYS A 1 298 ? 0.719   -43.028 7.671  1.00 85.03  ? 1515 CYS A SG    1 
ATOM   2290 N  N     . GLY A 1 299 ? -4.401  -42.604 6.603  1.00 115.30 ? 1516 GLY A N     1 
ATOM   2291 C  CA    . GLY A 1 299 ? -5.599  -43.088 5.917  1.00 114.00 ? 1516 GLY A CA    1 
ATOM   2292 C  C     . GLY A 1 299 ? -6.284  -41.951 5.186  1.00 98.65  ? 1516 GLY A C     1 
ATOM   2293 O  O     . GLY A 1 299 ? -6.451  -40.870 5.748  1.00 83.92  ? 1516 GLY A O     1 
ATOM   2294 N  N     . ILE A 1 300 ? -6.715  -42.213 3.941  1.00 94.24  ? 1517 ILE A N     1 
ATOM   2295 C  CA    . ILE A 1 300 ? -7.151  -41.081 3.125  1.00 87.60  ? 1517 ILE A CA    1 
ATOM   2296 C  C     . ILE A 1 300 ? -8.099  -41.402 1.964  1.00 75.39  ? 1517 ILE A C     1 
ATOM   2297 O  O     . ILE A 1 300 ? -8.420  -42.573 1.693  1.00 62.84  ? 1517 ILE A O     1 
ATOM   2298 C  CB    . ILE A 1 300 ? -5.908  -40.334 2.590  1.00 78.94  ? 1517 ILE A CB    1 
ATOM   2299 N  N     . THR A 1 301 ? -8.558  -40.309 1.300  1.00 69.40  ? 1518 THR A N     1 
ATOM   2300 C  CA    . THR A 1 301 ? -9.398  -40.189 0.103  1.00 73.27  ? 1518 THR A CA    1 
ATOM   2301 C  C     . THR A 1 301 ? -10.854 -40.616 0.289  1.00 86.43  ? 1518 THR A C     1 
ATOM   2302 O  O     . THR A 1 301 ? -11.569 -40.068 1.136  1.00 91.17  ? 1518 THR A O     1 
ATOM   2303 C  CB    . THR A 1 301 ? -8.769  -40.948 -1.070 1.00 75.62  ? 1518 THR A CB    1 
ATOM   2304 N  N     . ALA A 1 302 ? -11.316 -41.545 -0.557 1.00 95.76  ? 1519 ALA A N     1 
ATOM   2305 C  CA    . ALA A 1 302 ? -12.674 -42.079 -0.459 1.00 96.40  ? 1519 ALA A CA    1 
ATOM   2306 C  C     . ALA A 1 302 ? -12.868 -42.896 0.812  1.00 102.58 ? 1519 ALA A C     1 
ATOM   2307 O  O     . ALA A 1 302 ? -13.944 -42.872 1.415  1.00 100.44 ? 1519 ALA A O     1 
ATOM   2308 C  CB    . ALA A 1 302 ? -12.987 -42.933 -1.686 1.00 91.66  ? 1519 ALA A CB    1 
ATOM   2309 N  N     . THR A 1 303 ? -11.836 -43.622 1.235  1.00 117.71 ? 1520 THR A N     1 
ATOM   2310 C  CA    . THR A 1 303 ? -11.905 -44.502 2.403  1.00 128.08 ? 1520 THR A CA    1 
ATOM   2311 C  C     . THR A 1 303 ? -11.818 -43.660 3.678  1.00 121.45 ? 1520 THR A C     1 
ATOM   2312 O  O     . THR A 1 303 ? -10.811 -43.629 4.389  1.00 110.83 ? 1520 THR A O     1 
ATOM   2313 C  CB    . THR A 1 303 ? -10.809 -45.556 2.350  1.00 133.38 ? 1520 THR A CB    1 
ATOM   2314 N  N     . THR A 1 304 ? -12.863 -42.858 3.880  1.00 122.91 ? 1521 THR A N     1 
ATOM   2315 C  CA    . THR A 1 304 ? -12.954 -41.974 5.033  1.00 122.54 ? 1521 THR A CA    1 
ATOM   2316 C  C     . THR A 1 304 ? -14.281 -42.184 5.772  1.00 117.23 ? 1521 THR A C     1 
ATOM   2317 O  O     . THR A 1 304 ? -15.093 -41.262 5.869  1.00 125.07 ? 1521 THR A O     1 
ATOM   2318 C  CB    . THR A 1 304 ? -12.800 -40.514 4.607  1.00 118.61 ? 1521 THR A CB    1 
ATOM   2319 N  N     . THR A 1 305 ? -14.501 -43.381 6.309  1.00 101.02 ? 1522 THR A N     1 
ATOM   2320 C  CA    . THR A 1 305 ? -15.677 -43.555 7.130  1.00 91.54  ? 1522 THR A CA    1 
ATOM   2321 C  C     . THR A 1 305 ? -15.185 -42.709 8.252  1.00 107.08 ? 1522 THR A C     1 
ATOM   2322 O  O     . THR A 1 305 ? -14.336 -43.144 9.009  1.00 122.00 ? 1522 THR A O     1 
ATOM   2323 C  CB    . THR A 1 305 ? -15.831 -44.972 7.666  1.00 75.31  ? 1522 THR A CB    1 
ATOM   2324 N  N     . ASP A 1 306 ? -15.813 -41.550 8.471  1.00 105.54 ? 1523 ASP A N     1 
ATOM   2325 C  CA    . ASP A 1 306 ? -15.341 -40.527 9.434  1.00 96.39  ? 1523 ASP A CA    1 
ATOM   2326 C  C     . ASP A 1 306 ? -15.128 -41.014 10.838 1.00 91.21  ? 1523 ASP A C     1 
ATOM   2327 O  O     . ASP A 1 306 ? -14.366 -40.429 11.542 1.00 63.89  ? 1523 ASP A O     1 
ATOM   2328 C  CB    . ASP A 1 306 ? -16.216 -39.267 9.434  1.00 94.46  ? 1523 ASP A CB    1 
ATOM   2329 C  CG    . ASP A 1 306 ? -15.796 -38.252 8.396  1.00 84.74  ? 1523 ASP A CG    1 
ATOM   2330 O  OD1   . ASP A 1 306 ? -15.156 -37.259 8.745  1.00 67.56  ? 1523 ASP A OD1   1 
ATOM   2331 O  OD2   . ASP A 1 306 ? -16.116 -38.451 7.226  1.00 89.09  ? 1523 ASP A OD2   1 
ATOM   2332 N  N     . ASP A 1 307 ? -15.910 -41.985 11.275 1.00 113.85 ? 1524 ASP A N     1 
ATOM   2333 C  CA    . ASP A 1 307 ? -15.694 -42.707 12.506 1.00 120.17 ? 1524 ASP A CA    1 
ATOM   2334 C  C     . ASP A 1 307 ? -14.280 -43.281 12.494 1.00 121.01 ? 1524 ASP A C     1 
ATOM   2335 O  O     . ASP A 1 307 ? -13.608 -43.202 13.482 1.00 126.73 ? 1524 ASP A O     1 
ATOM   2336 C  CB    . ASP A 1 307 ? -16.704 -43.827 12.578 1.00 122.61 ? 1524 ASP A CB    1 
ATOM   2337 C  CG    . ASP A 1 307 ? -16.354 -44.860 13.582 1.00 129.90 ? 1524 ASP A CG    1 
ATOM   2338 O  OD1   . ASP A 1 307 ? -15.350 -45.558 13.432 1.00 130.90 ? 1524 ASP A OD1   1 
ATOM   2339 O  OD2   . ASP A 1 307 ? -17.133 -45.036 14.512 1.00 134.41 ? 1524 ASP A OD2   1 
ATOM   2340 N  N     . GLU A 1 308 ? -13.829 -43.915 11.422 1.00 107.35 ? 1525 GLU A N     1 
ATOM   2341 C  CA    . GLU A 1 308 ? -12.447 -44.383 11.430 1.00 92.86  ? 1525 GLU A CA    1 
ATOM   2342 C  C     . GLU A 1 308 ? -11.456 -43.221 11.459 1.00 95.59  ? 1525 GLU A C     1 
ATOM   2343 O  O     . GLU A 1 308 ? -10.396 -43.338 12.083 1.00 102.76 ? 1525 GLU A O     1 
ATOM   2344 C  CB    . GLU A 1 308 ? -12.181 -45.294 10.231 1.00 81.88  ? 1525 GLU A CB    1 
ATOM   2345 N  N     . ARG A 1 309 ? -11.770 -42.093 10.805 1.00 89.59  ? 1526 ARG A N     1 
ATOM   2346 C  CA    . ARG A 1 309 ? -10.858 -40.945 10.846 1.00 83.79  ? 1526 ARG A CA    1 
ATOM   2347 C  C     . ARG A 1 309 ? -10.787 -40.344 12.245 1.00 85.92  ? 1526 ARG A C     1 
ATOM   2348 O  O     . ARG A 1 309 ? -9.707  -39.951 12.707 1.00 80.17  ? 1526 ARG A O     1 
ATOM   2349 C  CB    . ARG A 1 309 ? -11.287 -39.887 9.827  1.00 79.47  ? 1526 ARG A CB    1 
ATOM   2350 N  N     . ARG A 1 310 ? -11.922 -40.299 12.948 1.00 97.54  ? 1527 ARG A N     1 
ATOM   2351 C  CA    . ARG A 1 310 ? -11.928 -39.819 14.324 1.00 94.00  ? 1527 ARG A CA    1 
ATOM   2352 C  C     . ARG A 1 310 ? -11.220 -40.806 15.240 1.00 82.77  ? 1527 ARG A C     1 
ATOM   2353 O  O     . ARG A 1 310 ? -10.522 -40.400 16.174 1.00 81.89  ? 1527 ARG A O     1 
ATOM   2354 C  CB    . ARG A 1 310 ? -13.363 -39.571 14.795 1.00 98.59  ? 1527 ARG A CB    1 
ATOM   2355 N  N     . ARG A 1 311 ? -11.386 -42.109 14.991 1.00 74.19  ? 1528 ARG A N     1 
ATOM   2356 C  CA    . ARG A 1 311 ? -10.686 -43.108 15.795 1.00 75.56  ? 1528 ARG A CA    1 
ATOM   2357 C  C     . ARG A 1 311 ? -9.173  -42.966 15.638 1.00 83.08  ? 1528 ARG A C     1 
ATOM   2358 O  O     . ARG A 1 311 ? -8.416  -43.005 16.625 1.00 90.31  ? 1528 ARG A O     1 
ATOM   2359 C  CB    . ARG A 1 311 ? -11.155 -44.514 15.395 1.00 68.70  ? 1528 ARG A CB    1 
ATOM   2360 N  N     . LEU A 1 312 ? -8.728  -42.754 14.401 1.00 81.08  ? 1529 LEU A N     1 
ATOM   2361 C  CA    . LEU A 1 312 ? -7.318  -42.533 14.135 1.00 78.81  ? 1529 LEU A CA    1 
ATOM   2362 C  C     . LEU A 1 312 ? -6.818  -41.289 14.841 1.00 68.18  ? 1529 LEU A C     1 
ATOM   2363 O  O     . LEU A 1 312 ? -5.771  -41.309 15.500 1.00 70.85  ? 1529 LEU A O     1 
ATOM   2364 C  CB    . LEU A 1 312 ? -7.094  -42.394 12.635 1.00 84.00  ? 1529 LEU A CB    1 
ATOM   2365 C  CG    . LEU A 1 312 ? -5.632  -42.190 12.272 1.00 80.57  ? 1529 LEU A CG    1 
ATOM   2366 C  CD1   . LEU A 1 312 ? -4.898  -43.342 12.872 1.00 74.73  ? 1529 LEU A CD1   1 
ATOM   2367 C  CD2   . LEU A 1 312 ? -5.461  -42.214 10.783 1.00 86.16  ? 1529 LEU A CD2   1 
ATOM   2368 N  N     . TYR A 1 313 ? -7.543  -40.185 14.706 1.00 70.64  ? 1530 TYR A N     1 
ATOM   2369 C  CA    . TYR A 1 313 ? -7.069  -38.950 15.322 1.00 76.78  ? 1530 TYR A CA    1 
ATOM   2370 C  C     . TYR A 1 313 ? -7.036  -39.064 16.844 1.00 79.29  ? 1530 TYR A C     1 
ATOM   2371 O  O     . TYR A 1 313 ? -6.077  -38.613 17.480 1.00 66.61  ? 1530 TYR A O     1 
ATOM   2372 C  CB    . TYR A 1 313 ? -7.935  -37.768 14.881 1.00 72.93  ? 1530 TYR A CB    1 
ATOM   2373 N  N     . GLU A 1 314 ? -8.046  -39.702 17.447 1.00 92.64  ? 1531 GLU A N     1 
ATOM   2374 C  CA    . GLU A 1 314 ? -8.107  -39.776 18.905 1.00 86.20  ? 1531 GLU A CA    1 
ATOM   2375 C  C     . GLU A 1 314 ? -6.985  -40.652 19.474 1.00 73.76  ? 1531 GLU A C     1 
ATOM   2376 O  O     . GLU A 1 314 ? -6.361  -40.295 20.490 1.00 69.94  ? 1531 GLU A O     1 
ATOM   2377 C  CB    . GLU A 1 314 ? -9.484  -40.312 19.308 1.00 94.22  ? 1531 GLU A CB    1 
ATOM   2378 C  CG    . GLU A 1 314 ? -9.820  -40.239 20.789 1.00 109.63 ? 1531 GLU A CG    1 
ATOM   2379 C  CD    . GLU A 1 314 ? -10.817 -41.319 21.227 1.00 120.33 ? 1531 GLU A CD    1 
ATOM   2380 O  OE1   . GLU A 1 314 ? -10.692 -41.811 22.369 1.00 123.77 ? 1531 GLU A OE1   1 
ATOM   2381 O  OE2   . GLU A 1 314 ? -11.723 -41.678 20.441 1.00 122.22 ? 1531 GLU A OE2   1 
ATOM   2382 N  N     . SER A 1 315 ? -6.616  -41.732 18.765 1.00 58.20  ? 1532 SER A N     1 
ATOM   2383 C  CA    . SER A 1 315 ? -5.488  -42.539 19.234 1.00 54.98  ? 1532 SER A CA    1 
ATOM   2384 C  C     . SER A 1 315 ? -4.149  -41.827 19.009 1.00 56.50  ? 1532 SER A C     1 
ATOM   2385 O  O     . SER A 1 315 ? -3.226  -41.945 19.828 1.00 62.99  ? 1532 SER A O     1 
ATOM   2386 C  CB    . SER A 1 315 ? -5.515  -43.899 18.531 1.00 63.58  ? 1532 SER A CB    1 
ATOM   2387 O  OG    . SER A 1 315 ? -4.272  -44.575 18.641 1.00 57.10  ? 1532 SER A OG    1 
ATOM   2388 N  N     . CYS A 1 316 ? -4.027  -41.044 17.941 1.00 57.30  ? 1533 CYS A N     1 
ATOM   2389 C  CA    . CYS A 1 316 ? -2.791  -40.297 17.754 1.00 58.48  ? 1533 CYS A CA    1 
ATOM   2390 C  C     . CYS A 1 316 ? -2.638  -39.200 18.796 1.00 68.16  ? 1533 CYS A C     1 
ATOM   2391 O  O     . CYS A 1 316 ? -1.522  -38.906 19.241 1.00 73.91  ? 1533 CYS A O     1 
ATOM   2392 C  CB    . CYS A 1 316 ? -2.751  -39.685 16.371 1.00 64.18  ? 1533 CYS A CB    1 
ATOM   2393 S  SG    . CYS A 1 316 ? -2.379  -40.900 15.153 1.00 72.37  ? 1533 CYS A SG    1 
ATOM   2394 N  N     . ARG A 1 317 ? -3.744  -38.575 19.188 1.00 71.33  ? 1534 ARG A N     1 
ATOM   2395 C  CA    . ARG A 1 317 ? -3.634  -37.579 20.244 1.00 70.96  ? 1534 ARG A CA    1 
ATOM   2396 C  C     . ARG A 1 317 ? -3.264  -38.244 21.560 1.00 60.91  ? 1534 ARG A C     1 
ATOM   2397 O  O     . ARG A 1 317 ? -2.461  -37.692 22.322 1.00 48.94  ? 1534 ARG A O     1 
ATOM   2398 C  CB    . ARG A 1 317 ? -4.930  -36.773 20.357 1.00 76.25  ? 1534 ARG A CB    1 
ATOM   2399 C  CG    . ARG A 1 317 ? -5.026  -35.627 19.325 1.00 85.31  ? 1534 ARG A CG    1 
ATOM   2400 C  CD    . ARG A 1 317 ? -6.374  -34.870 19.376 1.00 93.05  ? 1534 ARG A CD    1 
ATOM   2401 N  NE    . ARG A 1 317 ? -7.028  -34.763 18.060 1.00 92.06  ? 1534 ARG A NE    1 
ATOM   2402 C  CZ    . ARG A 1 317 ? -8.305  -35.075 17.809 1.00 90.79  ? 1534 ARG A CZ    1 
ATOM   2403 N  NH1   . ARG A 1 317 ? -9.099  -35.514 18.785 1.00 86.03  ? 1534 ARG A NH1   1 
ATOM   2404 N  NH2   . ARG A 1 317 ? -8.798  -34.939 16.578 1.00 86.15  ? 1534 ARG A NH2   1 
ATOM   2405 N  N     . GLU A 1 318 ? -3.754  -39.469 21.792 1.00 56.83  ? 1535 GLU A N     1 
ATOM   2406 C  CA    . GLU A 1 318 ? -3.349  -40.202 22.993 1.00 54.84  ? 1535 GLU A CA    1 
ATOM   2407 C  C     . GLU A 1 318 ? -1.853  -40.510 22.995 1.00 55.09  ? 1535 GLU A C     1 
ATOM   2408 O  O     . GLU A 1 318 ? -1.185  -40.348 24.025 1.00 65.76  ? 1535 GLU A O     1 
ATOM   2409 C  CB    . GLU A 1 318 ? -4.155  -41.494 23.108 1.00 60.96  ? 1535 GLU A CB    1 
ATOM   2410 C  CG    . GLU A 1 318 ? -3.526  -42.598 23.950 1.00 68.18  ? 1535 GLU A CG    1 
ATOM   2411 C  CD    . GLU A 1 318 ? -4.373  -43.873 23.952 1.00 73.82  ? 1535 GLU A CD    1 
ATOM   2412 O  OE1   . GLU A 1 318 ? -4.223  -44.683 24.891 1.00 69.67  ? 1535 GLU A OE1   1 
ATOM   2413 O  OE2   . GLU A 1 318 ? -5.181  -44.073 23.011 1.00 73.34  ? 1535 GLU A OE2   1 
ATOM   2414 N  N     . LEU A 1 319 ? -1.301  -40.937 21.853 1.00 48.38  ? 1536 LEU A N     1 
ATOM   2415 C  CA    . LEU A 1 319 ? 0.137   -41.212 21.794 1.00 46.79  ? 1536 LEU A CA    1 
ATOM   2416 C  C     . LEU A 1 319 ? 0.969   -39.942 21.977 1.00 65.46  ? 1536 LEU A C     1 
ATOM   2417 O  O     . LEU A 1 319 ? 1.955   -39.934 22.729 1.00 67.12  ? 1536 LEU A O     1 
ATOM   2418 C  CB    . LEU A 1 319 ? 0.500   -41.900 20.488 1.00 45.41  ? 1536 LEU A CB    1 
ATOM   2419 C  CG    . LEU A 1 319 ? 1.940   -42.439 20.443 1.00 51.56  ? 1536 LEU A CG    1 
ATOM   2420 C  CD1   . LEU A 1 319 ? 2.060   -43.764 21.155 1.00 46.81  ? 1536 LEU A CD1   1 
ATOM   2421 C  CD2   . LEU A 1 319 ? 2.481   -42.542 19.014 1.00 47.93  ? 1536 LEU A CD2   1 
ATOM   2422 N  N     . GLU A 1 320 ? 0.584   -38.832 21.357 1.00 76.25  ? 1537 GLU A N     1 
ATOM   2423 C  CA    . GLU A 1 320 ? 1.373   -37.611 21.552 1.00 72.88  ? 1537 GLU A CA    1 
ATOM   2424 C  C     . GLU A 1 320 ? 1.216   -37.065 22.951 1.00 70.02  ? 1537 GLU A C     1 
ATOM   2425 O  O     . GLU A 1 320 ? 2.128   -36.426 23.475 1.00 65.25  ? 1537 GLU A O     1 
ATOM   2426 C  CB    . GLU A 1 320 ? 1.045   -36.538 20.497 1.00 64.67  ? 1537 GLU A CB    1 
ATOM   2427 C  CG    . GLU A 1 320 ? -0.218  -35.726 20.752 1.00 65.63  ? 1537 GLU A CG    1 
ATOM   2428 C  CD    . GLU A 1 320 ? -0.265  -34.436 19.945 1.00 65.41  ? 1537 GLU A CD    1 
ATOM   2429 O  OE1   . GLU A 1 320 ? 0.679   -33.617 20.043 1.00 61.74  ? 1537 GLU A OE1   1 
ATOM   2430 O  OE2   . GLU A 1 320 ? -1.259  -34.233 19.217 1.00 66.92  ? 1537 GLU A OE2   1 
ATOM   2431 N  N     . GLN A 1 321 ? 0.066   -37.308 23.566 1.00 69.35  ? 1538 GLN A N     1 
ATOM   2432 C  CA    . GLN A 1 321 ? -0.092  -36.811 24.924 1.00 56.73  ? 1538 GLN A CA    1 
ATOM   2433 C  C     . GLN A 1 321 ? 0.791   -37.590 25.883 1.00 49.98  ? 1538 GLN A C     1 
ATOM   2434 O  O     . GLN A 1 321 ? 1.526   -37.000 26.696 1.00 40.34  ? 1538 GLN A O     1 
ATOM   2435 C  CB    . GLN A 1 321 ? -1.560  -36.934 25.341 1.00 57.85  ? 1538 GLN A CB    1 
ATOM   2436 C  CG    . GLN A 1 321 ? -2.386  -35.648 25.166 1.00 79.39  ? 1538 GLN A CG    1 
ATOM   2437 C  CD    . GLN A 1 321 ? -1.658  -34.369 25.646 1.00 97.34  ? 1538 GLN A CD    1 
ATOM   2438 O  OE1   . GLN A 1 321 ? -1.364  -34.199 26.837 1.00 100.53 ? 1538 GLN A OE1   1 
ATOM   2439 N  NE2   . GLN A 1 321 ? -1.384  -33.463 24.710 1.00 101.22 ? 1538 GLN A NE2   1 
ATOM   2440 N  N     . THR A 1 322 ? 0.776   -38.919 25.756 1.00 52.78  ? 1539 THR A N     1 
ATOM   2441 C  CA    . THR A 1 322 ? 1.640   -39.756 26.578 1.00 60.52  ? 1539 THR A CA    1 
ATOM   2442 C  C     . THR A 1 322 ? 3.112   -39.497 26.293 1.00 59.81  ? 1539 THR A C     1 
ATOM   2443 O  O     . THR A 1 322 ? 3.963   -39.709 27.166 1.00 48.20  ? 1539 THR A O     1 
ATOM   2444 C  CB    . THR A 1 322 ? 1.286   -41.214 26.335 1.00 59.25  ? 1539 THR A CB    1 
ATOM   2445 O  OG1   . THR A 1 322 ? 1.268   -41.445 24.926 1.00 67.36  ? 1539 THR A OG1   1 
ATOM   2446 C  CG2   . THR A 1 322 ? -0.098  -41.497 26.884 1.00 52.14  ? 1539 THR A CG2   1 
ATOM   2447 N  N     . PHE A 1 323 ? 3.430   -39.003 25.094 1.00 62.26  ? 1540 PHE A N     1 
ATOM   2448 C  CA    . PHE A 1 323 ? 4.802   -38.575 24.830 1.00 66.52  ? 1540 PHE A CA    1 
ATOM   2449 C  C     . PHE A 1 323 ? 5.156   -37.264 25.530 1.00 68.14  ? 1540 PHE A C     1 
ATOM   2450 O  O     . PHE A 1 323 ? 6.271   -37.120 26.044 1.00 74.44  ? 1540 PHE A O     1 
ATOM   2451 C  CB    . PHE A 1 323 ? 5.030   -38.444 23.336 1.00 60.90  ? 1540 PHE A CB    1 
ATOM   2452 C  CG    . PHE A 1 323 ? 5.524   -39.681 22.717 1.00 60.45  ? 1540 PHE A CG    1 
ATOM   2453 C  CD1   . PHE A 1 323 ? 6.459   -40.460 23.365 1.00 62.49  ? 1540 PHE A CD1   1 
ATOM   2454 C  CD2   . PHE A 1 323 ? 5.040   -40.091 21.489 1.00 67.65  ? 1540 PHE A CD2   1 
ATOM   2455 C  CE1   . PHE A 1 323 ? 6.918   -41.641 22.783 1.00 72.96  ? 1540 PHE A CE1   1 
ATOM   2456 C  CE2   . PHE A 1 323 ? 5.492   -41.260 20.899 1.00 73.52  ? 1540 PHE A CE2   1 
ATOM   2457 C  CZ    . PHE A 1 323 ? 6.435   -42.041 21.547 1.00 73.62  ? 1540 PHE A CZ    1 
ATOM   2458 N  N     . VAL A 1 324 ? 4.264   -36.270 25.510 1.00 57.88  ? 1541 VAL A N     1 
ATOM   2459 C  CA    . VAL A 1 324 ? 4.625   -35.013 26.156 1.00 63.70  ? 1541 VAL A CA    1 
ATOM   2460 C  C     . VAL A 1 324 ? 4.764   -35.211 27.662 1.00 74.58  ? 1541 VAL A C     1 
ATOM   2461 O  O     . VAL A 1 324 ? 5.687   -34.666 28.283 1.00 75.22  ? 1541 VAL A O     1 
ATOM   2462 C  CB    . VAL A 1 324 ? 3.647   -33.870 25.807 1.00 67.74  ? 1541 VAL A CB    1 
ATOM   2463 C  CG1   . VAL A 1 324 ? 3.494   -33.698 24.286 1.00 59.59  ? 1541 VAL A CG1   1 
ATOM   2464 C  CG2   . VAL A 1 324 ? 2.305   -34.040 26.508 1.00 80.04  ? 1541 VAL A CG2   1 
ATOM   2465 N  N     . LYS A 1 325 ? 3.883   -36.027 28.266 1.00 75.49  ? 1542 LYS A N     1 
ATOM   2466 C  CA    . LYS A 1 325 ? 3.970   -36.235 29.713 1.00 70.38  ? 1542 LYS A CA    1 
ATOM   2467 C  C     . LYS A 1 325 ? 5.298   -36.878 30.101 1.00 70.14  ? 1542 LYS A C     1 
ATOM   2468 O  O     . LYS A 1 325 ? 5.843   -36.596 31.176 1.00 67.91  ? 1542 LYS A O     1 
ATOM   2469 C  CB    . LYS A 1 325 ? 2.804   -37.099 30.214 1.00 64.50  ? 1542 LYS A CB    1 
ATOM   2470 C  CG    . LYS A 1 325 ? 2.591   -37.018 31.731 1.00 68.82  ? 1542 LYS A CG    1 
ATOM   2471 C  CD    . LYS A 1 325 ? 3.292   -38.163 32.478 1.00 82.77  ? 1542 LYS A CD    1 
ATOM   2472 C  CE    . LYS A 1 325 ? 3.709   -37.791 33.918 1.00 89.42  ? 1542 LYS A CE    1 
ATOM   2473 N  NZ    . LYS A 1 325 ? 4.994   -37.011 34.011 1.00 86.42  ? 1542 LYS A NZ    1 
ATOM   2474 N  N     . ALA A 1 326 ? 5.854   -37.710 29.229 1.00 75.54  ? 1543 ALA A N     1 
ATOM   2475 C  CA    . ALA A 1 326 ? 7.209   -38.214 29.409 1.00 71.69  ? 1543 ALA A CA    1 
ATOM   2476 C  C     . ALA A 1 326 ? 8.263   -37.221 28.915 1.00 75.15  ? 1543 ALA A C     1 
ATOM   2477 O  O     . ALA A 1 326 ? 9.368   -37.636 28.526 1.00 81.40  ? 1543 ALA A O     1 
ATOM   2478 C  CB    . ALA A 1 326 ? 7.371   -39.573 28.713 1.00 53.33  ? 1543 ALA A CB    1 
ATOM   2479 N  N     . GLY A 1 327 ? 7.910   -35.933 28.885 1.00 63.41  ? 1544 GLY A N     1 
ATOM   2480 C  CA    . GLY A 1 327 ? 8.876   -34.889 28.628 1.00 67.47  ? 1544 GLY A CA    1 
ATOM   2481 C  C     . GLY A 1 327 ? 9.426   -34.852 27.226 1.00 73.78  ? 1544 GLY A C     1 
ATOM   2482 O  O     . GLY A 1 327 ? 10.520  -34.324 27.017 1.00 83.28  ? 1544 GLY A O     1 
ATOM   2483 N  N     . ILE A 1 328 ? 8.731   -35.431 26.259 1.00 70.53  ? 1545 ILE A N     1 
ATOM   2484 C  CA    . ILE A 1 328 ? 9.209   -35.447 24.884 1.00 65.31  ? 1545 ILE A CA    1 
ATOM   2485 C  C     . ILE A 1 328 ? 8.430   -34.410 24.102 1.00 58.24  ? 1545 ILE A C     1 
ATOM   2486 O  O     . ILE A 1 328 ? 7.194   -34.378 24.144 1.00 52.24  ? 1545 ILE A O     1 
ATOM   2487 C  CB    . ILE A 1 328 ? 9.083   -36.840 24.245 1.00 59.86  ? 1545 ILE A CB    1 
ATOM   2488 C  CG1   . ILE A 1 328 ? 10.033  -37.830 24.911 1.00 50.67  ? 1545 ILE A CG1   1 
ATOM   2489 C  CG2   . ILE A 1 328 ? 9.429   -36.772 22.778 1.00 59.39  ? 1545 ILE A CG2   1 
ATOM   2490 C  CD1   . ILE A 1 328 ? 10.037  -39.176 24.239 1.00 49.20  ? 1545 ILE A CD1   1 
ATOM   2491 N  N     . ARG A 1 329 ? 9.146   -33.571 23.380 1.00 60.75  ? 1546 ARG A N     1 
ATOM   2492 C  CA    . ARG A 1 329 ? 8.469   -32.535 22.618 1.00 64.87  ? 1546 ARG A CA    1 
ATOM   2493 C  C     . ARG A 1 329 ? 7.859   -33.201 21.386 1.00 57.60  ? 1546 ARG A C     1 
ATOM   2494 O  O     . ARG A 1 329 ? 8.524   -33.436 20.376 1.00 52.13  ? 1546 ARG A O     1 
ATOM   2495 C  CB    . ARG A 1 329 ? 9.437   -31.398 22.288 1.00 62.01  ? 1546 ARG A CB    1 
ATOM   2496 C  CG    . ARG A 1 329 ? 10.211  -30.852 23.516 1.00 52.44  ? 1546 ARG A CG    1 
ATOM   2497 C  CD    . ARG A 1 329 ? 11.035  -29.580 23.201 1.00 53.19  ? 1546 ARG A CD    1 
ATOM   2498 N  NE    . ARG A 1 329 ? 12.217  -29.798 22.362 1.00 52.29  ? 1546 ARG A NE    1 
ATOM   2499 C  CZ    . ARG A 1 329 ? 13.363  -30.342 22.781 1.00 53.18  ? 1546 ARG A CZ    1 
ATOM   2500 N  NH1   . ARG A 1 329 ? 13.508  -30.745 24.037 1.00 54.47  ? 1546 ARG A NH1   1 
ATOM   2501 N  NH2   . ARG A 1 329 ? 14.376  -30.488 21.938 1.00 48.83  ? 1546 ARG A NH2   1 
ATOM   2502 N  N     . CYS A 1 330 ? 6.586   -33.583 21.503 1.00 55.70  ? 1547 CYS A N     1 
ATOM   2503 C  CA    . CYS A 1 330 ? 5.850   -34.213 20.413 1.00 59.84  ? 1547 CYS A CA    1 
ATOM   2504 C  C     . CYS A 1 330 ? 4.572   -33.431 20.138 1.00 65.81  ? 1547 CYS A C     1 
ATOM   2505 O  O     . CYS A 1 330 ? 3.885   -33.000 21.073 1.00 74.01  ? 1547 CYS A O     1 
ATOM   2506 C  CB    . CYS A 1 330 ? 5.498   -35.675 20.716 1.00 60.55  ? 1547 CYS A CB    1 
ATOM   2507 S  SG    . CYS A 1 330 ? 4.390   -36.455 19.482 1.00 59.43  ? 1547 CYS A SG    1 
ATOM   2508 N  N     . GLU A 1 331 ? 4.262   -33.245 18.854 1.00 59.99  ? 1548 GLU A N     1 
ATOM   2509 C  CA    . GLU A 1 331 ? 2.986   -32.703 18.409 1.00 61.18  ? 1548 GLU A CA    1 
ATOM   2510 C  C     . GLU A 1 331 ? 2.536   -33.539 17.218 1.00 60.49  ? 1548 GLU A C     1 
ATOM   2511 O  O     . GLU A 1 331 ? 3.356   -34.137 16.514 1.00 57.73  ? 1548 GLU A O     1 
ATOM   2512 C  CB    . GLU A 1 331 ? 3.064   -31.189 18.028 1.00 55.40  ? 1548 GLU A CB    1 
ATOM   2513 N  N     . GLY A 1 332 ? 1.231   -33.597 17.006 1.00 57.12  ? 1549 GLY A N     1 
ATOM   2514 C  CA    . GLY A 1 332 ? 0.680   -34.286 15.864 1.00 50.73  ? 1549 GLY A CA    1 
ATOM   2515 C  C     . GLY A 1 332 ? 0.333   -33.257 14.812 1.00 51.97  ? 1549 GLY A C     1 
ATOM   2516 O  O     . GLY A 1 332 ? 0.054   -32.106 15.127 1.00 67.01  ? 1549 GLY A O     1 
ATOM   2517 N  N     . ASP A 1 333 ? 0.336   -33.688 13.564 1.00 39.23  ? 1550 ASP A N     1 
ATOM   2518 C  CA    . ASP A 1 333 ? -0.021  -32.857 12.418 1.00 41.16  ? 1550 ASP A CA    1 
ATOM   2519 C  C     . ASP A 1 333 ? -1.325  -33.430 11.877 1.00 57.06  ? 1550 ASP A C     1 
ATOM   2520 O  O     . ASP A 1 333 ? -1.320  -34.413 11.135 1.00 65.11  ? 1550 ASP A O     1 
ATOM   2521 C  CB    . ASP A 1 333 ? 1.103   -32.881 11.394 1.00 47.47  ? 1550 ASP A CB    1 
ATOM   2522 C  CG    . ASP A 1 333 ? 0.774   -32.135 10.119 1.00 52.35  ? 1550 ASP A CG    1 
ATOM   2523 O  OD1   . ASP A 1 333 ? -0.313  -32.345 9.540  1.00 53.42  ? 1550 ASP A OD1   1 
ATOM   2524 O  OD2   . ASP A 1 333 ? 1.649   -31.368 9.672  1.00 52.58  ? 1550 ASP A OD2   1 
ATOM   2525 N  N     . TYR A 1 334 ? -2.433  -32.822 12.196 1.00 63.37  ? 1551 TYR A N     1 
ATOM   2526 C  CA    . TYR A 1 334 ? -3.674  -33.399 11.752 1.00 71.38  ? 1551 TYR A CA    1 
ATOM   2527 C  C     . TYR A 1 334 ? -4.437  -32.595 10.773 1.00 76.15  ? 1551 TYR A C     1 
ATOM   2528 O  O     . TYR A 1 334 ? -5.642  -32.798 10.621 1.00 94.72  ? 1551 TYR A O     1 
ATOM   2529 C  CB    . TYR A 1 334 ? -4.567  -33.497 12.928 1.00 71.89  ? 1551 TYR A CB    1 
ATOM   2530 C  CG    . TYR A 1 334 ? -3.918  -34.127 14.140 1.00 69.84  ? 1551 TYR A CG    1 
ATOM   2531 C  CD1   . TYR A 1 334 ? -4.023  -35.490 14.379 1.00 69.66  ? 1551 TYR A CD1   1 
ATOM   2532 C  CD2   . TYR A 1 334 ? -3.200  -33.357 15.046 1.00 79.89  ? 1551 TYR A CD2   1 
ATOM   2533 C  CE1   . TYR A 1 334 ? -3.432  -36.070 15.486 1.00 76.64  ? 1551 TYR A CE1   1 
ATOM   2534 C  CE2   . TYR A 1 334 ? -2.605  -33.927 16.155 1.00 83.65  ? 1551 TYR A CE2   1 
ATOM   2535 C  CZ    . TYR A 1 334 ? -2.725  -35.283 16.371 1.00 80.99  ? 1551 TYR A CZ    1 
ATOM   2536 O  OH    . TYR A 1 334 ? -2.134  -35.855 17.474 1.00 89.09  ? 1551 TYR A OH    1 
ATOM   2537 N  N     . ARG A 1 335 ? -3.803  -31.695 10.098 1.00 69.29  ? 1552 ARG A N     1 
ATOM   2538 C  CA    . ARG A 1 335 ? -4.507  -30.877 9.180  1.00 68.34  ? 1552 ARG A CA    1 
ATOM   2539 C  C     . ARG A 1 335 ? -5.100  -31.687 8.046  1.00 73.64  ? 1552 ARG A C     1 
ATOM   2540 O  O     . ARG A 1 335 ? -4.515  -32.581 7.562  1.00 64.64  ? 1552 ARG A O     1 
ATOM   2541 C  CB    . ARG A 1 335 ? -3.537  -29.782 8.762  1.00 63.32  ? 1552 ARG A CB    1 
ATOM   2542 C  CG    . ARG A 1 335 ? -2.849  -29.221 10.003 1.00 57.19  ? 1552 ARG A CG    1 
ATOM   2543 C  CD    . ARG A 1 335 ? -1.714  -28.244 9.789  1.00 59.66  ? 1552 ARG A CD    1 
ATOM   2544 N  NE    . ARG A 1 335 ? -0.816  -28.554 8.694  1.00 61.67  ? 1552 ARG A NE    1 
ATOM   2545 C  CZ    . ARG A 1 335 ? 0.484   -28.331 8.731  1.00 65.60  ? 1552 ARG A CZ    1 
ATOM   2546 N  NH1   . ARG A 1 335 ? 1.018   -27.836 9.808  1.00 69.39  ? 1552 ARG A NH1   1 
ATOM   2547 N  NH2   . ARG A 1 335 ? 1.249   -28.617 7.714  1.00 58.91  ? 1552 ARG A NH2   1 
ATOM   2548 N  N     . ASP A 1 336 ? -6.336  -31.408 7.722  1.00 90.68  ? 1553 ASP A N     1 
ATOM   2549 C  CA    . ASP A 1 336 ? -7.091  -32.043 6.661  1.00 100.10 ? 1553 ASP A CA    1 
ATOM   2550 C  C     . ASP A 1 336 ? -6.706  -31.755 5.268  1.00 96.66  ? 1553 ASP A C     1 
ATOM   2551 O  O     . ASP A 1 336 ? -6.888  -32.547 4.376  1.00 89.01  ? 1553 ASP A O     1 
ATOM   2552 C  CB    . ASP A 1 336 ? -8.519  -31.638 6.786  1.00 110.07 ? 1553 ASP A CB    1 
ATOM   2553 C  CG    . ASP A 1 336 ? -9.174  -32.370 7.839  1.00 122.72 ? 1553 ASP A CG    1 
ATOM   2554 O  OD1   . ASP A 1 336 ? -8.500  -32.612 8.840  1.00 125.05 ? 1553 ASP A OD1   1 
ATOM   2555 O  OD2   . ASP A 1 336 ? -10.328 -32.760 7.658  1.00 129.94 ? 1553 ASP A OD2   1 
ATOM   2556 N  N     . ASN A 1 337 ? -6.240  -30.554 5.078  1.00 97.34  ? 1554 ASN A N     1 
ATOM   2557 C  CA    . ASN A 1 337 ? -5.912  -30.095 3.779  1.00 97.82  ? 1554 ASN A CA    1 
ATOM   2558 C  C     . ASN A 1 337 ? -4.888  -30.901 3.107  1.00 97.35  ? 1554 ASN A C     1 
ATOM   2559 O  O     . ASN A 1 337 ? -5.025  -31.226 1.959  1.00 96.03  ? 1554 ASN A O     1 
ATOM   2560 C  CB    . ASN A 1 337 ? -5.311  -28.715 3.936  1.00 98.57  ? 1554 ASN A CB    1 
ATOM   2561 C  CG    . ASN A 1 337 ? -4.877  -28.094 2.624  1.00 110.39 ? 1554 ASN A CG    1 
ATOM   2562 O  OD1   . ASN A 1 337 ? -4.905  -28.712 1.559  1.00 110.29 ? 1554 ASN A OD1   1 
ATOM   2563 N  ND2   . ASN A 1 337 ? -4.491  -26.823 2.696  1.00 115.00 ? 1554 ASN A ND2   1 
ATOM   2564 N  N     . TYR A 1 338 ? -3.852  -31.243 3.822  1.00 96.46  ? 1555 TYR A N     1 
ATOM   2565 C  CA    . TYR A 1 338 ? -2.770  -31.895 3.192  1.00 95.65  ? 1555 TYR A CA    1 
ATOM   2566 C  C     . TYR A 1 338 ? -2.754  -33.377 3.299  1.00 97.70  ? 1555 TYR A C     1 
ATOM   2567 O  O     . TYR A 1 338 ? -3.400  -33.962 4.133  1.00 100.79 ? 1555 TYR A O     1 
ATOM   2568 C  CB    . TYR A 1 338 ? -1.507  -31.345 3.783  1.00 96.16  ? 1555 TYR A CB    1 
ATOM   2569 C  CG    . TYR A 1 338 ? -1.445  -29.860 3.859  1.00 97.54  ? 1555 TYR A CG    1 
ATOM   2570 C  CD1   . TYR A 1 338 ? -1.812  -29.205 4.989  1.00 100.24 ? 1555 TYR A CD1   1 
ATOM   2571 C  CD2   . TYR A 1 338 ? -0.987  -29.121 2.810  1.00 102.54 ? 1555 TYR A CD2   1 
ATOM   2572 C  CE1   . TYR A 1 338 ? -1.736  -27.844 5.070  1.00 104.92 ? 1555 TYR A CE1   1 
ATOM   2573 C  CE2   . TYR A 1 338 ? -0.916  -27.761 2.878  1.00 105.97 ? 1555 TYR A CE2   1 
ATOM   2574 C  CZ    . TYR A 1 338 ? -1.286  -27.132 4.019  1.00 102.85 ? 1555 TYR A CZ    1 
ATOM   2575 O  OH    . TYR A 1 338 ? -1.216  -25.771 4.107  1.00 91.21  ? 1555 TYR A OH    1 
ATOM   2576 N  N     . SER A 1 339 ? -1.982  -33.966 2.409  1.00 90.39  ? 1556 SER A N     1 
ATOM   2577 C  CA    . SER A 1 339 ? -1.791  -35.402 2.335  1.00 88.52  ? 1556 SER A CA    1 
ATOM   2578 C  C     . SER A 1 339 ? -0.644  -35.828 3.238  1.00 89.92  ? 1556 SER A C     1 
ATOM   2579 O  O     . SER A 1 339 ? 0.226   -35.019 3.579  1.00 99.28  ? 1556 SER A O     1 
ATOM   2580 C  CB    . SER A 1 339 ? -1.509  -35.842 0.896  1.00 92.59  ? 1556 SER A CB    1 
ATOM   2581 O  OG    . SER A 1 339 ? -0.713  -34.907 0.165  1.00 95.43  ? 1556 SER A OG    1 
ATOM   2582 N  N     . PRO A 1 340 ? -0.633  -37.101 3.656  1.00 81.84  ? 1557 PRO A N     1 
ATOM   2583 C  CA    . PRO A 1 340 ? 0.497   -37.614 4.448  1.00 69.12  ? 1557 PRO A CA    1 
ATOM   2584 C  C     . PRO A 1 340 ? 1.853   -37.469 3.770  1.00 70.70  ? 1557 PRO A C     1 
ATOM   2585 O  O     . PRO A 1 340 ? 2.860   -37.248 4.452  1.00 66.86  ? 1557 PRO A O     1 
ATOM   2586 C  CB    . PRO A 1 340 ? 0.122   -39.083 4.653  1.00 68.32  ? 1557 PRO A CB    1 
ATOM   2587 C  CG    . PRO A 1 340 ? -1.365  -39.064 4.669  1.00 77.10  ? 1557 PRO A CG    1 
ATOM   2588 C  CD    . PRO A 1 340 ? -1.801  -37.993 3.714  1.00 81.70  ? 1557 PRO A CD    1 
ATOM   2589 N  N     . GLY A 1 341 ? 1.924   -37.607 2.447  1.00 74.77  ? 1558 GLY A N     1 
ATOM   2590 C  CA    . GLY A 1 341 ? 3.208   -37.464 1.784  1.00 73.76  ? 1558 GLY A CA    1 
ATOM   2591 C  C     . GLY A 1 341 ? 3.701   -36.037 1.803  1.00 72.54  ? 1558 GLY A C     1 
ATOM   2592 O  O     . GLY A 1 341 ? 4.906   -35.783 1.948  1.00 69.76  ? 1558 GLY A O     1 
ATOM   2593 N  N     . TRP A 1 342 ? 2.777   -35.085 1.635  1.00 71.46  ? 1559 TRP A N     1 
ATOM   2594 C  CA    . TRP A 1 342 ? 3.118   -33.680 1.804  1.00 64.50  ? 1559 TRP A CA    1 
ATOM   2595 C  C     . TRP A 1 342 ? 3.671   -33.428 3.197  1.00 56.67  ? 1559 TRP A C     1 
ATOM   2596 O  O     . TRP A 1 342 ? 4.785   -32.920 3.335  1.00 48.94  ? 1559 TRP A O     1 
ATOM   2597 C  CB    . TRP A 1 342 ? 1.901   -32.798 1.532  1.00 69.22  ? 1559 TRP A CB    1 
ATOM   2598 C  CG    . TRP A 1 342 ? 2.208   -31.298 1.549  1.00 74.30  ? 1559 TRP A CG    1 
ATOM   2599 C  CD1   . TRP A 1 342 ? 2.457   -30.491 0.468  1.00 77.87  ? 1559 TRP A CD1   1 
ATOM   2600 C  CD2   . TRP A 1 342 ? 2.282   -30.450 2.701  1.00 61.98  ? 1559 TRP A CD2   1 
ATOM   2601 N  NE1   . TRP A 1 342 ? 2.684   -29.205 0.884  1.00 72.06  ? 1559 TRP A NE1   1 
ATOM   2602 C  CE2   . TRP A 1 342 ? 2.578   -29.155 2.248  1.00 61.86  ? 1559 TRP A CE2   1 
ATOM   2603 C  CE3   . TRP A 1 342 ? 2.129   -30.665 4.069  1.00 55.27  ? 1559 TRP A CE3   1 
ATOM   2604 C  CZ2   . TRP A 1 342 ? 2.724   -28.089 3.111  1.00 56.57  ? 1559 TRP A CZ2   1 
ATOM   2605 C  CZ3   . TRP A 1 342 ? 2.285   -29.610 4.922  1.00 54.29  ? 1559 TRP A CZ3   1 
ATOM   2606 C  CH2   . TRP A 1 342 ? 2.574   -28.337 4.446  1.00 57.78  ? 1559 TRP A CH2   1 
ATOM   2607 N  N     . LYS A 1 343 ? 2.928   -33.835 4.238  1.00 56.30  ? 1560 LYS A N     1 
ATOM   2608 C  CA    . LYS A 1 343 ? 3.385   -33.640 5.616  1.00 58.67  ? 1560 LYS A CA    1 
ATOM   2609 C  C     . LYS A 1 343 ? 4.750   -34.275 5.828  1.00 60.66  ? 1560 LYS A C     1 
ATOM   2610 O  O     . LYS A 1 343 ? 5.608   -33.713 6.516  1.00 59.98  ? 1560 LYS A O     1 
ATOM   2611 C  CB    . LYS A 1 343 ? 2.367   -34.224 6.598  1.00 56.70  ? 1560 LYS A CB    1 
ATOM   2612 C  CG    . LYS A 1 343 ? 0.941   -33.743 6.362  1.00 59.96  ? 1560 LYS A CG    1 
ATOM   2613 C  CD    . LYS A 1 343 ? -0.062  -34.476 7.246  1.00 58.14  ? 1560 LYS A CD    1 
ATOM   2614 C  CE    . LYS A 1 343 ? -1.495  -34.011 6.998  1.00 47.20  ? 1560 LYS A CE    1 
ATOM   2615 N  NZ    . LYS A 1 343 ? -2.376  -34.343 8.150  1.00 42.68  ? 1560 LYS A NZ    1 
ATOM   2616 N  N     . TYR A 1 344 ? 4.963   -35.452 5.242  1.00 70.96  ? 1561 TYR A N     1 
ATOM   2617 C  CA    . TYR A 1 344 ? 6.287   -36.052 5.205  1.00 70.72  ? 1561 TYR A CA    1 
ATOM   2618 C  C     . TYR A 1 344 ? 7.318   -35.039 4.750  1.00 67.80  ? 1561 TYR A C     1 
ATOM   2619 O  O     . TYR A 1 344 ? 8.241   -34.696 5.496  1.00 82.36  ? 1561 TYR A O     1 
ATOM   2620 C  CB    . TYR A 1 344 ? 6.287   -37.254 4.254  1.00 75.28  ? 1561 TYR A CB    1 
ATOM   2621 C  CG    . TYR A 1 344 ? 5.529   -38.444 4.755  1.00 86.35  ? 1561 TYR A CG    1 
ATOM   2622 C  CD1   . TYR A 1 344 ? 5.064   -38.493 6.059  1.00 88.80  ? 1561 TYR A CD1   1 
ATOM   2623 C  CD2   . TYR A 1 344 ? 5.275   -39.527 3.928  1.00 93.56  ? 1561 TYR A CD2   1 
ATOM   2624 C  CE1   . TYR A 1 344 ? 4.373   -39.589 6.532  1.00 90.96  ? 1561 TYR A CE1   1 
ATOM   2625 C  CE2   . TYR A 1 344 ? 4.581   -40.634 4.387  1.00 92.75  ? 1561 TYR A CE2   1 
ATOM   2626 C  CZ    . TYR A 1 344 ? 4.133   -40.658 5.692  1.00 91.54  ? 1561 TYR A CZ    1 
ATOM   2627 O  OH    . TYR A 1 344 ? 3.445   -41.752 6.161  1.00 89.30  ? 1561 TYR A OH    1 
ATOM   2628 N  N     . ASN A 1 345 ? 7.138   -34.507 3.536  1.00 42.46  ? 1562 ASN A N     1 
ATOM   2629 C  CA    . ASN A 1 345 ? 8.171   -33.644 2.968  1.00 44.57  ? 1562 ASN A CA    1 
ATOM   2630 C  C     . ASN A 1 345 ? 8.320   -32.360 3.771  1.00 46.25  ? 1562 ASN A C     1 
ATOM   2631 O  O     . ASN A 1 345 ? 9.432   -31.859 3.961  1.00 45.01  ? 1562 ASN A O     1 
ATOM   2632 C  CB    . ASN A 1 345 ? 7.880   -33.312 1.519  1.00 50.02  ? 1562 ASN A CB    1 
ATOM   2633 C  CG    . ASN A 1 345 ? 8.721   -32.152 1.045  1.00 62.30  ? 1562 ASN A CG    1 
ATOM   2634 O  OD1   . ASN A 1 345 ? 8.225   -31.035 0.860  1.00 62.70  ? 1562 ASN A OD1   1 
ATOM   2635 N  ND2   . ASN A 1 345 ? 10.016  -32.394 0.896  1.00 66.16  ? 1562 ASN A ND2   1 
ATOM   2636 N  N     . HIS A 1 346 ? 7.195   -31.786 4.186  1.00 53.36  ? 1563 HIS A N     1 
ATOM   2637 C  CA    . HIS A 1 346 ? 7.176   -30.580 4.996  1.00 59.36  ? 1563 HIS A CA    1 
ATOM   2638 C  C     . HIS A 1 346 ? 8.067   -30.733 6.211  1.00 61.70  ? 1563 HIS A C     1 
ATOM   2639 O  O     . HIS A 1 346 ? 9.053   -30.003 6.373  1.00 69.88  ? 1563 HIS A O     1 
ATOM   2640 C  CB    . HIS A 1 346 ? 5.735   -30.276 5.422  1.00 67.21  ? 1563 HIS A CB    1 
ATOM   2641 C  CG    . HIS A 1 346 ? 5.590   -29.057 6.283  1.00 70.18  ? 1563 HIS A CG    1 
ATOM   2642 N  ND1   . HIS A 1 346 ? 5.944   -27.794 5.856  1.00 70.86  ? 1563 HIS A ND1   1 
ATOM   2643 C  CD2   . HIS A 1 346 ? 5.106   -28.908 7.539  1.00 72.64  ? 1563 HIS A CD2   1 
ATOM   2644 C  CE1   . HIS A 1 346 ? 5.693   -26.923 6.817  1.00 73.87  ? 1563 HIS A CE1   1 
ATOM   2645 N  NE2   . HIS A 1 346 ? 5.183   -27.572 7.849  1.00 71.87  ? 1563 HIS A NE2   1 
ATOM   2646 N  N     . TRP A 1 347 ? 7.757   -31.711 7.065  1.00 53.41  ? 1564 TRP A N     1 
ATOM   2647 C  CA    . TRP A 1 347 ? 8.534   -31.818 8.294  1.00 50.36  ? 1564 TRP A CA    1 
ATOM   2648 C  C     . TRP A 1 347 ? 9.956   -32.300 8.041  1.00 51.95  ? 1564 TRP A C     1 
ATOM   2649 O  O     . TRP A 1 347 ? 10.841  -32.028 8.867  1.00 37.47  ? 1564 TRP A O     1 
ATOM   2650 C  CB    . TRP A 1 347 ? 7.811   -32.711 9.292  1.00 38.14  ? 1564 TRP A CB    1 
ATOM   2651 C  CG    . TRP A 1 347 ? 6.469   -32.189 9.670  1.00 52.89  ? 1564 TRP A CG    1 
ATOM   2652 C  CD1   . TRP A 1 347 ? 5.261   -32.657 9.252  1.00 65.36  ? 1564 TRP A CD1   1 
ATOM   2653 C  CD2   . TRP A 1 347 ? 6.192   -31.088 10.543 1.00 55.29  ? 1564 TRP A CD2   1 
ATOM   2654 N  NE1   . TRP A 1 347 ? 4.243   -31.921 9.815  1.00 66.69  ? 1564 TRP A NE1   1 
ATOM   2655 C  CE2   . TRP A 1 347 ? 4.790   -30.951 10.611 1.00 53.78  ? 1564 TRP A CE2   1 
ATOM   2656 C  CE3   . TRP A 1 347 ? 6.993   -30.209 11.276 1.00 52.57  ? 1564 TRP A CE3   1 
ATOM   2657 C  CZ2   . TRP A 1 347 ? 4.178   -29.984 11.383 1.00 56.59  ? 1564 TRP A CZ2   1 
ATOM   2658 C  CZ3   . TRP A 1 347 ? 6.387   -29.248 12.035 1.00 54.17  ? 1564 TRP A CZ3   1 
ATOM   2659 C  CH2   . TRP A 1 347 ? 4.992   -29.136 12.084 1.00 62.72  ? 1564 TRP A CH2   1 
ATOM   2660 N  N     . GLU A 1 348 ? 10.205  -32.977 6.909  1.00 59.07  ? 1565 GLU A N     1 
ATOM   2661 C  CA    . GLU A 1 348 ? 11.577  -33.348 6.569  1.00 67.21  ? 1565 GLU A CA    1 
ATOM   2662 C  C     . GLU A 1 348 ? 12.390  -32.119 6.187  1.00 65.43  ? 1565 GLU A C     1 
ATOM   2663 O  O     . GLU A 1 348 ? 13.612  -32.098 6.378  1.00 59.65  ? 1565 GLU A O     1 
ATOM   2664 C  CB    . GLU A 1 348 ? 11.578  -34.417 5.472  1.00 75.71  ? 1565 GLU A CB    1 
ATOM   2665 C  CG    . GLU A 1 348 ? 11.019  -35.747 6.013  1.00 89.16  ? 1565 GLU A CG    1 
ATOM   2666 C  CD    . GLU A 1 348 ? 11.346  -36.971 5.174  1.00 88.78  ? 1565 GLU A CD    1 
ATOM   2667 O  OE1   . GLU A 1 348 ? 11.586  -36.819 3.957  1.00 92.03  ? 1565 GLU A OE1   1 
ATOM   2668 O  OE2   . GLU A 1 348 ? 11.367  -38.084 5.753  1.00 82.65  ? 1565 GLU A OE2   1 
ATOM   2669 N  N     . LEU A 1 349 ? 11.731  -31.094 5.640  1.00 58.54  ? 1566 LEU A N     1 
ATOM   2670 C  CA    . LEU A 1 349 ? 12.398  -29.813 5.459  1.00 55.40  ? 1566 LEU A CA    1 
ATOM   2671 C  C     . LEU A 1 349 ? 12.668  -29.152 6.802  1.00 65.62  ? 1566 LEU A C     1 
ATOM   2672 O  O     . LEU A 1 349 ? 13.697  -28.484 6.982  1.00 69.40  ? 1566 LEU A O     1 
ATOM   2673 C  CB    . LEU A 1 349 ? 11.540  -28.887 4.619  1.00 46.43  ? 1566 LEU A CB    1 
ATOM   2674 C  CG    . LEU A 1 349 ? 11.248  -29.285 3.196  1.00 46.88  ? 1566 LEU A CG    1 
ATOM   2675 C  CD1   . LEU A 1 349 ? 9.821   -28.834 2.848  1.00 43.71  ? 1566 LEU A CD1   1 
ATOM   2676 C  CD2   . LEU A 1 349 ? 12.284  -28.648 2.293  1.00 38.74  ? 1566 LEU A CD2   1 
ATOM   2677 N  N     . LYS A 1 350 ? 11.735  -29.307 7.748  1.00 59.60  ? 1567 LYS A N     1 
ATOM   2678 C  CA    . LYS A 1 350 ? 11.888  -28.753 9.084  1.00 54.27  ? 1567 LYS A CA    1 
ATOM   2679 C  C     . LYS A 1 350 ? 12.849  -29.567 9.952  1.00 56.42  ? 1567 LYS A C     1 
ATOM   2680 O  O     . LYS A 1 350 ? 13.127  -29.163 11.091 1.00 58.12  ? 1567 LYS A O     1 
ATOM   2681 C  CB    . LYS A 1 350 ? 10.515  -28.647 9.760  1.00 46.84  ? 1567 LYS A CB    1 
ATOM   2682 C  CG    . LYS A 1 350 ? 9.671   -27.499 9.273  1.00 57.66  ? 1567 LYS A CG    1 
ATOM   2683 C  CD    . LYS A 1 350 ? 8.658   -27.100 10.330 1.00 61.45  ? 1567 LYS A CD    1 
ATOM   2684 C  CE    . LYS A 1 350 ? 7.700   -26.040 9.824  1.00 63.16  ? 1567 LYS A CE    1 
ATOM   2685 N  NZ    . LYS A 1 350 ? 6.359   -26.158 10.474 1.00 66.69  ? 1567 LYS A NZ    1 
ATOM   2686 N  N     . GLY A 1 351 ? 13.349  -30.697 9.453  1.00 46.74  ? 1568 GLY A N     1 
ATOM   2687 C  CA    . GLY A 1 351 ? 14.380  -31.423 10.159 1.00 45.98  ? 1568 GLY A CA    1 
ATOM   2688 C  C     . GLY A 1 351 ? 13.951  -31.998 11.484 1.00 47.81  ? 1568 GLY A C     1 
ATOM   2689 O  O     . GLY A 1 351 ? 14.785  -32.148 12.388 1.00 43.62  ? 1568 GLY A O     1 
ATOM   2690 N  N     . VAL A 1 352 ? 12.675  -32.334 11.629 1.00 46.63  ? 1569 VAL A N     1 
ATOM   2691 C  CA    . VAL A 1 352 ? 12.227  -33.012 12.844 1.00 48.05  ? 1569 VAL A CA    1 
ATOM   2692 C  C     . VAL A 1 352 ? 12.954  -34.344 12.967 1.00 45.03  ? 1569 VAL A C     1 
ATOM   2693 O  O     . VAL A 1 352 ? 12.870  -35.173 12.051 1.00 49.85  ? 1569 VAL A O     1 
ATOM   2694 C  CB    . VAL A 1 352 ? 10.714  -33.238 12.830 1.00 44.08  ? 1569 VAL A CB    1 
ATOM   2695 C  CG1   . VAL A 1 352 ? 10.332  -34.120 13.999 1.00 37.30  ? 1569 VAL A CG1   1 
ATOM   2696 C  CG2   . VAL A 1 352 ? 10.000  -31.903 12.868 1.00 39.66  ? 1569 VAL A CG2   1 
ATOM   2697 N  N     . PRO A 1 353 ? 13.644  -34.595 14.082 1.00 48.22  ? 1570 PRO A N     1 
ATOM   2698 C  CA    . PRO A 1 353 ? 14.516  -35.786 14.167 1.00 54.60  ? 1570 PRO A CA    1 
ATOM   2699 C  C     . PRO A 1 353 ? 13.849  -37.098 13.783 1.00 51.53  ? 1570 PRO A C     1 
ATOM   2700 O  O     . PRO A 1 353 ? 14.403  -37.857 12.968 1.00 54.72  ? 1570 PRO A O     1 
ATOM   2701 C  CB    . PRO A 1 353 ? 14.946  -35.768 15.635 1.00 55.83  ? 1570 PRO A CB    1 
ATOM   2702 C  CG    . PRO A 1 353 ? 15.005  -34.298 15.955 1.00 48.36  ? 1570 PRO A CG    1 
ATOM   2703 C  CD    . PRO A 1 353 ? 13.830  -33.692 15.226 1.00 44.52  ? 1570 PRO A CD    1 
ATOM   2704 N  N     . VAL A 1 354 ? 12.682  -37.401 14.345 1.00 41.09  ? 1571 VAL A N     1 
ATOM   2705 C  CA    . VAL A 1 354 ? 11.983  -38.632 14.009 1.00 47.11  ? 1571 VAL A CA    1 
ATOM   2706 C  C     . VAL A 1 354 ? 10.555  -38.308 13.628 1.00 40.76  ? 1571 VAL A C     1 
ATOM   2707 O  O     . VAL A 1 354 ? 9.836   -37.661 14.393 1.00 48.57  ? 1571 VAL A O     1 
ATOM   2708 C  CB    . VAL A 1 354 ? 12.016  -39.652 15.165 1.00 62.41  ? 1571 VAL A CB    1 
ATOM   2709 C  CG1   . VAL A 1 354 ? 11.375  -39.085 16.411 1.00 71.66  ? 1571 VAL A CG1   1 
ATOM   2710 C  CG2   . VAL A 1 354 ? 11.324  -40.934 14.762 1.00 60.99  ? 1571 VAL A CG2   1 
ATOM   2711 N  N     . ARG A 1 355 ? 10.136  -38.787 12.468 1.00 47.50  ? 1572 ARG A N     1 
ATOM   2712 C  CA    . ARG A 1 355 ? 8.745   -38.721 12.044 1.00 47.98  ? 1572 ARG A CA    1 
ATOM   2713 C  C     . ARG A 1 355 ? 8.051   -40.008 12.447 1.00 59.92  ? 1572 ARG A C     1 
ATOM   2714 O  O     . ARG A 1 355 ? 8.584   -41.103 12.259 1.00 70.53  ? 1572 ARG A O     1 
ATOM   2715 C  CB    . ARG A 1 355 ? 8.650   -38.529 10.527 1.00 45.39  ? 1572 ARG A CB    1 
ATOM   2716 C  CG    . ARG A 1 355 ? 7.288   -38.806 9.893  1.00 46.91  ? 1572 ARG A CG    1 
ATOM   2717 C  CD    . ARG A 1 355 ? 7.331   -38.488 8.407  1.00 51.39  ? 1572 ARG A CD    1 
ATOM   2718 N  NE    . ARG A 1 355 ? 7.719   -39.631 7.581  1.00 59.67  ? 1572 ARG A NE    1 
ATOM   2719 C  CZ    . ARG A 1 355 ? 8.930   -39.815 7.054  1.00 76.80  ? 1572 ARG A CZ    1 
ATOM   2720 N  NH1   . ARG A 1 355 ? 9.904   -38.929 7.268  1.00 75.97  ? 1572 ARG A NH1   1 
ATOM   2721 N  NH2   . ARG A 1 355 ? 9.169   -40.897 6.314  1.00 85.19  ? 1572 ARG A NH2   1 
ATOM   2722 N  N     . ILE A 1 356 ? 6.865   -39.879 12.999 1.00 49.11  ? 1573 ILE A N     1 
ATOM   2723 C  CA    . ILE A 1 356 ? 6.051   -41.034 13.319 1.00 47.74  ? 1573 ILE A CA    1 
ATOM   2724 C  C     . ILE A 1 356 ? 5.048   -41.224 12.197 1.00 59.37  ? 1573 ILE A C     1 
ATOM   2725 O  O     . ILE A 1 356 ? 4.382   -40.264 11.775 1.00 58.42  ? 1573 ILE A O     1 
ATOM   2726 C  CB    . ILE A 1 356 ? 5.333   -40.854 14.663 1.00 55.83  ? 1573 ILE A CB    1 
ATOM   2727 C  CG1   . ILE A 1 356 ? 6.258   -41.171 15.822 1.00 62.57  ? 1573 ILE A CG1   1 
ATOM   2728 C  CG2   . ILE A 1 356 ? 4.091   -41.736 14.750 1.00 61.23  ? 1573 ILE A CG2   1 
ATOM   2729 C  CD1   . ILE A 1 356 ? 5.505   -41.179 17.130 1.00 68.34  ? 1573 ILE A CD1   1 
ATOM   2730 N  N     . GLU A 1 357 ? 4.945   -42.460 11.700 1.00 63.07  ? 1574 GLU A N     1 
ATOM   2731 C  CA    . GLU A 1 357 ? 3.889   -42.854 10.774 1.00 61.63  ? 1574 GLU A CA    1 
ATOM   2732 C  C     . GLU A 1 357 ? 2.981   -43.849 11.488 1.00 59.78  ? 1574 GLU A C     1 
ATOM   2733 O  O     . GLU A 1 357 ? 3.453   -44.881 11.991 1.00 71.76  ? 1574 GLU A O     1 
ATOM   2734 C  CB    . GLU A 1 357 ? 4.470   -43.419 9.468  1.00 63.52  ? 1574 GLU A CB    1 
ATOM   2735 C  CG    . GLU A 1 357 ? 5.757   -42.691 8.975  1.00 71.12  ? 1574 GLU A CG    1 
ATOM   2736 C  CD    . GLU A 1 357 ? 6.291   -43.186 7.626  1.00 78.97  ? 1574 GLU A CD    1 
ATOM   2737 O  OE1   . GLU A 1 357 ? 5.981   -44.333 7.265  1.00 86.48  ? 1574 GLU A OE1   1 
ATOM   2738 O  OE2   . GLU A 1 357 ? 7.049   -42.454 6.946  1.00 78.06  ? 1574 GLU A OE2   1 
ATOM   2739 N  N     . LEU A 1 358 ? 1.696   -43.501 11.599 1.00 48.44  ? 1575 LEU A N     1 
ATOM   2740 C  CA    . LEU A 1 358 ? 0.681   -44.314 12.270 1.00 53.12  ? 1575 LEU A CA    1 
ATOM   2741 C  C     . LEU A 1 358 ? -0.539  -44.424 11.364 1.00 60.35  ? 1575 LEU A C     1 
ATOM   2742 O  O     . LEU A 1 358 ? -1.294  -43.460 11.220 1.00 58.13  ? 1575 LEU A O     1 
ATOM   2743 C  CB    . LEU A 1 358 ? 0.318   -43.754 13.640 1.00 48.59  ? 1575 LEU A CB    1 
ATOM   2744 C  CG    . LEU A 1 358 ? -0.617  -44.655 14.473 1.00 52.37  ? 1575 LEU A CG    1 
ATOM   2745 C  CD1   . LEU A 1 358 ? -0.320  -44.642 15.965 1.00 56.27  ? 1575 LEU A CD1   1 
ATOM   2746 C  CD2   . LEU A 1 358 ? -2.049  -44.296 14.269 1.00 54.12  ? 1575 LEU A CD2   1 
ATOM   2747 N  N     . GLY A 1 359 ? -0.716  -45.592 10.741 1.00 71.70  ? 1576 GLY A N     1 
ATOM   2748 C  CA    . GLY A 1 359 ? -1.863  -45.879 9.914  1.00 79.19  ? 1576 GLY A CA    1 
ATOM   2749 C  C     . GLY A 1 359 ? -2.860  -46.781 10.623 1.00 82.54  ? 1576 GLY A C     1 
ATOM   2750 O  O     . GLY A 1 359 ? -2.754  -47.055 11.819 1.00 87.48  ? 1576 GLY A O     1 
ATOM   2751 N  N     . PHE A 1 360 ? -3.856  -47.243 9.859  1.00 79.40  ? 1577 PHE A N     1 
ATOM   2752 C  CA    . PHE A 1 360 ? -4.851  -48.162 10.410 1.00 77.98  ? 1577 PHE A CA    1 
ATOM   2753 C  C     . PHE A 1 360 ? -4.244  -49.528 10.749 1.00 75.75  ? 1577 PHE A C     1 
ATOM   2754 O  O     . PHE A 1 360 ? -4.702  -50.193 11.687 1.00 74.21  ? 1577 PHE A O     1 
ATOM   2755 C  CB    . PHE A 1 360 ? -6.029  -48.325 9.429  1.00 77.04  ? 1577 PHE A CB    1 
ATOM   2756 C  CG    . PHE A 1 360 ? -6.796  -47.060 9.200  1.00 76.95  ? 1577 PHE A CG    1 
ATOM   2757 C  CD1   . PHE A 1 360 ? -7.427  -46.415 10.255 1.00 75.90  ? 1577 PHE A CD1   1 
ATOM   2758 C  CD2   . PHE A 1 360 ? -6.867  -46.489 7.946  1.00 78.57  ? 1577 PHE A CD2   1 
ATOM   2759 C  CE1   . PHE A 1 360 ? -8.116  -45.218 10.062 1.00 63.72  ? 1577 PHE A CE1   1 
ATOM   2760 C  CE2   . PHE A 1 360 ? -7.561  -45.293 7.752  1.00 68.33  ? 1577 PHE A CE2   1 
ATOM   2761 C  CZ    . PHE A 1 360 ? -8.185  -44.668 8.816  1.00 55.90  ? 1577 PHE A CZ    1 
ATOM   2762 N  N     . LYS A 1 361 ? -3.246  -49.987 9.988  1.00 65.06  ? 1578 LYS A N     1 
ATOM   2763 C  CA    . LYS A 1 361 ? -2.665  -51.293 10.275 1.00 71.29  ? 1578 LYS A CA    1 
ATOM   2764 C  C     . LYS A 1 361 ? -1.915  -51.283 11.600 1.00 74.27  ? 1578 LYS A C     1 
ATOM   2765 O  O     . LYS A 1 361 ? -2.168  -52.118 12.480 1.00 77.08  ? 1578 LYS A O     1 
ATOM   2766 C  CB    . LYS A 1 361 ? -1.745  -51.718 9.135  1.00 75.25  ? 1578 LYS A CB    1 
ATOM   2767 N  N     . ASP A 1 362 ? -1.037  -50.305 11.795 1.00 78.46  ? 1579 ASP A N     1 
ATOM   2768 C  CA    . ASP A 1 362 ? -0.380  -50.192 13.088 1.00 79.53  ? 1579 ASP A CA    1 
ATOM   2769 C  C     . ASP A 1 362 ? -1.406  -50.039 14.188 1.00 74.23  ? 1579 ASP A C     1 
ATOM   2770 O  O     . ASP A 1 362 ? -1.236  -50.590 15.279 1.00 76.24  ? 1579 ASP A O     1 
ATOM   2771 C  CB    . ASP A 1 362 ? 0.585   -49.014 13.089 1.00 82.80  ? 1579 ASP A CB    1 
ATOM   2772 C  CG    . ASP A 1 362 ? 1.283   -48.842 11.761 1.00 95.83  ? 1579 ASP A CG    1 
ATOM   2773 O  OD1   . ASP A 1 362 ? 2.020   -49.767 11.346 1.00 98.70  ? 1579 ASP A OD1   1 
ATOM   2774 O  OD2   . ASP A 1 362 ? 1.086   -47.783 11.127 1.00 99.49  ? 1579 ASP A OD2   1 
ATOM   2775 N  N     . LEU A 1 363 ? -2.510  -49.358 13.889 1.00 71.94  ? 1580 LEU A N     1 
ATOM   2776 C  CA    . LEU A 1 363 ? -3.595  -49.242 14.852 1.00 68.11  ? 1580 LEU A CA    1 
ATOM   2777 C  C     . LEU A 1 363 ? -4.112  -50.621 15.236 1.00 66.25  ? 1580 LEU A C     1 
ATOM   2778 O  O     . LEU A 1 363 ? -4.261  -50.942 16.420 1.00 63.07  ? 1580 LEU A O     1 
ATOM   2779 C  CB    . LEU A 1 363 ? -4.708  -48.369 14.258 1.00 63.34  ? 1580 LEU A CB    1 
ATOM   2780 C  CG    . LEU A 1 363 ? -5.701  -47.700 15.206 1.00 63.96  ? 1580 LEU A CG    1 
ATOM   2781 C  CD1   . LEU A 1 363 ? -5.975  -46.240 14.791 1.00 56.20  ? 1580 LEU A CD1   1 
ATOM   2782 C  CD2   . LEU A 1 363 ? -7.000  -48.532 15.290 1.00 71.66  ? 1580 LEU A CD2   1 
ATOM   2783 N  N     . GLN A 1 364 ? -4.348  -51.470 14.243 1.00 70.61  ? 1581 GLN A N     1 
ATOM   2784 C  CA    . GLN A 1 364 ? -4.800  -52.813 14.551 1.00 71.85  ? 1581 GLN A CA    1 
ATOM   2785 C  C     . GLN A 1 364 ? -3.776  -53.576 15.384 1.00 78.21  ? 1581 GLN A C     1 
ATOM   2786 O  O     . GLN A 1 364 ? -4.162  -54.413 16.206 1.00 85.96  ? 1581 GLN A O     1 
ATOM   2787 C  CB    . GLN A 1 364 ? -5.116  -53.564 13.257 1.00 73.75  ? 1581 GLN A CB    1 
ATOM   2788 N  N     . ASN A 1 365 ? -2.479  -53.261 15.251 1.00 78.98  ? 1582 ASN A N     1 
ATOM   2789 C  CA    . ASN A 1 365 ? -1.443  -54.049 15.922 1.00 73.69  ? 1582 ASN A CA    1 
ATOM   2790 C  C     . ASN A 1 365 ? -0.822  -53.345 17.114 1.00 73.62  ? 1582 ASN A C     1 
ATOM   2791 O  O     . ASN A 1 365 ? 0.204   -53.819 17.621 1.00 75.80  ? 1582 ASN A O     1 
ATOM   2792 C  CB    . ASN A 1 365 ? -0.312  -54.427 14.959 1.00 63.77  ? 1582 ASN A CB    1 
ATOM   2793 C  CG    . ASN A 1 365 ? -0.806  -55.121 13.701 1.00 64.04  ? 1582 ASN A CG    1 
ATOM   2794 O  OD1   . ASN A 1 365 ? -0.444  -54.747 12.591 1.00 69.94  ? 1582 ASN A OD1   1 
ATOM   2795 N  ND2   . ASN A 1 365 ? -1.631  -56.137 13.871 1.00 65.06  ? 1582 ASN A ND2   1 
ATOM   2796 N  N     . ASP A 1 366 ? -1.451  -52.271 17.612 1.00 71.33  ? 1583 ASP A N     1 
ATOM   2797 C  CA    . ASP A 1 366 ? -0.952  -51.524 18.783 1.00 71.22  ? 1583 ASP A CA    1 
ATOM   2798 C  C     . ASP A 1 366 ? 0.509   -51.126 18.637 1.00 60.66  ? 1583 ASP A C     1 
ATOM   2799 O  O     . ASP A 1 366 ? 1.339   -51.385 19.509 1.00 56.38  ? 1583 ASP A O     1 
ATOM   2800 C  CB    . ASP A 1 366 ? -1.138  -52.321 20.068 1.00 82.57  ? 1583 ASP A CB    1 
ATOM   2801 C  CG    . ASP A 1 366 ? -1.376  -51.434 21.278 1.00 93.44  ? 1583 ASP A CG    1 
ATOM   2802 O  OD1   . ASP A 1 366 ? -0.391  -50.746 21.644 1.00 104.78 ? 1583 ASP A OD1   1 
ATOM   2803 O  OD2   . ASP A 1 366 ? -2.484  -51.503 21.889 1.00 94.13  ? 1583 ASP A OD2   1 
ATOM   2804 N  N     . GLN A 1 367 ? 0.808   -50.448 17.540 1.00 62.41  ? 1584 GLN A N     1 
ATOM   2805 C  CA    . GLN A 1 367 ? 2.169   -50.092 17.208 1.00 63.72  ? 1584 GLN A CA    1 
ATOM   2806 C  C     . GLN A 1 367 ? 2.150   -48.820 16.364 1.00 69.14  ? 1584 GLN A C     1 
ATOM   2807 O  O     . GLN A 1 367 ? 1.096   -48.205 16.140 1.00 67.48  ? 1584 GLN A O     1 
ATOM   2808 C  CB    . GLN A 1 367 ? 2.838   -51.261 16.470 1.00 58.74  ? 1584 GLN A CB    1 
ATOM   2809 C  CG    . GLN A 1 367 ? 2.005   -51.795 15.312 1.00 69.78  ? 1584 GLN A CG    1 
ATOM   2810 C  CD    . GLN A 1 367 ? 2.830   -52.396 14.195 1.00 78.73  ? 1584 GLN A CD    1 
ATOM   2811 O  OE1   . GLN A 1 367 ? 3.228   -51.685 13.273 1.00 76.03  ? 1584 GLN A OE1   1 
ATOM   2812 N  NE2   . GLN A 1 367 ? 3.038   -53.724 14.234 1.00 83.84  ? 1584 GLN A NE2   1 
ATOM   2813 N  N     . PHE A 1 368 ? 3.343   -48.443 15.909 1.00 61.90  ? 1585 PHE A N     1 
ATOM   2814 C  CA    . PHE A 1 368 ? 3.575   -47.333 14.996 1.00 54.09  ? 1585 PHE A CA    1 
ATOM   2815 C  C     . PHE A 1 368 ? 4.979   -47.526 14.450 1.00 59.99  ? 1585 PHE A C     1 
ATOM   2816 O  O     . PHE A 1 368 ? 5.767   -48.291 15.013 1.00 69.60  ? 1585 PHE A O     1 
ATOM   2817 C  CB    . PHE A 1 368 ? 3.434   -45.990 15.712 1.00 49.57  ? 1585 PHE A CB    1 
ATOM   2818 C  CG    . PHE A 1 368 ? 4.314   -45.862 16.927 1.00 51.72  ? 1585 PHE A CG    1 
ATOM   2819 C  CD1   . PHE A 1 368 ? 3.859   -46.263 18.178 1.00 56.72  ? 1585 PHE A CD1   1 
ATOM   2820 C  CD2   . PHE A 1 368 ? 5.615   -45.358 16.814 1.00 48.04  ? 1585 PHE A CD2   1 
ATOM   2821 C  CE1   . PHE A 1 368 ? 4.693   -46.153 19.301 1.00 73.68  ? 1585 PHE A CE1   1 
ATOM   2822 C  CE2   . PHE A 1 368 ? 6.446   -45.250 17.925 1.00 53.82  ? 1585 PHE A CE2   1 
ATOM   2823 C  CZ    . PHE A 1 368 ? 5.989   -45.641 19.170 1.00 66.11  ? 1585 PHE A CZ    1 
ATOM   2824 N  N     . VAL A 1 369 ? 5.300   -46.872 13.338 1.00 58.65  ? 1586 VAL A N     1 
ATOM   2825 C  CA    . VAL A 1 369 ? 6.655   -46.971 12.813 1.00 57.07  ? 1586 VAL A CA    1 
ATOM   2826 C  C     . VAL A 1 369 ? 7.313   -45.595 12.839 1.00 59.00  ? 1586 VAL A C     1 
ATOM   2827 O  O     . VAL A 1 369 ? 6.743   -44.611 12.354 1.00 59.55  ? 1586 VAL A O     1 
ATOM   2828 C  CB    . VAL A 1 369 ? 6.684   -47.602 11.410 1.00 56.49  ? 1586 VAL A CB    1 
ATOM   2829 C  CG1   . VAL A 1 369 ? 5.639   -46.998 10.480 1.00 51.59  ? 1586 VAL A CG1   1 
ATOM   2830 C  CG2   . VAL A 1 369 ? 8.073   -47.478 10.839 1.00 66.87  ? 1586 VAL A CG2   1 
ATOM   2831 N  N     . ALA A 1 370 ? 8.529   -45.534 13.373 1.00 64.99  ? 1587 ALA A N     1 
ATOM   2832 C  CA    . ALA A 1 370 ? 9.287   -44.299 13.465 1.00 57.67  ? 1587 ALA A CA    1 
ATOM   2833 C  C     . ALA A 1 370 ? 10.368  -44.255 12.387 1.00 64.39  ? 1587 ALA A C     1 
ATOM   2834 O  O     . ALA A 1 370 ? 11.070  -45.245 12.157 1.00 64.60  ? 1587 ALA A O     1 
ATOM   2835 C  CB    . ALA A 1 370 ? 9.903   -44.188 14.856 1.00 51.36  ? 1587 ALA A CB    1 
ATOM   2836 N  N     . VAL A 1 371 ? 10.509  -43.098 11.735 1.00 65.05  ? 1588 VAL A N     1 
ATOM   2837 C  CA    . VAL A 1 371 ? 11.480  -42.892 10.666 1.00 61.82  ? 1588 VAL A CA    1 
ATOM   2838 C  C     . VAL A 1 371 ? 12.440  -41.805 11.104 1.00 58.92  ? 1588 VAL A C     1 
ATOM   2839 O  O     . VAL A 1 371 ? 12.009  -40.748 11.566 1.00 62.04  ? 1588 VAL A O     1 
ATOM   2840 C  CB    . VAL A 1 371 ? 10.810  -42.489 9.341  1.00 57.05  ? 1588 VAL A CB    1 
ATOM   2841 C  CG1   . VAL A 1 371 ? 11.823  -42.565 8.199  1.00 61.64  ? 1588 VAL A CG1   1 
ATOM   2842 C  CG2   . VAL A 1 371 ? 9.585   -43.339 9.071  1.00 52.69  ? 1588 VAL A CG2   1 
ATOM   2843 N  N     . ARG A 1 372 ? 13.716  -42.015 10.929 1.00 60.09  ? 1589 ARG A N     1 
ATOM   2844 C  CA    . ARG A 1 372 ? 14.736  -41.091 11.327 1.00 67.65  ? 1589 ARG A CA    1 
ATOM   2845 C  C     . ARG A 1 372 ? 15.039  -40.081 10.275 1.00 67.49  ? 1589 ARG A C     1 
ATOM   2846 O  O     . ARG A 1 372 ? 15.215  -40.446 9.150  1.00 69.54  ? 1589 ARG A O     1 
ATOM   2847 C  CB    . ARG A 1 372 ? 16.021  -41.874 11.543 1.00 77.41  ? 1589 ARG A CB    1 
ATOM   2848 C  CG    . ARG A 1 372 ? 16.179  -42.481 12.917 1.00 75.83  ? 1589 ARG A CG    1 
ATOM   2849 C  CD    . ARG A 1 372 ? 17.284  -43.500 12.994 1.00 69.55  ? 1589 ARG A CD    1 
ATOM   2850 N  NE    . ARG A 1 372 ? 18.582  -42.939 12.777 1.00 60.35  ? 1589 ARG A NE    1 
ATOM   2851 C  CZ    . ARG A 1 372 ? 19.656  -43.394 13.364 1.00 58.80  ? 1589 ARG A CZ    1 
ATOM   2852 N  NH1   . ARG A 1 372 ? 19.584  -44.386 14.179 1.00 59.84  ? 1589 ARG A NH1   1 
ATOM   2853 N  NH2   . ARG A 1 372 ? 20.791  -42.841 13.135 1.00 57.85  ? 1589 ARG A NH2   1 
ATOM   2854 N  N     . ARG A 1 373 ? 15.192  -38.818 10.646 1.00 57.18  ? 1590 ARG A N     1 
ATOM   2855 C  CA    . ARG A 1 373 ? 15.494  -37.805 9.642  1.00 52.03  ? 1590 ARG A CA    1 
ATOM   2856 C  C     . ARG A 1 373 ? 16.934  -37.908 9.144  1.00 55.14  ? 1590 ARG A C     1 
ATOM   2857 O  O     . ARG A 1 373 ? 17.213  -37.556 7.997  1.00 58.12  ? 1590 ARG A O     1 
ATOM   2858 C  CB    . ARG A 1 373 ? 15.203  -36.406 10.191 1.00 49.78  ? 1590 ARG A CB    1 
ATOM   2859 C  CG    . ARG A 1 373 ? 15.552  -35.259 9.234  1.00 44.22  ? 1590 ARG A CG    1 
ATOM   2860 C  CD    . ARG A 1 373 ? 14.910  -35.431 7.855  1.00 52.57  ? 1590 ARG A CD    1 
ATOM   2861 N  NE    . ARG A 1 373 ? 15.225  -34.319 6.957  1.00 61.73  ? 1590 ARG A NE    1 
ATOM   2862 C  CZ    . ARG A 1 373 ? 16.368  -34.188 6.284  1.00 57.85  ? 1590 ARG A CZ    1 
ATOM   2863 N  NH1   . ARG A 1 373 ? 17.307  -35.114 6.393  1.00 52.52  ? 1590 ARG A NH1   1 
ATOM   2864 N  NH2   . ARG A 1 373 ? 16.570  -33.130 5.499  1.00 53.35  ? 1590 ARG A NH2   1 
ATOM   2865 N  N     . ASP A 1 374 ? 17.855  -38.425 9.960  1.00 60.19  ? 1591 ASP A N     1 
ATOM   2866 C  CA    . ASP A 1 374 ? 19.243  -38.471 9.507  1.00 60.80  ? 1591 ASP A CA    1 
ATOM   2867 C  C     . ASP A 1 374 ? 19.506  -39.592 8.498  1.00 64.84  ? 1591 ASP A C     1 
ATOM   2868 O  O     . ASP A 1 374 ? 20.149  -39.339 7.475  1.00 77.12  ? 1591 ASP A O     1 
ATOM   2869 C  CB    . ASP A 1 374 ? 20.195  -38.555 10.707 1.00 61.12  ? 1591 ASP A CB    1 
ATOM   2870 C  CG    . ASP A 1 374 ? 19.989  -39.780 11.557 1.00 57.56  ? 1591 ASP A CG    1 
ATOM   2871 O  OD1   . ASP A 1 374 ? 18.986  -40.488 11.356 1.00 57.98  ? 1591 ASP A OD1   1 
ATOM   2872 O  OD2   . ASP A 1 374 ? 20.834  -40.011 12.455 1.00 52.34  ? 1591 ASP A OD2   1 
ATOM   2873 N  N     . ASN A 1 375 ? 19.032  -40.829 8.728  1.00 58.28  ? 1592 ASN A N     1 
ATOM   2874 C  CA    . ASN A 1 375 ? 19.173  -41.843 7.676  1.00 55.91  ? 1592 ASN A CA    1 
ATOM   2875 C  C     . ASN A 1 375 ? 17.896  -42.135 6.929  1.00 69.28  ? 1592 ASN A C     1 
ATOM   2876 O  O     . ASN A 1 375 ? 17.949  -42.832 5.909  1.00 70.31  ? 1592 ASN A O     1 
ATOM   2877 C  CB    . ASN A 1 375 ? 19.593  -43.210 8.190  1.00 47.33  ? 1592 ASN A CB    1 
ATOM   2878 C  CG    . ASN A 1 375 ? 20.955  -43.256 8.641  1.00 52.80  ? 1592 ASN A CG    1 
ATOM   2879 O  OD1   . ASN A 1 375 ? 21.759  -42.432 8.218  1.00 59.49  ? 1592 ASN A OD1   1 
ATOM   2880 N  ND2   . ASN A 1 375 ? 21.252  -44.174 9.568  1.00 59.04  ? 1592 ASN A ND2   1 
ATOM   2881 N  N     . GLY A 1 376 ? 16.757  -41.655 7.407  1.00 76.55  ? 1593 GLY A N     1 
ATOM   2882 C  CA    . GLY A 1 376 ? 15.538  -42.196 6.858  1.00 78.82  ? 1593 GLY A CA    1 
ATOM   2883 C  C     . GLY A 1 376 ? 15.318  -43.638 7.242  1.00 66.37  ? 1593 GLY A C     1 
ATOM   2884 O  O     . GLY A 1 376 ? 14.494  -44.306 6.618  1.00 68.26  ? 1593 GLY A O     1 
ATOM   2885 N  N     . ALA A 1 377 ? 16.055  -44.134 8.240  1.00 55.13  ? 1594 ALA A N     1 
ATOM   2886 C  CA    . ALA A 1 377 ? 15.894  -45.505 8.690  1.00 53.89  ? 1594 ALA A CA    1 
ATOM   2887 C  C     . ALA A 1 377 ? 14.609  -45.624 9.480  1.00 58.71  ? 1594 ALA A C     1 
ATOM   2888 O  O     . ALA A 1 377 ? 14.299  -44.767 10.318 1.00 53.06  ? 1594 ALA A O     1 
ATOM   2889 C  CB    . ALA A 1 377 ? 17.068  -45.969 9.540  1.00 54.48  ? 1594 ALA A CB    1 
ATOM   2890 N  N     . LYS A 1 378 ? 13.863  -46.684 9.182  1.00 66.05  ? 1595 LYS A N     1 
ATOM   2891 C  CA    . LYS A 1 378 ? 12.617  -47.010 9.857  1.00 70.47  ? 1595 LYS A CA    1 
ATOM   2892 C  C     . LYS A 1 378 ? 12.811  -48.085 10.926 1.00 65.26  ? 1595 LYS A C     1 
ATOM   2893 O  O     . LYS A 1 378 ? 13.729  -48.899 10.877 1.00 73.61  ? 1595 LYS A O     1 
ATOM   2894 C  CB    . LYS A 1 378 ? 11.555  -47.483 8.844  1.00 83.33  ? 1595 LYS A CB    1 
ATOM   2895 N  N     . GLN A 1 379 ? 11.902  -48.066 11.894 1.00 67.59  ? 1596 GLN A N     1 
ATOM   2896 C  CA    . GLN A 1 379 ? 11.929  -49.006 13.005 1.00 74.44  ? 1596 GLN A CA    1 
ATOM   2897 C  C     . GLN A 1 379 ? 10.561  -49.015 13.681 1.00 78.56  ? 1596 GLN A C     1 
ATOM   2898 O  O     . GLN A 1 379 ? 10.031  -47.958 14.043 1.00 76.45  ? 1596 GLN A O     1 
ATOM   2899 C  CB    . GLN A 1 379 ? 13.026  -48.625 13.999 1.00 76.75  ? 1596 GLN A CB    1 
ATOM   2900 C  CG    . GLN A 1 379 ? 12.878  -49.158 15.409 1.00 79.06  ? 1596 GLN A CG    1 
ATOM   2901 C  CD    . GLN A 1 379 ? 13.818  -48.445 16.365 1.00 87.95  ? 1596 GLN A CD    1 
ATOM   2902 O  OE1   . GLN A 1 379 ? 14.515  -47.509 15.973 1.00 91.34  ? 1596 GLN A OE1   1 
ATOM   2903 N  NE2   . GLN A 1 379 ? 13.840  -48.878 17.620 1.00 93.28  ? 1596 GLN A NE2   1 
ATOM   2904 N  N     . THR A 1 380 ? 9.988   -50.209 13.834 1.00 74.85  ? 1597 THR A N     1 
ATOM   2905 C  CA    . THR A 1 380 ? 8.645   -50.338 14.386 1.00 61.35  ? 1597 THR A CA    1 
ATOM   2906 C  C     . THR A 1 380 ? 8.646   -50.528 15.900 1.00 61.48  ? 1597 THR A C     1 
ATOM   2907 O  O     . THR A 1 380 ? 9.518   -51.183 16.475 1.00 60.64  ? 1597 THR A O     1 
ATOM   2908 C  CB    . THR A 1 380 ? 7.904   -51.466 13.693 1.00 55.59  ? 1597 THR A CB    1 
ATOM   2909 O  OG1   . THR A 1 380 ? 8.006   -51.243 12.283 1.00 55.68  ? 1597 THR A OG1   1 
ATOM   2910 C  CG2   . THR A 1 380 ? 6.450   -51.418 14.085 1.00 55.76  ? 1597 THR A CG2   1 
ATOM   2911 N  N     . ILE A 1 381 ? 7.664   -49.912 16.542 1.00 63.11  ? 1598 ILE A N     1 
ATOM   2912 C  CA    . ILE A 1 381 ? 7.632   -49.808 17.991 1.00 62.47  ? 1598 ILE A CA    1 
ATOM   2913 C  C     . ILE A 1 381 ? 6.210   -50.051 18.475 1.00 69.92  ? 1598 ILE A C     1 
ATOM   2914 O  O     . ILE A 1 381 ? 5.260   -49.429 17.979 1.00 75.70  ? 1598 ILE A O     1 
ATOM   2915 C  CB    . ILE A 1 381 ? 8.139   -48.424 18.428 1.00 54.49  ? 1598 ILE A CB    1 
ATOM   2916 C  CG1   . ILE A 1 381 ? 9.505   -48.150 17.776 1.00 50.31  ? 1598 ILE A CG1   1 
ATOM   2917 C  CG2   . ILE A 1 381 ? 8.142   -48.325 19.903 1.00 53.43  ? 1598 ILE A CG2   1 
ATOM   2918 C  CD1   . ILE A 1 381 ? 10.355  -47.145 18.455 1.00 48.89  ? 1598 ILE A CD1   1 
ATOM   2919 N  N     . LYS A 1 382 ? 6.061   -50.994 19.402 1.00 71.04  ? 1599 LYS A N     1 
ATOM   2920 C  CA    . LYS A 1 382 ? 4.774   -51.257 20.032 1.00 75.02  ? 1599 LYS A CA    1 
ATOM   2921 C  C     . LYS A 1 382 ? 4.455   -50.156 21.046 1.00 68.60  ? 1599 LYS A C     1 
ATOM   2922 O  O     . LYS A 1 382 ? 5.352   -49.488 21.572 1.00 66.62  ? 1599 LYS A O     1 
ATOM   2923 C  CB    . LYS A 1 382 ? 4.776   -52.640 20.689 1.00 76.12  ? 1599 LYS A CB    1 
ATOM   2924 N  N     . ARG A 1 383 ? 3.162   -49.944 21.301 1.00 62.17  ? 1600 ARG A N     1 
ATOM   2925 C  CA    . ARG A 1 383 ? 2.775   -48.746 22.038 1.00 69.30  ? 1600 ARG A CA    1 
ATOM   2926 C  C     . ARG A 1 383 ? 3.043   -48.815 23.538 1.00 75.90  ? 1600 ARG A C     1 
ATOM   2927 O  O     . ARG A 1 383 ? 3.062   -47.765 24.194 1.00 84.08  ? 1600 ARG A O     1 
ATOM   2928 C  CB    . ARG A 1 383 ? 1.310   -48.416 21.749 1.00 63.57  ? 1600 ARG A CB    1 
ATOM   2929 C  CG    . ARG A 1 383 ? 1.140   -48.037 20.288 1.00 76.90  ? 1600 ARG A CG    1 
ATOM   2930 C  CD    . ARG A 1 383 ? -0.066  -47.167 19.989 1.00 86.19  ? 1600 ARG A CD    1 
ATOM   2931 N  NE    . ARG A 1 383 ? -0.344  -46.174 21.020 1.00 84.03  ? 1600 ARG A NE    1 
ATOM   2932 C  CZ    . ARG A 1 383 ? -1.288  -45.248 20.907 1.00 83.28  ? 1600 ARG A CZ    1 
ATOM   2933 N  NH1   . ARG A 1 383 ? -2.031  -45.195 19.808 1.00 79.90  ? 1600 ARG A NH1   1 
ATOM   2934 N  NH2   . ARG A 1 383 ? -1.498  -44.384 21.890 1.00 85.91  ? 1600 ARG A NH2   1 
ATOM   2935 N  N     . ALA A 1 384 ? 3.283   -49.995 24.100 1.00 77.43  ? 1601 ALA A N     1 
ATOM   2936 C  CA    . ALA A 1 384 ? 3.647   -50.053 25.510 1.00 81.30  ? 1601 ALA A CA    1 
ATOM   2937 C  C     . ALA A 1 384 ? 5.052   -49.516 25.718 1.00 88.08  ? 1601 ALA A C     1 
ATOM   2938 O  O     . ALA A 1 384 ? 5.290   -48.664 26.589 1.00 95.47  ? 1601 ALA A O     1 
ATOM   2939 C  CB    . ALA A 1 384 ? 3.545   -51.485 26.026 1.00 85.69  ? 1601 ALA A CB    1 
ATOM   2940 N  N     . GLN A 1 385 ? 5.983   -49.966 24.881 1.00 86.06  ? 1602 GLN A N     1 
ATOM   2941 C  CA    . GLN A 1 385 ? 7.394   -49.627 24.985 1.00 81.09  ? 1602 GLN A CA    1 
ATOM   2942 C  C     . GLN A 1 385 ? 7.712   -48.248 24.415 1.00 63.08  ? 1602 GLN A C     1 
ATOM   2943 O  O     . GLN A 1 385 ? 8.880   -47.854 24.434 1.00 49.69  ? 1602 GLN A O     1 
ATOM   2944 C  CB    . GLN A 1 385 ? 8.223   -50.686 24.247 1.00 81.43  ? 1602 GLN A CB    1 
ATOM   2945 C  CG    . GLN A 1 385 ? 8.195   -50.453 22.738 1.00 90.92  ? 1602 GLN A CG    1 
ATOM   2946 C  CD    . GLN A 1 385 ? 8.747   -51.590 21.892 1.00 96.07  ? 1602 GLN A CD    1 
ATOM   2947 O  OE1   . GLN A 1 385 ? 9.763   -51.449 21.204 1.00 96.01  ? 1602 GLN A OE1   1 
ATOM   2948 N  NE2   . GLN A 1 385 ? 8.038   -52.697 21.884 1.00 97.29  ? 1602 GLN A NE2   1 
ATOM   2949 N  N     . ALA A 1 386 ? 6.702   -47.520 23.923 1.00 51.49  ? 1603 ALA A N     1 
ATOM   2950 C  CA    . ALA A 1 386 ? 6.911   -46.189 23.358 1.00 51.54  ? 1603 ALA A CA    1 
ATOM   2951 C  C     . ALA A 1 386 ? 7.636   -45.270 24.340 1.00 58.68  ? 1603 ALA A C     1 
ATOM   2952 O  O     . ALA A 1 386 ? 8.595   -44.572 23.968 1.00 45.93  ? 1603 ALA A O     1 
ATOM   2953 C  CB    . ALA A 1 386 ? 5.567   -45.601 22.931 1.00 49.54  ? 1603 ALA A CB    1 
ATOM   2954 N  N     . THR A 1 387 ? 7.227   -45.321 25.617 1.00 72.76  ? 1604 THR A N     1 
ATOM   2955 C  CA    . THR A 1 387 ? 7.791   -44.498 26.680 1.00 64.78  ? 1604 THR A CA    1 
ATOM   2956 C  C     . THR A 1 387 ? 9.274   -44.751 26.877 1.00 66.28  ? 1604 THR A C     1 
ATOM   2957 O  O     . THR A 1 387 ? 9.979   -43.863 27.365 1.00 64.08  ? 1604 THR A O     1 
ATOM   2958 C  CB    . THR A 1 387 ? 7.105   -44.844 28.012 1.00 76.16  ? 1604 THR A CB    1 
ATOM   2959 O  OG1   . THR A 1 387 ? 5.726   -45.172 27.790 1.00 94.76  ? 1604 THR A OG1   1 
ATOM   2960 C  CG2   . THR A 1 387 ? 7.219   -43.716 29.015 1.00 72.30  ? 1604 THR A CG2   1 
ATOM   2961 N  N     . VAL A 1 388 ? 9.776   -45.908 26.456 1.00 69.69  ? 1605 VAL A N     1 
ATOM   2962 C  CA    . VAL A 1 388 ? 11.194  -46.242 26.581 1.00 72.33  ? 1605 VAL A CA    1 
ATOM   2963 C  C     . VAL A 1 388 ? 11.919  -46.091 25.255 1.00 68.95  ? 1605 VAL A C     1 
ATOM   2964 O  O     . VAL A 1 388 ? 12.948  -45.421 25.172 1.00 74.97  ? 1605 VAL A O     1 
ATOM   2965 C  CB    . VAL A 1 388 ? 11.370  -47.678 27.133 1.00 70.94  ? 1605 VAL A CB    1 
ATOM   2966 C  CG1   . VAL A 1 388 ? 12.747  -48.202 26.791 1.00 49.69  ? 1605 VAL A CG1   1 
ATOM   2967 C  CG2   . VAL A 1 388 ? 11.152  -47.742 28.638 1.00 74.62  ? 1605 VAL A CG2   1 
ATOM   2968 N  N     . GLU A 1 389 ? 11.364  -46.684 24.200 1.00 60.66  ? 1606 GLU A N     1 
ATOM   2969 C  CA    . GLU A 1 389 ? 12.045  -46.731 22.914 1.00 55.32  ? 1606 GLU A CA    1 
ATOM   2970 C  C     . GLU A 1 389 ? 12.267  -45.339 22.342 1.00 60.79  ? 1606 GLU A C     1 
ATOM   2971 O  O     . GLU A 1 389 ? 13.301  -45.090 21.716 1.00 53.09  ? 1606 GLU A O     1 
ATOM   2972 C  CB    . GLU A 1 389 ? 11.276  -47.633 21.943 1.00 49.95  ? 1606 GLU A CB    1 
ATOM   2973 C  CG    . GLU A 1 389 ? 11.276  -49.129 22.354 1.00 50.84  ? 1606 GLU A CG    1 
ATOM   2974 C  CD    . GLU A 1 389 ? 12.663  -49.728 22.565 1.00 65.50  ? 1606 GLU A CD    1 
ATOM   2975 O  OE1   . GLU A 1 389 ? 13.474  -49.754 21.616 1.00 70.76  ? 1606 GLU A OE1   1 
ATOM   2976 O  OE2   . GLU A 1 389 ? 12.942  -50.185 23.690 1.00 70.04  ? 1606 GLU A OE2   1 
ATOM   2977 N  N     . MET A 1 390 ? 11.297  -44.426 22.495 1.00 76.58  ? 1607 MET A N     1 
ATOM   2978 C  CA    . MET A 1 390 ? 11.480  -43.109 21.880 1.00 74.02  ? 1607 MET A CA    1 
ATOM   2979 C  C     . MET A 1 390 ? 12.694  -42.350 22.411 1.00 78.36  ? 1607 MET A C     1 
ATOM   2980 O  O     . MET A 1 390 ? 13.523  -41.915 21.590 1.00 88.39  ? 1607 MET A O     1 
ATOM   2981 C  CB    . MET A 1 390 ? 10.213  -42.269 22.025 1.00 66.39  ? 1607 MET A CB    1 
ATOM   2982 C  CG    . MET A 1 390 ? 10.203  -41.109 21.085 1.00 59.37  ? 1607 MET A CG    1 
ATOM   2983 S  SD    . MET A 1 390 ? 10.952  -41.602 19.531 1.00 57.86  ? 1607 MET A SD    1 
ATOM   2984 C  CE    . MET A 1 390 ? 9.519   -41.902 18.498 1.00 43.56  ? 1607 MET A CE    1 
ATOM   2985 N  N     . PRO A 1 391 ? 12.880  -42.163 23.729 1.00 74.40  ? 1608 PRO A N     1 
ATOM   2986 C  CA    . PRO A 1 391 ? 14.087  -41.438 24.191 1.00 80.18  ? 1608 PRO A CA    1 
ATOM   2987 C  C     . PRO A 1 391 ? 15.405  -42.100 23.808 1.00 82.01  ? 1608 PRO A C     1 
ATOM   2988 O  O     . PRO A 1 391 ? 16.389  -41.389 23.529 1.00 90.78  ? 1608 PRO A O     1 
ATOM   2989 C  CB    . PRO A 1 391 ? 13.895  -41.381 25.711 1.00 74.10  ? 1608 PRO A CB    1 
ATOM   2990 C  CG    . PRO A 1 391 ? 12.412  -41.502 25.906 1.00 67.28  ? 1608 PRO A CG    1 
ATOM   2991 C  CD    . PRO A 1 391 ? 11.947  -42.434 24.839 1.00 63.07  ? 1608 PRO A CD    1 
ATOM   2992 N  N     . LYS A 1 392 ? 15.464  -43.439 23.824 1.00 64.98  ? 1609 LYS A N     1 
ATOM   2993 C  CA    . LYS A 1 392 ? 16.648  -44.132 23.322 1.00 51.47  ? 1609 LYS A CA    1 
ATOM   2994 C  C     . LYS A 1 392 ? 16.931  -43.739 21.878 1.00 44.30  ? 1609 LYS A C     1 
ATOM   2995 O  O     . LYS A 1 392 ? 18.087  -43.567 21.488 1.00 45.69  ? 1609 LYS A O     1 
ATOM   2996 C  CB    . LYS A 1 392 ? 16.490  -45.648 23.443 1.00 46.33  ? 1609 LYS A CB    1 
ATOM   2997 N  N     . LEU A 1 393 ? 15.893  -43.701 21.044 1.00 46.13  ? 1610 LEU A N     1 
ATOM   2998 C  CA    . LEU A 1 393 ? 16.077  -43.292 19.655 1.00 50.44  ? 1610 LEU A CA    1 
ATOM   2999 C  C     . LEU A 1 393 ? 16.586  -41.868 19.572 1.00 46.36  ? 1610 LEU A C     1 
ATOM   3000 O  O     . LEU A 1 393 ? 17.378  -41.536 18.688 1.00 54.26  ? 1610 LEU A O     1 
ATOM   3001 C  CB    . LEU A 1 393 ? 14.789  -43.466 18.845 1.00 63.35  ? 1610 LEU A CB    1 
ATOM   3002 C  CG    . LEU A 1 393 ? 15.006  -43.463 17.315 1.00 61.19  ? 1610 LEU A CG    1 
ATOM   3003 C  CD1   . LEU A 1 393 ? 15.712  -44.717 16.794 1.00 62.07  ? 1610 LEU A CD1   1 
ATOM   3004 C  CD2   . LEU A 1 393 ? 13.700  -43.250 16.585 1.00 54.92  ? 1610 LEU A CD2   1 
ATOM   3005 N  N     . LEU A 1 394 ? 16.080  -40.991 20.431 1.00 48.90  ? 1611 LEU A N     1 
ATOM   3006 C  CA    . LEU A 1 394 ? 16.559  -39.614 20.402 1.00 43.21  ? 1611 LEU A CA    1 
ATOM   3007 C  C     . LEU A 1 394 ? 18.047  -39.566 20.716 1.00 52.23  ? 1611 LEU A C     1 
ATOM   3008 O  O     . LEU A 1 394 ? 18.818  -38.891 20.017 1.00 68.38  ? 1611 LEU A O     1 
ATOM   3009 C  CB    . LEU A 1 394 ? 15.745  -38.752 21.368 1.00 40.08  ? 1611 LEU A CB    1 
ATOM   3010 C  CG    . LEU A 1 394 ? 14.319  -38.598 20.798 1.00 46.00  ? 1611 LEU A CG    1 
ATOM   3011 C  CD1   . LEU A 1 394 ? 13.366  -37.764 21.638 1.00 52.50  ? 1611 LEU A CD1   1 
ATOM   3012 C  CD2   . LEU A 1 394 ? 14.372  -38.051 19.384 1.00 44.89  ? 1611 LEU A CD2   1 
ATOM   3013 N  N     . GLU A 1 395 ? 18.484  -40.325 21.724 1.00 43.10  ? 1612 GLU A N     1 
ATOM   3014 C  CA    . GLU A 1 395 ? 19.914  -40.350 22.019 1.00 44.74  ? 1612 GLU A CA    1 
ATOM   3015 C  C     . GLU A 1 395 ? 20.702  -40.950 20.859 1.00 45.53  ? 1612 GLU A C     1 
ATOM   3016 O  O     . GLU A 1 395 ? 21.752  -40.416 20.474 1.00 54.67  ? 1612 GLU A O     1 
ATOM   3017 C  CB    . GLU A 1 395 ? 20.167  -41.094 23.327 1.00 41.70  ? 1612 GLU A CB    1 
ATOM   3018 C  CG    . GLU A 1 395 ? 19.980  -40.211 24.544 1.00 44.66  ? 1612 GLU A CG    1 
ATOM   3019 C  CD    . GLU A 1 395 ? 19.381  -40.951 25.715 1.00 45.44  ? 1612 GLU A CD    1 
ATOM   3020 N  N     . THR A 1 396 ? 20.210  -42.067 20.307 1.00 43.36  ? 1613 THR A N     1 
ATOM   3021 C  CA    . THR A 1 396 ? 20.835  -42.750 19.173 1.00 58.75  ? 1613 THR A CA    1 
ATOM   3022 C  C     . THR A 1 396 ? 21.036  -41.801 18.002 1.00 61.65  ? 1613 THR A C     1 
ATOM   3023 O  O     . THR A 1 396 ? 22.106  -41.766 17.376 1.00 56.92  ? 1613 THR A O     1 
ATOM   3024 C  CB    . THR A 1 396 ? 19.943  -43.936 18.750 1.00 48.26  ? 1613 THR A CB    1 
ATOM   3025 O  OG1   . THR A 1 396 ? 19.972  -44.934 19.761 1.00 50.07  ? 1613 THR A OG1   1 
ATOM   3026 C  CG2   . THR A 1 396 ? 20.380  -44.561 17.447 1.00 45.88  ? 1613 THR A CG2   1 
ATOM   3027 N  N     . ILE A 1 397 ? 20.012  -41.011 17.712 1.00 59.23  ? 1614 ILE A N     1 
ATOM   3028 C  CA    . ILE A 1 397 ? 20.071  -40.068 16.612 1.00 61.26  ? 1614 ILE A CA    1 
ATOM   3029 C  C     . ILE A 1 397 ? 21.085  -38.978 16.925 1.00 67.57  ? 1614 ILE A C     1 
ATOM   3030 O  O     . ILE A 1 397 ? 21.901  -38.599 16.072 1.00 72.92  ? 1614 ILE A O     1 
ATOM   3031 C  CB    . ILE A 1 397 ? 18.660  -39.518 16.343 1.00 49.10  ? 1614 ILE A CB    1 
ATOM   3032 C  CG1   . ILE A 1 397 ? 17.835  -40.574 15.614 1.00 42.84  ? 1614 ILE A CG1   1 
ATOM   3033 C  CG2   . ILE A 1 397 ? 18.692  -38.206 15.579 1.00 51.95  ? 1614 ILE A CG2   1 
ATOM   3034 C  CD1   . ILE A 1 397 ? 16.514  -40.064 15.084 1.00 50.87  ? 1614 ILE A CD1   1 
ATOM   3035 N  N     . HIS A 1 398 ? 21.052  -38.455 18.154 1.00 55.31  ? 1615 HIS A N     1 
ATOM   3036 C  CA    . HIS A 1 398 ? 22.039  -37.455 18.531 1.00 58.69  ? 1615 HIS A CA    1 
ATOM   3037 C  C     . HIS A 1 398 ? 23.454  -37.952 18.258 1.00 65.79  ? 1615 HIS A C     1 
ATOM   3038 O  O     . HIS A 1 398 ? 24.252  -37.289 17.580 1.00 68.66  ? 1615 HIS A O     1 
ATOM   3039 C  CB    . HIS A 1 398 ? 21.902  -37.084 20.004 1.00 50.55  ? 1615 HIS A CB    1 
ATOM   3040 C  CG    . HIS A 1 398 ? 23.015  -36.204 20.478 1.00 61.12  ? 1615 HIS A CG    1 
ATOM   3041 N  ND1   . HIS A 1 398 ? 24.325  -36.630 20.542 1.00 67.62  ? 1615 HIS A ND1   1 
ATOM   3042 C  CD2   . HIS A 1 398 ? 23.027  -34.903 20.851 1.00 67.98  ? 1615 HIS A CD2   1 
ATOM   3043 C  CE1   . HIS A 1 398 ? 25.093  -35.641 20.957 1.00 68.80  ? 1615 HIS A CE1   1 
ATOM   3044 N  NE2   . HIS A 1 398 ? 24.329  -34.583 21.156 1.00 69.09  ? 1615 HIS A NE2   1 
ATOM   3045 N  N     . THR A 1 399 ? 23.803  -39.090 18.855 1.00 58.28  ? 1616 THR A N     1 
ATOM   3046 C  CA    . THR A 1 399 ? 25.175  -39.551 18.719 1.00 63.16  ? 1616 THR A CA    1 
ATOM   3047 C  C     . THR A 1 399 ? 25.469  -39.948 17.280 1.00 56.77  ? 1616 THR A C     1 
ATOM   3048 O  O     . THR A 1 399 ? 26.597  -39.804 16.820 1.00 48.22  ? 1616 THR A O     1 
ATOM   3049 C  CB    . THR A 1 399 ? 25.526  -40.653 19.720 1.00 63.32  ? 1616 THR A CB    1 
ATOM   3050 O  OG1   . THR A 1 399 ? 24.419  -41.531 19.881 1.00 53.89  ? 1616 THR A OG1   1 
ATOM   3051 C  CG2   . THR A 1 399 ? 25.911  -40.046 21.089 1.00 69.88  ? 1616 THR A CG2   1 
ATOM   3052 N  N     . SER A 1 400 ? 24.498  -40.429 16.530 1.00 59.11  ? 1617 SER A N     1 
ATOM   3053 C  CA    . SER A 1 400 ? 24.857  -40.682 15.145 1.00 65.34  ? 1617 SER A CA    1 
ATOM   3054 C  C     . SER A 1 400 ? 25.185  -39.369 14.424 1.00 61.70  ? 1617 SER A C     1 
ATOM   3055 O  O     . SER A 1 400 ? 26.143  -39.321 13.642 1.00 65.00  ? 1617 SER A O     1 
ATOM   3056 C  CB    . SER A 1 400 ? 23.713  -41.444 14.467 1.00 67.45  ? 1617 SER A CB    1 
ATOM   3057 O  OG    . SER A 1 400 ? 23.664  -41.191 13.077 1.00 72.74  ? 1617 SER A OG    1 
ATOM   3058 N  N     . MET A 1 401 ? 24.545  -38.261 14.819 1.00 53.39  ? 1618 MET A N     1 
ATOM   3059 C  CA    . MET A 1 401 ? 24.885  -36.956 14.248 1.00 51.35  ? 1618 MET A CA    1 
ATOM   3060 C  C     . MET A 1 401 ? 26.297  -36.539 14.634 1.00 59.08  ? 1618 MET A C     1 
ATOM   3061 O  O     . MET A 1 401 ? 27.121  -36.205 13.767 1.00 50.93  ? 1618 MET A O     1 
ATOM   3062 C  CB    . MET A 1 401 ? 23.894  -35.898 14.718 1.00 44.90  ? 1618 MET A CB    1 
ATOM   3063 C  CG    . MET A 1 401 ? 22.598  -35.858 13.947 1.00 55.09  ? 1618 MET A CG    1 
ATOM   3064 S  SD    . MET A 1 401 ? 21.539  -34.519 14.521 1.00 61.97  ? 1618 MET A SD    1 
ATOM   3065 C  CE    . MET A 1 401 ? 19.903  -35.126 14.199 1.00 60.99  ? 1618 MET A CE    1 
ATOM   3066 N  N     . TYR A 1 402 ? 26.574  -36.523 15.943 1.00 65.29  ? 1619 TYR A N     1 
ATOM   3067 C  CA    . TYR A 1 402 ? 27.901  -36.145 16.412 1.00 59.74  ? 1619 TYR A CA    1 
ATOM   3068 C  C     . TYR A 1 402 ? 28.973  -37.025 15.782 1.00 63.86  ? 1619 TYR A C     1 
ATOM   3069 O  O     . TYR A 1 402 ? 30.010  -36.525 15.342 1.00 62.68  ? 1619 TYR A O     1 
ATOM   3070 C  CB    . TYR A 1 402 ? 28.017  -36.219 17.936 1.00 62.37  ? 1619 TYR A CB    1 
ATOM   3071 C  CG    . TYR A 1 402 ? 29.386  -35.718 18.384 1.00 74.21  ? 1619 TYR A CG    1 
ATOM   3072 C  CD1   . TYR A 1 402 ? 29.555  -34.419 18.832 1.00 75.57  ? 1619 TYR A CD1   1 
ATOM   3073 C  CD2   . TYR A 1 402 ? 30.520  -36.523 18.311 1.00 82.64  ? 1619 TYR A CD2   1 
ATOM   3074 C  CE1   . TYR A 1 402 ? 30.797  -33.941 19.210 1.00 68.86  ? 1619 TYR A CE1   1 
ATOM   3075 C  CE2   . TYR A 1 402 ? 31.768  -36.040 18.682 1.00 83.11  ? 1619 TYR A CE2   1 
ATOM   3076 C  CZ    . TYR A 1 402 ? 31.896  -34.748 19.134 1.00 68.67  ? 1619 TYR A CZ    1 
ATOM   3077 O  OH    . TYR A 1 402 ? 33.132  -34.272 19.511 1.00 71.36  ? 1619 TYR A OH    1 
ATOM   3078 N  N     . GLU A 1 403 ? 28.782  -38.348 15.815 1.00 59.12  ? 1620 GLU A N     1 
ATOM   3079 C  CA    . GLU A 1 403 ? 29.800  -39.259 15.311 1.00 49.84  ? 1620 GLU A CA    1 
ATOM   3080 C  C     . GLU A 1 403 ? 30.079  -39.027 13.837 1.00 48.54  ? 1620 GLU A C     1 
ATOM   3081 O  O     . GLU A 1 403 ? 31.246  -39.015 13.425 1.00 43.99  ? 1620 GLU A O     1 
ATOM   3082 C  CB    . GLU A 1 403 ? 29.392  -40.704 15.583 1.00 44.25  ? 1620 GLU A CB    1 
ATOM   3083 C  CG    . GLU A 1 403 ? 29.183  -40.963 17.070 1.00 44.08  ? 1620 GLU A CG    1 
ATOM   3084 C  CD    . GLU A 1 403 ? 29.922  -42.153 17.604 1.00 66.79  ? 1620 GLU A CD    1 
ATOM   3085 O  OE1   . GLU A 1 403 ? 30.333  -42.066 18.781 1.00 68.02  ? 1620 GLU A OE1   1 
ATOM   3086 O  OE2   . GLU A 1 403 ? 30.094  -43.156 16.861 1.00 71.85  ? 1620 GLU A OE2   1 
ATOM   3087 N  N     . ARG A 1 404 ? 29.033  -38.852 13.020 1.00 43.24  ? 1621 ARG A N     1 
ATOM   3088 C  CA    . ARG A 1 404 ? 29.267  -38.557 11.608 1.00 45.04  ? 1621 ARG A CA    1 
ATOM   3089 C  C     . ARG A 1 404 ? 30.025  -37.249 11.443 1.00 56.40  ? 1621 ARG A C     1 
ATOM   3090 O  O     . ARG A 1 404 ? 30.997  -37.178 10.675 1.00 72.00  ? 1621 ARG A O     1 
ATOM   3091 C  CB    . ARG A 1 404 ? 27.945  -38.502 10.851 1.00 46.37  ? 1621 ARG A CB    1 
ATOM   3092 C  CG    . ARG A 1 404 ? 28.061  -38.575 9.347  1.00 50.50  ? 1621 ARG A CG    1 
ATOM   3093 C  CD    . ARG A 1 404 ? 26.684  -38.435 8.678  1.00 60.84  ? 1621 ARG A CD    1 
ATOM   3094 N  NE    . ARG A 1 404 ? 25.752  -39.522 8.997  1.00 70.64  ? 1621 ARG A NE    1 
ATOM   3095 C  CZ    . ARG A 1 404 ? 24.829  -39.494 9.962  1.00 77.70  ? 1621 ARG A CZ    1 
ATOM   3096 N  NH1   . ARG A 1 404 ? 24.679  -38.423 10.739 1.00 82.05  ? 1621 ARG A NH1   1 
ATOM   3097 N  NH2   . ARG A 1 404 ? 24.044  -40.551 10.149 1.00 72.40  ? 1621 ARG A NH2   1 
ATOM   3098 N  N     . ALA A 1 405 ? 29.644  -36.221 12.214 1.00 46.28  ? 1622 ALA A N     1 
ATOM   3099 C  CA    . ALA A 1 405 ? 30.319  -34.935 12.088 1.00 49.98  ? 1622 ALA A CA    1 
ATOM   3100 C  C     . ALA A 1 405 ? 31.776  -35.040 12.507 1.00 60.21  ? 1622 ALA A C     1 
ATOM   3101 O  O     . ALA A 1 405 ? 32.647  -34.391 11.920 1.00 64.19  ? 1622 ALA A O     1 
ATOM   3102 C  CB    . ALA A 1 405 ? 29.597  -33.882 12.930 1.00 47.91  ? 1622 ALA A CB    1 
ATOM   3103 N  N     . GLU A 1 406 ? 32.057  -35.872 13.509 1.00 70.07  ? 1623 GLU A N     1 
ATOM   3104 C  CA    . GLU A 1 406 ? 33.420  -36.043 13.989 1.00 76.51  ? 1623 GLU A CA    1 
ATOM   3105 C  C     . GLU A 1 406 ? 34.257  -36.821 12.987 1.00 69.89  ? 1623 GLU A C     1 
ATOM   3106 O  O     . GLU A 1 406 ? 35.426  -36.496 12.773 1.00 73.28  ? 1623 GLU A O     1 
ATOM   3107 C  CB    . GLU A 1 406 ? 33.416  -36.732 15.352 1.00 84.38  ? 1623 GLU A CB    1 
ATOM   3108 C  CG    . GLU A 1 406 ? 34.785  -36.847 15.973 1.00 94.65  ? 1623 GLU A CG    1 
ATOM   3109 C  CD    . GLU A 1 406 ? 34.781  -37.753 17.176 1.00 101.14 ? 1623 GLU A CD    1 
ATOM   3110 O  OE1   . GLU A 1 406 ? 33.732  -38.380 17.438 1.00 95.88  ? 1623 GLU A OE1   1 
ATOM   3111 O  OE2   . GLU A 1 406 ? 35.825  -37.835 17.856 1.00 107.68 ? 1623 GLU A OE2   1 
ATOM   3112 N  N     . ARG A 1 407 ? 33.692  -37.869 12.387 1.00 58.08  ? 1624 ARG A N     1 
ATOM   3113 C  CA    . ARG A 1 407 ? 34.408  -38.559 11.327 1.00 56.96  ? 1624 ARG A CA    1 
ATOM   3114 C  C     . ARG A 1 407 ? 34.728  -37.605 10.181 1.00 69.29  ? 1624 ARG A C     1 
ATOM   3115 O  O     . ARG A 1 407 ? 35.814  -37.673 9.588  1.00 84.48  ? 1624 ARG A O     1 
ATOM   3116 C  CB    . ARG A 1 407 ? 33.601  -39.752 10.845 1.00 53.11  ? 1624 ARG A CB    1 
ATOM   3117 N  N     . ASP A 1 408 ? 33.808  -36.684 9.878  1.00 65.67  ? 1625 ASP A N     1 
ATOM   3118 C  CA    . ASP A 1 408 ? 34.064  -35.681 8.838  1.00 66.66  ? 1625 ASP A CA    1 
ATOM   3119 C  C     . ASP A 1 408 ? 35.208  -34.745 9.223  1.00 63.82  ? 1625 ASP A C     1 
ATOM   3120 O  O     . ASP A 1 408 ? 36.125  -34.481 8.427  1.00 62.61  ? 1625 ASP A O     1 
ATOM   3121 C  CB    . ASP A 1 408 ? 32.792  -34.881 8.568  1.00 65.67  ? 1625 ASP A CB    1 
ATOM   3122 C  CG    . ASP A 1 408 ? 32.763  -34.276 7.178  1.00 77.98  ? 1625 ASP A CG    1 
ATOM   3123 O  OD1   . ASP A 1 408 ? 33.579  -34.687 6.325  1.00 85.66  ? 1625 ASP A OD1   1 
ATOM   3124 O  OD2   . ASP A 1 408 ? 31.915  -33.391 6.937  1.00 81.88  ? 1625 ASP A OD2   1 
ATOM   3125 N  N     . LEU A 1 409 ? 35.146  -34.210 10.436 1.00 56.76  ? 1626 LEU A N     1 
ATOM   3126 C  CA    . LEU A 1 409 ? 36.203  -33.338 10.910 1.00 42.98  ? 1626 LEU A CA    1 
ATOM   3127 C  C     . LEU A 1 409 ? 37.543  -34.055 10.870 1.00 60.45  ? 1626 LEU A C     1 
ATOM   3128 O  O     . LEU A 1 409 ? 38.529  -33.518 10.356 1.00 66.42  ? 1626 LEU A O     1 
ATOM   3129 C  CB    . LEU A 1 409 ? 35.872  -32.856 12.325 1.00 42.98  ? 1626 LEU A CB    1 
ATOM   3130 C  CG    . LEU A 1 409 ? 36.926  -32.072 13.125 1.00 56.87  ? 1626 LEU A CG    1 
ATOM   3131 C  CD1   . LEU A 1 409 ? 36.893  -30.576 12.848 1.00 40.47  ? 1626 LEU A CD1   1 
ATOM   3132 C  CD2   . LEU A 1 409 ? 36.748  -32.318 14.605 1.00 68.37  ? 1626 LEU A CD2   1 
ATOM   3133 N  N     . GLN A 1 410 ? 37.587  -35.295 11.370 1.00 66.08  ? 1627 GLN A N     1 
ATOM   3134 C  CA    . GLN A 1 410 ? 38.853  -36.024 11.434 1.00 63.53  ? 1627 GLN A CA    1 
ATOM   3135 C  C     . GLN A 1 410 ? 39.393  -36.326 10.043 1.00 55.81  ? 1627 GLN A C     1 
ATOM   3136 O  O     . GLN A 1 410 ? 40.611  -36.243 9.819  1.00 53.62  ? 1627 GLN A O     1 
ATOM   3137 C  CB    . GLN A 1 410 ? 38.681  -37.309 12.257 1.00 65.36  ? 1627 GLN A CB    1 
ATOM   3138 C  CG    . GLN A 1 410 ? 38.790  -37.082 13.778 1.00 75.02  ? 1627 GLN A CG    1 
ATOM   3139 C  CD    . GLN A 1 410 ? 38.050  -38.118 14.618 1.00 87.79  ? 1627 GLN A CD    1 
ATOM   3140 O  OE1   . GLN A 1 410 ? 37.545  -39.116 14.102 1.00 92.86  ? 1627 GLN A OE1   1 
ATOM   3141 N  NE2   . GLN A 1 410 ? 37.956  -37.861 15.921 1.00 92.80  ? 1627 GLN A NE2   1 
ATOM   3142 N  N     . SER A 1 411 ? 38.505  -36.531 9.071  1.00 50.38  ? 1628 SER A N     1 
ATOM   3143 C  CA    . SER A 1 411 ? 38.969  -36.810 7.728  1.00 54.54  ? 1628 SER A CA    1 
ATOM   3144 C  C     . SER A 1 411 ? 39.368  -35.540 6.995  1.00 61.69  ? 1628 SER A C     1 
ATOM   3145 O  O     . SER A 1 411 ? 40.048  -35.612 5.968  1.00 55.24  ? 1628 SER A O     1 
ATOM   3146 C  CB    . SER A 1 411 ? 37.866  -37.554 6.969  1.00 62.38  ? 1628 SER A CB    1 
ATOM   3147 O  OG    . SER A 1 411 ? 37.878  -37.249 5.591  1.00 72.25  ? 1628 SER A OG    1 
ATOM   3148 N  N     . HIS A 1 412 ? 39.021  -34.373 7.531  1.00 71.85  ? 1629 HIS A N     1 
ATOM   3149 C  CA    . HIS A 1 412 ? 39.537  -33.121 6.994  1.00 71.91  ? 1629 HIS A CA    1 
ATOM   3150 C  C     . HIS A 1 412 ? 40.654  -32.508 7.837  1.00 73.41  ? 1629 HIS A C     1 
ATOM   3151 O  O     . HIS A 1 412 ? 41.190  -31.467 7.454  1.00 79.46  ? 1629 HIS A O     1 
ATOM   3152 C  CB    . HIS A 1 412 ? 38.405  -32.107 6.845  1.00 73.77  ? 1629 HIS A CB    1 
ATOM   3153 C  CG    . HIS A 1 412 ? 37.482  -32.378 5.699  1.00 77.17  ? 1629 HIS A CG    1 
ATOM   3154 N  ND1   . HIS A 1 412 ? 37.196  -31.430 4.740  1.00 76.45  ? 1629 HIS A ND1   1 
ATOM   3155 C  CD2   . HIS A 1 412 ? 36.763  -33.476 5.368  1.00 78.32  ? 1629 HIS A CD2   1 
ATOM   3156 C  CE1   . HIS A 1 412 ? 36.350  -31.935 3.861  1.00 75.35  ? 1629 HIS A CE1   1 
ATOM   3157 N  NE2   . HIS A 1 412 ? 36.070  -33.175 4.220  1.00 77.93  ? 1629 HIS A NE2   1 
ATOM   3158 N  N     . THR A 1 413 ? 41.033  -33.108 8.962  1.00 63.96  ? 1630 THR A N     1 
ATOM   3159 C  CA    . THR A 1 413 ? 42.156  -32.602 9.743  1.00 61.17  ? 1630 THR A CA    1 
ATOM   3160 C  C     . THR A 1 413 ? 43.392  -33.402 9.354  1.00 83.56  ? 1630 THR A C     1 
ATOM   3161 O  O     . THR A 1 413 ? 43.423  -34.628 9.526  1.00 95.32  ? 1630 THR A O     1 
ATOM   3162 C  CB    . THR A 1 413 ? 41.910  -32.718 11.248 1.00 54.54  ? 1630 THR A CB    1 
ATOM   3163 O  OG1   . THR A 1 413 ? 40.548  -32.412 11.557 1.00 48.70  ? 1630 THR A OG1   1 
ATOM   3164 C  CG2   . THR A 1 413 ? 42.801  -31.772 12.005 1.00 52.08  ? 1630 THR A CG2   1 
ATOM   3165 N  N     . LYS A 1 414 ? 44.395  -32.710 8.810  1.00 80.87  ? 1631 LYS A N     1 
ATOM   3166 C  CA    . LYS A 1 414 ? 45.642  -33.319 8.372  1.00 68.17  ? 1631 LYS A CA    1 
ATOM   3167 C  C     . LYS A 1 414 ? 46.823  -32.596 9.017  1.00 67.05  ? 1631 LYS A C     1 
ATOM   3168 O  O     . LYS A 1 414 ? 46.766  -31.391 9.264  1.00 72.32  ? 1631 LYS A O     1 
ATOM   3169 C  CB    . LYS A 1 414 ? 45.725  -33.284 6.846  1.00 50.32  ? 1631 LYS A CB    1 
ATOM   3170 N  N     . LEU A 1 415 ? 47.899  -33.334 9.282  1.00 65.48  ? 1632 LEU A N     1 
ATOM   3171 C  CA    . LEU A 1 415 ? 49.073  -32.819 9.983  1.00 67.15  ? 1632 LEU A CA    1 
ATOM   3172 C  C     . LEU A 1 415 ? 50.307  -32.888 9.085  1.00 78.53  ? 1632 LEU A C     1 
ATOM   3173 O  O     . LEU A 1 415 ? 50.478  -33.844 8.322  1.00 94.92  ? 1632 LEU A O     1 
ATOM   3174 C  CB    . LEU A 1 415 ? 49.309  -33.603 11.293 1.00 65.38  ? 1632 LEU A CB    1 
ATOM   3175 C  CG    . LEU A 1 415 ? 50.684  -33.583 11.993 1.00 72.12  ? 1632 LEU A CG    1 
ATOM   3176 C  CD1   . LEU A 1 415 ? 50.878  -32.361 12.878 1.00 77.73  ? 1632 LEU A CD1   1 
ATOM   3177 C  CD2   . LEU A 1 415 ? 50.887  -34.819 12.831 1.00 73.50  ? 1632 LEU A CD2   1 
ATOM   3178 N  N     . THR A 1 416 ? 51.163  -31.864 9.169  1.00 73.33  ? 1633 THR A N     1 
ATOM   3179 C  CA    . THR A 1 416 ? 52.378  -31.813 8.363  1.00 66.71  ? 1633 THR A CA    1 
ATOM   3180 C  C     . THR A 1 416 ? 53.401  -30.872 8.979  1.00 66.22  ? 1633 THR A C     1 
ATOM   3181 O  O     . THR A 1 416 ? 53.067  -30.004 9.791  1.00 67.61  ? 1633 THR A O     1 
ATOM   3182 C  CB    . THR A 1 416 ? 52.122  -31.346 6.930  1.00 63.55  ? 1633 THR A CB    1 
ATOM   3183 O  OG1   . THR A 1 416 ? 53.377  -31.307 6.252  1.00 71.31  ? 1633 THR A OG1   1 
ATOM   3184 C  CG2   . THR A 1 416 ? 51.548  -29.941 6.901  1.00 53.14  ? 1633 THR A CG2   1 
ATOM   3185 N  N     . LYS A 1 417 ? 54.671  -31.081 8.578  1.00 60.59  ? 1634 LYS A N     1 
ATOM   3186 C  CA    . LYS A 1 417 ? 55.785  -30.186 8.867  1.00 58.89  ? 1634 LYS A CA    1 
ATOM   3187 C  C     . LYS A 1 417 ? 56.444  -29.627 7.616  1.00 68.86  ? 1634 LYS A C     1 
ATOM   3188 O  O     . LYS A 1 417 ? 57.337  -28.783 7.735  1.00 74.49  ? 1634 LYS A O     1 
ATOM   3189 C  CB    . LYS A 1 417 ? 56.851  -30.887 9.724  1.00 66.02  ? 1634 LYS A CB    1 
ATOM   3190 C  CG    . LYS A 1 417 ? 56.297  -31.488 10.994 1.00 74.12  ? 1634 LYS A CG    1 
ATOM   3191 C  CD    . LYS A 1 417 ? 57.353  -32.243 11.799 1.00 82.39  ? 1634 LYS A CD    1 
ATOM   3192 C  CE    . LYS A 1 417 ? 56.757  -32.750 13.118 1.00 86.14  ? 1634 LYS A CE    1 
ATOM   3193 N  NZ    . LYS A 1 417 ? 55.263  -33.017 13.060 1.00 83.87  ? 1634 LYS A NZ    1 
ATOM   3194 N  N     . GLN A 1 418 ? 56.035  -30.059 6.429  1.00 73.80  ? 1635 GLN A N     1 
ATOM   3195 C  CA    . GLN A 1 418 ? 56.555  -29.502 5.191  1.00 82.81  ? 1635 GLN A CA    1 
ATOM   3196 C  C     . GLN A 1 418 ? 55.510  -28.562 4.601  1.00 83.78  ? 1635 GLN A C     1 
ATOM   3197 O  O     . GLN A 1 418 ? 54.383  -28.975 4.308  1.00 87.56  ? 1635 GLN A O     1 
ATOM   3198 C  CB    . GLN A 1 418 ? 56.916  -30.612 4.207  1.00 90.23  ? 1635 GLN A CB    1 
ATOM   3199 C  CG    . GLN A 1 418 ? 57.901  -30.177 3.146  1.00 99.78  ? 1635 GLN A CG    1 
ATOM   3200 C  CD    . GLN A 1 418 ? 58.967  -29.260 3.709  1.00 108.49 ? 1635 GLN A CD    1 
ATOM   3201 O  OE1   . GLN A 1 418 ? 59.119  -28.119 3.266  1.00 111.91 ? 1635 GLN A OE1   1 
ATOM   3202 N  NE2   . GLN A 1 418 ? 59.702  -29.748 4.707  1.00 108.53 ? 1635 GLN A NE2   1 
ATOM   3203 N  N     . TRP A 1 419 ? 55.908  -27.304 4.413  1.00 82.08  ? 1636 TRP A N     1 
ATOM   3204 C  CA    . TRP A 1 419 ? 55.043  -26.272 3.849  1.00 77.87  ? 1636 TRP A CA    1 
ATOM   3205 C  C     . TRP A 1 419 ? 54.370  -26.732 2.563  1.00 78.73  ? 1636 TRP A C     1 
ATOM   3206 O  O     . TRP A 1 419 ? 53.194  -26.429 2.327  1.00 80.66  ? 1636 TRP A O     1 
ATOM   3207 C  CB    . TRP A 1 419 ? 55.878  -25.014 3.631  1.00 81.51  ? 1636 TRP A CB    1 
ATOM   3208 C  CG    . TRP A 1 419 ? 55.206  -23.900 2.932  1.00 81.96  ? 1636 TRP A CG    1 
ATOM   3209 C  CD1   . TRP A 1 419 ? 55.487  -23.439 1.685  1.00 85.87  ? 1636 TRP A CD1   1 
ATOM   3210 C  CD2   . TRP A 1 419 ? 54.166  -23.064 3.448  1.00 79.83  ? 1636 TRP A CD2   1 
ATOM   3211 N  NE1   . TRP A 1 419 ? 54.678  -22.375 1.382  1.00 86.80  ? 1636 TRP A NE1   1 
ATOM   3212 C  CE2   . TRP A 1 419 ? 53.856  -22.123 2.448  1.00 82.11  ? 1636 TRP A CE2   1 
ATOM   3213 C  CE3   . TRP A 1 419 ? 53.461  -23.025 4.653  1.00 85.09  ? 1636 TRP A CE3   1 
ATOM   3214 C  CZ2   . TRP A 1 419 ? 52.865  -21.155 2.610  1.00 88.08  ? 1636 TRP A CZ2   1 
ATOM   3215 C  CZ3   . TRP A 1 419 ? 52.478  -22.061 4.818  1.00 88.36  ? 1636 TRP A CZ3   1 
ATOM   3216 C  CH2   . TRP A 1 419 ? 52.185  -21.142 3.798  1.00 91.37  ? 1636 TRP A CH2   1 
ATOM   3217 N  N     . ALA A 1 420 ? 55.114  -27.435 1.703  1.00 77.95  ? 1637 ALA A N     1 
ATOM   3218 C  CA    . ALA A 1 420 ? 54.575  -27.886 0.423  1.00 71.88  ? 1637 ALA A CA    1 
ATOM   3219 C  C     . ALA A 1 420 ? 53.298  -28.697 0.606  1.00 72.97  ? 1637 ALA A C     1 
ATOM   3220 O  O     . ALA A 1 420 ? 52.265  -28.420 -0.027 1.00 76.35  ? 1637 ALA A O     1 
ATOM   3221 C  CB    . ALA A 1 420 ? 55.621  -28.711 -0.320 1.00 70.84  ? 1637 ALA A CB    1 
ATOM   3222 N  N     . GLU A 1 421 ? 53.338  -29.713 1.457  1.00 67.89  ? 1638 GLU A N     1 
ATOM   3223 C  CA    . GLU A 1 421 ? 52.116  -30.485 1.587  1.00 75.90  ? 1638 GLU A CA    1 
ATOM   3224 C  C     . GLU A 1 421 ? 51.072  -29.787 2.445  1.00 75.10  ? 1638 GLU A C     1 
ATOM   3225 O  O     . GLU A 1 421 ? 49.888  -30.121 2.345  1.00 84.97  ? 1638 GLU A O     1 
ATOM   3226 C  CB    . GLU A 1 421 ? 52.416  -31.884 2.111  1.00 85.62  ? 1638 GLU A CB    1 
ATOM   3227 C  CG    . GLU A 1 421 ? 53.270  -31.970 3.326  1.00 89.61  ? 1638 GLU A CG    1 
ATOM   3228 C  CD    . GLU A 1 421 ? 53.165  -33.344 3.935  1.00 99.06  ? 1638 GLU A CD    1 
ATOM   3229 O  OE1   . GLU A 1 421 ? 52.826  -34.275 3.179  1.00 104.26 ? 1638 GLU A OE1   1 
ATOM   3230 O  OE2   . GLU A 1 421 ? 53.382  -33.496 5.154  1.00 102.18 ? 1638 GLU A OE2   1 
ATOM   3231 N  N     . PHE A 1 422 ? 51.474  -28.817 3.263  1.00 66.83  ? 1639 PHE A N     1 
ATOM   3232 C  CA    . PHE A 1 422 ? 50.505  -27.912 3.868  1.00 75.31  ? 1639 PHE A CA    1 
ATOM   3233 C  C     . PHE A 1 422 ? 49.652  -27.259 2.790  1.00 80.84  ? 1639 PHE A C     1 
ATOM   3234 O  O     . PHE A 1 422 ? 48.415  -27.267 2.858  1.00 84.91  ? 1639 PHE A O     1 
ATOM   3235 C  CB    . PHE A 1 422 ? 51.260  -26.873 4.704  1.00 87.44  ? 1639 PHE A CB    1 
ATOM   3236 C  CG    . PHE A 1 422 ? 50.422  -25.715 5.195  1.00 85.01  ? 1639 PHE A CG    1 
ATOM   3237 C  CD1   . PHE A 1 422 ? 49.931  -25.703 6.488  1.00 83.10  ? 1639 PHE A CD1   1 
ATOM   3238 C  CD2   . PHE A 1 422 ? 50.182  -24.614 4.388  1.00 78.68  ? 1639 PHE A CD2   1 
ATOM   3239 C  CE1   . PHE A 1 422 ? 49.184  -24.632 6.956  1.00 77.39  ? 1639 PHE A CE1   1 
ATOM   3240 C  CE2   . PHE A 1 422 ? 49.437  -23.541 4.851  1.00 73.14  ? 1639 PHE A CE2   1 
ATOM   3241 C  CZ    . PHE A 1 422 ? 48.942  -23.549 6.135  1.00 71.05  ? 1639 PHE A CZ    1 
ATOM   3242 N  N     . LEU A 1 423 ? 50.308  -26.711 1.762  1.00 84.16  ? 1640 LEU A N     1 
ATOM   3243 C  CA    . LEU A 1 423 ? 49.579  -26.073 0.668  1.00 76.07  ? 1640 LEU A CA    1 
ATOM   3244 C  C     . LEU A 1 423 ? 48.746  -27.084 -0.117 1.00 79.05  ? 1640 LEU A C     1 
ATOM   3245 O  O     . LEU A 1 423 ? 47.623  -26.776 -0.520 1.00 83.96  ? 1640 LEU A O     1 
ATOM   3246 C  CB    . LEU A 1 423 ? 50.549  -25.352 -0.269 1.00 62.00  ? 1640 LEU A CB    1 
ATOM   3247 C  CG    . LEU A 1 423 ? 51.164  -24.031 0.188  1.00 55.25  ? 1640 LEU A CG    1 
ATOM   3248 C  CD1   . LEU A 1 423 ? 52.023  -23.443 -0.929 1.00 55.85  ? 1640 LEU A CD1   1 
ATOM   3249 C  CD2   . LEU A 1 423 ? 50.102  -23.040 0.652  1.00 54.83  ? 1640 LEU A CD2   1 
ATOM   3250 N  N     . GLN A 1 424 ? 49.278  -28.288 -0.357 1.00 75.66  ? 1641 GLN A N     1 
ATOM   3251 C  CA    . GLN A 1 424 ? 48.476  -29.328 -1.007 1.00 74.84  ? 1641 GLN A CA    1 
ATOM   3252 C  C     . GLN A 1 424 ? 47.179  -29.602 -0.237 1.00 86.11  ? 1641 GLN A C     1 
ATOM   3253 O  O     . GLN A 1 424 ? 46.069  -29.510 -0.792 1.00 86.17  ? 1641 GLN A O     1 
ATOM   3254 C  CB    . GLN A 1 424 ? 49.296  -30.608 -1.164 1.00 70.94  ? 1641 GLN A CB    1 
ATOM   3255 N  N     . PHE A 1 425 ? 47.303  -29.945 1.051  1.00 101.30 ? 1642 PHE A N     1 
ATOM   3256 C  CA    . PHE A 1 425 ? 46.128  -30.228 1.878  1.00 101.24 ? 1642 PHE A CA    1 
ATOM   3257 C  C     . PHE A 1 425 ? 45.133  -29.084 1.826  1.00 95.32  ? 1642 PHE A C     1 
ATOM   3258 O  O     . PHE A 1 425 ? 43.942  -29.294 1.572  1.00 97.61  ? 1642 PHE A O     1 
ATOM   3259 C  CB    . PHE A 1 425 ? 46.533  -30.475 3.334  1.00 94.17  ? 1642 PHE A CB    1 
ATOM   3260 C  CG    . PHE A 1 425 ? 47.328  -31.713 3.540  1.00 93.26  ? 1642 PHE A CG    1 
ATOM   3261 C  CD1   . PHE A 1 425 ? 47.455  -32.644 2.530  1.00 90.90  ? 1642 PHE A CD1   1 
ATOM   3262 C  CD2   . PHE A 1 425 ? 47.957  -31.946 4.742  1.00 99.59  ? 1642 PHE A CD2   1 
ATOM   3263 C  CE1   . PHE A 1 425 ? 48.190  -33.781 2.713  1.00 93.66  ? 1642 PHE A CE1   1 
ATOM   3264 C  CE2   . PHE A 1 425 ? 48.694  -33.091 4.939  1.00 101.55 ? 1642 PHE A CE2   1 
ATOM   3265 C  CZ    . PHE A 1 425 ? 48.809  -34.012 3.918  1.00 99.62  ? 1642 PHE A CZ    1 
ATOM   3266 N  N     . LEU A 1 426 ? 45.604  -27.861 2.069  1.00 86.62  ? 1643 LEU A N     1 
ATOM   3267 C  CA    . LEU A 1 426 ? 44.695  -26.726 2.039  1.00 87.98  ? 1643 LEU A CA    1 
ATOM   3268 C  C     . LEU A 1 426 ? 44.018  -26.591 0.680  1.00 93.26  ? 1643 LEU A C     1 
ATOM   3269 O  O     . LEU A 1 426 ? 42.795  -26.416 0.607  1.00 98.04  ? 1643 LEU A O     1 
ATOM   3270 C  CB    . LEU A 1 426 ? 45.432  -25.438 2.394  1.00 85.54  ? 1643 LEU A CB    1 
ATOM   3271 C  CG    . LEU A 1 426 ? 44.515  -24.215 2.341  1.00 82.81  ? 1643 LEU A CG    1 
ATOM   3272 C  CD1   . LEU A 1 426 ? 43.284  -24.395 3.245  1.00 86.38  ? 1643 LEU A CD1   1 
ATOM   3273 C  CD2   . LEU A 1 426 ? 45.284  -22.988 2.722  1.00 77.19  ? 1643 LEU A CD2   1 
ATOM   3274 N  N     . GLU A 1 427 ? 44.784  -26.703 -0.410 1.00 88.88  ? 1644 GLU A N     1 
ATOM   3275 C  CA    . GLU A 1 427 ? 44.200  -26.525 -1.733 1.00 85.33  ? 1644 GLU A CA    1 
ATOM   3276 C  C     . GLU A 1 427 ? 43.075  -27.515 -1.982 1.00 91.17  ? 1644 GLU A C     1 
ATOM   3277 O  O     . GLU A 1 427 ? 42.106  -27.177 -2.669 1.00 93.29  ? 1644 GLU A O     1 
ATOM   3278 C  CB    . GLU A 1 427 ? 45.278  -26.661 -2.810 1.00 77.59  ? 1644 GLU A CB    1 
ATOM   3279 N  N     . THR A 1 428 ? 43.180  -28.734 -1.458 1.00 86.64  ? 1645 THR A N     1 
ATOM   3280 C  CA    . THR A 1 428 ? 42.045  -29.664 -1.538 1.00 74.13  ? 1645 THR A CA    1 
ATOM   3281 C  C     . THR A 1 428 ? 41.173  -29.662 -0.278 1.00 67.76  ? 1645 THR A C     1 
ATOM   3282 O  O     . THR A 1 428 ? 40.829  -30.715 0.248  1.00 69.45  ? 1645 THR A O     1 
ATOM   3283 C  CB    . THR A 1 428 ? 42.495  -31.075 -1.895 1.00 69.79  ? 1645 THR A CB    1 
ATOM   3284 O  OG1   . THR A 1 428 ? 42.857  -31.795 -0.705 1.00 73.04  ? 1645 THR A OG1   1 
ATOM   3285 C  CG2   . THR A 1 428 ? 43.661  -31.033 -2.901 1.00 62.62  ? 1645 THR A CG2   1 
ATOM   3286 N  N     . LYS A 1 429 ? 40.849  -28.480 0.245  1.00 66.19  ? 1646 LYS A N     1 
ATOM   3287 C  CA    . LYS A 1 429 ? 39.661  -28.273 1.087  1.00 68.95  ? 1646 LYS A CA    1 
ATOM   3288 C  C     . LYS A 1 429 ? 39.750  -28.909 2.484  1.00 62.64  ? 1646 LYS A C     1 
ATOM   3289 O  O     . LYS A 1 429 ? 38.742  -29.339 3.042  1.00 62.11  ? 1646 LYS A O     1 
ATOM   3290 C  CB    . LYS A 1 429 ? 38.409  -28.779 0.342  1.00 61.85  ? 1646 LYS A CB    1 
ATOM   3291 C  CG    . LYS A 1 429 ? 37.035  -28.274 0.811  1.00 58.14  ? 1646 LYS A CG    1 
ATOM   3292 C  CD    . LYS A 1 429 ? 35.910  -29.161 0.245  1.00 58.44  ? 1646 LYS A CD    1 
ATOM   3293 C  CE    . LYS A 1 429 ? 34.750  -28.330 -0.324 1.00 61.75  ? 1646 LYS A CE    1 
ATOM   3294 N  NZ    . LYS A 1 429 ? 35.018  -27.787 -1.710 1.00 59.06  ? 1646 LYS A NZ    1 
ATOM   3295 N  N     . ASN A 1 430 ? 40.912  -28.901 3.121  1.00 53.83  ? 1647 ASN A N     1 
ATOM   3296 C  CA    . ASN A 1 430 ? 40.889  -29.385 4.498  1.00 64.67  ? 1647 ASN A CA    1 
ATOM   3297 C  C     . ASN A 1 430 ? 41.894  -28.591 5.318  1.00 65.44  ? 1647 ASN A C     1 
ATOM   3298 O  O     . ASN A 1 430 ? 42.658  -27.779 4.788  1.00 69.40  ? 1647 ASN A O     1 
ATOM   3299 C  CB    . ASN A 1 430 ? 41.051  -30.932 4.592  1.00 66.13  ? 1647 ASN A CB    1 
ATOM   3300 C  CG    . ASN A 1 430 ? 42.412  -31.449 4.196  1.00 56.16  ? 1647 ASN A CG    1 
ATOM   3301 O  OD1   . ASN A 1 430 ? 42.721  -31.618 3.009  1.00 63.41  ? 1647 ASN A OD1   1 
ATOM   3302 N  ND2   . ASN A 1 430 ? 43.213  -31.777 5.192  1.00 49.26  ? 1647 ASN A ND2   1 
ATOM   3303 N  N     . ILE A 1 431 ? 41.786  -28.757 6.621  1.00 57.21  ? 1648 ILE A N     1 
ATOM   3304 C  CA    . ILE A 1 431 ? 42.558  -28.010 7.575  1.00 61.19  ? 1648 ILE A CA    1 
ATOM   3305 C  C     . ILE A 1 431 ? 43.806  -28.670 8.097  1.00 62.74  ? 1648 ILE A C     1 
ATOM   3306 O  O     . ILE A 1 431 ? 43.870  -29.842 8.249  1.00 69.58  ? 1648 ILE A O     1 
ATOM   3307 C  CB    . ILE A 1 431 ? 41.645  -27.511 8.675  1.00 57.53  ? 1648 ILE A CB    1 
ATOM   3308 C  CG1   . ILE A 1 431 ? 41.012  -28.663 9.372  1.00 50.28  ? 1648 ILE A CG1   1 
ATOM   3309 C  CG2   . ILE A 1 431 ? 40.519  -26.757 8.043  1.00 42.50  ? 1648 ILE A CG2   1 
ATOM   3310 C  CD1   . ILE A 1 431 ? 40.660  -28.377 10.785 1.00 42.22  ? 1648 ILE A CD1   1 
ATOM   3311 N  N     . ILE A 1 432 ? 44.796  -27.865 8.415  1.00 55.10  ? 1649 ILE A N     1 
ATOM   3312 C  CA    . ILE A 1 432 ? 46.097  -28.353 8.739  1.00 56.14  ? 1649 ILE A CA    1 
ATOM   3313 C  C     . ILE A 1 432 ? 46.719  -27.944 10.007 1.00 58.16  ? 1649 ILE A C     1 
ATOM   3314 O  O     . ILE A 1 432 ? 46.735  -26.826 10.322 1.00 53.86  ? 1649 ILE A O     1 
ATOM   3315 C  CB    . ILE A 1 432 ? 47.082  -27.709 7.784  1.00 57.88  ? 1649 ILE A CB    1 
ATOM   3316 C  CG1   . ILE A 1 432 ? 46.479  -27.454 6.433  1.00 60.57  ? 1649 ILE A CG1   1 
ATOM   3317 C  CG2   . ILE A 1 432 ? 48.266  -28.590 7.569  1.00 61.47  ? 1649 ILE A CG2   1 
ATOM   3318 C  CD1   . ILE A 1 432 ? 47.447  -26.844 5.497  1.00 58.96  ? 1649 ILE A CD1   1 
ATOM   3319 N  N     . MET A 1 433 ? 47.348  -28.888 10.661 1.00 69.45  ? 1650 MET A N     1 
ATOM   3320 C  CA    . MET A 1 433 ? 48.049  -28.672 11.878 1.00 67.91  ? 1650 MET A CA    1 
ATOM   3321 C  C     . MET A 1 433 ? 49.513  -28.793 11.626 1.00 69.30  ? 1650 MET A C     1 
ATOM   3322 O  O     . MET A 1 433 ? 49.966  -29.837 11.346 1.00 65.06  ? 1650 MET A O     1 
ATOM   3323 C  CB    . MET A 1 433 ? 47.672  -29.761 12.783 1.00 70.52  ? 1650 MET A CB    1 
ATOM   3324 C  CG    . MET A 1 433 ? 47.981  -29.384 14.163 1.00 87.17  ? 1650 MET A CG    1 
ATOM   3325 S  SD    . MET A 1 433 ? 46.592  -29.955 15.047 1.00 98.23  ? 1650 MET A SD    1 
ATOM   3326 C  CE    . MET A 1 433 ? 47.355  -30.134 16.625 1.00 95.49  ? 1650 MET A CE    1 
ATOM   3327 N  N     . ALA A 1 434 ? 50.254  -27.717 11.827 1.00 72.24  ? 1651 ALA A N     1 
ATOM   3328 C  CA    . ALA A 1 434 ? 51.664  -27.637 11.537 1.00 62.63  ? 1651 ALA A CA    1 
ATOM   3329 C  C     . ALA A 1 434 ? 52.416  -26.924 12.607 1.00 68.54  ? 1651 ALA A C     1 
ATOM   3330 O  O     . ALA A 1 434 ? 51.866  -26.145 13.317 1.00 68.91  ? 1651 ALA A O     1 
ATOM   3331 C  CB    . ALA A 1 434 ? 51.850  -26.879 10.266 1.00 49.92  ? 1651 ALA A CB    1 
ATOM   3332 N  N     . PRO A 1 435 ? 53.698  -27.206 12.738 1.00 61.54  ? 1652 PRO A N     1 
ATOM   3333 C  CA    . PRO A 1 435 ? 54.510  -26.503 13.740 1.00 65.27  ? 1652 PRO A CA    1 
ATOM   3334 C  C     . PRO A 1 435 ? 54.643  -25.013 13.426 1.00 64.94  ? 1652 PRO A C     1 
ATOM   3335 O  O     . PRO A 1 435 ? 54.856  -24.608 12.278 1.00 59.74  ? 1652 PRO A O     1 
ATOM   3336 C  CB    . PRO A 1 435 ? 55.864  -27.233 13.687 1.00 62.10  ? 1652 PRO A CB    1 
ATOM   3337 C  CG    . PRO A 1 435 ? 55.855  -28.048 12.476 1.00 55.24  ? 1652 PRO A CG    1 
ATOM   3338 C  CD    . PRO A 1 435 ? 54.432  -28.329 12.127 1.00 55.59  ? 1652 PRO A CD    1 
ATOM   3339 N  N     . PHE A 1 436 ? 54.595  -24.200 14.480 1.00 56.69  ? 1653 PHE A N     1 
ATOM   3340 C  CA    . PHE A 1 436 ? 54.498  -22.764 14.305 1.00 60.39  ? 1653 PHE A CA    1 
ATOM   3341 C  C     . PHE A 1 436 ? 55.245  -22.026 15.414 1.00 78.60  ? 1653 PHE A C     1 
ATOM   3342 O  O     . PHE A 1 436 ? 55.303  -22.469 16.579 1.00 78.50  ? 1653 PHE A O     1 
ATOM   3343 C  CB    . PHE A 1 436 ? 53.040  -22.313 14.272 1.00 54.80  ? 1653 PHE A CB    1 
ATOM   3344 C  CG    . PHE A 1 436 ? 52.877  -20.884 13.856 1.00 57.60  ? 1653 PHE A CG    1 
ATOM   3345 C  CD1   . PHE A 1 436 ? 53.600  -20.381 12.785 1.00 54.39  ? 1653 PHE A CD1   1 
ATOM   3346 C  CD2   . PHE A 1 436 ? 52.022  -20.037 14.549 1.00 58.90  ? 1653 PHE A CD2   1 
ATOM   3347 C  CE1   . PHE A 1 436 ? 53.464  -19.055 12.397 1.00 62.64  ? 1653 PHE A CE1   1 
ATOM   3348 C  CE2   . PHE A 1 436 ? 51.880  -18.714 14.172 1.00 61.69  ? 1653 PHE A CE2   1 
ATOM   3349 C  CZ    . PHE A 1 436 ? 52.601  -18.216 13.095 1.00 65.41  ? 1653 PHE A CZ    1 
ATOM   3350 N  N     . CYS A 1 437 ? 55.821  -20.891 15.004 1.00 81.76  ? 1654 CYS A N     1 
ATOM   3351 C  CA    . CYS A 1 437 ? 56.597  -20.028 15.881 1.00 80.43  ? 1654 CYS A CA    1 
ATOM   3352 C  C     . CYS A 1 437 ? 55.730  -19.143 16.771 1.00 91.40  ? 1654 CYS A C     1 
ATOM   3353 O  O     . CYS A 1 437 ? 56.130  -18.856 17.900 1.00 110.73 ? 1654 CYS A O     1 
ATOM   3354 C  CB    . CYS A 1 437 ? 57.540  -19.176 15.025 1.00 75.33  ? 1654 CYS A CB    1 
ATOM   3355 S  SG    . CYS A 1 437 ? 56.720  -17.886 14.078 1.00 77.95  ? 1654 CYS A SG    1 
ATOM   3356 N  N     . GLY A 1 438 ? 54.556  -18.707 16.302 1.00 82.98  ? 1655 GLY A N     1 
ATOM   3357 C  CA    . GLY A 1 438 ? 53.701  -17.825 17.066 1.00 77.63  ? 1655 GLY A CA    1 
ATOM   3358 C  C     . GLY A 1 438 ? 53.731  -16.369 16.652 1.00 79.45  ? 1655 GLY A C     1 
ATOM   3359 O  O     . GLY A 1 438 ? 52.853  -15.596 17.075 1.00 82.78  ? 1655 GLY A O     1 
ATOM   3360 N  N     . GLU A 1 439 ? 54.699  -15.983 15.832 1.00 79.16  ? 1656 GLU A N     1 
ATOM   3361 C  CA    . GLU A 1 439 ? 54.897  -14.597 15.426 1.00 87.37  ? 1656 GLU A CA    1 
ATOM   3362 C  C     . GLU A 1 439 ? 53.868  -14.125 14.398 1.00 91.20  ? 1656 GLU A C     1 
ATOM   3363 O  O     . GLU A 1 439 ? 53.410  -14.888 13.533 1.00 95.19  ? 1656 GLU A O     1 
ATOM   3364 C  CB    . GLU A 1 439 ? 56.301  -14.409 14.856 1.00 85.62  ? 1656 GLU A CB    1 
ATOM   3365 C  CG    . GLU A 1 439 ? 57.419  -14.864 15.796 1.00 86.26  ? 1656 GLU A CG    1 
ATOM   3366 C  CD    . GLU A 1 439 ? 57.534  -14.024 17.065 1.00 83.97  ? 1656 GLU A CD    1 
ATOM   3367 O  OE1   . GLU A 1 439 ? 57.380  -12.784 16.997 1.00 84.00  ? 1656 GLU A OE1   1 
ATOM   3368 O  OE2   . GLU A 1 439 ? 57.776  -14.611 18.140 1.00 80.83  ? 1656 GLU A OE2   1 
ATOM   3369 N  N     . ILE A 1 440 ? 53.491  -12.846 14.515 1.00 85.22  ? 1657 ILE A N     1 
ATOM   3370 C  CA    . ILE A 1 440 ? 52.409  -12.319 13.692 1.00 72.12  ? 1657 ILE A CA    1 
ATOM   3371 C  C     . ILE A 1 440 ? 52.872  -11.973 12.288 1.00 72.81  ? 1657 ILE A C     1 
ATOM   3372 O  O     . ILE A 1 440 ? 52.130  -12.176 11.329 1.00 76.16  ? 1657 ILE A O     1 
ATOM   3373 C  CB    . ILE A 1 440 ? 51.752  -11.093 14.337 1.00 63.63  ? 1657 ILE A CB    1 
ATOM   3374 C  CG1   . ILE A 1 440 ? 51.368  -11.352 15.785 1.00 62.23  ? 1657 ILE A CG1   1 
ATOM   3375 C  CG2   . ILE A 1 440 ? 50.558  -10.661 13.520 1.00 60.79  ? 1657 ILE A CG2   1 
ATOM   3376 C  CD1   . ILE A 1 440 ? 51.187  -10.068 16.546 1.00 55.77  ? 1657 ILE A CD1   1 
ATOM   3377 N  N     . SER A 1 441 ? 54.058  -11.383 12.136 1.00 73.97  ? 1658 SER A N     1 
ATOM   3378 C  CA    . SER A 1 441 ? 54.557  -11.119 10.788 1.00 75.28  ? 1658 SER A CA    1 
ATOM   3379 C  C     . SER A 1 441 ? 54.666  -12.415 9.987  1.00 79.69  ? 1658 SER A C     1 
ATOM   3380 O  O     . SER A 1 441 ? 54.310  -12.471 8.800  1.00 81.28  ? 1658 SER A O     1 
ATOM   3381 C  CB    . SER A 1 441 ? 55.886  -10.365 10.854 1.00 75.74  ? 1658 SER A CB    1 
ATOM   3382 O  OG    . SER A 1 441 ? 56.996  -11.224 10.701 1.00 82.55  ? 1658 SER A OG    1 
ATOM   3383 N  N     . CYS A 1 442 ? 55.138  -13.475 10.636 1.00 79.22  ? 1659 CYS A N     1 
ATOM   3384 C  CA    . CYS A 1 442 ? 55.218  -14.770 9.973  1.00 72.84  ? 1659 CYS A CA    1 
ATOM   3385 C  C     . CYS A 1 442 ? 53.830  -15.310 9.639  1.00 68.26  ? 1659 CYS A C     1 
ATOM   3386 O  O     . CYS A 1 442 ? 53.609  -15.832 8.539  1.00 72.52  ? 1659 CYS A O     1 
ATOM   3387 C  CB    . CYS A 1 442 ? 55.968  -15.744 10.884 1.00 68.38  ? 1659 CYS A CB    1 
ATOM   3388 S  SG    . CYS A 1 442 ? 56.114  -17.415 10.273 1.00 65.17  ? 1659 CYS A SG    1 
ATOM   3389 N  N     . GLU A 1 443 ? 52.874  -15.156 10.559 1.00 58.91  ? 1660 GLU A N     1 
ATOM   3390 C  CA    . GLU A 1 443 ? 51.498  -15.560 10.284 1.00 58.19  ? 1660 GLU A CA    1 
ATOM   3391 C  C     . GLU A 1 443 ? 50.929  -14.814 9.073  1.00 66.71  ? 1660 GLU A C     1 
ATOM   3392 O  O     . GLU A 1 443 ? 50.238  -15.410 8.236  1.00 76.33  ? 1660 GLU A O     1 
ATOM   3393 C  CB    . GLU A 1 443 ? 50.649  -15.332 11.536 1.00 52.86  ? 1660 GLU A CB    1 
ATOM   3394 C  CG    . GLU A 1 443 ? 49.388  -16.165 11.641 1.00 53.49  ? 1660 GLU A CG    1 
ATOM   3395 C  CD    . GLU A 1 443 ? 48.692  -15.987 12.978 1.00 61.68  ? 1660 GLU A CD    1 
ATOM   3396 O  OE1   . GLU A 1 443 ? 49.384  -15.975 14.019 1.00 67.91  ? 1660 GLU A OE1   1 
ATOM   3397 O  OE2   . GLU A 1 443 ? 47.453  -15.866 12.995 1.00 65.88  ? 1660 GLU A OE2   1 
ATOM   3398 N  N     . ASP A 1 444 ? 51.215  -13.507 8.968  1.00 66.98  ? 1661 ASP A N     1 
ATOM   3399 C  CA    . ASP A 1 444 ? 50.823  -12.726 7.797  1.00 66.79  ? 1661 ASP A CA    1 
ATOM   3400 C  C     . ASP A 1 444 ? 51.422  -13.309 6.532  1.00 72.69  ? 1661 ASP A C     1 
ATOM   3401 O  O     . ASP A 1 444 ? 50.746  -13.390 5.498  1.00 79.38  ? 1661 ASP A O     1 
ATOM   3402 C  CB    . ASP A 1 444 ? 51.271  -11.271 7.947  1.00 73.25  ? 1661 ASP A CB    1 
ATOM   3403 C  CG    . ASP A 1 444 ? 50.540  -10.541 9.052  1.00 84.32  ? 1661 ASP A CG    1 
ATOM   3404 O  OD1   . ASP A 1 444 ? 51.168  -9.682  9.708  1.00 84.26  ? 1661 ASP A OD1   1 
ATOM   3405 O  OD2   . ASP A 1 444 ? 49.342  -10.833 9.272  1.00 94.35  ? 1661 ASP A OD2   1 
ATOM   3406 N  N     . ARG A 1 445 ? 52.703  -13.695 6.589  1.00 72.30  ? 1662 ARG A N     1 
ATOM   3407 C  CA    . ARG A 1 445 ? 53.333  -14.294 5.417  1.00 68.65  ? 1662 ARG A CA    1 
ATOM   3408 C  C     . ARG A 1 445 ? 52.643  -15.599 5.046  1.00 78.43  ? 1662 ARG A C     1 
ATOM   3409 O  O     . ARG A 1 445 ? 52.453  -15.895 3.859  1.00 78.76  ? 1662 ARG A O     1 
ATOM   3410 C  CB    . ARG A 1 445 ? 54.823  -14.529 5.661  1.00 58.15  ? 1662 ARG A CB    1 
ATOM   3411 N  N     . ILE A 1 446 ? 52.246  -16.385 6.052  1.00 85.55  ? 1663 ILE A N     1 
ATOM   3412 C  CA    . ILE A 1 446 ? 51.500  -17.618 5.788  1.00 86.23  ? 1663 ILE A CA    1 
ATOM   3413 C  C     . ILE A 1 446 ? 50.195  -17.307 5.057  1.00 87.32  ? 1663 ILE A C     1 
ATOM   3414 O  O     . ILE A 1 446 ? 49.900  -17.877 3.997  1.00 83.67  ? 1663 ILE A O     1 
ATOM   3415 C  CB    . ILE A 1 446 ? 51.222  -18.380 7.098  1.00 81.50  ? 1663 ILE A CB    1 
ATOM   3416 C  CG1   . ILE A 1 446 ? 52.504  -18.904 7.742  1.00 77.00  ? 1663 ILE A CG1   1 
ATOM   3417 C  CG2   . ILE A 1 446 ? 50.295  -19.548 6.831  1.00 86.07  ? 1663 ILE A CG2   1 
ATOM   3418 C  CD1   . ILE A 1 446 ? 52.254  -19.793 8.975  1.00 60.93  ? 1663 ILE A CD1   1 
ATOM   3419 N  N     . LYS A 1 447 ? 49.391  -16.396 5.619  1.00 79.09  ? 1664 LYS A N     1 
ATOM   3420 C  CA    . LYS A 1 447 ? 48.108  -16.067 5.005  1.00 72.36  ? 1664 LYS A CA    1 
ATOM   3421 C  C     . LYS A 1 447 ? 48.296  -15.560 3.580  1.00 74.37  ? 1664 LYS A C     1 
ATOM   3422 O  O     . LYS A 1 447 ? 47.553  -15.949 2.672  1.00 78.18  ? 1664 LYS A O     1 
ATOM   3423 C  CB    . LYS A 1 447 ? 47.355  -15.040 5.855  1.00 64.35  ? 1664 LYS A CB    1 
ATOM   3424 N  N     . ALA A 1 448 ? 49.306  -14.722 3.354  1.00 68.23  ? 1665 ALA A N     1 
ATOM   3425 C  CA    . ALA A 1 448 ? 49.553  -14.212 2.009  1.00 60.36  ? 1665 ALA A CA    1 
ATOM   3426 C  C     . ALA A 1 448 ? 49.917  -15.336 1.042  1.00 60.76  ? 1665 ALA A C     1 
ATOM   3427 O  O     . ALA A 1 448 ? 49.364  -15.417 -0.060 1.00 57.19  ? 1665 ALA A O     1 
ATOM   3428 C  CB    . ALA A 1 448 ? 50.638  -13.140 2.037  1.00 54.47  ? 1665 ALA A CB    1 
ATOM   3429 N  N     . GLU A 1 449 ? 50.868  -16.204 1.429  1.00 66.58  ? 1666 GLU A N     1 
ATOM   3430 C  CA    . GLU A 1 449 ? 51.439  -17.205 0.525  1.00 67.24  ? 1666 GLU A CA    1 
ATOM   3431 C  C     . GLU A 1 449 ? 50.496  -18.361 0.219  1.00 75.13  ? 1666 GLU A C     1 
ATOM   3432 O  O     . GLU A 1 449 ? 50.908  -19.269 -0.511 1.00 80.17  ? 1666 GLU A O     1 
ATOM   3433 C  CB    . GLU A 1 449 ? 52.744  -17.762 1.105  1.00 68.26  ? 1666 GLU A CB    1 
ATOM   3434 N  N     . SER A 1 450 ? 49.259  -18.352 0.726  1.00 77.35  ? 1667 SER A N     1 
ATOM   3435 C  CA    . SER A 1 450 ? 48.261  -19.341 0.335  1.00 64.74  ? 1667 SER A CA    1 
ATOM   3436 C  C     . SER A 1 450 ? 47.365  -18.836 -0.784 1.00 70.05  ? 1667 SER A C     1 
ATOM   3437 O  O     . SER A 1 450 ? 47.003  -19.607 -1.677 1.00 69.17  ? 1667 SER A O     1 
ATOM   3438 C  CB    . SER A 1 450 ? 47.385  -19.696 1.542  1.00 59.24  ? 1667 SER A CB    1 
ATOM   3439 O  OG    . SER A 1 450 ? 48.149  -19.713 2.735  1.00 65.24  ? 1667 SER A OG    1 
ATOM   3440 N  N     . ALA A 1 451 ? 47.065  -17.533 -0.778 1.00 81.53  ? 1668 ALA A N     1 
ATOM   3441 C  CA    . ALA A 1 451 ? 46.284  -16.851 -1.814 1.00 90.79  ? 1668 ALA A CA    1 
ATOM   3442 C  C     . ALA A 1 451 ? 46.954  -16.861 -3.187 1.00 97.59  ? 1668 ALA A C     1 
ATOM   3443 O  O     . ALA A 1 451 ? 47.003  -15.832 -3.872 1.00 100.79 ? 1668 ALA A O     1 
ATOM   3444 C  CB    . ALA A 1 451 ? 46.005  -15.436 -1.396 1.00 91.72  ? 1668 ALA A CB    1 
ATOM   3445 N  N     . PRO A 1 462 ? 35.366  -15.130 2.900  1.00 74.94  ? 1679 PRO A N     1 
ATOM   3446 C  CA    . PRO A 1 462 ? 35.869  -14.540 1.677  1.00 80.65  ? 1679 PRO A CA    1 
ATOM   3447 C  C     . PRO A 1 462 ? 37.336  -14.266 1.736  1.00 87.70  ? 1679 PRO A C     1 
ATOM   3448 O  O     . PRO A 1 462 ? 37.829  -13.430 1.025  1.00 98.26  ? 1679 PRO A O     1 
ATOM   3449 C  CB    . PRO A 1 462 ? 35.082  -13.266 1.587  1.00 77.08  ? 1679 PRO A CB    1 
ATOM   3450 C  CG    . PRO A 1 462 ? 33.762  -13.693 2.086  1.00 82.35  ? 1679 PRO A CG    1 
ATOM   3451 C  CD    . PRO A 1 462 ? 33.947  -14.833 3.045  1.00 77.75  ? 1679 PRO A CD    1 
ATOM   3452 N  N     . ALA A 1 463 ? 38.041  -14.971 2.588  1.00 80.83  ? 1680 ALA A N     1 
ATOM   3453 C  CA    . ALA A 1 463 ? 39.454  -14.799 2.621  1.00 78.84  ? 1680 ALA A CA    1 
ATOM   3454 C  C     . ALA A 1 463 ? 39.933  -16.085 2.048  1.00 77.58  ? 1680 ALA A C     1 
ATOM   3455 O  O     . ALA A 1 463 ? 39.707  -17.129 2.612  1.00 72.60  ? 1680 ALA A O     1 
ATOM   3456 C  CB    . ALA A 1 463 ? 39.933  -14.630 4.036  1.00 74.26  ? 1680 ALA A CB    1 
ATOM   3457 N  N     . MET A 1 464 ? 40.608  -15.985 0.918  1.00 80.06  ? 1681 MET A N     1 
ATOM   3458 C  CA    . MET A 1 464 ? 41.109  -17.130 0.202  1.00 79.25  ? 1681 MET A CA    1 
ATOM   3459 C  C     . MET A 1 464 ? 42.420  -17.634 0.747  1.00 82.07  ? 1681 MET A C     1 
ATOM   3460 O  O     . MET A 1 464 ? 42.838  -18.703 0.438  1.00 77.60  ? 1681 MET A O     1 
ATOM   3461 C  CB    . MET A 1 464 ? 41.208  -16.799 -1.267 1.00 78.20  ? 1681 MET A CB    1 
ATOM   3462 C  CG    . MET A 1 464 ? 40.654  -17.874 -2.158 1.00 82.15  ? 1681 MET A CG    1 
ATOM   3463 S  SD    . MET A 1 464 ? 39.085  -18.521 -1.614 1.00 89.15  ? 1681 MET A SD    1 
ATOM   3464 C  CE    . MET A 1 464 ? 38.074  -17.062 -1.632 1.00 88.56  ? 1681 MET A CE    1 
ATOM   3465 N  N     . GLY A 1 465 ? 43.059  -16.839 1.576  1.00 94.03  ? 1682 GLY A N     1 
ATOM   3466 C  CA    . GLY A 1 465 ? 44.301  -17.189 2.244  1.00 97.04  ? 1682 GLY A CA    1 
ATOM   3467 C  C     . GLY A 1 465 ? 44.088  -18.015 3.488  1.00 89.41  ? 1682 GLY A C     1 
ATOM   3468 O  O     . GLY A 1 465 ? 42.988  -18.246 3.850  1.00 94.08  ? 1682 GLY A O     1 
ATOM   3469 N  N     . ALA A 1 466 ? 45.131  -18.504 4.121  1.00 81.95  ? 1683 ALA A N     1 
ATOM   3470 C  CA    . ALA A 1 466 ? 44.962  -19.290 5.329  1.00 74.86  ? 1683 ALA A CA    1 
ATOM   3471 C  C     . ALA A 1 466 ? 45.212  -18.549 6.608  1.00 68.91  ? 1683 ALA A C     1 
ATOM   3472 O  O     . ALA A 1 466 ? 46.226  -17.951 6.780  1.00 71.41  ? 1683 ALA A O     1 
ATOM   3473 C  CB    . ALA A 1 466 ? 45.829  -20.503 5.287  1.00 75.09  ? 1683 ALA A CB    1 
ATOM   3474 N  N     . LYS A 1 467 ? 44.269  -18.661 7.522  1.00 63.17  ? 1684 LYS A N     1 
ATOM   3475 C  CA    . LYS A 1 467 ? 44.286  -18.010 8.823  1.00 58.52  ? 1684 LYS A CA    1 
ATOM   3476 C  C     . LYS A 1 467 ? 44.732  -18.990 9.904  1.00 53.02  ? 1684 LYS A C     1 
ATOM   3477 O  O     . LYS A 1 467 ? 44.664  -20.206 9.745  1.00 46.40  ? 1684 LYS A O     1 
ATOM   3478 C  CB    . LYS A 1 467 ? 42.892  -17.466 9.164  1.00 47.72  ? 1684 LYS A CB    1 
ATOM   3479 N  N     . SER A 1 468 ? 45.174  -18.453 11.025 1.00 60.35  ? 1685 SER A N     1 
ATOM   3480 C  CA    . SER A 1 468 ? 45.394  -19.312 12.170 1.00 66.43  ? 1685 SER A CA    1 
ATOM   3481 C  C     . SER A 1 468 ? 44.036  -19.532 12.802 1.00 77.01  ? 1685 SER A C     1 
ATOM   3482 O  O     . SER A 1 468 ? 43.288  -18.576 13.040 1.00 83.90  ? 1685 SER A O     1 
ATOM   3483 C  CB    . SER A 1 468 ? 46.383  -18.695 13.163 1.00 70.29  ? 1685 SER A CB    1 
ATOM   3484 O  OG    . SER A 1 468 ? 45.729  -18.026 14.238 1.00 73.50  ? 1685 SER A OG    1 
ATOM   3485 N  N     . LEU A 1 469 ? 43.701  -20.795 13.040 1.00 77.99  ? 1686 LEU A N     1 
ATOM   3486 C  CA    . LEU A 1 469 ? 42.437  -21.100 13.692 1.00 76.29  ? 1686 LEU A CA    1 
ATOM   3487 C  C     . LEU A 1 469 ? 42.661  -21.127 15.190 1.00 74.84  ? 1686 LEU A C     1 
ATOM   3488 O  O     . LEU A 1 469 ? 42.033  -20.362 15.928 1.00 74.67  ? 1686 LEU A O     1 
ATOM   3489 C  CB    . LEU A 1 469 ? 41.858  -22.415 13.169 1.00 76.16  ? 1686 LEU A CB    1 
ATOM   3490 C  CG    . LEU A 1 469 ? 41.683  -22.308 11.655 1.00 87.06  ? 1686 LEU A CG    1 
ATOM   3491 C  CD1   . LEU A 1 469 ? 41.221  -23.616 11.021 1.00 87.04  ? 1686 LEU A CD1   1 
ATOM   3492 C  CD2   . LEU A 1 469 ? 40.735  -21.154 11.324 1.00 92.17  ? 1686 LEU A CD2   1 
ATOM   3493 N  N     . CYS A 1 470 ? 43.540  -22.009 15.650 1.00 75.58  ? 1687 CYS A N     1 
ATOM   3494 C  CA    . CYS A 1 470 ? 43.871  -21.961 17.073 1.00 68.20  ? 1687 CYS A CA    1 
ATOM   3495 C  C     . CYS A 1 470 ? 45.078  -22.842 17.347 1.00 67.40  ? 1687 CYS A C     1 
ATOM   3496 O  O     . CYS A 1 470 ? 45.414  -23.730 16.559 1.00 68.77  ? 1687 CYS A O     1 
ATOM   3497 C  CB    . CYS A 1 470 ? 42.703  -22.361 17.952 1.00 61.11  ? 1687 CYS A CB    1 
ATOM   3498 S  SG    . CYS A 1 470 ? 42.388  -24.090 17.897 1.00 70.89  ? 1687 CYS A SG    1 
ATOM   3499 N  N     . ILE A 1 471 ? 45.702  -22.610 18.500 1.00 61.83  ? 1688 ILE A N     1 
ATOM   3500 C  CA    . ILE A 1 471 ? 46.669  -23.543 19.074 1.00 57.09  ? 1688 ILE A CA    1 
ATOM   3501 C  C     . ILE A 1 471 ? 45.896  -24.559 19.911 1.00 56.34  ? 1688 ILE A C     1 
ATOM   3502 O  O     . ILE A 1 471 ? 45.403  -24.198 20.994 1.00 40.65  ? 1688 ILE A O     1 
ATOM   3503 C  CB    . ILE A 1 471 ? 47.723  -22.821 19.922 1.00 50.04  ? 1688 ILE A CB    1 
ATOM   3504 C  CG1   . ILE A 1 471 ? 48.274  -21.595 19.187 1.00 51.08  ? 1688 ILE A CG1   1 
ATOM   3505 C  CG2   . ILE A 1 471 ? 48.841  -23.771 20.274 1.00 42.84  ? 1688 ILE A CG2   1 
ATOM   3506 C  CD1   . ILE A 1 471 ? 48.819  -20.514 20.099 1.00 41.77  ? 1688 ILE A CD1   1 
ATOM   3507 N  N     . PRO A 1 472 ? 45.768  -25.812 19.462 1.00 62.52  ? 1689 PRO A N     1 
ATOM   3508 C  CA    . PRO A 1 472 ? 44.877  -26.757 20.146 1.00 59.65  ? 1689 PRO A CA    1 
ATOM   3509 C  C     . PRO A 1 472 ? 45.365  -27.075 21.544 1.00 56.70  ? 1689 PRO A C     1 
ATOM   3510 O  O     . PRO A 1 472 ? 46.562  -27.045 21.833 1.00 49.57  ? 1689 PRO A O     1 
ATOM   3511 C  CB    . PRO A 1 472 ? 44.925  -28.000 19.253 1.00 60.70  ? 1689 PRO A CB    1 
ATOM   3512 C  CG    . PRO A 1 472 ? 45.464  -27.523 17.947 1.00 62.49  ? 1689 PRO A CG    1 
ATOM   3513 C  CD    . PRO A 1 472 ? 46.403  -26.421 18.285 1.00 63.42  ? 1689 PRO A CD    1 
ATOM   3514 N  N     . PHE A 1 473 ? 44.407  -27.348 22.431 1.00 66.10  ? 1690 PHE A N     1 
ATOM   3515 C  CA    . PHE A 1 473 ? 44.760  -27.810 23.768 1.00 70.89  ? 1690 PHE A CA    1 
ATOM   3516 C  C     . PHE A 1 473 ? 45.263  -29.237 23.743 1.00 73.48  ? 1690 PHE A C     1 
ATOM   3517 O  O     . PHE A 1 473 ? 46.055  -29.622 24.604 1.00 79.41  ? 1690 PHE A O     1 
ATOM   3518 C  CB    . PHE A 1 473 ? 43.570  -27.684 24.704 1.00 75.74  ? 1690 PHE A CB    1 
ATOM   3519 C  CG    . PHE A 1 473 ? 43.303  -26.276 25.128 1.00 71.70  ? 1690 PHE A CG    1 
ATOM   3520 C  CD1   . PHE A 1 473 ? 44.203  -25.273 24.814 1.00 63.12  ? 1690 PHE A CD1   1 
ATOM   3521 C  CD2   . PHE A 1 473 ? 42.152  -25.952 25.830 1.00 67.17  ? 1690 PHE A CD2   1 
ATOM   3522 C  CE1   . PHE A 1 473 ? 43.959  -23.978 25.189 1.00 60.01  ? 1690 PHE A CE1   1 
ATOM   3523 C  CE2   . PHE A 1 473 ? 41.910  -24.646 26.214 1.00 58.90  ? 1690 PHE A CE2   1 
ATOM   3524 C  CZ    . PHE A 1 473 ? 42.809  -23.664 25.893 1.00 58.00  ? 1690 PHE A CZ    1 
ATOM   3525 N  N     . GLU A 1 474 ? 44.850  -29.985 22.741 1.00 68.31  ? 1691 GLU A N     1 
ATOM   3526 C  CA    . GLU A 1 474 ? 45.276  -31.334 22.572 1.00 58.97  ? 1691 GLU A CA    1 
ATOM   3527 C  C     . GLU A 1 474 ? 46.261  -31.302 21.494 1.00 60.89  ? 1691 GLU A C     1 
ATOM   3528 O  O     . GLU A 1 474 ? 45.932  -31.435 20.360 1.00 54.95  ? 1691 GLU A O     1 
ATOM   3529 C  CB    . GLU A 1 474 ? 44.135  -32.207 22.132 1.00 66.61  ? 1691 GLU A CB    1 
ATOM   3530 C  CG    . GLU A 1 474 ? 43.225  -32.588 23.273 1.00 80.86  ? 1691 GLU A CG    1 
ATOM   3531 C  CD    . GLU A 1 474 ? 42.024  -33.388 22.858 1.00 85.93  ? 1691 GLU A CD    1 
ATOM   3532 O  OE1   . GLU A 1 474 ? 42.016  -33.944 21.767 1.00 88.71  ? 1691 GLU A OE1   1 
ATOM   3533 O  OE2   . GLU A 1 474 ? 41.095  -33.473 23.645 1.00 85.58  ? 1691 GLU A OE2   1 
ATOM   3534 N  N     . GLN A 1 475 ? 47.495  -31.051 21.852 1.00 69.96  ? 1692 GLN A N     1 
ATOM   3535 C  CA    . GLN A 1 475 ? 48.547  -31.061 20.879 1.00 81.38  ? 1692 GLN A CA    1 
ATOM   3536 C  C     . GLN A 1 475 ? 48.918  -32.480 20.491 1.00 87.87  ? 1692 GLN A C     1 
ATOM   3537 O  O     . GLN A 1 475 ? 48.793  -33.407 21.270 1.00 73.04  ? 1692 GLN A O     1 
ATOM   3538 C  CB    . GLN A 1 475 ? 49.774  -30.373 21.439 1.00 81.99  ? 1692 GLN A CB    1 
ATOM   3539 C  CG    . GLN A 1 475 ? 49.656  -28.889 21.610 1.00 77.63  ? 1692 GLN A CG    1 
ATOM   3540 C  CD    . GLN A 1 475 ? 49.996  -28.115 20.379 1.00 71.60  ? 1692 GLN A CD    1 
ATOM   3541 O  OE1   . GLN A 1 475 ? 51.086  -28.173 19.887 1.00 74.38  ? 1692 GLN A OE1   1 
ATOM   3542 N  NE2   . GLN A 1 475 ? 49.070  -27.359 19.910 1.00 62.92  ? 1692 GLN A NE2   1 
ATOM   3543 N  N     . PRO A 1 476 ? 49.349  -32.656 19.258 1.00 101.63 ? 1693 PRO A N     1 
ATOM   3544 C  CA    . PRO A 1 476 ? 49.814  -33.956 18.832 1.00 106.97 ? 1693 PRO A CA    1 
ATOM   3545 C  C     . PRO A 1 476 ? 51.289  -33.758 18.762 1.00 115.47 ? 1693 PRO A C     1 
ATOM   3546 O  O     . PRO A 1 476 ? 51.679  -32.853 18.038 1.00 123.72 ? 1693 PRO A O     1 
ATOM   3547 C  CB    . PRO A 1 476 ? 49.285  -34.048 17.427 1.00 103.00 ? 1693 PRO A CB    1 
ATOM   3548 C  CG    . PRO A 1 476 ? 49.221  -32.643 16.965 1.00 103.01 ? 1693 PRO A CG    1 
ATOM   3549 C  CD    . PRO A 1 476 ? 49.232  -31.729 18.138 1.00 102.79 ? 1693 PRO A CD    1 
ATOM   3550 N  N     . ALA A 1 477 ? 52.036  -34.428 19.627 1.00 111.10 ? 1694 ALA A N     1 
ATOM   3551 C  CA    . ALA A 1 477 ? 53.498  -34.423 19.717 1.00 104.99 ? 1694 ALA A CA    1 
ATOM   3552 C  C     . ALA A 1 477 ? 54.098  -33.232 20.388 1.00 106.27 ? 1694 ALA A C     1 
ATOM   3553 O  O     . ALA A 1 477 ? 53.622  -32.129 20.256 1.00 108.75 ? 1694 ALA A O     1 
ATOM   3554 C  CB    . ALA A 1 477 ? 54.211  -34.727 18.415 1.00 99.40  ? 1694 ALA A CB    1 
ATOM   3555 N  N     . LYS A 1 478 ? 55.209  -33.457 21.054 1.00 100.28 ? 1695 LYS A N     1 
ATOM   3556 C  CA    . LYS A 1 478 ? 55.886  -32.381 21.696 1.00 94.77  ? 1695 LYS A CA    1 
ATOM   3557 C  C     . LYS A 1 478 ? 56.562  -31.626 20.596 1.00 86.96  ? 1695 LYS A C     1 
ATOM   3558 O  O     . LYS A 1 478 ? 57.051  -32.197 19.653 1.00 78.31  ? 1695 LYS A O     1 
ATOM   3559 C  CB    . LYS A 1 478 ? 56.883  -32.913 22.705 1.00 97.63  ? 1695 LYS A CB    1 
ATOM   3560 N  N     . ILE A 1 479 ? 56.558  -30.325 20.695 1.00 86.51  ? 1696 ILE A N     1 
ATOM   3561 C  CA    . ILE A 1 479 ? 57.205  -29.552 19.693 1.00 82.57  ? 1696 ILE A CA    1 
ATOM   3562 C  C     . ILE A 1 479 ? 58.508  -29.309 20.340 1.00 91.41  ? 1696 ILE A C     1 
ATOM   3563 O  O     . ILE A 1 479 ? 58.746  -28.270 20.887 1.00 98.80  ? 1696 ILE A O     1 
ATOM   3564 C  CB    . ILE A 1 479 ? 56.507  -28.229 19.420 1.00 65.06  ? 1696 ILE A CB    1 
ATOM   3565 N  N     . ASP A 1 480 ? 59.353  -30.311 20.268 1.00 95.75  ? 1697 ASP A N     1 
ATOM   3566 C  CA    . ASP A 1 480 ? 60.670  -30.297 20.866 1.00 105.20 ? 1697 ASP A CA    1 
ATOM   3567 C  C     . ASP A 1 480 ? 61.708  -29.513 20.052 1.00 106.42 ? 1697 ASP A C     1 
ATOM   3568 O  O     . ASP A 1 480 ? 62.024  -29.866 18.951 1.00 100.71 ? 1697 ASP A O     1 
ATOM   3569 C  CB    . ASP A 1 480 ? 61.092  -31.726 21.028 1.00 108.45 ? 1697 ASP A CB    1 
ATOM   3570 N  N     . PRO A 1 481 ? 62.364  -28.542 20.665 1.00 105.56 ? 1698 PRO A N     1 
ATOM   3571 C  CA    . PRO A 1 481 ? 63.253  -27.626 19.971 1.00 100.02 ? 1698 PRO A CA    1 
ATOM   3572 C  C     . PRO A 1 481 ? 64.573  -28.109 19.500 1.00 102.47 ? 1698 PRO A C     1 
ATOM   3573 O  O     . PRO A 1 481 ? 65.299  -27.271 18.999 1.00 102.86 ? 1698 PRO A O     1 
ATOM   3574 C  CB    . PRO A 1 481 ? 63.450  -26.502 20.974 1.00 94.33  ? 1698 PRO A CB    1 
ATOM   3575 C  CG    . PRO A 1 481 ? 62.223  -26.525 21.780 1.00 95.34  ? 1698 PRO A CG    1 
ATOM   3576 C  CD    . PRO A 1 481 ? 61.985  -27.993 21.962 1.00 104.18 ? 1698 PRO A CD    1 
ATOM   3577 N  N     . LYS A 1 482 ? 64.924  -29.373 19.679 1.00 109.35 ? 1699 LYS A N     1 
ATOM   3578 C  CA    . LYS A 1 482 ? 66.223  -29.800 19.215 1.00 110.90 ? 1699 LYS A CA    1 
ATOM   3579 C  C     . LYS A 1 482 ? 66.323  -29.593 17.757 1.00 105.13 ? 1699 LYS A C     1 
ATOM   3580 O  O     . LYS A 1 482 ? 67.254  -28.987 17.297 1.00 109.08 ? 1699 LYS A O     1 
ATOM   3581 C  CB    . LYS A 1 482 ? 66.372  -31.277 19.428 1.00 111.70 ? 1699 LYS A CB    1 
ATOM   3582 N  N     . VAL A 1 483 ? 65.333  -30.038 17.018 1.00 99.18  ? 1700 VAL A N     1 
ATOM   3583 C  CA    . VAL A 1 483 ? 65.365  -29.793 15.612 1.00 99.52  ? 1700 VAL A CA    1 
ATOM   3584 C  C     . VAL A 1 483 ? 64.133  -29.076 15.066 1.00 97.66  ? 1700 VAL A C     1 
ATOM   3585 O  O     . VAL A 1 483 ? 64.222  -28.414 14.053 1.00 98.36  ? 1700 VAL A O     1 
ATOM   3586 C  CB    . VAL A 1 483 ? 65.606  -31.089 14.842 1.00 96.36  ? 1700 VAL A CB    1 
ATOM   3587 N  N     . ASP A 1 484 ? 63.008  -29.154 15.759 1.00 88.88  ? 1701 ASP A N     1 
ATOM   3588 C  CA    . ASP A 1 484 ? 61.764  -28.580 15.255 1.00 85.65  ? 1701 ASP A CA    1 
ATOM   3589 C  C     . ASP A 1 484 ? 61.788  -27.164 14.808 1.00 88.11  ? 1701 ASP A C     1 
ATOM   3590 O  O     . ASP A 1 484 ? 62.162  -26.311 15.536 1.00 93.55  ? 1701 ASP A O     1 
ATOM   3591 C  CB    . ASP A 1 484 ? 60.659  -28.769 16.247 1.00 79.39  ? 1701 ASP A CB    1 
ATOM   3592 C  CG    . ASP A 1 484 ? 60.114  -30.110 16.194 1.00 79.25  ? 1701 ASP A CG    1 
ATOM   3593 O  OD1   . ASP A 1 484 ? 60.169  -30.676 15.116 1.00 86.52  ? 1701 ASP A OD1   1 
ATOM   3594 O  OD2   . ASP A 1 484 ? 59.653  -30.618 17.207 1.00 71.71  ? 1701 ASP A OD2   1 
ATOM   3595 N  N     . LYS A 1 485 ? 61.306  -26.926 13.608 1.00 79.64  ? 1702 LYS A N     1 
ATOM   3596 C  CA    . LYS A 1 485 ? 61.292  -25.592 13.028 1.00 65.81  ? 1702 LYS A CA    1 
ATOM   3597 C  C     . LYS A 1 485 ? 59.907  -25.239 12.502 1.00 79.40  ? 1702 LYS A C     1 
ATOM   3598 O  O     . LYS A 1 485 ? 59.114  -26.118 12.142 1.00 87.80  ? 1702 LYS A O     1 
ATOM   3599 C  CB    . LYS A 1 485 ? 62.319  -25.497 11.900 1.00 62.72  ? 1702 LYS A CB    1 
ATOM   3600 N  N     . CYS A 1 486 ? 59.648  -23.930 12.414 1.00 78.82  ? 1703 CYS A N     1 
ATOM   3601 C  CA    . CYS A 1 486 ? 58.354  -23.460 11.940 1.00 76.26  ? 1703 CYS A CA    1 
ATOM   3602 C  C     . CYS A 1 486 ? 58.150  -23.928 10.510 1.00 75.02  ? 1703 CYS A C     1 
ATOM   3603 O  O     . CYS A 1 486 ? 59.109  -24.072 9.750  1.00 81.67  ? 1703 CYS A O     1 
ATOM   3604 C  CB    . CYS A 1 486 ? 58.275  -21.930 12.031 1.00 77.52  ? 1703 CYS A CB    1 
ATOM   3605 S  SG    . CYS A 1 486 ? 56.787  -21.124 11.326 1.00 69.87  ? 1703 CYS A SG    1 
ATOM   3606 N  N     . VAL A 1 487 ? 56.886  -24.111 10.121 1.00 69.02  ? 1704 VAL A N     1 
ATOM   3607 C  CA    . VAL A 1 487 ? 56.598  -24.725 8.825  1.00 66.83  ? 1704 VAL A CA    1 
ATOM   3608 C  C     . VAL A 1 487 ? 56.825  -23.768 7.668  1.00 74.68  ? 1704 VAL A C     1 
ATOM   3609 O  O     . VAL A 1 487 ? 56.995  -24.216 6.524  1.00 79.82  ? 1704 VAL A O     1 
ATOM   3610 C  CB    . VAL A 1 487 ? 55.147  -25.230 8.824  1.00 63.15  ? 1704 VAL A CB    1 
ATOM   3611 C  CG1   . VAL A 1 487 ? 54.221  -24.098 9.267  1.00 51.44  ? 1704 VAL A CG1   1 
ATOM   3612 C  CG2   . VAL A 1 487 ? 54.734  -25.813 7.461  1.00 55.98  ? 1704 VAL A CG2   1 
ATOM   3613 N  N     . HIS A 1 488 ? 56.954  -22.472 7.948  1.00 72.41  ? 1705 HIS A N     1 
ATOM   3614 C  CA    . HIS A 1 488 ? 57.170  -21.608 6.801  1.00 70.30  ? 1705 HIS A CA    1 
ATOM   3615 C  C     . HIS A 1 488 ? 58.659  -21.528 6.509  1.00 74.56  ? 1705 HIS A C     1 
ATOM   3616 O  O     . HIS A 1 488 ? 59.473  -21.492 7.438  1.00 84.82  ? 1705 HIS A O     1 
ATOM   3617 C  CB    . HIS A 1 488 ? 56.631  -20.211 7.097  1.00 77.35  ? 1705 HIS A CB    1 
ATOM   3618 C  CG    . HIS A 1 488 ? 56.574  -19.301 5.909  1.00 82.96  ? 1705 HIS A CG    1 
ATOM   3619 N  ND1   . HIS A 1 488 ? 55.891  -19.613 4.752  1.00 85.80  ? 1705 HIS A ND1   1 
ATOM   3620 C  CD2   . HIS A 1 488 ? 57.095  -18.067 5.714  1.00 85.35  ? 1705 HIS A CD2   1 
ATOM   3621 C  CE1   . HIS A 1 488 ? 56.000  -18.613 3.894  1.00 84.97  ? 1705 HIS A CE1   1 
ATOM   3622 N  NE2   . HIS A 1 488 ? 56.730  -17.664 4.451  1.00 84.57  ? 1705 HIS A NE2   1 
ATOM   3623 N  N     . PRO A 1 489 ? 59.012  -21.490 5.226  1.00 71.83  ? 1706 PRO A N     1 
ATOM   3624 C  CA    . PRO A 1 489 ? 60.431  -21.491 4.858  1.00 76.12  ? 1706 PRO A CA    1 
ATOM   3625 C  C     . PRO A 1 489 ? 61.230  -20.328 5.402  1.00 80.12  ? 1706 PRO A C     1 
ATOM   3626 O  O     . PRO A 1 489 ? 62.422  -20.504 5.686  1.00 94.96  ? 1706 PRO A O     1 
ATOM   3627 C  CB    . PRO A 1 489 ? 60.380  -21.488 3.328  1.00 77.86  ? 1706 PRO A CB    1 
ATOM   3628 C  CG    . PRO A 1 489 ? 59.143  -22.280 3.036  1.00 74.96  ? 1706 PRO A CG    1 
ATOM   3629 C  CD    . PRO A 1 489 ? 58.154  -21.798 4.072  1.00 73.81  ? 1706 PRO A CD    1 
ATOM   3630 N  N     . ALA A 1 490 ? 60.637  -19.146 5.538  1.00 76.74  ? 1707 ALA A N     1 
ATOM   3631 C  CA    . ALA A 1 490 ? 61.375  -17.972 5.981  1.00 87.38  ? 1707 ALA A CA    1 
ATOM   3632 C  C     . ALA A 1 490 ? 61.223  -17.643 7.466  1.00 93.01  ? 1707 ALA A C     1 
ATOM   3633 O  O     . ALA A 1 490 ? 61.785  -16.639 7.919  1.00 95.15  ? 1707 ALA A O     1 
ATOM   3634 C  CB    . ALA A 1 490 ? 60.947  -16.764 5.146  1.00 89.35  ? 1707 ALA A CB    1 
ATOM   3635 N  N     . CYS A 1 491 ? 60.536  -18.467 8.248  1.00 95.09  ? 1708 CYS A N     1 
ATOM   3636 C  CA    . CYS A 1 491 ? 60.327  -18.071 9.629  1.00 96.00  ? 1708 CYS A CA    1 
ATOM   3637 C  C     . CYS A 1 491 ? 61.578  -18.236 10.491 1.00 111.30 ? 1708 CYS A C     1 
ATOM   3638 O  O     . CYS A 1 491 ? 62.488  -19.025 10.197 1.00 106.45 ? 1708 CYS A O     1 
ATOM   3639 C  CB    . CYS A 1 491 ? 59.196  -18.866 10.249 1.00 80.72  ? 1708 CYS A CB    1 
ATOM   3640 S  SG    . CYS A 1 491 ? 59.112  -18.463 11.945 1.00 79.12  ? 1708 CYS A SG    1 
ATOM   3641 N  N     . GLY A 1 492 ? 61.553  -17.520 11.625 1.00 129.02 ? 1709 GLY A N     1 
ATOM   3642 C  CA    . GLY A 1 492 ? 62.496  -17.655 12.720 1.00 127.32 ? 1709 GLY A CA    1 
ATOM   3643 C  C     . GLY A 1 492 ? 62.036  -18.848 13.514 1.00 114.70 ? 1709 GLY A C     1 
ATOM   3644 O  O     . GLY A 1 492 ? 61.241  -18.757 14.453 1.00 104.99 ? 1709 GLY A O     1 
ATOM   3645 N  N     . ARG A 1 493 ? 62.579  -19.986 13.101 1.00 111.47 ? 1710 ARG A N     1 
ATOM   3646 C  CA    . ARG A 1 493 ? 62.032  -21.308 13.376 1.00 112.38 ? 1710 ARG A CA    1 
ATOM   3647 C  C     . ARG A 1 493 ? 62.038  -21.669 14.862 1.00 111.49 ? 1710 ARG A C     1 
ATOM   3648 O  O     . ARG A 1 493 ? 62.742  -22.567 15.326 1.00 117.82 ? 1710 ARG A O     1 
ATOM   3649 C  CB    . ARG A 1 493 ? 62.806  -22.321 12.556 1.00 112.83 ? 1710 ARG A CB    1 
ATOM   3650 N  N     . VAL A 1 494 ? 61.188  -20.981 15.614 1.00 105.31 ? 1711 VAL A N     1 
ATOM   3651 C  CA    . VAL A 1 494 ? 61.080  -21.306 17.026 1.00 112.22 ? 1711 VAL A CA    1 
ATOM   3652 C  C     . VAL A 1 494 ? 60.464  -22.688 17.196 1.00 110.53 ? 1711 VAL A C     1 
ATOM   3653 O  O     . VAL A 1 494 ? 60.942  -23.500 17.997 1.00 117.84 ? 1711 VAL A O     1 
ATOM   3654 C  CB    . VAL A 1 494 ? 60.257  -20.236 17.769 1.00 116.35 ? 1711 VAL A CB    1 
ATOM   3655 N  N     . ALA A 1 495 ? 59.443  -22.998 16.400 1.00 98.12  ? 1712 ALA A N     1 
ATOM   3656 C  CA    . ALA A 1 495 ? 58.603  -24.171 16.615 1.00 87.54  ? 1712 ALA A CA    1 
ATOM   3657 C  C     . ALA A 1 495 ? 58.119  -24.165 18.066 1.00 80.97  ? 1712 ALA A C     1 
ATOM   3658 O  O     . ALA A 1 495 ? 58.443  -25.033 18.882 1.00 78.83  ? 1712 ALA A O     1 
ATOM   3659 C  CB    . ALA A 1 495 ? 59.327  -25.471 16.258 1.00 83.29  ? 1712 ALA A CB    1 
ATOM   3660 N  N     . LYS A 1 496 ? 57.322  -23.141 18.373 1.00 73.28  ? 1713 LYS A N     1 
ATOM   3661 C  CA    . LYS A 1 496 ? 56.802  -23.001 19.720 1.00 75.51  ? 1713 LYS A CA    1 
ATOM   3662 C  C     . LYS A 1 496 ? 55.692  -24.003 20.002 1.00 84.02  ? 1713 LYS A C     1 
ATOM   3663 O  O     . LYS A 1 496 ? 55.568  -24.473 21.141 1.00 83.36  ? 1713 LYS A O     1 
ATOM   3664 C  CB    . LYS A 1 496 ? 56.313  -21.570 19.949 1.00 68.67  ? 1713 LYS A CB    1 
ATOM   3665 N  N     . PHE A 1 497 ? 54.875  -24.359 19.021 1.00 89.63  ? 1714 PHE A N     1 
ATOM   3666 C  CA    . PHE A 1 497 ? 53.787  -25.338 19.203 1.00 94.97  ? 1714 PHE A CA    1 
ATOM   3667 C  C     . PHE A 1 497 ? 53.201  -25.707 17.889 1.00 102.30 ? 1714 PHE A C     1 
ATOM   3668 O  O     . PHE A 1 497 ? 53.719  -25.352 16.866 1.00 114.56 ? 1714 PHE A O     1 
ATOM   3669 C  CB    . PHE A 1 497 ? 52.607  -24.774 19.975 1.00 89.19  ? 1714 PHE A CB    1 
ATOM   3670 C  CG    . PHE A 1 497 ? 52.399  -23.338 19.759 1.00 85.84  ? 1714 PHE A CG    1 
ATOM   3671 C  CD1   . PHE A 1 497 ? 52.310  -22.850 18.520 1.00 87.11  ? 1714 PHE A CD1   1 
ATOM   3672 C  CD2   . PHE A 1 497 ? 52.419  -22.490 20.801 1.00 83.44  ? 1714 PHE A CD2   1 
ATOM   3673 C  CE1   . PHE A 1 497 ? 52.161  -21.527 18.309 1.00 85.99  ? 1714 PHE A CE1   1 
ATOM   3674 C  CE2   . PHE A 1 497 ? 52.285  -21.158 20.603 1.00 84.73  ? 1714 PHE A CE2   1 
ATOM   3675 C  CZ    . PHE A 1 497 ? 52.158  -20.673 19.350 1.00 83.08  ? 1714 PHE A CZ    1 
ATOM   3676 N  N     . TYR A 1 498 ? 52.126  -26.468 17.930 1.00 92.04  ? 1715 TYR A N     1 
ATOM   3677 C  CA    . TYR A 1 498 ? 51.372  -26.784 16.727 1.00 78.58  ? 1715 TYR A CA    1 
ATOM   3678 C  C     . TYR A 1 498 ? 50.206  -25.806 16.634 1.00 63.49  ? 1715 TYR A C     1 
ATOM   3679 O  O     . TYR A 1 498 ? 49.557  -25.499 17.640 1.00 53.36  ? 1715 TYR A O     1 
ATOM   3680 C  CB    . TYR A 1 498 ? 50.877  -28.238 16.741 1.00 77.70  ? 1715 TYR A CB    1 
ATOM   3681 C  CG    . TYR A 1 498 ? 51.967  -29.265 16.473 1.00 80.23  ? 1715 TYR A CG    1 
ATOM   3682 C  CD1   . TYR A 1 498 ? 52.280  -29.663 15.174 1.00 72.30  ? 1715 TYR A CD1   1 
ATOM   3683 C  CD2   . TYR A 1 498 ? 52.689  -29.831 17.520 1.00 85.21  ? 1715 TYR A CD2   1 
ATOM   3684 C  CE1   . TYR A 1 498 ? 53.277  -30.581 14.927 1.00 63.97  ? 1715 TYR A CE1   1 
ATOM   3685 C  CE2   . TYR A 1 498 ? 53.690  -30.754 17.280 1.00 81.76  ? 1715 TYR A CE2   1 
ATOM   3686 C  CZ    . TYR A 1 498 ? 53.977  -31.122 15.985 1.00 75.90  ? 1715 TYR A CZ    1 
ATOM   3687 O  OH    . TYR A 1 498 ? 54.976  -32.039 15.758 1.00 85.83  ? 1715 TYR A OH    1 
ATOM   3688 N  N     . THR A 1 499 ? 49.985  -25.261 15.452 1.00 52.52  ? 1716 THR A N     1 
ATOM   3689 C  CA    . THR A 1 499 ? 48.812  -24.444 15.223 1.00 47.65  ? 1716 THR A CA    1 
ATOM   3690 C  C     . THR A 1 499 ? 47.960  -25.033 14.111 1.00 56.80  ? 1716 THR A C     1 
ATOM   3691 O  O     . THR A 1 499 ? 48.475  -25.518 13.091 1.00 49.25  ? 1716 THR A O     1 
ATOM   3692 C  CB    . THR A 1 499 ? 49.195  -23.023 14.878 1.00 49.58  ? 1716 THR A CB    1 
ATOM   3693 O  OG1   . THR A 1 499 ? 50.021  -22.508 15.926 1.00 45.14  ? 1716 THR A OG1   1 
ATOM   3694 C  CG2   . THR A 1 499 ? 47.928  -22.165 14.710 1.00 49.93  ? 1716 THR A CG2   1 
ATOM   3695 N  N     . LEU A 1 500 ? 46.650  -24.968 14.324 1.00 68.67  ? 1717 LEU A N     1 
ATOM   3696 C  CA    . LEU A 1 500 ? 45.663  -25.351 13.342 1.00 70.60  ? 1717 LEU A CA    1 
ATOM   3697 C  C     . LEU A 1 500 ? 45.347  -24.128 12.503 1.00 81.80  ? 1717 LEU A C     1 
ATOM   3698 O  O     . LEU A 1 500 ? 44.973  -23.070 13.049 1.00 95.35  ? 1717 LEU A O     1 
ATOM   3699 C  CB    . LEU A 1 500 ? 44.410  -25.883 14.036 1.00 72.22  ? 1717 LEU A CB    1 
ATOM   3700 C  CG    . LEU A 1 500 ? 43.338  -26.594 13.213 1.00 79.25  ? 1717 LEU A CG    1 
ATOM   3701 C  CD1   . LEU A 1 500 ? 43.696  -28.050 12.985 1.00 83.13  ? 1717 LEU A CD1   1 
ATOM   3702 C  CD2   . LEU A 1 500 ? 41.987  -26.468 13.904 1.00 78.48  ? 1717 LEU A CD2   1 
ATOM   3703 N  N     . PHE A 1 501 ? 45.494  -24.310 11.183 1.00 69.63  ? 1718 PHE A N     1 
ATOM   3704 C  CA    . PHE A 1 501 ? 45.325  -23.363 10.092 1.00 63.01  ? 1718 PHE A CA    1 
ATOM   3705 C  C     . PHE A 1 501 ? 44.287  -23.886 9.108  1.00 75.25  ? 1718 PHE A C     1 
ATOM   3706 O  O     . PHE A 1 501 ? 44.044  -25.091 9.000  1.00 88.73  ? 1718 PHE A O     1 
ATOM   3707 C  CB    . PHE A 1 501 ? 46.628  -23.171 9.292  1.00 55.98  ? 1718 PHE A CB    1 
ATOM   3708 C  CG    . PHE A 1 501 ? 47.706  -22.409 10.015 1.00 62.66  ? 1718 PHE A CG    1 
ATOM   3709 C  CD1   . PHE A 1 501 ? 48.743  -23.080 10.653 1.00 60.67  ? 1718 PHE A CD1   1 
ATOM   3710 C  CD2   . PHE A 1 501 ? 47.707  -21.019 10.026 1.00 66.83  ? 1718 PHE A CD2   1 
ATOM   3711 C  CE1   . PHE A 1 501 ? 49.750  -22.381 11.305 1.00 57.09  ? 1718 PHE A CE1   1 
ATOM   3712 C  CE2   . PHE A 1 501 ? 48.711  -20.317 10.674 1.00 63.68  ? 1718 PHE A CE2   1 
ATOM   3713 C  CZ    . PHE A 1 501 ? 49.732  -21.004 11.315 1.00 61.11  ? 1718 PHE A CZ    1 
ATOM   3714 N  N     . GLY A 1 502 ? 43.703  -22.962 8.366  1.00 75.31  ? 1719 GLY A N     1 
ATOM   3715 C  CA    . GLY A 1 502 ? 42.828  -23.299 7.263  1.00 70.64  ? 1719 GLY A CA    1 
ATOM   3716 C  C     . GLY A 1 502 ? 42.063  -22.064 6.872  1.00 65.88  ? 1719 GLY A C     1 
ATOM   3717 O  O     . GLY A 1 502 ? 42.043  -21.067 7.592  1.00 60.60  ? 1719 GLY A O     1 
ATOM   3718 N  N     . ARG A 1 503 ? 41.364  -22.165 5.751  1.00 70.59  ? 1720 ARG A N     1 
ATOM   3719 C  CA    . ARG A 1 503 ? 40.449  -21.094 5.394  1.00 67.33  ? 1720 ARG A CA    1 
ATOM   3720 C  C     . ARG A 1 503 ? 39.366  -21.035 6.450  1.00 64.95  ? 1720 ARG A C     1 
ATOM   3721 O  O     . ARG A 1 503 ? 38.939  -22.067 6.978  1.00 72.61  ? 1720 ARG A O     1 
ATOM   3722 C  CB    . ARG A 1 503 ? 39.828  -21.341 4.018  1.00 76.20  ? 1720 ARG A CB    1 
ATOM   3723 C  CG    . ARG A 1 503 ? 40.850  -21.452 2.889  1.00 75.19  ? 1720 ARG A CG    1 
ATOM   3724 C  CD    . ARG A 1 503 ? 40.256  -21.096 1.552  1.00 66.44  ? 1720 ARG A CD    1 
ATOM   3725 N  NE    . ARG A 1 503 ? 41.266  -21.168 0.507  1.00 69.39  ? 1720 ARG A NE    1 
ATOM   3726 C  CZ    . ARG A 1 503 ? 41.507  -22.253 -0.221 1.00 76.00  ? 1720 ARG A CZ    1 
ATOM   3727 N  NH1   . ARG A 1 503 ? 40.810  -23.366 -0.004 1.00 83.00  ? 1720 ARG A NH1   1 
ATOM   3728 N  NH2   . ARG A 1 503 ? 42.450  -22.233 -1.159 1.00 72.16  ? 1720 ARG A NH2   1 
ATOM   3729 N  N     . SER A 1 504 ? 38.944  -19.825 6.791  1.00 67.41  ? 1721 SER A N     1 
ATOM   3730 C  CA    . SER A 1 504 ? 37.934  -19.650 7.825  1.00 72.01  ? 1721 SER A CA    1 
ATOM   3731 C  C     . SER A 1 504 ? 36.997  -18.516 7.437  1.00 73.55  ? 1721 SER A C     1 
ATOM   3732 O  O     . SER A 1 504 ? 37.257  -17.742 6.508  1.00 65.20  ? 1721 SER A O     1 
ATOM   3733 C  CB    . SER A 1 504 ? 38.569  -19.397 9.203  1.00 70.01  ? 1721 SER A CB    1 
ATOM   3734 O  OG    . SER A 1 504 ? 37.704  -18.721 10.113 1.00 74.63  ? 1721 SER A OG    1 
ATOM   3735 N  N     . TYR A 1 505 ? 35.905  -18.423 8.191  1.00 79.53  ? 1722 TYR A N     1 
ATOM   3736 C  CA    . TYR A 1 505 ? 34.928  -17.364 8.052  1.00 79.57  ? 1722 TYR A CA    1 
ATOM   3737 C  C     . TYR A 1 505 ? 35.473  -16.158 8.805  1.00 89.50  ? 1722 TYR A C     1 
ATOM   3738 O  O     . TYR A 1 505 ? 36.394  -16.306 9.622  1.00 93.05  ? 1722 TYR A O     1 
ATOM   3739 C  CB    . TYR A 1 505 ? 33.567  -17.796 8.612  1.00 71.58  ? 1722 TYR A CB    1 
ATOM   3740 C  CG    . TYR A 1 505 ? 32.757  -18.653 7.678  1.00 70.43  ? 1722 TYR A CG    1 
ATOM   3741 C  CD1   . TYR A 1 505 ? 31.830  -18.083 6.824  1.00 71.51  ? 1722 TYR A CD1   1 
ATOM   3742 C  CD2   . TYR A 1 505 ? 32.922  -20.031 7.646  1.00 71.72  ? 1722 TYR A CD2   1 
ATOM   3743 C  CE1   . TYR A 1 505 ? 31.082  -18.861 5.959  1.00 67.01  ? 1722 TYR A CE1   1 
ATOM   3744 C  CE2   . TYR A 1 505 ? 32.175  -20.818 6.782  1.00 68.22  ? 1722 TYR A CE2   1 
ATOM   3745 C  CZ    . TYR A 1 505 ? 31.257  -20.220 5.943  1.00 59.03  ? 1722 TYR A CZ    1 
ATOM   3746 O  OH    . TYR A 1 505 ? 30.509  -20.958 5.078  1.00 54.98  ? 1722 TYR A OH    1 
ATOM   3747 O  OXT   . TYR A 1 505 ? 35.026  -15.024 8.605  1.00 92.28  ? 1722 TYR A OXT   1 
ATOM   3748 N  N     . LEU B 1 6   ? 18.360  6.768   53.800 1.00 38.68  ? 1223 LEU B N     1 
ATOM   3749 C  CA    . LEU B 1 6   ? 17.334  7.310   52.910 1.00 55.86  ? 1223 LEU B CA    1 
ATOM   3750 C  C     . LEU B 1 6   ? 17.094  8.763   53.283 1.00 68.21  ? 1223 LEU B C     1 
ATOM   3751 O  O     . LEU B 1 6   ? 16.652  9.066   54.397 1.00 76.90  ? 1223 LEU B O     1 
ATOM   3752 C  CB    . LEU B 1 6   ? 16.020  6.505   52.988 1.00 59.15  ? 1223 LEU B CB    1 
ATOM   3753 C  CG    . LEU B 1 6   ? 15.204  6.429   51.671 1.00 56.10  ? 1223 LEU B CG    1 
ATOM   3754 C  CD1   . LEU B 1 6   ? 16.017  5.787   50.530 1.00 50.65  ? 1223 LEU B CD1   1 
ATOM   3755 C  CD2   . LEU B 1 6   ? 13.871  5.701   51.830 1.00 48.93  ? 1223 LEU B CD2   1 
ATOM   3756 N  N     . GLU B 1 7   ? 17.331  9.653   52.321 1.00 68.64  ? 1224 GLU B N     1 
ATOM   3757 C  CA    . GLU B 1 7   ? 17.401  11.086  52.581 1.00 74.81  ? 1224 GLU B CA    1 
ATOM   3758 C  C     . GLU B 1 7   ? 16.038  11.771  52.570 1.00 83.62  ? 1224 GLU B C     1 
ATOM   3759 O  O     . GLU B 1 7   ? 15.750  12.582  53.462 1.00 86.04  ? 1224 GLU B O     1 
ATOM   3760 C  CB    . GLU B 1 7   ? 18.335  11.746  51.558 1.00 78.71  ? 1224 GLU B CB    1 
ATOM   3761 C  CG    . GLU B 1 7   ? 19.805  11.343  51.710 1.00 90.12  ? 1224 GLU B CG    1 
ATOM   3762 C  CD    . GLU B 1 7   ? 20.741  12.066  50.733 1.00 97.56  ? 1224 GLU B CD    1 
ATOM   3763 O  OE1   . GLU B 1 7   ? 20.352  13.124  50.182 1.00 96.76  ? 1224 GLU B OE1   1 
ATOM   3764 O  OE2   . GLU B 1 7   ? 21.869  11.565  50.519 1.00 98.03  ? 1224 GLU B OE2   1 
ATOM   3765 N  N     . ALA B 1 8   ? 15.216  11.482  51.554 1.00 76.04  ? 1225 ALA B N     1 
ATOM   3766 C  CA    . ALA B 1 8   ? 13.924  12.119  51.316 1.00 65.54  ? 1225 ALA B CA    1 
ATOM   3767 C  C     . ALA B 1 8   ? 12.736  11.283  51.809 1.00 65.14  ? 1225 ALA B C     1 
ATOM   3768 O  O     . ALA B 1 8   ? 12.835  10.067  51.997 1.00 67.70  ? 1225 ALA B O     1 
ATOM   3769 C  CB    . ALA B 1 8   ? 13.774  12.402  49.824 1.00 62.95  ? 1225 ALA B CB    1 
ATOM   3770 N  N     . THR B 1 9   ? 11.588  11.952  51.994 1.00 57.56  ? 1226 THR B N     1 
ATOM   3771 C  CA    . THR B 1 9   ? 10.360  11.269  52.392 1.00 56.96  ? 1226 THR B CA    1 
ATOM   3772 C  C     . THR B 1 9   ? 9.364   11.186  51.240 1.00 60.08  ? 1226 THR B C     1 
ATOM   3773 O  O     . THR B 1 9   ? 9.309   12.060  50.372 1.00 53.58  ? 1226 THR B O     1 
ATOM   3774 C  CB    . THR B 1 9   ? 9.659   11.934  53.578 1.00 51.01  ? 1226 THR B CB    1 
ATOM   3775 O  OG1   . THR B 1 9   ? 9.768   13.361  53.495 1.00 47.26  ? 1226 THR B OG1   1 
ATOM   3776 C  CG2   . THR B 1 9   ? 10.241  11.426  54.863 1.00 54.66  ? 1226 THR B CG2   1 
ATOM   3777 N  N     . LYS B 1 10  ? 8.532   10.140  51.283 1.00 63.11  ? 1227 LYS B N     1 
ATOM   3778 C  CA    . LYS B 1 10  ? 7.586   9.888   50.201 1.00 62.99  ? 1227 LYS B CA    1 
ATOM   3779 C  C     . LYS B 1 10  ? 6.527   10.979  50.090 1.00 71.60  ? 1227 LYS B C     1 
ATOM   3780 O  O     . LYS B 1 10  ? 6.086   11.294  48.982 1.00 69.75  ? 1227 LYS B O     1 
ATOM   3781 C  CB    . LYS B 1 10  ? 6.929   8.518   50.398 1.00 51.27  ? 1227 LYS B CB    1 
ATOM   3782 C  CG    . LYS B 1 10  ? 6.298   7.902   49.144 1.00 41.91  ? 1227 LYS B CG    1 
ATOM   3783 C  CD    . LYS B 1 10  ? 5.760   6.511   49.437 1.00 42.91  ? 1227 LYS B CD    1 
ATOM   3784 C  CE    . LYS B 1 10  ? 4.968   5.934   48.270 1.00 50.36  ? 1227 LYS B CE    1 
ATOM   3785 N  NZ    . LYS B 1 10  ? 4.653   4.481   48.465 1.00 50.10  ? 1227 LYS B NZ    1 
ATOM   3786 N  N     . GLU B 1 11  ? 6.104   11.565  51.211 1.00 83.48  ? 1228 GLU B N     1 
ATOM   3787 C  CA    . GLU B 1 11  ? 4.987   12.505  51.175 1.00 92.04  ? 1228 GLU B CA    1 
ATOM   3788 C  C     . GLU B 1 11  ? 5.425   13.891  50.712 1.00 89.84  ? 1228 GLU B C     1 
ATOM   3789 O  O     . GLU B 1 11  ? 4.789   14.495  49.839 1.00 92.24  ? 1228 GLU B O     1 
ATOM   3790 C  CB    . GLU B 1 11  ? 4.321   12.578  52.550 1.00 92.82  ? 1228 GLU B CB    1 
ATOM   3791 C  CG    . GLU B 1 11  ? 4.005   11.216  53.122 1.00 85.45  ? 1228 GLU B CG    1 
ATOM   3792 C  CD    . GLU B 1 11  ? 5.006   10.781  54.156 1.00 87.70  ? 1228 GLU B CD    1 
ATOM   3793 O  OE1   . GLU B 1 11  ? 5.782   11.626  54.642 1.00 89.15  ? 1228 GLU B OE1   1 
ATOM   3794 O  OE2   . GLU B 1 11  ? 5.013   9.584   54.487 1.00 93.93  ? 1228 GLU B OE2   1 
ATOM   3795 N  N     . ASP B 1 12  ? 6.491   14.419  51.297 1.00 80.02  ? 1229 ASP B N     1 
ATOM   3796 C  CA    . ASP B 1 12  ? 7.083   15.667  50.849 1.00 78.08  ? 1229 ASP B CA    1 
ATOM   3797 C  C     . ASP B 1 12  ? 8.265   15.348  49.950 1.00 83.37  ? 1229 ASP B C     1 
ATOM   3798 O  O     . ASP B 1 12  ? 9.180   14.639  50.368 1.00 97.99  ? 1229 ASP B O     1 
ATOM   3799 C  CB    . ASP B 1 12  ? 7.501   16.475  52.065 1.00 91.28  ? 1229 ASP B CB    1 
ATOM   3800 C  CG    . ASP B 1 12  ? 6.480   16.367  53.186 1.00 108.91 ? 1229 ASP B CG    1 
ATOM   3801 O  OD1   . ASP B 1 12  ? 5.615   17.266  53.305 1.00 112.48 ? 1229 ASP B OD1   1 
ATOM   3802 O  OD2   . ASP B 1 12  ? 6.515   15.354  53.922 1.00 113.53 ? 1229 ASP B OD2   1 
ATOM   3803 N  N     . ASN B 1 13  ? 8.245   15.874  48.726 1.00 75.64  ? 1230 ASN B N     1 
ATOM   3804 C  CA    . ASN B 1 13  ? 9.278   15.650  47.700 1.00 79.39  ? 1230 ASN B CA    1 
ATOM   3805 C  C     . ASN B 1 13  ? 9.351   14.175  47.256 1.00 66.38  ? 1230 ASN B C     1 
ATOM   3806 O  O     . ASN B 1 13  ? 10.307  13.440  47.530 1.00 57.54  ? 1230 ASN B O     1 
ATOM   3807 C  CB    . ASN B 1 13  ? 10.652  16.169  48.159 1.00 80.55  ? 1230 ASN B CB    1 
ATOM   3808 C  CG    . ASN B 1 13  ? 11.625  16.336  46.996 1.00 87.82  ? 1230 ASN B CG    1 
ATOM   3809 O  OD1   . ASN B 1 13  ? 11.250  16.233  45.829 1.00 91.47  ? 1230 ASN B OD1   1 
ATOM   3810 N  ND2   . ASN B 1 13  ? 12.888  16.562  47.315 1.00 94.94  ? 1230 ASN B ND2   1 
ATOM   3811 N  N     . LEU B 1 14  ? 8.337   13.786  46.471 1.00 58.30  ? 1231 LEU B N     1 
ATOM   3812 C  CA    . LEU B 1 14  ? 8.200   12.469  45.857 1.00 54.14  ? 1231 LEU B CA    1 
ATOM   3813 C  C     . LEU B 1 14  ? 9.266   12.151  44.807 1.00 66.03  ? 1231 LEU B C     1 
ATOM   3814 O  O     . LEU B 1 14  ? 9.790   11.031  44.822 1.00 76.45  ? 1231 LEU B O     1 
ATOM   3815 C  CB    . LEU B 1 14  ? 6.807   12.309  45.219 1.00 48.12  ? 1231 LEU B CB    1 
ATOM   3816 C  CG    . LEU B 1 14  ? 6.414   10.874  44.815 1.00 51.59  ? 1231 LEU B CG    1 
ATOM   3817 C  CD1   . LEU B 1 14  ? 6.211   10.032  46.065 1.00 57.69  ? 1231 LEU B CD1   1 
ATOM   3818 C  CD2   . LEU B 1 14  ? 5.157   10.804  43.955 1.00 40.49  ? 1231 LEU B CD2   1 
ATOM   3819 N  N     . PRO B 1 15  ? 9.612   13.053  43.878 1.00 68.00  ? 1232 PRO B N     1 
ATOM   3820 C  CA    . PRO B 1 15  ? 10.559  12.647  42.816 1.00 60.48  ? 1232 PRO B CA    1 
ATOM   3821 C  C     . PRO B 1 15  ? 11.916  12.233  43.356 1.00 53.51  ? 1232 PRO B C     1 
ATOM   3822 O  O     . PRO B 1 15  ? 12.559  11.327  42.797 1.00 52.55  ? 1232 PRO B O     1 
ATOM   3823 C  CB    . PRO B 1 15  ? 10.642  13.895  41.922 1.00 63.66  ? 1232 PRO B CB    1 
ATOM   3824 C  CG    . PRO B 1 15  ? 10.202  15.022  42.787 1.00 68.52  ? 1232 PRO B CG    1 
ATOM   3825 C  CD    . PRO B 1 15  ? 9.158   14.442  43.682 1.00 73.52  ? 1232 PRO B CD    1 
ATOM   3826 N  N     . ASP B 1 16  ? 12.343  12.830  44.478 1.00 55.04  ? 1233 ASP B N     1 
ATOM   3827 C  CA    . ASP B 1 16  ? 13.647  12.507  45.022 1.00 65.72  ? 1233 ASP B CA    1 
ATOM   3828 C  C     . ASP B 1 16  ? 13.580  11.400  46.056 1.00 67.86  ? 1233 ASP B C     1 
ATOM   3829 O  O     . ASP B 1 16  ? 14.549  10.659  46.223 1.00 68.67  ? 1233 ASP B O     1 
ATOM   3830 C  CB    . ASP B 1 16  ? 14.303  13.753  45.574 1.00 71.83  ? 1233 ASP B CB    1 
ATOM   3831 C  CG    . ASP B 1 16  ? 14.607  14.674  44.482 1.00 82.79  ? 1233 ASP B CG    1 
ATOM   3832 O  OD1   . ASP B 1 16  ? 14.009  14.419  43.412 1.00 83.39  ? 1233 ASP B OD1   1 
ATOM   3833 O  OD2   . ASP B 1 16  ? 15.514  15.516  44.618 1.00 93.01  ? 1233 ASP B OD2   1 
ATOM   3834 N  N     . TRP B 1 17  ? 12.409  11.173  46.634 1.00 65.73  ? 1234 TRP B N     1 
ATOM   3835 C  CA    . TRP B 1 17  ? 12.168  9.897   47.299 1.00 54.12  ? 1234 TRP B CA    1 
ATOM   3836 C  C     . TRP B 1 17  ? 12.307  8.729   46.328 1.00 41.32  ? 1234 TRP B C     1 
ATOM   3837 O  O     . TRP B 1 17  ? 13.024  7.767   46.608 1.00 48.66  ? 1234 TRP B O     1 
ATOM   3838 C  CB    . TRP B 1 17  ? 10.778  9.913   47.939 1.00 59.82  ? 1234 TRP B CB    1 
ATOM   3839 C  CG    . TRP B 1 17  ? 10.390  8.583   48.465 1.00 66.26  ? 1234 TRP B CG    1 
ATOM   3840 C  CD1   . TRP B 1 17  ? 10.746  8.041   49.668 1.00 72.98  ? 1234 TRP B CD1   1 
ATOM   3841 C  CD2   . TRP B 1 17  ? 9.579   7.606   47.810 1.00 69.49  ? 1234 TRP B CD2   1 
ATOM   3842 N  NE1   . TRP B 1 17  ? 10.208  6.783   49.798 1.00 76.09  ? 1234 TRP B NE1   1 
ATOM   3843 C  CE2   . TRP B 1 17  ? 9.483   6.496   48.672 1.00 73.65  ? 1234 TRP B CE2   1 
ATOM   3844 C  CE3   . TRP B 1 17  ? 8.918   7.565   46.582 1.00 65.25  ? 1234 TRP B CE3   1 
ATOM   3845 C  CZ2   . TRP B 1 17  ? 8.756   5.367   48.343 1.00 68.04  ? 1234 TRP B CZ2   1 
ATOM   3846 C  CZ3   . TRP B 1 17  ? 8.201   6.449   46.262 1.00 59.88  ? 1234 TRP B CZ3   1 
ATOM   3847 C  CH2   . TRP B 1 17  ? 8.125   5.363   47.134 1.00 66.91  ? 1234 TRP B CH2   1 
ATOM   3848 N  N     . TYR B 1 18  ? 11.627  8.799   45.178 1.00 36.06  ? 1235 TYR B N     1 
ATOM   3849 C  CA    . TYR B 1 18  ? 11.741  7.748   44.161 1.00 47.11  ? 1235 TYR B CA    1 
ATOM   3850 C  C     . TYR B 1 18  ? 13.194  7.565   43.726 1.00 52.48  ? 1235 TYR B C     1 
ATOM   3851 O  O     . TYR B 1 18  ? 13.685  6.428   43.619 1.00 54.55  ? 1235 TYR B O     1 
ATOM   3852 C  CB    . TYR B 1 18  ? 10.832  8.082   42.962 1.00 46.53  ? 1235 TYR B CB    1 
ATOM   3853 C  CG    . TYR B 1 18  ? 10.737  7.074   41.798 1.00 54.83  ? 1235 TYR B CG    1 
ATOM   3854 C  CD1   . TYR B 1 18  ? 10.201  5.785   41.960 1.00 56.50  ? 1235 TYR B CD1   1 
ATOM   3855 C  CD2   . TYR B 1 18  ? 11.123  7.453   40.514 1.00 60.95  ? 1235 TYR B CD2   1 
ATOM   3856 C  CE1   . TYR B 1 18  ? 10.101  4.888   40.854 1.00 60.02  ? 1235 TYR B CE1   1 
ATOM   3857 C  CE2   . TYR B 1 18  ? 11.021  6.590   39.422 1.00 65.07  ? 1235 TYR B CE2   1 
ATOM   3858 C  CZ    . TYR B 1 18  ? 10.516  5.309   39.579 1.00 63.84  ? 1235 TYR B CZ    1 
ATOM   3859 O  OH    . TYR B 1 18  ? 10.449  4.495   38.443 1.00 48.10  ? 1235 TYR B OH    1 
ATOM   3860 N  N     . SER B 1 19  ? 13.911  8.674   43.493 1.00 53.59  ? 1236 SER B N     1 
ATOM   3861 C  CA    . SER B 1 19  ? 15.309  8.556   43.087 1.00 53.58  ? 1236 SER B CA    1 
ATOM   3862 C  C     . SER B 1 19  ? 16.141  7.853   44.156 1.00 55.35  ? 1236 SER B C     1 
ATOM   3863 O  O     . SER B 1 19  ? 16.867  6.886   43.880 1.00 54.63  ? 1236 SER B O     1 
ATOM   3864 C  CB    . SER B 1 19  ? 15.885  9.939   42.798 1.00 40.78  ? 1236 SER B CB    1 
ATOM   3865 O  OG    . SER B 1 19  ? 17.291  9.897   42.839 1.00 38.89  ? 1236 SER B OG    1 
ATOM   3866 N  N     . GLN B 1 20  ? 15.977  8.295   45.390 1.00 54.85  ? 1237 GLN B N     1 
ATOM   3867 C  CA    . GLN B 1 20  ? 16.694  7.703   46.501 1.00 57.13  ? 1237 GLN B CA    1 
ATOM   3868 C  C     . GLN B 1 20  ? 16.426  6.215   46.595 1.00 61.16  ? 1237 GLN B C     1 
ATOM   3869 O  O     . GLN B 1 20  ? 17.334  5.424   46.878 1.00 69.73  ? 1237 GLN B O     1 
ATOM   3870 C  CB    . GLN B 1 20  ? 16.266  8.403   47.788 1.00 52.64  ? 1237 GLN B CB    1 
ATOM   3871 C  CG    . GLN B 1 20  ? 17.067  9.640   48.054 1.00 56.93  ? 1237 GLN B CG    1 
ATOM   3872 C  CD    . GLN B 1 20  ? 18.326  9.330   48.800 1.00 64.22  ? 1237 GLN B CD    1 
ATOM   3873 O  OE1   . GLN B 1 20  ? 18.295  9.008   49.984 1.00 75.30  ? 1237 GLN B OE1   1 
ATOM   3874 N  NE2   . GLN B 1 20  ? 19.447  9.395   48.108 1.00 62.70  ? 1237 GLN B NE2   1 
ATOM   3875 N  N     . VAL B 1 21  ? 15.171  5.824   46.423 1.00 48.95  ? 1238 VAL B N     1 
ATOM   3876 C  CA    . VAL B 1 21  ? 14.823  4.423   46.579 1.00 49.03  ? 1238 VAL B CA    1 
ATOM   3877 C  C     . VAL B 1 21  ? 15.463  3.596   45.474 1.00 46.85  ? 1238 VAL B C     1 
ATOM   3878 O  O     . VAL B 1 21  ? 16.107  2.574   45.733 1.00 43.05  ? 1238 VAL B O     1 
ATOM   3879 C  CB    . VAL B 1 21  ? 13.297  4.251   46.628 1.00 50.37  ? 1238 VAL B CB    1 
ATOM   3880 C  CG1   . VAL B 1 21  ? 12.924  2.810   46.384 1.00 52.22  ? 1238 VAL B CG1   1 
ATOM   3881 C  CG2   . VAL B 1 21  ? 12.779  4.722   47.980 1.00 48.92  ? 1238 VAL B CG2   1 
ATOM   3882 N  N     . ILE B 1 22  ? 15.326  4.030   44.223 1.00 45.07  ? 1239 ILE B N     1 
ATOM   3883 C  CA    . ILE B 1 22  ? 15.870  3.197   43.154 1.00 51.04  ? 1239 ILE B CA    1 
ATOM   3884 C  C     . ILE B 1 22  ? 17.397  3.128   43.174 1.00 56.66  ? 1239 ILE B C     1 
ATOM   3885 O  O     . ILE B 1 22  ? 17.981  2.238   42.544 1.00 72.66  ? 1239 ILE B O     1 
ATOM   3886 C  CB    . ILE B 1 22  ? 15.359  3.660   41.782 1.00 42.66  ? 1239 ILE B CB    1 
ATOM   3887 C  CG1   . ILE B 1 22  ? 15.862  5.069   41.468 1.00 49.95  ? 1239 ILE B CG1   1 
ATOM   3888 C  CG2   . ILE B 1 22  ? 13.862  3.575   41.771 1.00 30.26  ? 1239 ILE B CG2   1 
ATOM   3889 C  CD1   . ILE B 1 22  ? 15.590  5.535   40.053 1.00 52.94  ? 1239 ILE B CD1   1 
ATOM   3890 N  N     . THR B 1 23  ? 18.071  4.054   43.849 1.00 41.66  ? 1240 THR B N     1 
ATOM   3891 C  CA    . THR B 1 23  ? 19.527  3.980   43.930 1.00 38.63  ? 1240 THR B CA    1 
ATOM   3892 C  C     . THR B 1 23  ? 20.041  3.291   45.194 1.00 44.07  ? 1240 THR B C     1 
ATOM   3893 O  O     . THR B 1 23  ? 20.940  2.439   45.124 1.00 41.06  ? 1240 THR B O     1 
ATOM   3894 C  CB    . THR B 1 23  ? 20.109  5.385   43.826 1.00 35.82  ? 1240 THR B CB    1 
ATOM   3895 O  OG1   . THR B 1 23  ? 19.460  6.219   44.788 1.00 41.02  ? 1240 THR B OG1   1 
ATOM   3896 C  CG2   . THR B 1 23  ? 19.902  5.935   42.422 1.00 31.92  ? 1240 THR B CG2   1 
ATOM   3897 N  N     . LYS B 1 24  ? 19.555  3.702   46.366 1.00 40.99  ? 1241 LYS B N     1 
ATOM   3898 C  CA    . LYS B 1 24  ? 19.962  3.013   47.575 1.00 42.04  ? 1241 LYS B CA    1 
ATOM   3899 C  C     . LYS B 1 24  ? 19.400  1.602   47.629 1.00 50.59  ? 1241 LYS B C     1 
ATOM   3900 O  O     . LYS B 1 24  ? 19.864  0.803   48.441 1.00 57.27  ? 1241 LYS B O     1 
ATOM   3901 C  CB    . LYS B 1 24  ? 19.556  3.826   48.811 1.00 34.40  ? 1241 LYS B CB    1 
ATOM   3902 C  CG    . LYS B 1 24  ? 20.172  5.204   48.794 1.00 50.47  ? 1241 LYS B CG    1 
ATOM   3903 C  CD    . LYS B 1 24  ? 20.611  5.722   50.162 1.00 60.98  ? 1241 LYS B CD    1 
ATOM   3904 C  CE    . LYS B 1 24  ? 20.862  7.238   50.086 1.00 72.67  ? 1241 LYS B CE    1 
ATOM   3905 N  NZ    . LYS B 1 24  ? 21.599  7.854   51.240 1.00 80.80  ? 1241 LYS B NZ    1 
ATOM   3906 N  N     . GLY B 1 25  ? 18.423  1.281   46.789 1.00 50.70  ? 1242 GLY B N     1 
ATOM   3907 C  CA    . GLY B 1 25  ? 17.924  -0.064  46.618 1.00 47.66  ? 1242 GLY B CA    1 
ATOM   3908 C  C     . GLY B 1 25  ? 18.633  -0.884  45.570 1.00 58.91  ? 1242 GLY B C     1 
ATOM   3909 O  O     . GLY B 1 25  ? 18.302  -2.056  45.387 1.00 63.17  ? 1242 GLY B O     1 
ATOM   3910 N  N     . GLU B 1 26  ? 19.587  -0.297  44.853 1.00 72.51  ? 1243 GLU B N     1 
ATOM   3911 C  CA    . GLU B 1 26  ? 20.475  -1.039  43.962 1.00 66.86  ? 1243 GLU B CA    1 
ATOM   3912 C  C     . GLU B 1 26  ? 19.723  -1.649  42.790 1.00 69.33  ? 1243 GLU B C     1 
ATOM   3913 O  O     . GLU B 1 26  ? 19.943  -2.808  42.444 1.00 82.06  ? 1243 GLU B O     1 
ATOM   3914 C  CB    . GLU B 1 26  ? 21.238  -2.129  44.706 1.00 64.30  ? 1243 GLU B CB    1 
ATOM   3915 C  CG    . GLU B 1 26  ? 22.019  -1.655  45.877 1.00 68.77  ? 1243 GLU B CG    1 
ATOM   3916 C  CD    . GLU B 1 26  ? 22.788  -2.784  46.493 1.00 77.30  ? 1243 GLU B CD    1 
ATOM   3917 O  OE1   . GLU B 1 26  ? 23.291  -2.613  47.621 1.00 80.81  ? 1243 GLU B OE1   1 
ATOM   3918 O  OE2   . GLU B 1 26  ? 22.878  -3.852  45.844 1.00 81.43  ? 1243 GLU B OE2   1 
ATOM   3919 N  N     . MET B 1 27  ? 18.831  -0.879  42.174 1.00 59.85  ? 1244 MET B N     1 
ATOM   3920 C  CA    . MET B 1 27  ? 18.122  -1.327  40.981 1.00 41.73  ? 1244 MET B CA    1 
ATOM   3921 C  C     . MET B 1 27  ? 18.477  -0.557  39.734 1.00 40.27  ? 1244 MET B C     1 
ATOM   3922 O  O     . MET B 1 27  ? 18.342  -1.086  38.638 1.00 48.36  ? 1244 MET B O     1 
ATOM   3923 C  CB    . MET B 1 27  ? 16.623  -1.233  41.200 1.00 38.97  ? 1244 MET B CB    1 
ATOM   3924 C  CG    . MET B 1 27  ? 16.198  -2.244  42.182 1.00 46.44  ? 1244 MET B CG    1 
ATOM   3925 S  SD    . MET B 1 27  ? 14.559  -1.855  42.688 1.00 56.18  ? 1244 MET B SD    1 
ATOM   3926 C  CE    . MET B 1 27  ? 13.597  -2.713  41.453 1.00 51.82  ? 1244 MET B CE    1 
ATOM   3927 N  N     . ILE B 1 28  ? 18.887  0.684   39.901 1.00 40.19  ? 1245 ILE B N     1 
ATOM   3928 C  CA    . ILE B 1 28  ? 19.195  1.647   38.864 1.00 36.00  ? 1245 ILE B CA    1 
ATOM   3929 C  C     . ILE B 1 28  ? 20.640  2.089   39.019 1.00 39.93  ? 1245 ILE B C     1 
ATOM   3930 O  O     . ILE B 1 28  ? 21.203  2.086   40.121 1.00 46.60  ? 1245 ILE B O     1 
ATOM   3931 C  CB    . ILE B 1 28  ? 18.201  2.832   39.000 1.00 46.49  ? 1245 ILE B CB    1 
ATOM   3932 C  CG1   . ILE B 1 28  ? 16.832  2.356   38.538 1.00 49.08  ? 1245 ILE B CG1   1 
ATOM   3933 C  CG2   . ILE B 1 28  ? 18.663  4.174   38.333 1.00 35.35  ? 1245 ILE B CG2   1 
ATOM   3934 C  CD1   . ILE B 1 28  ? 16.957  1.328   37.489 1.00 44.60  ? 1245 ILE B CD1   1 
ATOM   3935 N  N     . GLU B 1 29  ? 21.253  2.432   37.894 1.00 33.71  ? 1246 GLU B N     1 
ATOM   3936 C  CA    . GLU B 1 29  ? 22.350  3.387   37.888 1.00 36.65  ? 1246 GLU B CA    1 
ATOM   3937 C  C     . GLU B 1 29  ? 22.021  4.397   36.807 1.00 41.94  ? 1246 GLU B C     1 
ATOM   3938 O  O     . GLU B 1 29  ? 21.560  4.012   35.731 1.00 47.03  ? 1246 GLU B O     1 
ATOM   3939 C  CB    . GLU B 1 29  ? 23.720  2.747   37.653 1.00 50.18  ? 1246 GLU B CB    1 
ATOM   3940 C  CG    . GLU B 1 29  ? 24.843  3.305   38.581 1.00 49.27  ? 1246 GLU B CG    1 
ATOM   3941 C  CD    . GLU B 1 29  ? 24.672  2.894   40.049 1.00 55.96  ? 1246 GLU B CD    1 
ATOM   3942 O  OE1   . GLU B 1 29  ? 24.295  3.747   40.892 1.00 58.80  ? 1246 GLU B OE1   1 
ATOM   3943 O  OE2   . GLU B 1 29  ? 24.908  1.704   40.359 1.00 57.05  ? 1246 GLU B OE2   1 
ATOM   3944 N  N     . TYR B 1 30  ? 22.113  5.686   37.137 1.00 38.51  ? 1247 TYR B N     1 
ATOM   3945 C  CA    . TYR B 1 30  ? 21.809  6.699   36.136 1.00 38.27  ? 1247 TYR B CA    1 
ATOM   3946 C  C     . TYR B 1 30  ? 22.827  6.625   35.009 1.00 42.85  ? 1247 TYR B C     1 
ATOM   3947 O  O     . TYR B 1 30  ? 23.968  6.204   35.191 1.00 42.79  ? 1247 TYR B O     1 
ATOM   3948 C  CB    . TYR B 1 30  ? 21.789  8.111   36.736 1.00 31.31  ? 1247 TYR B CB    1 
ATOM   3949 C  CG    . TYR B 1 30  ? 20.544  8.412   37.551 1.00 31.42  ? 1247 TYR B CG    1 
ATOM   3950 C  CD1   . TYR B 1 30  ? 19.293  8.459   36.954 1.00 41.93  ? 1247 TYR B CD1   1 
ATOM   3951 C  CD2   . TYR B 1 30  ? 20.625  8.644   38.916 1.00 31.95  ? 1247 TYR B CD2   1 
ATOM   3952 C  CE1   . TYR B 1 30  ? 18.163  8.707   37.695 1.00 38.36  ? 1247 TYR B CE1   1 
ATOM   3953 C  CE2   . TYR B 1 30  ? 19.503  8.897   39.666 1.00 32.12  ? 1247 TYR B CE2   1 
ATOM   3954 C  CZ    . TYR B 1 30  ? 18.275  8.926   39.054 1.00 38.64  ? 1247 TYR B CZ    1 
ATOM   3955 O  OH    . TYR B 1 30  ? 17.140  9.177   39.795 1.00 49.17  ? 1247 TYR B OH    1 
ATOM   3956 N  N     . TYR B 1 31  ? 22.417  7.072   33.843 1.00 49.87  ? 1248 TYR B N     1 
ATOM   3957 C  CA    . TYR B 1 31  ? 23.162  6.774   32.639 1.00 50.86  ? 1248 TYR B CA    1 
ATOM   3958 C  C     . TYR B 1 31  ? 23.264  8.039   31.806 1.00 50.23  ? 1248 TYR B C     1 
ATOM   3959 O  O     . TYR B 1 31  ? 22.383  8.902   31.847 1.00 54.17  ? 1248 TYR B O     1 
ATOM   3960 C  CB    . TYR B 1 31  ? 22.486  5.642   31.876 1.00 44.91  ? 1248 TYR B CB    1 
ATOM   3961 C  CG    . TYR B 1 31  ? 23.281  5.088   30.738 1.00 43.26  ? 1248 TYR B CG    1 
ATOM   3962 C  CD1   . TYR B 1 31  ? 24.399  4.298   30.967 1.00 29.40  ? 1248 TYR B CD1   1 
ATOM   3963 C  CD2   . TYR B 1 31  ? 22.904  5.331   29.431 1.00 45.58  ? 1248 TYR B CD2   1 
ATOM   3964 C  CE1   . TYR B 1 31  ? 25.118  3.773   29.923 1.00 29.22  ? 1248 TYR B CE1   1 
ATOM   3965 C  CE2   . TYR B 1 31  ? 23.616  4.797   28.382 1.00 42.93  ? 1248 TYR B CE2   1 
ATOM   3966 C  CZ    . TYR B 1 31  ? 24.725  4.027   28.635 1.00 37.01  ? 1248 TYR B CZ    1 
ATOM   3967 O  OH    . TYR B 1 31  ? 25.439  3.523   27.586 1.00 44.60  ? 1248 TYR B OH    1 
ATOM   3968 N  N     . ASP B 1 32  ? 24.354  8.145   31.058 1.00 41.80  ? 1249 ASP B N     1 
ATOM   3969 C  CA    . ASP B 1 32  ? 24.705  9.393   30.414 1.00 37.68  ? 1249 ASP B CA    1 
ATOM   3970 C  C     . ASP B 1 32  ? 24.079  9.555   29.037 1.00 40.21  ? 1249 ASP B C     1 
ATOM   3971 O  O     . ASP B 1 32  ? 24.440  10.496  28.333 1.00 54.36  ? 1249 ASP B O     1 
ATOM   3972 C  CB    . ASP B 1 32  ? 26.227  9.545   30.331 1.00 48.24  ? 1249 ASP B CB    1 
ATOM   3973 C  CG    . ASP B 1 32  ? 26.865  8.569   29.372 1.00 59.69  ? 1249 ASP B CG    1 
ATOM   3974 O  OD1   . ASP B 1 32  ? 26.244  7.531   29.116 1.00 70.33  ? 1249 ASP B OD1   1 
ATOM   3975 O  OD2   . ASP B 1 32  ? 27.985  8.822   28.884 1.00 60.42  ? 1249 ASP B OD2   1 
ATOM   3976 N  N     . VAL B 1 33  ? 23.170  8.674   28.618 1.00 41.17  ? 1250 VAL B N     1 
ATOM   3977 C  CA    . VAL B 1 33  ? 22.277  8.988   27.500 1.00 50.68  ? 1250 VAL B CA    1 
ATOM   3978 C  C     . VAL B 1 33  ? 20.899  9.223   28.112 1.00 58.24  ? 1250 VAL B C     1 
ATOM   3979 O  O     . VAL B 1 33  ? 20.320  8.329   28.744 1.00 63.37  ? 1250 VAL B O     1 
ATOM   3980 C  CB    . VAL B 1 33  ? 22.275  7.919   26.398 1.00 49.34  ? 1250 VAL B CB    1 
ATOM   3981 C  CG1   . VAL B 1 33  ? 23.689  7.449   26.105 1.00 39.51  ? 1250 VAL B CG1   1 
ATOM   3982 C  CG2   . VAL B 1 33  ? 21.395  6.780   26.709 1.00 59.23  ? 1250 VAL B CG2   1 
ATOM   3983 N  N     . SER B 1 34  ? 20.425  10.465  28.011 1.00 60.59  ? 1251 SER B N     1 
ATOM   3984 C  CA    . SER B 1 34  ? 19.284  10.945  28.788 1.00 67.88  ? 1251 SER B CA    1 
ATOM   3985 C  C     . SER B 1 34  ? 18.092  9.987   28.725 1.00 62.53  ? 1251 SER B C     1 
ATOM   3986 O  O     . SER B 1 34  ? 17.681  9.543   27.649 1.00 61.16  ? 1251 SER B O     1 
ATOM   3987 C  CB    . SER B 1 34  ? 18.866  12.325  28.258 1.00 80.90  ? 1251 SER B CB    1 
ATOM   3988 O  OG    . SER B 1 34  ? 18.898  12.340  26.842 1.00 86.04  ? 1251 SER B OG    1 
ATOM   3989 N  N     . GLY B 1 35  ? 17.561  9.634   29.885 1.00 52.21  ? 1252 GLY B N     1 
ATOM   3990 C  CA    . GLY B 1 35  ? 16.307  8.927   29.885 1.00 50.71  ? 1252 GLY B CA    1 
ATOM   3991 C  C     . GLY B 1 35  ? 16.394  7.431   29.706 1.00 59.77  ? 1252 GLY B C     1 
ATOM   3992 O  O     . GLY B 1 35  ? 15.350  6.791   29.544 1.00 65.99  ? 1252 GLY B O     1 
ATOM   3993 N  N     . CYS B 1 36  ? 17.597  6.854   29.691 1.00 59.33  ? 1253 CYS B N     1 
ATOM   3994 C  CA    . CYS B 1 36  ? 17.804  5.417   29.808 1.00 45.10  ? 1253 CYS B CA    1 
ATOM   3995 C  C     . CYS B 1 36  ? 18.647  5.145   31.037 1.00 45.12  ? 1253 CYS B C     1 
ATOM   3996 O  O     . CYS B 1 36  ? 19.479  5.971   31.423 1.00 52.65  ? 1253 CYS B O     1 
ATOM   3997 C  CB    . CYS B 1 36  ? 18.521  4.854   28.610 1.00 40.99  ? 1253 CYS B CB    1 
ATOM   3998 S  SG    . CYS B 1 36  ? 18.164  5.710   27.101 1.00 51.31  ? 1253 CYS B SG    1 
ATOM   3999 N  N     . TYR B 1 37  ? 18.454  3.974   31.641 1.00 39.36  ? 1254 TYR B N     1 
ATOM   4000 C  CA    . TYR B 1 37  ? 19.004  3.740   32.970 1.00 37.51  ? 1254 TYR B CA    1 
ATOM   4001 C  C     . TYR B 1 37  ? 19.543  2.330   33.074 1.00 48.10  ? 1254 TYR B C     1 
ATOM   4002 O  O     . TYR B 1 37  ? 18.851  1.370   32.732 1.00 50.29  ? 1254 TYR B O     1 
ATOM   4003 C  CB    . TYR B 1 37  ? 17.969  3.963   34.078 1.00 28.83  ? 1254 TYR B CB    1 
ATOM   4004 C  CG    . TYR B 1 37  ? 17.182  5.237   33.921 1.00 37.04  ? 1254 TYR B CG    1 
ATOM   4005 C  CD1   . TYR B 1 37  ? 17.490  6.376   34.660 1.00 38.19  ? 1254 TYR B CD1   1 
ATOM   4006 C  CD2   . TYR B 1 37  ? 16.147  5.304   33.013 1.00 35.03  ? 1254 TYR B CD2   1 
ATOM   4007 C  CE1   . TYR B 1 37  ? 16.768  7.525   34.500 1.00 37.47  ? 1254 TYR B CE1   1 
ATOM   4008 C  CE2   . TYR B 1 37  ? 15.443  6.443   32.836 1.00 44.99  ? 1254 TYR B CE2   1 
ATOM   4009 C  CZ    . TYR B 1 37  ? 15.736  7.550   33.571 1.00 49.87  ? 1254 TYR B CZ    1 
ATOM   4010 O  OH    . TYR B 1 37  ? 14.959  8.666   33.335 1.00 57.63  ? 1254 TYR B OH    1 
ATOM   4011 N  N     . ILE B 1 38  ? 20.752  2.218   33.625 1.00 54.49  ? 1255 ILE B N     1 
ATOM   4012 C  CA    . ILE B 1 38  ? 21.388  0.926   33.810 1.00 46.43  ? 1255 ILE B CA    1 
ATOM   4013 C  C     . ILE B 1 38  ? 20.538  0.123   34.771 1.00 46.51  ? 1255 ILE B C     1 
ATOM   4014 O  O     . ILE B 1 38  ? 20.239  0.587   35.880 1.00 57.76  ? 1255 ILE B O     1 
ATOM   4015 C  CB    . ILE B 1 38  ? 22.795  1.099   34.368 1.00 38.85  ? 1255 ILE B CB    1 
ATOM   4016 C  CG1   . ILE B 1 38  ? 23.770  1.558   33.288 1.00 34.27  ? 1255 ILE B CG1   1 
ATOM   4017 C  CG2   . ILE B 1 38  ? 23.248  -0.200  35.004 1.00 47.92  ? 1255 ILE B CG2   1 
ATOM   4018 C  CD1   . ILE B 1 38  ? 25.066  2.132   33.880 1.00 29.13  ? 1255 ILE B CD1   1 
ATOM   4019 N  N     . LEU B 1 39  ? 20.111  -1.062  34.335 1.00 39.87  ? 1256 LEU B N     1 
ATOM   4020 C  CA    . LEU B 1 39  ? 19.313  -1.972  35.151 1.00 47.18  ? 1256 LEU B CA    1 
ATOM   4021 C  C     . LEU B 1 39  ? 20.197  -2.918  35.954 1.00 43.90  ? 1256 LEU B C     1 
ATOM   4022 O  O     . LEU B 1 39  ? 20.770  -3.867  35.403 1.00 46.16  ? 1256 LEU B O     1 
ATOM   4023 C  CB    . LEU B 1 39  ? 18.353  -2.750  34.263 1.00 49.35  ? 1256 LEU B CB    1 
ATOM   4024 C  CG    . LEU B 1 39  ? 17.156  -1.925  33.832 1.00 34.02  ? 1256 LEU B CG    1 
ATOM   4025 C  CD1   . LEU B 1 39  ? 16.417  -2.650  32.752 1.00 26.27  ? 1256 LEU B CD1   1 
ATOM   4026 C  CD2   . LEU B 1 39  ? 16.290  -1.719  35.069 1.00 29.47  ? 1256 LEU B CD2   1 
ATOM   4027 N  N     . ARG B 1 40  ? 20.239  -2.716  37.266 1.00 27.75  ? 1257 ARG B N     1 
ATOM   4028 C  CA    . ARG B 1 40  ? 21.018  -3.592  38.126 1.00 53.52  ? 1257 ARG B CA    1 
ATOM   4029 C  C     . ARG B 1 40  ? 20.319  -4.950  38.345 1.00 44.58  ? 1257 ARG B C     1 
ATOM   4030 O  O     . ARG B 1 40  ? 19.178  -5.175  37.935 1.00 27.53  ? 1257 ARG B O     1 
ATOM   4031 C  CB    . ARG B 1 40  ? 21.312  -2.886  39.451 1.00 39.57  ? 1257 ARG B CB    1 
ATOM   4032 C  CG    . ARG B 1 40  ? 21.749  -1.476  39.267 1.00 30.84  ? 1257 ARG B CG    1 
ATOM   4033 C  CD    . ARG B 1 40  ? 22.334  -0.887  40.547 1.00 37.99  ? 1257 ARG B CD    1 
ATOM   4034 N  NE    . ARG B 1 40  ? 23.502  -1.617  41.023 1.00 42.76  ? 1257 ARG B NE    1 
ATOM   4035 C  CZ    . ARG B 1 40  ? 24.114  -1.384  42.177 1.00 41.75  ? 1257 ARG B CZ    1 
ATOM   4036 N  NH1   . ARG B 1 40  ? 23.667  -0.439  42.989 1.00 52.29  ? 1257 ARG B NH1   1 
ATOM   4037 N  NH2   . ARG B 1 40  ? 25.169  -2.103  42.521 1.00 30.79  ? 1257 ARG B NH2   1 
ATOM   4038 N  N     . HIS B 1 41  ? 21.032  -5.857  39.026 1.00 37.26  ? 1258 HIS B N     1 
ATOM   4039 C  CA    . HIS B 1 41  ? 20.552  -7.216  39.250 1.00 38.91  ? 1258 HIS B CA    1 
ATOM   4040 C  C     . HIS B 1 41  ? 19.220  -7.217  39.993 1.00 48.27  ? 1258 HIS B C     1 
ATOM   4041 O  O     . HIS B 1 41  ? 18.302  -7.972  39.636 1.00 69.66  ? 1258 HIS B O     1 
ATOM   4042 C  CB    . HIS B 1 41  ? 21.629  -8.004  40.005 1.00 51.87  ? 1258 HIS B CB    1 
ATOM   4043 C  CG    . HIS B 1 41  ? 21.201  -9.360  40.473 1.00 77.45  ? 1258 HIS B CG    1 
ATOM   4044 N  ND1   . HIS B 1 41  ? 20.935  -9.636  41.797 1.00 84.79  ? 1258 HIS B ND1   1 
ATOM   4045 C  CD2   . HIS B 1 41  ? 21.024  -10.526 39.802 1.00 83.71  ? 1258 HIS B CD2   1 
ATOM   4046 C  CE1   . HIS B 1 41  ? 20.589  -10.908 41.919 1.00 87.19  ? 1258 HIS B CE1   1 
ATOM   4047 N  NE2   . HIS B 1 41  ? 20.639  -11.470 40.724 1.00 83.62  ? 1258 HIS B NE2   1 
ATOM   4048 N  N     . TRP B 1 42  ? 19.071  -6.327  40.982 1.00 38.04  ? 1259 TRP B N     1 
ATOM   4049 C  CA    . TRP B 1 42  ? 17.884  -6.340  41.835 1.00 42.00  ? 1259 TRP B CA    1 
ATOM   4050 C  C     . TRP B 1 42  ? 16.619  -6.144  41.014 1.00 46.55  ? 1259 TRP B C     1 
ATOM   4051 O  O     . TRP B 1 42  ? 15.675  -6.936  41.110 1.00 50.33  ? 1259 TRP B O     1 
ATOM   4052 C  CB    . TRP B 1 42  ? 18.002  -5.274  42.924 1.00 43.59  ? 1259 TRP B CB    1 
ATOM   4053 C  CG    . TRP B 1 42  ? 17.280  -5.609  44.222 1.00 54.23  ? 1259 TRP B CG    1 
ATOM   4054 C  CD1   . TRP B 1 42  ? 16.272  -4.898  44.795 1.00 60.37  ? 1259 TRP B CD1   1 
ATOM   4055 C  CD2   . TRP B 1 42  ? 17.538  -6.711  45.106 1.00 48.88  ? 1259 TRP B CD2   1 
ATOM   4056 N  NE1   . TRP B 1 42  ? 15.871  -5.492  45.962 1.00 53.42  ? 1259 TRP B NE1   1 
ATOM   4057 C  CE2   . TRP B 1 42  ? 16.635  -6.606  46.177 1.00 57.27  ? 1259 TRP B CE2   1 
ATOM   4058 C  CE3   . TRP B 1 42  ? 18.429  -7.788  45.082 1.00 46.43  ? 1259 TRP B CE3   1 
ATOM   4059 C  CZ2   . TRP B 1 42  ? 16.601  -7.533  47.222 1.00 73.66  ? 1259 TRP B CZ2   1 
ATOM   4060 C  CZ3   . TRP B 1 42  ? 18.390  -8.713  46.114 1.00 57.40  ? 1259 TRP B CZ3   1 
ATOM   4061 C  CH2   . TRP B 1 42  ? 17.488  -8.577  47.174 1.00 68.79  ? 1259 TRP B CH2   1 
ATOM   4062 N  N     . SER B 1 43  ? 16.582  -5.084  40.205 1.00 52.81  ? 1260 SER B N     1 
ATOM   4063 C  CA    . SER B 1 43  ? 15.417  -4.803  39.365 1.00 57.42  ? 1260 SER B CA    1 
ATOM   4064 C  C     . SER B 1 43  ? 15.210  -5.881  38.325 1.00 50.08  ? 1260 SER B C     1 
ATOM   4065 O  O     . SER B 1 43  ? 14.068  -6.310  38.068 1.00 48.44  ? 1260 SER B O     1 
ATOM   4066 C  CB    . SER B 1 43  ? 15.583  -3.457  38.653 1.00 61.13  ? 1260 SER B CB    1 
ATOM   4067 O  OG    . SER B 1 43  ? 16.898  -3.294  38.123 1.00 64.89  ? 1260 SER B OG    1 
ATOM   4068 N  N     . PHE B 1 44  ? 16.309  -6.299  37.693 1.00 41.56  ? 1261 PHE B N     1 
ATOM   4069 C  CA    . PHE B 1 44  ? 16.188  -7.162  36.535 1.00 35.86  ? 1261 PHE B CA    1 
ATOM   4070 C  C     . PHE B 1 44  ? 15.619  -8.506  36.910 1.00 53.77  ? 1261 PHE B C     1 
ATOM   4071 O  O     . PHE B 1 44  ? 14.881  -9.095  36.111 1.00 50.15  ? 1261 PHE B O     1 
ATOM   4072 C  CB    . PHE B 1 44  ? 17.524  -7.335  35.839 1.00 26.66  ? 1261 PHE B CB    1 
ATOM   4073 C  CG    . PHE B 1 44  ? 17.380  -7.802  34.444 1.00 39.84  ? 1261 PHE B CG    1 
ATOM   4074 C  CD1   . PHE B 1 44  ? 16.950  -6.942  33.458 1.00 49.76  ? 1261 PHE B CD1   1 
ATOM   4075 C  CD2   . PHE B 1 44  ? 17.618  -9.115  34.118 1.00 47.80  ? 1261 PHE B CD2   1 
ATOM   4076 C  CE1   . PHE B 1 44  ? 16.785  -7.381  32.160 1.00 54.41  ? 1261 PHE B CE1   1 
ATOM   4077 C  CE2   . PHE B 1 44  ? 17.463  -9.562  32.825 1.00 52.92  ? 1261 PHE B CE2   1 
ATOM   4078 C  CZ    . PHE B 1 44  ? 17.049  -8.696  31.843 1.00 51.47  ? 1261 PHE B CZ    1 
ATOM   4079 N  N     . ALA B 1 45  ? 15.904  -8.981  38.129 1.00 60.23  ? 1262 ALA B N     1 
ATOM   4080 C  CA    . ALA B 1 45  ? 15.295  -10.231 38.574 1.00 55.07  ? 1262 ALA B CA    1 
ATOM   4081 C  C     . ALA B 1 45  ? 13.780  -10.090 38.707 1.00 59.51  ? 1262 ALA B C     1 
ATOM   4082 O  O     . ALA B 1 45  ? 13.032  -11.026 38.393 1.00 60.00  ? 1262 ALA B O     1 
ATOM   4083 C  CB    . ALA B 1 45  ? 15.933  -10.689 39.881 1.00 43.76  ? 1262 ALA B CB    1 
ATOM   4084 N  N     . ILE B 1 46  ? 13.308  -8.931  39.178 1.00 60.10  ? 1263 ILE B N     1 
ATOM   4085 C  CA    . ILE B 1 46  ? 11.870  -8.687  39.240 1.00 51.76  ? 1263 ILE B CA    1 
ATOM   4086 C  C     . ILE B 1 46  ? 11.279  -8.795  37.846 1.00 47.43  ? 1263 ILE B C     1 
ATOM   4087 O  O     . ILE B 1 46  ? 10.245  -9.453  37.627 1.00 48.41  ? 1263 ILE B O     1 
ATOM   4088 C  CB    . ILE B 1 46  ? 11.578  -7.308  39.863 1.00 51.59  ? 1263 ILE B CB    1 
ATOM   4089 C  CG1   . ILE B 1 46  ? 12.367  -7.117  41.148 1.00 48.13  ? 1263 ILE B CG1   1 
ATOM   4090 C  CG2   . ILE B 1 46  ? 10.068  -7.125  40.139 1.00 52.60  ? 1263 ILE B CG2   1 
ATOM   4091 C  CD1   . ILE B 1 46  ? 11.914  -5.940  41.959 1.00 41.57  ? 1263 ILE B CD1   1 
ATOM   4092 N  N     . TRP B 1 47  ? 11.924  -8.134  36.881 1.00 42.27  ? 1264 TRP B N     1 
ATOM   4093 C  CA    . TRP B 1 47  ? 11.444  -8.247  35.503 1.00 47.22  ? 1264 TRP B CA    1 
ATOM   4094 C  C     . TRP B 1 47  ? 11.447  -9.707  35.038 1.00 51.74  ? 1264 TRP B C     1 
ATOM   4095 O  O     . TRP B 1 47  ? 10.535  -10.141 34.327 1.00 44.28  ? 1264 TRP B O     1 
ATOM   4096 C  CB    . TRP B 1 47  ? 12.264  -7.374  34.556 1.00 32.69  ? 1264 TRP B CB    1 
ATOM   4097 C  CG    . TRP B 1 47  ? 11.959  -7.586  33.098 1.00 30.68  ? 1264 TRP B CG    1 
ATOM   4098 C  CD1   . TRP B 1 47  ? 12.804  -8.071  32.143 1.00 46.70  ? 1264 TRP B CD1   1 
ATOM   4099 C  CD2   . TRP B 1 47  ? 10.730  -7.291  32.426 1.00 32.15  ? 1264 TRP B CD2   1 
ATOM   4100 N  NE1   . TRP B 1 47  ? 12.176  -8.101  30.916 1.00 50.17  ? 1264 TRP B NE1   1 
ATOM   4101 C  CE2   . TRP B 1 47  ? 10.903  -7.619  31.067 1.00 40.85  ? 1264 TRP B CE2   1 
ATOM   4102 C  CE3   . TRP B 1 47  ? 9.500   -6.777  32.842 1.00 30.56  ? 1264 TRP B CE3   1 
ATOM   4103 C  CZ2   . TRP B 1 47  ? 9.894   -7.450  30.130 1.00 41.34  ? 1264 TRP B CZ2   1 
ATOM   4104 C  CZ3   . TRP B 1 47  ? 8.506   -6.619  31.915 1.00 32.41  ? 1264 TRP B CZ3   1 
ATOM   4105 C  CH2   . TRP B 1 47  ? 8.703   -6.958  30.573 1.00 39.02  ? 1264 TRP B CH2   1 
ATOM   4106 N  N     . LYS B 1 48  ? 12.470  -10.478 35.424 1.00 47.54  ? 1265 LYS B N     1 
ATOM   4107 C  CA    . LYS B 1 48  ? 12.528  -11.880 35.014 1.00 36.26  ? 1265 LYS B CA    1 
ATOM   4108 C  C     . LYS B 1 48  ? 11.335  -12.654 35.542 1.00 26.95  ? 1265 LYS B C     1 
ATOM   4109 O  O     . LYS B 1 48  ? 10.712  -13.414 34.805 1.00 34.34  ? 1265 LYS B O     1 
ATOM   4110 C  CB    . LYS B 1 48  ? 13.818  -12.529 35.498 1.00 26.82  ? 1265 LYS B CB    1 
ATOM   4111 C  CG    . LYS B 1 48  ? 15.003  -12.247 34.645 1.00 26.55  ? 1265 LYS B CG    1 
ATOM   4112 C  CD    . LYS B 1 48  ? 16.172  -13.003 35.196 1.00 40.33  ? 1265 LYS B CD    1 
ATOM   4113 C  CE    . LYS B 1 48  ? 17.340  -12.942 34.258 1.00 50.03  ? 1265 LYS B CE    1 
ATOM   4114 N  NZ    . LYS B 1 48  ? 18.261  -14.082 34.501 1.00 56.61  ? 1265 LYS B NZ    1 
ATOM   4115 N  N     . ALA B 1 49  ? 11.011  -12.473 36.824 1.00 27.32  ? 1266 ALA B N     1 
ATOM   4116 C  CA    . ALA B 1 49  ? 9.835   -13.118 37.412 1.00 27.74  ? 1266 ALA B CA    1 
ATOM   4117 C  C     . ALA B 1 49  ? 8.570   -12.766 36.633 1.00 45.02  ? 1266 ALA B C     1 
ATOM   4118 O  O     . ALA B 1 49  ? 7.788   -13.655 36.240 1.00 48.98  ? 1266 ALA B O     1 
ATOM   4119 C  CB    . ALA B 1 49  ? 9.689   -12.719 38.888 1.00 28.20  ? 1266 ALA B CB    1 
ATOM   4120 N  N     . ILE B 1 50  ? 8.365   -11.471 36.375 1.00 38.79  ? 1267 ILE B N     1 
ATOM   4121 C  CA    . ILE B 1 50  ? 7.188   -11.057 35.605 1.00 45.85  ? 1267 ILE B CA    1 
ATOM   4122 C  C     . ILE B 1 50  ? 7.184   -11.715 34.221 1.00 40.35  ? 1267 ILE B C     1 
ATOM   4123 O  O     . ILE B 1 50  ? 6.195   -12.342 33.811 1.00 27.11  ? 1267 ILE B O     1 
ATOM   4124 C  CB    . ILE B 1 50  ? 7.126   -9.521  35.514 1.00 31.65  ? 1267 ILE B CB    1 
ATOM   4125 C  CG1   . ILE B 1 50  ? 6.742   -8.928  36.878 1.00 35.88  ? 1267 ILE B CG1   1 
ATOM   4126 C  CG2   . ILE B 1 50  ? 6.131   -9.123  34.494 1.00 26.91  ? 1267 ILE B CG2   1 
ATOM   4127 C  CD1   . ILE B 1 50  ? 6.982   -7.407  37.007 1.00 40.56  ? 1267 ILE B CD1   1 
ATOM   4128 N  N     . ARG B 1 51  ? 8.321   -11.633 33.517 1.00 38.10  ? 1268 ARG B N     1 
ATOM   4129 C  CA    . ARG B 1 51  ? 8.455   -12.141 32.151 1.00 42.64  ? 1268 ARG B CA    1 
ATOM   4130 C  C     . ARG B 1 51  ? 8.178   -13.641 32.089 1.00 42.49  ? 1268 ARG B C     1 
ATOM   4131 O  O     . ARG B 1 51  ? 7.429   -14.113 31.224 1.00 41.19  ? 1268 ARG B O     1 
ATOM   4132 C  CB    . ARG B 1 51  ? 9.867   -11.808 31.618 1.00 39.94  ? 1268 ARG B CB    1 
ATOM   4133 C  CG    . ARG B 1 51  ? 10.254  -12.425 30.249 1.00 35.01  ? 1268 ARG B CG    1 
ATOM   4134 C  CD    . ARG B 1 51  ? 11.710  -12.125 29.893 1.00 49.39  ? 1268 ARG B CD    1 
ATOM   4135 N  NE    . ARG B 1 51  ? 12.641  -13.036 30.562 1.00 72.57  ? 1268 ARG B NE    1 
ATOM   4136 C  CZ    . ARG B 1 51  ? 13.957  -12.846 30.649 1.00 85.78  ? 1268 ARG B CZ    1 
ATOM   4137 N  NH1   . ARG B 1 51  ? 14.506  -11.763 30.119 1.00 78.24  ? 1268 ARG B NH1   1 
ATOM   4138 N  NH2   . ARG B 1 51  ? 14.721  -13.730 31.284 1.00 98.15  ? 1268 ARG B NH2   1 
ATOM   4139 N  N     . ASN B 1 52  ? 8.763   -14.397 33.022 1.00 31.36  ? 1269 ASN B N     1 
ATOM   4140 C  CA    . ASN B 1 52  ? 8.644   -15.845 33.030 1.00 29.99  ? 1269 ASN B CA    1 
ATOM   4141 C  C     . ASN B 1 52  ? 7.217   -16.301 33.289 1.00 36.63  ? 1269 ASN B C     1 
ATOM   4142 O  O     . ASN B 1 52  ? 6.684   -17.141 32.550 1.00 40.96  ? 1269 ASN B O     1 
ATOM   4143 C  CB    . ASN B 1 52  ? 9.567   -16.402 34.096 1.00 45.17  ? 1269 ASN B CB    1 
ATOM   4144 C  CG    . ASN B 1 52  ? 11.003  -16.359 33.675 1.00 46.75  ? 1269 ASN B CG    1 
ATOM   4145 O  OD1   . ASN B 1 52  ? 11.319  -16.137 32.495 1.00 44.17  ? 1269 ASN B OD1   1 
ATOM   4146 N  ND2   . ASN B 1 52  ? 11.895  -16.590 34.630 1.00 43.52  ? 1269 ASN B ND2   1 
ATOM   4147 N  N     . TRP B 1 53  ? 6.572   -15.750 34.326 1.00 37.21  ? 1270 TRP B N     1 
ATOM   4148 C  CA    . TRP B 1 53  ? 5.162   -16.069 34.532 1.00 28.33  ? 1270 TRP B CA    1 
ATOM   4149 C  C     . TRP B 1 53  ? 4.367   -15.816 33.258 1.00 33.17  ? 1270 TRP B C     1 
ATOM   4150 O  O     . TRP B 1 53  ? 3.665   -16.710 32.764 1.00 45.15  ? 1270 TRP B O     1 
ATOM   4151 C  CB    . TRP B 1 53  ? 4.611   -15.266 35.713 1.00 28.57  ? 1270 TRP B CB    1 
ATOM   4152 C  CG    . TRP B 1 53  ? 3.212   -15.631 36.148 1.00 36.24  ? 1270 TRP B CG    1 
ATOM   4153 C  CD1   . TRP B 1 53  ? 2.862   -16.498 37.140 1.00 41.07  ? 1270 TRP B CD1   1 
ATOM   4154 C  CD2   . TRP B 1 53  ? 1.974   -15.110 35.618 1.00 46.04  ? 1270 TRP B CD2   1 
ATOM   4155 N  NE1   . TRP B 1 53  ? 1.485   -16.568 37.259 1.00 44.05  ? 1270 TRP B NE1   1 
ATOM   4156 C  CE2   . TRP B 1 53  ? 0.916   -15.730 36.338 1.00 42.74  ? 1270 TRP B CE2   1 
ATOM   4157 C  CE3   . TRP B 1 53  ? 1.655   -14.186 34.599 1.00 38.62  ? 1270 TRP B CE3   1 
ATOM   4158 C  CZ2   . TRP B 1 53  ? -0.430  -15.459 36.077 1.00 41.95  ? 1270 TRP B CZ2   1 
ATOM   4159 C  CZ3   . TRP B 1 53  ? 0.318   -13.915 34.343 1.00 41.50  ? 1270 TRP B CZ3   1 
ATOM   4160 C  CH2   . TRP B 1 53  ? -0.712  -14.547 35.087 1.00 49.02  ? 1270 TRP B CH2   1 
ATOM   4161 N  N     . PHE B 1 54  ? 4.481   -14.603 32.695 1.00 34.11  ? 1271 PHE B N     1 
ATOM   4162 C  CA    . PHE B 1 54  ? 3.630   -14.262 31.555 1.00 44.22  ? 1271 PHE B CA    1 
ATOM   4163 C  C     . PHE B 1 54  ? 3.923   -15.134 30.344 1.00 50.84  ? 1271 PHE B C     1 
ATOM   4164 O  O     . PHE B 1 54  ? 3.002   -15.513 29.605 1.00 55.44  ? 1271 PHE B O     1 
ATOM   4165 C  CB    . PHE B 1 54  ? 3.776   -12.793 31.162 1.00 35.25  ? 1271 PHE B CB    1 
ATOM   4166 C  CG    . PHE B 1 54  ? 2.811   -12.375 30.075 1.00 34.74  ? 1271 PHE B CG    1 
ATOM   4167 C  CD1   . PHE B 1 54  ? 1.501   -12.049 30.374 1.00 29.25  ? 1271 PHE B CD1   1 
ATOM   4168 C  CD2   . PHE B 1 54  ? 3.203   -12.359 28.753 1.00 35.56  ? 1271 PHE B CD2   1 
ATOM   4169 C  CE1   . PHE B 1 54  ? 0.612   -11.698 29.375 1.00 27.59  ? 1271 PHE B CE1   1 
ATOM   4170 C  CE2   . PHE B 1 54  ? 2.315   -12.013 27.758 1.00 27.00  ? 1271 PHE B CE2   1 
ATOM   4171 C  CZ    . PHE B 1 54  ? 1.021   -11.683 28.066 1.00 27.33  ? 1271 PHE B CZ    1 
ATOM   4172 N  N     . ASP B 1 55  ? 5.184   -15.476 30.119 1.00 44.56  ? 1272 ASP B N     1 
ATOM   4173 C  CA    . ASP B 1 55  ? 5.466   -16.263 28.928 1.00 42.75  ? 1272 ASP B CA    1 
ATOM   4174 C  C     . ASP B 1 55  ? 4.980   -17.689 29.105 1.00 42.43  ? 1272 ASP B C     1 
ATOM   4175 O  O     . ASP B 1 55  ? 4.476   -18.288 28.158 1.00 37.14  ? 1272 ASP B O     1 
ATOM   4176 C  CB    . ASP B 1 55  ? 6.957   -16.236 28.581 1.00 40.82  ? 1272 ASP B CB    1 
ATOM   4177 C  CG    . ASP B 1 55  ? 7.261   -16.933 27.269 1.00 46.88  ? 1272 ASP B CG    1 
ATOM   4178 O  OD1   . ASP B 1 55  ? 7.047   -16.345 26.172 1.00 45.49  ? 1272 ASP B OD1   1 
ATOM   4179 O  OD2   . ASP B 1 55  ? 7.699   -18.099 27.341 1.00 62.45  ? 1272 ASP B OD2   1 
ATOM   4180 N  N     . ALA B 1 56  ? 5.144   -18.262 30.301 1.00 50.97  ? 1273 ALA B N     1 
ATOM   4181 C  CA    . ALA B 1 56  ? 4.558   -19.572 30.544 1.00 58.57  ? 1273 ALA B CA    1 
ATOM   4182 C  C     . ALA B 1 56  ? 3.080   -19.522 30.230 1.00 58.05  ? 1273 ALA B C     1 
ATOM   4183 O  O     . ALA B 1 56  ? 2.545   -20.396 29.527 1.00 56.46  ? 1273 ALA B O     1 
ATOM   4184 C  CB    . ALA B 1 56  ? 4.795   -20.006 31.991 1.00 55.18  ? 1273 ALA B CB    1 
ATOM   4185 N  N     . GLU B 1 57  ? 2.425   -18.452 30.684 1.00 41.40  ? 1274 GLU B N     1 
ATOM   4186 C  CA    . GLU B 1 57  ? 0.992   -18.323 30.486 1.00 35.52  ? 1274 GLU B CA    1 
ATOM   4187 C  C     . GLU B 1 57  ? 0.641   -18.301 29.006 1.00 38.84  ? 1274 GLU B C     1 
ATOM   4188 O  O     . GLU B 1 57  ? -0.280  -18.991 28.558 1.00 40.56  ? 1274 GLU B O     1 
ATOM   4189 C  CB    . GLU B 1 57  ? 0.499   -17.075 31.201 1.00 35.97  ? 1274 GLU B CB    1 
ATOM   4190 C  CG    . GLU B 1 57  ? 0.285   -17.335 32.662 1.00 48.56  ? 1274 GLU B CG    1 
ATOM   4191 C  CD    . GLU B 1 57  ? -0.387  -18.669 32.894 1.00 63.94  ? 1274 GLU B CD    1 
ATOM   4192 O  OE1   . GLU B 1 57  ? -1.487  -18.895 32.334 1.00 63.37  ? 1274 GLU B OE1   1 
ATOM   4193 O  OE2   . GLU B 1 57  ? 0.198   -19.498 33.618 1.00 67.62  ? 1274 GLU B OE2   1 
ATOM   4194 N  N     . ILE B 1 58  ? 1.339   -17.480 28.230 1.00 40.52  ? 1275 ILE B N     1 
ATOM   4195 C  CA    . ILE B 1 58  ? 0.916   -17.317 26.844 1.00 43.01  ? 1275 ILE B CA    1 
ATOM   4196 C  C     . ILE B 1 58  ? 1.418   -18.428 25.954 1.00 38.47  ? 1275 ILE B C     1 
ATOM   4197 O  O     . ILE B 1 58  ? 0.867   -18.626 24.859 1.00 30.42  ? 1275 ILE B O     1 
ATOM   4198 C  CB    . ILE B 1 58  ? 1.315   -15.953 26.257 1.00 43.26  ? 1275 ILE B CB    1 
ATOM   4199 C  CG1   . ILE B 1 58  ? 2.825   -15.838 26.123 1.00 43.83  ? 1275 ILE B CG1   1 
ATOM   4200 C  CG2   . ILE B 1 58  ? 0.761   -14.888 27.110 1.00 27.96  ? 1275 ILE B CG2   1 
ATOM   4201 C  CD1   . ILE B 1 58  ? 3.228   -15.349 24.772 1.00 44.12  ? 1275 ILE B CD1   1 
ATOM   4202 N  N     . THR B 1 59  ? 2.470   -19.128 26.368 1.00 38.84  ? 1276 THR B N     1 
ATOM   4203 C  CA    . THR B 1 59  ? 2.923   -20.287 25.615 1.00 47.34  ? 1276 THR B CA    1 
ATOM   4204 C  C     . THR B 1 59  ? 2.035   -21.488 25.874 1.00 46.08  ? 1276 THR B C     1 
ATOM   4205 O  O     . THR B 1 59  ? 1.803   -22.287 24.959 1.00 48.48  ? 1276 THR B O     1 
ATOM   4206 C  CB    . THR B 1 59  ? 4.369   -20.604 25.970 1.00 46.42  ? 1276 THR B CB    1 
ATOM   4207 O  OG1   . THR B 1 59  ? 5.215   -19.650 25.314 1.00 42.12  ? 1276 THR B OG1   1 
ATOM   4208 C  CG2   . THR B 1 59  ? 4.738   -21.987 25.506 1.00 29.26  ? 1276 THR B CG2   1 
ATOM   4209 N  N     . ARG B 1 60  ? 1.459   -21.568 27.075 1.00 36.13  ? 1277 ARG B N     1 
ATOM   4210 C  CA    . ARG B 1 60  ? 0.408   -22.543 27.329 1.00 30.82  ? 1277 ARG B CA    1 
ATOM   4211 C  C     . ARG B 1 60  ? -0.777  -22.328 26.404 1.00 35.13  ? 1277 ARG B C     1 
ATOM   4212 O  O     . ARG B 1 60  ? -1.420  -23.285 25.985 1.00 52.90  ? 1277 ARG B O     1 
ATOM   4213 C  CB    . ARG B 1 60  ? -0.026  -22.431 28.786 1.00 49.86  ? 1277 ARG B CB    1 
ATOM   4214 C  CG    . ARG B 1 60  ? -0.677  -23.643 29.378 1.00 57.36  ? 1277 ARG B CG    1 
ATOM   4215 C  CD    . ARG B 1 60  ? -0.994  -23.394 30.852 1.00 67.99  ? 1277 ARG B CD    1 
ATOM   4216 N  NE    . ARG B 1 60  ? -1.798  -22.183 31.035 1.00 79.79  ? 1277 ARG B NE    1 
ATOM   4217 C  CZ    . ARG B 1 60  ? -3.090  -22.072 30.716 1.00 80.30  ? 1277 ARG B CZ    1 
ATOM   4218 N  NH1   . ARG B 1 60  ? -3.748  -23.097 30.195 1.00 84.46  ? 1277 ARG B NH1   1 
ATOM   4219 N  NH2   . ARG B 1 60  ? -3.731  -20.931 30.915 1.00 75.42  ? 1277 ARG B NH2   1 
ATOM   4220 N  N     . LEU B 1 61  ? -1.076  -21.082 26.078 1.00 48.65  ? 1278 LEU B N     1 
ATOM   4221 C  CA    . LEU B 1 61  ? -2.194  -20.706 25.219 1.00 53.85  ? 1278 LEU B CA    1 
ATOM   4222 C  C     . LEU B 1 61  ? -1.977  -20.972 23.739 1.00 51.48  ? 1278 LEU B C     1 
ATOM   4223 O  O     . LEU B 1 61  ? -2.938  -20.903 22.968 1.00 53.09  ? 1278 LEU B O     1 
ATOM   4224 C  CB    . LEU B 1 61  ? -2.492  -19.219 25.410 1.00 54.22  ? 1278 LEU B CB    1 
ATOM   4225 C  CG    . LEU B 1 61  ? -2.979  -18.967 26.823 1.00 44.54  ? 1278 LEU B CG    1 
ATOM   4226 C  CD1   . LEU B 1 61  ? -3.291  -17.499 27.023 1.00 32.96  ? 1278 LEU B CD1   1 
ATOM   4227 C  CD2   . LEU B 1 61  ? -4.196  -19.881 27.099 1.00 39.79  ? 1278 LEU B CD2   1 
ATOM   4228 N  N     . GLY B 1 62  ? -0.741  -21.103 23.291 1.00 50.93  ? 1279 GLY B N     1 
ATOM   4229 C  CA    . GLY B 1 62  ? -0.490  -21.344 21.891 1.00 52.33  ? 1279 GLY B CA    1 
ATOM   4230 C  C     . GLY B 1 62  ? 0.201   -20.219 21.172 1.00 53.90  ? 1279 GLY B C     1 
ATOM   4231 O  O     . GLY B 1 62  ? 0.254   -20.231 19.939 1.00 62.70  ? 1279 GLY B O     1 
ATOM   4232 N  N     . VAL B 1 63  ? 0.667   -19.214 21.875 1.00 48.07  ? 1280 VAL B N     1 
ATOM   4233 C  CA    . VAL B 1 63  ? 1.378   -18.137 21.219 1.00 46.17  ? 1280 VAL B CA    1 
ATOM   4234 C  C     . VAL B 1 63  ? 2.829   -18.551 21.073 1.00 43.79  ? 1280 VAL B C     1 
ATOM   4235 O  O     . VAL B 1 63  ? 3.500   -18.845 22.069 1.00 41.94  ? 1280 VAL B O     1 
ATOM   4236 C  CB    . VAL B 1 63  ? 1.236   -16.832 22.010 1.00 42.57  ? 1280 VAL B CB    1 
ATOM   4237 C  CG1   . VAL B 1 63  ? 1.635   -15.677 21.138 1.00 36.70  ? 1280 VAL B CG1   1 
ATOM   4238 C  CG2   . VAL B 1 63  ? -0.200  -16.681 22.500 1.00 32.42  ? 1280 VAL B CG2   1 
ATOM   4239 N  N     . LYS B 1 64  ? 3.341   -18.490 19.852 1.00 41.41  ? 1281 LYS B N     1 
ATOM   4240 C  CA    . LYS B 1 64  ? 4.731   -18.832 19.598 1.00 41.40  ? 1281 LYS B CA    1 
ATOM   4241 C  C     . LYS B 1 64  ? 5.558   -17.559 19.607 1.00 47.57  ? 1281 LYS B C     1 
ATOM   4242 O  O     . LYS B 1 64  ? 5.033   -16.447 19.549 1.00 52.64  ? 1281 LYS B O     1 
ATOM   4243 C  CB    . LYS B 1 64  ? 4.923   -19.561 18.261 1.00 32.76  ? 1281 LYS B CB    1 
ATOM   4244 C  CG    . LYS B 1 64  ? 4.120   -20.838 18.062 1.00 48.25  ? 1281 LYS B CG    1 
ATOM   4245 C  CD    . LYS B 1 64  ? 3.514   -20.890 16.634 1.00 65.74  ? 1281 LYS B CD    1 
ATOM   4246 C  CE    . LYS B 1 64  ? 2.864   -22.256 16.324 1.00 77.82  ? 1281 LYS B CE    1 
ATOM   4247 N  NZ    . LYS B 1 64  ? 2.538   -22.459 14.870 1.00 84.47  ? 1281 LYS B NZ    1 
ATOM   4248 N  N     . GLU B 1 65  ? 6.871   -17.746 19.684 1.00 47.59  ? 1282 GLU B N     1 
ATOM   4249 C  CA    . GLU B 1 65  ? 7.833   -16.680 19.896 1.00 27.18  ? 1282 GLU B CA    1 
ATOM   4250 C  C     . GLU B 1 65  ? 8.796   -16.533 18.719 1.00 42.73  ? 1282 GLU B C     1 
ATOM   4251 O  O     . GLU B 1 65  ? 9.325   -17.523 18.205 1.00 45.73  ? 1282 GLU B O     1 
ATOM   4252 C  CB    . GLU B 1 65  ? 8.585   -16.961 21.164 1.00 26.99  ? 1282 GLU B CB    1 
ATOM   4253 C  CG    . GLU B 1 65  ? 9.811   -16.128 21.352 1.00 35.81  ? 1282 GLU B CG    1 
ATOM   4254 C  CD    . GLU B 1 65  ? 10.129  -15.913 22.815 1.00 46.77  ? 1282 GLU B CD    1 
ATOM   4255 O  OE1   . GLU B 1 65  ? 9.397   -16.482 23.660 1.00 63.22  ? 1282 GLU B OE1   1 
ATOM   4256 O  OE2   . GLU B 1 65  ? 11.055  -15.135 23.120 1.00 37.06  ? 1282 GLU B OE2   1 
ATOM   4257 N  N     . CYS B 1 66  ? 9.027   -15.287 18.303 1.00 47.70  ? 1283 CYS B N     1 
ATOM   4258 C  CA    . CYS B 1 66  ? 9.930   -14.964 17.198 1.00 49.20  ? 1283 CYS B CA    1 
ATOM   4259 C  C     . CYS B 1 66  ? 10.695  -13.705 17.590 1.00 51.51  ? 1283 CYS B C     1 
ATOM   4260 O  O     . CYS B 1 66  ? 10.622  -13.239 18.732 1.00 42.31  ? 1283 CYS B O     1 
ATOM   4261 C  CB    . CYS B 1 66  ? 9.168   -14.799 15.877 1.00 43.52  ? 1283 CYS B CB    1 
ATOM   4262 S  SG    . CYS B 1 66  ? 7.834   -13.619 16.007 1.00 57.07  ? 1283 CYS B SG    1 
ATOM   4263 N  N     . TYR B 1 67  ? 11.463  -13.170 16.643 1.00 57.31  ? 1284 TYR B N     1 
ATOM   4264 C  CA    . TYR B 1 67  ? 12.219  -11.950 16.898 1.00 50.21  ? 1284 TYR B CA    1 
ATOM   4265 C  C     . TYR B 1 67  ? 12.532  -11.240 15.591 1.00 43.26  ? 1284 TYR B C     1 
ATOM   4266 O  O     . TYR B 1 67  ? 13.314  -11.755 14.786 1.00 39.63  ? 1284 TYR B O     1 
ATOM   4267 C  CB    . TYR B 1 67  ? 13.494  -12.259 17.641 1.00 54.00  ? 1284 TYR B CB    1 
ATOM   4268 C  CG    . TYR B 1 67  ? 14.326  -11.014 17.818 1.00 63.26  ? 1284 TYR B CG    1 
ATOM   4269 C  CD1   . TYR B 1 67  ? 14.020  -10.089 18.809 1.00 70.31  ? 1284 TYR B CD1   1 
ATOM   4270 C  CD2   . TYR B 1 67  ? 15.400  -10.747 16.982 1.00 64.40  ? 1284 TYR B CD2   1 
ATOM   4271 C  CE1   . TYR B 1 67  ? 14.773  -8.942  18.975 1.00 77.78  ? 1284 TYR B CE1   1 
ATOM   4272 C  CE2   . TYR B 1 67  ? 16.165  -9.604  17.140 1.00 75.60  ? 1284 TYR B CE2   1 
ATOM   4273 C  CZ    . TYR B 1 67  ? 15.850  -8.700  18.136 1.00 80.15  ? 1284 TYR B CZ    1 
ATOM   4274 O  OH    . TYR B 1 67  ? 16.615  -7.555  18.286 1.00 76.56  ? 1284 TYR B OH    1 
ATOM   4275 N  N     . PHE B 1 68  ? 11.939  -10.038 15.395 1.00 36.14  ? 1285 PHE B N     1 
ATOM   4276 C  CA    . PHE B 1 68  ? 12.259  -9.203  14.241 1.00 35.31  ? 1285 PHE B CA    1 
ATOM   4277 C  C     . PHE B 1 68  ? 13.402  -8.266  14.586 1.00 33.88  ? 1285 PHE B C     1 
ATOM   4278 O  O     . PHE B 1 68  ? 13.622  -7.988  15.764 1.00 34.98  ? 1285 PHE B O     1 
ATOM   4279 C  CB    . PHE B 1 68  ? 11.028  -8.417  13.806 1.00 39.60  ? 1285 PHE B CB    1 
ATOM   4280 C  CG    . PHE B 1 68  ? 10.005  -9.250  13.073 1.00 48.84  ? 1285 PHE B CG    1 
ATOM   4281 C  CD1   . PHE B 1 68  ? 9.568   -10.460 13.595 1.00 46.43  ? 1285 PHE B CD1   1 
ATOM   4282 C  CD2   . PHE B 1 68  ? 9.471   -8.819  11.876 1.00 56.18  ? 1285 PHE B CD2   1 
ATOM   4283 C  CE1   . PHE B 1 68  ? 8.645   -11.222 12.950 1.00 41.22  ? 1285 PHE B CE1   1 
ATOM   4284 C  CE2   . PHE B 1 68  ? 8.537   -9.584  11.216 1.00 59.41  ? 1285 PHE B CE2   1 
ATOM   4285 C  CZ    . PHE B 1 68  ? 8.126   -10.792 11.751 1.00 49.13  ? 1285 PHE B CZ    1 
ATOM   4286 N  N     . PRO B 1 69  ? 14.147  -7.765  13.586 1.00 39.25  ? 1286 PRO B N     1 
ATOM   4287 C  CA    . PRO B 1 69  ? 15.335  -6.938  13.872 1.00 30.17  ? 1286 PRO B CA    1 
ATOM   4288 C  C     . PRO B 1 69  ? 14.956  -5.627  14.545 1.00 31.83  ? 1286 PRO B C     1 
ATOM   4289 O  O     . PRO B 1 69  ? 13.817  -5.174  14.438 1.00 42.28  ? 1286 PRO B O     1 
ATOM   4290 C  CB    . PRO B 1 69  ? 15.939  -6.673  12.483 1.00 30.75  ? 1286 PRO B CB    1 
ATOM   4291 C  CG    . PRO B 1 69  ? 15.199  -7.511  11.524 1.00 33.97  ? 1286 PRO B CG    1 
ATOM   4292 C  CD    . PRO B 1 69  ? 13.855  -7.794  12.140 1.00 39.42  ? 1286 PRO B CD    1 
ATOM   4293 N  N     . ILE B 1 70  ? 15.925  -5.020  15.250 1.00 28.81  ? 1287 ILE B N     1 
ATOM   4294 C  CA    . ILE B 1 70  ? 15.707  -3.699  15.863 1.00 43.21  ? 1287 ILE B CA    1 
ATOM   4295 C  C     . ILE B 1 70  ? 15.564  -2.589  14.842 1.00 44.21  ? 1287 ILE B C     1 
ATOM   4296 O  O     . ILE B 1 70  ? 15.118  -1.491  15.193 1.00 41.50  ? 1287 ILE B O     1 
ATOM   4297 C  CB    . ILE B 1 70  ? 16.842  -3.200  16.779 1.00 45.85  ? 1287 ILE B CB    1 
ATOM   4298 C  CG1   . ILE B 1 70  ? 18.190  -3.485  16.162 1.00 45.38  ? 1287 ILE B CG1   1 
ATOM   4299 C  CG2   . ILE B 1 70  ? 16.705  -3.683  18.194 1.00 55.54  ? 1287 ILE B CG2   1 
ATOM   4300 C  CD1   . ILE B 1 70  ? 19.243  -2.798  16.889 1.00 59.61  ? 1287 ILE B CD1   1 
ATOM   4301 N  N     . PHE B 1 71  ? 15.990  -2.818  13.615 1.00 28.09  ? 1288 PHE B N     1 
ATOM   4302 C  CA    . PHE B 1 71  ? 15.981  -1.784  12.606 1.00 28.68  ? 1288 PHE B CA    1 
ATOM   4303 C  C     . PHE B 1 71  ? 14.758  -1.902  11.702 1.00 28.92  ? 1288 PHE B C     1 
ATOM   4304 O  O     . PHE B 1 71  ? 14.369  -2.998  11.303 1.00 37.05  ? 1288 PHE B O     1 
ATOM   4305 C  CB    . PHE B 1 71  ? 17.249  -1.868  11.770 1.00 43.95  ? 1288 PHE B CB    1 
ATOM   4306 C  CG    . PHE B 1 71  ? 18.461  -1.513  12.528 1.00 48.23  ? 1288 PHE B CG    1 
ATOM   4307 C  CD1   . PHE B 1 71  ? 18.398  -0.538  13.509 1.00 44.09  ? 1288 PHE B CD1   1 
ATOM   4308 C  CD2   . PHE B 1 71  ? 19.660  -2.148  12.278 1.00 50.37  ? 1288 PHE B CD2   1 
ATOM   4309 C  CE1   . PHE B 1 71  ? 19.510  -0.192  14.225 1.00 41.02  ? 1288 PHE B CE1   1 
ATOM   4310 C  CE2   . PHE B 1 71  ? 20.781  -1.817  12.999 1.00 46.85  ? 1288 PHE B CE2   1 
ATOM   4311 C  CZ    . PHE B 1 71  ? 20.702  -0.837  13.980 1.00 45.82  ? 1288 PHE B CZ    1 
ATOM   4312 N  N     . VAL B 1 72  ? 14.173  -0.755  11.375 1.00 35.89  ? 1289 VAL B N     1 
ATOM   4313 C  CA    . VAL B 1 72  ? 13.028  -0.627  10.485 1.00 34.16  ? 1289 VAL B CA    1 
ATOM   4314 C  C     . VAL B 1 72  ? 13.440  0.334   9.375  1.00 33.27  ? 1289 VAL B C     1 
ATOM   4315 O  O     . VAL B 1 72  ? 13.851  1.455   9.662  1.00 48.64  ? 1289 VAL B O     1 
ATOM   4316 C  CB    . VAL B 1 72  ? 11.793  -0.111  11.233 1.00 33.02  ? 1289 VAL B CB    1 
ATOM   4317 C  CG1   . VAL B 1 72  ? 10.564  -0.270  10.355 1.00 29.79  ? 1289 VAL B CG1   1 
ATOM   4318 C  CG2   . VAL B 1 72  ? 11.617  -0.884  12.543 1.00 37.31  ? 1289 VAL B CG2   1 
ATOM   4319 N  N     . SER B 1 73  ? 13.367  -0.104  8.122  1.00 30.97  ? 1290 SER B N     1 
ATOM   4320 C  CA    . SER B 1 73  ? 13.573  0.814   6.995  1.00 34.78  ? 1290 SER B CA    1 
ATOM   4321 C  C     . SER B 1 73  ? 12.680  2.069   7.057  1.00 39.93  ? 1290 SER B C     1 
ATOM   4322 O  O     . SER B 1 73  ? 11.590  2.067   7.630  1.00 31.83  ? 1290 SER B O     1 
ATOM   4323 C  CB    . SER B 1 73  ? 13.324  0.086   5.678  1.00 35.44  ? 1290 SER B CB    1 
ATOM   4324 O  OG    . SER B 1 73  ? 11.953  0.144   5.348  1.00 33.53  ? 1290 SER B OG    1 
ATOM   4325 N  N     . ARG B 1 74  ? 13.165  3.170   6.484  1.00 39.95  ? 1291 ARG B N     1 
ATOM   4326 C  CA    . ARG B 1 74  ? 12.279  4.314   6.285  1.00 45.54  ? 1291 ARG B CA    1 
ATOM   4327 C  C     . ARG B 1 74  ? 11.024  3.881   5.532  1.00 36.79  ? 1291 ARG B C     1 
ATOM   4328 O  O     . ARG B 1 74  ? 9.901   4.140   5.970  1.00 39.60  ? 1291 ARG B O     1 
ATOM   4329 C  CB    . ARG B 1 74  ? 13.004  5.454   5.543  1.00 49.04  ? 1291 ARG B CB    1 
ATOM   4330 N  N     . ALA B 1 75  ? 11.199  3.163   4.423  1.00 34.19  ? 1292 ALA B N     1 
ATOM   4331 C  CA    . ALA B 1 75  ? 10.054  2.777   3.606  1.00 39.20  ? 1292 ALA B CA    1 
ATOM   4332 C  C     . ALA B 1 75  ? 9.071   1.904   4.385  1.00 38.72  ? 1292 ALA B C     1 
ATOM   4333 O  O     . ALA B 1 75  ? 7.851   2.056   4.253  1.00 55.06  ? 1292 ALA B O     1 
ATOM   4334 C  CB    . ALA B 1 75  ? 10.535  2.069   2.346  1.00 53.74  ? 1292 ALA B CB    1 
ATOM   4335 N  N     . ALA B 1 76  ? 9.577   0.964   5.174  1.00 32.90  ? 1293 ALA B N     1 
ATOM   4336 C  CA    . ALA B 1 76  ? 8.702   0.167   6.031  1.00 43.72  ? 1293 ALA B CA    1 
ATOM   4337 C  C     . ALA B 1 76  ? 7.835   1.047   6.914  1.00 49.13  ? 1293 ALA B C     1 
ATOM   4338 O  O     . ALA B 1 76  ? 6.603   0.961   6.898  1.00 57.64  ? 1293 ALA B O     1 
ATOM   4339 C  CB    . ALA B 1 76  ? 9.541   -0.765  6.909  1.00 45.02  ? 1293 ALA B CB    1 
ATOM   4340 N  N     . LEU B 1 77  ? 8.479   1.933   7.666  1.00 53.17  ? 1294 LEU B N     1 
ATOM   4341 C  CA    . LEU B 1 77  ? 7.784   2.763   8.639  1.00 51.60  ? 1294 LEU B CA    1 
ATOM   4342 C  C     . LEU B 1 77  ? 6.799   3.721   7.980  1.00 62.77  ? 1294 LEU B C     1 
ATOM   4343 O  O     . LEU B 1 77  ? 5.754   4.030   8.565  1.00 65.18  ? 1294 LEU B O     1 
ATOM   4344 C  CB    . LEU B 1 77  ? 8.828   3.518   9.453  1.00 45.84  ? 1294 LEU B CB    1 
ATOM   4345 C  CG    . LEU B 1 77  ? 8.496   3.983   10.868 1.00 53.10  ? 1294 LEU B CG    1 
ATOM   4346 C  CD1   . LEU B 1 77  ? 7.923   2.871   11.716 1.00 48.09  ? 1294 LEU B CD1   1 
ATOM   4347 C  CD2   . LEU B 1 77  ? 9.746   4.532   11.517 1.00 52.67  ? 1294 LEU B CD2   1 
ATOM   4348 N  N     . GLU B 1 78  ? 7.110   4.183   6.767  1.00 63.91  ? 1295 GLU B N     1 
ATOM   4349 C  CA    . GLU B 1 78  ? 6.343   5.200   6.046  1.00 67.86  ? 1295 GLU B CA    1 
ATOM   4350 C  C     . GLU B 1 78  ? 5.389   4.580   5.026  1.00 75.57  ? 1295 GLU B C     1 
ATOM   4351 O  O     . GLU B 1 78  ? 5.731   4.385   3.863  1.00 74.62  ? 1295 GLU B O     1 
ATOM   4352 C  CB    . GLU B 1 78  ? 7.297   6.199   5.402  1.00 78.03  ? 1295 GLU B CB    1 
ATOM   4353 C  CG    . GLU B 1 78  ? 8.303   6.751   6.421  1.00 87.50  ? 1295 GLU B CG    1 
ATOM   4354 C  CD    . GLU B 1 78  ? 8.969   8.069   6.019  1.00 100.18 ? 1295 GLU B CD    1 
ATOM   4355 O  OE1   . GLU B 1 78  ? 9.638   8.681   6.890  1.00 97.16  ? 1295 GLU B OE1   1 
ATOM   4356 O  OE2   . GLU B 1 78  ? 8.830   8.492   4.846  1.00 105.40 ? 1295 GLU B OE2   1 
ATOM   4357 N  N     . ARG B 1 79  ? 4.226   4.165   5.498  1.00 82.00  ? 1296 ARG B N     1 
ATOM   4358 C  CA    . ARG B 1 79  ? 3.168   3.688   4.622  1.00 79.85  ? 1296 ARG B CA    1 
ATOM   4359 C  C     . ARG B 1 79  ? 1.840   3.593   5.341  1.00 74.28  ? 1296 ARG B C     1 
ATOM   4360 O  O     . ARG B 1 79  ? 1.218   4.626   5.595  1.00 73.41  ? 1296 ARG B O     1 
ATOM   4361 C  CB    . ARG B 1 79  ? 3.577   2.379   3.913  1.00 89.03  ? 1296 ARG B CB    1 
ATOM   4362 C  CG    . ARG B 1 79  ? 2.455   1.392   3.516  1.00 102.49 ? 1296 ARG B CG    1 
ATOM   4363 C  CD    . ARG B 1 79  ? 3.072   0.048   3.089  1.00 108.02 ? 1296 ARG B CD    1 
ATOM   4364 N  NE    . ARG B 1 79  ? 2.099   -0.861  2.468  1.00 112.92 ? 1296 ARG B NE    1 
ATOM   4365 C  CZ    . ARG B 1 79  ? 2.114   -2.184  2.612  1.00 108.55 ? 1296 ARG B CZ    1 
ATOM   4366 N  NH1   . ARG B 1 79  ? 3.128   -2.750  3.248  1.00 97.02  ? 1296 ARG B NH1   1 
ATOM   4367 N  NH2   . ARG B 1 79  ? 1.181   -2.945  2.048  1.00 111.76 ? 1296 ARG B NH2   1 
ATOM   4368 N  N     . ASP B 1 86  ? 0.416   9.957   13.724 1.00 74.67  ? 1303 ASP B N     1 
ATOM   4369 C  CA    . ASP B 1 86  ? 1.821   10.293  13.561 1.00 70.92  ? 1303 ASP B CA    1 
ATOM   4370 C  C     . ASP B 1 86  ? 2.474   10.529  14.916 1.00 86.35  ? 1303 ASP B C     1 
ATOM   4371 O  O     . ASP B 1 86  ? 2.134   11.473  15.629 1.00 89.46  ? 1303 ASP B O     1 
ATOM   4372 C  CB    . ASP B 1 86  ? 2.003   11.535  12.673 1.00 42.74  ? 1303 ASP B CB    1 
ATOM   4373 N  N     . PHE B 1 87  ? 3.371   9.609   15.277 1.00 86.41  ? 1304 PHE B N     1 
ATOM   4374 C  CA    . PHE B 1 87  ? 4.336   9.767   16.358 1.00 76.32  ? 1304 PHE B CA    1 
ATOM   4375 C  C     . PHE B 1 87  ? 5.700   10.163  15.815 1.00 71.31  ? 1304 PHE B C     1 
ATOM   4376 O  O     . PHE B 1 87  ? 6.709   9.924   16.481 1.00 68.59  ? 1304 PHE B O     1 
ATOM   4377 C  CB    . PHE B 1 87  ? 4.523   8.483   17.184 1.00 74.10  ? 1304 PHE B CB    1 
ATOM   4378 C  CG    . PHE B 1 87  ? 3.255   7.779   17.586 1.00 63.21  ? 1304 PHE B CG    1 
ATOM   4379 C  CD1   . PHE B 1 87  ? 2.742   7.927   18.866 1.00 71.04  ? 1304 PHE B CD1   1 
ATOM   4380 C  CD2   . PHE B 1 87  ? 2.610   6.928   16.709 1.00 43.67  ? 1304 PHE B CD2   1 
ATOM   4381 C  CE1   . PHE B 1 87  ? 1.588   7.267   19.248 1.00 65.46  ? 1304 PHE B CE1   1 
ATOM   4382 C  CE2   . PHE B 1 87  ? 1.457   6.280   17.080 1.00 45.68  ? 1304 PHE B CE2   1 
ATOM   4383 C  CZ    . PHE B 1 87  ? 0.947   6.441   18.355 1.00 56.72  ? 1304 PHE B CZ    1 
ATOM   4384 N  N     . ALA B 1 88  ? 5.757   10.698  14.588 1.00 71.22  ? 1305 ALA B N     1 
ATOM   4385 C  CA    . ALA B 1 88  ? 7.013   10.928  13.875 1.00 58.77  ? 1305 ALA B CA    1 
ATOM   4386 C  C     . ALA B 1 88  ? 8.097   11.559  14.751 1.00 55.28  ? 1305 ALA B C     1 
ATOM   4387 O  O     . ALA B 1 88  ? 9.265   11.145  14.665 1.00 50.23  ? 1305 ALA B O     1 
ATOM   4388 C  CB    . ALA B 1 88  ? 6.766   11.780  12.627 1.00 44.02  ? 1305 ALA B CB    1 
ATOM   4389 N  N     . PRO B 1 89  ? 7.776   12.523  15.626 1.00 53.85  ? 1306 PRO B N     1 
ATOM   4390 C  CA    . PRO B 1 89  ? 8.835   13.125  16.452 1.00 54.25  ? 1306 PRO B CA    1 
ATOM   4391 C  C     . PRO B 1 89  ? 9.478   12.185  17.463 1.00 59.49  ? 1306 PRO B C     1 
ATOM   4392 O  O     . PRO B 1 89  ? 10.506  12.578  18.042 1.00 55.67  ? 1306 PRO B O     1 
ATOM   4393 C  CB    . PRO B 1 89  ? 8.107   14.275  17.152 1.00 51.82  ? 1306 PRO B CB    1 
ATOM   4394 C  CG    . PRO B 1 89  ? 7.067   14.670  16.168 1.00 56.26  ? 1306 PRO B CG    1 
ATOM   4395 C  CD    . PRO B 1 89  ? 6.555   13.351  15.679 1.00 57.99  ? 1306 PRO B CD    1 
ATOM   4396 N  N     . GLU B 1 90  ? 8.955   10.954  17.649 1.00 53.19  ? 1307 GLU B N     1 
ATOM   4397 C  CA    . GLU B 1 90  ? 9.448   10.000  18.646 1.00 32.75  ? 1307 GLU B CA    1 
ATOM   4398 C  C     . GLU B 1 90  ? 10.407  8.956   18.078 1.00 30.58  ? 1307 GLU B C     1 
ATOM   4399 O  O     . GLU B 1 90  ? 10.890  8.111   18.821 1.00 38.09  ? 1307 GLU B O     1 
ATOM   4400 C  CB    . GLU B 1 90  ? 8.264   9.293   19.341 1.00 33.84  ? 1307 GLU B CB    1 
ATOM   4401 C  CG    . GLU B 1 90  ? 7.497   10.170  20.348 1.00 58.78  ? 1307 GLU B CG    1 
ATOM   4402 C  CD    . GLU B 1 90  ? 6.703   9.387   21.416 1.00 74.01  ? 1307 GLU B CD    1 
ATOM   4403 O  OE1   . GLU B 1 90  ? 6.403   8.186   21.212 1.00 74.91  ? 1307 GLU B OE1   1 
ATOM   4404 O  OE2   . GLU B 1 90  ? 6.385   9.982   22.478 1.00 72.08  ? 1307 GLU B OE2   1 
ATOM   4405 N  N     . VAL B 1 91  ? 10.734  9.015   16.808 1.00 33.44  ? 1308 VAL B N     1 
ATOM   4406 C  CA    . VAL B 1 91  ? 11.540  7.983   16.165 1.00 40.37  ? 1308 VAL B CA    1 
ATOM   4407 C  C     . VAL B 1 91  ? 13.027  8.325   16.242 1.00 42.46  ? 1308 VAL B C     1 
ATOM   4408 O  O     . VAL B 1 91  ? 13.462  9.387   15.790 1.00 46.02  ? 1308 VAL B O     1 
ATOM   4409 C  CB    . VAL B 1 91  ? 11.104  7.811   14.703 1.00 42.80  ? 1308 VAL B CB    1 
ATOM   4410 C  CG1   . VAL B 1 91  ? 11.956  6.762   14.004 1.00 42.83  ? 1308 VAL B CG1   1 
ATOM   4411 C  CG2   . VAL B 1 91  ? 9.635   7.450   14.657 1.00 47.85  ? 1308 VAL B CG2   1 
ATOM   4412 N  N     . ALA B 1 92  ? 13.823  7.396   16.744 1.00 44.18  ? 1309 ALA B N     1 
ATOM   4413 C  CA    . ALA B 1 92  ? 15.265  7.574   16.767 1.00 36.37  ? 1309 ALA B CA    1 
ATOM   4414 C  C     . ALA B 1 92  ? 15.827  7.037   15.462 1.00 45.45  ? 1309 ALA B C     1 
ATOM   4415 O  O     . ALA B 1 92  ? 15.498  5.914   15.059 1.00 52.46  ? 1309 ALA B O     1 
ATOM   4416 C  CB    . ALA B 1 92  ? 15.889  6.853   17.957 1.00 29.84  ? 1309 ALA B CB    1 
ATOM   4417 N  N     . TRP B 1 93  ? 16.637  7.853   14.783 1.00 31.41  ? 1310 TRP B N     1 
ATOM   4418 C  CA    . TRP B 1 93  ? 17.108  7.540   13.435 1.00 34.55  ? 1310 TRP B CA    1 
ATOM   4419 C  C     . TRP B 1 93  ? 18.609  7.289   13.393 1.00 47.69  ? 1310 TRP B C     1 
ATOM   4420 O  O     . TRP B 1 93  ? 19.405  8.171   13.723 1.00 54.25  ? 1310 TRP B O     1 
ATOM   4421 C  CB    . TRP B 1 93  ? 16.761  8.655   12.464 1.00 34.49  ? 1310 TRP B CB    1 
ATOM   4422 C  CG    . TRP B 1 93  ? 15.361  8.607   12.145 1.00 55.35  ? 1310 TRP B CG    1 
ATOM   4423 C  CD1   . TRP B 1 93  ? 14.358  9.347   12.709 1.00 63.28  ? 1310 TRP B CD1   1 
ATOM   4424 C  CD2   . TRP B 1 93  ? 14.749  7.734   11.207 1.00 58.00  ? 1310 TRP B CD2   1 
ATOM   4425 N  NE1   . TRP B 1 93  ? 13.158  8.990   12.155 1.00 63.56  ? 1310 TRP B NE1   1 
ATOM   4426 C  CE2   . TRP B 1 93  ? 13.375  8.001   11.228 1.00 55.32  ? 1310 TRP B CE2   1 
ATOM   4427 C  CE3   . TRP B 1 93  ? 15.234  6.760   10.337 1.00 58.73  ? 1310 TRP B CE3   1 
ATOM   4428 C  CZ2   . TRP B 1 93  ? 12.485  7.321   10.424 1.00 45.96  ? 1310 TRP B CZ2   1 
ATOM   4429 C  CZ3   . TRP B 1 93  ? 14.350  6.098   9.536  1.00 52.72  ? 1310 TRP B CZ3   1 
ATOM   4430 C  CH2   . TRP B 1 93  ? 12.990  6.383   9.578  1.00 44.78  ? 1310 TRP B CH2   1 
ATOM   4431 N  N     . VAL B 1 94  ? 18.995  6.099   12.970 1.00 49.40  ? 1311 VAL B N     1 
ATOM   4432 C  CA    . VAL B 1 94  ? 20.362  5.898   12.536 1.00 53.52  ? 1311 VAL B CA    1 
ATOM   4433 C  C     . VAL B 1 94  ? 20.481  6.488   11.147 1.00 52.99  ? 1311 VAL B C     1 
ATOM   4434 O  O     . VAL B 1 94  ? 19.694  6.163   10.246 1.00 59.33  ? 1311 VAL B O     1 
ATOM   4435 C  CB    . VAL B 1 94  ? 20.742  4.411   12.540 1.00 48.81  ? 1311 VAL B CB    1 
ATOM   4436 C  CG1   . VAL B 1 94  ? 22.163  4.254   12.004 1.00 44.06  ? 1311 VAL B CG1   1 
ATOM   4437 C  CG2   . VAL B 1 94  ? 20.583  3.816   13.938 1.00 35.99  ? 1311 VAL B CG2   1 
ATOM   4438 N  N     . THR B 1 95  ? 21.436  7.386   10.988 1.00 52.37  ? 1312 THR B N     1 
ATOM   4439 C  CA    . THR B 1 95  ? 21.691  8.068   9.737  1.00 53.29  ? 1312 THR B CA    1 
ATOM   4440 C  C     . THR B 1 95  ? 23.071  7.768   9.165  1.00 53.59  ? 1312 THR B C     1 
ATOM   4441 O  O     . THR B 1 95  ? 23.310  8.050   7.981  1.00 50.98  ? 1312 THR B O     1 
ATOM   4442 C  CB    . THR B 1 95  ? 21.543  9.579   9.958  1.00 52.26  ? 1312 THR B CB    1 
ATOM   4443 O  OG1   . THR B 1 95  ? 22.687  10.077  10.664 1.00 50.35  ? 1312 THR B OG1   1 
ATOM   4444 C  CG2   . THR B 1 95  ? 20.321  9.846   10.823 1.00 45.24  ? 1312 THR B CG2   1 
ATOM   4445 N  N     . LYS B 1 96  ? 23.966  7.192   9.971  1.00 55.67  ? 1313 LYS B N     1 
ATOM   4446 C  CA    . LYS B 1 96  ? 25.401  7.132   9.724  1.00 53.97  ? 1313 LYS B CA    1 
ATOM   4447 C  C     . LYS B 1 96  ? 25.991  5.804   10.225 1.00 60.35  ? 1313 LYS B C     1 
ATOM   4448 O  O     . LYS B 1 96  ? 25.671  5.351   11.328 1.00 61.14  ? 1313 LYS B O     1 
ATOM   4449 C  CB    . LYS B 1 96  ? 26.051  8.323   10.436 1.00 35.82  ? 1313 LYS B CB    1 
ATOM   4450 C  CG    . LYS B 1 96  ? 27.327  8.842   9.849  1.00 43.91  ? 1313 LYS B CG    1 
ATOM   4451 C  CD    . LYS B 1 96  ? 28.161  9.506   10.951 1.00 53.72  ? 1313 LYS B CD    1 
ATOM   4452 C  CE    . LYS B 1 96  ? 27.744  10.932  11.233 1.00 51.05  ? 1313 LYS B CE    1 
ATOM   4453 N  NZ    . LYS B 1 96  ? 28.866  11.863  10.941 1.00 57.88  ? 1313 LYS B NZ    1 
ATOM   4454 N  N     . SER B 1 97  ? 26.874  5.196   9.432  1.00 50.10  ? 1314 SER B N     1 
ATOM   4455 C  CA    . SER B 1 97  ? 27.646  4.026   9.859  1.00 47.17  ? 1314 SER B CA    1 
ATOM   4456 C  C     . SER B 1 97  ? 29.102  4.469   9.988  1.00 51.38  ? 1314 SER B C     1 
ATOM   4457 O  O     . SER B 1 97  ? 29.851  4.519   9.012  1.00 54.61  ? 1314 SER B O     1 
ATOM   4458 C  CB    . SER B 1 97  ? 27.483  2.823   8.908  1.00 53.74  ? 1314 SER B CB    1 
ATOM   4459 O  OG    . SER B 1 97  ? 27.986  3.064   7.601  1.00 63.84  ? 1314 SER B OG    1 
ATOM   4460 N  N     . GLY B 1 98  ? 29.466  4.895   11.182 1.00 52.49  ? 1315 GLY B N     1 
ATOM   4461 C  CA    . GLY B 1 98  ? 30.821  5.322   11.455 1.00 49.21  ? 1315 GLY B CA    1 
ATOM   4462 C  C     . GLY B 1 98  ? 30.982  6.743   10.992 1.00 52.63  ? 1315 GLY B C     1 
ATOM   4463 O  O     . GLY B 1 98  ? 30.394  7.645   11.589 1.00 49.55  ? 1315 GLY B O     1 
ATOM   4464 N  N     . ASP B 1 99  ? 31.758  6.954   9.924  1.00 62.27  ? 1316 ASP B N     1 
ATOM   4465 C  CA    . ASP B 1 99  ? 31.813  8.232   9.223  1.00 53.60  ? 1316 ASP B CA    1 
ATOM   4466 C  C     . ASP B 1 99  ? 31.036  8.222   7.920  1.00 59.81  ? 1316 ASP B C     1 
ATOM   4467 O  O     . ASP B 1 99  ? 30.760  9.292   7.385  1.00 65.36  ? 1316 ASP B O     1 
ATOM   4468 C  CB    . ASP B 1 99  ? 33.256  8.677   8.977  1.00 56.95  ? 1316 ASP B CB    1 
ATOM   4469 C  CG    . ASP B 1 99  ? 33.659  9.816   9.899  1.00 71.12  ? 1316 ASP B CG    1 
ATOM   4470 O  OD1   . ASP B 1 99  ? 34.860  10.184  9.908  1.00 80.28  ? 1316 ASP B OD1   1 
ATOM   4471 O  OD2   . ASP B 1 99  ? 32.765  10.325  10.628 1.00 63.35  ? 1316 ASP B OD2   1 
ATOM   4472 N  N     . SER B 1 100 ? 30.769  7.048   7.355  1.00 73.68  ? 1317 SER B N     1 
ATOM   4473 C  CA    . SER B 1 100 ? 30.039  6.951   6.101  1.00 80.05  ? 1317 SER B CA    1 
ATOM   4474 C  C     . SER B 1 100 ? 28.555  7.204   6.363  1.00 73.06  ? 1317 SER B C     1 
ATOM   4475 O  O     . SER B 1 100 ? 27.936  6.539   7.201  1.00 61.61  ? 1317 SER B O     1 
ATOM   4476 C  CB    . SER B 1 100 ? 30.249  5.577   5.464  1.00 92.66  ? 1317 SER B CB    1 
ATOM   4477 O  OG    . SER B 1 100 ? 29.126  5.176   4.694  1.00 103.44 ? 1317 SER B OG    1 
ATOM   4478 N  N     . GLU B 1 101 ? 27.991  8.181   5.659  1.00 74.46  ? 1318 GLU B N     1 
ATOM   4479 C  CA    . GLU B 1 101 ? 26.577  8.479   5.793  1.00 66.47  ? 1318 GLU B CA    1 
ATOM   4480 C  C     . GLU B 1 101 ? 25.745  7.517   4.955  1.00 56.36  ? 1318 GLU B C     1 
ATOM   4481 O  O     . GLU B 1 101 ? 26.115  7.184   3.822  1.00 53.51  ? 1318 GLU B O     1 
ATOM   4482 C  CB    . GLU B 1 101 ? 26.296  9.922   5.381  1.00 69.09  ? 1318 GLU B CB    1 
ATOM   4483 C  CG    . GLU B 1 101 ? 25.180  10.514  6.202  1.00 77.95  ? 1318 GLU B CG    1 
ATOM   4484 C  CD    . GLU B 1 101 ? 24.501  11.660  5.532  1.00 86.91  ? 1318 GLU B CD    1 
ATOM   4485 O  OE1   . GLU B 1 101 ? 23.296  11.853  5.817  1.00 90.25  ? 1318 GLU B OE1   1 
ATOM   4486 O  OE2   . GLU B 1 101 ? 25.172  12.368  4.748  1.00 87.48  ? 1318 GLU B OE2   1 
ATOM   4487 N  N     . LEU B 1 102 ? 24.598  7.102   5.512  1.00 53.63  ? 1319 LEU B N     1 
ATOM   4488 C  CA    . LEU B 1 102 ? 23.806  5.997   4.969  1.00 53.92  ? 1319 LEU B CA    1 
ATOM   4489 C  C     . LEU B 1 102 ? 22.958  6.448   3.794  1.00 57.51  ? 1319 LEU B C     1 
ATOM   4490 O  O     . LEU B 1 102 ? 22.361  7.526   3.828  1.00 57.21  ? 1319 LEU B O     1 
ATOM   4491 C  CB    . LEU B 1 102 ? 22.856  5.449   6.027  1.00 45.50  ? 1319 LEU B CB    1 
ATOM   4492 C  CG    . LEU B 1 102 ? 23.317  4.512   7.128  1.00 52.06  ? 1319 LEU B CG    1 
ATOM   4493 C  CD1   . LEU B 1 102 ? 22.129  4.193   8.017  1.00 49.05  ? 1319 LEU B CD1   1 
ATOM   4494 C  CD2   . LEU B 1 102 ? 23.925  3.248   6.533  1.00 60.70  ? 1319 LEU B CD2   1 
ATOM   4495 N  N     . ALA B 1 103 ? 22.844  5.580   2.789  1.00 61.60  ? 1320 ALA B N     1 
ATOM   4496 C  CA    . ALA B 1 103 ? 22.014  5.871   1.626  1.00 62.33  ? 1320 ALA B CA    1 
ATOM   4497 C  C     . ALA B 1 103 ? 20.641  6.329   2.096  1.00 66.49  ? 1320 ALA B C     1 
ATOM   4498 O  O     . ALA B 1 103 ? 20.269  7.491   1.902  1.00 72.24  ? 1320 ALA B O     1 
ATOM   4499 C  CB    . ALA B 1 103 ? 21.913  4.653   0.700  1.00 58.58  ? 1320 ALA B CB    1 
ATOM   4500 N  N     . GLU B 1 104 ? 19.882  5.428   2.706  1.00 66.37  ? 1321 GLU B N     1 
ATOM   4501 C  CA    . GLU B 1 104 ? 18.660  5.755   3.424  1.00 62.56  ? 1321 GLU B CA    1 
ATOM   4502 C  C     . GLU B 1 104 ? 18.845  5.539   4.925  1.00 62.29  ? 1321 GLU B C     1 
ATOM   4503 O  O     . GLU B 1 104 ? 19.560  4.616   5.332  1.00 71.27  ? 1321 GLU B O     1 
ATOM   4504 C  CB    . GLU B 1 104 ? 17.484  4.907   2.922  1.00 63.44  ? 1321 GLU B CB    1 
ATOM   4505 N  N     . PRO B 1 105 ? 18.225  6.358   5.771  1.00 60.92  ? 1322 PRO B N     1 
ATOM   4506 C  CA    . PRO B 1 105 ? 18.280  6.106   7.218  1.00 60.31  ? 1322 PRO B CA    1 
ATOM   4507 C  C     . PRO B 1 105 ? 17.442  4.903   7.638  1.00 53.19  ? 1322 PRO B C     1 
ATOM   4508 O  O     . PRO B 1 105 ? 16.440  4.554   7.004  1.00 52.63  ? 1322 PRO B O     1 
ATOM   4509 C  CB    . PRO B 1 105 ? 17.718  7.398   7.836  1.00 46.97  ? 1322 PRO B CB    1 
ATOM   4510 C  CG    . PRO B 1 105 ? 17.600  8.368   6.732  1.00 58.38  ? 1322 PRO B CG    1 
ATOM   4511 C  CD    . PRO B 1 105 ? 17.499  7.595   5.459  1.00 63.68  ? 1322 PRO B CD    1 
ATOM   4512 N  N     . ILE B 1 106 ? 17.854  4.277   8.743  1.00 36.44  ? 1323 ILE B N     1 
ATOM   4513 C  CA    . ILE B 1 106 ? 17.067  3.192   9.313  1.00 38.54  ? 1323 ILE B CA    1 
ATOM   4514 C  C     . ILE B 1 106 ? 16.614  3.652   10.683 1.00 39.48  ? 1323 ILE B C     1 
ATOM   4515 O  O     . ILE B 1 106 ? 17.282  4.462   11.329 1.00 42.93  ? 1323 ILE B O     1 
ATOM   4516 C  CB    . ILE B 1 106 ? 17.818  1.841   9.408  1.00 36.43  ? 1323 ILE B CB    1 
ATOM   4517 C  CG1   . ILE B 1 106 ? 19.163  2.037   10.062 1.00 43.36  ? 1323 ILE B CG1   1 
ATOM   4518 C  CG2   . ILE B 1 106 ? 18.031  1.214   8.039  1.00 31.89  ? 1323 ILE B CG2   1 
ATOM   4519 C  CD1   . ILE B 1 106 ? 20.061  0.868   9.859  1.00 44.63  ? 1323 ILE B CD1   1 
ATOM   4520 N  N     . ALA B 1 107 ? 15.464  3.155   11.121 1.00 31.87  ? 1324 ALA B N     1 
ATOM   4521 C  CA    . ALA B 1 107 ? 14.833  3.622   12.338 1.00 31.86  ? 1324 ALA B CA    1 
ATOM   4522 C  C     . ALA B 1 107 ? 14.916  2.565   13.420 1.00 29.49  ? 1324 ALA B C     1 
ATOM   4523 O  O     . ALA B 1 107 ? 14.644  1.405   13.171 1.00 29.18  ? 1324 ALA B O     1 
ATOM   4524 C  CB    . ALA B 1 107 ? 13.374  3.968   12.082 1.00 30.43  ? 1324 ALA B CB    1 
ATOM   4525 N  N     . VAL B 1 108 ? 15.145  2.950   14.637 1.00 29.21  ? 1325 VAL B N     1 
ATOM   4526 C  CA    . VAL B 1 108 ? 15.157  2.028   15.709 1.00 32.62  ? 1325 VAL B CA    1 
ATOM   4527 C  C     . VAL B 1 108 ? 13.733  1.830   16.128 1.00 38.04  ? 1325 VAL B C     1 
ATOM   4528 O  O     . VAL B 1 108 ? 13.073  2.731   16.474 1.00 53.08  ? 1325 VAL B O     1 
ATOM   4529 C  CB    . VAL B 1 108 ? 15.942  2.567   16.867 1.00 37.95  ? 1325 VAL B CB    1 
ATOM   4530 C  CG1   . VAL B 1 108 ? 16.067  1.542   17.926 1.00 27.81  ? 1325 VAL B CG1   1 
ATOM   4531 C  CG2   . VAL B 1 108 ? 17.307  2.950   16.415 1.00 34.32  ? 1325 VAL B CG2   1 
ATOM   4532 N  N     . ARG B 1 109 ? 13.288  0.609   16.191 1.00 36.00  ? 1326 ARG B N     1 
ATOM   4533 C  CA    . ARG B 1 109 ? 11.921  0.349   16.436 1.00 40.58  ? 1326 ARG B CA    1 
ATOM   4534 C  C     . ARG B 1 109 ? 11.364  0.782   17.696 1.00 37.52  ? 1326 ARG B C     1 
ATOM   4535 O  O     . ARG B 1 109 ? 11.972  0.715   18.678 1.00 43.76  ? 1326 ARG B O     1 
ATOM   4536 C  CB    . ARG B 1 109 ? 11.692  -1.138  16.334 1.00 49.73  ? 1326 ARG B CB    1 
ATOM   4537 C  CG    . ARG B 1 109 ? 12.313  -1.928  17.445 1.00 42.16  ? 1326 ARG B CG    1 
ATOM   4538 C  CD    . ARG B 1 109 ? 11.653  -3.230  17.782 1.00 37.66  ? 1326 ARG B CD    1 
ATOM   4539 N  NE    . ARG B 1 109 ? 12.550  -3.931  18.655 1.00 41.40  ? 1326 ARG B NE    1 
ATOM   4540 C  CZ    . ARG B 1 109 ? 13.217  -5.002  18.322 1.00 43.20  ? 1326 ARG B CZ    1 
ATOM   4541 N  NH1   . ARG B 1 109 ? 13.048  -5.510  17.155 1.00 49.14  ? 1326 ARG B NH1   1 
ATOM   4542 N  NH2   . ARG B 1 109 ? 14.040  -5.560  19.148 1.00 36.15  ? 1326 ARG B NH2   1 
ATOM   4543 N  N     . PRO B 1 110 ? 10.168  1.271   17.635 1.00 40.64  ? 1327 PRO B N     1 
ATOM   4544 C  CA    . PRO B 1 110 ? 9.240   1.745   18.620 1.00 44.79  ? 1327 PRO B CA    1 
ATOM   4545 C  C     . PRO B 1 110 ? 8.178   0.752   18.927 1.00 41.09  ? 1327 PRO B C     1 
ATOM   4546 O  O     . PRO B 1 110 ? 7.707   0.766   19.997 1.00 44.70  ? 1327 PRO B O     1 
ATOM   4547 C  CB    . PRO B 1 110 ? 8.638   2.921   17.955 1.00 44.29  ? 1327 PRO B CB    1 
ATOM   4548 C  CG    . PRO B 1 110 ? 8.748   2.663   16.541 1.00 44.09  ? 1327 PRO B CG    1 
ATOM   4549 C  CD    . PRO B 1 110 ? 9.906   1.815   16.321 1.00 43.33  ? 1327 PRO B CD    1 
ATOM   4550 N  N     . THR B 1 111 ? 7.871   -0.096  17.974 1.00 31.53  ? 1328 THR B N     1 
ATOM   4551 C  CA    . THR B 1 111 ? 6.901   -1.152  17.930 1.00 30.79  ? 1328 THR B CA    1 
ATOM   4552 C  C     . THR B 1 111 ? 7.064   -1.826  16.585 1.00 37.82  ? 1328 THR B C     1 
ATOM   4553 O  O     . THR B 1 111 ? 7.700   -1.342  15.708 1.00 47.19  ? 1328 THR B O     1 
ATOM   4554 C  CB    . THR B 1 111 ? 5.483   -0.708  18.226 1.00 42.08  ? 1328 THR B CB    1 
ATOM   4555 O  OG1   . THR B 1 111 ? 4.731   -1.820  18.636 1.00 45.12  ? 1328 THR B OG1   1 
ATOM   4556 C  CG2   . THR B 1 111 ? 4.824   -0.174  17.079 1.00 49.71  ? 1328 THR B CG2   1 
ATOM   4557 N  N     . SER B 1 112 ? 6.450   -2.962  16.377 1.00 39.41  ? 1329 SER B N     1 
ATOM   4558 C  CA    . SER B 1 112 ? 6.754   -3.745  15.175 1.00 43.05  ? 1329 SER B CA    1 
ATOM   4559 C  C     . SER B 1 112 ? 5.574   -3.970  14.235 1.00 45.91  ? 1329 SER B C     1 
ATOM   4560 O  O     . SER B 1 112 ? 5.718   -4.752  13.289 1.00 56.03  ? 1329 SER B O     1 
ATOM   4561 C  CB    . SER B 1 112 ? 7.331   -5.123  15.543 1.00 36.05  ? 1329 SER B CB    1 
ATOM   4562 O  OG    . SER B 1 112 ? 8.582   -5.056  16.190 1.00 26.81  ? 1329 SER B OG    1 
ATOM   4563 N  N     . GLU B 1 113 ? 4.470   -3.231  14.380 1.00 37.34  ? 1330 GLU B N     1 
ATOM   4564 C  CA    . GLU B 1 113 ? 3.345   -3.411  13.461 1.00 36.74  ? 1330 GLU B CA    1 
ATOM   4565 C  C     . GLU B 1 113 ? 3.796   -3.291  12.016 1.00 41.21  ? 1330 GLU B C     1 
ATOM   4566 O  O     . GLU B 1 113 ? 3.540   -4.172  11.199 1.00 45.80  ? 1330 GLU B O     1 
ATOM   4567 C  CB    . GLU B 1 113 ? 2.248   -2.377  13.747 1.00 36.12  ? 1330 GLU B CB    1 
ATOM   4568 C  CG    . GLU B 1 113 ? 1.279   -2.745  14.850 1.00 40.83  ? 1330 GLU B CG    1 
ATOM   4569 C  CD    . GLU B 1 113 ? 1.821   -2.364  16.189 1.00 44.84  ? 1330 GLU B CD    1 
ATOM   4570 O  OE1   . GLU B 1 113 ? 3.010   -2.008  16.205 1.00 36.93  ? 1330 GLU B OE1   1 
ATOM   4571 O  OE2   . GLU B 1 113 ? 1.084   -2.420  17.206 1.00 53.59  ? 1330 GLU B OE2   1 
ATOM   4572 N  N     . THR B 1 114 ? 4.505   -2.206  11.708 1.00 46.90  ? 1331 THR B N     1 
ATOM   4573 C  CA    . THR B 1 114 ? 5.029   -1.917  10.380 1.00 48.84  ? 1331 THR B CA    1 
ATOM   4574 C  C     . THR B 1 114 ? 5.892   -3.027  9.811  1.00 41.80  ? 1331 THR B C     1 
ATOM   4575 O  O     . THR B 1 114 ? 6.118   -3.056  8.601  1.00 37.94  ? 1331 THR B O     1 
ATOM   4576 C  CB    . THR B 1 114 ? 5.842   -0.629  10.432 1.00 51.32  ? 1331 THR B CB    1 
ATOM   4577 O  OG1   . THR B 1 114 ? 6.535   -0.566  11.691 1.00 59.80  ? 1331 THR B OG1   1 
ATOM   4578 C  CG2   . THR B 1 114 ? 4.943   0.567   10.265 1.00 34.27  ? 1331 THR B CG2   1 
ATOM   4579 N  N     . VAL B 1 115 ? 6.427   -3.911  10.637 1.00 54.50  ? 1332 VAL B N     1 
ATOM   4580 C  CA    . VAL B 1 115 ? 7.321   -4.955  10.167 1.00 58.53  ? 1332 VAL B CA    1 
ATOM   4581 C  C     . VAL B 1 115 ? 6.668   -6.328  10.262 1.00 51.17  ? 1332 VAL B C     1 
ATOM   4582 O  O     . VAL B 1 115 ? 6.798   -7.145  9.347  1.00 53.41  ? 1332 VAL B O     1 
ATOM   4583 C  CB    . VAL B 1 115 ? 8.662   -4.924  10.926 1.00 55.94  ? 1332 VAL B CB    1 
ATOM   4584 C  CG1   . VAL B 1 115 ? 9.696   -5.631  10.141 1.00 59.32  ? 1332 VAL B CG1   1 
ATOM   4585 C  CG2   . VAL B 1 115 ? 9.106   -3.506  11.116 1.00 67.48  ? 1332 VAL B CG2   1 
ATOM   4586 N  N     . MET B 1 116 ? 5.905   -6.564  11.324 1.00 38.47  ? 1333 MET B N     1 
ATOM   4587 C  CA    . MET B 1 116 ? 5.229   -7.833  11.491 1.00 34.59  ? 1333 MET B CA    1 
ATOM   4588 C  C     . MET B 1 116 ? 4.022   -7.986  10.578 1.00 34.71  ? 1333 MET B C     1 
ATOM   4589 O  O     . MET B 1 116 ? 3.735   -9.104  10.136 1.00 39.82  ? 1333 MET B O     1 
ATOM   4590 C  CB    . MET B 1 116 ? 4.804   -8.007  12.946 1.00 45.20  ? 1333 MET B CB    1 
ATOM   4591 C  CG    . MET B 1 116 ? 5.927   -8.457  13.861 1.00 56.06  ? 1333 MET B CG    1 
ATOM   4592 S  SD    . MET B 1 116 ? 5.319   -8.876  15.499 1.00 69.53  ? 1333 MET B SD    1 
ATOM   4593 C  CE    . MET B 1 116 ? 4.198   -10.205 15.068 1.00 64.73  ? 1333 MET B CE    1 
ATOM   4594 N  N     . TYR B 1 117 ? 3.315   -6.913  10.251 1.00 42.31  ? 1334 TYR B N     1 
ATOM   4595 C  CA    . TYR B 1 117 ? 2.083   -7.173  9.501  1.00 47.94  ? 1334 TYR B CA    1 
ATOM   4596 C  C     . TYR B 1 117 ? 2.346   -7.497  8.034  1.00 59.52  ? 1334 TYR B C     1 
ATOM   4597 O  O     . TYR B 1 117 ? 1.660   -8.368  7.477  1.00 70.55  ? 1334 TYR B O     1 
ATOM   4598 C  CB    . TYR B 1 117 ? 1.098   -6.013  9.627  1.00 33.42  ? 1334 TYR B CB    1 
ATOM   4599 C  CG    . TYR B 1 117 ? 0.620   -5.870  11.049 1.00 44.05  ? 1334 TYR B CG    1 
ATOM   4600 C  CD1   . TYR B 1 117 ? 0.846   -6.879  11.980 1.00 48.69  ? 1334 TYR B CD1   1 
ATOM   4601 C  CD2   . TYR B 1 117 ? -0.005  -4.722  11.483 1.00 47.37  ? 1334 TYR B CD2   1 
ATOM   4602 C  CE1   . TYR B 1 117 ? 0.442   -6.750  13.295 1.00 48.89  ? 1334 TYR B CE1   1 
ATOM   4603 C  CE2   . TYR B 1 117 ? -0.426  -4.595  12.788 1.00 49.78  ? 1334 TYR B CE2   1 
ATOM   4604 C  CZ    . TYR B 1 117 ? -0.199  -5.609  13.691 1.00 49.35  ? 1334 TYR B CZ    1 
ATOM   4605 O  OH    . TYR B 1 117 ? -0.604  -5.468  14.999 1.00 52.34  ? 1334 TYR B OH    1 
ATOM   4606 N  N     . PRO B 1 118 ? 3.328   -6.870  7.376  1.00 53.22  ? 1335 PRO B N     1 
ATOM   4607 C  CA    . PRO B 1 118 ? 3.710   -7.374  6.050  1.00 41.97  ? 1335 PRO B CA    1 
ATOM   4608 C  C     . PRO B 1 118 ? 4.126   -8.835  6.088  1.00 40.06  ? 1335 PRO B C     1 
ATOM   4609 O  O     . PRO B 1 118 ? 3.734   -9.620  5.209  1.00 32.12  ? 1335 PRO B O     1 
ATOM   4610 C  CB    . PRO B 1 118 ? 4.872   -6.453  5.647  1.00 31.73  ? 1335 PRO B CB    1 
ATOM   4611 C  CG    . PRO B 1 118 ? 4.674   -5.294  6.370  1.00 31.44  ? 1335 PRO B CG    1 
ATOM   4612 C  CD    . PRO B 1 118 ? 4.061   -5.641  7.692  1.00 30.81  ? 1335 PRO B CD    1 
ATOM   4613 N  N     . ALA B 1 119 ? 4.911   -9.224  7.096  1.00 42.07  ? 1336 ALA B N     1 
ATOM   4614 C  CA    . ALA B 1 119 ? 5.233   -10.636 7.247  1.00 46.98  ? 1336 ALA B CA    1 
ATOM   4615 C  C     . ALA B 1 119 ? 3.962   -11.464 7.310  1.00 46.42  ? 1336 ALA B C     1 
ATOM   4616 O  O     . ALA B 1 119 ? 3.833   -12.445 6.578  1.00 39.70  ? 1336 ALA B O     1 
ATOM   4617 C  CB    . ALA B 1 119 ? 6.081   -10.869 8.503  1.00 41.19  ? 1336 ALA B CB    1 
ATOM   4618 N  N     . TYR B 1 120 ? 2.968   -11.004 8.087  1.00 49.30  ? 1337 TYR B N     1 
ATOM   4619 C  CA    . TYR B 1 120 ? 1.694   -11.715 8.202  1.00 44.80  ? 1337 TYR B CA    1 
ATOM   4620 C  C     . TYR B 1 120 ? 0.992   -11.857 6.855  1.00 42.97  ? 1337 TYR B C     1 
ATOM   4621 O  O     . TYR B 1 120 ? 0.343   -12.878 6.589  1.00 50.09  ? 1337 TYR B O     1 
ATOM   4622 C  CB    . TYR B 1 120 ? 0.767   -11.019 9.190  1.00 35.81  ? 1337 TYR B CB    1 
ATOM   4623 C  CG    . TYR B 1 120 ? 1.054   -11.306 10.644 1.00 39.18  ? 1337 TYR B CG    1 
ATOM   4624 C  CD1   . TYR B 1 120 ? 2.300   -11.730 11.060 1.00 40.82  ? 1337 TYR B CD1   1 
ATOM   4625 C  CD2   . TYR B 1 120 ? 0.068   -11.117 11.605 1.00 43.21  ? 1337 TYR B CD2   1 
ATOM   4626 C  CE1   . TYR B 1 120 ? 2.557   -11.963 12.412 1.00 55.48  ? 1337 TYR B CE1   1 
ATOM   4627 C  CE2   . TYR B 1 120 ? 0.308   -11.344 12.940 1.00 49.23  ? 1337 TYR B CE2   1 
ATOM   4628 C  CZ    . TYR B 1 120 ? 1.552   -11.766 13.348 1.00 54.37  ? 1337 TYR B CZ    1 
ATOM   4629 O  OH    . TYR B 1 120 ? 1.780   -11.999 14.691 1.00 47.62  ? 1337 TYR B OH    1 
ATOM   4630 N  N     . ALA B 1 121 ? 1.030   -10.816 6.029  1.00 37.21  ? 1338 ALA B N     1 
ATOM   4631 C  CA    . ALA B 1 121 ? 0.461   -10.957 4.692  1.00 35.89  ? 1338 ALA B CA    1 
ATOM   4632 C  C     . ALA B 1 121 ? 1.205   -12.012 3.884  1.00 38.62  ? 1338 ALA B C     1 
ATOM   4633 O  O     . ALA B 1 121 ? 0.589   -12.720 3.079  1.00 44.17  ? 1338 ALA B O     1 
ATOM   4634 C  CB    . ALA B 1 121 ? 0.459   -9.617  3.961  1.00 35.72  ? 1338 ALA B CB    1 
ATOM   4635 N  N     . LYS B 1 122 ? 2.526   -12.122 4.084  1.00 43.06  ? 1339 LYS B N     1 
ATOM   4636 C  CA    . LYS B 1 122 ? 3.319   -13.121 3.357  1.00 48.10  ? 1339 LYS B CA    1 
ATOM   4637 C  C     . LYS B 1 122 ? 3.078   -14.538 3.864  1.00 50.96  ? 1339 LYS B C     1 
ATOM   4638 O  O     . LYS B 1 122 ? 3.177   -15.498 3.094  1.00 55.34  ? 1339 LYS B O     1 
ATOM   4639 C  CB    . LYS B 1 122 ? 4.814   -12.817 3.462  1.00 43.29  ? 1339 LYS B CB    1 
ATOM   4640 N  N     . TRP B 1 123 ? 2.794   -14.691 5.144  1.00 42.18  ? 1340 TRP B N     1 
ATOM   4641 C  CA    . TRP B 1 123 ? 2.726   -16.003 5.739  1.00 42.84  ? 1340 TRP B CA    1 
ATOM   4642 C  C     . TRP B 1 123 ? 1.349   -16.618 5.568  1.00 57.47  ? 1340 TRP B C     1 
ATOM   4643 O  O     . TRP B 1 123 ? 1.214   -17.849 5.573  1.00 60.30  ? 1340 TRP B O     1 
ATOM   4644 C  CB    . TRP B 1 123 ? 3.148   -15.912 7.208  1.00 31.99  ? 1340 TRP B CB    1 
ATOM   4645 C  CG    . TRP B 1 123 ? 4.645   -15.673 7.349  1.00 38.91  ? 1340 TRP B CG    1 
ATOM   4646 C  CD1   . TRP B 1 123 ? 5.623   -15.951 6.414  1.00 36.55  ? 1340 TRP B CD1   1 
ATOM   4647 C  CD2   . TRP B 1 123 ? 5.331   -15.104 8.477  1.00 43.48  ? 1340 TRP B CD2   1 
ATOM   4648 N  NE1   . TRP B 1 123 ? 6.872   -15.595 6.898  1.00 35.70  ? 1340 TRP B NE1   1 
ATOM   4649 C  CE2   . TRP B 1 123 ? 6.720   -15.068 8.155  1.00 43.08  ? 1340 TRP B CE2   1 
ATOM   4650 C  CE3   . TRP B 1 123 ? 4.911   -14.606 9.716  1.00 38.02  ? 1340 TRP B CE3   1 
ATOM   4651 C  CZ2   . TRP B 1 123 ? 7.677   -14.556 9.031  1.00 32.57  ? 1340 TRP B CZ2   1 
ATOM   4652 C  CZ3   . TRP B 1 123 ? 5.867   -14.101 10.588 1.00 38.51  ? 1340 TRP B CZ3   1 
ATOM   4653 C  CH2   . TRP B 1 123 ? 7.234   -14.089 10.243 1.00 37.71  ? 1340 TRP B CH2   1 
ATOM   4654 N  N     . ILE B 1 124 ? 0.328   -15.793 5.377  1.00 62.20  ? 1341 ILE B N     1 
ATOM   4655 C  CA    . ILE B 1 124 ? -1.027  -16.290 5.171  1.00 70.40  ? 1341 ILE B CA    1 
ATOM   4656 C  C     . ILE B 1 124 ? -1.222  -16.495 3.671  1.00 73.01  ? 1341 ILE B C     1 
ATOM   4657 O  O     . ILE B 1 124 ? -1.670  -15.609 2.945  1.00 78.12  ? 1341 ILE B O     1 
ATOM   4658 C  CB    . ILE B 1 124 ? -2.058  -15.357 5.789  1.00 62.97  ? 1341 ILE B CB    1 
ATOM   4659 C  CG1   . ILE B 1 124 ? -1.759  -15.250 7.295  1.00 61.28  ? 1341 ILE B CG1   1 
ATOM   4660 C  CG2   . ILE B 1 124 ? -3.473  -15.823 5.475  1.00 56.52  ? 1341 ILE B CG2   1 
ATOM   4661 C  CD1   . ILE B 1 124 ? -2.937  -14.948 8.155  1.00 63.45  ? 1341 ILE B CD1   1 
ATOM   4662 N  N     . GLN B 1 125 ? -0.901  -17.698 3.204  1.00 66.16  ? 1342 GLN B N     1 
ATOM   4663 C  CA    . GLN B 1 125 ? -1.167  -18.041 1.819  1.00 54.60  ? 1342 GLN B CA    1 
ATOM   4664 C  C     . GLN B 1 125 ? -2.579  -18.605 1.619  1.00 45.44  ? 1342 GLN B C     1 
ATOM   4665 O  O     . GLN B 1 125 ? -3.060  -18.640 0.481  1.00 38.51  ? 1342 GLN B O     1 
ATOM   4666 C  CB    . GLN B 1 125 ? -0.081  -19.005 1.311  1.00 37.09  ? 1342 GLN B CB    1 
ATOM   4667 N  N     . SER B 1 126 ? -3.242  -19.071 2.681  1.00 43.41  ? 1343 SER B N     1 
ATOM   4668 C  CA    . SER B 1 126 ? -4.575  -19.667 2.582  1.00 53.21  ? 1343 SER B CA    1 
ATOM   4669 C  C     . SER B 1 126 ? -5.290  -19.486 3.911  1.00 58.93  ? 1343 SER B C     1 
ATOM   4670 O  O     . SER B 1 126 ? -4.678  -19.128 4.917  1.00 52.80  ? 1343 SER B O     1 
ATOM   4671 C  CB    . SER B 1 126 ? -4.534  -21.163 2.196  1.00 51.13  ? 1343 SER B CB    1 
ATOM   4672 O  OG    . SER B 1 126 ? -3.676  -21.929 3.040  1.00 47.09  ? 1343 SER B OG    1 
ATOM   4673 N  N     . TYR B 1 127 ? -6.587  -19.807 3.924  1.00 76.77  ? 1344 TYR B N     1 
ATOM   4674 C  CA    . TYR B 1 127 ? -7.302  -19.896 5.195  1.00 85.88  ? 1344 TYR B CA    1 
ATOM   4675 C  C     . TYR B 1 127 ? -6.646  -20.904 6.135  1.00 88.62  ? 1344 TYR B C     1 
ATOM   4676 O  O     . TYR B 1 127 ? -6.736  -20.766 7.360  1.00 96.26  ? 1344 TYR B O     1 
ATOM   4677 C  CB    . TYR B 1 127 ? -8.763  -20.291 4.955  1.00 95.70  ? 1344 TYR B CB    1 
ATOM   4678 C  CG    . TYR B 1 127 ? -8.948  -21.715 4.422  1.00 111.33 ? 1344 TYR B CG    1 
ATOM   4679 C  CD1   . TYR B 1 127 ? -9.280  -22.770 5.279  1.00 113.36 ? 1344 TYR B CD1   1 
ATOM   4680 C  CD2   . TYR B 1 127 ? -8.803  -22.005 3.056  1.00 113.12 ? 1344 TYR B CD2   1 
ATOM   4681 C  CE1   . TYR B 1 127 ? -9.456  -24.066 4.797  1.00 109.56 ? 1344 TYR B CE1   1 
ATOM   4682 C  CE2   . TYR B 1 127 ? -8.974  -23.305 2.572  1.00 106.55 ? 1344 TYR B CE2   1 
ATOM   4683 C  CZ    . TYR B 1 127 ? -9.301  -24.321 3.452  1.00 106.65 ? 1344 TYR B CZ    1 
ATOM   4684 O  OH    . TYR B 1 127 ? -9.473  -25.605 3.003  1.00 108.26 ? 1344 TYR B OH    1 
ATOM   4685 N  N     . ARG B 1 128 ? -5.960  -21.904 5.586  1.00 79.54  ? 1345 ARG B N     1 
ATOM   4686 C  CA    . ARG B 1 128 ? -5.356  -22.928 6.426  1.00 81.55  ? 1345 ARG B CA    1 
ATOM   4687 C  C     . ARG B 1 128 ? -4.241  -22.382 7.323  1.00 73.93  ? 1345 ARG B C     1 
ATOM   4688 O  O     . ARG B 1 128 ? -3.866  -23.052 8.293  1.00 69.58  ? 1345 ARG B O     1 
ATOM   4689 C  CB    . ARG B 1 128 ? -4.831  -24.070 5.549  1.00 86.41  ? 1345 ARG B CB    1 
ATOM   4690 N  N     . ASP B 1 129 ? -3.668  -21.217 7.008  1.00 61.44  ? 1346 ASP B N     1 
ATOM   4691 C  CA    . ASP B 1 129 ? -2.577  -20.707 7.829  1.00 58.33  ? 1346 ASP B CA    1 
ATOM   4692 C  C     . ASP B 1 129 ? -3.036  -19.951 9.079  1.00 57.34  ? 1346 ASP B C     1 
ATOM   4693 O  O     . ASP B 1 129 ? -2.182  -19.550 9.880  1.00 55.71  ? 1346 ASP B O     1 
ATOM   4694 C  CB    . ASP B 1 129 ? -1.674  -19.810 6.983  1.00 58.31  ? 1346 ASP B CB    1 
ATOM   4695 C  CG    . ASP B 1 129 ? -1.229  -20.481 5.685  1.00 67.01  ? 1346 ASP B CG    1 
ATOM   4696 O  OD1   . ASP B 1 129 ? -0.439  -21.458 5.719  1.00 65.52  ? 1346 ASP B OD1   1 
ATOM   4697 O  OD2   . ASP B 1 129 ? -1.690  -20.037 4.617  1.00 66.15  ? 1346 ASP B OD2   1 
ATOM   4698 N  N     . LEU B 1 130 ? -4.346  -19.782 9.295  1.00 51.73  ? 1347 LEU B N     1 
ATOM   4699 C  CA    . LEU B 1 130 ? -4.799  -18.987 10.432 1.00 44.32  ? 1347 LEU B CA    1 
ATOM   4700 C  C     . LEU B 1 130 ? -5.199  -19.904 11.561 1.00 39.35  ? 1347 LEU B C     1 
ATOM   4701 O  O     . LEU B 1 130 ? -5.885  -20.885 11.319 1.00 55.69  ? 1347 LEU B O     1 
ATOM   4702 C  CB    . LEU B 1 130 ? -6.007  -18.121 10.054 1.00 51.19  ? 1347 LEU B CB    1 
ATOM   4703 C  CG    . LEU B 1 130 ? -5.831  -16.782 9.319  1.00 52.81  ? 1347 LEU B CG    1 
ATOM   4704 C  CD1   . LEU B 1 130 ? -7.022  -16.525 8.403  1.00 47.43  ? 1347 LEU B CD1   1 
ATOM   4705 C  CD2   . LEU B 1 130 ? -5.640  -15.617 10.307 1.00 52.37  ? 1347 LEU B CD2   1 
ATOM   4706 N  N     . PRO B 1 131 ? -4.934  -19.593 12.835 1.00 45.25  ? 1348 PRO B N     1 
ATOM   4707 C  CA    . PRO B 1 131 ? -4.438  -18.311 13.380 1.00 51.79  ? 1348 PRO B CA    1 
ATOM   4708 C  C     . PRO B 1 131 ? -2.935  -18.094 13.461 1.00 57.24  ? 1348 PRO B C     1 
ATOM   4709 O  O     . PRO B 1 131 ? -2.136  -19.023 13.604 1.00 65.97  ? 1348 PRO B O     1 
ATOM   4710 C  CB    . PRO B 1 131 ? -5.004  -18.296 14.809 1.00 53.20  ? 1348 PRO B CB    1 
ATOM   4711 C  CG    . PRO B 1 131 ? -5.156  -19.785 15.181 1.00 50.97  ? 1348 PRO B CG    1 
ATOM   4712 C  CD    . PRO B 1 131 ? -5.420  -20.517 13.886 1.00 41.97  ? 1348 PRO B CD    1 
ATOM   4713 N  N     . ILE B 1 132 ? -2.560  -16.819 13.400 1.00 55.53  ? 1349 ILE B N     1 
ATOM   4714 C  CA    . ILE B 1 132 ? -1.198  -16.390 13.678 1.00 42.93  ? 1349 ILE B CA    1 
ATOM   4715 C  C     . ILE B 1 132 ? -1.160  -15.795 15.068 1.00 36.63  ? 1349 ILE B C     1 
ATOM   4716 O  O     . ILE B 1 132 ? -1.977  -14.931 15.392 1.00 45.70  ? 1349 ILE B O     1 
ATOM   4717 C  CB    . ILE B 1 132 ? -0.712  -15.376 12.647 1.00 30.60  ? 1349 ILE B CB    1 
ATOM   4718 C  CG1   . ILE B 1 132 ? -0.903  -15.962 11.264 1.00 31.30  ? 1349 ILE B CG1   1 
ATOM   4719 C  CG2   . ILE B 1 132 ? 0.754   -15.100 12.903 1.00 33.53  ? 1349 ILE B CG2   1 
ATOM   4720 C  CD1   . ILE B 1 132 ? -0.246  -17.319 11.128 1.00 46.73  ? 1349 ILE B CD1   1 
ATOM   4721 N  N     . ARG B 1 133 ? -0.273  -16.303 15.915 1.00 29.71  ? 1350 ARG B N     1 
ATOM   4722 C  CA    . ARG B 1 133 ? -0.193  -15.832 17.300 1.00 30.71  ? 1350 ARG B CA    1 
ATOM   4723 C  C     . ARG B 1 133 ? 1.277   -15.755 17.676 1.00 37.59  ? 1350 ARG B C     1 
ATOM   4724 O  O     . ARG B 1 133 ? 1.858   -16.727 18.168 1.00 44.89  ? 1350 ARG B O     1 
ATOM   4725 C  CB    . ARG B 1 133 ? -0.964  -16.725 18.252 1.00 29.55  ? 1350 ARG B CB    1 
ATOM   4726 C  CG    . ARG B 1 133 ? -2.458  -16.562 18.128 1.00 41.37  ? 1350 ARG B CG    1 
ATOM   4727 C  CD    . ARG B 1 133 ? -3.150  -17.642 18.889 1.00 59.39  ? 1350 ARG B CD    1 
ATOM   4728 N  NE    . ARG B 1 133 ? -3.966  -17.141 19.986 1.00 66.85  ? 1350 ARG B NE    1 
ATOM   4729 C  CZ    . ARG B 1 133 ? -4.363  -17.899 21.001 1.00 81.77  ? 1350 ARG B CZ    1 
ATOM   4730 N  NH1   . ARG B 1 133 ? -3.996  -19.187 21.059 1.00 88.99  ? 1350 ARG B NH1   1 
ATOM   4731 N  NH2   . ARG B 1 133 ? -5.133  -17.377 21.948 1.00 79.13  ? 1350 ARG B NH2   1 
ATOM   4732 N  N     . LEU B 1 134 ? 1.870   -14.590 17.477 1.00 39.93  ? 1351 LEU B N     1 
ATOM   4733 C  CA    . LEU B 1 134 ? 3.293   -14.458 17.712 1.00 46.14  ? 1351 LEU B CA    1 
ATOM   4734 C  C     . LEU B 1 134 ? 3.510   -13.474 18.836 1.00 45.74  ? 1351 LEU B C     1 
ATOM   4735 O  O     . LEU B 1 134 ? 2.707   -12.557 19.054 1.00 54.74  ? 1351 LEU B O     1 
ATOM   4736 C  CB    . LEU B 1 134 ? 4.045   -14.005 16.472 1.00 39.58  ? 1351 LEU B CB    1 
ATOM   4737 C  CG    . LEU B 1 134 ? 3.975   -15.036 15.342 1.00 43.21  ? 1351 LEU B CG    1 
ATOM   4738 C  CD1   . LEU B 1 134 ? 4.618   -14.473 14.080 1.00 43.63  ? 1351 LEU B CD1   1 
ATOM   4739 C  CD2   . LEU B 1 134 ? 4.598   -16.360 15.740 1.00 28.51  ? 1351 LEU B CD2   1 
ATOM   4740 N  N     . ASN B 1 135 ? 4.587   -13.692 19.567 1.00 27.12  ? 1352 ASN B N     1 
ATOM   4741 C  CA    . ASN B 1 135 ? 4.937   -12.765 20.619 1.00 32.99  ? 1352 ASN B CA    1 
ATOM   4742 C  C     . ASN B 1 135 ? 6.434   -12.511 20.568 1.00 39.22  ? 1352 ASN B C     1 
ATOM   4743 O  O     . ASN B 1 135 ? 7.229   -13.405 20.273 1.00 28.94  ? 1352 ASN B O     1 
ATOM   4744 C  CB    . ASN B 1 135 ? 4.510   -13.269 21.982 1.00 35.62  ? 1352 ASN B CB    1 
ATOM   4745 C  CG    . ASN B 1 135 ? 5.209   -12.544 23.109 1.00 48.57  ? 1352 ASN B CG    1 
ATOM   4746 O  OD1   . ASN B 1 135 ? 4.868   -11.401 23.442 1.00 54.83  ? 1352 ASN B OD1   1 
ATOM   4747 N  ND2   . ASN B 1 135 ? 6.206   -13.197 23.699 1.00 46.97  ? 1352 ASN B ND2   1 
ATOM   4748 N  N     . GLN B 1 136 ? 6.810   -11.277 20.884 1.00 44.07  ? 1353 GLN B N     1 
ATOM   4749 C  CA    . GLN B 1 136 ? 8.207   -10.899 20.974 1.00 51.08  ? 1353 GLN B CA    1 
ATOM   4750 C  C     . GLN B 1 136 ? 8.488   -10.341 22.353 1.00 49.29  ? 1353 GLN B C     1 
ATOM   4751 O  O     . GLN B 1 136 ? 7.765   -9.459  22.829 1.00 55.69  ? 1353 GLN B O     1 
ATOM   4752 C  CB    . GLN B 1 136 ? 8.559   -9.839  19.926 1.00 43.59  ? 1353 GLN B CB    1 
ATOM   4753 C  CG    . GLN B 1 136 ? 8.684   -10.351 18.507 1.00 43.55  ? 1353 GLN B CG    1 
ATOM   4754 C  CD    . GLN B 1 136 ? 9.379   -9.334  17.593 1.00 47.69  ? 1353 GLN B CD    1 
ATOM   4755 O  OE1   . GLN B 1 136 ? 10.596  -9.152  17.680 1.00 47.77  ? 1353 GLN B OE1   1 
ATOM   4756 N  NE2   . GLN B 1 136 ? 8.604   -8.662  16.715 1.00 26.62  ? 1353 GLN B NE2   1 
ATOM   4757 N  N     . TRP B 1 137 ? 9.509   -10.895 23.000 1.00 43.63  ? 1354 TRP B N     1 
ATOM   4758 C  CA    . TRP B 1 137 ? 10.156  -10.254 24.135 1.00 45.62  ? 1354 TRP B CA    1 
ATOM   4759 C  C     . TRP B 1 137 ? 11.325  -9.477  23.562 1.00 44.83  ? 1354 TRP B C     1 
ATOM   4760 O  O     . TRP B 1 137 ? 12.318  -10.075 23.143 1.00 49.85  ? 1354 TRP B O     1 
ATOM   4761 C  CB    . TRP B 1 137 ? 10.627  -11.274 25.166 1.00 36.07  ? 1354 TRP B CB    1 
ATOM   4762 C  CG    . TRP B 1 137 ? 9.536   -12.056 25.742 1.00 33.82  ? 1354 TRP B CG    1 
ATOM   4763 C  CD1   . TRP B 1 137 ? 9.101   -13.258 25.316 1.00 43.68  ? 1354 TRP B CD1   1 
ATOM   4764 C  CD2   . TRP B 1 137 ? 8.708   -11.694 26.854 1.00 43.71  ? 1354 TRP B CD2   1 
ATOM   4765 N  NE1   . TRP B 1 137 ? 8.049   -13.685 26.089 1.00 60.58  ? 1354 TRP B NE1   1 
ATOM   4766 C  CE2   . TRP B 1 137 ? 7.786   -12.739 27.042 1.00 55.07  ? 1354 TRP B CE2   1 
ATOM   4767 C  CE3   . TRP B 1 137 ? 8.650   -10.587 27.697 1.00 42.99  ? 1354 TRP B CE3   1 
ATOM   4768 C  CZ2   . TRP B 1 137 ? 6.827   -12.721 28.045 1.00 53.61  ? 1354 TRP B CZ2   1 
ATOM   4769 C  CZ3   . TRP B 1 137 ? 7.704   -10.570 28.693 1.00 54.22  ? 1354 TRP B CZ3   1 
ATOM   4770 C  CH2   . TRP B 1 137 ? 6.802   -11.637 28.861 1.00 59.29  ? 1354 TRP B CH2   1 
ATOM   4771 N  N     . ASN B 1 138 ? 11.221  -8.152  23.552 1.00 47.15  ? 1355 ASN B N     1 
ATOM   4772 C  CA    . ASN B 1 138 ? 12.287  -7.355  22.965 1.00 49.54  ? 1355 ASN B CA    1 
ATOM   4773 C  C     . ASN B 1 138 ? 12.362  -6.017  23.672 1.00 49.91  ? 1355 ASN B C     1 
ATOM   4774 O  O     . ASN B 1 138 ? 11.703  -5.787  24.686 1.00 54.21  ? 1355 ASN B O     1 
ATOM   4775 C  CB    . ASN B 1 138 ? 12.133  -7.160  21.443 1.00 39.81  ? 1355 ASN B CB    1 
ATOM   4776 C  CG    . ASN B 1 138 ? 10.821  -6.537  21.048 1.00 44.47  ? 1355 ASN B CG    1 
ATOM   4777 O  OD1   . ASN B 1 138 ? 10.168  -5.920  21.866 1.00 56.06  ? 1355 ASN B OD1   1 
ATOM   4778 N  ND2   . ASN B 1 138 ? 10.438  -6.673  19.770 1.00 39.51  ? 1355 ASN B ND2   1 
ATOM   4779 N  N     . ASN B 1 139 ? 13.271  -5.185  23.181 1.00 44.80  ? 1356 ASN B N     1 
ATOM   4780 C  CA    . ASN B 1 139 ? 13.466  -3.827  23.650 1.00 43.51  ? 1356 ASN B CA    1 
ATOM   4781 C  C     . ASN B 1 139 ? 13.087  -2.887  22.521 1.00 46.55  ? 1356 ASN B C     1 
ATOM   4782 O  O     . ASN B 1 139 ? 13.384  -3.156  21.354 1.00 57.87  ? 1356 ASN B O     1 
ATOM   4783 C  CB    . ASN B 1 139 ? 14.917  -3.584  24.066 1.00 43.50  ? 1356 ASN B CB    1 
ATOM   4784 C  CG    . ASN B 1 139 ? 15.905  -3.800  22.925 1.00 43.27  ? 1356 ASN B CG    1 
ATOM   4785 O  OD1   . ASN B 1 139 ? 15.699  -4.634  22.037 1.00 42.09  ? 1356 ASN B OD1   1 
ATOM   4786 N  ND2   . ASN B 1 139 ? 16.985  -3.032  22.943 1.00 41.78  ? 1356 ASN B ND2   1 
ATOM   4787 N  N     . VAL B 1 140 ? 12.464  -1.772  22.868 1.00 44.14  ? 1357 VAL B N     1 
ATOM   4788 C  CA    . VAL B 1 140 ? 12.037  -0.793  21.879 1.00 44.27  ? 1357 VAL B CA    1 
ATOM   4789 C  C     . VAL B 1 140 ? 12.426  0.585   22.378 1.00 45.44  ? 1357 VAL B C     1 
ATOM   4790 O  O     . VAL B 1 140 ? 12.568  0.836   23.583 1.00 50.38  ? 1357 VAL B O     1 
ATOM   4791 C  CB    . VAL B 1 140 ? 10.518  -0.851  21.600 1.00 40.30  ? 1357 VAL B CB    1 
ATOM   4792 C  CG1   . VAL B 1 140 ? 10.063  -2.277  21.373 1.00 26.08  ? 1357 VAL B CG1   1 
ATOM   4793 C  CG2   . VAL B 1 140 ? 9.763   -0.241  22.745 1.00 43.43  ? 1357 VAL B CG2   1 
ATOM   4794 N  N     . VAL B 1 141 ? 12.611  1.486   21.436 1.00 34.75  ? 1358 VAL B N     1 
ATOM   4795 C  CA    . VAL B 1 141 ? 13.090  2.817   21.744 1.00 38.37  ? 1358 VAL B CA    1 
ATOM   4796 C  C     . VAL B 1 141 ? 12.090  3.814   21.217 1.00 30.71  ? 1358 VAL B C     1 
ATOM   4797 O  O     . VAL B 1 141 ? 11.827  3.872   20.008 1.00 34.70  ? 1358 VAL B O     1 
ATOM   4798 C  CB    . VAL B 1 141 ? 14.490  3.076   21.169 1.00 48.56  ? 1358 VAL B CB    1 
ATOM   4799 C  CG1   . VAL B 1 141 ? 15.094  4.267   21.825 1.00 45.08  ? 1358 VAL B CG1   1 
ATOM   4800 C  CG2   . VAL B 1 141 ? 15.373  1.885   21.424 1.00 39.79  ? 1358 VAL B CG2   1 
ATOM   4801 N  N     . ARG B 1 142 ? 11.634  4.676   22.106 1.00 30.27  ? 1359 ARG B N     1 
ATOM   4802 C  CA    . ARG B 1 142 ? 10.772  5.793   21.786 1.00 36.77  ? 1359 ARG B CA    1 
ATOM   4803 C  C     . ARG B 1 142 ? 11.449  7.030   22.352 1.00 40.29  ? 1359 ARG B C     1 
ATOM   4804 O  O     . ARG B 1 142 ? 11.790  7.067   23.538 1.00 39.53  ? 1359 ARG B O     1 
ATOM   4805 C  CB    . ARG B 1 142 ? 9.387   5.582   22.401 1.00 35.18  ? 1359 ARG B CB    1 
ATOM   4806 C  CG    . ARG B 1 142 ? 8.616   4.405   21.829 1.00 32.01  ? 1359 ARG B CG    1 
ATOM   4807 C  CD    . ARG B 1 142 ? 7.248   4.282   22.475 1.00 31.76  ? 1359 ARG B CD    1 
ATOM   4808 N  NE    . ARG B 1 142 ? 6.525   3.144   21.936 1.00 31.74  ? 1359 ARG B NE    1 
ATOM   4809 C  CZ    . ARG B 1 142 ? 5.396   2.655   22.429 1.00 42.17  ? 1359 ARG B CZ    1 
ATOM   4810 N  NH1   . ARG B 1 142 ? 4.820   3.197   23.491 1.00 59.57  ? 1359 ARG B NH1   1 
ATOM   4811 N  NH2   . ARG B 1 142 ? 4.838   1.614   21.840 1.00 51.47  ? 1359 ARG B NH2   1 
ATOM   4812 N  N     . TRP B 1 143 ? 11.701  8.017   21.503 1.00 49.21  ? 1360 TRP B N     1 
ATOM   4813 C  CA    . TRP B 1 143 ? 12.379  9.215   21.989 1.00 57.46  ? 1360 TRP B CA    1 
ATOM   4814 C  C     . TRP B 1 143 ? 11.346  10.086  22.684 1.00 56.23  ? 1360 TRP B C     1 
ATOM   4815 O  O     . TRP B 1 143 ? 10.901  11.109  22.170 1.00 46.16  ? 1360 TRP B O     1 
ATOM   4816 C  CB    . TRP B 1 143 ? 13.097  9.968   20.883 1.00 58.00  ? 1360 TRP B CB    1 
ATOM   4817 C  CG    . TRP B 1 143 ? 14.225  10.690  21.480 1.00 60.15  ? 1360 TRP B CG    1 
ATOM   4818 C  CD1   . TRP B 1 143 ? 14.366  12.037  21.594 1.00 55.72  ? 1360 TRP B CD1   1 
ATOM   4819 C  CD2   . TRP B 1 143 ? 15.356  10.106  22.147 1.00 69.56  ? 1360 TRP B CD2   1 
ATOM   4820 N  NE1   . TRP B 1 143 ? 15.538  12.337  22.254 1.00 56.16  ? 1360 TRP B NE1   1 
ATOM   4821 C  CE2   . TRP B 1 143 ? 16.164  11.171  22.607 1.00 64.18  ? 1360 TRP B CE2   1 
ATOM   4822 C  CE3   . TRP B 1 143 ? 15.776  8.783   22.380 1.00 70.37  ? 1360 TRP B CE3   1 
ATOM   4823 C  CZ2   . TRP B 1 143 ? 17.368  10.962  23.286 1.00 65.12  ? 1360 TRP B CZ2   1 
ATOM   4824 C  CZ3   . TRP B 1 143 ? 16.980  8.571   23.057 1.00 65.33  ? 1360 TRP B CZ3   1 
ATOM   4825 C  CH2   . TRP B 1 143 ? 17.760  9.658   23.499 1.00 66.03  ? 1360 TRP B CH2   1 
ATOM   4826 N  N     . GLU B 1 144 ? 10.966  9.654   23.886 1.00 64.49  ? 1361 GLU B N     1 
ATOM   4827 C  CA    . GLU B 1 144 ? 9.850   10.267  24.580 1.00 64.56  ? 1361 GLU B CA    1 
ATOM   4828 C  C     . GLU B 1 144 ? 10.131  11.740  24.771 1.00 60.69  ? 1361 GLU B C     1 
ATOM   4829 O  O     . GLU B 1 144 ? 11.242  12.120  25.156 1.00 53.14  ? 1361 GLU B O     1 
ATOM   4830 C  CB    . GLU B 1 144 ? 9.645   9.598   25.946 1.00 58.90  ? 1361 GLU B CB    1 
ATOM   4831 C  CG    . GLU B 1 144 ? 9.135   8.186   25.893 1.00 57.16  ? 1361 GLU B CG    1 
ATOM   4832 C  CD    . GLU B 1 144 ? 7.625   8.125   25.789 1.00 73.55  ? 1361 GLU B CD    1 
ATOM   4833 O  OE1   . GLU B 1 144 ? 7.060   7.002   25.709 1.00 81.75  ? 1361 GLU B OE1   1 
ATOM   4834 O  OE2   . GLU B 1 144 ? 6.999   9.207   25.785 1.00 80.39  ? 1361 GLU B OE2   1 
ATOM   4835 N  N     . PHE B 1 145 ? 9.131   12.573  24.464 1.00 73.17  ? 1362 PHE B N     1 
ATOM   4836 C  CA    . PHE B 1 145 ? 9.238   13.998  24.768 1.00 73.28  ? 1362 PHE B CA    1 
ATOM   4837 C  C     . PHE B 1 145 ? 8.766   14.314  26.176 1.00 64.03  ? 1362 PHE B C     1 
ATOM   4838 O  O     . PHE B 1 145 ? 9.299   15.230  26.810 1.00 62.41  ? 1362 PHE B O     1 
ATOM   4839 C  CB    . PHE B 1 145 ? 8.459   14.851  23.756 1.00 66.10  ? 1362 PHE B CB    1 
ATOM   4840 C  CG    . PHE B 1 145 ? 7.053   14.370  23.460 1.00 69.67  ? 1362 PHE B CG    1 
ATOM   4841 C  CD1   . PHE B 1 145 ? 5.955   15.007  24.018 1.00 65.49  ? 1362 PHE B CD1   1 
ATOM   4842 C  CD2   . PHE B 1 145 ? 6.828   13.315  22.579 1.00 72.75  ? 1362 PHE B CD2   1 
ATOM   4843 C  CE1   . PHE B 1 145 ? 4.662   14.580  23.728 1.00 68.85  ? 1362 PHE B CE1   1 
ATOM   4844 C  CE2   . PHE B 1 145 ? 5.539   12.888  22.285 1.00 72.77  ? 1362 PHE B CE2   1 
ATOM   4845 C  CZ    . PHE B 1 145 ? 4.454   13.521  22.860 1.00 69.62  ? 1362 PHE B CZ    1 
ATOM   4846 N  N     . LYS B 1 146 ? 7.834   13.525  26.701 1.00 50.02  ? 1363 LYS B N     1 
ATOM   4847 C  CA    . LYS B 1 146 ? 7.382   13.735  28.060 1.00 43.29  ? 1363 LYS B CA    1 
ATOM   4848 C  C     . LYS B 1 146 ? 8.535   13.418  29.011 1.00 48.68  ? 1363 LYS B C     1 
ATOM   4849 O  O     . LYS B 1 146 ? 9.416   12.601  28.705 1.00 42.96  ? 1363 LYS B O     1 
ATOM   4850 C  CB    . LYS B 1 146 ? 6.161   12.858  28.356 1.00 40.22  ? 1363 LYS B CB    1 
ATOM   4851 C  CG    . LYS B 1 146 ? 5.336   12.483  27.124 1.00 36.23  ? 1363 LYS B CG    1 
ATOM   4852 C  CD    . LYS B 1 146 ? 3.929   11.982  27.500 1.00 45.67  ? 1363 LYS B CD    1 
ATOM   4853 C  CE    . LYS B 1 146 ? 3.397   10.944  26.484 1.00 53.05  ? 1363 LYS B CE    1 
ATOM   4854 N  NZ    . LYS B 1 146 ? 2.219   10.140  26.968 1.00 57.33  ? 1363 LYS B NZ    1 
ATOM   4855 N  N     . HIS B 1 147 ? 8.524   13.979  30.194 1.00 47.48  ? 1364 HIS B N     1 
ATOM   4856 C  CA    . HIS B 1 147 ? 9.576   13.761  31.150 1.00 41.23  ? 1364 HIS B CA    1 
ATOM   4857 C  C     . HIS B 1 147 ? 9.776   12.349  31.440 1.00 39.57  ? 1364 HIS B C     1 
ATOM   4858 O  O     . HIS B 1 147 ? 8.856   11.697  31.780 1.00 40.43  ? 1364 HIS B O     1 
ATOM   4859 C  CB    . HIS B 1 147 ? 9.213   14.394  32.441 1.00 43.74  ? 1364 HIS B CB    1 
ATOM   4860 C  CG    . HIS B 1 147 ? 9.358   15.862  32.444 1.00 67.51  ? 1364 HIS B CG    1 
ATOM   4861 N  ND1   . HIS B 1 147 ? 9.331   16.609  31.295 1.00 74.17  ? 1364 HIS B ND1   1 
ATOM   4862 C  CD2   . HIS B 1 147 ? 9.510   16.735  33.454 1.00 70.76  ? 1364 HIS B CD2   1 
ATOM   4863 C  CE1   . HIS B 1 147 ? 9.468   17.881  31.595 1.00 68.74  ? 1364 HIS B CE1   1 
ATOM   4864 N  NE2   . HIS B 1 147 ? 9.575   17.983  32.901 1.00 71.04  ? 1364 HIS B NE2   1 
ATOM   4865 N  N     . PRO B 1 148 ? 10.979  11.859  31.195 1.00 46.59  ? 1365 PRO B N     1 
ATOM   4866 C  CA    . PRO B 1 148 ? 11.250  10.443  31.464 1.00 52.00  ? 1365 PRO B CA    1 
ATOM   4867 C  C     . PRO B 1 148 ? 11.468  10.164  32.944 1.00 58.50  ? 1365 PRO B C     1 
ATOM   4868 O  O     . PRO B 1 148 ? 12.130  10.930  33.649 1.00 63.02  ? 1365 PRO B O     1 
ATOM   4869 C  CB    . PRO B 1 148 ? 12.538  10.187  30.675 1.00 42.39  ? 1365 PRO B CB    1 
ATOM   4870 C  CG    . PRO B 1 148 ? 12.644  11.359  29.706 1.00 33.84  ? 1365 PRO B CG    1 
ATOM   4871 C  CD    . PRO B 1 148 ? 12.035  12.487  30.389 1.00 40.95  ? 1365 PRO B CD    1 
ATOM   4872 N  N     . GLN B 1 149 ? 10.954  9.017   33.397 1.00 57.15  ? 1366 GLN B N     1 
ATOM   4873 C  CA    . GLN B 1 149 ? 11.070  8.556   34.771 1.00 60.10  ? 1366 GLN B CA    1 
ATOM   4874 C  C     . GLN B 1 149 ? 11.592  7.131   34.773 1.00 54.78  ? 1366 GLN B C     1 
ATOM   4875 O  O     . GLN B 1 149 ? 11.179  6.316   33.944 1.00 52.49  ? 1366 GLN B O     1 
ATOM   4876 C  CB    . GLN B 1 149 ? 9.718   8.601   35.506 1.00 75.18  ? 1366 GLN B CB    1 
ATOM   4877 C  CG    . GLN B 1 149 ? 9.082   9.993   35.663 1.00 80.29  ? 1366 GLN B CG    1 
ATOM   4878 C  CD    . GLN B 1 149 ? 9.342   10.618  37.027 1.00 84.73  ? 1366 GLN B CD    1 
ATOM   4879 O  OE1   . GLN B 1 149 ? 8.799   10.169  38.037 1.00 93.34  ? 1366 GLN B OE1   1 
ATOM   4880 N  NE2   . GLN B 1 149 ? 10.172  11.661  37.059 1.00 77.61  ? 1366 GLN B NE2   1 
ATOM   4881 N  N     . PRO B 1 150 ? 12.442  6.788   35.731 1.00 61.39  ? 1367 PRO B N     1 
ATOM   4882 C  CA    . PRO B 1 150 ? 13.293  5.602   35.578 1.00 61.63  ? 1367 PRO B CA    1 
ATOM   4883 C  C     . PRO B 1 150 ? 12.586  4.303   35.290 1.00 66.22  ? 1367 PRO B C     1 
ATOM   4884 O  O     . PRO B 1 150 ? 13.170  3.481   34.581 1.00 98.43  ? 1367 PRO B O     1 
ATOM   4885 C  CB    . PRO B 1 150 ? 14.051  5.560   36.900 1.00 60.24  ? 1367 PRO B CB    1 
ATOM   4886 C  CG    . PRO B 1 150 ? 14.278  7.039   37.165 1.00 70.46  ? 1367 PRO B CG    1 
ATOM   4887 C  CD    . PRO B 1 150 ? 13.143  7.818   36.496 1.00 67.65  ? 1367 PRO B CD    1 
ATOM   4888 N  N     . PHE B 1 151 ? 11.391  4.034   35.786 1.00 35.91  ? 1368 PHE B N     1 
ATOM   4889 C  CA    . PHE B 1 151 ? 10.773  2.835   35.216 1.00 27.93  ? 1368 PHE B CA    1 
ATOM   4890 C  C     . PHE B 1 151 ? 9.505   3.132   34.456 1.00 60.73  ? 1368 PHE B C     1 
ATOM   4891 O  O     . PHE B 1 151 ? 9.145   2.366   33.558 1.00 27.53  ? 1368 PHE B O     1 
ATOM   4892 C  CB    . PHE B 1 151 ? 10.482  1.795   36.287 1.00 33.69  ? 1368 PHE B CB    1 
ATOM   4893 C  CG    . PHE B 1 151 ? 11.692  1.102   36.775 1.00 46.02  ? 1368 PHE B CG    1 
ATOM   4894 C  CD1   . PHE B 1 151 ? 12.068  -0.126  36.251 1.00 51.46  ? 1368 PHE B CD1   1 
ATOM   4895 C  CD2   . PHE B 1 151 ? 12.474  1.681   37.757 1.00 49.27  ? 1368 PHE B CD2   1 
ATOM   4896 C  CE1   . PHE B 1 151 ? 13.208  -0.775  36.712 1.00 53.89  ? 1368 PHE B CE1   1 
ATOM   4897 C  CE2   . PHE B 1 151 ? 13.615  1.049   38.220 1.00 51.51  ? 1368 PHE B CE2   1 
ATOM   4898 C  CZ    . PHE B 1 151 ? 13.980  -0.183  37.696 1.00 55.66  ? 1368 PHE B CZ    1 
ATOM   4899 N  N     . LEU B 1 152 ? 8.845   4.236   34.807 1.00 65.99  ? 1369 LEU B N     1 
ATOM   4900 C  CA    . LEU B 1 152 ? 7.561   4.613   34.239 1.00 61.96  ? 1369 LEU B CA    1 
ATOM   4901 C  C     . LEU B 1 152 ? 7.677   4.991   32.768 1.00 55.46  ? 1369 LEU B C     1 
ATOM   4902 O  O     . LEU B 1 152 ? 6.834   4.598   31.955 1.00 69.93  ? 1369 LEU B O     1 
ATOM   4903 C  CB    . LEU B 1 152 ? 6.989   5.763   35.068 1.00 57.67  ? 1369 LEU B CB    1 
ATOM   4904 C  CG    . LEU B 1 152 ? 6.994   5.538   36.591 1.00 52.93  ? 1369 LEU B CG    1 
ATOM   4905 C  CD1   . LEU B 1 152 ? 6.154   6.531   37.349 1.00 38.55  ? 1369 LEU B CD1   1 
ATOM   4906 C  CD2   . LEU B 1 152 ? 6.515   4.139   36.934 1.00 65.31  ? 1369 LEU B CD2   1 
ATOM   4907 N  N     . ARG B 1 153 ? 8.693   5.768   32.405 1.00 39.71  ? 1370 ARG B N     1 
ATOM   4908 C  CA    . ARG B 1 153 ? 8.808   6.236   31.022 1.00 44.24  ? 1370 ARG B CA    1 
ATOM   4909 C  C     . ARG B 1 153 ? 10.289  6.378   30.711 1.00 41.62  ? 1370 ARG B C     1 
ATOM   4910 O  O     . ARG B 1 153 ? 10.877  7.430   30.958 1.00 53.51  ? 1370 ARG B O     1 
ATOM   4911 C  CB    . ARG B 1 153 ? 8.073   7.558   30.799 1.00 49.36  ? 1370 ARG B CB    1 
ATOM   4912 C  CG    . ARG B 1 153 ? 8.025   8.028   29.313 1.00 56.87  ? 1370 ARG B CG    1 
ATOM   4913 C  CD    . ARG B 1 153 ? 7.260   9.360   29.067 1.00 46.39  ? 1370 ARG B CD    1 
ATOM   4914 N  NE    . ARG B 1 153 ? 5.978   9.359   29.753 1.00 48.29  ? 1370 ARG B NE    1 
ATOM   4915 C  CZ    . ARG B 1 153 ? 4.883   8.785   29.262 1.00 45.05  ? 1370 ARG B CZ    1 
ATOM   4916 N  NH1   . ARG B 1 153 ? 3.750   8.806   29.944 1.00 46.78  ? 1370 ARG B NH1   1 
ATOM   4917 N  NH2   . ARG B 1 153 ? 4.912   8.201   28.077 1.00 37.44  ? 1370 ARG B NH2   1 
ATOM   4918 N  N     . THR B 1 154 ? 10.851  5.351   30.105 1.00 27.94  ? 1371 THR B N     1 
ATOM   4919 C  CA    . THR B 1 154 ? 12.233  5.323   29.688 1.00 27.88  ? 1371 THR B CA    1 
ATOM   4920 C  C     . THR B 1 154 ? 12.285  5.306   28.170 1.00 34.95  ? 1371 THR B C     1 
ATOM   4921 O  O     . THR B 1 154 ? 11.373  4.810   27.509 1.00 36.10  ? 1371 THR B O     1 
ATOM   4922 C  CB    . THR B 1 154 ? 12.932  4.101   30.277 1.00 31.41  ? 1371 THR B CB    1 
ATOM   4923 O  OG1   . THR B 1 154 ? 12.155  2.911   30.022 1.00 39.26  ? 1371 THR B OG1   1 
ATOM   4924 C  CG2   . THR B 1 154 ? 13.044  4.286   31.769 1.00 27.72  ? 1371 THR B CG2   1 
ATOM   4925 N  N     . ARG B 1 155 ? 13.362  5.865   27.618 1.00 40.10  ? 1372 ARG B N     1 
ATOM   4926 C  CA    . ARG B 1 155 ? 13.425  6.032   26.175 1.00 33.65  ? 1372 ARG B CA    1 
ATOM   4927 C  C     . ARG B 1 155 ? 13.687  4.711   25.488 1.00 34.65  ? 1372 ARG B C     1 
ATOM   4928 O  O     . ARG B 1 155 ? 13.152  4.451   24.407 1.00 29.96  ? 1372 ARG B O     1 
ATOM   4929 C  CB    . ARG B 1 155 ? 14.495  7.066   25.816 1.00 45.94  ? 1372 ARG B CB    1 
ATOM   4930 C  CG    . ARG B 1 155 ? 13.990  8.499   25.951 1.00 49.86  ? 1372 ARG B CG    1 
ATOM   4931 C  CD    . ARG B 1 155 ? 15.073  9.525   25.725 1.00 55.87  ? 1372 ARG B CD    1 
ATOM   4932 N  NE    . ARG B 1 155 ? 14.813  10.732  26.502 1.00 61.09  ? 1372 ARG B NE    1 
ATOM   4933 C  CZ    . ARG B 1 155 ? 14.222  11.813  26.022 1.00 60.92  ? 1372 ARG B CZ    1 
ATOM   4934 N  NH1   . ARG B 1 155 ? 13.838  11.836  24.764 1.00 67.79  ? 1372 ARG B NH1   1 
ATOM   4935 N  NH2   . ARG B 1 155 ? 13.999  12.856  26.804 1.00 66.16  ? 1372 ARG B NH2   1 
ATOM   4936 N  N     . GLU B 1 156 ? 14.468  3.851   26.113 1.00 37.34  ? 1373 GLU B N     1 
ATOM   4937 C  CA    . GLU B 1 156 ? 14.476  2.448   25.771 1.00 42.92  ? 1373 GLU B CA    1 
ATOM   4938 C  C     . GLU B 1 156 ? 13.755  1.719   26.880 1.00 42.35  ? 1373 GLU B C     1 
ATOM   4939 O  O     . GLU B 1 156 ? 13.992  1.996   28.058 1.00 43.00  ? 1373 GLU B O     1 
ATOM   4940 C  CB    . GLU B 1 156 ? 15.901  1.922   25.623 1.00 53.75  ? 1373 GLU B CB    1 
ATOM   4941 C  CG    . GLU B 1 156 ? 15.946  0.440   25.287 1.00 62.78  ? 1373 GLU B CG    1 
ATOM   4942 C  CD    . GLU B 1 156 ? 17.248  -0.226  25.681 1.00 60.66  ? 1373 GLU B CD    1 
ATOM   4943 O  OE1   . GLU B 1 156 ? 17.960  0.295   26.566 1.00 60.45  ? 1373 GLU B OE1   1 
ATOM   4944 O  OE2   . GLU B 1 156 ? 17.559  -1.274  25.087 1.00 59.73  ? 1373 GLU B OE2   1 
ATOM   4945 N  N     . PHE B 1 157 ? 12.878  0.790   26.507 1.00 41.50  ? 1374 PHE B N     1 
ATOM   4946 C  CA    . PHE B 1 157 ? 12.266  -0.071  27.506 1.00 39.38  ? 1374 PHE B CA    1 
ATOM   4947 C  C     . PHE B 1 157 ? 12.095  -1.458  26.938 1.00 39.51  ? 1374 PHE B C     1 
ATOM   4948 O  O     . PHE B 1 157 ? 12.010  -1.645  25.727 1.00 48.28  ? 1374 PHE B O     1 
ATOM   4949 C  CB    . PHE B 1 157 ? 10.915  0.433   28.032 1.00 48.12  ? 1374 PHE B CB    1 
ATOM   4950 C  CG    . PHE B 1 157 ? 9.906   0.804   26.975 1.00 53.01  ? 1374 PHE B CG    1 
ATOM   4951 C  CD1   . PHE B 1 157 ? 8.894   -0.075  26.617 1.00 50.24  ? 1374 PHE B CD1   1 
ATOM   4952 C  CD2   . PHE B 1 157 ? 9.907   2.081   26.404 1.00 52.75  ? 1374 PHE B CD2   1 
ATOM   4953 C  CE1   . PHE B 1 157 ? 7.924   0.315   25.656 1.00 54.56  ? 1374 PHE B CE1   1 
ATOM   4954 C  CE2   . PHE B 1 157 ? 8.948   2.470   25.449 1.00 38.00  ? 1374 PHE B CE2   1 
ATOM   4955 C  CZ    . PHE B 1 157 ? 7.960   1.600   25.076 1.00 32.73  ? 1374 PHE B CZ    1 
ATOM   4956 N  N     . LEU B 1 158 ? 12.102  -2.434  27.830 1.00 34.32  ? 1375 LEU B N     1 
ATOM   4957 C  CA    . LEU B 1 158 ? 11.874  -3.817  27.442 1.00 37.73  ? 1375 LEU B CA    1 
ATOM   4958 C  C     . LEU B 1 158 ? 10.399  -4.175  27.611 1.00 40.98  ? 1375 LEU B C     1 
ATOM   4959 O  O     . LEU B 1 158 ? 9.762   -3.816  28.612 1.00 48.13  ? 1375 LEU B O     1 
ATOM   4960 C  CB    . LEU B 1 158 ? 12.725  -4.756  28.300 1.00 37.03  ? 1375 LEU B CB    1 
ATOM   4961 C  CG    . LEU B 1 158 ? 14.110  -4.318  28.759 1.00 30.44  ? 1375 LEU B CG    1 
ATOM   4962 C  CD1   . LEU B 1 158 ? 14.720  -5.391  29.612 1.00 25.46  ? 1375 LEU B CD1   1 
ATOM   4963 C  CD2   . LEU B 1 158 ? 14.952  -4.063  27.557 1.00 26.35  ? 1375 LEU B CD2   1 
ATOM   4964 N  N     . TRP B 1 159 ? 9.868   -4.961  26.685 1.00 30.25  ? 1376 TRP B N     1 
ATOM   4965 C  CA    . TRP B 1 159 ? 8.467   -5.347  26.758 1.00 33.89  ? 1376 TRP B CA    1 
ATOM   4966 C  C     . TRP B 1 159 ? 8.200   -6.571  25.919 1.00 42.55  ? 1376 TRP B C     1 
ATOM   4967 O  O     . TRP B 1 159 ? 9.108   -7.125  25.298 1.00 50.48  ? 1376 TRP B O     1 
ATOM   4968 C  CB    . TRP B 1 159 ? 7.648   -4.274  26.132 1.00 30.39  ? 1376 TRP B CB    1 
ATOM   4969 C  CG    . TRP B 1 159 ? 7.746   -4.137  24.700 1.00 31.75  ? 1376 TRP B CG    1 
ATOM   4970 C  CD1   . TRP B 1 159 ? 8.779   -4.554  23.932 1.00 32.26  ? 1376 TRP B CD1   1 
ATOM   4971 C  CD2   . TRP B 1 159 ? 6.832   -3.489  23.863 1.00 25.97  ? 1376 TRP B CD2   1 
ATOM   4972 N  NE1   . TRP B 1 159 ? 8.546   -4.232  22.643 1.00 42.19  ? 1376 TRP B NE1   1 
ATOM   4973 C  CE2   . TRP B 1 159 ? 7.352   -3.568  22.584 1.00 26.00  ? 1376 TRP B CE2   1 
ATOM   4974 C  CE3   . TRP B 1 159 ? 5.602   -2.853  24.065 1.00 26.22  ? 1376 TRP B CE3   1 
ATOM   4975 C  CZ2   . TRP B 1 159 ? 6.687   -3.041  21.476 1.00 30.26  ? 1376 TRP B CZ2   1 
ATOM   4976 C  CZ3   . TRP B 1 159 ? 4.944   -2.326  22.974 1.00 36.96  ? 1376 TRP B CZ3   1 
ATOM   4977 C  CH2   . TRP B 1 159 ? 5.488   -2.423  21.693 1.00 33.10  ? 1376 TRP B CH2   1 
ATOM   4978 N  N     . GLN B 1 160 ? 6.941   -6.995  25.900 1.00 36.57  ? 1377 GLN B N     1 
ATOM   4979 C  CA    . GLN B 1 160 ? 6.583   -8.060  25.047 1.00 47.05  ? 1377 GLN B CA    1 
ATOM   4980 C  C     . GLN B 1 160 ? 5.471   -7.532  24.203 1.00 50.23  ? 1377 GLN B C     1 
ATOM   4981 O  O     . GLN B 1 160 ? 4.599   -6.922  24.698 1.00 56.37  ? 1377 GLN B O     1 
ATOM   4982 C  CB    . GLN B 1 160 ? 6.055   -9.217  25.848 1.00 55.53  ? 1377 GLN B CB    1 
ATOM   4983 C  CG    . GLN B 1 160 ? 4.941   -8.883  26.798 1.00 54.74  ? 1377 GLN B CG    1 
ATOM   4984 C  CD    . GLN B 1 160 ? 3.630   -8.967  26.170 1.00 52.81  ? 1377 GLN B CD    1 
ATOM   4985 O  OE1   . GLN B 1 160 ? 2.695   -8.346  26.574 1.00 63.44  ? 1377 GLN B OE1   1 
ATOM   4986 N  NE2   . GLN B 1 160 ? 3.560   -9.724  25.160 1.00 53.98  ? 1377 GLN B NE2   1 
ATOM   4987 N  N     . GLU B 1 161 ? 5.486   -7.826  22.921 1.00 44.29  ? 1378 GLU B N     1 
ATOM   4988 C  CA    . GLU B 1 161 ? 4.390   -7.368  22.108 1.00 48.46  ? 1378 GLU B CA    1 
ATOM   4989 C  C     . GLU B 1 161 ? 3.854   -8.542  21.304 1.00 55.43  ? 1378 GLU B C     1 
ATOM   4990 O  O     . GLU B 1 161 ? 4.609   -9.218  20.606 1.00 59.37  ? 1378 GLU B O     1 
ATOM   4991 C  CB    . GLU B 1 161 ? 4.823   -6.247  21.193 1.00 37.21  ? 1378 GLU B CB    1 
ATOM   4992 C  CG    . GLU B 1 161 ? 5.945   -6.683  20.299 1.00 38.04  ? 1378 GLU B CG    1 
ATOM   4993 C  CD    . GLU B 1 161 ? 6.223   -5.701  19.236 1.00 37.49  ? 1378 GLU B CD    1 
ATOM   4994 O  OE1   . GLU B 1 161 ? 5.449   -4.730  19.104 1.00 33.52  ? 1378 GLU B OE1   1 
ATOM   4995 O  OE2   . GLU B 1 161 ? 7.222   -5.879  18.507 1.00 33.53  ? 1378 GLU B OE2   1 
ATOM   4996 N  N     . GLY B 1 162 ? 2.552   -8.788  21.401 1.00 49.87  ? 1379 GLY B N     1 
ATOM   4997 C  CA    . GLY B 1 162 ? 1.978   -9.896  20.702 1.00 42.21  ? 1379 GLY B CA    1 
ATOM   4998 C  C     . GLY B 1 162 ? 1.027   -9.399  19.683 1.00 48.16  ? 1379 GLY B C     1 
ATOM   4999 O  O     . GLY B 1 162 ? 0.352   -8.472  19.939 1.00 42.79  ? 1379 GLY B O     1 
ATOM   5000 N  N     . HIS B 1 163 ? 1.035   -10.011 18.512 1.00 48.57  ? 1380 HIS B N     1 
ATOM   5001 C  CA    . HIS B 1 163 ? 0.243   -9.657  17.375 1.00 33.97  ? 1380 HIS B CA    1 
ATOM   5002 C  C     . HIS B 1 163 ? -0.341  -10.937 16.886 1.00 41.56  ? 1380 HIS B C     1 
ATOM   5003 O  O     . HIS B 1 163 ? 0.328   -11.872 16.660 1.00 41.66  ? 1380 HIS B O     1 
ATOM   5004 C  CB    . HIS B 1 163 ? 1.146   -9.077  16.342 1.00 35.65  ? 1380 HIS B CB    1 
ATOM   5005 C  CG    . HIS B 1 163 ? 1.876   -7.855  16.788 1.00 46.99  ? 1380 HIS B CG    1 
ATOM   5006 N  ND1   . HIS B 1 163 ? 1.384   -6.595  16.618 1.00 42.12  ? 1380 HIS B ND1   1 
ATOM   5007 C  CD2   . HIS B 1 163 ? 3.072   -7.707  17.375 1.00 42.29  ? 1380 HIS B CD2   1 
ATOM   5008 C  CE1   . HIS B 1 163 ? 2.228   -5.730  17.118 1.00 34.41  ? 1380 HIS B CE1   1 
ATOM   5009 N  NE2   . HIS B 1 163 ? 3.263   -6.376  17.574 1.00 38.87  ? 1380 HIS B NE2   1 
ATOM   5010 N  N     . THR B 1 164 ? -1.635  -10.946 16.685 1.00 42.74  ? 1381 THR B N     1 
ATOM   5011 C  CA    . THR B 1 164 ? -2.428  -12.116 16.411 1.00 29.46  ? 1381 THR B CA    1 
ATOM   5012 C  C     . THR B 1 164 ? -3.406  -11.798 15.299 1.00 49.94  ? 1381 THR B C     1 
ATOM   5013 O  O     . THR B 1 164 ? -3.936  -10.685 15.201 1.00 58.04  ? 1381 THR B O     1 
ATOM   5014 C  CB    . THR B 1 164 ? -3.201  -12.578 17.645 1.00 41.60  ? 1381 THR B CB    1 
ATOM   5015 O  OG1   . THR B 1 164 ? -4.097  -11.539 18.078 1.00 41.54  ? 1381 THR B OG1   1 
ATOM   5016 C  CG2   . THR B 1 164 ? -2.238  -12.974 18.767 1.00 31.95  ? 1381 THR B CG2   1 
ATOM   5017 N  N     . ALA B 1 165 ? -3.663  -12.820 14.499 1.00 47.51  ? 1382 ALA B N     1 
ATOM   5018 C  CA    . ALA B 1 165 ? -4.530  -12.767 13.345 1.00 46.05  ? 1382 ALA B CA    1 
ATOM   5019 C  C     . ALA B 1 165 ? -5.416  -13.989 13.391 1.00 45.72  ? 1382 ALA B C     1 
ATOM   5020 O  O     . ALA B 1 165 ? -4.940  -15.094 13.657 1.00 50.27  ? 1382 ALA B O     1 
ATOM   5021 C  CB    . ALA B 1 165 ? -3.739  -12.745 12.045 1.00 58.19  ? 1382 ALA B CB    1 
ATOM   5022 N  N     . PHE B 1 166 ? -6.702  -13.765 13.127 1.00 51.56  ? 1383 PHE B N     1 
ATOM   5023 C  CA    . PHE B 1 166 ? -7.788  -14.685 13.405 1.00 54.01  ? 1383 PHE B CA    1 
ATOM   5024 C  C     . PHE B 1 166 ? -8.754  -14.697 12.237 1.00 56.12  ? 1383 PHE B C     1 
ATOM   5025 O  O     . PHE B 1 166 ? -8.929  -13.687 11.556 1.00 51.12  ? 1383 PHE B O     1 
ATOM   5026 C  CB    . PHE B 1 166 ? -8.551  -14.288 14.662 1.00 50.94  ? 1383 PHE B CB    1 
ATOM   5027 C  CG    . PHE B 1 166 ? -7.789  -14.505 15.920 1.00 55.45  ? 1383 PHE B CG    1 
ATOM   5028 C  CD1   . PHE B 1 166 ? -7.479  -13.447 16.743 1.00 69.49  ? 1383 PHE B CD1   1 
ATOM   5029 C  CD2   . PHE B 1 166 ? -7.381  -15.758 16.283 1.00 32.30  ? 1383 PHE B CD2   1 
ATOM   5030 C  CE1   . PHE B 1 166 ? -6.779  -13.650 17.905 1.00 59.39  ? 1383 PHE B CE1   1 
ATOM   5031 C  CE2   . PHE B 1 166 ? -6.696  -15.956 17.422 1.00 44.32  ? 1383 PHE B CE2   1 
ATOM   5032 C  CZ    . PHE B 1 166 ? -6.393  -14.904 18.238 1.00 48.73  ? 1383 PHE B CZ    1 
ATOM   5033 N  N     . ALA B 1 167 ? -9.379  -15.856 12.014 1.00 62.40  ? 1384 ALA B N     1 
ATOM   5034 C  CA    . ALA B 1 167 ? -10.405 -15.961 10.984 1.00 69.61  ? 1384 ALA B CA    1 
ATOM   5035 C  C     . ALA B 1 167 ? -11.639 -15.137 11.338 1.00 75.79  ? 1384 ALA B C     1 
ATOM   5036 O  O     . ALA B 1 167 ? -12.004 -14.204 10.610 1.00 81.83  ? 1384 ALA B O     1 
ATOM   5037 C  CB    . ALA B 1 167 ? -10.779 -17.426 10.779 1.00 78.52  ? 1384 ALA B CB    1 
ATOM   5038 N  N     . THR B 1 168 ? -12.287 -15.444 12.461 1.00 70.68  ? 1385 THR B N     1 
ATOM   5039 C  CA    . THR B 1 168 ? -13.477 -14.704 12.860 1.00 75.93  ? 1385 THR B CA    1 
ATOM   5040 C  C     . THR B 1 168 ? -13.241 -13.851 14.093 1.00 80.80  ? 1385 THR B C     1 
ATOM   5041 O  O     . THR B 1 168 ? -12.436 -14.194 14.961 1.00 83.75  ? 1385 THR B O     1 
ATOM   5042 C  CB    . THR B 1 168 ? -14.651 -15.613 13.165 1.00 72.33  ? 1385 THR B CB    1 
ATOM   5043 O  OG1   . THR B 1 168 ? -15.684 -14.840 13.792 1.00 81.48  ? 1385 THR B OG1   1 
ATOM   5044 C  CG2   . THR B 1 168 ? -14.215 -16.646 14.130 1.00 62.86  ? 1385 THR B CG2   1 
ATOM   5045 N  N     . GLN B 1 169 ? -14.076 -12.804 14.207 1.00 71.96  ? 1386 GLN B N     1 
ATOM   5046 C  CA    . GLN B 1 169 ? -13.936 -11.795 15.257 1.00 57.88  ? 1386 GLN B CA    1 
ATOM   5047 C  C     . GLN B 1 169 ? -14.136 -12.373 16.654 1.00 56.72  ? 1386 GLN B C     1 
ATOM   5048 O  O     . GLN B 1 169 ? -13.626 -11.816 17.632 1.00 47.47  ? 1386 GLN B O     1 
ATOM   5049 C  CB    . GLN B 1 169 ? -14.916 -10.651 15.007 1.00 54.81  ? 1386 GLN B CB    1 
ATOM   5050 C  CG    . GLN B 1 169 ? -14.983 -9.600  16.107 1.00 64.89  ? 1386 GLN B CG    1 
ATOM   5051 C  CD    . GLN B 1 169 ? -15.715 -8.341  15.689 1.00 69.91  ? 1386 GLN B CD    1 
ATOM   5052 O  OE1   . GLN B 1 169 ? -16.682 -8.387  14.910 1.00 63.71  ? 1386 GLN B OE1   1 
ATOM   5053 N  NE2   . GLN B 1 169 ? -15.241 -7.195  16.193 1.00 68.03  ? 1386 GLN B NE2   1 
ATOM   5054 N  N     . LYS B 1 170 ? -14.883 -13.467 16.778 1.00 63.01  ? 1387 LYS B N     1 
ATOM   5055 C  CA    . LYS B 1 170 ? -15.062 -14.075 18.093 1.00 63.03  ? 1387 LYS B CA    1 
ATOM   5056 C  C     . LYS B 1 170 ? -13.721 -14.453 18.718 1.00 51.52  ? 1387 LYS B C     1 
ATOM   5057 O  O     . LYS B 1 170 ? -13.465 -14.165 19.897 1.00 59.66  ? 1387 LYS B O     1 
ATOM   5058 C  CB    . LYS B 1 170 ? -15.983 -15.285 17.989 1.00 69.46  ? 1387 LYS B CB    1 
ATOM   5059 C  CG    . LYS B 1 170 ? -16.988 -15.376 19.124 1.00 71.35  ? 1387 LYS B CG    1 
ATOM   5060 C  CD    . LYS B 1 170 ? -17.610 -16.749 19.127 1.00 76.33  ? 1387 LYS B CD    1 
ATOM   5061 C  CE    . LYS B 1 170 ? -18.910 -16.783 19.886 1.00 78.19  ? 1387 LYS B CE    1 
ATOM   5062 N  NZ    . LYS B 1 170 ? -19.525 -18.132 19.727 1.00 75.56  ? 1387 LYS B NZ    1 
ATOM   5063 N  N     . GLU B 1 171 ? -12.867 -15.136 17.959 1.00 42.48  ? 1388 GLU B N     1 
ATOM   5064 C  CA    . GLU B 1 171 ? -11.538 -15.466 18.471 1.00 50.31  ? 1388 GLU B CA    1 
ATOM   5065 C  C     . GLU B 1 171 ? -10.807 -14.227 18.974 1.00 47.95  ? 1388 GLU B C     1 
ATOM   5066 O  O     . GLU B 1 171 ? -10.221 -14.233 20.065 1.00 55.84  ? 1388 GLU B O     1 
ATOM   5067 C  CB    . GLU B 1 171 ? -10.706 -16.158 17.388 1.00 59.99  ? 1388 GLU B CB    1 
ATOM   5068 C  CG    . GLU B 1 171 ? -11.368 -17.375 16.737 1.00 61.62  ? 1388 GLU B CG    1 
ATOM   5069 C  CD    . GLU B 1 171 ? -10.568 -17.929 15.571 1.00 63.95  ? 1388 GLU B CD    1 
ATOM   5070 O  OE1   . GLU B 1 171 ? -9.480  -18.497 15.822 1.00 68.82  ? 1388 GLU B OE1   1 
ATOM   5071 O  OE2   . GLU B 1 171 ? -11.026 -17.798 14.410 1.00 62.46  ? 1388 GLU B OE2   1 
ATOM   5072 N  N     . ALA B 1 172 ? -10.866 -13.143 18.203 1.00 41.98  ? 1389 ALA B N     1 
ATOM   5073 C  CA    . ALA B 1 172 ? -10.151 -11.925 18.549 1.00 37.04  ? 1389 ALA B CA    1 
ATOM   5074 C  C     . ALA B 1 172 ? -10.701 -11.282 19.827 1.00 35.27  ? 1389 ALA B C     1 
ATOM   5075 O  O     . ALA B 1 172 ? -9.930  -10.901 20.717 1.00 39.67  ? 1389 ALA B O     1 
ATOM   5076 C  CB    . ALA B 1 172 ? -10.203 -10.978 17.359 1.00 32.54  ? 1389 ALA B CB    1 
ATOM   5077 N  N     . ASP B 1 173 ? -12.024 -11.125 19.933 1.00 33.15  ? 1390 ASP B N     1 
ATOM   5078 C  CA    . ASP B 1 173 ? -12.596 -10.547 21.149 1.00 37.60  ? 1390 ASP B CA    1 
ATOM   5079 C  C     . ASP B 1 173 ? -12.205 -11.367 22.379 1.00 44.34  ? 1390 ASP B C     1 
ATOM   5080 O  O     . ASP B 1 173 ? -11.776 -10.819 23.416 1.00 46.02  ? 1390 ASP B O     1 
ATOM   5081 C  CB    . ASP B 1 173 ? -14.125 -10.441 21.012 1.00 44.64  ? 1390 ASP B CB    1 
ATOM   5082 C  CG    . ASP B 1 173 ? -14.570 -9.377  19.979 1.00 51.96  ? 1390 ASP B CG    1 
ATOM   5083 O  OD1   . ASP B 1 173 ? -13.724 -8.633  19.445 1.00 54.53  ? 1390 ASP B OD1   1 
ATOM   5084 O  OD2   . ASP B 1 173 ? -15.778 -9.264  19.702 1.00 50.33  ? 1390 ASP B OD2   1 
ATOM   5085 N  N     . GLU B 1 174 ? -12.282 -12.696 22.255 1.00 60.41  ? 1391 GLU B N     1 
ATOM   5086 C  CA    . GLU B 1 174 ? -11.976 -13.565 23.387 1.00 56.67  ? 1391 GLU B CA    1 
ATOM   5087 C  C     . GLU B 1 174 ? -10.512 -13.474 23.781 1.00 48.39  ? 1391 GLU B C     1 
ATOM   5088 O  O     . GLU B 1 174 ? -10.193 -13.448 24.976 1.00 51.84  ? 1391 GLU B O     1 
ATOM   5089 C  CB    . GLU B 1 174 ? -12.345 -14.999 23.054 1.00 48.36  ? 1391 GLU B CB    1 
ATOM   5090 C  CG    . GLU B 1 174 ? -13.823 -15.188 22.920 1.00 56.31  ? 1391 GLU B CG    1 
ATOM   5091 C  CD    . GLU B 1 174 ? -14.198 -16.612 22.558 1.00 69.06  ? 1391 GLU B CD    1 
ATOM   5092 O  OE1   . GLU B 1 174 ? -13.314 -17.510 22.599 1.00 59.39  ? 1391 GLU B OE1   1 
ATOM   5093 O  OE2   . GLU B 1 174 ? -15.394 -16.833 22.253 1.00 83.16  ? 1391 GLU B OE2   1 
ATOM   5094 N  N     . GLU B 1 175 ? -9.607  -13.431 22.800 1.00 39.31  ? 1392 GLU B N     1 
ATOM   5095 C  CA    . GLU B 1 175 ? -8.195  -13.342 23.154 1.00 46.48  ? 1392 GLU B CA    1 
ATOM   5096 C  C     . GLU B 1 175 ? -7.861  -11.999 23.789 1.00 49.74  ? 1392 GLU B C     1 
ATOM   5097 O  O     . GLU B 1 175 ? -7.066  -11.946 24.735 1.00 55.25  ? 1392 GLU B O     1 
ATOM   5098 C  CB    . GLU B 1 175 ? -7.296  -13.583 21.943 1.00 46.90  ? 1392 GLU B CB    1 
ATOM   5099 C  CG    . GLU B 1 175 ? -5.797  -13.564 22.323 1.00 47.59  ? 1392 GLU B CG    1 
ATOM   5100 C  CD    . GLU B 1 175 ? -4.845  -13.405 21.133 1.00 49.37  ? 1392 GLU B CD    1 
ATOM   5101 O  OE1   . GLU B 1 175 ? -4.124  -14.370 20.803 1.00 57.18  ? 1392 GLU B OE1   1 
ATOM   5102 O  OE2   . GLU B 1 175 ? -4.817  -12.325 20.519 1.00 49.70  ? 1392 GLU B OE2   1 
ATOM   5103 N  N     . VAL B 1 176 ? -8.430  -10.902 23.279 1.00 45.53  ? 1393 VAL B N     1 
ATOM   5104 C  CA    . VAL B 1 176 ? -8.193  -9.612  23.924 1.00 47.48  ? 1393 VAL B CA    1 
ATOM   5105 C  C     . VAL B 1 176 ? -8.490  -9.734  25.408 1.00 47.84  ? 1393 VAL B C     1 
ATOM   5106 O  O     . VAL B 1 176 ? -7.663  -9.384  26.265 1.00 50.47  ? 1393 VAL B O     1 
ATOM   5107 C  CB    . VAL B 1 176 ? -9.029  -8.486  23.277 1.00 46.49  ? 1393 VAL B CB    1 
ATOM   5108 C  CG1   . VAL B 1 176 ? -8.965  -7.215  24.134 1.00 35.09  ? 1393 VAL B CG1   1 
ATOM   5109 C  CG2   . VAL B 1 176 ? -8.547  -8.163  21.882 1.00 44.42  ? 1393 VAL B CG2   1 
ATOM   5110 N  N     . LEU B 1 177 ? -9.666  -10.273 25.733 1.00 34.49  ? 1394 LEU B N     1 
ATOM   5111 C  CA    . LEU B 1 177 ? -10.034 -10.311 27.133 1.00 32.55  ? 1394 LEU B CA    1 
ATOM   5112 C  C     . LEU B 1 177 ? -9.181  -11.273 27.940 1.00 35.39  ? 1394 LEU B C     1 
ATOM   5113 O  O     . LEU B 1 177 ? -8.870  -11.013 29.102 1.00 39.60  ? 1394 LEU B O     1 
ATOM   5114 C  CB    . LEU B 1 177 ? -11.518 -10.566 27.281 1.00 36.38  ? 1394 LEU B CB    1 
ATOM   5115 C  CG    . LEU B 1 177 ? -12.451 -9.515  26.676 1.00 43.31  ? 1394 LEU B CG    1 
ATOM   5116 C  CD1   . LEU B 1 177 ? -13.904 -9.941  26.818 1.00 44.61  ? 1394 LEU B CD1   1 
ATOM   5117 C  CD2   . LEU B 1 177 ? -12.221 -8.157  27.322 1.00 37.93  ? 1394 LEU B CD2   1 
ATOM   5118 N  N     . THR B 1 178 ? -8.799  -12.392 27.321 1.00 31.39  ? 1395 THR B N     1 
ATOM   5119 C  CA    . THR B 1 178 ? -7.927  -13.363 27.974 1.00 38.13  ? 1395 THR B CA    1 
ATOM   5120 C  C     . THR B 1 178 ? -6.615  -12.718 28.376 1.00 38.30  ? 1395 THR B C     1 
ATOM   5121 O  O     . THR B 1 178 ? -6.192  -12.784 29.546 1.00 48.30  ? 1395 THR B O     1 
ATOM   5122 C  CB    . THR B 1 178 ? -7.681  -14.559 27.033 1.00 45.24  ? 1395 THR B CB    1 
ATOM   5123 O  OG1   . THR B 1 178 ? -8.903  -15.274 26.814 1.00 58.06  ? 1395 THR B OG1   1 
ATOM   5124 C  CG2   . THR B 1 178 ? -6.717  -15.533 27.613 1.00 31.11  ? 1395 THR B CG2   1 
ATOM   5125 N  N     . ILE B 1 179 ? -5.964  -12.077 27.410 1.00 42.47  ? 1396 ILE B N     1 
ATOM   5126 C  CA    . ILE B 1 179 ? -4.702  -11.388 27.662 1.00 48.36  ? 1396 ILE B CA    1 
ATOM   5127 C  C     . ILE B 1 179 ? -4.876  -10.319 28.746 1.00 47.80  ? 1396 ILE B C     1 
ATOM   5128 O  O     . ILE B 1 179 ? -3.983  -10.096 29.580 1.00 44.04  ? 1396 ILE B O     1 
ATOM   5129 C  CB    . ILE B 1 179 ? -4.164  -10.810 26.339 1.00 49.78  ? 1396 ILE B CB    1 
ATOM   5130 C  CG1   . ILE B 1 179 ? -4.057  -11.924 25.272 1.00 38.10  ? 1396 ILE B CG1   1 
ATOM   5131 C  CG2   . ILE B 1 179 ? -2.894  -9.984  26.565 1.00 60.42  ? 1396 ILE B CG2   1 
ATOM   5132 C  CD1   . ILE B 1 179 ? -2.900  -12.867 25.379 1.00 28.73  ? 1396 ILE B CD1   1 
ATOM   5133 N  N     . LEU B 1 180 ? -6.011  -9.621  28.739 1.00 50.34  ? 1397 LEU B N     1 
ATOM   5134 C  CA    . LEU B 1 180 ? -6.203  -8.593  29.756 1.00 55.65  ? 1397 LEU B CA    1 
ATOM   5135 C  C     . LEU B 1 180 ? -6.284  -9.185  31.150 1.00 47.64  ? 1397 LEU B C     1 
ATOM   5136 O  O     . LEU B 1 180 ? -5.782  -8.595  32.116 1.00 52.36  ? 1397 LEU B O     1 
ATOM   5137 C  CB    . LEU B 1 180 ? -7.456  -7.777  29.472 1.00 55.19  ? 1397 LEU B CB    1 
ATOM   5138 C  CG    . LEU B 1 180 ? -7.416  -6.558  30.386 1.00 42.81  ? 1397 LEU B CG    1 
ATOM   5139 C  CD1   . LEU B 1 180 ? -6.413  -5.586  29.803 1.00 29.89  ? 1397 LEU B CD1   1 
ATOM   5140 C  CD2   . LEU B 1 180 ? -8.808  -5.955  30.621 1.00 34.06  ? 1397 LEU B CD2   1 
ATOM   5141 N  N     . ASP B 1 181 ? -6.968  -10.316 31.280 1.00 49.36  ? 1398 ASP B N     1 
ATOM   5142 C  CA    . ASP B 1 181 ? -7.020  -10.999 32.569 1.00 55.42  ? 1398 ASP B CA    1 
ATOM   5143 C  C     . ASP B 1 181 ? -5.625  -11.408 33.014 1.00 50.66  ? 1398 ASP B C     1 
ATOM   5144 O  O     . ASP B 1 181 ? -5.294  -11.340 34.205 1.00 45.60  ? 1398 ASP B O     1 
ATOM   5145 C  CB    . ASP B 1 181 ? -7.939  -12.215 32.486 1.00 60.80  ? 1398 ASP B CB    1 
ATOM   5146 C  CG    . ASP B 1 181 ? -8.193  -12.829 33.832 1.00 69.12  ? 1398 ASP B CG    1 
ATOM   5147 O  OD1   . ASP B 1 181 ? -7.880  -14.027 34.013 1.00 64.60  ? 1398 ASP B OD1   1 
ATOM   5148 O  OD2   . ASP B 1 181 ? -8.681  -12.097 34.717 1.00 80.29  ? 1398 ASP B OD2   1 
ATOM   5149 N  N     . LEU B 1 182 ? -4.791  -11.828 32.061 1.00 47.61  ? 1399 LEU B N     1 
ATOM   5150 C  CA    . LEU B 1 182 ? -3.399  -12.148 32.381 1.00 49.03  ? 1399 LEU B CA    1 
ATOM   5151 C  C     . LEU B 1 182 ? -2.648  -10.938 32.926 1.00 56.67  ? 1399 LEU B C     1 
ATOM   5152 O  O     . LEU B 1 182 ? -1.948  -11.028 33.943 1.00 54.35  ? 1399 LEU B O     1 
ATOM   5153 C  CB    . LEU B 1 182 ? -2.696  -12.671 31.134 1.00 51.54  ? 1399 LEU B CB    1 
ATOM   5154 C  CG    . LEU B 1 182 ? -3.098  -14.096 30.772 1.00 51.22  ? 1399 LEU B CG    1 
ATOM   5155 C  CD1   . LEU B 1 182 ? -2.240  -14.641 29.597 1.00 29.17  ? 1399 LEU B CD1   1 
ATOM   5156 C  CD2   . LEU B 1 182 ? -2.959  -14.893 32.055 1.00 29.93  ? 1399 LEU B CD2   1 
ATOM   5157 N  N     . TYR B 1 183 ? -2.822  -9.802  32.269 1.00 60.25  ? 1400 TYR B N     1 
ATOM   5158 C  CA    . TYR B 1 183 ? -2.177  -8.572  32.678 1.00 44.48  ? 1400 TYR B CA    1 
ATOM   5159 C  C     . TYR B 1 183 ? -2.606  -8.208  34.104 1.00 41.16  ? 1400 TYR B C     1 
ATOM   5160 O  O     . TYR B 1 183 ? -1.760  -7.968  34.966 1.00 51.60  ? 1400 TYR B O     1 
ATOM   5161 C  CB    . TYR B 1 183 ? -2.502  -7.473  31.675 1.00 48.07  ? 1400 TYR B CB    1 
ATOM   5162 C  CG    . TYR B 1 183 ? -1.740  -7.579  30.377 1.00 42.95  ? 1400 TYR B CG    1 
ATOM   5163 C  CD1   . TYR B 1 183 ? -0.440  -7.102  30.271 1.00 40.36  ? 1400 TYR B CD1   1 
ATOM   5164 C  CD2   . TYR B 1 183 ? -2.319  -8.156  29.255 1.00 36.71  ? 1400 TYR B CD2   1 
ATOM   5165 C  CE1   . TYR B 1 183 ? 0.261   -7.197  29.084 1.00 36.35  ? 1400 TYR B CE1   1 
ATOM   5166 C  CE2   . TYR B 1 183 ? -1.626  -8.255  28.063 1.00 32.73  ? 1400 TYR B CE2   1 
ATOM   5167 C  CZ    . TYR B 1 183 ? -0.336  -7.774  27.984 1.00 30.56  ? 1400 TYR B CZ    1 
ATOM   5168 O  OH    . TYR B 1 183 ? 0.358   -7.871  26.800 1.00 27.10  ? 1400 TYR B OH    1 
ATOM   5169 N  N     . ALA B 1 184 ? -3.914  -8.166  34.351 1.00 29.76  ? 1401 ALA B N     1 
ATOM   5170 C  CA    . ALA B 1 184 ? -4.425  -7.892  35.686 1.00 30.33  ? 1401 ALA B CA    1 
ATOM   5171 C  C     . ALA B 1 184 ? -3.869  -8.879  36.722 1.00 45.08  ? 1401 ALA B C     1 
ATOM   5172 O  O     . ALA B 1 184 ? -3.587  -8.497  37.867 1.00 45.77  ? 1401 ALA B O     1 
ATOM   5173 C  CB    . ALA B 1 184 ? -5.952  -7.935  35.659 1.00 30.99  ? 1401 ALA B CB    1 
ATOM   5174 N  N     . LYS B 1 185 ? -3.678  -10.149 36.339 1.00 31.72  ? 1402 LYS B N     1 
ATOM   5175 C  CA    . LYS B 1 185 ? -3.131  -11.106 37.303 1.00 42.51  ? 1402 LYS B CA    1 
ATOM   5176 C  C     . LYS B 1 185 ? -1.658  -10.839 37.583 1.00 50.36  ? 1402 LYS B C     1 
ATOM   5177 O  O     . LYS B 1 185 ? -1.177  -11.090 38.695 1.00 44.63  ? 1402 LYS B O     1 
ATOM   5178 C  CB    . LYS B 1 185 ? -3.346  -12.546 36.830 1.00 40.30  ? 1402 LYS B CB    1 
ATOM   5179 C  CG    . LYS B 1 185 ? -4.708  -13.137 37.197 1.00 41.75  ? 1402 LYS B CG    1 
ATOM   5180 C  CD    . LYS B 1 185 ? -4.874  -14.517 36.599 1.00 53.97  ? 1402 LYS B CD    1 
ATOM   5181 C  CE    . LYS B 1 185 ? -6.022  -15.294 37.233 1.00 66.47  ? 1402 LYS B CE    1 
ATOM   5182 N  NZ    . LYS B 1 185 ? -6.057  -16.746 36.772 1.00 69.46  ? 1402 LYS B NZ    1 
ATOM   5183 N  N     . VAL B 1 186 ? -0.916  -10.392 36.571 1.00 47.19  ? 1403 VAL B N     1 
ATOM   5184 C  CA    . VAL B 1 186 ? 0.451   -9.943  36.820 1.00 44.17  ? 1403 VAL B CA    1 
ATOM   5185 C  C     . VAL B 1 186 ? 0.444   -8.872  37.891 1.00 47.18  ? 1403 VAL B C     1 
ATOM   5186 O  O     . VAL B 1 186 ? 1.296   -8.850  38.788 1.00 40.49  ? 1403 VAL B O     1 
ATOM   5187 C  CB    . VAL B 1 186 ? 1.085   -9.393  35.531 1.00 43.81  ? 1403 VAL B CB    1 
ATOM   5188 C  CG1   . VAL B 1 186 ? 2.339   -8.590  35.860 1.00 28.09  ? 1403 VAL B CG1   1 
ATOM   5189 C  CG2   . VAL B 1 186 ? 1.372   -10.492 34.552 1.00 48.83  ? 1403 VAL B CG2   1 
ATOM   5190 N  N     . TYR B 1 187 ? -0.541  -7.976  37.832 1.00 55.98  ? 1404 TYR B N     1 
ATOM   5191 C  CA    . TYR B 1 187 ? -0.502  -6.861  38.772 1.00 61.35  ? 1404 TYR B CA    1 
ATOM   5192 C  C     . TYR B 1 187 ? -0.896  -7.301  40.168 1.00 63.78  ? 1404 TYR B C     1 
ATOM   5193 O  O     . TYR B 1 187 ? -0.191  -6.991  41.137 1.00 63.96  ? 1404 TYR B O     1 
ATOM   5194 C  CB    . TYR B 1 187 ? -1.377  -5.703  38.284 1.00 56.86  ? 1404 TYR B CB    1 
ATOM   5195 C  CG    . TYR B 1 187 ? -0.541  -4.749  37.474 1.00 43.22  ? 1404 TYR B CG    1 
ATOM   5196 C  CD1   . TYR B 1 187 ? -0.416  -4.906  36.104 1.00 39.24  ? 1404 TYR B CD1   1 
ATOM   5197 C  CD2   . TYR B 1 187 ? 0.206   -3.758  38.092 1.00 36.28  ? 1404 TYR B CD2   1 
ATOM   5198 C  CE1   . TYR B 1 187 ? 0.391   -4.073  35.354 1.00 40.98  ? 1404 TYR B CE1   1 
ATOM   5199 C  CE2   . TYR B 1 187 ? 1.021   -2.914  37.356 1.00 37.67  ? 1404 TYR B CE2   1 
ATOM   5200 C  CZ    . TYR B 1 187 ? 1.107   -3.077  35.984 1.00 42.60  ? 1404 TYR B CZ    1 
ATOM   5201 O  OH    . TYR B 1 187 ? 1.905   -2.249  35.234 1.00 42.91  ? 1404 TYR B OH    1 
ATOM   5202 N  N     . THR B 1 188 ? -1.969  -8.088  40.287 1.00 60.56  ? 1405 THR B N     1 
ATOM   5203 C  CA    . THR B 1 188 ? -2.504  -8.355  41.619 1.00 54.46  ? 1405 THR B CA    1 
ATOM   5204 C  C     . THR B 1 188 ? -1.900  -9.581  42.255 1.00 52.20  ? 1405 THR B C     1 
ATOM   5205 O  O     . THR B 1 188 ? -1.736  -9.617  43.480 1.00 52.94  ? 1405 THR B O     1 
ATOM   5206 C  CB    . THR B 1 188 ? -4.021  -8.559  41.596 1.00 46.56  ? 1405 THR B CB    1 
ATOM   5207 O  OG1   . THR B 1 188 ? -4.282  -9.884  41.147 1.00 50.42  ? 1405 THR B OG1   1 
ATOM   5208 C  CG2   . THR B 1 188 ? -4.714  -7.580  40.679 1.00 40.28  ? 1405 THR B CG2   1 
ATOM   5209 N  N     . ASP B 1 189 ? -1.575  -10.582 41.449 1.00 62.39  ? 1406 ASP B N     1 
ATOM   5210 C  CA    . ASP B 1 189 ? -1.055  -11.849 41.941 1.00 62.97  ? 1406 ASP B CA    1 
ATOM   5211 C  C     . ASP B 1 189 ? 0.461   -11.898 42.007 1.00 57.74  ? 1406 ASP B C     1 
ATOM   5212 O  O     . ASP B 1 189 ? 1.006   -12.597 42.860 1.00 51.58  ? 1406 ASP B O     1 
ATOM   5213 C  CB    . ASP B 1 189 ? -1.595  -12.971 41.066 1.00 50.25  ? 1406 ASP B CB    1 
ATOM   5214 C  CG    . ASP B 1 189 ? -3.096  -12.971 41.032 1.00 47.59  ? 1406 ASP B CG    1 
ATOM   5215 O  OD1   . ASP B 1 189 ? -3.697  -12.366 41.946 1.00 43.97  ? 1406 ASP B OD1   1 
ATOM   5216 O  OD2   . ASP B 1 189 ? -3.676  -13.527 40.081 1.00 50.35  ? 1406 ASP B OD2   1 
ATOM   5217 N  N     . LEU B 1 190 ? 1.164   -11.162 41.155 1.00 61.47  ? 1407 LEU B N     1 
ATOM   5218 C  CA    . LEU B 1 190 ? 2.615   -11.112 41.277 1.00 56.25  ? 1407 LEU B CA    1 
ATOM   5219 C  C     . LEU B 1 190 ? 3.070   -9.913  42.102 1.00 59.13  ? 1407 LEU B C     1 
ATOM   5220 O  O     . LEU B 1 190 ? 3.803   -10.087 43.082 1.00 74.02  ? 1407 LEU B O     1 
ATOM   5221 C  CB    . LEU B 1 190 ? 3.275   -11.084 39.889 1.00 43.95  ? 1407 LEU B CB    1 
ATOM   5222 C  CG    . LEU B 1 190 ? 3.035   -12.245 38.909 1.00 38.59  ? 1407 LEU B CG    1 
ATOM   5223 C  CD1   . LEU B 1 190 ? 3.894   -12.136 37.674 1.00 28.70  ? 1407 LEU B CD1   1 
ATOM   5224 C  CD2   . LEU B 1 190 ? 3.259   -13.581 39.545 1.00 29.91  ? 1407 LEU B CD2   1 
ATOM   5225 N  N     . LEU B 1 191 ? 2.580   -8.711  41.781 1.00 46.77  ? 1408 LEU B N     1 
ATOM   5226 C  CA    . LEU B 1 191 ? 3.053   -7.471  42.389 1.00 41.95  ? 1408 LEU B CA    1 
ATOM   5227 C  C     . LEU B 1 191 ? 2.155   -6.951  43.499 1.00 42.59  ? 1408 LEU B C     1 
ATOM   5228 O  O     . LEU B 1 191 ? 2.476   -5.923  44.095 1.00 44.08  ? 1408 LEU B O     1 
ATOM   5229 C  CB    . LEU B 1 191 ? 3.213   -6.394  41.319 1.00 35.76  ? 1408 LEU B CB    1 
ATOM   5230 C  CG    . LEU B 1 191 ? 4.219   -6.853  40.263 1.00 35.24  ? 1408 LEU B CG    1 
ATOM   5231 C  CD1   . LEU B 1 191 ? 4.275   -5.939  39.041 1.00 28.61  ? 1408 LEU B CD1   1 
ATOM   5232 C  CD2   . LEU B 1 191 ? 5.577   -7.009  40.920 1.00 29.09  ? 1408 LEU B CD2   1 
ATOM   5233 N  N     . ALA B 1 192 ? 1.043   -7.627  43.785 1.00 45.99  ? 1409 ALA B N     1 
ATOM   5234 C  CA    . ALA B 1 192 ? 0.131   -7.264  44.878 1.00 50.00  ? 1409 ALA B CA    1 
ATOM   5235 C  C     . ALA B 1 192 ? -0.377  -5.830  44.718 1.00 50.79  ? 1409 ALA B C     1 
ATOM   5236 O  O     . ALA B 1 192 ? -0.454  -5.057  45.680 1.00 42.47  ? 1409 ALA B O     1 
ATOM   5237 C  CB    . ALA B 1 192 ? 0.776   -7.470  46.251 1.00 33.05  ? 1409 ALA B CB    1 
ATOM   5238 N  N     . ILE B 1 193 ? -0.763  -5.502  43.488 1.00 43.99  ? 1410 ILE B N     1 
ATOM   5239 C  CA    . ILE B 1 193 ? -1.294  -4.188  43.153 1.00 51.33  ? 1410 ILE B CA    1 
ATOM   5240 C  C     . ILE B 1 193 ? -2.731  -4.308  42.671 1.00 56.93  ? 1410 ILE B C     1 
ATOM   5241 O  O     . ILE B 1 193 ? -3.046  -5.200  41.871 1.00 63.28  ? 1410 ILE B O     1 
ATOM   5242 C  CB    . ILE B 1 193 ? -0.429  -3.510  42.086 1.00 55.15  ? 1410 ILE B CB    1 
ATOM   5243 C  CG1   . ILE B 1 193 ? 0.981   -3.294  42.625 1.00 56.20  ? 1410 ILE B CG1   1 
ATOM   5244 C  CG2   . ILE B 1 193 ? -1.045  -2.192  41.660 1.00 50.74  ? 1410 ILE B CG2   1 
ATOM   5245 C  CD1   . ILE B 1 193 ? 1.892   -2.709  41.618 1.00 57.41  ? 1410 ILE B CD1   1 
ATOM   5246 N  N     . PRO B 1 194 ? -3.633  -3.458  43.150 1.00 53.70  ? 1411 PRO B N     1 
ATOM   5247 C  CA    . PRO B 1 194 ? -4.992  -3.436  42.607 1.00 44.35  ? 1411 PRO B CA    1 
ATOM   5248 C  C     . PRO B 1 194 ? -5.077  -2.588  41.352 1.00 52.02  ? 1411 PRO B C     1 
ATOM   5249 O  O     . PRO B 1 194 ? -4.443  -1.535  41.249 1.00 62.43  ? 1411 PRO B O     1 
ATOM   5250 C  CB    . PRO B 1 194 ? -5.815  -2.832  43.750 1.00 46.59  ? 1411 PRO B CB    1 
ATOM   5251 C  CG    . PRO B 1 194 ? -4.860  -1.958  44.468 1.00 56.25  ? 1411 PRO B CG    1 
ATOM   5252 C  CD    . PRO B 1 194 ? -3.509  -2.644  44.366 1.00 61.97  ? 1411 PRO B CD    1 
ATOM   5253 N  N     . VAL B 1 195 ? -5.858  -3.076  40.384 1.00 55.54  ? 1412 VAL B N     1 
ATOM   5254 C  CA    . VAL B 1 195 ? -6.016  -2.446  39.079 1.00 48.51  ? 1412 VAL B CA    1 
ATOM   5255 C  C     . VAL B 1 195 ? -7.467  -2.518  38.629 1.00 49.99  ? 1412 VAL B C     1 
ATOM   5256 O  O     . VAL B 1 195 ? -8.207  -3.438  38.981 1.00 47.97  ? 1412 VAL B O     1 
ATOM   5257 C  CB    . VAL B 1 195 ? -5.136  -3.076  37.985 1.00 45.05  ? 1412 VAL B CB    1 
ATOM   5258 C  CG1   . VAL B 1 195 ? -3.684  -2.954  38.333 1.00 40.62  ? 1412 VAL B CG1   1 
ATOM   5259 C  CG2   . VAL B 1 195 ? -5.570  -4.524  37.691 1.00 40.28  ? 1412 VAL B CG2   1 
ATOM   5260 N  N     . VAL B 1 196 ? -7.858  -1.524  37.840 1.00 57.67  ? 1413 VAL B N     1 
ATOM   5261 C  CA    . VAL B 1 196 ? -9.183  -1.409  37.246 1.00 49.64  ? 1413 VAL B CA    1 
ATOM   5262 C  C     . VAL B 1 196 ? -9.097  -1.813  35.775 1.00 51.28  ? 1413 VAL B C     1 
ATOM   5263 O  O     . VAL B 1 196 ? -8.389  -1.169  34.988 1.00 58.31  ? 1413 VAL B O     1 
ATOM   5264 C  CB    . VAL B 1 196 ? -9.714  0.028   37.414 1.00 46.92  ? 1413 VAL B CB    1 
ATOM   5265 C  CG1   . VAL B 1 196 ? -10.842 0.332   36.488 1.00 40.89  ? 1413 VAL B CG1   1 
ATOM   5266 C  CG2   . VAL B 1 196 ? -10.183 0.245   38.838 1.00 43.66  ? 1413 VAL B CG2   1 
ATOM   5267 N  N     . LYS B 1 197 ? -9.808  -2.880  35.402 1.00 46.89  ? 1414 LYS B N     1 
ATOM   5268 C  CA    . LYS B 1 197 ? -9.950  -3.257  33.996 1.00 46.32  ? 1414 LYS B CA    1 
ATOM   5269 C  C     . LYS B 1 197 ? -10.990 -2.373  33.307 1.00 45.22  ? 1414 LYS B C     1 
ATOM   5270 O  O     . LYS B 1 197 ? -12.071 -2.126  33.855 1.00 42.31  ? 1414 LYS B O     1 
ATOM   5271 C  CB    . LYS B 1 197 ? -10.411 -4.710  33.857 1.00 49.80  ? 1414 LYS B CB    1 
ATOM   5272 C  CG    . LYS B 1 197 ? -9.429  -5.816  34.086 1.00 47.59  ? 1414 LYS B CG    1 
ATOM   5273 C  CD    . LYS B 1 197 ? -10.189 -7.140  34.052 1.00 38.41  ? 1414 LYS B CD    1 
ATOM   5274 C  CE    . LYS B 1 197 ? -9.280  -8.321  33.749 1.00 56.63  ? 1414 LYS B CE    1 
ATOM   5275 N  NZ    . LYS B 1 197 ? -9.994  -9.453  33.045 1.00 62.64  ? 1414 LYS B NZ    1 
ATOM   5276 N  N     . GLY B 1 198 ? -10.685 -1.921  32.089 1.00 47.02  ? 1415 GLY B N     1 
ATOM   5277 C  CA    . GLY B 1 198 ? -11.697 -1.169  31.360 1.00 43.97  ? 1415 GLY B CA    1 
ATOM   5278 C  C     . GLY B 1 198 ? -11.430 -1.050  29.872 1.00 48.95  ? 1415 GLY B C     1 
ATOM   5279 O  O     . GLY B 1 198 ? -10.449 -1.577  29.346 1.00 48.41  ? 1415 GLY B O     1 
ATOM   5280 N  N     . ARG B 1 199 ? -12.356 -0.375  29.186 1.00 55.85  ? 1416 ARG B N     1 
ATOM   5281 C  CA    . ARG B 1 199 ? -12.190 0.053   27.797 1.00 59.84  ? 1416 ARG B CA    1 
ATOM   5282 C  C     . ARG B 1 199 ? -11.751 1.507   27.773 1.00 64.19  ? 1416 ARG B C     1 
ATOM   5283 O  O     . ARG B 1 199 ? -12.239 2.325   28.559 1.00 67.08  ? 1416 ARG B O     1 
ATOM   5284 C  CB    . ARG B 1 199 ? -13.499 -0.059  27.009 1.00 64.25  ? 1416 ARG B CB    1 
ATOM   5285 C  CG    . ARG B 1 199 ? -13.620 -1.238  26.076 1.00 75.71  ? 1416 ARG B CG    1 
ATOM   5286 C  CD    . ARG B 1 199 ? -14.910 -1.172  25.252 1.00 76.23  ? 1416 ARG B CD    1 
ATOM   5287 N  NE    . ARG B 1 199 ? -14.775 -0.260  24.128 1.00 66.50  ? 1416 ARG B NE    1 
ATOM   5288 C  CZ    . ARG B 1 199 ? -15.410 -0.399  22.974 1.00 64.32  ? 1416 ARG B CZ    1 
ATOM   5289 N  NH1   . ARG B 1 199 ? -16.230 -1.416  22.798 1.00 67.22  ? 1416 ARG B NH1   1 
ATOM   5290 N  NH2   . ARG B 1 199 ? -15.214 0.475   21.993 1.00 64.36  ? 1416 ARG B NH2   1 
ATOM   5291 N  N     . LYS B 1 200 ? -10.837 1.834   26.870 1.00 64.13  ? 1417 LYS B N     1 
ATOM   5292 C  CA    . LYS B 1 200 ? -10.465 3.234   26.721 1.00 64.58  ? 1417 LYS B CA    1 
ATOM   5293 C  C     . LYS B 1 200 ? -11.481 3.934   25.822 1.00 67.02  ? 1417 LYS B C     1 
ATOM   5294 O  O     . LYS B 1 200 ? -12.075 3.329   24.915 1.00 65.74  ? 1417 LYS B O     1 
ATOM   5295 C  CB    . LYS B 1 200 ? -9.053  3.385   26.152 1.00 53.64  ? 1417 LYS B CB    1 
ATOM   5296 C  CG    . LYS B 1 200 ? -7.940  3.016   27.112 1.00 56.94  ? 1417 LYS B CG    1 
ATOM   5297 C  CD    . LYS B 1 200 ? -7.311  4.229   27.760 1.00 60.14  ? 1417 LYS B CD    1 
ATOM   5298 C  CE    . LYS B 1 200 ? -6.031  3.839   28.447 1.00 64.51  ? 1417 LYS B CE    1 
ATOM   5299 N  NZ    . LYS B 1 200 ? -5.299  5.015   28.982 1.00 76.98  ? 1417 LYS B NZ    1 
ATOM   5300 N  N     . THR B 1 201 ? -11.693 5.217   26.097 1.00 58.84  ? 1418 THR B N     1 
ATOM   5301 C  CA    . THR B 1 201 ? -12.632 5.983   25.302 1.00 51.23  ? 1418 THR B CA    1 
ATOM   5302 C  C     . THR B 1 201 ? -12.162 6.066   23.850 1.00 50.51  ? 1418 THR B C     1 
ATOM   5303 O  O     . THR B 1 201 ? -11.028 5.722   23.506 1.00 40.48  ? 1418 THR B O     1 
ATOM   5304 C  CB    . THR B 1 201 ? -12.797 7.386   25.878 1.00 53.52  ? 1418 THR B CB    1 
ATOM   5305 O  OG1   . THR B 1 201 ? -11.543 8.081   25.799 1.00 61.45  ? 1418 THR B OG1   1 
ATOM   5306 C  CG2   . THR B 1 201 ? -13.242 7.315   27.319 1.00 46.56  ? 1418 THR B CG2   1 
ATOM   5307 N  N     . GLU B 1 202 ? -13.071 6.533   22.990 1.00 61.20  ? 1419 GLU B N     1 
ATOM   5308 C  CA    . GLU B 1 202 ? -12.717 6.791   21.599 1.00 61.84  ? 1419 GLU B CA    1 
ATOM   5309 C  C     . GLU B 1 202 ? -11.578 7.801   21.487 1.00 64.88  ? 1419 GLU B C     1 
ATOM   5310 O  O     . GLU B 1 202 ? -10.826 7.783   20.505 1.00 67.39  ? 1419 GLU B O     1 
ATOM   5311 C  CB    . GLU B 1 202 ? -13.951 7.241   20.826 1.00 59.21  ? 1419 GLU B CB    1 
ATOM   5312 C  CG    . GLU B 1 202 ? -14.912 6.069   20.531 1.00 72.97  ? 1419 GLU B CG    1 
ATOM   5313 C  CD    . GLU B 1 202 ? -14.230 4.855   19.874 1.00 71.61  ? 1419 GLU B CD    1 
ATOM   5314 O  OE1   . GLU B 1 202 ? -13.781 3.955   20.608 1.00 74.85  ? 1419 GLU B OE1   1 
ATOM   5315 O  OE2   . GLU B 1 202 ? -14.148 4.790   18.627 1.00 70.53  ? 1419 GLU B OE2   1 
ATOM   5316 N  N     . LYS B 1 203 ? -11.445 8.704   22.463 1.00 58.09  ? 1420 LYS B N     1 
ATOM   5317 C  CA    . LYS B 1 203 ? -10.317 9.629   22.445 1.00 60.85  ? 1420 LYS B CA    1 
ATOM   5318 C  C     . LYS B 1 203 ? -9.013  8.941   22.841 1.00 62.38  ? 1420 LYS B C     1 
ATOM   5319 O  O     . LYS B 1 203 ? -7.949  9.260   22.300 1.00 62.15  ? 1420 LYS B O     1 
ATOM   5320 C  CB    . LYS B 1 203 ? -10.598 10.816  23.367 1.00 66.11  ? 1420 LYS B CB    1 
ATOM   5321 C  CG    . LYS B 1 203 ? -9.425  11.754  23.500 1.00 69.58  ? 1420 LYS B CG    1 
ATOM   5322 C  CD    . LYS B 1 203 ? -9.760  13.056  24.204 1.00 69.65  ? 1420 LYS B CD    1 
ATOM   5323 C  CE    . LYS B 1 203 ? -8.466  13.764  24.616 1.00 68.51  ? 1420 LYS B CE    1 
ATOM   5324 N  NZ    . LYS B 1 203 ? -8.622  14.569  25.868 1.00 72.22  ? 1420 LYS B NZ    1 
ATOM   5325 N  N     . GLU B 1 204 ? -9.071  7.981   23.754 1.00 56.52  ? 1421 GLU B N     1 
ATOM   5326 C  CA    . GLU B 1 204 ? -7.864  7.385   24.290 1.00 50.35  ? 1421 GLU B CA    1 
ATOM   5327 C  C     . GLU B 1 204 ? -7.527  6.029   23.683 1.00 43.12  ? 1421 GLU B C     1 
ATOM   5328 O  O     . GLU B 1 204 ? -6.480  5.464   24.026 1.00 40.44  ? 1421 GLU B O     1 
ATOM   5329 C  CB    . GLU B 1 204 ? -7.977  7.252   25.808 1.00 64.20  ? 1421 GLU B CB    1 
ATOM   5330 C  CG    . GLU B 1 204 ? -8.273  8.552   26.528 1.00 76.56  ? 1421 GLU B CG    1 
ATOM   5331 C  CD    . GLU B 1 204 ? -7.178  9.603   26.361 1.00 83.12  ? 1421 GLU B CD    1 
ATOM   5332 O  OE1   . GLU B 1 204 ? -6.029  9.228   26.033 1.00 86.85  ? 1421 GLU B OE1   1 
ATOM   5333 O  OE2   . GLU B 1 204 ? -7.463  10.805  26.590 1.00 81.76  ? 1421 GLU B OE2   1 
ATOM   5334 N  N     . LYS B 1 205 ? -8.352  5.506   22.777 1.00 37.29  ? 1422 LYS B N     1 
ATOM   5335 C  CA    . LYS B 1 205 ? -8.054  4.209   22.181 1.00 39.34  ? 1422 LYS B CA    1 
ATOM   5336 C  C     . LYS B 1 205 ? -6.801  4.299   21.297 1.00 44.40  ? 1422 LYS B C     1 
ATOM   5337 O  O     . LYS B 1 205 ? -6.250  5.374   21.053 1.00 49.40  ? 1422 LYS B O     1 
ATOM   5338 C  CB    . LYS B 1 205 ? -9.281  3.686   21.412 1.00 32.68  ? 1422 LYS B CB    1 
ATOM   5339 C  CG    . LYS B 1 205 ? -9.475  4.198   19.981 1.00 33.14  ? 1422 LYS B CG    1 
ATOM   5340 C  CD    . LYS B 1 205 ? -10.721 3.635   19.277 1.00 33.71  ? 1422 LYS B CD    1 
ATOM   5341 C  CE    . LYS B 1 205 ? -10.739 4.068   17.814 1.00 39.69  ? 1422 LYS B CE    1 
ATOM   5342 N  NZ    . LYS B 1 205 ? -11.073 3.061   16.728 1.00 34.27  ? 1422 LYS B NZ    1 
ATOM   5343 N  N     . PHE B 1 206 ? -6.286  3.141   20.898 1.00 42.25  ? 1423 PHE B N     1 
ATOM   5344 C  CA    . PHE B 1 206 ? -5.191  3.112   19.935 1.00 39.21  ? 1423 PHE B CA    1 
ATOM   5345 C  C     . PHE B 1 206 ? -5.765  3.456   18.566 1.00 45.64  ? 1423 PHE B C     1 
ATOM   5346 O  O     . PHE B 1 206 ? -6.790  2.905   18.168 1.00 63.24  ? 1423 PHE B O     1 
ATOM   5347 C  CB    . PHE B 1 206 ? -4.532  1.732   19.951 1.00 43.42  ? 1423 PHE B CB    1 
ATOM   5348 C  CG    . PHE B 1 206 ? -3.477  1.531   18.906 1.00 53.80  ? 1423 PHE B CG    1 
ATOM   5349 C  CD1   . PHE B 1 206 ? -2.634  2.551   18.536 1.00 66.20  ? 1423 PHE B CD1   1 
ATOM   5350 C  CD2   . PHE B 1 206 ? -3.307  0.301   18.320 1.00 60.88  ? 1423 PHE B CD2   1 
ATOM   5351 C  CE1   . PHE B 1 206 ? -1.659  2.349   17.582 1.00 63.86  ? 1423 PHE B CE1   1 
ATOM   5352 C  CE2   . PHE B 1 206 ? -2.337  0.100   17.370 1.00 54.95  ? 1423 PHE B CE2   1 
ATOM   5353 C  CZ    . PHE B 1 206 ? -1.514  1.121   17.005 1.00 54.07  ? 1423 PHE B CZ    1 
ATOM   5354 N  N     . ALA B 1 207 ? -5.152  4.407   17.864 1.00 43.72  ? 1424 ALA B N     1 
ATOM   5355 C  CA    . ALA B 1 207 ? -5.824  4.998   16.703 1.00 49.64  ? 1424 ALA B CA    1 
ATOM   5356 C  C     . ALA B 1 207 ? -6.125  3.963   15.627 1.00 40.94  ? 1424 ALA B C     1 
ATOM   5357 O  O     . ALA B 1 207 ? -7.244  3.905   15.085 1.00 40.14  ? 1424 ALA B O     1 
ATOM   5358 C  CB    . ALA B 1 207 ? -4.998  6.149   16.126 1.00 59.64  ? 1424 ALA B CB    1 
ATOM   5359 N  N     . GLY B 1 208 ? -5.142  3.155   15.284 1.00 41.82  ? 1425 GLY B N     1 
ATOM   5360 C  CA    . GLY B 1 208 ? -5.418  2.177   14.248 1.00 57.85  ? 1425 GLY B CA    1 
ATOM   5361 C  C     . GLY B 1 208 ? -6.255  0.992   14.685 1.00 49.14  ? 1425 GLY B C     1 
ATOM   5362 O  O     . GLY B 1 208 ? -6.583  0.139   13.861 1.00 44.34  ? 1425 GLY B O     1 
ATOM   5363 N  N     . GLY B 1 209 ? -6.667  0.938   15.929 1.00 41.87  ? 1426 GLY B N     1 
ATOM   5364 C  CA    . GLY B 1 209 ? -7.438  -0.146  16.452 1.00 31.76  ? 1426 GLY B CA    1 
ATOM   5365 C  C     . GLY B 1 209 ? -8.905  0.013   16.339 1.00 41.44  ? 1426 GLY B C     1 
ATOM   5366 O  O     . GLY B 1 209 ? -9.339  0.768   15.566 1.00 56.48  ? 1426 GLY B O     1 
ATOM   5367 N  N     . ASP B 1 210 ? -9.672  -0.733  17.103 1.00 44.67  ? 1427 ASP B N     1 
ATOM   5368 C  CA    . ASP B 1 210 ? -11.102 -0.673  17.068 1.00 47.95  ? 1427 ASP B CA    1 
ATOM   5369 C  C     . ASP B 1 210 ? -11.436 -0.217  18.407 1.00 45.29  ? 1427 ASP B C     1 
ATOM   5370 O  O     . ASP B 1 210 ? -11.987 0.785   18.620 1.00 41.45  ? 1427 ASP B O     1 
ATOM   5371 C  CB    . ASP B 1 210 ? -11.611 -2.083  16.983 1.00 54.65  ? 1427 ASP B CB    1 
ATOM   5372 C  CG    . ASP B 1 210 ? -12.743 -2.248  16.070 1.00 65.24  ? 1427 ASP B CG    1 
ATOM   5373 O  OD1   . ASP B 1 210 ? -12.674 -1.821  14.942 1.00 72.96  ? 1427 ASP B OD1   1 
ATOM   5374 O  OD2   . ASP B 1 210 ? -13.704 -2.870  16.465 1.00 68.05  ? 1427 ASP B OD2   1 
ATOM   5375 N  N     . TYR B 1 211 ? -11.057 -1.041  19.367 1.00 51.94  ? 1428 TYR B N     1 
ATOM   5376 C  CA    . TYR B 1 211 ? -11.264 -0.724  20.732 1.00 57.38  ? 1428 TYR B CA    1 
ATOM   5377 C  C     . TYR B 1 211 ? -10.047 -1.129  21.491 1.00 40.20  ? 1428 TYR B C     1 
ATOM   5378 O  O     . TYR B 1 211 ? -9.233  -1.940  21.038 1.00 49.53  ? 1428 TYR B O     1 
ATOM   5379 C  CB    . TYR B 1 211 ? -12.502 -1.371  21.332 1.00 63.32  ? 1428 TYR B CB    1 
ATOM   5380 C  CG    . TYR B 1 211 ? -12.558 -2.852  21.362 1.00 54.85  ? 1428 TYR B CG    1 
ATOM   5381 C  CD1   . TYR B 1 211 ? -11.986 -3.567  22.405 1.00 55.31  ? 1428 TYR B CD1   1 
ATOM   5382 C  CD2   . TYR B 1 211 ? -13.186 -3.563  20.348 1.00 44.65  ? 1428 TYR B CD2   1 
ATOM   5383 C  CE1   . TYR B 1 211 ? -12.036 -4.948  22.437 1.00 38.28  ? 1428 TYR B CE1   1 
ATOM   5384 C  CE2   . TYR B 1 211 ? -13.242 -4.943  20.371 1.00 36.71  ? 1428 TYR B CE2   1 
ATOM   5385 C  CZ    . TYR B 1 211 ? -12.665 -5.630  21.418 1.00 38.20  ? 1428 TYR B CZ    1 
ATOM   5386 O  OH    . TYR B 1 211 ? -12.718 -7.005  21.446 1.00 57.72  ? 1428 TYR B OH    1 
ATOM   5387 N  N     . THR B 1 212 ? -9.921  -0.569  22.671 1.00 31.86  ? 1429 THR B N     1 
ATOM   5388 C  CA    . THR B 1 212 ? -8.724  -0.894  23.435 1.00 31.16  ? 1429 THR B CA    1 
ATOM   5389 C  C     . THR B 1 212 ? -9.068  -1.172  24.889 1.00 48.14  ? 1429 THR B C     1 
ATOM   5390 O  O     . THR B 1 212 ? -9.775  -0.378  25.517 1.00 54.25  ? 1429 THR B O     1 
ATOM   5391 C  CB    . THR B 1 212 ? -7.713  0.240   23.367 1.00 41.09  ? 1429 THR B CB    1 
ATOM   5392 O  OG1   . THR B 1 212 ? -7.060  0.239   22.095 1.00 50.34  ? 1429 THR B OG1   1 
ATOM   5393 C  CG2   . THR B 1 212 ? -6.697  0.087   24.437 1.00 34.13  ? 1429 THR B CG2   1 
ATOM   5394 N  N     . THR B 1 213 ? -8.617  -2.320  25.399 1.00 41.91  ? 1430 THR B N     1 
ATOM   5395 C  CA    . THR B 1 213 ? -8.713  -2.654  26.818 1.00 51.15  ? 1430 THR B CA    1 
ATOM   5396 C  C     . THR B 1 213 ? -7.471  -2.190  27.571 1.00 50.30  ? 1430 THR B C     1 
ATOM   5397 O  O     . THR B 1 213 ? -6.363  -2.207  27.043 1.00 53.28  ? 1430 THR B O     1 
ATOM   5398 C  CB    . THR B 1 213 ? -8.900  -4.154  27.048 1.00 48.55  ? 1430 THR B CB    1 
ATOM   5399 O  OG1   . THR B 1 213 ? -7.842  -4.879  26.403 1.00 51.27  ? 1430 THR B OG1   1 
ATOM   5400 C  CG2   . THR B 1 213 ? -10.226 -4.603  26.523 1.00 44.07  ? 1430 THR B CG2   1 
ATOM   5401 N  N     . THR B 1 214 ? -7.651  -1.895  28.853 1.00 45.12  ? 1431 THR B N     1 
ATOM   5402 C  CA    . THR B 1 214 ? -6.525  -1.470  29.658 1.00 43.15  ? 1431 THR B CA    1 
ATOM   5403 C  C     . THR B 1 214 ? -6.701  -1.930  31.090 1.00 40.47  ? 1431 THR B C     1 
ATOM   5404 O  O     . THR B 1 214 ? -7.800  -2.268  31.542 1.00 50.36  ? 1431 THR B O     1 
ATOM   5405 C  CB    . THR B 1 214 ? -6.352  0.068   29.619 1.00 42.54  ? 1431 THR B CB    1 
ATOM   5406 O  OG1   . THR B 1 214 ? -5.090  0.411   30.179 1.00 46.18  ? 1431 THR B OG1   1 
ATOM   5407 C  CG2   . THR B 1 214 ? -7.422  0.794   30.436 1.00 32.13  ? 1431 THR B CG2   1 
ATOM   5408 N  N     . VAL B 1 215 ? -5.587  -1.860  31.809 1.00 36.21  ? 1432 VAL B N     1 
ATOM   5409 C  CA    . VAL B 1 215 ? -5.478  -2.243  33.210 1.00 39.84  ? 1432 VAL B CA    1 
ATOM   5410 C  C     . VAL B 1 215 ? -4.837  -1.028  33.873 1.00 46.24  ? 1432 VAL B C     1 
ATOM   5411 O  O     . VAL B 1 215 ? -3.643  -0.789  33.709 1.00 48.80  ? 1432 VAL B O     1 
ATOM   5412 C  CB    . VAL B 1 215 ? -4.637  -3.515  33.402 1.00 39.34  ? 1432 VAL B CB    1 
ATOM   5413 C  CG1   . VAL B 1 215 ? -3.967  -3.539  34.735 1.00 46.07  ? 1432 VAL B CG1   1 
ATOM   5414 C  CG2   . VAL B 1 215 ? -5.543  -4.708  33.291 1.00 41.77  ? 1432 VAL B CG2   1 
ATOM   5415 N  N     . GLU B 1 216 ? -5.646  -0.227  34.560 1.00 51.85  ? 1433 GLU B N     1 
ATOM   5416 C  CA    . GLU B 1 216 ? -5.169  1.026   35.136 1.00 60.73  ? 1433 GLU B CA    1 
ATOM   5417 C  C     . GLU B 1 216 ? -4.840  0.840   36.609 1.00 65.06  ? 1433 GLU B C     1 
ATOM   5418 O  O     . GLU B 1 216 ? -5.479  0.055   37.313 1.00 70.41  ? 1433 GLU B O     1 
ATOM   5419 C  CB    . GLU B 1 216 ? -6.201  2.161   35.001 1.00 55.11  ? 1433 GLU B CB    1 
ATOM   5420 C  CG    . GLU B 1 216 ? -6.716  2.446   33.581 1.00 58.04  ? 1433 GLU B CG    1 
ATOM   5421 C  CD    . GLU B 1 216 ? -5.822  3.386   32.802 1.00 63.15  ? 1433 GLU B CD    1 
ATOM   5422 O  OE1   . GLU B 1 216 ? -5.328  3.005   31.722 1.00 65.69  ? 1433 GLU B OE1   1 
ATOM   5423 O  OE2   . GLU B 1 216 ? -5.599  4.510   33.279 1.00 66.19  ? 1433 GLU B OE2   1 
ATOM   5424 N  N     . ALA B 1 217 ? -3.849  1.599   37.078 1.00 56.97  ? 1434 ALA B N     1 
ATOM   5425 C  CA    . ALA B 1 217 ? -3.450  1.590   38.474 1.00 54.22  ? 1434 ALA B CA    1 
ATOM   5426 C  C     . ALA B 1 217 ? -3.286  3.035   38.920 1.00 55.31  ? 1434 ALA B C     1 
ATOM   5427 O  O     . ALA B 1 217 ? -3.130  3.928   38.094 1.00 46.99  ? 1434 ALA B O     1 
ATOM   5428 C  CB    . ALA B 1 217 ? -2.156  0.792   38.678 1.00 49.71  ? 1434 ALA B CB    1 
ATOM   5429 N  N     . TYR B 1 218 ? -3.352  3.261   40.234 1.00 57.09  ? 1435 TYR B N     1 
ATOM   5430 C  CA    . TYR B 1 218 ? -3.402  4.595   40.827 1.00 50.70  ? 1435 TYR B CA    1 
ATOM   5431 C  C     . TYR B 1 218 ? -2.264  4.775   41.822 1.00 51.37  ? 1435 TYR B C     1 
ATOM   5432 O  O     . TYR B 1 218 ? -2.088  3.939   42.710 1.00 62.88  ? 1435 TYR B O     1 
ATOM   5433 C  CB    . TYR B 1 218 ? -4.740  4.791   41.540 1.00 55.01  ? 1435 TYR B CB    1 
ATOM   5434 C  CG    . TYR B 1 218 ? -4.956  6.174   42.106 1.00 56.70  ? 1435 TYR B CG    1 
ATOM   5435 C  CD1   . TYR B 1 218 ? -5.219  7.259   41.267 1.00 50.35  ? 1435 TYR B CD1   1 
ATOM   5436 C  CD2   . TYR B 1 218 ? -4.904  6.397   43.477 1.00 55.78  ? 1435 TYR B CD2   1 
ATOM   5437 C  CE1   . TYR B 1 218 ? -5.424  8.518   41.781 1.00 59.00  ? 1435 TYR B CE1   1 
ATOM   5438 C  CE2   . TYR B 1 218 ? -5.104  7.662   44.000 1.00 58.51  ? 1435 TYR B CE2   1 
ATOM   5439 C  CZ    . TYR B 1 218 ? -5.371  8.718   43.150 1.00 64.26  ? 1435 TYR B CZ    1 
ATOM   5440 O  OH    . TYR B 1 218 ? -5.577  9.982   43.662 1.00 64.96  ? 1435 TYR B OH    1 
ATOM   5441 N  N     . ILE B 1 219 ? -1.534  5.885   41.725 1.00 48.16  ? 1436 ILE B N     1 
ATOM   5442 C  CA    . ILE B 1 219 ? -0.493  6.244   42.687 1.00 52.56  ? 1436 ILE B CA    1 
ATOM   5443 C  C     . ILE B 1 219 ? -1.070  7.318   43.596 1.00 63.06  ? 1436 ILE B C     1 
ATOM   5444 O  O     . ILE B 1 219 ? -1.349  8.441   43.140 1.00 70.16  ? 1436 ILE B O     1 
ATOM   5445 C  CB    . ILE B 1 219 ? 0.784   6.762   42.002 1.00 48.91  ? 1436 ILE B CB    1 
ATOM   5446 C  CG1   . ILE B 1 219 ? 1.467   5.685   41.173 1.00 56.30  ? 1436 ILE B CG1   1 
ATOM   5447 C  CG2   . ILE B 1 219 ? 1.785   7.206   43.032 1.00 40.10  ? 1436 ILE B CG2   1 
ATOM   5448 C  CD1   . ILE B 1 219 ? 1.003   5.629   39.787 1.00 53.44  ? 1436 ILE B CD1   1 
ATOM   5449 N  N     . SER B 1 220 ? -1.248  6.983   44.885 1.00 65.52  ? 1437 SER B N     1 
ATOM   5450 C  CA    . SER B 1 220 ? -1.799  7.971   45.811 1.00 76.68  ? 1437 SER B CA    1 
ATOM   5451 C  C     . SER B 1 220 ? -0.797  9.082   46.060 1.00 89.33  ? 1437 SER B C     1 
ATOM   5452 O  O     . SER B 1 220 ? -1.171  10.254  46.145 1.00 100.98 ? 1437 SER B O     1 
ATOM   5453 C  CB    . SER B 1 220 ? -2.169  7.345   47.156 1.00 72.64  ? 1437 SER B CB    1 
ATOM   5454 O  OG    . SER B 1 220 ? -2.819  6.110   47.012 1.00 74.16  ? 1437 SER B OG    1 
ATOM   5455 N  N     . ALA B 1 221 ? 0.481   8.722   46.169 1.00 83.03  ? 1438 ALA B N     1 
ATOM   5456 C  CA    . ALA B 1 221 ? 1.551   9.700   46.294 1.00 69.01  ? 1438 ALA B CA    1 
ATOM   5457 C  C     . ALA B 1 221 ? 1.443   10.763  45.210 1.00 69.68  ? 1438 ALA B C     1 
ATOM   5458 O  O     . ALA B 1 221 ? 1.320   11.957  45.498 1.00 70.59  ? 1438 ALA B O     1 
ATOM   5459 C  CB    . ALA B 1 221 ? 2.896   8.986   46.220 1.00 63.86  ? 1438 ALA B CB    1 
ATOM   5460 N  N     . SER B 1 222 ? 1.443   10.331  43.948 1.00 66.16  ? 1439 SER B N     1 
ATOM   5461 C  CA    . SER B 1 222 ? 1.324   11.250  42.830 1.00 53.80  ? 1439 SER B CA    1 
ATOM   5462 C  C     . SER B 1 222 ? -0.082  11.766  42.639 1.00 52.74  ? 1439 SER B C     1 
ATOM   5463 O  O     . SER B 1 222 ? -0.265  12.720  41.884 1.00 60.74  ? 1439 SER B O     1 
ATOM   5464 C  CB    . SER B 1 222 ? 1.737   10.542  41.533 1.00 59.74  ? 1439 SER B CB    1 
ATOM   5465 O  OG    . SER B 1 222 ? 3.147   10.502  41.375 1.00 69.19  ? 1439 SER B OG    1 
ATOM   5466 N  N     . GLY B 1 223 ? -1.075  11.172  43.296 1.00 56.29  ? 1440 GLY B N     1 
ATOM   5467 C  CA    . GLY B 1 223 ? -2.448  11.542  43.007 1.00 61.63  ? 1440 GLY B CA    1 
ATOM   5468 C  C     . GLY B 1 223 ? -2.831  11.288  41.564 1.00 64.62  ? 1440 GLY B C     1 
ATOM   5469 O  O     . GLY B 1 223 ? -3.770  11.902  41.049 1.00 72.90  ? 1440 GLY B O     1 
ATOM   5470 N  N     . ARG B 1 224 ? -2.112  10.401  40.889 1.00 63.92  ? 1441 ARG B N     1 
ATOM   5471 C  CA    . ARG B 1 224 ? -2.250  10.243  39.451 1.00 65.75  ? 1441 ARG B CA    1 
ATOM   5472 C  C     . ARG B 1 224 ? -2.370  8.764   39.121 1.00 73.17  ? 1441 ARG B C     1 
ATOM   5473 O  O     . ARG B 1 224 ? -1.844  7.916   39.834 1.00 83.08  ? 1441 ARG B O     1 
ATOM   5474 C  CB    . ARG B 1 224 ? -1.060  10.861  38.704 1.00 63.38  ? 1441 ARG B CB    1 
ATOM   5475 C  CG    . ARG B 1 224 ? -0.917  12.348  38.937 1.00 67.29  ? 1441 ARG B CG    1 
ATOM   5476 C  CD    . ARG B 1 224 ? 0.267   12.929  38.194 1.00 76.33  ? 1441 ARG B CD    1 
ATOM   5477 N  NE    . ARG B 1 224 ? -0.123  13.508  36.911 1.00 86.41  ? 1441 ARG B NE    1 
ATOM   5478 C  CZ    . ARG B 1 224 ? -0.355  14.803  36.721 1.00 97.76  ? 1441 ARG B CZ    1 
ATOM   5479 N  NH1   . ARG B 1 224 ? -0.233  15.651  37.739 1.00 94.35  ? 1441 ARG B NH1   1 
ATOM   5480 N  NH2   . ARG B 1 224 ? -0.712  15.251  35.519 1.00 106.94 ? 1441 ARG B NH2   1 
ATOM   5481 N  N     . ALA B 1 225 ? -3.060  8.453   38.036 1.00 68.53  ? 1442 ALA B N     1 
ATOM   5482 C  CA    . ALA B 1 225 ? -3.190  7.076   37.592 1.00 61.38  ? 1442 ALA B CA    1 
ATOM   5483 C  C     . ALA B 1 225 ? -2.235  6.808   36.436 1.00 56.37  ? 1442 ALA B C     1 
ATOM   5484 O  O     . ALA B 1 225 ? -1.699  7.719   35.816 1.00 59.08  ? 1442 ALA B O     1 
ATOM   5485 C  CB    . ALA B 1 225 ? -4.634  6.774   37.194 1.00 62.68  ? 1442 ALA B CB    1 
ATOM   5486 N  N     . ILE B 1 226 ? -2.043  5.533   36.135 1.00 56.73  ? 1443 ILE B N     1 
ATOM   5487 C  CA    . ILE B 1 226 ? -1.102  5.119   35.106 1.00 59.23  ? 1443 ILE B CA    1 
ATOM   5488 C  C     . ILE B 1 226 ? -1.605  3.826   34.464 1.00 54.47  ? 1443 ILE B C     1 
ATOM   5489 O  O     . ILE B 1 226 ? -2.151  2.937   35.127 1.00 34.44  ? 1443 ILE B O     1 
ATOM   5490 C  CB    . ILE B 1 226 ? 0.321   4.981   35.695 1.00 43.80  ? 1443 ILE B CB    1 
ATOM   5491 C  CG1   . ILE B 1 226 ? 1.339   4.573   34.626 1.00 37.19  ? 1443 ILE B CG1   1 
ATOM   5492 C  CG2   . ILE B 1 226 ? 0.326   4.014   36.871 1.00 39.44  ? 1443 ILE B CG2   1 
ATOM   5493 C  CD1   . ILE B 1 226 ? 2.764   4.472   35.188 1.00 37.28  ? 1443 ILE B CD1   1 
ATOM   5494 N  N     . GLN B 1 227 ? -1.414  3.745   33.159 1.00 58.26  ? 1444 GLN B N     1 
ATOM   5495 C  CA    . GLN B 1 227 ? -1.764  2.567   32.395 1.00 53.92  ? 1444 GLN B CA    1 
ATOM   5496 C  C     . GLN B 1 227 ? -0.722  1.494   32.647 1.00 48.66  ? 1444 GLN B C     1 
ATOM   5497 O  O     . GLN B 1 227 ? 0.478   1.759   32.523 1.00 38.97  ? 1444 GLN B O     1 
ATOM   5498 C  CB    . GLN B 1 227 ? -1.823  2.926   30.916 1.00 53.81  ? 1444 GLN B CB    1 
ATOM   5499 C  CG    . GLN B 1 227 ? -1.633  1.783   29.999 1.00 50.02  ? 1444 GLN B CG    1 
ATOM   5500 C  CD    . GLN B 1 227 ? -2.476  1.931   28.771 1.00 59.65  ? 1444 GLN B CD    1 
ATOM   5501 O  OE1   . GLN B 1 227 ? -3.501  1.269   28.637 1.00 59.35  ? 1444 GLN B OE1   1 
ATOM   5502 N  NE2   . GLN B 1 227 ? -2.066  2.811   27.865 1.00 70.95  ? 1444 GLN B NE2   1 
ATOM   5503 N  N     . GLY B 1 228 ? -1.173  0.300   33.058 1.00 44.24  ? 1445 GLY B N     1 
ATOM   5504 C  CA    . GLY B 1 228 ? -0.298  -0.803  33.386 1.00 35.70  ? 1445 GLY B CA    1 
ATOM   5505 C  C     . GLY B 1 228 ? 0.033   -1.721  32.228 1.00 36.22  ? 1445 GLY B C     1 
ATOM   5506 O  O     . GLY B 1 228 ? 1.119   -2.311  32.227 1.00 36.49  ? 1445 GLY B O     1 
ATOM   5507 N  N     . ALA B 1 229 ? -0.858  -1.818  31.233 1.00 28.24  ? 1446 ALA B N     1 
ATOM   5508 C  CA    . ALA B 1 229 ? -0.662  -2.617  30.015 1.00 27.91  ? 1446 ALA B CA    1 
ATOM   5509 C  C     . ALA B 1 229 ? -1.830  -2.346  29.082 1.00 34.19  ? 1446 ALA B C     1 
ATOM   5510 O  O     . ALA B 1 229 ? -2.817  -1.724  29.476 1.00 42.90  ? 1446 ALA B O     1 
ATOM   5511 C  CB    . ALA B 1 229 ? -0.574  -4.123  30.285 1.00 33.31  ? 1446 ALA B CB    1 
ATOM   5512 N  N     . THR B 1 230 ? -1.740  -2.862  27.857 1.00 38.35  ? 1447 THR B N     1 
ATOM   5513 C  CA    . THR B 1 230 ? -2.848  -2.747  26.911 1.00 52.40  ? 1447 THR B CA    1 
ATOM   5514 C  C     . THR B 1 230 ? -3.042  -4.022  26.130 1.00 56.73  ? 1447 THR B C     1 
ATOM   5515 O  O     . THR B 1 230 ? -2.082  -4.698  25.750 1.00 66.31  ? 1447 THR B O     1 
ATOM   5516 C  CB    . THR B 1 230 ? -2.702  -1.699  25.778 1.00 47.80  ? 1447 THR B CB    1 
ATOM   5517 O  OG1   . THR B 1 230 ? -1.340  -1.628  25.301 1.00 40.25  ? 1447 THR B OG1   1 
ATOM   5518 C  CG2   . THR B 1 230 ? -3.242  -0.380  26.183 1.00 54.36  ? 1447 THR B CG2   1 
ATOM   5519 N  N     . SER B 1 231 ? -4.302  -4.260  25.804 1.00 44.24  ? 1448 SER B N     1 
ATOM   5520 C  CA    . SER B 1 231 ? -4.703  -5.305  24.882 1.00 43.02  ? 1448 SER B CA    1 
ATOM   5521 C  C     . SER B 1 231 ? -5.723  -4.652  23.961 1.00 47.64  ? 1448 SER B C     1 
ATOM   5522 O  O     . SER B 1 231 ? -6.786  -4.228  24.426 1.00 45.41  ? 1448 SER B O     1 
ATOM   5523 C  CB    . SER B 1 231 ? -5.285  -6.498  25.630 1.00 53.13  ? 1448 SER B CB    1 
ATOM   5524 O  OG    . SER B 1 231 ? -5.049  -7.697  24.928 1.00 60.11  ? 1448 SER B OG    1 
ATOM   5525 N  N     . HIS B 1 232 ? -5.379  -4.490  22.684 1.00 54.89  ? 1449 HIS B N     1 
ATOM   5526 C  CA    . HIS B 1 232 ? -6.286  -3.891  21.714 1.00 49.73  ? 1449 HIS B CA    1 
ATOM   5527 C  C     . HIS B 1 232 ? -6.906  -4.989  20.880 1.00 43.24  ? 1449 HIS B C     1 
ATOM   5528 O  O     . HIS B 1 232 ? -6.328  -6.069  20.723 1.00 35.51  ? 1449 HIS B O     1 
ATOM   5529 C  CB    . HIS B 1 232 ? -5.613  -2.905  20.752 1.00 43.15  ? 1449 HIS B CB    1 
ATOM   5530 C  CG    . HIS B 1 232 ? -4.562  -2.068  21.381 1.00 42.89  ? 1449 HIS B CG    1 
ATOM   5531 N  ND1   . HIS B 1 232 ? -4.856  -1.024  22.221 1.00 42.38  ? 1449 HIS B ND1   1 
ATOM   5532 C  CD2   . HIS B 1 232 ? -3.211  -2.131  21.311 1.00 49.68  ? 1449 HIS B CD2   1 
ATOM   5533 C  CE1   . HIS B 1 232 ? -3.731  -0.475  22.644 1.00 50.07  ? 1449 HIS B CE1   1 
ATOM   5534 N  NE2   . HIS B 1 232 ? -2.717  -1.128  22.105 1.00 49.94  ? 1449 HIS B NE2   1 
ATOM   5535 N  N     . HIS B 1 233 ? -8.107  -4.699  20.372 1.00 41.56  ? 1450 HIS B N     1 
ATOM   5536 C  CA    . HIS B 1 233 ? -8.703  -5.444  19.271 1.00 46.53  ? 1450 HIS B CA    1 
ATOM   5537 C  C     . HIS B 1 233 ? -8.568  -4.569  18.044 1.00 39.10  ? 1450 HIS B C     1 
ATOM   5538 O  O     . HIS B 1 233 ? -9.151  -3.493  17.987 1.00 38.71  ? 1450 HIS B O     1 
ATOM   5539 C  CB    . HIS B 1 233 ? -10.161 -5.784  19.516 1.00 55.08  ? 1450 HIS B CB    1 
ATOM   5540 C  CG    . HIS B 1 233 ? -10.850 -6.321  18.308 1.00 68.24  ? 1450 HIS B CG    1 
ATOM   5541 N  ND1   . HIS B 1 233 ? -10.340 -7.363  17.568 1.00 73.73  ? 1450 HIS B ND1   1 
ATOM   5542 C  CD2   . HIS B 1 233 ? -12.008 -5.963  17.704 1.00 75.33  ? 1450 HIS B CD2   1 
ATOM   5543 C  CE1   . HIS B 1 233 ? -11.159 -7.633  16.566 1.00 77.04  ? 1450 HIS B CE1   1 
ATOM   5544 N  NE2   . HIS B 1 233 ? -12.180 -6.797  16.624 1.00 75.87  ? 1450 HIS B NE2   1 
ATOM   5545 N  N     . LEU B 1 234 ? -7.767  -5.013  17.087 1.00 38.17  ? 1451 LEU B N     1 
ATOM   5546 C  CA    . LEU B 1 234 ? -7.496  -4.215  15.910 1.00 36.72  ? 1451 LEU B CA    1 
ATOM   5547 C  C     . LEU B 1 234 ? -8.611  -4.307  14.902 1.00 47.08  ? 1451 LEU B C     1 
ATOM   5548 O  O     . LEU B 1 234 ? -8.781  -3.382  14.095 1.00 49.31  ? 1451 LEU B O     1 
ATOM   5549 C  CB    . LEU B 1 234 ? -6.195  -4.688  15.270 1.00 30.95  ? 1451 LEU B CB    1 
ATOM   5550 C  CG    . LEU B 1 234 ? -5.058  -4.671  16.261 1.00 42.39  ? 1451 LEU B CG    1 
ATOM   5551 C  CD1   . LEU B 1 234 ? -3.792  -4.884  15.497 1.00 53.79  ? 1451 LEU B CD1   1 
ATOM   5552 C  CD2   . LEU B 1 234 ? -5.033  -3.316  16.982 1.00 46.13  ? 1451 LEU B CD2   1 
ATOM   5553 N  N     . GLY B 1 235 ? -9.393  -5.380  14.973 1.00 45.73  ? 1452 GLY B N     1 
ATOM   5554 C  CA    . GLY B 1 235 ? -10.441 -5.582  13.984 1.00 33.29  ? 1452 GLY B CA    1 
ATOM   5555 C  C     . GLY B 1 235 ? -9.813  -5.832  12.626 1.00 48.04  ? 1452 GLY B C     1 
ATOM   5556 O  O     . GLY B 1 235 ? -8.789  -6.518  12.505 1.00 57.96  ? 1452 GLY B O     1 
ATOM   5557 N  N     . GLN B 1 236 ? -10.375 -5.216  11.592 1.00 46.94  ? 1453 GLN B N     1 
ATOM   5558 C  CA    . GLN B 1 236 ? -9.872  -5.436  10.244 1.00 53.51  ? 1453 GLN B CA    1 
ATOM   5559 C  C     . GLN B 1 236 ? -9.149  -4.224  9.696  1.00 54.52  ? 1453 GLN B C     1 
ATOM   5560 O  O     . GLN B 1 236 ? -8.888  -4.161  8.491  1.00 46.93  ? 1453 GLN B O     1 
ATOM   5561 C  CB    . GLN B 1 236 ? -11.008 -5.845  9.309  1.00 57.66  ? 1453 GLN B CB    1 
ATOM   5562 C  CG    . GLN B 1 236 ? -11.338 -7.330  9.373  1.00 56.04  ? 1453 GLN B CG    1 
ATOM   5563 C  CD    . GLN B 1 236 ? -12.548 -7.690  8.540  1.00 59.68  ? 1453 GLN B CD    1 
ATOM   5564 O  OE1   . GLN B 1 236 ? -13.576 -7.011  8.587  1.00 46.94  ? 1453 GLN B OE1   1 
ATOM   5565 N  NE2   . GLN B 1 236 ? -12.434 -8.769  7.766  1.00 72.89  ? 1453 GLN B NE2   1 
ATOM   5566 N  N     . ASN B 1 237 ? -8.814  -3.270  10.566 1.00 65.69  ? 1454 ASN B N     1 
ATOM   5567 C  CA    . ASN B 1 237 ? -8.190  -2.022  10.146 1.00 71.16  ? 1454 ASN B CA    1 
ATOM   5568 C  C     . ASN B 1 237 ? -6.834  -2.269  9.501  1.00 66.67  ? 1454 ASN B C     1 
ATOM   5569 O  O     . ASN B 1 237 ? -6.571  -1.849  8.364  1.00 80.66  ? 1454 ASN B O     1 
ATOM   5570 C  CB    . ASN B 1 237 ? -8.066  -1.098  11.355 1.00 78.43  ? 1454 ASN B CB    1 
ATOM   5571 C  CG    . ASN B 1 237 ? -9.422  -0.710  11.938 1.00 87.00  ? 1454 ASN B CG    1 
ATOM   5572 O  OD1   . ASN B 1 237 ? -10.170 -1.565  12.413 1.00 93.78  ? 1454 ASN B OD1   1 
ATOM   5573 N  ND2   . ASN B 1 237 ? -9.742  0.583   11.901 1.00 90.35  ? 1454 ASN B ND2   1 
ATOM   5574 N  N     . PHE B 1 238 ? -5.953  -2.951  10.219 1.00 52.71  ? 1455 PHE B N     1 
ATOM   5575 C  CA    . PHE B 1 238 ? -4.608  -3.147  9.701  1.00 44.04  ? 1455 PHE B CA    1 
ATOM   5576 C  C     . PHE B 1 238 ? -4.615  -4.147  8.561  1.00 42.98  ? 1455 PHE B C     1 
ATOM   5577 O  O     . PHE B 1 238 ? -3.926  -3.944  7.555  1.00 45.07  ? 1455 PHE B O     1 
ATOM   5578 C  CB    . PHE B 1 238 ? -3.667  -3.614  10.814 1.00 39.56  ? 1455 PHE B CB    1 
ATOM   5579 C  CG    . PHE B 1 238 ? -3.218  -2.517  11.739 1.00 46.13  ? 1455 PHE B CG    1 
ATOM   5580 C  CD1   . PHE B 1 238 ? -3.974  -2.169  12.846 1.00 52.55  ? 1455 PHE B CD1   1 
ATOM   5581 C  CD2   . PHE B 1 238 ? -2.034  -1.835  11.511 1.00 44.54  ? 1455 PHE B CD2   1 
ATOM   5582 C  CE1   . PHE B 1 238 ? -3.566  -1.161  13.699 1.00 47.57  ? 1455 PHE B CE1   1 
ATOM   5583 C  CE2   . PHE B 1 238 ? -1.617  -0.841  12.369 1.00 35.77  ? 1455 PHE B CE2   1 
ATOM   5584 C  CZ    . PHE B 1 238 ? -2.386  -0.508  13.465 1.00 37.93  ? 1455 PHE B CZ    1 
ATOM   5585 N  N     . SER B 1 239 ? -5.428  -5.206  8.672  1.00 40.07  ? 1456 SER B N     1 
ATOM   5586 C  CA    . SER B 1 239 ? -5.489  -6.193  7.595  1.00 43.62  ? 1456 SER B CA    1 
ATOM   5587 C  C     . SER B 1 239 ? -5.914  -5.541  6.296  1.00 47.29  ? 1456 SER B C     1 
ATOM   5588 O  O     . SER B 1 239 ? -5.567  -6.032  5.218  1.00 53.53  ? 1456 SER B O     1 
ATOM   5589 C  CB    . SER B 1 239 ? -6.406  -7.387  7.957  1.00 51.00  ? 1456 SER B CB    1 
ATOM   5590 O  OG    . SER B 1 239 ? -7.678  -7.046  8.507  1.00 54.23  ? 1456 SER B OG    1 
ATOM   5591 N  N     . ARG B 1 240 ? -6.628  -4.421  6.382  1.00 46.78  ? 1457 ARG B N     1 
ATOM   5592 C  CA    . ARG B 1 240 ? -6.889  -3.628  5.193  1.00 52.94  ? 1457 ARG B CA    1 
ATOM   5593 C  C     . ARG B 1 240 ? -5.666  -2.799  4.828  1.00 50.55  ? 1457 ARG B C     1 
ATOM   5594 O  O     . ARG B 1 240 ? -5.299  -2.712  3.650  1.00 56.57  ? 1457 ARG B O     1 
ATOM   5595 C  CB    . ARG B 1 240 ? -8.101  -2.732  5.421  1.00 61.72  ? 1457 ARG B CB    1 
ATOM   5596 C  CG    . ARG B 1 240 ? -9.375  -3.332  4.900  1.00 76.06  ? 1457 ARG B CG    1 
ATOM   5597 C  CD    . ARG B 1 240 ? -10.523 -3.153  5.853  1.00 82.50  ? 1457 ARG B CD    1 
ATOM   5598 N  NE    . ARG B 1 240 ? -11.618 -4.026  5.459  1.00 87.67  ? 1457 ARG B NE    1 
ATOM   5599 C  CZ    . ARG B 1 240 ? -12.677 -4.275  6.213  1.00 86.76  ? 1457 ARG B CZ    1 
ATOM   5600 N  NH1   . ARG B 1 240 ? -12.783 -3.700  7.407  1.00 91.18  ? 1457 ARG B NH1   1 
ATOM   5601 N  NH2   . ARG B 1 240 ? -13.623 -5.096  5.776  1.00 78.07  ? 1457 ARG B NH2   1 
ATOM   5602 N  N     . MET B 1 241 ? -5.020  -2.190  5.821  1.00 40.00  ? 1458 MET B N     1 
ATOM   5603 C  CA    . MET B 1 241 ? -3.818  -1.420  5.530  1.00 46.17  ? 1458 MET B CA    1 
ATOM   5604 C  C     . MET B 1 241 ? -2.768  -2.282  4.837  1.00 49.68  ? 1458 MET B C     1 
ATOM   5605 O  O     . MET B 1 241 ? -2.305  -1.953  3.743  1.00 45.24  ? 1458 MET B O     1 
ATOM   5606 C  CB    . MET B 1 241 ? -3.249  -0.827  6.822  1.00 63.14  ? 1458 MET B CB    1 
ATOM   5607 C  CG    . MET B 1 241 ? -3.767  0.562   7.194  1.00 79.82  ? 1458 MET B CG    1 
ATOM   5608 S  SD    . MET B 1 241 ? -2.577  1.491   8.214  1.00 88.70  ? 1458 MET B SD    1 
ATOM   5609 C  CE    . MET B 1 241 ? -1.320  2.056   7.053  1.00 81.21  ? 1458 MET B CE    1 
ATOM   5610 N  N     . PHE B 1 242 ? -2.426  -3.428  5.432  1.00 61.16  ? 1459 PHE B N     1 
ATOM   5611 C  CA    . PHE B 1 242 ? -1.301  -4.240  4.986  1.00 57.33  ? 1459 PHE B CA    1 
ATOM   5612 C  C     . PHE B 1 242 ? -1.703  -5.454  4.163  1.00 61.59  ? 1459 PHE B C     1 
ATOM   5613 O  O     . PHE B 1 242 ? -0.830  -6.217  3.742  1.00 60.01  ? 1459 PHE B O     1 
ATOM   5614 C  CB    . PHE B 1 242 ? -0.495  -4.675  6.185  1.00 48.06  ? 1459 PHE B CB    1 
ATOM   5615 C  CG    . PHE B 1 242 ? 0.190   -3.541  6.846  1.00 48.64  ? 1459 PHE B CG    1 
ATOM   5616 C  CD1   . PHE B 1 242 ? 1.414   -3.118  6.386  1.00 40.16  ? 1459 PHE B CD1   1 
ATOM   5617 C  CD2   . PHE B 1 242 ? -0.399  -2.858  7.895  1.00 48.06  ? 1459 PHE B CD2   1 
ATOM   5618 C  CE1   . PHE B 1 242 ? 2.046   -2.084  6.965  1.00 35.01  ? 1459 PHE B CE1   1 
ATOM   5619 C  CE2   . PHE B 1 242 ? 0.250   -1.806  8.484  1.00 31.76  ? 1459 PHE B CE2   1 
ATOM   5620 C  CZ    . PHE B 1 242 ? 1.466   -1.430  8.017  1.00 31.77  ? 1459 PHE B CZ    1 
ATOM   5621 N  N     . ASP B 1 243 ? -2.989  -5.587  3.881  1.00 60.46  ? 1460 ASP B N     1 
ATOM   5622 C  CA    . ASP B 1 243 ? -3.525  -6.449  2.861  1.00 62.20  ? 1460 ASP B CA    1 
ATOM   5623 C  C     . ASP B 1 243 ? -3.292  -7.914  3.247  1.00 65.59  ? 1460 ASP B C     1 
ATOM   5624 O  O     . ASP B 1 243 ? -2.981  -8.789  2.408  1.00 40.83  ? 1460 ASP B O     1 
ATOM   5625 C  CB    . ASP B 1 243 ? -2.861  -6.125  1.529  1.00 75.94  ? 1460 ASP B CB    1 
ATOM   5626 C  CG    . ASP B 1 243 ? -3.238  -4.730  1.043  1.00 97.93  ? 1460 ASP B CG    1 
ATOM   5627 O  OD1   . ASP B 1 243 ? -4.437  -4.367  1.011  1.00 108.22 ? 1460 ASP B OD1   1 
ATOM   5628 O  OD2   . ASP B 1 243 ? -2.242  -4.015  0.684  1.00 108.30 ? 1460 ASP B OD2   1 
ATOM   5629 N  N     . ILE B 1 244 ? -3.512  -8.191  4.532  1.00 78.28  ? 1461 ILE B N     1 
ATOM   5630 C  CA    . ILE B 1 244 ? -3.460  -9.519  5.124  1.00 76.54  ? 1461 ILE B CA    1 
ATOM   5631 C  C     . ILE B 1 244 ? -4.807  -10.142 4.842  1.00 65.71  ? 1461 ILE B C     1 
ATOM   5632 O  O     . ILE B 1 244 ? -5.774  -9.931  5.578  1.00 60.24  ? 1461 ILE B O     1 
ATOM   5633 C  CB    . ILE B 1 244 ? -3.161  -9.445  6.638  1.00 73.06  ? 1461 ILE B CB    1 
ATOM   5634 C  CG1   . ILE B 1 244 ? -2.085  -8.380  6.898  1.00 64.44  ? 1461 ILE B CG1   1 
ATOM   5635 C  CG2   . ILE B 1 244 ? -2.791  -10.861 7.219  1.00 70.93  ? 1461 ILE B CG2   1 
ATOM   5636 C  CD1   . ILE B 1 244 ? -1.762  -8.164  8.344  1.00 60.20  ? 1461 ILE B CD1   1 
ATOM   5637 N  N     . VAL B 1 245 ? -4.884  -10.886 3.753  1.00 69.85  ? 1462 VAL B N     1 
ATOM   5638 C  CA    . VAL B 1 245 ? -6.150  -11.396 3.272  1.00 67.87  ? 1462 VAL B CA    1 
ATOM   5639 C  C     . VAL B 1 245 ? -5.959  -12.862 2.942  1.00 65.19  ? 1462 VAL B C     1 
ATOM   5640 O  O     . VAL B 1 245 ? -4.843  -13.369 2.867  1.00 63.10  ? 1462 VAL B O     1 
ATOM   5641 C  CB    . VAL B 1 245 ? -6.669  -10.626 2.043  1.00 58.72  ? 1462 VAL B CB    1 
ATOM   5642 C  CG1   . VAL B 1 245 ? -7.172  -9.288  2.455  1.00 61.16  ? 1462 VAL B CG1   1 
ATOM   5643 C  CG2   . VAL B 1 245 ? -5.558  -10.460 1.047  1.00 51.87  ? 1462 VAL B CG2   1 
ATOM   5644 N  N     . TYR B 1 246 ? -7.080  -13.541 2.770  1.00 72.82  ? 1463 TYR B N     1 
ATOM   5645 C  CA    . TYR B 1 246 ? -7.094  -14.910 2.287  1.00 69.19  ? 1463 TYR B CA    1 
ATOM   5646 C  C     . TYR B 1 246 ? -8.421  -15.101 1.568  1.00 63.32  ? 1463 TYR B C     1 
ATOM   5647 O  O     . TYR B 1 246 ? -9.393  -14.373 1.807  1.00 44.09  ? 1463 TYR B O     1 
ATOM   5648 C  CB    . TYR B 1 246 ? -6.931  -15.915 3.428  1.00 61.76  ? 1463 TYR B CB    1 
ATOM   5649 C  CG    . TYR B 1 246 ? -8.111  -15.840 4.339  1.00 58.54  ? 1463 TYR B CG    1 
ATOM   5650 C  CD1   . TYR B 1 246 ? -9.081  -16.815 4.327  1.00 54.39  ? 1463 TYR B CD1   1 
ATOM   5651 C  CD2   . TYR B 1 246 ? -8.283  -14.751 5.176  1.00 64.69  ? 1463 TYR B CD2   1 
ATOM   5652 C  CE1   . TYR B 1 246 ? -10.179 -16.719 5.146  1.00 58.42  ? 1463 TYR B CE1   1 
ATOM   5653 C  CE2   . TYR B 1 246 ? -9.374  -14.644 5.987  1.00 64.20  ? 1463 TYR B CE2   1 
ATOM   5654 C  CZ    . TYR B 1 246 ? -10.319 -15.629 5.974  1.00 59.84  ? 1463 TYR B CZ    1 
ATOM   5655 O  OH    . TYR B 1 246 ? -11.402 -15.508 6.807  1.00 63.53  ? 1463 TYR B OH    1 
ATOM   5656 N  N     . GLU B 1 247 ? -8.463  -16.093 0.692  1.00 67.08  ? 1464 GLU B N     1 
ATOM   5657 C  CA    . GLU B 1 247 ? -9.684  -16.384 -0.036 1.00 58.38  ? 1464 GLU B CA    1 
ATOM   5658 C  C     . GLU B 1 247 ? -10.543 -17.329 0.781  1.00 62.98  ? 1464 GLU B C     1 
ATOM   5659 O  O     . GLU B 1 247 ? -10.033 -18.245 1.440  1.00 62.49  ? 1464 GLU B O     1 
ATOM   5660 C  CB    . GLU B 1 247 ? -9.364  -16.975 -1.399 1.00 58.60  ? 1464 GLU B CB    1 
ATOM   5661 N  N     . HIS B 1 248 ? -11.841 -17.073 0.777  1.00 64.00  ? 1465 HIS B N     1 
ATOM   5662 C  CA    . HIS B 1 248 ? -12.709 -17.924 1.557  1.00 73.77  ? 1465 HIS B CA    1 
ATOM   5663 C  C     . HIS B 1 248 ? -12.639 -19.345 1.008  1.00 85.60  ? 1465 HIS B C     1 
ATOM   5664 O  O     . HIS B 1 248 ? -12.679 -19.543 -0.216 1.00 91.21  ? 1465 HIS B O     1 
ATOM   5665 C  CB    . HIS B 1 248 ? -14.142 -17.414 1.498  1.00 77.67  ? 1465 HIS B CB    1 
ATOM   5666 C  CG    . HIS B 1 248 ? -14.925 -17.729 2.723  1.00 83.11  ? 1465 HIS B CG    1 
ATOM   5667 N  ND1   . HIS B 1 248 ? -15.642 -18.894 2.864  1.00 86.69  ? 1465 HIS B ND1   1 
ATOM   5668 C  CD2   . HIS B 1 248 ? -15.088 -17.041 3.877  1.00 84.86  ? 1465 HIS B CD2   1 
ATOM   5669 C  CE1   . HIS B 1 248 ? -16.218 -18.911 4.053  1.00 86.52  ? 1465 HIS B CE1   1 
ATOM   5670 N  NE2   . HIS B 1 248 ? -15.903 -17.794 4.684  1.00 84.57  ? 1465 HIS B NE2   1 
ATOM   5671 N  N     . PRO B 1 249 ? -12.561 -20.354 1.878  1.00 78.62  ? 1466 PRO B N     1 
ATOM   5672 C  CA    . PRO B 1 249 ? -12.468 -21.736 1.385  1.00 79.68  ? 1466 PRO B CA    1 
ATOM   5673 C  C     . PRO B 1 249 ? -13.656 -22.113 0.525  1.00 94.36  ? 1466 PRO B C     1 
ATOM   5674 O  O     . PRO B 1 249 ? -13.492 -22.587 -0.608 1.00 101.10 ? 1466 PRO B O     1 
ATOM   5675 C  CB    . PRO B 1 249 ? -12.420 -22.560 2.678  1.00 80.05  ? 1466 PRO B CB    1 
ATOM   5676 C  CG    . PRO B 1 249 ? -12.077 -21.585 3.755  1.00 72.97  ? 1466 PRO B CG    1 
ATOM   5677 C  CD    . PRO B 1 249 ? -12.591 -20.271 3.343  1.00 71.51  ? 1466 PRO B CD    1 
ATOM   5678 N  N     . GLU B 1 250 ? -14.860 -21.876 1.031  1.00 98.39  ? 1467 GLU B N     1 
ATOM   5679 C  CA    . GLU B 1 250 ? -16.090 -22.042 0.283  1.00 94.89  ? 1467 GLU B CA    1 
ATOM   5680 C  C     . GLU B 1 250 ? -16.575 -20.647 -0.082 1.00 96.77  ? 1467 GLU B C     1 
ATOM   5681 O  O     . GLU B 1 250 ? -16.348 -19.687 0.661  1.00 95.66  ? 1467 GLU B O     1 
ATOM   5682 C  CB    . GLU B 1 250 ? -17.145 -22.800 1.097  1.00 89.77  ? 1467 GLU B CB    1 
ATOM   5683 N  N     . THR B 1 251 ? -17.193 -20.528 -1.253 1.00 97.91  ? 1468 THR B N     1 
ATOM   5684 C  CA    . THR B 1 251 ? -17.659 -19.238 -1.764 1.00 98.26  ? 1468 THR B CA    1 
ATOM   5685 C  C     . THR B 1 251 ? -16.510 -18.237 -1.808 1.00 92.80  ? 1468 THR B C     1 
ATOM   5686 O  O     . THR B 1 251 ? -16.599 -17.121 -1.286 1.00 77.33  ? 1468 THR B O     1 
ATOM   5687 C  CB    . THR B 1 251 ? -18.819 -18.690 -0.927 1.00 102.71 ? 1468 THR B CB    1 
ATOM   5688 N  N     . LYS B 1 252 ? -15.440 -18.664 -2.489 1.00 104.79 ? 1469 LYS B N     1 
ATOM   5689 C  CA    . LYS B 1 252 ? -14.163 -17.960 -2.489 1.00 104.53 ? 1469 LYS B CA    1 
ATOM   5690 C  C     . LYS B 1 252 ? -14.344 -16.493 -2.826 1.00 100.41 ? 1469 LYS B C     1 
ATOM   5691 O  O     . LYS B 1 252 ? -14.881 -16.140 -3.880 1.00 99.80  ? 1469 LYS B O     1 
ATOM   5692 C  CB    . LYS B 1 252 ? -13.191 -18.618 -3.469 1.00 103.47 ? 1469 LYS B CB    1 
ATOM   5693 C  CG    . LYS B 1 252 ? -11.733 -18.366 -3.136 1.00 100.97 ? 1469 LYS B CG    1 
ATOM   5694 C  CD    . LYS B 1 252 ? -10.788 -19.228 -3.978 1.00 99.98  ? 1469 LYS B CD    1 
ATOM   5695 C  CE    . LYS B 1 252 ? -9.577  -19.781 -3.197 1.00 86.83  ? 1469 LYS B CE    1 
ATOM   5696 N  NZ    . LYS B 1 252 ? -9.894  -20.571 -1.963 1.00 76.36  ? 1469 LYS B NZ    1 
ATOM   5697 N  N     . GLU B 1 253 ? -13.914 -15.658 -1.891 1.00 89.69  ? 1470 GLU B N     1 
ATOM   5698 C  CA    . GLU B 1 253 ? -14.032 -14.215 -1.936 1.00 81.29  ? 1470 GLU B CA    1 
ATOM   5699 C  C     . GLU B 1 253 ? -13.004 -13.694 -0.943 1.00 80.47  ? 1470 GLU B C     1 
ATOM   5700 O  O     . GLU B 1 253 ? -12.674 -14.375 0.034  1.00 76.21  ? 1470 GLU B O     1 
ATOM   5701 C  CB    . GLU B 1 253 ? -15.455 -13.742 -1.596 1.00 76.30  ? 1470 GLU B CB    1 
ATOM   5702 N  N     . LYS B 1 254 ? -12.467 -12.509 -1.229 1.00 77.77  ? 1471 LYS B N     1 
ATOM   5703 C  CA    . LYS B 1 254 ? -11.344 -11.965 -0.474 1.00 72.78  ? 1471 LYS B CA    1 
ATOM   5704 C  C     . LYS B 1 254 ? -11.808 -11.561 0.916  1.00 71.55  ? 1471 LYS B C     1 
ATOM   5705 O  O     . LYS B 1 254 ? -12.578 -10.604 1.067  1.00 68.32  ? 1471 LYS B O     1 
ATOM   5706 C  CB    . LYS B 1 254 ? -10.754 -10.767 -1.216 1.00 76.73  ? 1471 LYS B CB    1 
ATOM   5707 C  CG    . LYS B 1 254 ? -9.583  -10.044 -0.507 1.00 71.15  ? 1471 LYS B CG    1 
ATOM   5708 C  CD    . LYS B 1 254 ? -9.377  -8.601  -1.005 1.00 61.72  ? 1471 LYS B CD    1 
ATOM   5709 C  CE    . LYS B 1 254 ? -8.642  -8.580  -2.333 1.00 62.35  ? 1471 LYS B CE    1 
ATOM   5710 N  NZ    . LYS B 1 254 ? -7.450  -7.702  -2.266 1.00 72.60  ? 1471 LYS B NZ    1 
ATOM   5711 N  N     . GLU B 1 255 ? -11.302 -12.255 1.934  1.00 71.04  ? 1472 GLU B N     1 
ATOM   5712 C  CA    . GLU B 1 255 ? -11.625 -11.971 3.319  1.00 73.41  ? 1472 GLU B CA    1 
ATOM   5713 C  C     . GLU B 1 255 ? -10.411 -11.420 4.057  1.00 75.65  ? 1472 GLU B C     1 
ATOM   5714 O  O     . GLU B 1 255 ? -9.296  -11.936 3.915  1.00 79.07  ? 1472 GLU B O     1 
ATOM   5715 C  CB    . GLU B 1 255 ? -12.128 -13.241 3.992  1.00 68.13  ? 1472 GLU B CB    1 
ATOM   5716 C  CG    . GLU B 1 255 ? -13.391 -13.761 3.352  1.00 75.74  ? 1472 GLU B CG    1 
ATOM   5717 C  CD    . GLU B 1 255 ? -14.636 -13.281 4.057  1.00 88.15  ? 1472 GLU B CD    1 
ATOM   5718 O  OE1   . GLU B 1 255 ? -14.947 -13.865 5.115  1.00 94.73  ? 1472 GLU B OE1   1 
ATOM   5719 O  OE2   . GLU B 1 255 ? -15.306 -12.343 3.553  1.00 92.19  ? 1472 GLU B OE2   1 
ATOM   5720 N  N     . TYR B 1 256 ? -10.641 -10.393 4.870  1.00 69.16  ? 1473 TYR B N     1 
ATOM   5721 C  CA    . TYR B 1 256 ? -9.594  -9.794  5.680  1.00 63.66  ? 1473 TYR B CA    1 
ATOM   5722 C  C     . TYR B 1 256 ? -9.621  -10.401 7.079  1.00 63.14  ? 1473 TYR B C     1 
ATOM   5723 O  O     . TYR B 1 256 ? -10.687 -10.593 7.674  1.00 67.14  ? 1473 TYR B O     1 
ATOM   5724 C  CB    . TYR B 1 256 ? -9.763  -8.274  5.763  1.00 68.06  ? 1473 TYR B CB    1 
ATOM   5725 C  CG    . TYR B 1 256 ? -9.663  -7.538  4.432  1.00 71.40  ? 1473 TYR B CG    1 
ATOM   5726 C  CD1   . TYR B 1 256 ? -8.539  -6.779  4.102  1.00 71.19  ? 1473 TYR B CD1   1 
ATOM   5727 C  CD2   . TYR B 1 256 ? -10.706 -7.587  3.516  1.00 71.05  ? 1473 TYR B CD2   1 
ATOM   5728 C  CE1   . TYR B 1 256 ? -8.461  -6.108  2.877  1.00 75.53  ? 1473 TYR B CE1   1 
ATOM   5729 C  CE2   . TYR B 1 256 ? -10.640 -6.923  2.302  1.00 66.67  ? 1473 TYR B CE2   1 
ATOM   5730 C  CZ    . TYR B 1 256 ? -9.526  -6.190  1.979  1.00 75.17  ? 1473 TYR B CZ    1 
ATOM   5731 O  OH    . TYR B 1 256 ? -9.500  -5.543  0.757  1.00 81.26  ? 1473 TYR B OH    1 
ATOM   5732 N  N     . VAL B 1 257 ? -8.442  -10.680 7.607  1.00 52.92  ? 1474 VAL B N     1 
ATOM   5733 C  CA    . VAL B 1 257 ? -8.342  -11.318 8.905  1.00 41.48  ? 1474 VAL B CA    1 
ATOM   5734 C  C     . VAL B 1 257 ? -8.599  -10.300 10.009 1.00 51.65  ? 1474 VAL B C     1 
ATOM   5735 O  O     . VAL B 1 257 ? -8.576  -9.079  9.798  1.00 54.95  ? 1474 VAL B O     1 
ATOM   5736 C  CB    . VAL B 1 257 ? -6.970  -11.972 9.061  1.00 41.74  ? 1474 VAL B CB    1 
ATOM   5737 C  CG1   . VAL B 1 257 ? -6.728  -12.892 7.896  1.00 47.31  ? 1474 VAL B CG1   1 
ATOM   5738 C  CG2   . VAL B 1 257 ? -5.912  -10.900 9.104  1.00 40.03  ? 1474 VAL B CG2   1 
ATOM   5739 N  N     . PHE B 1 258 ? -8.856  -10.818 11.205 1.00 33.64  ? 1475 PHE B N     1 
ATOM   5740 C  CA    . PHE B 1 258 ? -9.109  -9.996  12.377 1.00 38.47  ? 1475 PHE B CA    1 
ATOM   5741 C  C     . PHE B 1 258 ? -7.885  -10.029 13.260 1.00 45.22  ? 1475 PHE B C     1 
ATOM   5742 O  O     . PHE B 1 258 ? -7.345  -11.101 13.540 1.00 46.10  ? 1475 PHE B O     1 
ATOM   5743 C  CB    . PHE B 1 258 ? -10.322 -10.486 13.171 1.00 51.33  ? 1475 PHE B CB    1 
ATOM   5744 C  CG    . PHE B 1 258 ? -11.616 -10.178 12.519 1.00 55.85  ? 1475 PHE B CG    1 
ATOM   5745 C  CD1   . PHE B 1 258 ? -12.288 -9.003  12.815 1.00 57.62  ? 1475 PHE B CD1   1 
ATOM   5746 C  CD2   . PHE B 1 258 ? -12.145 -11.047 11.578 1.00 46.27  ? 1475 PHE B CD2   1 
ATOM   5747 C  CE1   . PHE B 1 258 ? -13.472 -8.708  12.201 1.00 58.67  ? 1475 PHE B CE1   1 
ATOM   5748 C  CE2   . PHE B 1 258 ? -13.316 -10.760 10.957 1.00 48.70  ? 1475 PHE B CE2   1 
ATOM   5749 C  CZ    . PHE B 1 258 ? -13.995 -9.595  11.268 1.00 59.66  ? 1475 PHE B CZ    1 
ATOM   5750 N  N     . GLN B 1 259 ? -7.487  -8.869  13.753 1.00 44.20  ? 1476 GLN B N     1 
ATOM   5751 C  CA    . GLN B 1 259 ? -6.210  -8.777  14.423 1.00 35.91  ? 1476 GLN B CA    1 
ATOM   5752 C  C     . GLN B 1 259 ? -6.401  -8.211  15.801 1.00 30.83  ? 1476 GLN B C     1 
ATOM   5753 O  O     . GLN B 1 259 ? -7.377  -7.494  16.055 1.00 36.44  ? 1476 GLN B O     1 
ATOM   5754 C  CB    . GLN B 1 259 ? -5.240  -7.915  13.662 1.00 42.25  ? 1476 GLN B CB    1 
ATOM   5755 C  CG    . GLN B 1 259 ? -4.654  -8.601  12.471 1.00 47.20  ? 1476 GLN B CG    1 
ATOM   5756 C  CD    . GLN B 1 259 ? -3.761  -7.686  11.703 1.00 53.70  ? 1476 GLN B CD    1 
ATOM   5757 O  OE1   . GLN B 1 259 ? -4.212  -6.990  10.795 1.00 42.41  ? 1476 GLN B OE1   1 
ATOM   5758 N  NE2   . GLN B 1 259 ? -2.479  -7.650  12.079 1.00 68.33  ? 1476 GLN B NE2   1 
ATOM   5759 N  N     . ASN B 1 260 ? -5.386  -8.441  16.594 1.00 30.24  ? 1477 ASN B N     1 
ATOM   5760 C  CA    . ASN B 1 260 ? -5.186  -7.975  17.932 1.00 29.81  ? 1477 ASN B CA    1 
ATOM   5761 C  C     . ASN B 1 260 ? -3.733  -7.728  18.157 1.00 38.31  ? 1477 ASN B C     1 
ATOM   5762 O  O     . ASN B 1 260 ? -2.943  -8.230  17.500 1.00 47.82  ? 1477 ASN B O     1 
ATOM   5763 C  CB    . ASN B 1 260 ? -5.401  -9.089  18.880 1.00 33.42  ? 1477 ASN B CB    1 
ATOM   5764 C  CG    . ASN B 1 260 ? -6.817  -9.426  19.111 1.00 48.55  ? 1477 ASN B CG    1 
ATOM   5765 O  OD1   . ASN B 1 260 ? -7.674  -8.701  18.803 1.00 55.08  ? 1477 ASN B OD1   1 
ATOM   5766 N  ND2   . ASN B 1 260 ? -7.047  -10.539 19.678 1.00 49.47  ? 1477 ASN B ND2   1 
ATOM   5767 N  N     . SER B 1 261 ? -3.381  -6.863  19.053 1.00 36.09  ? 1478 SER B N     1 
ATOM   5768 C  CA    . SER B 1 261 ? -2.016  -6.700  19.551 1.00 47.48  ? 1478 SER B CA    1 
ATOM   5769 C  C     . SER B 1 261 ? -2.099  -6.361  21.031 1.00 52.58  ? 1478 SER B C     1 
ATOM   5770 O  O     . SER B 1 261 ? -3.105  -5.836  21.499 1.00 64.23  ? 1478 SER B O     1 
ATOM   5771 C  CB    . SER B 1 261 ? -1.196  -5.634  18.778 1.00 48.08  ? 1478 SER B CB    1 
ATOM   5772 O  OG    . SER B 1 261 ? -1.858  -4.386  18.606 1.00 46.32  ? 1478 SER B OG    1 
ATOM   5773 N  N     . TRP B 1 262 ? -1.067  -6.727  21.779 1.00 56.33  ? 1479 TRP B N     1 
ATOM   5774 C  CA    . TRP B 1 262 ? -1.064  -6.458  23.215 1.00 56.04  ? 1479 TRP B CA    1 
ATOM   5775 C  C     . TRP B 1 262 ? 0.368   -6.282  23.695 1.00 52.47  ? 1479 TRP B C     1 
ATOM   5776 O  O     . TRP B 1 262 ? 1.316   -6.788  23.088 1.00 37.97  ? 1479 TRP B O     1 
ATOM   5777 C  CB    . TRP B 1 262 ? -1.761  -7.564  24.033 1.00 47.81  ? 1479 TRP B CB    1 
ATOM   5778 C  CG    . TRP B 1 262 ? -1.779  -8.922  23.388 1.00 48.93  ? 1479 TRP B CG    1 
ATOM   5779 C  CD1   . TRP B 1 262 ? -2.720  -9.403  22.537 1.00 28.29  ? 1479 TRP B CD1   1 
ATOM   5780 C  CD2   . TRP B 1 262 ? -0.817  -9.968  23.549 1.00 48.94  ? 1479 TRP B CD2   1 
ATOM   5781 N  NE1   . TRP B 1 262 ? -2.412  -10.662 22.161 1.00 28.33  ? 1479 TRP B NE1   1 
ATOM   5782 C  CE2   . TRP B 1 262 ? -1.246  -11.045 22.768 1.00 40.64  ? 1479 TRP B CE2   1 
ATOM   5783 C  CE3   . TRP B 1 262 ? 0.361   -10.100 24.282 1.00 50.30  ? 1479 TRP B CE3   1 
ATOM   5784 C  CZ2   . TRP B 1 262 ? -0.540  -12.247 22.697 1.00 27.86  ? 1479 TRP B CZ2   1 
ATOM   5785 C  CZ3   . TRP B 1 262 ? 1.057   -11.293 24.212 1.00 39.10  ? 1479 TRP B CZ3   1 
ATOM   5786 C  CH2   . TRP B 1 262 ? 0.611   -12.338 23.420 1.00 39.37  ? 1479 TRP B CH2   1 
ATOM   5787 N  N     . GLY B 1 263 ? 0.508   -5.613  24.840 1.00 55.16  ? 1480 GLY B N     1 
ATOM   5788 C  CA    . GLY B 1 263 ? 1.830   -5.328  25.346 1.00 51.49  ? 1480 GLY B CA    1 
ATOM   5789 C  C     . GLY B 1 263 ? 1.944   -4.972  26.816 1.00 43.46  ? 1480 GLY B C     1 
ATOM   5790 O  O     . GLY B 1 263 ? 1.029   -4.452  27.472 1.00 35.21  ? 1480 GLY B O     1 
ATOM   5791 N  N     . ILE B 1 264 ? 3.110   -5.302  27.359 1.00 41.59  ? 1481 ILE B N     1 
ATOM   5792 C  CA    . ILE B 1 264 ? 3.414   -4.925  28.734 1.00 36.65  ? 1481 ILE B CA    1 
ATOM   5793 C  C     . ILE B 1 264 ? 4.915   -4.750  28.856 1.00 36.50  ? 1481 ILE B C     1 
ATOM   5794 O  O     . ILE B 1 264 ? 5.693   -5.385  28.139 1.00 31.32  ? 1481 ILE B O     1 
ATOM   5795 C  CB    . ILE B 1 264 ? 2.857   -5.925  29.771 1.00 36.20  ? 1481 ILE B CB    1 
ATOM   5796 C  CG1   . ILE B 1 264 ? 2.561   -5.213  31.085 1.00 38.32  ? 1481 ILE B CG1   1 
ATOM   5797 C  CG2   . ILE B 1 264 ? 3.855   -6.977  30.108 1.00 37.93  ? 1481 ILE B CG2   1 
ATOM   5798 C  CD1   . ILE B 1 264 ? 2.076   -6.128  32.240 1.00 33.67  ? 1481 ILE B CD1   1 
ATOM   5799 N  N     . THR B 1 265 ? 5.315   -3.833  29.738 1.00 43.23  ? 1482 THR B N     1 
ATOM   5800 C  CA    . THR B 1 265 ? 6.698   -3.381  29.802 1.00 41.85  ? 1482 THR B CA    1 
ATOM   5801 C  C     . THR B 1 265 ? 7.297   -3.432  31.202 1.00 47.71  ? 1482 THR B C     1 
ATOM   5802 O  O     . THR B 1 265 ? 6.645   -3.822  32.172 1.00 62.86  ? 1482 THR B O     1 
ATOM   5803 C  CB    . THR B 1 265 ? 6.765   -1.943  29.303 1.00 38.99  ? 1482 THR B CB    1 
ATOM   5804 O  OG1   . THR B 1 265 ? 6.090   -1.120  30.252 1.00 35.29  ? 1482 THR B OG1   1 
ATOM   5805 C  CG2   . THR B 1 265 ? 6.078   -1.797  27.963 1.00 42.16  ? 1482 THR B CG2   1 
ATOM   5806 N  N     . THR B 1 266 ? 8.514   -2.935  31.326 1.00 37.46  ? 1483 THR B N     1 
ATOM   5807 C  CA    . THR B 1 266 ? 9.127   -2.783  32.630 1.00 36.02  ? 1483 THR B CA    1 
ATOM   5808 C  C     . THR B 1 266 ? 8.459   -1.705  33.472 1.00 47.92  ? 1483 THR B C     1 
ATOM   5809 O  O     . THR B 1 266 ? 8.830   -1.549  34.638 1.00 54.84  ? 1483 THR B O     1 
ATOM   5810 C  CB    . THR B 1 266 ? 10.567  -2.376  32.460 1.00 33.48  ? 1483 THR B CB    1 
ATOM   5811 O  OG1   . THR B 1 266 ? 10.548  -1.054  31.915 1.00 37.23  ? 1483 THR B OG1   1 
ATOM   5812 C  CG2   . THR B 1 266 ? 11.283  -3.310  31.507 1.00 34.00  ? 1483 THR B CG2   1 
ATOM   5813 N  N     . ARG B 1 267 ? 7.491   -0.959  32.931 1.00 46.89  ? 1484 ARG B N     1 
ATOM   5814 C  CA    . ARG B 1 267 ? 6.808   0.046   33.737 1.00 46.52  ? 1484 ARG B CA    1 
ATOM   5815 C  C     . ARG B 1 267 ? 6.274   -0.573  35.009 1.00 47.86  ? 1484 ARG B C     1 
ATOM   5816 O  O     . ARG B 1 267 ? 6.241   0.084   36.053 1.00 45.58  ? 1484 ARG B O     1 
ATOM   5817 C  CB    . ARG B 1 267 ? 5.670   0.679   32.933 1.00 44.15  ? 1484 ARG B CB    1 
ATOM   5818 C  CG    . ARG B 1 267 ? 4.780   1.658   33.700 1.00 27.95  ? 1484 ARG B CG    1 
ATOM   5819 C  CD    . ARG B 1 267 ? 3.728   2.247   32.776 1.00 31.23  ? 1484 ARG B CD    1 
ATOM   5820 N  NE    . ARG B 1 267 ? 4.264   3.343   31.972 1.00 52.27  ? 1484 ARG B NE    1 
ATOM   5821 C  CZ    . ARG B 1 267 ? 3.548   4.116   31.158 1.00 62.73  ? 1484 ARG B CZ    1 
ATOM   5822 N  NH1   . ARG B 1 267 ? 2.243   3.935   31.024 1.00 65.63  ? 1484 ARG B NH1   1 
ATOM   5823 N  NH2   . ARG B 1 267 ? 4.147   5.075   30.473 1.00 68.46  ? 1484 ARG B NH2   1 
ATOM   5824 N  N     . THR B 1 268 ? 5.952   -1.866  34.945 1.00 55.87  ? 1485 THR B N     1 
ATOM   5825 C  CA    . THR B 1 268 ? 5.536   -2.641  36.106 1.00 53.95  ? 1485 THR B CA    1 
ATOM   5826 C  C     . THR B 1 268 ? 6.400   -2.343  37.320 1.00 50.44  ? 1485 THR B C     1 
ATOM   5827 O  O     . THR B 1 268 ? 5.889   -2.012  38.399 1.00 53.66  ? 1485 THR B O     1 
ATOM   5828 C  CB    . THR B 1 268 ? 5.635   -4.116  35.752 1.00 52.16  ? 1485 THR B CB    1 
ATOM   5829 O  OG1   . THR B 1 268 ? 6.995   -4.409  35.423 1.00 52.59  ? 1485 THR B OG1   1 
ATOM   5830 C  CG2   . THR B 1 268 ? 4.803   -4.404  34.554 1.00 59.45  ? 1485 THR B CG2   1 
ATOM   5831 N  N     . ILE B 1 269 ? 7.721   -2.417  37.155 1.00 33.82  ? 1486 ILE B N     1 
ATOM   5832 C  CA    . ILE B 1 269 ? 8.599   -2.249  38.305 1.00 50.94  ? 1486 ILE B CA    1 
ATOM   5833 C  C     . ILE B 1 269 ? 8.351   -0.895  38.947 1.00 52.71  ? 1486 ILE B C     1 
ATOM   5834 O  O     . ILE B 1 269 ? 8.058   -0.800  40.152 1.00 47.04  ? 1486 ILE B O     1 
ATOM   5835 C  CB    . ILE B 1 269 ? 10.067  -2.435  37.885 1.00 44.00  ? 1486 ILE B CB    1 
ATOM   5836 C  CG1   . ILE B 1 269 ? 10.211  -3.848  37.318 1.00 35.03  ? 1486 ILE B CG1   1 
ATOM   5837 C  CG2   . ILE B 1 269 ? 10.988  -2.213  39.074 1.00 27.96  ? 1486 ILE B CG2   1 
ATOM   5838 C  CD1   . ILE B 1 269 ? 11.541  -4.199  36.757 1.00 35.20  ? 1486 ILE B CD1   1 
ATOM   5839 N  N     . GLY B 1 270 ? 8.309   0.149   38.117 1.00 45.74  ? 1487 GLY B N     1 
ATOM   5840 C  CA    . GLY B 1 270 ? 8.039   1.473   38.633 1.00 41.02  ? 1487 GLY B CA    1 
ATOM   5841 C  C     . GLY B 1 270 ? 6.731   1.525   39.382 1.00 37.84  ? 1487 GLY B C     1 
ATOM   5842 O  O     . GLY B 1 270 ? 6.672   2.029   40.509 1.00 35.65  ? 1487 GLY B O     1 
ATOM   5843 N  N     . VAL B 1 271 ? 5.683   0.922   38.813 1.00 35.96  ? 1488 VAL B N     1 
ATOM   5844 C  CA    . VAL B 1 271 ? 4.385   0.984   39.479 1.00 39.62  ? 1488 VAL B CA    1 
ATOM   5845 C  C     . VAL B 1 271 ? 4.478   0.292   40.828 1.00 40.56  ? 1488 VAL B C     1 
ATOM   5846 O  O     . VAL B 1 271 ? 4.055   0.846   41.854 1.00 43.66  ? 1488 VAL B O     1 
ATOM   5847 C  CB    . VAL B 1 271 ? 3.278   0.373   38.593 1.00 29.34  ? 1488 VAL B CB    1 
ATOM   5848 C  CG1   . VAL B 1 271 ? 1.924   0.419   39.304 1.00 29.94  ? 1488 VAL B CG1   1 
ATOM   5849 C  CG2   . VAL B 1 271 ? 3.206   1.073   37.240 1.00 29.06  ? 1488 VAL B CG2   1 
ATOM   5850 N  N     . MET B 1 272 ? 5.164   -0.860  40.868 1.00 36.55  ? 1489 MET B N     1 
ATOM   5851 C  CA    . MET B 1 272 ? 5.392   -1.533  42.137 1.00 37.44  ? 1489 MET B CA    1 
ATOM   5852 C  C     . MET B 1 272 ? 5.992   -0.562  43.136 1.00 39.62  ? 1489 MET B C     1 
ATOM   5853 O  O     . MET B 1 272 ? 5.401   -0.296  44.191 1.00 39.60  ? 1489 MET B O     1 
ATOM   5854 C  CB    . MET B 1 272 ? 6.295   -2.750  41.939 1.00 41.39  ? 1489 MET B CB    1 
ATOM   5855 C  CG    . MET B 1 272 ? 6.715   -3.434  43.233 1.00 39.27  ? 1489 MET B CG    1 
ATOM   5856 S  SD    . MET B 1 272 ? 8.114   -4.511  42.915 1.00 48.69  ? 1489 MET B SD    1 
ATOM   5857 C  CE    . MET B 1 272 ? 9.447   -3.402  42.501 1.00 43.20  ? 1489 MET B CE    1 
ATOM   5858 N  N     . ILE B 1 273 ? 7.098   0.082   42.752 1.00 35.78  ? 1490 ILE B N     1 
ATOM   5859 C  CA    . ILE B 1 273 ? 7.755   1.009   43.668 1.00 36.48  ? 1490 ILE B CA    1 
ATOM   5860 C  C     . ILE B 1 273 ? 6.746   2.001   44.205 1.00 41.33  ? 1490 ILE B C     1 
ATOM   5861 O  O     . ILE B 1 273 ? 6.491   2.064   45.416 1.00 55.08  ? 1490 ILE B O     1 
ATOM   5862 C  CB    . ILE B 1 273 ? 8.905   1.746   42.959 1.00 34.93  ? 1490 ILE B CB    1 
ATOM   5863 C  CG1   . ILE B 1 273 ? 10.020  0.790   42.572 1.00 29.99  ? 1490 ILE B CG1   1 
ATOM   5864 C  CG2   . ILE B 1 273 ? 9.451   2.833   43.838 1.00 35.53  ? 1490 ILE B CG2   1 
ATOM   5865 C  CD1   . ILE B 1 273 ? 11.043  1.420   41.715 1.00 38.16  ? 1490 ILE B CD1   1 
ATOM   5866 N  N     . MET B 1 274 ? 6.048   2.675   43.293 1.00 31.27  ? 1491 MET B N     1 
ATOM   5867 C  CA    . MET B 1 274 ? 5.211   3.799   43.689 1.00 37.35  ? 1491 MET B CA    1 
ATOM   5868 C  C     . MET B 1 274 ? 4.115   3.366   44.633 1.00 42.59  ? 1491 MET B C     1 
ATOM   5869 O  O     . MET B 1 274 ? 3.722   4.126   45.522 1.00 49.64  ? 1491 MET B O     1 
ATOM   5870 C  CB    . MET B 1 274 ? 4.617   4.442   42.452 1.00 45.47  ? 1491 MET B CB    1 
ATOM   5871 C  CG    . MET B 1 274 ? 5.646   5.196   41.667 1.00 61.35  ? 1491 MET B CG    1 
ATOM   5872 S  SD    . MET B 1 274 ? 5.567   6.877   42.234 1.00 80.52  ? 1491 MET B SD    1 
ATOM   5873 C  CE    . MET B 1 274 ? 7.268   7.400   42.112 1.00 75.51  ? 1491 MET B CE    1 
ATOM   5874 N  N     . VAL B 1 275 ? 3.665   2.123   44.502 1.00 41.70  ? 1492 VAL B N     1 
ATOM   5875 C  CA    . VAL B 1 275 ? 2.537   1.674   45.290 1.00 43.90  ? 1492 VAL B CA    1 
ATOM   5876 C  C     . VAL B 1 275 ? 2.982   1.180   46.649 1.00 45.59  ? 1492 VAL B C     1 
ATOM   5877 O  O     . VAL B 1 275 ? 2.275   1.386   47.638 1.00 52.24  ? 1492 VAL B O     1 
ATOM   5878 C  CB    . VAL B 1 275 ? 1.808   0.572   44.504 1.00 55.44  ? 1492 VAL B CB    1 
ATOM   5879 C  CG1   . VAL B 1 275 ? 0.872   -0.255  45.400 1.00 32.92  ? 1492 VAL B CG1   1 
ATOM   5880 C  CG2   . VAL B 1 275 ? 1.107   1.176   43.290 1.00 60.07  ? 1492 VAL B CG2   1 
ATOM   5881 N  N     . HIS B 1 276 ? 4.176   0.579   46.741 1.00 45.01  ? 1493 HIS B N     1 
ATOM   5882 C  CA    . HIS B 1 276 ? 4.578   -0.167  47.934 1.00 39.45  ? 1493 HIS B CA    1 
ATOM   5883 C  C     . HIS B 1 276 ? 5.717   0.433   48.743 1.00 38.57  ? 1493 HIS B C     1 
ATOM   5884 O  O     . HIS B 1 276 ? 5.743   0.235   49.964 1.00 51.09  ? 1493 HIS B O     1 
ATOM   5885 C  CB    . HIS B 1 276 ? 4.959   -1.607  47.562 1.00 38.57  ? 1493 HIS B CB    1 
ATOM   5886 C  CG    . HIS B 1 276 ? 3.810   -2.413  47.041 1.00 36.51  ? 1493 HIS B CG    1 
ATOM   5887 N  ND1   . HIS B 1 276 ? 2.569   -2.416  47.650 1.00 42.31  ? 1493 HIS B ND1   1 
ATOM   5888 C  CD2   . HIS B 1 276 ? 3.710   -3.235  45.966 1.00 32.12  ? 1493 HIS B CD2   1 
ATOM   5889 C  CE1   . HIS B 1 276 ? 1.758   -3.212  46.973 1.00 48.35  ? 1493 HIS B CE1   1 
ATOM   5890 N  NE2   . HIS B 1 276 ? 2.425   -3.718  45.945 1.00 37.54  ? 1493 HIS B NE2   1 
ATOM   5891 N  N     . ALA B 1 277 ? 6.686   1.104   48.124 1.00 36.89  ? 1494 ALA B N     1 
ATOM   5892 C  CA    . ALA B 1 277 ? 7.858   1.523   48.889 1.00 44.77  ? 1494 ALA B CA    1 
ATOM   5893 C  C     . ALA B 1 277 ? 7.455   2.577   49.906 1.00 48.65  ? 1494 ALA B C     1 
ATOM   5894 O  O     . ALA B 1 277 ? 6.624   3.444   49.621 1.00 46.56  ? 1494 ALA B O     1 
ATOM   5895 C  CB    . ALA B 1 277 ? 8.963   2.056   47.978 1.00 33.24  ? 1494 ALA B CB    1 
ATOM   5896 N  N     . ASP B 1 278 ? 8.028   2.474   51.110 1.00 45.63  ? 1495 ASP B N     1 
ATOM   5897 C  CA    . ASP B 1 278 ? 7.780   3.395   52.202 1.00 38.96  ? 1495 ASP B CA    1 
ATOM   5898 C  C     . ASP B 1 278 ? 8.970   4.337   52.361 1.00 43.27  ? 1495 ASP B C     1 
ATOM   5899 O  O     . ASP B 1 278 ? 9.813   4.446   51.469 1.00 43.39  ? 1495 ASP B O     1 
ATOM   5900 C  CB    . ASP B 1 278 ? 7.486   2.616   53.480 1.00 43.09  ? 1495 ASP B CB    1 
ATOM   5901 C  CG    . ASP B 1 278 ? 8.544   1.575   53.798 1.00 59.55  ? 1495 ASP B CG    1 
ATOM   5902 O  OD1   . ASP B 1 278 ? 9.683   1.687   53.281 1.00 62.89  ? 1495 ASP B OD1   1 
ATOM   5903 O  OD2   . ASP B 1 278 ? 8.234   0.669   54.612 1.00 57.45  ? 1495 ASP B OD2   1 
ATOM   5904 N  N     . ASN B 1 279 ? 9.070   4.997   53.510 1.00 60.62  ? 1496 ASN B N     1 
ATOM   5905 C  CA    . ASN B 1 279 ? 10.127  5.978   53.711 1.00 67.05  ? 1496 ASN B CA    1 
ATOM   5906 C  C     . ASN B 1 279 ? 11.412  5.345   54.210 1.00 66.14  ? 1496 ASN B C     1 
ATOM   5907 O  O     . ASN B 1 279 ? 12.320  6.071   54.629 1.00 76.54  ? 1496 ASN B O     1 
ATOM   5908 C  CB    . ASN B 1 279 ? 9.695   7.065   54.710 1.00 71.46  ? 1496 ASN B CB    1 
ATOM   5909 C  CG    . ASN B 1 279 ? 8.476   7.855   54.258 1.00 75.38  ? 1496 ASN B CG    1 
ATOM   5910 O  OD1   . ASN B 1 279 ? 8.591   8.815   53.491 1.00 71.12  ? 1496 ASN B OD1   1 
ATOM   5911 N  ND2   . ASN B 1 279 ? 7.301   7.475   54.767 1.00 76.17  ? 1496 ASN B ND2   1 
ATOM   5912 N  N     . GLN B 1 280 ? 11.517  4.017   54.178 1.00 51.91  ? 1497 GLN B N     1 
ATOM   5913 C  CA    . GLN B 1 280 ? 12.750  3.347   54.568 1.00 59.21  ? 1497 GLN B CA    1 
ATOM   5914 C  C     . GLN B 1 280 ? 13.313  2.482   53.455 1.00 64.88  ? 1497 GLN B C     1 
ATOM   5915 O  O     . GLN B 1 280 ? 14.317  1.788   53.669 1.00 66.57  ? 1497 GLN B O     1 
ATOM   5916 C  CB    . GLN B 1 280 ? 12.552  2.524   55.843 1.00 58.35  ? 1497 GLN B CB    1 
ATOM   5917 C  CG    . GLN B 1 280 ? 12.708  3.363   57.094 1.00 69.06  ? 1497 GLN B CG    1 
ATOM   5918 C  CD    . GLN B 1 280 ? 11.582  3.145   58.061 1.00 74.73  ? 1497 GLN B CD    1 
ATOM   5919 O  OE1   . GLN B 1 280 ? 11.224  2.003   58.349 1.00 86.93  ? 1497 GLN B OE1   1 
ATOM   5920 N  NE2   . GLN B 1 280 ? 10.993  4.234   58.554 1.00 64.85  ? 1497 GLN B NE2   1 
ATOM   5921 N  N     . GLY B 1 281 ? 12.706  2.519   52.271 1.00 58.40  ? 1498 GLY B N     1 
ATOM   5922 C  CA    . GLY B 1 281 ? 13.245  1.840   51.120 1.00 47.96  ? 1498 GLY B CA    1 
ATOM   5923 C  C     . GLY B 1 281 ? 12.167  1.081   50.397 1.00 46.03  ? 1498 GLY B C     1 
ATOM   5924 O  O     . GLY B 1 281 ? 10.973  1.328   50.591 1.00 48.25  ? 1498 GLY B O     1 
ATOM   5925 N  N     . LEU B 1 282 ? 12.606  0.166   49.535 1.00 43.17  ? 1499 LEU B N     1 
ATOM   5926 C  CA    . LEU B 1 282 ? 11.705  -0.690  48.788 1.00 40.52  ? 1499 LEU B CA    1 
ATOM   5927 C  C     . LEU B 1 282 ? 10.887  -1.580  49.717 1.00 55.90  ? 1499 LEU B C     1 
ATOM   5928 O  O     . LEU B 1 282 ? 11.222  -1.799  50.885 1.00 56.75  ? 1499 LEU B O     1 
ATOM   5929 C  CB    . LEU B 1 282 ? 12.478  -1.576  47.826 1.00 32.18  ? 1499 LEU B CB    1 
ATOM   5930 C  CG    . LEU B 1 282 ? 13.191  -0.927  46.645 1.00 34.79  ? 1499 LEU B CG    1 
ATOM   5931 C  CD1   . LEU B 1 282 ? 14.482  -1.694  46.279 1.00 34.92  ? 1499 LEU B CD1   1 
ATOM   5932 C  CD2   . LEU B 1 282 ? 12.253  -0.896  45.465 1.00 30.95  ? 1499 LEU B CD2   1 
ATOM   5933 N  N     . VAL B 1 283 ? 9.800   -2.109  49.164 1.00 57.49  ? 1500 VAL B N     1 
ATOM   5934 C  CA    . VAL B 1 283 ? 9.023   -3.172  49.780 1.00 51.55  ? 1500 VAL B CA    1 
ATOM   5935 C  C     . VAL B 1 283 ? 8.601   -4.128  48.671 1.00 45.52  ? 1500 VAL B C     1 
ATOM   5936 O  O     . VAL B 1 283 ? 7.619   -3.891  47.967 1.00 48.14  ? 1500 VAL B O     1 
ATOM   5937 C  CB    . VAL B 1 283 ? 7.816   -2.619  50.555 1.00 46.36  ? 1500 VAL B CB    1 
ATOM   5938 C  CG1   . VAL B 1 283 ? 7.012   -3.752  51.157 1.00 42.58  ? 1500 VAL B CG1   1 
ATOM   5939 C  CG2   . VAL B 1 283 ? 8.277   -1.698  51.654 1.00 45.42  ? 1500 VAL B CG2   1 
ATOM   5940 N  N     . LEU B 1 284 ? 9.337   -5.194  48.507 1.00 45.61  ? 1501 LEU B N     1 
ATOM   5941 C  CA    . LEU B 1 284 ? 9.123   -6.095  47.390 1.00 46.16  ? 1501 LEU B CA    1 
ATOM   5942 C  C     . LEU B 1 284 ? 7.934   -7.025  47.662 1.00 47.53  ? 1501 LEU B C     1 
ATOM   5943 O  O     . LEU B 1 284 ? 7.732   -7.458  48.806 1.00 39.99  ? 1501 LEU B O     1 
ATOM   5944 C  CB    . LEU B 1 284 ? 10.398  -6.899  47.136 1.00 37.19  ? 1501 LEU B CB    1 
ATOM   5945 C  CG    . LEU B 1 284 ? 11.535  -5.959  46.698 1.00 42.11  ? 1501 LEU B CG    1 
ATOM   5946 C  CD1   . LEU B 1 284 ? 12.860  -6.651  46.438 1.00 36.80  ? 1501 LEU B CD1   1 
ATOM   5947 C  CD2   . LEU B 1 284 ? 11.117  -5.210  45.449 1.00 47.18  ? 1501 LEU B CD2   1 
ATOM   5948 N  N     . PRO B 1 285 ? 7.085   -7.264  46.655 1.00 48.01  ? 1502 PRO B N     1 
ATOM   5949 C  CA    . PRO B 1 285 ? 6.059   -8.287  46.777 1.00 54.59  ? 1502 PRO B CA    1 
ATOM   5950 C  C     . PRO B 1 285 ? 6.719   -9.648  46.809 1.00 57.57  ? 1502 PRO B C     1 
ATOM   5951 O  O     . PRO B 1 285 ? 7.630   -9.912  46.014 1.00 59.84  ? 1502 PRO B O     1 
ATOM   5952 C  CB    . PRO B 1 285 ? 5.212   -8.109  45.505 1.00 56.97  ? 1502 PRO B CB    1 
ATOM   5953 C  CG    . PRO B 1 285 ? 5.633   -6.821  44.903 1.00 45.88  ? 1502 PRO B CG    1 
ATOM   5954 C  CD    . PRO B 1 285 ? 7.054   -6.643  45.325 1.00 47.53  ? 1502 PRO B CD    1 
ATOM   5955 N  N     . PRO B 1 286 ? 6.280   -10.543 47.685 1.00 53.32  ? 1503 PRO B N     1 
ATOM   5956 C  CA    . PRO B 1 286 ? 7.062   -11.760 47.909 1.00 44.46  ? 1503 PRO B CA    1 
ATOM   5957 C  C     . PRO B 1 286 ? 7.255   -12.572 46.651 1.00 52.89  ? 1503 PRO B C     1 
ATOM   5958 O  O     . PRO B 1 286 ? 8.316   -13.186 46.492 1.00 58.45  ? 1503 PRO B O     1 
ATOM   5959 C  CB    . PRO B 1 286 ? 6.240   -12.520 48.960 1.00 53.57  ? 1503 PRO B CB    1 
ATOM   5960 C  CG    . PRO B 1 286 ? 5.245   -11.531 49.510 1.00 54.90  ? 1503 PRO B CG    1 
ATOM   5961 C  CD    . PRO B 1 286 ? 4.974   -10.594 48.356 1.00 54.11  ? 1503 PRO B CD    1 
ATOM   5962 N  N     . ARG B 1 287 ? 6.282   -12.565 45.729 1.00 54.36  ? 1504 ARG B N     1 
ATOM   5963 C  CA    . ARG B 1 287 ? 6.309   -13.471 44.583 1.00 42.23  ? 1504 ARG B CA    1 
ATOM   5964 C  C     . ARG B 1 287 ? 7.225   -12.995 43.470 1.00 38.90  ? 1504 ARG B C     1 
ATOM   5965 O  O     . ARG B 1 287 ? 7.388   -13.712 42.484 1.00 44.75  ? 1504 ARG B O     1 
ATOM   5966 C  CB    . ARG B 1 287 ? 4.902   -13.647 43.998 1.00 42.10  ? 1504 ARG B CB    1 
ATOM   5967 C  CG    . ARG B 1 287 ? 3.816   -13.749 45.044 1.00 50.77  ? 1504 ARG B CG    1 
ATOM   5968 C  CD    . ARG B 1 287 ? 2.650   -14.606 44.580 1.00 50.45  ? 1504 ARG B CD    1 
ATOM   5969 N  NE    . ARG B 1 287 ? 1.796   -14.927 45.719 1.00 57.99  ? 1504 ARG B NE    1 
ATOM   5970 C  CZ    . ARG B 1 287 ? 0.527   -14.558 45.868 1.00 54.61  ? 1504 ARG B CZ    1 
ATOM   5971 N  NH1   . ARG B 1 287 ? -0.094  -13.840 44.944 1.00 50.33  ? 1504 ARG B NH1   1 
ATOM   5972 N  NH2   . ARG B 1 287 ? -0.128  -14.929 46.957 1.00 65.67  ? 1504 ARG B NH2   1 
ATOM   5973 N  N     . VAL B 1 288 ? 7.875   -11.872 43.652 1.00 35.34  ? 1505 VAL B N     1 
ATOM   5974 C  CA    . VAL B 1 288 ? 8.789   -11.402 42.663 1.00 33.83  ? 1505 VAL B CA    1 
ATOM   5975 C  C     . VAL B 1 288 ? 10.079  -10.972 43.232 1.00 43.27  ? 1505 VAL B C     1 
ATOM   5976 O  O     . VAL B 1 288 ? 10.992  -10.766 42.519 1.00 50.81  ? 1505 VAL B O     1 
ATOM   5977 C  CB    . VAL B 1 288 ? 8.313   -10.190 41.957 1.00 42.56  ? 1505 VAL B CB    1 
ATOM   5978 C  CG1   . VAL B 1 288 ? 7.148   -10.494 41.076 1.00 53.90  ? 1505 VAL B CG1   1 
ATOM   5979 C  CG2   . VAL B 1 288 ? 7.984   -9.128  42.927 1.00 50.39  ? 1505 VAL B CG2   1 
ATOM   5980 N  N     . ALA B 1 289 ? 10.178  -10.888 44.532 1.00 41.65  ? 1506 ALA B N     1 
ATOM   5981 C  CA    . ALA B 1 289 ? 11.370  -10.459 45.154 1.00 35.52  ? 1506 ALA B CA    1 
ATOM   5982 C  C     . ALA B 1 289 ? 12.422  -11.418 44.881 1.00 42.64  ? 1506 ALA B C     1 
ATOM   5983 O  O     . ALA B 1 289 ? 12.209  -12.552 45.040 1.00 52.31  ? 1506 ALA B O     1 
ATOM   5984 C  CB    . ALA B 1 289 ? 11.132  -10.425 46.609 1.00 37.18  ? 1506 ALA B CB    1 
ATOM   5985 N  N     . CYS B 1 290 ? 13.566  -10.910 44.523 1.00 42.30  ? 1507 CYS B N     1 
ATOM   5986 C  CA    . CYS B 1 290 ? 14.709  -11.706 44.241 1.00 43.52  ? 1507 CYS B CA    1 
ATOM   5987 C  C     . CYS B 1 290 ? 15.063  -12.652 45.364 1.00 51.68  ? 1507 CYS B C     1 
ATOM   5988 O  O     . CYS B 1 290 ? 15.201  -13.860 45.171 1.00 67.33  ? 1507 CYS B O     1 
ATOM   5989 C  CB    . CYS B 1 290 ? 15.771  -10.694 44.062 1.00 43.49  ? 1507 CYS B CB    1 
ATOM   5990 S  SG    . CYS B 1 290 ? 17.389  -11.376 43.630 1.00 54.90  ? 1507 CYS B SG    1 
ATOM   5991 N  N     . ILE B 1 291 ? 15.208  -12.078 46.545 1.00 57.86  ? 1508 ILE B N     1 
ATOM   5992 C  CA    . ILE B 1 291 ? 15.550  -12.815 47.720 1.00 69.38  ? 1508 ILE B CA    1 
ATOM   5993 C  C     . ILE B 1 291 ? 14.371  -12.577 48.560 1.00 72.92  ? 1508 ILE B C     1 
ATOM   5994 O  O     . ILE B 1 291 ? 14.058  -11.488 48.845 1.00 88.35  ? 1508 ILE B O     1 
ATOM   5995 C  CB    . ILE B 1 291 ? 16.675  -12.221 48.496 1.00 75.38  ? 1508 ILE B CB    1 
ATOM   5996 C  CG1   . ILE B 1 291 ? 17.949  -12.268 47.705 1.00 76.40  ? 1508 ILE B CG1   1 
ATOM   5997 C  CG2   . ILE B 1 291 ? 16.886  -13.059 49.716 1.00 73.71  ? 1508 ILE B CG2   1 
ATOM   5998 C  CD1   . ILE B 1 291 ? 19.148  -12.314 48.587 1.00 77.81  ? 1508 ILE B CD1   1 
ATOM   5999 N  N     . GLN B 1 292 ? 13.705  -13.615 48.943 1.00 62.36  ? 1509 GLN B N     1 
ATOM   6000 C  CA    . GLN B 1 292 ? 12.481  -13.548 49.722 1.00 50.00  ? 1509 GLN B CA    1 
ATOM   6001 C  C     . GLN B 1 292 ? 12.741  -13.542 51.213 1.00 52.32  ? 1509 GLN B C     1 
ATOM   6002 O  O     . GLN B 1 292 ? 11.989  -12.923 51.970 1.00 54.24  ? 1509 GLN B O     1 
ATOM   6003 C  CB    . GLN B 1 292 ? 11.591  -14.713 49.348 1.00 54.07  ? 1509 GLN B CB    1 
ATOM   6004 C  CG    . GLN B 1 292 ? 11.099  -14.616 47.933 1.00 55.85  ? 1509 GLN B CG    1 
ATOM   6005 C  CD    . GLN B 1 292 ? 10.327  -15.830 47.530 1.00 54.11  ? 1509 GLN B CD    1 
ATOM   6006 O  OE1   . GLN B 1 292 ? 10.767  -16.956 47.762 1.00 55.95  ? 1509 GLN B OE1   1 
ATOM   6007 N  NE2   . GLN B 1 292 ? 9.153   -15.620 46.935 1.00 60.41  ? 1509 GLN B NE2   1 
ATOM   6008 N  N     . VAL B 1 293 ? 13.743  -14.300 51.646 1.00 55.81  ? 1510 VAL B N     1 
ATOM   6009 C  CA    . VAL B 1 293 ? 14.153  -14.391 53.040 1.00 53.18  ? 1510 VAL B CA    1 
ATOM   6010 C  C     . VAL B 1 293 ? 15.654  -14.130 53.079 1.00 64.70  ? 1510 VAL B C     1 
ATOM   6011 O  O     . VAL B 1 293 ? 16.399  -14.725 52.294 1.00 69.07  ? 1510 VAL B O     1 
ATOM   6012 C  CB    . VAL B 1 293 ? 13.835  -15.778 53.630 1.00 41.77  ? 1510 VAL B CB    1 
ATOM   6013 C  CG1   . VAL B 1 293 ? 14.373  -15.879 55.044 1.00 38.34  ? 1510 VAL B CG1   1 
ATOM   6014 C  CG2   . VAL B 1 293 ? 12.362  -16.038 53.594 1.00 37.33  ? 1510 VAL B CG2   1 
ATOM   6015 N  N     . VAL B 1 294 ? 16.107  -13.257 53.981 1.00 61.51  ? 1511 VAL B N     1 
ATOM   6016 C  CA    . VAL B 1 294 ? 17.539  -13.151 54.258 1.00 63.85  ? 1511 VAL B CA    1 
ATOM   6017 C  C     . VAL B 1 294 ? 17.823  -13.383 55.735 1.00 69.26  ? 1511 VAL B C     1 
ATOM   6018 O  O     . VAL B 1 294 ? 17.242  -12.716 56.606 1.00 72.49  ? 1511 VAL B O     1 
ATOM   6019 C  CB    . VAL B 1 294 ? 18.132  -11.805 53.812 1.00 49.50  ? 1511 VAL B CB    1 
ATOM   6020 C  CG1   . VAL B 1 294 ? 17.447  -10.660 54.517 1.00 37.59  ? 1511 VAL B CG1   1 
ATOM   6021 C  CG2   . VAL B 1 294 ? 19.636  -11.799 54.072 1.00 52.72  ? 1511 VAL B CG2   1 
ATOM   6022 N  N     . ILE B 1 295 ? 18.761  -14.287 56.008 1.00 59.12  ? 1512 ILE B N     1 
ATOM   6023 C  CA    . ILE B 1 295 ? 19.196  -14.587 57.361 1.00 57.03  ? 1512 ILE B CA    1 
ATOM   6024 C  C     . ILE B 1 295 ? 20.338  -13.654 57.706 1.00 58.29  ? 1512 ILE B C     1 
ATOM   6025 O  O     . ILE B 1 295 ? 21.295  -13.542 56.935 1.00 69.84  ? 1512 ILE B O     1 
ATOM   6026 C  CB    . ILE B 1 295 ? 19.647  -16.045 57.491 1.00 55.75  ? 1512 ILE B CB    1 
ATOM   6027 C  CG1   . ILE B 1 295 ? 18.521  -16.998 57.093 1.00 70.21  ? 1512 ILE B CG1   1 
ATOM   6028 C  CG2   . ILE B 1 295 ? 20.088  -16.291 58.925 1.00 43.25  ? 1512 ILE B CG2   1 
ATOM   6029 C  CD1   . ILE B 1 295 ? 18.953  -18.444 57.053 1.00 72.64  ? 1512 ILE B CD1   1 
ATOM   6030 N  N     . VAL B 1 296 ? 20.254  -13.004 58.865 1.00 44.20  ? 1513 VAL B N     1 
ATOM   6031 C  CA    . VAL B 1 296 ? 21.292  -12.060 59.271 1.00 53.43  ? 1513 VAL B CA    1 
ATOM   6032 C  C     . VAL B 1 296 ? 21.796  -12.481 60.646 1.00 64.09  ? 1513 VAL B C     1 
ATOM   6033 O  O     . VAL B 1 296 ? 21.111  -12.245 61.658 1.00 70.45  ? 1513 VAL B O     1 
ATOM   6034 C  CB    . VAL B 1 296 ? 20.792  -10.601 59.285 1.00 51.91  ? 1513 VAL B CB    1 
ATOM   6035 C  CG1   . VAL B 1 296 ? 21.846  -9.703  59.863 1.00 41.78  ? 1513 VAL B CG1   1 
ATOM   6036 C  CG2   . VAL B 1 296 ? 20.499  -10.119 57.885 1.00 56.59  ? 1513 VAL B CG2   1 
ATOM   6037 N  N     . PRO B 1 297 ? 22.970  -13.110 60.732 1.00 63.56  ? 1514 PRO B N     1 
ATOM   6038 C  CA    . PRO B 1 297 ? 23.450  -13.578 62.034 1.00 57.72  ? 1514 PRO B CA    1 
ATOM   6039 C  C     . PRO B 1 297 ? 23.856  -12.426 62.933 1.00 53.47  ? 1514 PRO B C     1 
ATOM   6040 O  O     . PRO B 1 297 ? 24.477  -11.455 62.494 1.00 51.84  ? 1514 PRO B O     1 
ATOM   6041 C  CB    . PRO B 1 297 ? 24.658  -14.446 61.668 1.00 57.14  ? 1514 PRO B CB    1 
ATOM   6042 C  CG    . PRO B 1 297 ? 25.157  -13.842 60.370 1.00 54.70  ? 1514 PRO B CG    1 
ATOM   6043 C  CD    . PRO B 1 297 ? 23.907  -13.440 59.642 1.00 60.82  ? 1514 PRO B CD    1 
ATOM   6044 N  N     . CYS B 1 298 ? 23.538  -12.576 64.216 1.00 58.49  ? 1515 CYS B N     1 
ATOM   6045 C  CA    . CYS B 1 298 ? 23.759  -11.555 65.224 1.00 70.71  ? 1515 CYS B CA    1 
ATOM   6046 C  C     . CYS B 1 298 ? 24.205  -12.231 66.508 1.00 69.75  ? 1515 CYS B C     1 
ATOM   6047 O  O     . CYS B 1 298 ? 24.105  -13.448 66.670 1.00 70.49  ? 1515 CYS B O     1 
ATOM   6048 C  CB    . CYS B 1 298 ? 22.507  -10.693 65.481 1.00 85.12  ? 1515 CYS B CB    1 
ATOM   6049 S  SG    . CYS B 1 298 ? 20.897  -11.528 65.375 1.00 89.58  ? 1515 CYS B SG    1 
ATOM   6050 N  N     . GLY B 1 299 ? 24.649  -11.415 67.447 1.00 73.07  ? 1516 GLY B N     1 
ATOM   6051 C  CA    . GLY B 1 299 ? 25.095  -11.899 68.731 1.00 74.31  ? 1516 GLY B CA    1 
ATOM   6052 C  C     . GLY B 1 299 ? 26.584  -12.067 68.800 1.00 79.85  ? 1516 GLY B C     1 
ATOM   6053 O  O     . GLY B 1 299 ? 27.100  -12.454 69.857 1.00 84.76  ? 1516 GLY B O     1 
ATOM   6054 N  N     . ILE B 1 300 ? 27.285  -11.769 67.708 1.00 76.21  ? 1517 ILE B N     1 
ATOM   6055 C  CA    . ILE B 1 300 ? 28.714  -12.041 67.585 1.00 72.92  ? 1517 ILE B CA    1 
ATOM   6056 C  C     . ILE B 1 300 ? 29.425  -10.826 68.180 1.00 85.82  ? 1517 ILE B C     1 
ATOM   6057 O  O     . ILE B 1 300 ? 29.812  -9.896  67.473 1.00 88.90  ? 1517 ILE B O     1 
ATOM   6058 C  CB    . ILE B 1 300 ? 29.112  -12.325 66.135 1.00 50.17  ? 1517 ILE B CB    1 
ATOM   6059 N  N     . THR B 1 301 ? 29.603  -10.840 69.509 1.00 90.76  ? 1518 THR B N     1 
ATOM   6060 C  CA    . THR B 1 301 ? 30.237  -9.744  70.243 1.00 83.96  ? 1518 THR B CA    1 
ATOM   6061 C  C     . THR B 1 301 ? 31.752  -9.755  70.057 1.00 98.59  ? 1518 THR B C     1 
ATOM   6062 O  O     . THR B 1 301 ? 32.302  -10.435 69.188 1.00 102.37 ? 1518 THR B O     1 
ATOM   6063 C  CB    . THR B 1 301 ? 29.901  -9.829  71.734 1.00 62.11  ? 1518 THR B CB    1 
ATOM   6064 N  N     . ALA B 1 302 ? 32.447  -8.980  70.891 1.00 107.26 ? 1519 ALA B N     1 
ATOM   6065 C  CA    . ALA B 1 302 ? 33.904  -8.995  70.863 1.00 109.20 ? 1519 ALA B CA    1 
ATOM   6066 C  C     . ALA B 1 302 ? 34.445  -10.291 71.446 1.00 105.21 ? 1519 ALA B C     1 
ATOM   6067 O  O     . ALA B 1 302 ? 35.429  -10.844 70.940 1.00 109.49 ? 1519 ALA B O     1 
ATOM   6068 C  CB    . ALA B 1 302 ? 34.463  -7.794  71.626 1.00 113.81 ? 1519 ALA B CB    1 
ATOM   6069 N  N     . THR B 1 303 ? 33.830  -10.771 72.530 1.00 94.24  ? 1520 THR B N     1 
ATOM   6070 C  CA    . THR B 1 303 ? 34.269  -11.980 73.216 1.00 86.20  ? 1520 THR B CA    1 
ATOM   6071 C  C     . THR B 1 303 ? 33.693  -13.254 72.596 1.00 88.57  ? 1520 THR B C     1 
ATOM   6072 O  O     . THR B 1 303 ? 33.513  -14.259 73.295 1.00 85.85  ? 1520 THR B O     1 
ATOM   6073 C  CB    . THR B 1 303 ? 33.878  -11.896 74.695 1.00 62.26  ? 1520 THR B CB    1 
ATOM   6074 N  N     . THR B 1 304 ? 33.459  -13.260 71.286 1.00 84.86  ? 1521 THR B N     1 
ATOM   6075 C  CA    . THR B 1 304 ? 32.835  -14.405 70.621 1.00 75.07  ? 1521 THR B CA    1 
ATOM   6076 C  C     . THR B 1 304 ? 33.911  -15.433 70.281 1.00 78.64  ? 1521 THR B C     1 
ATOM   6077 O  O     . THR B 1 304 ? 34.735  -15.211 69.388 1.00 78.32  ? 1521 THR B O     1 
ATOM   6078 C  CB    . THR B 1 304 ? 32.083  -13.949 69.372 1.00 55.46  ? 1521 THR B CB    1 
ATOM   6079 N  N     . THR B 1 305 ? 33.901  -16.569 70.980 1.00 77.92  ? 1522 THR B N     1 
ATOM   6080 C  CA    . THR B 1 305 ? 34.850  -17.639 70.688 1.00 79.57  ? 1522 THR B CA    1 
ATOM   6081 C  C     . THR B 1 305 ? 34.599  -18.185 69.313 1.00 78.90  ? 1522 THR B C     1 
ATOM   6082 O  O     . THR B 1 305 ? 33.463  -18.536 68.977 1.00 91.22  ? 1522 THR B O     1 
ATOM   6083 C  CB    . THR B 1 305 ? 34.798  -18.783 71.705 1.00 90.47  ? 1522 THR B CB    1 
ATOM   6084 O  OG1   . THR B 1 305 ? 35.790  -19.782 71.402 1.00 94.95  ? 1522 THR B OG1   1 
ATOM   6085 C  CG2   . THR B 1 305 ? 33.424  -19.494 71.762 1.00 89.54  ? 1522 THR B CG2   1 
ATOM   6086 N  N     . ASP B 1 306 ? 35.669  -18.268 68.515 1.00 77.83  ? 1523 ASP B N     1 
ATOM   6087 C  CA    . ASP B 1 306 ? 35.568  -18.538 67.082 1.00 80.65  ? 1523 ASP B CA    1 
ATOM   6088 C  C     . ASP B 1 306 ? 34.762  -19.797 66.789 1.00 80.51  ? 1523 ASP B C     1 
ATOM   6089 O  O     . ASP B 1 306 ? 34.067  -19.867 65.765 1.00 64.79  ? 1523 ASP B O     1 
ATOM   6090 C  CB    . ASP B 1 306 ? 36.988  -18.639 66.526 1.00 75.07  ? 1523 ASP B CB    1 
ATOM   6091 C  CG    . ASP B 1 306 ? 37.036  -19.045 65.076 1.00 68.05  ? 1523 ASP B CG    1 
ATOM   6092 O  OD1   . ASP B 1 306 ? 36.490  -18.294 64.228 1.00 57.93  ? 1523 ASP B OD1   1 
ATOM   6093 O  OD2   . ASP B 1 306 ? 37.646  -20.120 64.813 1.00 63.43  ? 1523 ASP B OD2   1 
ATOM   6094 N  N     . ASP B 1 307 ? 34.792  -20.766 67.712 1.00 85.23  ? 1524 ASP B N     1 
ATOM   6095 C  CA    . ASP B 1 307 ? 33.935  -21.935 67.596 1.00 86.24  ? 1524 ASP B CA    1 
ATOM   6096 C  C     . ASP B 1 307 ? 32.472  -21.539 67.598 1.00 85.89  ? 1524 ASP B C     1 
ATOM   6097 O  O     . ASP B 1 307 ? 31.686  -22.059 66.804 1.00 87.61  ? 1524 ASP B O     1 
ATOM   6098 C  CB    . ASP B 1 307 ? 34.211  -22.917 68.732 1.00 90.96  ? 1524 ASP B CB    1 
ATOM   6099 C  CG    . ASP B 1 307 ? 35.581  -23.528 68.645 1.00 91.34  ? 1524 ASP B CG    1 
ATOM   6100 O  OD1   . ASP B 1 307 ? 36.169  -23.534 67.532 1.00 84.98  ? 1524 ASP B OD1   1 
ATOM   6101 O  OD2   . ASP B 1 307 ? 36.052  -24.017 69.695 1.00 90.26  ? 1524 ASP B OD2   1 
ATOM   6102 N  N     . GLU B 1 308 ? 32.090  -20.616 68.485 1.00 80.49  ? 1525 GLU B N     1 
ATOM   6103 C  CA    . GLU B 1 308 ? 30.707  -20.164 68.524 1.00 61.96  ? 1525 GLU B CA    1 
ATOM   6104 C  C     . GLU B 1 308 ? 30.329  -19.410 67.252 1.00 56.36  ? 1525 GLU B C     1 
ATOM   6105 O  O     . GLU B 1 308 ? 29.198  -19.533 66.776 1.00 64.35  ? 1525 GLU B O     1 
ATOM   6106 C  CB    . GLU B 1 308 ? 30.477  -19.302 69.761 1.00 56.78  ? 1525 GLU B CB    1 
ATOM   6107 N  N     . ARG B 1 309 ? 31.258  -18.642 66.667 1.00 58.39  ? 1526 ARG B N     1 
ATOM   6108 C  CA    . ARG B 1 309 ? 30.946  -17.937 65.421 1.00 55.95  ? 1526 ARG B CA    1 
ATOM   6109 C  C     . ARG B 1 309 ? 30.758  -18.924 64.285 1.00 57.76  ? 1526 ARG B C     1 
ATOM   6110 O  O     . ARG B 1 309 ? 29.881  -18.747 63.420 1.00 55.35  ? 1526 ARG B O     1 
ATOM   6111 C  CB    . ARG B 1 309 ? 32.049  -16.936 65.076 1.00 60.99  ? 1526 ARG B CB    1 
ATOM   6112 N  N     . ARG B 1 310 ? 31.554  -19.997 64.299 1.00 60.86  ? 1527 ARG B N     1 
ATOM   6113 C  CA    . ARG B 1 310 ? 31.401  -21.039 63.290 1.00 62.23  ? 1527 ARG B CA    1 
ATOM   6114 C  C     . ARG B 1 310 ? 30.111  -21.825 63.480 1.00 61.75  ? 1527 ARG B C     1 
ATOM   6115 O  O     . ARG B 1 310 ? 29.448  -22.182 62.502 1.00 60.80  ? 1527 ARG B O     1 
ATOM   6116 C  CB    . ARG B 1 310 ? 32.578  -21.985 63.353 1.00 61.00  ? 1527 ARG B CB    1 
ATOM   6117 C  CG    . ARG B 1 310 ? 33.822  -21.445 62.838 1.00 57.82  ? 1527 ARG B CG    1 
ATOM   6118 C  CD    . ARG B 1 310 ? 34.746  -22.597 62.703 1.00 60.99  ? 1527 ARG B CD    1 
ATOM   6119 N  NE    . ARG B 1 310 ? 36.125  -22.122 62.739 1.00 66.89  ? 1527 ARG B NE    1 
ATOM   6120 C  CZ    . ARG B 1 310 ? 36.677  -21.426 61.743 1.00 65.94  ? 1527 ARG B CZ    1 
ATOM   6121 N  NH1   . ARG B 1 310 ? 35.971  -21.134 60.672 1.00 56.41  ? 1527 ARG B NH1   1 
ATOM   6122 N  NH2   . ARG B 1 310 ? 37.933  -20.995 61.796 1.00 65.22  ? 1527 ARG B NH2   1 
ATOM   6123 N  N     . ARG B 1 311 ? 29.755  -22.108 64.735 1.00 57.56  ? 1528 ARG B N     1 
ATOM   6124 C  CA    . ARG B 1 311 ? 28.524  -22.824 65.046 1.00 60.65  ? 1528 ARG B CA    1 
ATOM   6125 C  C     . ARG B 1 311 ? 27.317  -22.029 64.594 1.00 71.95  ? 1528 ARG B C     1 
ATOM   6126 O  O     . ARG B 1 311 ? 26.391  -22.570 63.972 1.00 86.30  ? 1528 ARG B O     1 
ATOM   6127 C  CB    . ARG B 1 311 ? 28.470  -23.089 66.549 1.00 54.09  ? 1528 ARG B CB    1 
ATOM   6128 C  CG    . ARG B 1 311 ? 27.769  -24.355 66.972 1.00 62.14  ? 1528 ARG B CG    1 
ATOM   6129 C  CD    . ARG B 1 311 ? 28.020  -24.659 68.456 1.00 63.69  ? 1528 ARG B CD    1 
ATOM   6130 N  NE    . ARG B 1 311 ? 27.601  -23.591 69.368 1.00 59.20  ? 1528 ARG B NE    1 
ATOM   6131 C  CZ    . ARG B 1 311 ? 26.344  -23.389 69.754 1.00 61.17  ? 1528 ARG B CZ    1 
ATOM   6132 N  NH1   . ARG B 1 311 ? 25.368  -24.162 69.291 1.00 57.25  ? 1528 ARG B NH1   1 
ATOM   6133 N  NH2   . ARG B 1 311 ? 26.060  -22.401 70.589 1.00 61.83  ? 1528 ARG B NH2   1 
ATOM   6134 N  N     . LEU B 1 312 ? 27.338  -20.724 64.853 1.00 67.90  ? 1529 LEU B N     1 
ATOM   6135 C  CA    . LEU B 1 312 ? 26.269  -19.864 64.378 1.00 64.08  ? 1529 LEU B CA    1 
ATOM   6136 C  C     . LEU B 1 312 ? 26.187  -19.894 62.861 1.00 61.27  ? 1529 LEU B C     1 
ATOM   6137 O  O     . LEU B 1 312 ? 25.093  -20.030 62.295 1.00 54.62  ? 1529 LEU B O     1 
ATOM   6138 C  CB    . LEU B 1 312 ? 26.486  -18.435 64.885 1.00 68.86  ? 1529 LEU B CB    1 
ATOM   6139 C  CG    . LEU B 1 312 ? 25.423  -17.397 64.505 1.00 71.07  ? 1529 LEU B CG    1 
ATOM   6140 C  CD1   . LEU B 1 312 ? 24.186  -17.606 65.344 1.00 77.73  ? 1529 LEU B CD1   1 
ATOM   6141 C  CD2   . LEU B 1 312 ? 25.932  -15.977 64.662 1.00 67.53  ? 1529 LEU B CD2   1 
ATOM   6142 N  N     . TYR B 1 313 ? 27.338  -19.760 62.180 1.00 61.27  ? 1530 TYR B N     1 
ATOM   6143 C  CA    . TYR B 1 313 ? 27.319  -19.722 60.719 1.00 55.77  ? 1530 TYR B CA    1 
ATOM   6144 C  C     . TYR B 1 313 ? 26.793  -21.038 60.155 1.00 65.93  ? 1530 TYR B C     1 
ATOM   6145 O  O     . TYR B 1 313 ? 25.972  -21.034 59.229 1.00 67.45  ? 1530 TYR B O     1 
ATOM   6146 C  CB    . TYR B 1 313 ? 28.712  -19.359 60.190 1.00 45.81  ? 1530 TYR B CB    1 
ATOM   6147 N  N     . GLU B 1 314 ? 27.164  -22.169 60.782 1.00 79.93  ? 1531 GLU B N     1 
ATOM   6148 C  CA    . GLU B 1 314 ? 26.730  -23.488 60.333 1.00 81.79  ? 1531 GLU B CA    1 
ATOM   6149 C  C     . GLU B 1 314 ? 25.229  -23.623 60.433 1.00 70.50  ? 1531 GLU B C     1 
ATOM   6150 O  O     . GLU B 1 314 ? 24.580  -24.099 59.506 1.00 80.05  ? 1531 GLU B O     1 
ATOM   6151 C  CB    . GLU B 1 314 ? 27.235  -24.578 61.285 1.00 102.00 ? 1531 GLU B CB    1 
ATOM   6152 C  CG    . GLU B 1 314 ? 27.033  -26.053 60.914 1.00 119.84 ? 1531 GLU B CG    1 
ATOM   6153 C  CD    . GLU B 1 314 ? 28.308  -26.929 61.101 1.00 134.45 ? 1531 GLU B CD    1 
ATOM   6154 O  OE1   . GLU B 1 314 ? 29.262  -26.552 61.844 1.00 136.70 ? 1531 GLU B OE1   1 
ATOM   6155 O  OE2   . GLU B 1 314 ? 28.285  -28.095 60.642 1.00 139.72 ? 1531 GLU B OE2   1 
ATOM   6156 N  N     . SER B 1 315 ? 24.675  -23.145 61.536 1.00 61.45  ? 1532 SER B N     1 
ATOM   6157 C  CA    . SER B 1 315 ? 23.239  -23.246 61.726 1.00 57.73  ? 1532 SER B CA    1 
ATOM   6158 C  C     . SER B 1 315 ? 22.487  -22.304 60.807 1.00 67.44  ? 1532 SER B C     1 
ATOM   6159 O  O     . SER B 1 315 ? 21.403  -22.636 60.315 1.00 68.99  ? 1532 SER B O     1 
ATOM   6160 C  CB    . SER B 1 315 ? 22.895  -22.890 63.159 1.00 52.72  ? 1532 SER B CB    1 
ATOM   6161 O  OG    . SER B 1 315 ? 21.501  -22.769 63.290 1.00 53.12  ? 1532 SER B OG    1 
ATOM   6162 N  N     . CYS B 1 316 ? 23.072  -21.145 60.540 1.00 64.14  ? 1533 CYS B N     1 
ATOM   6163 C  CA    . CYS B 1 316 ? 22.428  -20.219 59.629 1.00 57.89  ? 1533 CYS B CA    1 
ATOM   6164 C  C     . CYS B 1 316 ? 22.422  -20.771 58.219 1.00 59.35  ? 1533 CYS B C     1 
ATOM   6165 O  O     . CYS B 1 316 ? 21.419  -20.652 57.503 1.00 62.53  ? 1533 CYS B O     1 
ATOM   6166 C  CB    . CYS B 1 316 ? 23.161  -18.875 59.668 1.00 56.58  ? 1533 CYS B CB    1 
ATOM   6167 S  SG    . CYS B 1 316 ? 22.735  -17.824 61.088 1.00 69.85  ? 1533 CYS B SG    1 
ATOM   6168 N  N     . ARG B 1 317 ? 23.510  -21.427 57.818 1.00 52.68  ? 1534 ARG B N     1 
ATOM   6169 C  CA    . ARG B 1 317 ? 23.543  -21.976 56.469 1.00 58.98  ? 1534 ARG B CA    1 
ATOM   6170 C  C     . ARG B 1 317 ? 22.622  -23.185 56.347 1.00 63.57  ? 1534 ARG B C     1 
ATOM   6171 O  O     . ARG B 1 317 ? 21.967  -23.373 55.305 1.00 61.99  ? 1534 ARG B O     1 
ATOM   6172 C  CB    . ARG B 1 317 ? 24.987  -22.268 56.058 1.00 58.54  ? 1534 ARG B CB    1 
ATOM   6173 C  CG    . ARG B 1 317 ? 25.679  -21.000 55.526 1.00 60.69  ? 1534 ARG B CG    1 
ATOM   6174 C  CD    . ARG B 1 317 ? 26.972  -21.279 54.782 1.00 68.80  ? 1534 ARG B CD    1 
ATOM   6175 N  NE    . ARG B 1 317 ? 28.049  -20.409 55.242 1.00 77.79  ? 1534 ARG B NE    1 
ATOM   6176 C  CZ    . ARG B 1 317 ? 28.791  -20.651 56.320 1.00 85.49  ? 1534 ARG B CZ    1 
ATOM   6177 N  NH1   . ARG B 1 317 ? 28.567  -21.734 57.042 1.00 90.54  ? 1534 ARG B NH1   1 
ATOM   6178 N  NH2   . ARG B 1 317 ? 29.753  -19.817 56.686 1.00 83.18  ? 1534 ARG B NH2   1 
ATOM   6179 N  N     . GLU B 1 318 ? 22.495  -23.968 57.418 1.00 63.93  ? 1535 GLU B N     1 
ATOM   6180 C  CA    . GLU B 1 318 ? 21.543  -25.071 57.382 1.00 74.72  ? 1535 GLU B CA    1 
ATOM   6181 C  C     . GLU B 1 318 ? 20.110  -24.559 57.282 1.00 80.67  ? 1535 GLU B C     1 
ATOM   6182 O  O     . GLU B 1 318 ? 19.291  -25.120 56.539 1.00 88.75  ? 1535 GLU B O     1 
ATOM   6183 C  CB    . GLU B 1 318 ? 21.706  -25.972 58.605 1.00 83.86  ? 1535 GLU B CB    1 
ATOM   6184 C  CG    . GLU B 1 318 ? 20.780  -27.186 58.547 1.00 95.81  ? 1535 GLU B CG    1 
ATOM   6185 C  CD    . GLU B 1 318 ? 20.488  -27.777 59.909 1.00 106.17 ? 1535 GLU B CD    1 
ATOM   6186 O  OE1   . GLU B 1 318 ? 19.713  -28.766 59.996 1.00 108.27 ? 1535 GLU B OE1   1 
ATOM   6187 O  OE2   . GLU B 1 318 ? 21.060  -27.260 60.891 1.00 108.27 ? 1535 GLU B OE2   1 
ATOM   6188 N  N     . LEU B 1 319 ? 19.788  -23.497 58.020 1.00 76.17  ? 1536 LEU B N     1 
ATOM   6189 C  CA    . LEU B 1 319 ? 18.452  -22.924 57.916 1.00 64.36  ? 1536 LEU B CA    1 
ATOM   6190 C  C     . LEU B 1 319 ? 18.189  -22.385 56.516 1.00 64.97  ? 1536 LEU B C     1 
ATOM   6191 O  O     . LEU B 1 319 ? 17.117  -22.622 55.934 1.00 66.40  ? 1536 LEU B O     1 
ATOM   6192 C  CB    . LEU B 1 319 ? 18.273  -21.809 58.944 1.00 55.31  ? 1536 LEU B CB    1 
ATOM   6193 C  CG    . LEU B 1 319 ? 16.916  -21.098 58.961 1.00 56.64  ? 1536 LEU B CG    1 
ATOM   6194 C  CD1   . LEU B 1 319 ? 15.773  -22.090 59.165 1.00 62.62  ? 1536 LEU B CD1   1 
ATOM   6195 C  CD2   . LEU B 1 319 ? 16.876  -20.026 60.038 1.00 48.94  ? 1536 LEU B CD2   1 
ATOM   6196 N  N     . GLU B 1 320 ? 19.159  -21.676 55.943 1.00 58.55  ? 1537 GLU B N     1 
ATOM   6197 C  CA    . GLU B 1 320 ? 18.924  -21.109 54.623 1.00 56.36  ? 1537 GLU B CA    1 
ATOM   6198 C  C     . GLU B 1 320 ? 18.683  -22.204 53.592 1.00 52.74  ? 1537 GLU B C     1 
ATOM   6199 O  O     . GLU B 1 320 ? 17.779  -22.096 52.754 1.00 38.85  ? 1537 GLU B O     1 
ATOM   6200 C  CB    . GLU B 1 320 ? 20.099  -20.202 54.226 1.00 58.27  ? 1537 GLU B CB    1 
ATOM   6201 C  CG    . GLU B 1 320 ? 21.147  -20.823 53.300 1.00 60.54  ? 1537 GLU B CG    1 
ATOM   6202 C  CD    . GLU B 1 320 ? 22.279  -19.871 52.980 1.00 65.52  ? 1537 GLU B CD    1 
ATOM   6203 O  OE1   . GLU B 1 320 ? 22.477  -19.556 51.784 1.00 37.46  ? 1537 GLU B OE1   1 
ATOM   6204 O  OE2   . GLU B 1 320 ? 22.953  -19.416 53.933 1.00 77.35  ? 1537 GLU B OE2   1 
ATOM   6205 N  N     . GLN B 1 321 ? 19.421  -23.303 53.673 1.00 65.18  ? 1538 GLN B N     1 
ATOM   6206 C  CA    . GLN B 1 321 ? 19.233  -24.320 52.647 1.00 87.48  ? 1538 GLN B CA    1 
ATOM   6207 C  C     . GLN B 1 321 ? 17.958  -25.153 52.870 1.00 84.53  ? 1538 GLN B C     1 
ATOM   6208 O  O     . GLN B 1 321 ? 17.327  -25.585 51.901 1.00 88.65  ? 1538 GLN B O     1 
ATOM   6209 C  CB    . GLN B 1 321 ? 20.507  -25.138 52.454 1.00 102.95 ? 1538 GLN B CB    1 
ATOM   6210 C  CG    . GLN B 1 321 ? 21.522  -24.281 51.625 1.00 115.15 ? 1538 GLN B CG    1 
ATOM   6211 C  CD    . GLN B 1 321 ? 21.297  -24.381 50.093 1.00 122.64 ? 1538 GLN B CD    1 
ATOM   6212 O  OE1   . GLN B 1 321 ? 20.766  -25.380 49.589 1.00 130.08 ? 1538 GLN B OE1   1 
ATOM   6213 N  NE2   . GLN B 1 321 ? 21.553  -23.271 49.387 1.00 119.98 ? 1538 GLN B NE2   1 
ATOM   6214 N  N     . THR B 1 322 ? 17.581  -25.432 54.120 1.00 66.43  ? 1539 THR B N     1 
ATOM   6215 C  CA    . THR B 1 322 ? 16.258  -26.036 54.292 1.00 68.08  ? 1539 THR B CA    1 
ATOM   6216 C  C     . THR B 1 322 ? 15.140  -25.106 53.824 1.00 71.30  ? 1539 THR B C     1 
ATOM   6217 O  O     . THR B 1 322 ? 14.044  -25.584 53.517 1.00 81.27  ? 1539 THR B O     1 
ATOM   6218 C  CB    . THR B 1 322 ? 15.995  -26.467 55.737 1.00 76.62  ? 1539 THR B CB    1 
ATOM   6219 O  OG1   . THR B 1 322 ? 14.817  -27.277 55.761 1.00 88.52  ? 1539 THR B OG1   1 
ATOM   6220 C  CG2   . THR B 1 322 ? 15.771  -25.278 56.630 1.00 73.11  ? 1539 THR B CG2   1 
ATOM   6221 N  N     . PHE B 1 323 ? 15.384  -23.791 53.771 1.00 63.37  ? 1540 PHE B N     1 
ATOM   6222 C  CA    . PHE B 1 323 ? 14.429  -22.911 53.097 1.00 55.70  ? 1540 PHE B CA    1 
ATOM   6223 C  C     . PHE B 1 323 ? 14.454  -23.129 51.596 1.00 65.70  ? 1540 PHE B C     1 
ATOM   6224 O  O     . PHE B 1 323 ? 13.405  -23.156 50.947 1.00 70.29  ? 1540 PHE B O     1 
ATOM   6225 C  CB    . PHE B 1 323 ? 14.732  -21.450 53.392 1.00 46.87  ? 1540 PHE B CB    1 
ATOM   6226 C  CG    . PHE B 1 323 ? 14.196  -20.994 54.687 1.00 55.47  ? 1540 PHE B CG    1 
ATOM   6227 C  CD1   . PHE B 1 323 ? 12.882  -21.232 55.018 1.00 60.85  ? 1540 PHE B CD1   1 
ATOM   6228 C  CD2   . PHE B 1 323 ? 15.007  -20.346 55.595 1.00 62.87  ? 1540 PHE B CD2   1 
ATOM   6229 C  CE1   . PHE B 1 323 ? 12.380  -20.824 56.247 1.00 65.30  ? 1540 PHE B CE1   1 
ATOM   6230 C  CE2   . PHE B 1 323 ? 14.511  -19.938 56.817 1.00 67.40  ? 1540 PHE B CE2   1 
ATOM   6231 C  CZ    . PHE B 1 323 ? 13.197  -20.175 57.146 1.00 63.69  ? 1540 PHE B CZ    1 
ATOM   6232 N  N     . VAL B 1 324 ? 15.646  -23.274 51.025 1.00 68.46  ? 1541 VAL B N     1 
ATOM   6233 C  CA    . VAL B 1 324 ? 15.729  -23.458 49.580 1.00 61.35  ? 1541 VAL B CA    1 
ATOM   6234 C  C     . VAL B 1 324 ? 15.015  -24.740 49.170 1.00 67.88  ? 1541 VAL B C     1 
ATOM   6235 O  O     . VAL B 1 324 ? 14.249  -24.761 48.198 1.00 63.88  ? 1541 VAL B O     1 
ATOM   6236 C  CB    . VAL B 1 324 ? 17.201  -23.469 49.126 1.00 40.83  ? 1541 VAL B CB    1 
ATOM   6237 C  CG1   . VAL B 1 324 ? 17.289  -23.558 47.616 1.00 35.94  ? 1541 VAL B CG1   1 
ATOM   6238 C  CG2   . VAL B 1 324 ? 17.922  -22.233 49.610 1.00 36.63  ? 1541 VAL B CG2   1 
ATOM   6239 N  N     . LYS B 1 325 ? 15.205  -25.814 49.944 1.00 73.57  ? 1542 LYS B N     1 
ATOM   6240 C  CA    . LYS B 1 325 ? 14.582  -27.095 49.620 1.00 73.17  ? 1542 LYS B CA    1 
ATOM   6241 C  C     . LYS B 1 325 ? 13.059  -27.011 49.702 1.00 78.35  ? 1542 LYS B C     1 
ATOM   6242 O  O     . LYS B 1 325 ? 12.354  -27.704 48.960 1.00 83.20  ? 1542 LYS B O     1 
ATOM   6243 C  CB    . LYS B 1 325 ? 15.125  -28.195 50.546 1.00 59.47  ? 1542 LYS B CB    1 
ATOM   6244 N  N     . ALA B 1 326 ? 12.530  -26.169 50.589 1.00 67.46  ? 1543 ALA B N     1 
ATOM   6245 C  CA    . ALA B 1 326 ? 11.109  -25.876 50.606 1.00 53.84  ? 1543 ALA B CA    1 
ATOM   6246 C  C     . ALA B 1 326 ? 10.755  -24.790 49.627 1.00 66.13  ? 1543 ALA B C     1 
ATOM   6247 O  O     . ALA B 1 326 ? 9.753   -24.103 49.831 1.00 72.18  ? 1543 ALA B O     1 
ATOM   6248 C  CB    . ALA B 1 326 ? 10.647  -25.465 52.003 1.00 46.68  ? 1543 ALA B CB    1 
ATOM   6249 N  N     . GLY B 1 327 ? 11.574  -24.594 48.592 1.00 70.72  ? 1544 GLY B N     1 
ATOM   6250 C  CA    . GLY B 1 327 ? 11.220  -23.702 47.508 1.00 65.77  ? 1544 GLY B CA    1 
ATOM   6251 C  C     . GLY B 1 327 ? 11.233  -22.229 47.835 1.00 63.63  ? 1544 GLY B C     1 
ATOM   6252 O  O     . GLY B 1 327 ? 10.563  -21.452 47.165 1.00 71.20  ? 1544 GLY B O     1 
ATOM   6253 N  N     . ILE B 1 328 ? 11.960  -21.813 48.853 1.00 62.72  ? 1545 ILE B N     1 
ATOM   6254 C  CA    . ILE B 1 328 ? 12.018  -20.412 49.232 1.00 55.19  ? 1545 ILE B CA    1 
ATOM   6255 C  C     . ILE B 1 328 ? 13.330  -19.807 48.754 1.00 62.37  ? 1545 ILE B C     1 
ATOM   6256 O  O     . ILE B 1 328 ? 14.400  -20.396 48.943 1.00 63.90  ? 1545 ILE B O     1 
ATOM   6257 C  CB    . ILE B 1 328 ? 11.874  -20.249 50.748 1.00 47.24  ? 1545 ILE B CB    1 
ATOM   6258 C  CG1   . ILE B 1 328 ? 10.417  -20.497 51.165 1.00 44.22  ? 1545 ILE B CG1   1 
ATOM   6259 C  CG2   . ILE B 1 328 ? 12.423  -18.876 51.177 1.00 41.48  ? 1545 ILE B CG2   1 
ATOM   6260 C  CD1   . ILE B 1 328 ? 10.211  -20.559 52.685 1.00 39.84  ? 1545 ILE B CD1   1 
ATOM   6261 N  N     . ARG B 1 329 ? 13.253  -18.642 48.111 1.00 62.52  ? 1546 ARG B N     1 
ATOM   6262 C  CA    . ARG B 1 329 ? 14.459  -17.925 47.702 1.00 58.09  ? 1546 ARG B CA    1 
ATOM   6263 C  C     . ARG B 1 329 ? 15.009  -17.278 48.959 1.00 63.67  ? 1546 ARG B C     1 
ATOM   6264 O  O     . ARG B 1 329 ? 14.579  -16.208 49.377 1.00 67.51  ? 1546 ARG B O     1 
ATOM   6265 C  CB    . ARG B 1 329 ? 14.167  -16.910 46.613 1.00 47.46  ? 1546 ARG B CB    1 
ATOM   6266 C  CG    . ARG B 1 329 ? 13.773  -17.545 45.295 1.00 55.20  ? 1546 ARG B CG    1 
ATOM   6267 C  CD    . ARG B 1 329 ? 13.619  -16.517 44.189 1.00 59.61  ? 1546 ARG B CD    1 
ATOM   6268 N  NE    . ARG B 1 329 ? 12.549  -15.565 44.476 1.00 56.86  ? 1546 ARG B NE    1 
ATOM   6269 C  CZ    . ARG B 1 329 ? 11.260  -15.820 44.299 1.00 57.44  ? 1546 ARG B CZ    1 
ATOM   6270 N  NH1   . ARG B 1 329 ? 10.877  -16.998 43.837 1.00 64.34  ? 1546 ARG B NH1   1 
ATOM   6271 N  NH2   . ARG B 1 329 ? 10.356  -14.903 44.584 1.00 58.49  ? 1546 ARG B NH2   1 
ATOM   6272 N  N     . CYS B 1 330 ? 15.937  -17.975 49.605 1.00 53.51  ? 1547 CYS B N     1 
ATOM   6273 C  CA    . CYS B 1 330 ? 16.518  -17.528 50.856 1.00 40.59  ? 1547 CYS B CA    1 
ATOM   6274 C  C     . CYS B 1 330 ? 18.039  -17.468 50.717 1.00 47.82  ? 1547 CYS B C     1 
ATOM   6275 O  O     . CYS B 1 330 ? 18.664  -18.352 50.130 1.00 50.16  ? 1547 CYS B O     1 
ATOM   6276 C  CB    . CYS B 1 330 ? 16.142  -18.432 52.013 1.00 36.75  ? 1547 CYS B CB    1 
ATOM   6277 S  SG    . CYS B 1 330 ? 17.214  -18.163 53.409 1.00 53.00  ? 1547 CYS B SG    1 
ATOM   6278 N  N     . GLU B 1 331 ? 18.618  -16.407 51.268 1.00 46.79  ? 1548 GLU B N     1 
ATOM   6279 C  CA    . GLU B 1 331 ? 20.063  -16.309 51.369 1.00 48.06  ? 1548 GLU B CA    1 
ATOM   6280 C  C     . GLU B 1 331 ? 20.442  -15.754 52.730 1.00 49.84  ? 1548 GLU B C     1 
ATOM   6281 O  O     . GLU B 1 331 ? 19.643  -15.098 53.396 1.00 49.56  ? 1548 GLU B O     1 
ATOM   6282 C  CB    . GLU B 1 331 ? 20.627  -15.441 50.258 1.00 57.65  ? 1548 GLU B CB    1 
ATOM   6283 C  CG    . GLU B 1 331 ? 20.882  -16.229 49.002 1.00 73.69  ? 1548 GLU B CG    1 
ATOM   6284 C  CD    . GLU B 1 331 ? 21.036  -15.345 47.769 1.00 80.57  ? 1548 GLU B CD    1 
ATOM   6285 O  OE1   . GLU B 1 331 ? 20.396  -15.654 46.731 1.00 84.63  ? 1548 GLU B OE1   1 
ATOM   6286 O  OE2   . GLU B 1 331 ? 21.800  -14.353 47.840 1.00 74.76  ? 1548 GLU B OE2   1 
ATOM   6287 N  N     . GLY B 1 332 ? 21.660  -16.063 53.160 1.00 48.43  ? 1549 GLY B N     1 
ATOM   6288 C  CA    . GLY B 1 332 ? 22.208  -15.507 54.379 1.00 58.73  ? 1549 GLY B CA    1 
ATOM   6289 C  C     . GLY B 1 332 ? 23.168  -14.380 54.047 1.00 59.87  ? 1549 GLY B C     1 
ATOM   6290 O  O     . GLY B 1 332 ? 23.720  -14.323 52.955 1.00 73.02  ? 1549 GLY B O     1 
ATOM   6291 N  N     . ASP B 1 333 ? 23.346  -13.459 54.982 1.00 47.85  ? 1550 ASP B N     1 
ATOM   6292 C  CA    . ASP B 1 333 ? 24.324  -12.386 54.827 1.00 49.77  ? 1550 ASP B CA    1 
ATOM   6293 C  C     . ASP B 1 333 ? 25.390  -12.573 55.909 1.00 60.52  ? 1550 ASP B C     1 
ATOM   6294 O  O     . ASP B 1 333 ? 25.182  -12.178 57.063 1.00 49.48  ? 1550 ASP B O     1 
ATOM   6295 C  CB    . ASP B 1 333 ? 23.627  -11.029 54.924 1.00 56.91  ? 1550 ASP B CB    1 
ATOM   6296 C  CG    . ASP B 1 333 ? 24.590  -9.846  54.869 1.00 63.76  ? 1550 ASP B CG    1 
ATOM   6297 O  OD1   . ASP B 1 333 ? 25.472  -9.699  55.749 1.00 69.07  ? 1550 ASP B OD1   1 
ATOM   6298 O  OD2   . ASP B 1 333 ? 24.440  -9.039  53.935 1.00 63.18  ? 1550 ASP B OD2   1 
ATOM   6299 N  N     . TYR B 1 334 ? 26.518  -13.207 55.559 1.00 67.43  ? 1551 TYR B N     1 
ATOM   6300 C  CA    . TYR B 1 334 ? 27.575  -13.441 56.543 1.00 65.78  ? 1551 TYR B CA    1 
ATOM   6301 C  C     . TYR B 1 334 ? 28.843  -12.675 56.190 1.00 74.12  ? 1551 TYR B C     1 
ATOM   6302 O  O     . TYR B 1 334 ? 29.877  -13.287 55.908 1.00 93.87  ? 1551 TYR B O     1 
ATOM   6303 C  CB    . TYR B 1 334 ? 27.932  -14.929 56.673 1.00 64.53  ? 1551 TYR B CB    1 
ATOM   6304 C  CG    . TYR B 1 334 ? 26.802  -15.898 56.444 1.00 69.44  ? 1551 TYR B CG    1 
ATOM   6305 C  CD1   . TYR B 1 334 ? 25.941  -16.235 57.467 1.00 80.76  ? 1551 TYR B CD1   1 
ATOM   6306 C  CD2   . TYR B 1 334 ? 26.613  -16.500 55.212 1.00 59.87  ? 1551 TYR B CD2   1 
ATOM   6307 C  CE1   . TYR B 1 334 ? 24.907  -17.126 57.268 1.00 77.54  ? 1551 TYR B CE1   1 
ATOM   6308 C  CE2   . TYR B 1 334 ? 25.580  -17.390 55.006 1.00 54.40  ? 1551 TYR B CE2   1 
ATOM   6309 C  CZ    . TYR B 1 334 ? 24.730  -17.699 56.035 1.00 63.69  ? 1551 TYR B CZ    1 
ATOM   6310 O  OH    . TYR B 1 334 ? 23.695  -18.583 55.837 1.00 66.99  ? 1551 TYR B OH    1 
ATOM   6311 N  N     . ARG B 1 335 ? 28.789  -11.357 56.164 1.00 63.37  ? 1552 ARG B N     1 
ATOM   6312 C  CA    . ARG B 1 335 ? 29.965  -10.560 55.852 1.00 57.00  ? 1552 ARG B CA    1 
ATOM   6313 C  C     . ARG B 1 335 ? 30.527  -10.040 57.160 1.00 67.17  ? 1552 ARG B C     1 
ATOM   6314 O  O     . ARG B 1 335 ? 29.786  -9.458  57.958 1.00 78.63  ? 1552 ARG B O     1 
ATOM   6315 C  CB    . ARG B 1 335 ? 29.606  -9.400  54.925 1.00 48.34  ? 1552 ARG B CB    1 
ATOM   6316 C  CG    . ARG B 1 335 ? 29.047  -9.843  53.625 1.00 42.86  ? 1552 ARG B CG    1 
ATOM   6317 C  CD    . ARG B 1 335 ? 28.456  -8.694  52.874 1.00 51.03  ? 1552 ARG B CD    1 
ATOM   6318 N  NE    . ARG B 1 335 ? 27.158  -8.304  53.396 1.00 61.61  ? 1552 ARG B NE    1 
ATOM   6319 C  CZ    . ARG B 1 335 ? 26.481  -7.243  52.968 1.00 69.94  ? 1552 ARG B CZ    1 
ATOM   6320 N  NH1   . ARG B 1 335 ? 26.981  -6.482  52.006 1.00 64.99  ? 1552 ARG B NH1   1 
ATOM   6321 N  NH2   . ARG B 1 335 ? 25.298  -6.955  53.491 1.00 75.70  ? 1552 ARG B NH2   1 
ATOM   6322 N  N     . ASP B 1 336 ? 31.821  -10.243 57.391 1.00 69.99  ? 1553 ASP B N     1 
ATOM   6323 C  CA    . ASP B 1 336 ? 32.299  -9.899  58.723 1.00 76.87  ? 1553 ASP B CA    1 
ATOM   6324 C  C     . ASP B 1 336 ? 32.654  -8.417  58.873 1.00 71.21  ? 1553 ASP B C     1 
ATOM   6325 O  O     . ASP B 1 336 ? 32.967  -7.985  59.992 1.00 70.82  ? 1553 ASP B O     1 
ATOM   6326 C  CB    . ASP B 1 336 ? 33.478  -10.817 59.122 1.00 91.88  ? 1553 ASP B CB    1 
ATOM   6327 C  CG    . ASP B 1 336 ? 34.558  -10.940 58.050 1.00 104.07 ? 1553 ASP B CG    1 
ATOM   6328 O  OD1   . ASP B 1 336 ? 35.157  -9.907  57.674 1.00 110.50 ? 1553 ASP B OD1   1 
ATOM   6329 O  OD2   . ASP B 1 336 ? 34.849  -12.085 57.621 1.00 105.50 ? 1553 ASP B OD2   1 
ATOM   6330 N  N     . ASN B 1 337 ? 32.607  -7.637  57.786 1.00 69.79  ? 1554 ASN B N     1 
ATOM   6331 C  CA    . ASN B 1 337 ? 32.870  -6.197  57.787 1.00 73.86  ? 1554 ASN B CA    1 
ATOM   6332 C  C     . ASN B 1 337 ? 31.676  -5.326  58.175 1.00 77.23  ? 1554 ASN B C     1 
ATOM   6333 O  O     . ASN B 1 337 ? 31.813  -4.096  58.160 1.00 83.51  ? 1554 ASN B O     1 
ATOM   6334 C  CB    . ASN B 1 337 ? 33.436  -5.715  56.447 1.00 73.94  ? 1554 ASN B CB    1 
ATOM   6335 C  CG    . ASN B 1 337 ? 32.804  -6.378  55.260 1.00 80.11  ? 1554 ASN B CG    1 
ATOM   6336 O  OD1   . ASN B 1 337 ? 32.669  -7.597  55.210 1.00 87.70  ? 1554 ASN B OD1   1 
ATOM   6337 N  ND2   . ASN B 1 337 ? 32.445  -5.578  54.270 1.00 80.11  ? 1554 ASN B ND2   1 
ATOM   6338 N  N     . TYR B 1 338 ? 30.480  -5.882  58.352 1.00 71.78  ? 1555 TYR B N     1 
ATOM   6339 C  CA    . TYR B 1 338 ? 29.321  -5.054  58.675 1.00 68.57  ? 1555 TYR B CA    1 
ATOM   6340 C  C     . TYR B 1 338 ? 28.654  -5.492  59.976 1.00 61.88  ? 1555 TYR B C     1 
ATOM   6341 O  O     . TYR B 1 338 ? 28.645  -6.676  60.332 1.00 64.74  ? 1555 TYR B O     1 
ATOM   6342 C  CB    . TYR B 1 338 ? 28.305  -5.070  57.560 1.00 75.68  ? 1555 TYR B CB    1 
ATOM   6343 C  CG    . TYR B 1 338 ? 28.838  -4.481  56.289 1.00 81.63  ? 1555 TYR B CG    1 
ATOM   6344 C  CD1   . TYR B 1 338 ? 28.842  -5.219  55.112 1.00 79.63  ? 1555 TYR B CD1   1 
ATOM   6345 C  CD2   . TYR B 1 338 ? 29.347  -3.195  56.262 1.00 84.32  ? 1555 TYR B CD2   1 
ATOM   6346 C  CE1   . TYR B 1 338 ? 29.330  -4.691  53.940 1.00 77.59  ? 1555 TYR B CE1   1 
ATOM   6347 C  CE2   . TYR B 1 338 ? 29.840  -2.657  55.091 1.00 87.01  ? 1555 TYR B CE2   1 
ATOM   6348 C  CZ    . TYR B 1 338 ? 29.828  -3.411  53.935 1.00 83.43  ? 1555 TYR B CZ    1 
ATOM   6349 O  OH    . TYR B 1 338 ? 30.315  -2.887  52.766 1.00 83.71  ? 1555 TYR B OH    1 
ATOM   6350 N  N     . SER B 1 339 ? 28.055  -4.531  60.659 1.00 51.84  ? 1556 SER B N     1 
ATOM   6351 C  CA    . SER B 1 339 ? 27.327  -4.836  61.874 1.00 58.04  ? 1556 SER B CA    1 
ATOM   6352 C  C     . SER B 1 339 ? 25.967  -5.430  61.530 1.00 82.13  ? 1556 SER B C     1 
ATOM   6353 O  O     . SER B 1 339 ? 25.446  -5.212  60.434 1.00 90.41  ? 1556 SER B O     1 
ATOM   6354 C  CB    . SER B 1 339 ? 27.117  -3.567  62.675 1.00 54.00  ? 1556 SER B CB    1 
ATOM   6355 O  OG    . SER B 1 339 ? 26.292  -2.703  61.925 1.00 44.71  ? 1556 SER B OG    1 
ATOM   6356 N  N     . PRO B 1 340 ? 25.365  -6.194  62.446 1.00 90.95  ? 1557 PRO B N     1 
ATOM   6357 C  CA    . PRO B 1 340 ? 24.010  -6.701  62.174 1.00 85.76  ? 1557 PRO B CA    1 
ATOM   6358 C  C     . PRO B 1 340 ? 23.004  -5.603  61.890 1.00 73.09  ? 1557 PRO B C     1 
ATOM   6359 O  O     . PRO B 1 340 ? 22.112  -5.784  61.053 1.00 62.21  ? 1557 PRO B O     1 
ATOM   6360 C  CB    . PRO B 1 340 ? 23.676  -7.479  63.452 1.00 89.56  ? 1557 PRO B CB    1 
ATOM   6361 C  CG    . PRO B 1 340 ? 24.994  -8.012  63.882 1.00 96.12  ? 1557 PRO B CG    1 
ATOM   6362 C  CD    . PRO B 1 340 ? 25.987  -6.898  63.581 1.00 100.17 ? 1557 PRO B CD    1 
ATOM   6363 N  N     . GLY B 1 341 ? 23.131  -4.457  62.555 1.00 71.93  ? 1558 GLY B N     1 
ATOM   6364 C  CA    . GLY B 1 341 ? 22.215  -3.364  62.279 1.00 66.82  ? 1558 GLY B CA    1 
ATOM   6365 C  C     . GLY B 1 341 ? 22.436  -2.764  60.906 1.00 55.45  ? 1558 GLY B C     1 
ATOM   6366 O  O     . GLY B 1 341 ? 21.475  -2.409  60.214 1.00 50.02  ? 1558 GLY B O     1 
ATOM   6367 N  N     . TRP B 1 342 ? 23.703  -2.649  60.490 1.00 45.42  ? 1559 TRP B N     1 
ATOM   6368 C  CA    . TRP B 1 342 ? 23.981  -2.243  59.122 1.00 47.66  ? 1559 TRP B CA    1 
ATOM   6369 C  C     . TRP B 1 342 ? 23.270  -3.168  58.147 1.00 62.26  ? 1559 TRP B C     1 
ATOM   6370 O  O     . TRP B 1 342 ? 22.619  -2.705  57.203 1.00 66.51  ? 1559 TRP B O     1 
ATOM   6371 C  CB    . TRP B 1 342 ? 25.487  -2.232  58.859 1.00 47.58  ? 1559 TRP B CB    1 
ATOM   6372 C  CG    . TRP B 1 342 ? 25.862  -1.671  57.495 1.00 64.82  ? 1559 TRP B CG    1 
ATOM   6373 C  CD1   . TRP B 1 342 ? 26.350  -0.429  57.236 1.00 73.76  ? 1559 TRP B CD1   1 
ATOM   6374 C  CD2   . TRP B 1 342 ? 25.760  -2.334  56.213 1.00 66.33  ? 1559 TRP B CD2   1 
ATOM   6375 N  NE1   . TRP B 1 342 ? 26.571  -0.277  55.888 1.00 73.15  ? 1559 TRP B NE1   1 
ATOM   6376 C  CE2   . TRP B 1 342 ? 26.216  -1.429  55.241 1.00 62.84  ? 1559 TRP B CE2   1 
ATOM   6377 C  CE3   . TRP B 1 342 ? 25.343  -3.606  55.803 1.00 66.72  ? 1559 TRP B CE3   1 
ATOM   6378 C  CZ2   . TRP B 1 342 ? 26.261  -1.746  53.890 1.00 59.85  ? 1559 TRP B CZ2   1 
ATOM   6379 C  CZ3   . TRP B 1 342 ? 25.395  -3.918  54.466 1.00 65.86  ? 1559 TRP B CZ3   1 
ATOM   6380 C  CH2   . TRP B 1 342 ? 25.845  -2.989  53.522 1.00 60.18  ? 1559 TRP B CH2   1 
ATOM   6381 N  N     . LYS B 1 343 ? 23.429  -4.487  58.345 1.00 69.33  ? 1560 LYS B N     1 
ATOM   6382 C  CA    . LYS B 1 343 ? 22.805  -5.490  57.483 1.00 65.48  ? 1560 LYS B CA    1 
ATOM   6383 C  C     . LYS B 1 343 ? 21.286  -5.363  57.470 1.00 59.01  ? 1560 LYS B C     1 
ATOM   6384 O  O     . LYS B 1 343 ? 20.658  -5.493  56.406 1.00 48.16  ? 1560 LYS B O     1 
ATOM   6385 C  CB    . LYS B 1 343 ? 23.229  -6.886  57.938 1.00 67.21  ? 1560 LYS B CB    1 
ATOM   6386 N  N     . TYR B 1 344 ? 20.686  -5.132  58.652 1.00 66.93  ? 1561 TYR B N     1 
ATOM   6387 C  CA    . TYR B 1 344 ? 19.266  -4.786  58.776 1.00 71.72  ? 1561 TYR B CA    1 
ATOM   6388 C  C     . TYR B 1 344 ? 18.886  -3.650  57.832 1.00 66.43  ? 1561 TYR B C     1 
ATOM   6389 O  O     . TYR B 1 344 ? 17.919  -3.753  57.064 1.00 65.77  ? 1561 TYR B O     1 
ATOM   6390 C  CB    . TYR B 1 344 ? 18.921  -4.379  60.212 1.00 86.34  ? 1561 TYR B CB    1 
ATOM   6391 C  CG    . TYR B 1 344 ? 19.009  -5.444  61.300 1.00 95.48  ? 1561 TYR B CG    1 
ATOM   6392 C  CD1   . TYR B 1 344 ? 19.300  -6.765  61.002 1.00 97.92  ? 1561 TYR B CD1   1 
ATOM   6393 C  CD2   . TYR B 1 344 ? 18.785  -5.110  62.643 1.00 95.03  ? 1561 TYR B CD2   1 
ATOM   6394 C  CE1   . TYR B 1 344 ? 19.380  -7.725  62.007 1.00 97.87  ? 1561 TYR B CE1   1 
ATOM   6395 C  CE2   . TYR B 1 344 ? 18.854  -6.060  63.645 1.00 91.95  ? 1561 TYR B CE2   1 
ATOM   6396 C  CZ    . TYR B 1 344 ? 19.154  -7.366  63.319 1.00 94.47  ? 1561 TYR B CZ    1 
ATOM   6397 O  OH    . TYR B 1 344 ? 19.232  -8.319  64.304 1.00 97.98  ? 1561 TYR B OH    1 
ATOM   6398 N  N     . ASN B 1 345 ? 19.602  -2.529  57.921 1.00 39.78  ? 1562 ASN B N     1 
ATOM   6399 C  CA    . ASN B 1 345 ? 19.226  -1.394  57.085 1.00 43.98  ? 1562 ASN B CA    1 
ATOM   6400 C  C     . ASN B 1 345 ? 19.422  -1.711  55.611 1.00 42.95  ? 1562 ASN B C     1 
ATOM   6401 O  O     . ASN B 1 345 ? 18.552  -1.425  54.779 1.00 37.20  ? 1562 ASN B O     1 
ATOM   6402 C  CB    . ASN B 1 345 ? 20.031  -0.146  57.433 1.00 50.58  ? 1562 ASN B CB    1 
ATOM   6403 C  CG    . ASN B 1 345 ? 19.651  1.038   56.551 1.00 60.15  ? 1562 ASN B CG    1 
ATOM   6404 O  OD1   . ASN B 1 345 ? 20.370  1.409   55.610 1.00 62.21  ? 1562 ASN B OD1   1 
ATOM   6405 N  ND2   . ASN B 1 345 ? 18.492  1.615   56.834 1.00 62.45  ? 1562 ASN B ND2   1 
ATOM   6406 N  N     . HIS B 1 346 ? 20.568  -2.288  55.267 1.00 37.70  ? 1563 HIS B N     1 
ATOM   6407 C  CA    . HIS B 1 346 ? 20.853  -2.621  53.878 1.00 59.65  ? 1563 HIS B CA    1 
ATOM   6408 C  C     . HIS B 1 346 ? 19.714  -3.409  53.254 1.00 53.87  ? 1563 HIS B C     1 
ATOM   6409 O  O     . HIS B 1 346 ? 19.174  -3.043  52.202 1.00 35.11  ? 1563 HIS B O     1 
ATOM   6410 C  CB    . HIS B 1 346 ? 22.145  -3.414  53.792 1.00 60.96  ? 1563 HIS B CB    1 
ATOM   6411 C  CG    . HIS B 1 346 ? 22.510  -3.800  52.398 1.00 50.68  ? 1563 HIS B CG    1 
ATOM   6412 N  ND1   . HIS B 1 346 ? 22.498  -5.107  51.964 1.00 52.37  ? 1563 HIS B ND1   1 
ATOM   6413 C  CD2   . HIS B 1 346 ? 22.887  -3.051  51.339 1.00 44.82  ? 1563 HIS B CD2   1 
ATOM   6414 C  CE1   . HIS B 1 346 ? 22.863  -5.151  50.696 1.00 54.82  ? 1563 HIS B CE1   1 
ATOM   6415 N  NE2   . HIS B 1 346 ? 23.104  -3.916  50.295 1.00 56.25  ? 1563 HIS B NE2   1 
ATOM   6416 N  N     . TRP B 1 347 ? 19.371  -4.533  53.870 1.00 52.91  ? 1564 TRP B N     1 
ATOM   6417 C  CA    . TRP B 1 347 ? 18.296  -5.320  53.303 1.00 52.74  ? 1564 TRP B CA    1 
ATOM   6418 C  C     . TRP B 1 347 ? 16.941  -4.644  53.461 1.00 47.81  ? 1564 TRP B C     1 
ATOM   6419 O  O     . TRP B 1 347 ? 16.029  -4.953  52.694 1.00 52.26  ? 1564 TRP B O     1 
ATOM   6420 C  CB    . TRP B 1 347 ? 18.310  -6.719  53.914 1.00 59.17  ? 1564 TRP B CB    1 
ATOM   6421 C  CG    . TRP B 1 347 ? 19.624  -7.383  53.648 1.00 58.26  ? 1564 TRP B CG    1 
ATOM   6422 C  CD1   . TRP B 1 347 ? 20.616  -7.635  54.548 1.00 54.15  ? 1564 TRP B CD1   1 
ATOM   6423 C  CD2   . TRP B 1 347 ? 20.112  -7.833  52.378 1.00 53.52  ? 1564 TRP B CD2   1 
ATOM   6424 N  NE1   . TRP B 1 347 ? 21.679  -8.238  53.921 1.00 47.43  ? 1564 TRP B NE1   1 
ATOM   6425 C  CE2   . TRP B 1 347 ? 21.393  -8.370  52.589 1.00 41.58  ? 1564 TRP B CE2   1 
ATOM   6426 C  CE3   . TRP B 1 347 ? 19.584  -7.839  51.085 1.00 60.55  ? 1564 TRP B CE3   1 
ATOM   6427 C  CZ2   . TRP B 1 347 ? 22.154  -8.901  51.560 1.00 40.82  ? 1564 TRP B CZ2   1 
ATOM   6428 C  CZ3   . TRP B 1 347 ? 20.345  -8.371  50.064 1.00 59.25  ? 1564 TRP B CZ3   1 
ATOM   6429 C  CH2   . TRP B 1 347 ? 21.615  -8.895  50.309 1.00 50.71  ? 1564 TRP B CH2   1 
ATOM   6430 N  N     . GLU B 1 348 ? 16.780  -3.708  54.400 1.00 45.01  ? 1565 GLU B N     1 
ATOM   6431 C  CA    . GLU B 1 348 ? 15.514  -2.984  54.446 1.00 49.27  ? 1565 GLU B CA    1 
ATOM   6432 C  C     . GLU B 1 348 ? 15.355  -2.061  53.244 1.00 49.24  ? 1565 GLU B C     1 
ATOM   6433 O  O     . GLU B 1 348 ? 14.234  -1.868  52.764 1.00 45.10  ? 1565 GLU B O     1 
ATOM   6434 C  CB    . GLU B 1 348 ? 15.414  -2.167  55.738 1.00 58.35  ? 1565 GLU B CB    1 
ATOM   6435 C  CG    . GLU B 1 348 ? 14.973  -2.927  56.977 1.00 68.99  ? 1565 GLU B CG    1 
ATOM   6436 C  CD    . GLU B 1 348 ? 14.294  -2.029  58.015 1.00 94.93  ? 1565 GLU B CD    1 
ATOM   6437 O  OE1   . GLU B 1 348 ? 13.681  -2.572  58.961 1.00 101.71 ? 1565 GLU B OE1   1 
ATOM   6438 O  OE2   . GLU B 1 348 ? 14.359  -0.781  57.885 1.00 106.07 ? 1565 GLU B OE2   1 
ATOM   6439 N  N     . LEU B 1 349 ? 16.461  -1.493  52.739 1.00 50.40  ? 1566 LEU B N     1 
ATOM   6440 C  CA    . LEU B 1 349 ? 16.390  -0.688  51.521 1.00 42.10  ? 1566 LEU B CA    1 
ATOM   6441 C  C     . LEU B 1 349 ? 16.124  -1.566  50.315 1.00 49.94  ? 1566 LEU B C     1 
ATOM   6442 O  O     . LEU B 1 349 ? 15.473  -1.137  49.360 1.00 55.95  ? 1566 LEU B O     1 
ATOM   6443 C  CB    . LEU B 1 349 ? 17.667  0.138   51.307 1.00 40.06  ? 1566 LEU B CB    1 
ATOM   6444 C  CG    . LEU B 1 349 ? 17.999  1.370   52.178 1.00 45.41  ? 1566 LEU B CG    1 
ATOM   6445 C  CD1   . LEU B 1 349 ? 19.478  1.693   52.210 1.00 36.01  ? 1566 LEU B CD1   1 
ATOM   6446 C  CD2   . LEU B 1 349 ? 17.242  2.580   51.723 1.00 51.07  ? 1566 LEU B CD2   1 
ATOM   6447 N  N     . LYS B 1 350 ? 16.669  -2.776  50.308 1.00 57.94  ? 1567 LYS B N     1 
ATOM   6448 C  CA    . LYS B 1 350 ? 16.412  -3.686  49.201 1.00 53.55  ? 1567 LYS B CA    1 
ATOM   6449 C  C     . LYS B 1 350 ? 15.045  -4.350  49.306 1.00 49.75  ? 1567 LYS B C     1 
ATOM   6450 O  O     . LYS B 1 350 ? 14.627  -5.041  48.374 1.00 44.98  ? 1567 LYS B O     1 
ATOM   6451 C  CB    . LYS B 1 350 ? 17.542  -4.709  49.103 1.00 46.06  ? 1567 LYS B CB    1 
ATOM   6452 C  CG    . LYS B 1 350 ? 18.879  -4.046  48.719 1.00 45.38  ? 1567 LYS B CG    1 
ATOM   6453 C  CD    . LYS B 1 350 ? 19.962  -5.068  48.453 1.00 49.68  ? 1567 LYS B CD    1 
ATOM   6454 C  CE    . LYS B 1 350 ? 20.295  -5.084  46.989 1.00 47.92  ? 1567 LYS B CE    1 
ATOM   6455 N  NZ    . LYS B 1 350 ? 21.250  -6.165  46.668 1.00 40.80  ? 1567 LYS B NZ    1 
ATOM   6456 N  N     . GLY B 1 351 ? 14.326  -4.114  50.397 1.00 55.31  ? 1568 GLY B N     1 
ATOM   6457 C  CA    . GLY B 1 351 ? 12.940  -4.525  50.490 1.00 59.87  ? 1568 GLY B CA    1 
ATOM   6458 C  C     . GLY B 1 351 ? 12.682  -6.010  50.472 1.00 56.48  ? 1568 GLY B C     1 
ATOM   6459 O  O     . GLY B 1 351 ? 11.608  -6.436  50.026 1.00 56.30  ? 1568 GLY B O     1 
ATOM   6460 N  N     . VAL B 1 352 ? 13.633  -6.808  50.952 1.00 55.27  ? 1569 VAL B N     1 
ATOM   6461 C  CA    . VAL B 1 352 ? 13.451  -8.259  51.068 1.00 43.83  ? 1569 VAL B CA    1 
ATOM   6462 C  C     . VAL B 1 352 ? 12.296  -8.530  52.009 1.00 40.15  ? 1569 VAL B C     1 
ATOM   6463 O  O     . VAL B 1 352 ? 12.260  -7.968  53.125 1.00 35.53  ? 1569 VAL B O     1 
ATOM   6464 C  CB    . VAL B 1 352 ? 14.731  -8.924  51.566 1.00 46.14  ? 1569 VAL B CB    1 
ATOM   6465 C  CG1   . VAL B 1 352 ? 14.499  -10.395 51.778 1.00 50.28  ? 1569 VAL B CG1   1 
ATOM   6466 C  CG2   . VAL B 1 352 ? 15.858  -8.697  50.564 1.00 50.74  ? 1569 VAL B CG2   1 
ATOM   6467 N  N     . PRO B 1 353 ? 11.303  -9.315  51.599 1.00 40.85  ? 1570 PRO B N     1 
ATOM   6468 C  CA    . PRO B 1 353 ? 10.066  -9.394  52.392 1.00 42.22  ? 1570 PRO B CA    1 
ATOM   6469 C  C     . PRO B 1 353 ? 10.290  -9.729  53.857 1.00 49.23  ? 1570 PRO B C     1 
ATOM   6470 O  O     . PRO B 1 353 ? 9.828   -8.987  54.734 1.00 59.13  ? 1570 PRO B O     1 
ATOM   6471 C  CB    . PRO B 1 353 ? 9.256   -10.448 51.636 1.00 41.63  ? 1570 PRO B CB    1 
ATOM   6472 C  CG    . PRO B 1 353 ? 9.686   -10.259 50.170 1.00 33.83  ? 1570 PRO B CG    1 
ATOM   6473 C  CD    . PRO B 1 353 ? 11.173  -9.970  50.277 1.00 33.71  ? 1570 PRO B CD    1 
ATOM   6474 N  N     . VAL B 1 354 ? 11.050  -10.775 54.153 1.00 51.68  ? 1571 VAL B N     1 
ATOM   6475 C  CA    . VAL B 1 354 ? 11.268  -11.191 55.530 1.00 52.62  ? 1571 VAL B CA    1 
ATOM   6476 C  C     . VAL B 1 354 ? 12.758  -11.270 55.827 1.00 57.91  ? 1571 VAL B C     1 
ATOM   6477 O  O     . VAL B 1 354 ? 13.519  -11.884 55.075 1.00 69.35  ? 1571 VAL B O     1 
ATOM   6478 C  CB    . VAL B 1 354 ? 10.605  -12.542 55.819 1.00 53.16  ? 1571 VAL B CB    1 
ATOM   6479 C  CG1   . VAL B 1 354 ? 11.342  -13.246 56.943 1.00 54.73  ? 1571 VAL B CG1   1 
ATOM   6480 C  CG2   . VAL B 1 354 ? 9.148   -12.317 56.179 1.00 63.96  ? 1571 VAL B CG2   1 
ATOM   6481 N  N     . ARG B 1 355 ? 13.166  -10.622 56.908 1.00 38.84  ? 1572 ARG B N     1 
ATOM   6482 C  CA    . ARG B 1 355 ? 14.499  -10.777 57.467 1.00 53.27  ? 1572 ARG B CA    1 
ATOM   6483 C  C     . ARG B 1 355 ? 14.444  -11.810 58.582 1.00 60.91  ? 1572 ARG B C     1 
ATOM   6484 O  O     . ARG B 1 355 ? 13.489  -11.844 59.360 1.00 65.67  ? 1572 ARG B O     1 
ATOM   6485 C  CB    . ARG B 1 355 ? 15.026  -9.458  58.042 1.00 51.57  ? 1572 ARG B CB    1 
ATOM   6486 C  CG    . ARG B 1 355 ? 16.208  -9.604  58.995 1.00 45.73  ? 1572 ARG B CG    1 
ATOM   6487 C  CD    . ARG B 1 355 ? 16.373  -8.367  59.850 1.00 59.57  ? 1572 ARG B CD    1 
ATOM   6488 N  NE    . ARG B 1 355 ? 15.761  -7.199  59.224 1.00 77.19  ? 1572 ARG B NE    1 
ATOM   6489 C  CZ    . ARG B 1 355 ? 15.312  -6.152  59.903 1.00 84.68  ? 1572 ARG B CZ    1 
ATOM   6490 N  NH1   . ARG B 1 355 ? 15.423  -6.140  61.218 1.00 65.23  ? 1572 ARG B NH1   1 
ATOM   6491 N  NH2   . ARG B 1 355 ? 14.752  -5.127  59.274 1.00 102.46 ? 1572 ARG B NH2   1 
ATOM   6492 N  N     . ILE B 1 356 ? 15.435  -12.688 58.627 1.00 56.39  ? 1573 ILE B N     1 
ATOM   6493 C  CA    . ILE B 1 356 ? 15.576  -13.611 59.743 1.00 59.26  ? 1573 ILE B CA    1 
ATOM   6494 C  C     . ILE B 1 356 ? 16.663  -13.092 60.669 1.00 42.69  ? 1573 ILE B C     1 
ATOM   6495 O  O     . ILE B 1 356 ? 17.737  -12.685 60.206 1.00 42.18  ? 1573 ILE B O     1 
ATOM   6496 C  CB    . ILE B 1 356 ? 15.885  -15.034 59.266 1.00 61.91  ? 1573 ILE B CB    1 
ATOM   6497 C  CG1   . ILE B 1 356 ? 14.605  -15.668 58.751 1.00 55.12  ? 1573 ILE B CG1   1 
ATOM   6498 C  CG2   . ILE B 1 356 ? 16.394  -15.858 60.418 1.00 63.87  ? 1573 ILE B CG2   1 
ATOM   6499 C  CD1   . ILE B 1 356 ? 14.660  -17.160 58.673 1.00 52.22  ? 1573 ILE B CD1   1 
ATOM   6500 N  N     . GLU B 1 357 ? 16.368  -13.079 61.969 1.00 43.98  ? 1574 GLU B N     1 
ATOM   6501 C  CA    . GLU B 1 357 ? 17.319  -12.772 63.027 1.00 73.82  ? 1574 GLU B CA    1 
ATOM   6502 C  C     . GLU B 1 357 ? 17.582  -14.078 63.759 1.00 81.34  ? 1574 GLU B C     1 
ATOM   6503 O  O     . GLU B 1 357 ? 16.668  -14.648 64.379 1.00 93.82  ? 1574 GLU B O     1 
ATOM   6504 C  CB    . GLU B 1 357 ? 16.781  -11.712 63.995 1.00 68.68  ? 1574 GLU B CB    1 
ATOM   6505 C  CG    . GLU B 1 357 ? 16.571  -10.315 63.389 1.00 68.79  ? 1574 GLU B CG    1 
ATOM   6506 C  CD    . GLU B 1 357 ? 15.875  -9.334  64.343 1.00 64.82  ? 1574 GLU B CD    1 
ATOM   6507 O  OE1   . GLU B 1 357 ? 15.643  -9.685  65.523 1.00 66.35  ? 1574 GLU B OE1   1 
ATOM   6508 O  OE2   . GLU B 1 357 ? 15.552  -8.209  63.910 1.00 55.50  ? 1574 GLU B OE2   1 
ATOM   6509 N  N     . LEU B 1 358 ? 18.831  -14.533 63.705 1.00 66.40  ? 1575 LEU B N     1 
ATOM   6510 C  CA    . LEU B 1 358 ? 19.234  -15.792 64.310 1.00 61.47  ? 1575 LEU B CA    1 
ATOM   6511 C  C     . LEU B 1 358 ? 20.428  -15.477 65.197 1.00 58.25  ? 1575 LEU B C     1 
ATOM   6512 O  O     . LEU B 1 358 ? 21.555  -15.360 64.714 1.00 47.75  ? 1575 LEU B O     1 
ATOM   6513 C  CB    . LEU B 1 358 ? 19.584  -16.815 63.231 1.00 60.51  ? 1575 LEU B CB    1 
ATOM   6514 C  CG    . LEU B 1 358 ? 19.694  -18.309 63.579 1.00 61.75  ? 1575 LEU B CG    1 
ATOM   6515 C  CD1   . LEU B 1 358 ? 21.070  -18.653 64.085 1.00 65.03  ? 1575 LEU B CD1   1 
ATOM   6516 C  CD2   . LEU B 1 358 ? 18.644  -18.758 64.584 1.00 48.53  ? 1575 LEU B CD2   1 
ATOM   6517 N  N     . GLY B 1 359 ? 20.164  -15.328 66.495 1.00 62.76  ? 1576 GLY B N     1 
ATOM   6518 C  CA    . GLY B 1 359 ? 21.199  -15.117 67.477 1.00 71.22  ? 1576 GLY B CA    1 
ATOM   6519 C  C     . GLY B 1 359 ? 21.457  -16.372 68.293 1.00 77.15  ? 1576 GLY B C     1 
ATOM   6520 O  O     . GLY B 1 359 ? 20.870  -17.430 68.074 1.00 75.03  ? 1576 GLY B O     1 
ATOM   6521 N  N     . PHE B 1 360 ? 22.350  -16.223 69.277 1.00 77.48  ? 1577 PHE B N     1 
ATOM   6522 C  CA    . PHE B 1 360 ? 22.714  -17.371 70.100 1.00 77.93  ? 1577 PHE B CA    1 
ATOM   6523 C  C     . PHE B 1 360 ? 21.568  -17.783 71.011 1.00 83.87  ? 1577 PHE B C     1 
ATOM   6524 O  O     . PHE B 1 360 ? 21.367  -18.978 71.254 1.00 95.59  ? 1577 PHE B O     1 
ATOM   6525 C  CB    . PHE B 1 360 ? 23.982  -17.073 70.912 1.00 74.62  ? 1577 PHE B CB    1 
ATOM   6526 C  CG    . PHE B 1 360 ? 25.227  -16.995 70.075 1.00 74.69  ? 1577 PHE B CG    1 
ATOM   6527 C  CD1   . PHE B 1 360 ? 25.748  -18.130 69.476 1.00 77.33  ? 1577 PHE B CD1   1 
ATOM   6528 C  CD2   . PHE B 1 360 ? 25.852  -15.784 69.845 1.00 71.18  ? 1577 PHE B CD2   1 
ATOM   6529 C  CE1   . PHE B 1 360 ? 26.883  -18.062 68.677 1.00 68.42  ? 1577 PHE B CE1   1 
ATOM   6530 C  CE2   . PHE B 1 360 ? 26.979  -15.715 69.048 1.00 64.52  ? 1577 PHE B CE2   1 
ATOM   6531 C  CZ    . PHE B 1 360 ? 27.491  -16.859 68.464 1.00 64.65  ? 1577 PHE B CZ    1 
ATOM   6532 N  N     . LYS B 1 361 ? 20.803  -16.816 71.521 1.00 73.33  ? 1578 LYS B N     1 
ATOM   6533 C  CA    . LYS B 1 361 ? 19.683  -17.165 72.388 1.00 72.69  ? 1578 LYS B CA    1 
ATOM   6534 C  C     . LYS B 1 361 ? 18.613  -17.915 71.604 1.00 77.50  ? 1578 LYS B C     1 
ATOM   6535 O  O     . LYS B 1 361 ? 17.990  -18.852 72.121 1.00 82.83  ? 1578 LYS B O     1 
ATOM   6536 C  CB    . LYS B 1 361 ? 19.116  -15.916 73.058 1.00 68.37  ? 1578 LYS B CB    1 
ATOM   6537 N  N     . ASP B 1 362 ? 18.338  -17.467 70.379 1.00 74.27  ? 1579 ASP B N     1 
ATOM   6538 C  CA    . ASP B 1 362 ? 17.434  -18.207 69.512 1.00 79.22  ? 1579 ASP B CA    1 
ATOM   6539 C  C     . ASP B 1 362 ? 17.968  -19.605 69.210 1.00 81.22  ? 1579 ASP B C     1 
ATOM   6540 O  O     . ASP B 1 362 ? 17.190  -20.562 69.116 1.00 89.92  ? 1579 ASP B O     1 
ATOM   6541 C  CB    . ASP B 1 362 ? 17.193  -17.414 68.228 1.00 89.28  ? 1579 ASP B CB    1 
ATOM   6542 C  CG    . ASP B 1 362 ? 16.871  -15.944 68.499 1.00 105.48 ? 1579 ASP B CG    1 
ATOM   6543 O  OD1   . ASP B 1 362 ? 17.653  -15.059 68.073 1.00 107.57 ? 1579 ASP B OD1   1 
ATOM   6544 O  OD2   . ASP B 1 362 ? 15.834  -15.675 69.153 1.00 111.52 ? 1579 ASP B OD2   1 
ATOM   6545 N  N     . LEU B 1 363 ? 19.291  -19.748 69.066 1.00 74.23  ? 1580 LEU B N     1 
ATOM   6546 C  CA    . LEU B 1 363 ? 19.895  -21.068 68.851 1.00 63.82  ? 1580 LEU B CA    1 
ATOM   6547 C  C     . LEU B 1 363 ? 19.646  -21.996 70.034 1.00 70.02  ? 1580 LEU B C     1 
ATOM   6548 O  O     . LEU B 1 363 ? 19.297  -23.171 69.870 1.00 75.53  ? 1580 LEU B O     1 
ATOM   6549 C  CB    . LEU B 1 363 ? 21.396  -20.927 68.612 1.00 60.26  ? 1580 LEU B CB    1 
ATOM   6550 C  CG    . LEU B 1 363 ? 21.956  -21.081 67.200 1.00 66.46  ? 1580 LEU B CG    1 
ATOM   6551 C  CD1   . LEU B 1 363 ? 23.429  -20.707 67.198 1.00 76.44  ? 1580 LEU B CD1   1 
ATOM   6552 C  CD2   . LEU B 1 363 ? 21.768  -22.486 66.659 1.00 62.19  ? 1580 LEU B CD2   1 
ATOM   6553 N  N     . GLN B 1 364 ? 19.851  -21.485 71.241 1.00 69.52  ? 1581 GLN B N     1 
ATOM   6554 C  CA    . GLN B 1 364 ? 19.630  -22.284 72.427 1.00 71.10  ? 1581 GLN B CA    1 
ATOM   6555 C  C     . GLN B 1 364 ? 18.204  -22.803 72.509 1.00 77.16  ? 1581 GLN B C     1 
ATOM   6556 O  O     . GLN B 1 364 ? 17.962  -23.788 73.218 1.00 80.41  ? 1581 GLN B O     1 
ATOM   6557 C  CB    . GLN B 1 364 ? 19.971  -21.460 73.656 1.00 70.85  ? 1581 GLN B CB    1 
ATOM   6558 C  CG    . GLN B 1 364 ? 21.439  -21.173 73.776 1.00 74.05  ? 1581 GLN B CG    1 
ATOM   6559 C  CD    . GLN B 1 364 ? 21.756  -20.614 75.126 1.00 81.13  ? 1581 GLN B CD    1 
ATOM   6560 O  OE1   . GLN B 1 364 ? 20.914  -19.949 75.727 1.00 76.42  ? 1581 GLN B OE1   1 
ATOM   6561 N  NE2   . GLN B 1 364 ? 22.953  -20.909 75.640 1.00 87.50  ? 1581 GLN B NE2   1 
ATOM   6562 N  N     . ASN B 1 365 ? 17.305  -22.157 71.797 1.00 75.69  ? 1582 ASN B N     1 
ATOM   6563 C  CA    . ASN B 1 365 ? 15.925  -22.541 71.831 1.00 77.42  ? 1582 ASN B CA    1 
ATOM   6564 C  C     . ASN B 1 365 ? 15.327  -23.123 70.597 1.00 77.16  ? 1582 ASN B C     1 
ATOM   6565 O  O     . ASN B 1 365 ? 14.143  -23.214 70.485 1.00 88.96  ? 1582 ASN B O     1 
ATOM   6566 C  CB    . ASN B 1 365 ? 15.108  -21.396 72.273 1.00 73.98  ? 1582 ASN B CB    1 
ATOM   6567 C  CG    . ASN B 1 365 ? 14.494  -21.637 73.599 1.00 85.93  ? 1582 ASN B CG    1 
ATOM   6568 O  OD1   . ASN B 1 365 ? 13.818  -22.633 73.797 1.00 88.60  ? 1582 ASN B OD1   1 
ATOM   6569 N  ND2   . ASN B 1 365 ? 14.725  -20.730 74.525 1.00 90.55  ? 1582 ASN B ND2   1 
ATOM   6570 N  N     . ASP B 1 366 ? 16.169  -23.546 69.698 1.00 66.82  ? 1583 ASP B N     1 
ATOM   6571 C  CA    . ASP B 1 366 ? 15.764  -24.187 68.447 1.00 64.85  ? 1583 ASP B CA    1 
ATOM   6572 C  C     . ASP B 1 366 ? 14.695  -23.382 67.714 1.00 69.37  ? 1583 ASP B C     1 
ATOM   6573 O  O     . ASP B 1 366 ? 13.680  -23.908 67.249 1.00 63.96  ? 1583 ASP B O     1 
ATOM   6574 C  CB    . ASP B 1 366 ? 15.298  -25.621 68.704 1.00 73.42  ? 1583 ASP B CB    1 
ATOM   6575 C  CG    . ASP B 1 366 ? 15.277  -26.470 67.433 1.00 85.78  ? 1583 ASP B CG    1 
ATOM   6576 O  OD1   . ASP B 1 366 ? 16.179  -26.306 66.582 1.00 83.55  ? 1583 ASP B OD1   1 
ATOM   6577 O  OD2   . ASP B 1 366 ? 14.363  -27.319 67.293 1.00 93.14  ? 1583 ASP B OD2   1 
ATOM   6578 N  N     . GLN B 1 367 ? 14.979  -22.099 67.534 1.00 77.36  ? 1584 GLN B N     1 
ATOM   6579 C  CA    . GLN B 1 367 ? 14.029  -21.188 66.928 1.00 78.55  ? 1584 GLN B CA    1 
ATOM   6580 C  C     . GLN B 1 367 ? 14.806  -20.081 66.225 1.00 75.70  ? 1584 GLN B C     1 
ATOM   6581 O  O     . GLN B 1 367 ? 16.037  -20.129 66.127 1.00 72.36  ? 1584 GLN B O     1 
ATOM   6582 C  CB    . GLN B 1 367 ? 13.066  -20.644 67.990 1.00 77.19  ? 1584 GLN B CB    1 
ATOM   6583 C  CG    . GLN B 1 367 ? 13.784  -20.150 69.214 1.00 82.22  ? 1584 GLN B CG    1 
ATOM   6584 C  CD    . GLN B 1 367 ? 12.853  -19.568 70.254 1.00 85.57  ? 1584 GLN B CD    1 
ATOM   6585 O  OE1   . GLN B 1 367 ? 11.860  -20.198 70.644 1.00 86.41  ? 1584 GLN B OE1   1 
ATOM   6586 N  NE2   . GLN B 1 367 ? 13.182  -18.361 70.731 1.00 80.76  ? 1584 GLN B NE2   1 
ATOM   6587 N  N     . PHE B 1 368 ? 14.064  -19.100 65.712 1.00 71.63  ? 1585 PHE B N     1 
ATOM   6588 C  CA    . PHE B 1 368 ? 14.590  -17.911 65.050 1.00 62.55  ? 1585 PHE B CA    1 
ATOM   6589 C  C     . PHE B 1 368 ? 13.474  -16.888 65.006 1.00 56.64  ? 1585 PHE B C     1 
ATOM   6590 O  O     . PHE B 1 368 ? 12.303  -17.248 65.114 1.00 63.15  ? 1585 PHE B O     1 
ATOM   6591 C  CB    . PHE B 1 368 ? 15.072  -18.232 63.635 1.00 64.62  ? 1585 PHE B CB    1 
ATOM   6592 C  CG    . PHE B 1 368 ? 13.999  -18.771 62.741 1.00 64.89  ? 1585 PHE B CG    1 
ATOM   6593 C  CD1   . PHE B 1 368 ? 13.685  -20.125 62.757 1.00 70.28  ? 1585 PHE B CD1   1 
ATOM   6594 C  CD2   . PHE B 1 368 ? 13.311  -17.925 61.869 1.00 58.95  ? 1585 PHE B CD2   1 
ATOM   6595 C  CE1   . PHE B 1 368 ? 12.692  -20.629 61.931 1.00 76.30  ? 1585 PHE B CE1   1 
ATOM   6596 C  CE2   . PHE B 1 368 ? 12.324  -18.412 61.032 1.00 52.24  ? 1585 PHE B CE2   1 
ATOM   6597 C  CZ    . PHE B 1 368 ? 12.007  -19.762 61.058 1.00 66.80  ? 1585 PHE B CZ    1 
ATOM   6598 N  N     . VAL B 1 369 ? 13.804  -15.615 64.794 1.00 56.04  ? 1586 VAL B N     1 
ATOM   6599 C  CA    . VAL B 1 369 ? 12.756  -14.596 64.714 1.00 66.66  ? 1586 VAL B CA    1 
ATOM   6600 C  C     . VAL B 1 369 ? 12.667  -14.069 63.296 1.00 68.29  ? 1586 VAL B C     1 
ATOM   6601 O  O     . VAL B 1 369 ? 13.693  -13.772 62.672 1.00 65.71  ? 1586 VAL B O     1 
ATOM   6602 C  CB    . VAL B 1 369 ? 12.983  -13.448 65.712 1.00 64.46  ? 1586 VAL B CB    1 
ATOM   6603 C  CG1   . VAL B 1 369 ? 11.676  -12.680 65.933 1.00 56.16  ? 1586 VAL B CG1   1 
ATOM   6604 C  CG2   . VAL B 1 369 ? 13.537  -13.974 67.034 1.00 67.47  ? 1586 VAL B CG2   1 
ATOM   6605 N  N     . ALA B 1 370 ? 11.444  -13.980 62.773 1.00 65.15  ? 1587 ALA B N     1 
ATOM   6606 C  CA    . ALA B 1 370 ? 11.180  -13.443 61.447 1.00 67.45  ? 1587 ALA B CA    1 
ATOM   6607 C  C     . ALA B 1 370 ? 10.624  -12.029 61.582 1.00 65.45  ? 1587 ALA B C     1 
ATOM   6608 O  O     . ALA B 1 370 ? 9.786   -11.768 62.451 1.00 76.05  ? 1587 ALA B O     1 
ATOM   6609 C  CB    . ALA B 1 370 ? 10.207  -14.340 60.688 1.00 65.50  ? 1587 ALA B CB    1 
ATOM   6610 N  N     . VAL B 1 371 ? 11.130  -11.108 60.759 1.00 48.46  ? 1588 VAL B N     1 
ATOM   6611 C  CA    . VAL B 1 371 ? 10.717  -9.709  60.775 1.00 58.41  ? 1588 VAL B CA    1 
ATOM   6612 C  C     . VAL B 1 371 ? 10.229  -9.326  59.381 1.00 59.88  ? 1588 VAL B C     1 
ATOM   6613 O  O     . VAL B 1 371 ? 10.952  -9.521  58.398 1.00 59.96  ? 1588 VAL B O     1 
ATOM   6614 C  CB    . VAL B 1 371 ? 11.877  -8.804  61.236 1.00 56.47  ? 1588 VAL B CB    1 
ATOM   6615 C  CG1   . VAL B 1 371 ? 11.488  -7.335  61.209 1.00 42.65  ? 1588 VAL B CG1   1 
ATOM   6616 C  CG2   . VAL B 1 371 ? 12.312  -9.204  62.633 1.00 57.89  ? 1588 VAL B CG2   1 
ATOM   6617 N  N     . ARG B 1 372 ? 9.035   -8.725  59.303 1.00 59.28  ? 1589 ARG B N     1 
ATOM   6618 C  CA    . ARG B 1 372 ? 8.424   -8.382  58.017 1.00 65.88  ? 1589 ARG B CA    1 
ATOM   6619 C  C     . ARG B 1 372 ? 8.834   -6.993  57.542 1.00 61.24  ? 1589 ARG B C     1 
ATOM   6620 O  O     . ARG B 1 372 ? 8.904   -6.050  58.334 1.00 56.55  ? 1589 ARG B O     1 
ATOM   6621 C  CB    . ARG B 1 372 ? 6.904   -8.444  58.112 1.00 71.84  ? 1589 ARG B CB    1 
ATOM   6622 C  CG    . ARG B 1 372 ? 6.390   -9.750  58.636 1.00 76.08  ? 1589 ARG B CG    1 
ATOM   6623 C  CD    . ARG B 1 372 ? 4.986   -9.585  59.162 1.00 74.46  ? 1589 ARG B CD    1 
ATOM   6624 N  NE    . ARG B 1 372 ? 4.113   -9.057  58.128 1.00 68.86  ? 1589 ARG B NE    1 
ATOM   6625 C  CZ    . ARG B 1 372 ? 2.793   -9.035  58.205 1.00 65.39  ? 1589 ARG B CZ    1 
ATOM   6626 N  NH1   . ARG B 1 372 ? 2.181   -9.521  59.279 1.00 65.73  ? 1589 ARG B NH1   1 
ATOM   6627 N  NH2   . ARG B 1 372 ? 2.094   -8.519  57.204 1.00 63.14  ? 1589 ARG B NH2   1 
ATOM   6628 N  N     . ARG B 1 373 ? 9.057   -6.860  56.228 1.00 50.51  ? 1590 ARG B N     1 
ATOM   6629 C  CA    . ARG B 1 373 ? 9.478   -5.567  55.702 1.00 40.85  ? 1590 ARG B CA    1 
ATOM   6630 C  C     . ARG B 1 373 ? 8.340   -4.568  55.726 1.00 52.85  ? 1590 ARG B C     1 
ATOM   6631 O  O     . ARG B 1 373 ? 8.577   -3.376  55.927 1.00 49.06  ? 1590 ARG B O     1 
ATOM   6632 C  CB    . ARG B 1 373 ? 10.027  -5.730  54.288 1.00 43.63  ? 1590 ARG B CB    1 
ATOM   6633 C  CG    . ARG B 1 373 ? 10.529  -4.452  53.623 1.00 38.36  ? 1590 ARG B CG    1 
ATOM   6634 C  CD    . ARG B 1 373 ? 11.552  -3.671  54.473 1.00 36.65  ? 1590 ARG B CD    1 
ATOM   6635 N  NE    . ARG B 1 373 ? 11.904  -2.401  53.842 1.00 41.16  ? 1590 ARG B NE    1 
ATOM   6636 C  CZ    . ARG B 1 373 ? 11.097  -1.344  53.812 1.00 45.15  ? 1590 ARG B CZ    1 
ATOM   6637 N  NH1   . ARG B 1 373 ? 9.914   -1.406  54.394 1.00 57.52  ? 1590 ARG B NH1   1 
ATOM   6638 N  NH2   . ARG B 1 373 ? 11.456  -0.232  53.190 1.00 38.88  ? 1590 ARG B NH2   1 
ATOM   6639 N  N     . ASP B 1 374 ? 7.108   -5.029  55.509 1.00 72.80  ? 1591 ASP B N     1 
ATOM   6640 C  CA    . ASP B 1 374 ? 5.908   -4.216  55.692 1.00 67.31  ? 1591 ASP B CA    1 
ATOM   6641 C  C     . ASP B 1 374 ? 5.469   -4.334  57.150 1.00 74.43  ? 1591 ASP B C     1 
ATOM   6642 O  O     . ASP B 1 374 ? 5.359   -5.441  57.681 1.00 91.30  ? 1591 ASP B O     1 
ATOM   6643 C  CB    . ASP B 1 374 ? 4.800   -4.664  54.736 1.00 54.66  ? 1591 ASP B CB    1 
ATOM   6644 C  CG    . ASP B 1 374 ? 4.170   -6.001  55.132 1.00 54.08  ? 1591 ASP B CG    1 
ATOM   6645 O  OD1   . ASP B 1 374 ? 4.846   -6.873  55.718 1.00 52.82  ? 1591 ASP B OD1   1 
ATOM   6646 O  OD2   . ASP B 1 374 ? 2.972   -6.178  54.861 1.00 58.37  ? 1591 ASP B OD2   1 
ATOM   6647 N  N     . ASN B 1 375 ? 5.271   -3.201  57.803 1.00 57.64  ? 1592 ASN B N     1 
ATOM   6648 C  CA    . ASN B 1 375 ? 4.800   -3.113  59.192 1.00 64.89  ? 1592 ASN B CA    1 
ATOM   6649 C  C     . ASN B 1 375 ? 5.798   -3.640  60.225 1.00 63.29  ? 1592 ASN B C     1 
ATOM   6650 O  O     . ASN B 1 375 ? 5.549   -3.514  61.430 1.00 55.39  ? 1592 ASN B O     1 
ATOM   6651 C  CB    . ASN B 1 375 ? 3.394   -3.742  59.365 1.00 61.30  ? 1592 ASN B CB    1 
ATOM   6652 C  CG    . ASN B 1 375 ? 3.384   -5.248  59.579 1.00 60.57  ? 1592 ASN B CG    1 
ATOM   6653 O  OD1   . ASN B 1 375 ? 4.267   -5.846  60.177 1.00 64.52  ? 1592 ASN B OD1   1 
ATOM   6654 N  ND2   . ASN B 1 375 ? 2.336   -5.865  59.089 1.00 67.72  ? 1592 ASN B ND2   1 
ATOM   6655 N  N     . GLY B 1 376 ? 6.890   -4.273  59.786 1.00 65.78  ? 1593 GLY B N     1 
ATOM   6656 C  CA    . GLY B 1 376 ? 8.000   -4.544  60.688 1.00 56.99  ? 1593 GLY B CA    1 
ATOM   6657 C  C     . GLY B 1 376 ? 7.714   -5.475  61.831 1.00 61.39  ? 1593 GLY B C     1 
ATOM   6658 O  O     . GLY B 1 376 ? 8.432   -5.441  62.833 1.00 66.24  ? 1593 GLY B O     1 
ATOM   6659 N  N     . ALA B 1 377 ? 6.653   -6.266  61.738 1.00 68.78  ? 1594 ALA B N     1 
ATOM   6660 C  CA    . ALA B 1 377 ? 6.275   -7.136  62.838 1.00 62.06  ? 1594 ALA B CA    1 
ATOM   6661 C  C     . ALA B 1 377 ? 7.255   -8.284  62.974 1.00 64.15  ? 1594 ALA B C     1 
ATOM   6662 O  O     . ALA B 1 377 ? 7.634   -8.926  61.991 1.00 64.92  ? 1594 ALA B O     1 
ATOM   6663 C  CB    . ALA B 1 377 ? 4.872   -7.691  62.629 1.00 60.08  ? 1594 ALA B CB    1 
ATOM   6664 N  N     . LYS B 1 378 ? 7.658   -8.535  64.209 1.00 70.87  ? 1595 LYS B N     1 
ATOM   6665 C  CA    . LYS B 1 378 ? 8.516   -9.652  64.550 1.00 75.04  ? 1595 LYS B CA    1 
ATOM   6666 C  C     . LYS B 1 378 ? 7.664   -10.812 65.044 1.00 81.56  ? 1595 LYS B C     1 
ATOM   6667 O  O     . LYS B 1 378 ? 6.582   -10.615 65.598 1.00 79.13  ? 1595 LYS B O     1 
ATOM   6668 C  CB    . LYS B 1 378 ? 9.519   -9.230  65.618 1.00 74.08  ? 1595 LYS B CB    1 
ATOM   6669 C  CG    . LYS B 1 378 ? 10.224  -7.938  65.266 1.00 74.96  ? 1595 LYS B CG    1 
ATOM   6670 C  CD    . LYS B 1 378 ? 11.374  -7.669  66.205 1.00 80.91  ? 1595 LYS B CD    1 
ATOM   6671 C  CE    . LYS B 1 378 ? 12.571  -7.089  65.469 1.00 75.56  ? 1595 LYS B CE    1 
ATOM   6672 N  NZ    . LYS B 1 378 ? 13.815  -7.813  65.832 1.00 73.51  ? 1595 LYS B NZ    1 
ATOM   6673 N  N     . GLN B 1 379 ? 8.176   -12.025 64.857 1.00 87.54  ? 1596 GLN B N     1 
ATOM   6674 C  CA    . GLN B 1 379 ? 7.463   -13.222 65.289 1.00 90.81  ? 1596 GLN B CA    1 
ATOM   6675 C  C     . GLN B 1 379 ? 8.439   -14.387 65.325 1.00 91.69  ? 1596 GLN B C     1 
ATOM   6676 O  O     . GLN B 1 379 ? 9.138   -14.635 64.339 1.00 92.12  ? 1596 GLN B O     1 
ATOM   6677 C  CB    . GLN B 1 379 ? 6.296   -13.536 64.352 1.00 85.42  ? 1596 GLN B CB    1 
ATOM   6678 C  CG    . GLN B 1 379 ? 5.748   -14.928 64.531 1.00 83.05  ? 1596 GLN B CG    1 
ATOM   6679 C  CD    . GLN B 1 379 ? 5.307   -15.545 63.230 1.00 80.79  ? 1596 GLN B CD    1 
ATOM   6680 O  OE1   . GLN B 1 379 ? 5.527   -14.981 62.160 1.00 78.30  ? 1596 GLN B OE1   1 
ATOM   6681 N  NE2   . GLN B 1 379 ? 4.689   -16.718 63.310 1.00 82.00  ? 1596 GLN B NE2   1 
ATOM   6682 N  N     . THR B 1 380 ? 8.491   -15.090 66.455 1.00 86.27  ? 1597 THR B N     1 
ATOM   6683 C  CA    . THR B 1 380 ? 9.442   -16.181 66.645 1.00 83.08  ? 1597 THR B CA    1 
ATOM   6684 C  C     . THR B 1 380 ? 8.864   -17.508 66.163 1.00 79.34  ? 1597 THR B C     1 
ATOM   6685 O  O     . THR B 1 380 ? 7.653   -17.740 66.243 1.00 78.15  ? 1597 THR B O     1 
ATOM   6686 C  CB    . THR B 1 380 ? 9.866   -16.287 68.108 1.00 78.97  ? 1597 THR B CB    1 
ATOM   6687 O  OG1   . THR B 1 380 ? 8.853   -16.977 68.847 1.00 83.67  ? 1597 THR B OG1   1 
ATOM   6688 C  CG2   . THR B 1 380 ? 10.085  -14.891 68.693 1.00 76.30  ? 1597 THR B CG2   1 
ATOM   6689 N  N     . ILE B 1 381 ? 9.737   -18.348 65.601 1.00 72.47  ? 1598 ILE B N     1 
ATOM   6690 C  CA    . ILE B 1 381 ? 9.371   -19.586 64.916 1.00 66.34  ? 1598 ILE B CA    1 
ATOM   6691 C  C     . ILE B 1 381 ? 10.388  -20.672 65.259 1.00 68.15  ? 1598 ILE B C     1 
ATOM   6692 O  O     . ILE B 1 381 ? 11.592  -20.479 65.071 1.00 65.56  ? 1598 ILE B O     1 
ATOM   6693 C  CB    . ILE B 1 381 ? 9.309   -19.368 63.391 1.00 63.70  ? 1598 ILE B CB    1 
ATOM   6694 C  CG1   . ILE B 1 381 ? 8.382   -18.185 63.072 1.00 64.60  ? 1598 ILE B CG1   1 
ATOM   6695 C  CG2   . ILE B 1 381 ? 8.895   -20.660 62.669 1.00 61.41  ? 1598 ILE B CG2   1 
ATOM   6696 C  CD1   . ILE B 1 381 ? 8.537   -17.581 61.695 1.00 62.92  ? 1598 ILE B CD1   1 
ATOM   6697 N  N     . LYS B 1 382 ? 9.909   -21.819 65.736 1.00 70.41  ? 1599 LYS B N     1 
ATOM   6698 C  CA    . LYS B 1 382 ? 10.790  -22.942 66.024 1.00 58.76  ? 1599 LYS B CA    1 
ATOM   6699 C  C     . LYS B 1 382 ? 11.273  -23.571 64.721 1.00 59.53  ? 1599 LYS B C     1 
ATOM   6700 O  O     . LYS B 1 382 ? 10.587  -23.532 63.696 1.00 61.44  ? 1599 LYS B O     1 
ATOM   6701 C  CB    . LYS B 1 382 ? 10.060  -23.982 66.878 1.00 54.24  ? 1599 LYS B CB    1 
ATOM   6702 N  N     . ARG B 1 383 ? 12.452  -24.195 64.767 1.00 64.91  ? 1600 ARG B N     1 
ATOM   6703 C  CA    . ARG B 1 383 ? 13.067  -24.622 63.511 1.00 76.66  ? 1600 ARG B CA    1 
ATOM   6704 C  C     . ARG B 1 383 ? 12.327  -25.784 62.865 1.00 74.75  ? 1600 ARG B C     1 
ATOM   6705 O  O     . ARG B 1 383 ? 12.537  -26.058 61.677 1.00 62.23  ? 1600 ARG B O     1 
ATOM   6706 C  CB    . ARG B 1 383 ? 14.524  -25.034 63.727 1.00 86.59  ? 1600 ARG B CB    1 
ATOM   6707 C  CG    . ARG B 1 383 ? 15.360  -24.047 64.524 1.00 97.77  ? 1600 ARG B CG    1 
ATOM   6708 C  CD    . ARG B 1 383 ? 16.136  -23.046 63.663 1.00 103.16 ? 1600 ARG B CD    1 
ATOM   6709 N  NE    . ARG B 1 383 ? 16.939  -23.657 62.602 1.00 103.97 ? 1600 ARG B NE    1 
ATOM   6710 C  CZ    . ARG B 1 383 ? 18.185  -23.292 62.306 1.00 101.50 ? 1600 ARG B CZ    1 
ATOM   6711 N  NH1   . ARG B 1 383 ? 18.766  -22.326 63.004 1.00 104.24 ? 1600 ARG B NH1   1 
ATOM   6712 N  NH2   . ARG B 1 383 ? 18.851  -23.886 61.318 1.00 94.03  ? 1600 ARG B NH2   1 
ATOM   6713 N  N     . ALA B 1 384 ? 11.452  -26.460 63.606 1.00 83.99  ? 1601 ALA B N     1 
ATOM   6714 C  CA    . ALA B 1 384 ? 10.668  -27.523 62.994 1.00 84.18  ? 1601 ALA B CA    1 
ATOM   6715 C  C     . ALA B 1 384 ? 9.655   -26.935 62.031 1.00 82.18  ? 1601 ALA B C     1 
ATOM   6716 O  O     . ALA B 1 384 ? 9.579   -27.339 60.865 1.00 78.57  ? 1601 ALA B O     1 
ATOM   6717 C  CB    . ALA B 1 384 ? 9.971   -28.354 64.070 1.00 77.32  ? 1601 ALA B CB    1 
ATOM   6718 N  N     . GLN B 1 385 ? 8.945   -25.907 62.476 1.00 87.36  ? 1602 GLN B N     1 
ATOM   6719 C  CA    . GLN B 1 385 ? 7.879   -25.284 61.712 1.00 81.26  ? 1602 GLN B CA    1 
ATOM   6720 C  C     . GLN B 1 385 ? 8.411   -24.350 60.644 1.00 67.10  ? 1602 GLN B C     1 
ATOM   6721 O  O     . GLN B 1 385 ? 7.624   -23.693 59.958 1.00 60.28  ? 1602 GLN B O     1 
ATOM   6722 C  CB    . GLN B 1 385 ? 6.929   -24.530 62.653 1.00 78.83  ? 1602 GLN B CB    1 
ATOM   6723 N  N     . ALA B 1 386 ? 9.728   -24.302 60.473 1.00 66.39  ? 1603 ALA B N     1 
ATOM   6724 C  CA    . ALA B 1 386 ? 10.312  -23.410 59.488 1.00 45.88  ? 1603 ALA B CA    1 
ATOM   6725 C  C     . ALA B 1 386 ? 9.711   -23.602 58.091 1.00 64.59  ? 1603 ALA B C     1 
ATOM   6726 O  O     . ALA B 1 386 ? 9.300   -22.630 57.449 1.00 66.03  ? 1603 ALA B O     1 
ATOM   6727 C  CB    . ALA B 1 386 ? 11.822  -23.606 59.482 1.00 45.77  ? 1603 ALA B CB    1 
ATOM   6728 N  N     . THR B 1 387 ? 9.637   -24.843 57.596 1.00 73.44  ? 1604 THR B N     1 
ATOM   6729 C  CA    . THR B 1 387 ? 9.074   -25.049 56.252 1.00 75.80  ? 1604 THR B CA    1 
ATOM   6730 C  C     . THR B 1 387 ? 7.558   -24.858 56.166 1.00 83.11  ? 1604 THR B C     1 
ATOM   6731 O  O     . THR B 1 387 ? 7.029   -24.888 55.050 1.00 88.20  ? 1604 THR B O     1 
ATOM   6732 C  CB    . THR B 1 387 ? 9.440   -26.411 55.655 1.00 65.88  ? 1604 THR B CB    1 
ATOM   6733 O  OG1   . THR B 1 387 ? 8.840   -27.452 56.422 1.00 75.02  ? 1604 THR B OG1   1 
ATOM   6734 C  CG2   . THR B 1 387 ? 10.952  -26.591 55.574 1.00 57.02  ? 1604 THR B CG2   1 
ATOM   6735 N  N     . VAL B 1 388 ? 6.828   -24.751 57.273 1.00 81.90  ? 1605 VAL B N     1 
ATOM   6736 C  CA    . VAL B 1 388 ? 5.390   -24.493 57.191 1.00 75.82  ? 1605 VAL B CA    1 
ATOM   6737 C  C     . VAL B 1 388 ? 5.070   -23.030 57.460 1.00 73.50  ? 1605 VAL B C     1 
ATOM   6738 O  O     . VAL B 1 388 ? 4.323   -22.410 56.704 1.00 73.85  ? 1605 VAL B O     1 
ATOM   6739 C  CB    . VAL B 1 388 ? 4.592   -25.428 58.125 1.00 80.27  ? 1605 VAL B CB    1 
ATOM   6740 C  CG1   . VAL B 1 388 ? 4.397   -26.767 57.455 1.00 88.17  ? 1605 VAL B CG1   1 
ATOM   6741 C  CG2   . VAL B 1 388 ? 5.282   -25.594 59.447 1.00 80.29  ? 1605 VAL B CG2   1 
ATOM   6742 N  N     . GLU B 1 389 ? 5.630   -22.453 58.528 1.00 76.59  ? 1606 GLU B N     1 
ATOM   6743 C  CA    . GLU B 1 389 ? 5.315   -21.065 58.863 1.00 78.54  ? 1606 GLU B CA    1 
ATOM   6744 C  C     . GLU B 1 389 ? 5.793   -20.108 57.779 1.00 72.26  ? 1606 GLU B C     1 
ATOM   6745 O  O     . GLU B 1 389 ? 5.043   -19.229 57.339 1.00 67.38  ? 1606 GLU B O     1 
ATOM   6746 C  CB    . GLU B 1 389 ? 5.953   -20.671 60.196 1.00 86.10  ? 1606 GLU B CB    1 
ATOM   6747 C  CG    . GLU B 1 389 ? 5.248   -21.183 61.426 1.00 95.01  ? 1606 GLU B CG    1 
ATOM   6748 C  CD    . GLU B 1 389 ? 3.751   -21.206 61.267 1.00 99.64  ? 1606 GLU B CD    1 
ATOM   6749 O  OE1   . GLU B 1 389 ? 3.158   -22.272 61.537 1.00 102.61 ? 1606 GLU B OE1   1 
ATOM   6750 O  OE2   . GLU B 1 389 ? 3.170   -20.169 60.867 1.00 100.21 ? 1606 GLU B OE2   1 
ATOM   6751 N  N     . MET B 1 390 ? 7.025   -20.297 57.300 1.00 64.90  ? 1607 MET B N     1 
ATOM   6752 C  CA    . MET B 1 390 ? 7.613   -19.322 56.386 1.00 53.60  ? 1607 MET B CA    1 
ATOM   6753 C  C     . MET B 1 390 ? 6.778   -19.127 55.132 1.00 55.93  ? 1607 MET B C     1 
ATOM   6754 O  O     . MET B 1 390 ? 6.497   -17.968 54.786 1.00 69.58  ? 1607 MET B O     1 
ATOM   6755 C  CB    . MET B 1 390 ? 9.057   -19.708 56.063 1.00 41.49  ? 1607 MET B CB    1 
ATOM   6756 C  CG    . MET B 1 390 ? 9.917   -18.533 55.627 1.00 43.34  ? 1607 MET B CG    1 
ATOM   6757 S  SD    . MET B 1 390 ? 9.661   -16.978 56.547 1.00 53.64  ? 1607 MET B SD    1 
ATOM   6758 C  CE    . MET B 1 390 ? 10.993  -16.956 57.738 1.00 43.91  ? 1607 MET B CE    1 
ATOM   6759 N  N     . PRO B 1 391 ? 6.351   -20.162 54.409 1.00 45.98  ? 1608 PRO B N     1 
ATOM   6760 C  CA    . PRO B 1 391 ? 5.487   -19.881 53.258 1.00 44.83  ? 1608 PRO B CA    1 
ATOM   6761 C  C     . PRO B 1 391 ? 4.200   -19.199 53.661 1.00 51.50  ? 1608 PRO B C     1 
ATOM   6762 O  O     . PRO B 1 391 ? 3.742   -18.295 52.949 1.00 66.23  ? 1608 PRO B O     1 
ATOM   6763 C  CB    . PRO B 1 391 ? 5.261   -21.269 52.646 1.00 47.29  ? 1608 PRO B CB    1 
ATOM   6764 C  CG    . PRO B 1 391 ? 6.490   -22.015 53.011 1.00 42.64  ? 1608 PRO B CG    1 
ATOM   6765 C  CD    . PRO B 1 391 ? 6.749   -21.579 54.433 1.00 43.37  ? 1608 PRO B CD    1 
ATOM   6766 N  N     . LYS B 1 392 ? 3.628   -19.557 54.812 1.00 45.93  ? 1609 LYS B N     1 
ATOM   6767 C  CA    . LYS B 1 392 ? 2.436   -18.847 55.258 1.00 60.06  ? 1609 LYS B CA    1 
ATOM   6768 C  C     . LYS B 1 392 ? 2.721   -17.354 55.344 1.00 67.90  ? 1609 LYS B C     1 
ATOM   6769 O  O     . LYS B 1 392 ? 2.043   -16.542 54.694 1.00 76.03  ? 1609 LYS B O     1 
ATOM   6770 C  CB    . LYS B 1 392 ? 1.953   -19.397 56.602 1.00 58.59  ? 1609 LYS B CB    1 
ATOM   6771 N  N     . LEU B 1 393 ? 3.817   -17.016 55.962 1.00 58.67  ? 1610 LEU B N     1 
ATOM   6772 C  CA    . LEU B 1 393 ? 4.212   -15.661 56.114 1.00 48.27  ? 1610 LEU B CA    1 
ATOM   6773 C  C     . LEU B 1 393 ? 4.399   -14.971 54.809 1.00 56.56  ? 1610 LEU B C     1 
ATOM   6774 O  O     . LEU B 1 393 ? 4.068   -13.845 54.681 1.00 65.43  ? 1610 LEU B O     1 
ATOM   6775 C  CB    . LEU B 1 393 ? 5.494   -15.640 56.864 1.00 40.98  ? 1610 LEU B CB    1 
ATOM   6776 C  CG    . LEU B 1 393 ? 5.936   -14.314 57.359 1.00 53.64  ? 1610 LEU B CG    1 
ATOM   6777 C  CD1   . LEU B 1 393 ? 4.795   -13.624 58.000 1.00 50.89  ? 1610 LEU B CD1   1 
ATOM   6778 C  CD2   . LEU B 1 393 ? 7.031   -14.459 58.347 1.00 48.86  ? 1610 LEU B CD2   1 
ATOM   6779 N  N     . LEU B 1 394 ? 4.956   -15.613 53.819 1.00 38.62  ? 1611 LEU B N     1 
ATOM   6780 C  CA    . LEU B 1 394 ? 5.125   -14.947 52.537 1.00 51.50  ? 1611 LEU B CA    1 
ATOM   6781 C  C     . LEU B 1 394 ? 3.769   -14.640 51.915 1.00 56.08  ? 1611 LEU B C     1 
ATOM   6782 O  O     . LEU B 1 394 ? 3.498   -13.491 51.532 1.00 63.76  ? 1611 LEU B O     1 
ATOM   6783 C  CB    . LEU B 1 394 ? 6.023   -15.775 51.616 1.00 40.85  ? 1611 LEU B CB    1 
ATOM   6784 C  CG    . LEU B 1 394 ? 7.478   -15.945 52.090 1.00 43.26  ? 1611 LEU B CG    1 
ATOM   6785 C  CD1   . LEU B 1 394 ? 8.430   -16.055 50.896 1.00 41.49  ? 1611 LEU B CD1   1 
ATOM   6786 C  CD2   . LEU B 1 394 ? 7.946   -14.850 53.042 1.00 37.13  ? 1611 LEU B CD2   1 
ATOM   6787 N  N     . GLU B 1 395 ? 2.854   -15.608 51.946 1.00 53.14  ? 1612 GLU B N     1 
ATOM   6788 C  CA    . GLU B 1 395 ? 1.525   -15.335 51.424 1.00 62.14  ? 1612 GLU B CA    1 
ATOM   6789 C  C     . GLU B 1 395 ? 0.863   -14.247 52.250 1.00 70.86  ? 1612 GLU B C     1 
ATOM   6790 O  O     . GLU B 1 395 ? 0.350   -13.261 51.702 1.00 85.76  ? 1612 GLU B O     1 
ATOM   6791 C  CB    . GLU B 1 395 ? 0.689   -16.615 51.404 1.00 61.62  ? 1612 GLU B CB    1 
ATOM   6792 C  CG    . GLU B 1 395 ? 0.974   -17.503 50.195 1.00 62.67  ? 1612 GLU B CG    1 
ATOM   6793 C  CD    . GLU B 1 395 ? -0.215  -18.359 49.798 1.00 69.50  ? 1612 GLU B CD    1 
ATOM   6794 N  N     . THR B 1 396 ? 0.962   -14.360 53.578 1.00 56.91  ? 1613 THR B N     1 
ATOM   6795 C  CA    . THR B 1 396 ? 0.395   -13.352 54.472 1.00 53.51  ? 1613 THR B CA    1 
ATOM   6796 C  C     . THR B 1 396 ? 0.888   -11.953 54.118 1.00 49.75  ? 1613 THR B C     1 
ATOM   6797 O  O     . THR B 1 396 ? 0.136   -10.976 54.200 1.00 46.55  ? 1613 THR B O     1 
ATOM   6798 C  CB    . THR B 1 396 ? 0.725   -13.699 55.929 1.00 53.85  ? 1613 THR B CB    1 
ATOM   6799 O  OG1   . THR B 1 396 ? -0.123  -14.769 56.369 1.00 60.78  ? 1613 THR B OG1   1 
ATOM   6800 C  CG2   . THR B 1 396 ? 0.540   -12.489 56.848 1.00 41.70  ? 1613 THR B CG2   1 
ATOM   6801 N  N     . ILE B 1 397 ? 2.161   -11.834 53.747 1.00 53.37  ? 1614 ILE B N     1 
ATOM   6802 C  CA    . ILE B 1 397 ? 2.690   -10.520 53.415 1.00 61.55  ? 1614 ILE B CA    1 
ATOM   6803 C  C     . ILE B 1 397 ? 2.048   -10.018 52.133 1.00 63.08  ? 1614 ILE B C     1 
ATOM   6804 O  O     . ILE B 1 397 ? 1.523   -8.898  52.078 1.00 64.31  ? 1614 ILE B O     1 
ATOM   6805 C  CB    . ILE B 1 397 ? 4.224   -10.579 53.306 1.00 65.85  ? 1614 ILE B CB    1 
ATOM   6806 C  CG1   . ILE B 1 397 ? 4.829   -10.703 54.711 1.00 63.03  ? 1614 ILE B CG1   1 
ATOM   6807 C  CG2   . ILE B 1 397 ? 4.738   -9.376  52.538 1.00 67.08  ? 1614 ILE B CG2   1 
ATOM   6808 C  CD1   . ILE B 1 397 ? 6.324   -10.546 54.799 1.00 58.90  ? 1614 ILE B CD1   1 
ATOM   6809 N  N     . HIS B 1 398 ? 2.002   -10.882 51.115 1.00 56.21  ? 1615 HIS B N     1 
ATOM   6810 C  CA    . HIS B 1 398 ? 1.389   -10.534 49.843 1.00 51.16  ? 1615 HIS B CA    1 
ATOM   6811 C  C     . HIS B 1 398 ? 0.015   -9.938  50.058 1.00 46.58  ? 1615 HIS B C     1 
ATOM   6812 O  O     . HIS B 1 398 ? -0.258  -8.801  49.661 1.00 47.65  ? 1615 HIS B O     1 
ATOM   6813 C  CB    . HIS B 1 398 ? 1.277   -11.766 48.956 1.00 52.01  ? 1615 HIS B CB    1 
ATOM   6814 C  CG    . HIS B 1 398 ? 0.702   -11.468 47.615 1.00 42.99  ? 1615 HIS B CG    1 
ATOM   6815 N  ND1   . HIS B 1 398 ? 1.477   -11.049 46.553 1.00 51.20  ? 1615 HIS B ND1   1 
ATOM   6816 C  CD2   . HIS B 1 398 ? -0.570  -11.499 47.168 1.00 44.49  ? 1615 HIS B CD2   1 
ATOM   6817 C  CE1   . HIS B 1 398 ? 0.701   -10.838 45.505 1.00 54.72  ? 1615 HIS B CE1   1 
ATOM   6818 N  NE2   . HIS B 1 398 ? -0.545  -11.105 45.851 1.00 52.51  ? 1615 HIS B NE2   1 
ATOM   6819 N  N     . THR B 1 399 ? -0.834  -10.673 50.771 1.00 48.38  ? 1616 THR B N     1 
ATOM   6820 C  CA    . THR B 1 399 ? -2.205  -10.229 50.964 1.00 49.38  ? 1616 THR B CA    1 
ATOM   6821 C  C     . THR B 1 399 ? -2.233  -8.896  51.673 1.00 54.34  ? 1616 THR B C     1 
ATOM   6822 O  O     . THR B 1 399 ? -2.849  -7.938  51.189 1.00 59.26  ? 1616 THR B O     1 
ATOM   6823 C  CB    . THR B 1 399 ? -2.953  -11.237 51.835 1.00 47.50  ? 1616 THR B CB    1 
ATOM   6824 O  OG1   . THR B 1 399 ? -2.612  -12.581 51.458 1.00 48.25  ? 1616 THR B OG1   1 
ATOM   6825 C  CG2   . THR B 1 399 ? -4.419  -10.993 51.726 1.00 39.15  ? 1616 THR B CG2   1 
ATOM   6826 N  N     . SER B 1 400 ? -1.418  -8.770  52.724 1.00 52.21  ? 1617 SER B N     1 
ATOM   6827 C  CA    . SER B 1 400 ? -1.452  -7.559  53.518 1.00 48.71  ? 1617 SER B CA    1 
ATOM   6828 C  C     . SER B 1 400 ? -0.937  -6.382  52.720 1.00 43.77  ? 1617 SER B C     1 
ATOM   6829 O  O     . SER B 1 400 ? -1.358  -5.250  52.946 1.00 43.31  ? 1617 SER B O     1 
ATOM   6830 C  CB    . SER B 1 400 ? -0.665  -7.731  54.800 1.00 54.22  ? 1617 SER B CB    1 
ATOM   6831 O  OG    . SER B 1 400 ? -0.347  -6.455  55.309 1.00 72.84  ? 1617 SER B OG    1 
ATOM   6832 N  N     . MET B 1 401 ? -0.057  -6.634  51.763 1.00 38.41  ? 1618 MET B N     1 
ATOM   6833 C  CA    . MET B 1 401 ? 0.327   -5.568  50.853 1.00 47.23  ? 1618 MET B CA    1 
ATOM   6834 C  C     . MET B 1 401 ? -0.828  -5.218  49.929 1.00 58.97  ? 1618 MET B C     1 
ATOM   6835 O  O     . MET B 1 401 ? -1.283  -4.068  49.885 1.00 65.46  ? 1618 MET B O     1 
ATOM   6836 C  CB    . MET B 1 401 ? 1.559   -5.992  50.056 1.00 44.07  ? 1618 MET B CB    1 
ATOM   6837 C  CG    . MET B 1 401 ? 2.842   -5.987  50.860 1.00 45.42  ? 1618 MET B CG    1 
ATOM   6838 S  SD    . MET B 1 401 ? 4.227   -6.645  49.933 1.00 49.20  ? 1618 MET B SD    1 
ATOM   6839 C  CE    . MET B 1 401 ? 4.545   -5.349  48.738 1.00 39.41  ? 1618 MET B CE    1 
ATOM   6840 N  N     . TYR B 1 402 ? -1.348  -6.225  49.221 1.00 56.89  ? 1619 TYR B N     1 
ATOM   6841 C  CA    . TYR B 1 402 ? -2.395  -5.973  48.243 1.00 56.70  ? 1619 TYR B CA    1 
ATOM   6842 C  C     . TYR B 1 402 ? -3.583  -5.281  48.881 1.00 60.55  ? 1619 TYR B C     1 
ATOM   6843 O  O     . TYR B 1 402 ? -4.026  -4.225  48.418 1.00 52.98  ? 1619 TYR B O     1 
ATOM   6844 C  CB    . TYR B 1 402 ? -2.844  -7.275  47.602 1.00 54.74  ? 1619 TYR B CB    1 
ATOM   6845 C  CG    . TYR B 1 402 ? -4.011  -7.069  46.675 1.00 60.08  ? 1619 TYR B CG    1 
ATOM   6846 C  CD1   . TYR B 1 402 ? -3.864  -6.358  45.491 1.00 62.87  ? 1619 TYR B CD1   1 
ATOM   6847 C  CD2   . TYR B 1 402 ? -5.262  -7.552  46.994 1.00 57.71  ? 1619 TYR B CD2   1 
ATOM   6848 C  CE1   . TYR B 1 402 ? -4.923  -6.169  44.647 1.00 60.27  ? 1619 TYR B CE1   1 
ATOM   6849 C  CE2   . TYR B 1 402 ? -6.330  -7.354  46.152 1.00 60.93  ? 1619 TYR B CE2   1 
ATOM   6850 C  CZ    . TYR B 1 402 ? -6.152  -6.665  44.981 1.00 60.09  ? 1619 TYR B CZ    1 
ATOM   6851 O  OH    . TYR B 1 402 ? -7.218  -6.463  44.142 1.00 70.00  ? 1619 TYR B OH    1 
ATOM   6852 N  N     . GLU B 1 403 ? -4.101  -5.853  49.964 1.00 69.08  ? 1620 GLU B N     1 
ATOM   6853 C  CA    . GLU B 1 403 ? -5.243  -5.238  50.622 1.00 66.82  ? 1620 GLU B CA    1 
ATOM   6854 C  C     . GLU B 1 403 ? -4.905  -3.826  51.065 1.00 60.96  ? 1620 GLU B C     1 
ATOM   6855 O  O     . GLU B 1 403 ? -5.699  -2.904  50.856 1.00 66.56  ? 1620 GLU B O     1 
ATOM   6856 C  CB    . GLU B 1 403 ? -5.688  -6.090  51.803 1.00 70.86  ? 1620 GLU B CB    1 
ATOM   6857 C  CG    . GLU B 1 403 ? -5.872  -7.538  51.428 1.00 74.64  ? 1620 GLU B CG    1 
ATOM   6858 C  CD    . GLU B 1 403 ? -6.648  -8.316  52.454 1.00 87.86  ? 1620 GLU B CD    1 
ATOM   6859 O  OE1   . GLU B 1 403 ? -6.560  -7.985  53.656 1.00 97.96  ? 1620 GLU B OE1   1 
ATOM   6860 O  OE2   . GLU B 1 403 ? -7.333  -9.278  52.058 1.00 93.17  ? 1620 GLU B OE2   1 
ATOM   6861 N  N     . ARG B 1 404 ? -3.704  -3.616  51.612 1.00 52.43  ? 1621 ARG B N     1 
ATOM   6862 C  CA    . ARG B 1 404 ? -3.355  -2.268  52.038 1.00 43.35  ? 1621 ARG B CA    1 
ATOM   6863 C  C     . ARG B 1 404 ? -3.466  -1.303  50.871 1.00 48.59  ? 1621 ARG B C     1 
ATOM   6864 O  O     . ARG B 1 404 ? -3.977  -0.189  51.031 1.00 63.34  ? 1621 ARG B O     1 
ATOM   6865 C  CB    . ARG B 1 404 ? -1.958  -2.236  52.642 1.00 38.37  ? 1621 ARG B CB    1 
ATOM   6866 C  CG    . ARG B 1 404 ? -1.564  -0.891  53.213 1.00 53.11  ? 1621 ARG B CG    1 
ATOM   6867 C  CD    . ARG B 1 404 ? -0.134  -0.847  53.774 1.00 58.34  ? 1621 ARG B CD    1 
ATOM   6868 N  NE    . ARG B 1 404 ? 0.800   -1.658  52.993 1.00 72.25  ? 1621 ARG B NE    1 
ATOM   6869 C  CZ    . ARG B 1 404 ? 1.270   -2.863  53.346 1.00 74.15  ? 1621 ARG B CZ    1 
ATOM   6870 N  NH1   . ARG B 1 404 ? 0.914   -3.453  54.495 1.00 64.20  ? 1621 ARG B NH1   1 
ATOM   6871 N  NH2   . ARG B 1 404 ? 2.113   -3.483  52.535 1.00 66.59  ? 1621 ARG B NH2   1 
ATOM   6872 N  N     . ALA B 1 405 ? -3.013  -1.721  49.681 1.00 39.26  ? 1622 ALA B N     1 
ATOM   6873 C  CA    . ALA B 1 405 ? -3.140  -0.868  48.502 1.00 43.34  ? 1622 ALA B CA    1 
ATOM   6874 C  C     . ALA B 1 405 ? -4.581  -0.790  48.007 1.00 49.43  ? 1622 ALA B C     1 
ATOM   6875 O  O     . ALA B 1 405 ? -5.034  0.271   47.566 1.00 51.02  ? 1622 ALA B O     1 
ATOM   6876 C  CB    . ALA B 1 405 ? -2.222  -1.355  47.386 1.00 37.54  ? 1622 ALA B CB    1 
ATOM   6877 N  N     . GLU B 1 406 ? -5.334  -1.877  48.122 1.00 55.91  ? 1623 GLU B N     1 
ATOM   6878 C  CA    . GLU B 1 406 ? -6.686  -1.864  47.585 1.00 56.36  ? 1623 GLU B CA    1 
ATOM   6879 C  C     . GLU B 1 406 ? -7.575  -0.932  48.389 1.00 48.40  ? 1623 GLU B C     1 
ATOM   6880 O  O     . GLU B 1 406 ? -8.271  -0.084  47.809 1.00 51.67  ? 1623 GLU B O     1 
ATOM   6881 C  CB    . GLU B 1 406 ? -7.239  -3.288  47.563 1.00 63.54  ? 1623 GLU B CB    1 
ATOM   6882 C  CG    . GLU B 1 406 ? -8.612  -3.452  46.973 1.00 70.76  ? 1623 GLU B CG    1 
ATOM   6883 C  CD    . GLU B 1 406 ? -9.310  -4.668  47.553 1.00 93.35  ? 1623 GLU B CD    1 
ATOM   6884 O  OE1   . GLU B 1 406 ? -9.498  -4.716  48.790 1.00 100.75 ? 1623 GLU B OE1   1 
ATOM   6885 O  OE2   . GLU B 1 406 ? -9.621  -5.604  46.781 1.00 99.88  ? 1623 GLU B OE2   1 
ATOM   6886 N  N     . ARG B 1 407 ? -7.489  -1.005  49.723 1.00 42.26  ? 1624 ARG B N     1 
ATOM   6887 C  CA    . ARG B 1 407 ? -8.196  -0.031  50.547 1.00 51.17  ? 1624 ARG B CA    1 
ATOM   6888 C  C     . ARG B 1 407 ? -7.750  1.371   50.173 1.00 54.89  ? 1624 ARG B C     1 
ATOM   6889 O  O     . ARG B 1 407 ? -8.579  2.278   50.009 1.00 56.35  ? 1624 ARG B O     1 
ATOM   6890 C  CB    . ARG B 1 407 ? -7.943  -0.289  52.033 1.00 59.50  ? 1624 ARG B CB    1 
ATOM   6891 C  CG    . ARG B 1 407 ? -8.964  -1.196  52.738 1.00 73.41  ? 1624 ARG B CG    1 
ATOM   6892 C  CD    . ARG B 1 407 ? -8.288  -2.066  53.823 1.00 84.51  ? 1624 ARG B CD    1 
ATOM   6893 N  NE    . ARG B 1 407 ? -7.190  -1.358  54.492 1.00 86.42  ? 1624 ARG B NE    1 
ATOM   6894 C  CZ    . ARG B 1 407 ? -6.040  -1.924  54.845 1.00 76.65  ? 1624 ARG B CZ    1 
ATOM   6895 N  NH1   . ARG B 1 407 ? -5.830  -3.211  54.590 1.00 65.43  ? 1624 ARG B NH1   1 
ATOM   6896 N  NH2   . ARG B 1 407 ? -5.100  -1.197  55.440 1.00 77.51  ? 1624 ARG B NH2   1 
ATOM   6897 N  N     . ASP B 1 408 ? -6.460  1.524   49.880 1.00 51.10  ? 1625 ASP B N     1 
ATOM   6898 C  CA    . ASP B 1 408 ? -5.972  2.821   49.458 1.00 51.11  ? 1625 ASP B CA    1 
ATOM   6899 C  C     . ASP B 1 408 ? -6.724  3.284   48.219 1.00 51.88  ? 1625 ASP B C     1 
ATOM   6900 O  O     . ASP B 1 408 ? -7.361  4.349   48.223 1.00 61.15  ? 1625 ASP B O     1 
ATOM   6901 C  CB    . ASP B 1 408 ? -4.480  2.720   49.182 1.00 46.25  ? 1625 ASP B CB    1 
ATOM   6902 C  CG    . ASP B 1 408 ? -3.791  4.037   49.284 1.00 57.72  ? 1625 ASP B CG    1 
ATOM   6903 O  OD1   . ASP B 1 408 ? -4.257  4.909   50.066 1.00 58.92  ? 1625 ASP B OD1   1 
ATOM   6904 O  OD2   . ASP B 1 408 ? -2.790  4.192   48.555 1.00 60.49  ? 1625 ASP B OD2   1 
ATOM   6905 N  N     . LEU B 1 409 ? -6.775  2.428   47.199 1.00 38.19  ? 1626 LEU B N     1 
ATOM   6906 C  CA    . LEU B 1 409 ? -7.511  2.774   45.993 1.00 45.99  ? 1626 LEU B CA    1 
ATOM   6907 C  C     . LEU B 1 409 ? -8.965  3.080   46.316 1.00 58.23  ? 1626 LEU B C     1 
ATOM   6908 O  O     . LEU B 1 409 ? -9.530  4.063   45.824 1.00 59.81  ? 1626 LEU B O     1 
ATOM   6909 C  CB    . LEU B 1 409 ? -7.416  1.639   44.983 1.00 40.27  ? 1626 LEU B CB    1 
ATOM   6910 C  CG    . LEU B 1 409 ? -7.430  1.976   43.498 1.00 39.82  ? 1626 LEU B CG    1 
ATOM   6911 C  CD1   . LEU B 1 409 ? -7.143  0.693   42.768 1.00 44.71  ? 1626 LEU B CD1   1 
ATOM   6912 C  CD2   . LEU B 1 409 ? -8.767  2.529   43.062 1.00 43.86  ? 1626 LEU B CD2   1 
ATOM   6913 N  N     . GLN B 1 410 ? -9.591  2.254   47.153 1.00 59.25  ? 1627 GLN B N     1 
ATOM   6914 C  CA    . GLN B 1 410 ? -11.012 2.462   47.397 1.00 63.26  ? 1627 GLN B CA    1 
ATOM   6915 C  C     . GLN B 1 410 ? -11.258 3.788   48.089 1.00 63.76  ? 1627 GLN B C     1 
ATOM   6916 O  O     . GLN B 1 410 ? -12.327 4.384   47.931 1.00 63.95  ? 1627 GLN B O     1 
ATOM   6917 C  CB    . GLN B 1 410 ? -11.577 1.270   48.167 1.00 70.77  ? 1627 GLN B CB    1 
ATOM   6918 C  CG    . GLN B 1 410 ? -11.709 0.098   47.196 1.00 78.70  ? 1627 GLN B CG    1 
ATOM   6919 C  CD    . GLN B 1 410 ? -12.357 -1.142  47.768 1.00 81.08  ? 1627 GLN B CD    1 
ATOM   6920 O  OE1   . GLN B 1 410 ? -12.305 -1.401  48.972 1.00 86.58  ? 1627 GLN B OE1   1 
ATOM   6921 N  NE2   . GLN B 1 410 ? -12.992 -1.917  46.895 1.00 70.35  ? 1627 GLN B NE2   1 
ATOM   6922 N  N     . SER B 1 411 ? -10.268 4.289   48.824 1.00 67.97  ? 1628 SER B N     1 
ATOM   6923 C  CA    . SER B 1 411 ? -10.448 5.567   49.483 1.00 62.48  ? 1628 SER B CA    1 
ATOM   6924 C  C     . SER B 1 411 ? -10.157 6.740   48.577 1.00 59.19  ? 1628 SER B C     1 
ATOM   6925 O  O     . SER B 1 411 ? -10.578 7.853   48.887 1.00 67.03  ? 1628 SER B O     1 
ATOM   6926 C  CB    . SER B 1 411 ? -9.573  5.661   50.716 1.00 55.41  ? 1628 SER B CB    1 
ATOM   6927 O  OG    . SER B 1 411 ? -9.928  4.639   51.627 1.00 60.24  ? 1628 SER B OG    1 
ATOM   6928 N  N     . HIS B 1 412 ? -9.530  6.512   47.432 1.00 55.14  ? 1629 HIS B N     1 
ATOM   6929 C  CA    . HIS B 1 412 ? -9.325  7.576   46.462 1.00 58.25  ? 1629 HIS B CA    1 
ATOM   6930 C  C     . HIS B 1 412 ? -10.279 7.534   45.276 1.00 63.53  ? 1629 HIS B C     1 
ATOM   6931 O  O     . HIS B 1 412 ? -10.156 8.357   44.365 1.00 63.70  ? 1629 HIS B O     1 
ATOM   6932 C  CB    . HIS B 1 412 ? -7.881  7.544   45.995 1.00 56.79  ? 1629 HIS B CB    1 
ATOM   6933 C  CG    . HIS B 1 412 ? -6.941  8.036   47.043 1.00 68.98  ? 1629 HIS B CG    1 
ATOM   6934 N  ND1   . HIS B 1 412 ? -6.983  7.575   48.341 1.00 70.92  ? 1629 HIS B ND1   1 
ATOM   6935 C  CD2   . HIS B 1 412 ? -5.963  8.970   47.004 1.00 70.73  ? 1629 HIS B CD2   1 
ATOM   6936 C  CE1   . HIS B 1 412 ? -6.058  8.194   49.051 1.00 72.47  ? 1629 HIS B CE1   1 
ATOM   6937 N  NE2   . HIS B 1 412 ? -5.423  9.043   48.263 1.00 72.07  ? 1629 HIS B NE2   1 
ATOM   6938 N  N     . THR B 1 413 ? -11.185 6.577   45.217 1.00 66.49  ? 1630 THR B N     1 
ATOM   6939 C  CA    . THR B 1 413 ? -12.195 6.592   44.178 1.00 63.92  ? 1630 THR B CA    1 
ATOM   6940 C  C     . THR B 1 413 ? -13.519 7.076   44.746 1.00 69.69  ? 1630 THR B C     1 
ATOM   6941 O  O     . THR B 1 413 ? -14.085 6.471   45.663 1.00 72.36  ? 1630 THR B O     1 
ATOM   6942 C  CB    . THR B 1 413 ? -12.337 5.239   43.512 1.00 51.89  ? 1630 THR B CB    1 
ATOM   6943 O  OG1   . THR B 1 413 ? -11.035 4.829   43.098 1.00 57.52  ? 1630 THR B OG1   1 
ATOM   6944 C  CG2   . THR B 1 413 ? -13.226 5.384   42.285 1.00 40.78  ? 1630 THR B CG2   1 
ATOM   6945 N  N     . LYS B 1 414 ? -14.009 8.154   44.178 1.00 41.36  ? 1631 LYS B N     1 
ATOM   6946 C  CA    . LYS B 1 414 ? -15.268 8.718   44.561 1.00 54.23  ? 1631 LYS B CA    1 
ATOM   6947 C  C     . LYS B 1 414 ? -16.139 8.694   43.321 1.00 69.66  ? 1631 LYS B C     1 
ATOM   6948 O  O     . LYS B 1 414 ? -15.643 8.745   42.193 1.00 74.37  ? 1631 LYS B O     1 
ATOM   6949 C  CB    . LYS B 1 414 ? -15.096 10.142  45.081 1.00 45.46  ? 1631 LYS B CB    1 
ATOM   6950 C  CG    . LYS B 1 414 ? -13.943 10.311  46.034 1.00 52.60  ? 1631 LYS B CG    1 
ATOM   6951 C  CD    . LYS B 1 414 ? -14.361 9.884   47.422 1.00 63.53  ? 1631 LYS B CD    1 
ATOM   6952 C  CE    . LYS B 1 414 ? -13.167 9.388   48.202 1.00 68.64  ? 1631 LYS B CE    1 
ATOM   6953 N  NZ    . LYS B 1 414 ? -13.360 7.959   48.624 1.00 67.58  ? 1631 LYS B NZ    1 
ATOM   6954 N  N     . LEU B 1 415 ? -17.431 8.564   43.534 1.00 66.95  ? 1632 LEU B N     1 
ATOM   6955 C  CA    . LEU B 1 415 ? -18.376 8.493   42.444 1.00 61.10  ? 1632 LEU B CA    1 
ATOM   6956 C  C     . LEU B 1 415 ? -19.255 9.714   42.566 1.00 62.46  ? 1632 LEU B C     1 
ATOM   6957 O  O     . LEU B 1 415 ? -19.653 10.088  43.672 1.00 71.83  ? 1632 LEU B O     1 
ATOM   6958 C  CB    . LEU B 1 415 ? -19.202 7.222   42.519 1.00 63.75  ? 1632 LEU B CB    1 
ATOM   6959 C  CG    . LEU B 1 415 ? -20.447 7.117   41.656 1.00 58.22  ? 1632 LEU B CG    1 
ATOM   6960 C  CD1   . LEU B 1 415 ? -20.057 6.537   40.317 1.00 52.10  ? 1632 LEU B CD1   1 
ATOM   6961 C  CD2   . LEU B 1 415 ? -21.486 6.252   42.362 1.00 58.83  ? 1632 LEU B CD2   1 
ATOM   6962 N  N     . THR B 1 416 ? -19.568 10.323  41.432 1.00 55.36  ? 1633 THR B N     1 
ATOM   6963 C  CA    . THR B 1 416 ? -20.390 11.514  41.477 1.00 51.12  ? 1633 THR B CA    1 
ATOM   6964 C  C     . THR B 1 416 ? -21.064 11.697  40.133 1.00 51.00  ? 1633 THR B C     1 
ATOM   6965 O  O     . THR B 1 416 ? -20.575 11.241  39.094 1.00 44.88  ? 1633 THR B O     1 
ATOM   6966 C  CB    . THR B 1 416 ? -19.565 12.752  41.850 1.00 53.76  ? 1633 THR B CB    1 
ATOM   6967 O  OG1   . THR B 1 416 ? -20.444 13.851  42.080 1.00 63.03  ? 1633 THR B OG1   1 
ATOM   6968 C  CG2   . THR B 1 416 ? -18.608 13.126  40.735 1.00 45.04  ? 1633 THR B CG2   1 
ATOM   6969 N  N     . LYS B 1 417 ? -22.166 12.438  40.166 1.00 56.94  ? 1634 LYS B N     1 
ATOM   6970 C  CA    . LYS B 1 417 ? -22.870 12.807  38.956 1.00 64.72  ? 1634 LYS B CA    1 
ATOM   6971 C  C     . LYS B 1 417 ? -22.781 14.307  38.674 1.00 82.71  ? 1634 LYS B C     1 
ATOM   6972 O  O     . LYS B 1 417 ? -23.234 14.747  37.610 1.00 84.58  ? 1634 LYS B O     1 
ATOM   6973 C  CB    . LYS B 1 417 ? -24.333 12.340  39.058 1.00 51.04  ? 1634 LYS B CB    1 
ATOM   6974 N  N     . GLN B 1 418 ? -22.198 15.100  39.590 1.00 88.44  ? 1635 GLN B N     1 
ATOM   6975 C  CA    . GLN B 1 418 ? -21.979 16.534  39.408 1.00 91.21  ? 1635 GLN B CA    1 
ATOM   6976 C  C     . GLN B 1 418 ? -20.552 17.021  39.252 1.00 81.08  ? 1635 GLN B C     1 
ATOM   6977 O  O     . GLN B 1 418 ? -19.660 16.735  40.063 1.00 72.97  ? 1635 GLN B O     1 
ATOM   6978 C  CB    . GLN B 1 418 ? -22.719 17.409  40.420 1.00 99.63  ? 1635 GLN B CB    1 
ATOM   6979 C  CG    . GLN B 1 418 ? -22.591 18.820  39.830 1.00 119.44 ? 1635 GLN B CG    1 
ATOM   6980 C  CD    . GLN B 1 418 ? -23.371 19.075  38.583 1.00 124.98 ? 1635 GLN B CD    1 
ATOM   6981 O  OE1   . GLN B 1 418 ? -22.693 19.328  37.586 1.00 131.23 ? 1635 GLN B OE1   1 
ATOM   6982 N  NE2   . GLN B 1 418 ? -24.713 19.243  38.625 1.00 121.91 ? 1635 GLN B NE2   1 
ATOM   6983 N  N     . TRP B 1 419 ? -20.404 17.805  38.186 1.00 78.08  ? 1636 TRP B N     1 
ATOM   6984 C  CA    . TRP B 1 419 ? -19.194 18.504  37.815 1.00 75.33  ? 1636 TRP B CA    1 
ATOM   6985 C  C     . TRP B 1 419 ? -18.555 19.240  38.984 1.00 73.50  ? 1636 TRP B C     1 
ATOM   6986 O  O     . TRP B 1 419 ? -17.340 19.168  39.186 1.00 67.26  ? 1636 TRP B O     1 
ATOM   6987 C  CB    . TRP B 1 419 ? -19.608 19.499  36.743 1.00 79.07  ? 1636 TRP B CB    1 
ATOM   6988 C  CG    . TRP B 1 419 ? -18.510 20.281  36.238 1.00 76.62  ? 1636 TRP B CG    1 
ATOM   6989 C  CD1   . TRP B 1 419 ? -18.257 21.605  36.439 1.00 61.19  ? 1636 TRP B CD1   1 
ATOM   6990 C  CD2   . TRP B 1 419 ? -17.454 19.778  35.449 1.00 79.69  ? 1636 TRP B CD2   1 
ATOM   6991 N  NE1   . TRP B 1 419 ? -17.088 21.955  35.803 1.00 62.77  ? 1636 TRP B NE1   1 
ATOM   6992 C  CE2   . TRP B 1 419 ? -16.580 20.843  35.181 1.00 72.58  ? 1636 TRP B CE2   1 
ATOM   6993 C  CE3   . TRP B 1 419 ? -17.166 18.517  34.931 1.00 78.51  ? 1636 TRP B CE3   1 
ATOM   6994 C  CZ2   . TRP B 1 419 ? -15.439 20.681  34.410 1.00 72.46  ? 1636 TRP B CZ2   1 
ATOM   6995 C  CZ3   . TRP B 1 419 ? -16.060 18.358  34.180 1.00 75.58  ? 1636 TRP B CZ3   1 
ATOM   6996 C  CH2   . TRP B 1 419 ? -15.201 19.432  33.916 1.00 74.56  ? 1636 TRP B CH2   1 
ATOM   6997 N  N     . ALA B 1 420 ? -19.360 19.996  39.737 1.00 68.91  ? 1637 ALA B N     1 
ATOM   6998 C  CA    . ALA B 1 420 ? -18.820 20.780  40.838 1.00 61.59  ? 1637 ALA B CA    1 
ATOM   6999 C  C     . ALA B 1 420 ? -18.059 19.889  41.807 1.00 68.04  ? 1637 ALA B C     1 
ATOM   7000 O  O     . ALA B 1 420 ? -16.876 20.122  42.099 1.00 64.68  ? 1637 ALA B O     1 
ATOM   7001 C  CB    . ALA B 1 420 ? -19.953 21.518  41.545 1.00 57.07  ? 1637 ALA B CB    1 
ATOM   7002 N  N     . GLU B 1 421 ? -18.707 18.824  42.283 1.00 70.89  ? 1638 GLU B N     1 
ATOM   7003 C  CA    . GLU B 1 421 ? -18.022 17.933  43.203 1.00 69.58  ? 1638 GLU B CA    1 
ATOM   7004 C  C     . GLU B 1 421 ? -17.055 17.011  42.490 1.00 58.57  ? 1638 GLU B C     1 
ATOM   7005 O  O     . GLU B 1 421 ? -16.159 16.473  43.138 1.00 56.49  ? 1638 GLU B O     1 
ATOM   7006 C  CB    . GLU B 1 421 ? -19.013 17.113  44.024 1.00 75.87  ? 1638 GLU B CB    1 
ATOM   7007 C  CG    . GLU B 1 421 ? -20.271 16.720  43.313 1.00 86.09  ? 1638 GLU B CG    1 
ATOM   7008 C  CD    . GLU B 1 421 ? -21.046 15.700  44.118 1.00 96.68  ? 1638 GLU B CD    1 
ATOM   7009 O  OE1   . GLU B 1 421 ? -20.490 15.219  45.128 1.00 100.24 ? 1638 GLU B OE1   1 
ATOM   7010 O  OE2   . GLU B 1 421 ? -22.198 15.381  43.753 1.00 99.50  ? 1638 GLU B OE2   1 
ATOM   7011 N  N     . PHE B 1 422 ? -17.215 16.828  41.180 1.00 46.44  ? 1639 PHE B N     1 
ATOM   7012 C  CA    . PHE B 1 422 ? -16.168 16.209  40.375 1.00 55.92  ? 1639 PHE B CA    1 
ATOM   7013 C  C     . PHE B 1 422 ? -14.859 16.974  40.533 1.00 58.34  ? 1639 PHE B C     1 
ATOM   7014 O  O     . PHE B 1 422 ? -13.802 16.390  40.810 1.00 49.27  ? 1639 PHE B O     1 
ATOM   7015 C  CB    . PHE B 1 422 ? -16.642 16.175  38.918 1.00 59.51  ? 1639 PHE B CB    1 
ATOM   7016 C  CG    . PHE B 1 422 ? -15.653 15.613  37.914 1.00 56.08  ? 1639 PHE B CG    1 
ATOM   7017 C  CD1   . PHE B 1 422 ? -15.896 14.398  37.306 1.00 63.55  ? 1639 PHE B CD1   1 
ATOM   7018 C  CD2   . PHE B 1 422 ? -14.556 16.347  37.498 1.00 46.23  ? 1639 PHE B CD2   1 
ATOM   7019 C  CE1   . PHE B 1 422 ? -15.026 13.901  36.352 1.00 66.83  ? 1639 PHE B CE1   1 
ATOM   7020 C  CE2   . PHE B 1 422 ? -13.689 15.862  36.555 1.00 51.18  ? 1639 PHE B CE2   1 
ATOM   7021 C  CZ    . PHE B 1 422 ? -13.918 14.638  35.977 1.00 62.06  ? 1639 PHE B CZ    1 
ATOM   7022 N  N     . LEU B 1 423 ? -14.925 18.295  40.364 1.00 60.19  ? 1640 LEU B N     1 
ATOM   7023 C  CA    . LEU B 1 423 ? -13.752 19.149  40.504 1.00 55.58  ? 1640 LEU B CA    1 
ATOM   7024 C  C     . LEU B 1 423 ? -13.265 19.161  41.941 1.00 53.37  ? 1640 LEU B C     1 
ATOM   7025 O  O     . LEU B 1 423 ? -12.053 19.213  42.200 1.00 48.74  ? 1640 LEU B O     1 
ATOM   7026 C  CB    . LEU B 1 423 ? -14.090 20.562  40.056 1.00 46.66  ? 1640 LEU B CB    1 
ATOM   7027 C  CG    . LEU B 1 423 ? -13.970 20.931  38.590 1.00 46.35  ? 1640 LEU B CG    1 
ATOM   7028 C  CD1   . LEU B 1 423 ? -14.460 19.826  37.721 1.00 57.26  ? 1640 LEU B CD1   1 
ATOM   7029 C  CD2   . LEU B 1 423 ? -14.771 22.201  38.332 1.00 47.74  ? 1640 LEU B CD2   1 
ATOM   7030 N  N     . GLN B 1 424 ? -14.206 19.161  42.885 1.00 47.69  ? 1641 GLN B N     1 
ATOM   7031 C  CA    . GLN B 1 424 ? -13.837 19.043  44.286 1.00 51.92  ? 1641 GLN B CA    1 
ATOM   7032 C  C     . GLN B 1 424 ? -12.971 17.802  44.499 1.00 54.52  ? 1641 GLN B C     1 
ATOM   7033 O  O     . GLN B 1 424 ? -11.810 17.891  44.911 1.00 46.86  ? 1641 GLN B O     1 
ATOM   7034 C  CB    . GLN B 1 424 ? -15.109 18.994  45.138 1.00 50.26  ? 1641 GLN B CB    1 
ATOM   7035 N  N     . PHE B 1 425 ? -13.509 16.635  44.144 1.00 56.05  ? 1642 PHE B N     1 
ATOM   7036 C  CA    . PHE B 1 425 ? -12.787 15.379  44.287 1.00 49.21  ? 1642 PHE B CA    1 
ATOM   7037 C  C     . PHE B 1 425 ? -11.444 15.429  43.581 1.00 57.42  ? 1642 PHE B C     1 
ATOM   7038 O  O     . PHE B 1 425 ? -10.416 15.041  44.150 1.00 56.13  ? 1642 PHE B O     1 
ATOM   7039 C  CB    . PHE B 1 425 ? -13.637 14.239  43.747 1.00 43.80  ? 1642 PHE B CB    1 
ATOM   7040 C  CG    . PHE B 1 425 ? -14.858 13.962  44.563 1.00 57.06  ? 1642 PHE B CG    1 
ATOM   7041 C  CD1   . PHE B 1 425 ? -14.862 14.170  45.922 1.00 54.41  ? 1642 PHE B CD1   1 
ATOM   7042 C  CD2   . PHE B 1 425 ? -16.017 13.512  43.962 1.00 65.70  ? 1642 PHE B CD2   1 
ATOM   7043 C  CE1   . PHE B 1 425 ? -15.999 13.912  46.670 1.00 58.94  ? 1642 PHE B CE1   1 
ATOM   7044 C  CE2   . PHE B 1 425 ? -17.156 13.259  44.707 1.00 65.78  ? 1642 PHE B CE2   1 
ATOM   7045 C  CZ    . PHE B 1 425 ? -17.146 13.456  46.060 1.00 59.60  ? 1642 PHE B CZ    1 
ATOM   7046 N  N     . LEU B 1 426 ? -11.435 15.902  42.331 1.00 61.91  ? 1643 LEU B N     1 
ATOM   7047 C  CA    . LEU B 1 426 ? -10.192 15.934  41.570 1.00 54.83  ? 1643 LEU B CA    1 
ATOM   7048 C  C     . LEU B 1 426 ? -9.138  16.727  42.312 1.00 50.98  ? 1643 LEU B C     1 
ATOM   7049 O  O     . LEU B 1 426 ? -8.010  16.257  42.494 1.00 51.61  ? 1643 LEU B O     1 
ATOM   7050 C  CB    . LEU B 1 426 ? -10.427 16.532  40.187 1.00 53.74  ? 1643 LEU B CB    1 
ATOM   7051 C  CG    . LEU B 1 426 ? -9.144  16.802  39.404 1.00 52.94  ? 1643 LEU B CG    1 
ATOM   7052 C  CD1   . LEU B 1 426 ? -8.398  15.531  39.267 1.00 39.89  ? 1643 LEU B CD1   1 
ATOM   7053 C  CD2   . LEU B 1 426 ? -9.425  17.383  38.024 1.00 62.41  ? 1643 LEU B CD2   1 
ATOM   7054 N  N     . GLU B 1 427 ? -9.497  17.923  42.783 1.00 48.58  ? 1644 GLU B N     1 
ATOM   7055 C  CA    . GLU B 1 427 ? -8.528  18.690  43.550 1.00 54.82  ? 1644 GLU B CA    1 
ATOM   7056 C  C     . GLU B 1 427 ? -8.138  17.949  44.828 1.00 60.06  ? 1644 GLU B C     1 
ATOM   7057 O  O     . GLU B 1 427 ? -6.974  17.991  45.232 1.00 54.96  ? 1644 GLU B O     1 
ATOM   7058 C  CB    . GLU B 1 427 ? -9.064  20.095  43.841 1.00 57.19  ? 1644 GLU B CB    1 
ATOM   7059 N  N     . THR B 1 428 ? -9.046  17.167  45.411 1.00 68.18  ? 1645 THR B N     1 
ATOM   7060 C  CA    . THR B 1 428 ? -8.668  16.403  46.605 1.00 70.44  ? 1645 THR B CA    1 
ATOM   7061 C  C     . THR B 1 428 ? -7.930  15.110  46.267 1.00 74.21  ? 1645 THR B C     1 
ATOM   7062 O  O     . THR B 1 428 ? -8.072  14.108  46.970 1.00 71.08  ? 1645 THR B O     1 
ATOM   7063 C  CB    . THR B 1 428 ? -9.920  16.092  47.431 1.00 63.88  ? 1645 THR B CB    1 
ATOM   7064 O  OG1   . THR B 1 428 ? -10.701 15.072  46.772 1.00 64.96  ? 1645 THR B OG1   1 
ATOM   7065 C  CG2   . THR B 1 428 ? -10.759 17.338  47.677 1.00 50.26  ? 1645 THR B CG2   1 
ATOM   7066 N  N     . LYS B 1 429 ? -7.119  15.114  45.209 1.00 76.98  ? 1646 LYS B N     1 
ATOM   7067 C  CA    . LYS B 1 429 ? -6.064  14.114  45.026 1.00 76.99  ? 1646 LYS B CA    1 
ATOM   7068 C  C     . LYS B 1 429 ? -6.652  12.715  44.871 1.00 80.52  ? 1646 LYS B C     1 
ATOM   7069 O  O     . LYS B 1 429 ? -6.104  11.732  45.367 1.00 91.70  ? 1646 LYS B O     1 
ATOM   7070 C  CB    . LYS B 1 429 ? -5.065  14.161  46.182 1.00 67.25  ? 1646 LYS B CB    1 
ATOM   7071 C  CG    . LYS B 1 429 ? -3.682  13.542  45.956 1.00 53.86  ? 1646 LYS B CG    1 
ATOM   7072 C  CD    . LYS B 1 429 ? -3.017  13.485  47.327 1.00 61.88  ? 1646 LYS B CD    1 
ATOM   7073 C  CE    . LYS B 1 429 ? -1.687  12.771  47.348 1.00 72.52  ? 1646 LYS B CE    1 
ATOM   7074 N  NZ    . LYS B 1 429 ? -1.340  12.197  48.701 1.00 77.44  ? 1646 LYS B NZ    1 
ATOM   7075 N  N     . ASN B 1 430 ? -7.777  12.614  44.181 1.00 77.18  ? 1647 ASN B N     1 
ATOM   7076 C  CA    . ASN B 1 430 ? -8.365  11.307  43.965 1.00 75.63  ? 1647 ASN B CA    1 
ATOM   7077 C  C     . ASN B 1 430 ? -9.055  11.294  42.613 1.00 71.29  ? 1647 ASN B C     1 
ATOM   7078 O  O     . ASN B 1 430 ? -9.199  12.326  41.953 1.00 73.00  ? 1647 ASN B O     1 
ATOM   7079 C  CB    . ASN B 1 430 ? -9.306  10.927  45.131 1.00 85.66  ? 1647 ASN B CB    1 
ATOM   7080 C  CG    . ASN B 1 430 ? -10.538 11.833  45.263 1.00 86.69  ? 1647 ASN B CG    1 
ATOM   7081 O  OD1   . ASN B 1 430 ? -11.051 12.363  44.288 1.00 89.89  ? 1647 ASN B OD1   1 
ATOM   7082 N  ND2   . ASN B 1 430 ? -11.039 11.961  46.490 1.00 78.33  ? 1647 ASN B ND2   1 
ATOM   7083 N  N     . ILE B 1 431 ? -9.438  10.107  42.172 1.00 64.98  ? 1648 ILE B N     1 
ATOM   7084 C  CA    . ILE B 1 431 ? -10.022 9.982   40.856 1.00 67.57  ? 1648 ILE B CA    1 
ATOM   7085 C  C     . ILE B 1 431 ? -11.500 9.649   41.011 1.00 62.78  ? 1648 ILE B C     1 
ATOM   7086 O  O     . ILE B 1 431 ? -11.954 9.157   42.052 1.00 50.70  ? 1648 ILE B O     1 
ATOM   7087 C  CB    . ILE B 1 431 ? -9.268  8.978   39.969 1.00 74.32  ? 1648 ILE B CB    1 
ATOM   7088 C  CG1   . ILE B 1 431 ? -9.096  7.617   40.632 1.00 66.26  ? 1648 ILE B CG1   1 
ATOM   7089 C  CG2   . ILE B 1 431 ? -7.891  9.535   39.644 1.00 83.09  ? 1648 ILE B CG2   1 
ATOM   7090 C  CD1   . ILE B 1 431 ? -8.891  6.535   39.624 1.00 57.19  ? 1648 ILE B CD1   1 
ATOM   7091 N  N     . ILE B 1 432 ? -12.257 9.914   39.941 1.00 64.47  ? 1649 ILE B N     1 
ATOM   7092 C  CA    . ILE B 1 432 ? -13.690 10.179  40.025 1.00 63.95  ? 1649 ILE B CA    1 
ATOM   7093 C  C     . ILE B 1 432 ? -14.426 9.351   38.984 1.00 68.97  ? 1649 ILE B C     1 
ATOM   7094 O  O     . ILE B 1 432 ? -14.064 9.343   37.802 1.00 75.99  ? 1649 ILE B O     1 
ATOM   7095 C  CB    . ILE B 1 432 ? -14.016 11.674  39.832 1.00 68.52  ? 1649 ILE B CB    1 
ATOM   7096 C  CG1   . ILE B 1 432 ? -13.013 12.582  40.551 1.00 69.18  ? 1649 ILE B CG1   1 
ATOM   7097 C  CG2   . ILE B 1 432 ? -15.412 11.969  40.304 1.00 73.72  ? 1649 ILE B CG2   1 
ATOM   7098 C  CD1   . ILE B 1 432 ? -11.794 12.955  39.699 1.00 68.21  ? 1649 ILE B CD1   1 
ATOM   7099 N  N     . MET B 1 433 ? -15.480 8.693   39.414 1.00 67.74  ? 1650 MET B N     1 
ATOM   7100 C  CA    . MET B 1 433 ? -16.319 7.917   38.531 1.00 57.08  ? 1650 MET B CA    1 
ATOM   7101 C  C     . MET B 1 433 ? -17.577 8.702   38.232 1.00 54.56  ? 1650 MET B C     1 
ATOM   7102 O  O     . MET B 1 433 ? -18.346 9.007   39.148 1.00 69.32  ? 1650 MET B O     1 
ATOM   7103 C  CB    . MET B 1 433 ? -16.664 6.596   39.194 1.00 60.59  ? 1650 MET B CB    1 
ATOM   7104 C  CG    . MET B 1 433 ? -17.286 5.655   38.253 1.00 71.26  ? 1650 MET B CG    1 
ATOM   7105 S  SD    . MET B 1 433 ? -16.542 4.061   38.423 1.00 69.58  ? 1650 MET B SD    1 
ATOM   7106 C  CE    . MET B 1 433 ? -17.052 3.406   36.863 1.00 66.42  ? 1650 MET B CE    1 
ATOM   7107 N  N     . ALA B 1 434 ? -17.781 9.043   36.971 1.00 42.43  ? 1651 ALA B N     1 
ATOM   7108 C  CA    . ALA B 1 434 ? -18.938 9.854   36.641 1.00 48.78  ? 1651 ALA B CA    1 
ATOM   7109 C  C     . ALA B 1 434 ? -19.584 9.366   35.356 1.00 49.83  ? 1651 ALA B C     1 
ATOM   7110 O  O     . ALA B 1 434 ? -18.941 8.705   34.537 1.00 51.55  ? 1651 ALA B O     1 
ATOM   7111 C  CB    . ALA B 1 434 ? -18.558 11.333  36.518 1.00 42.57  ? 1651 ALA B CB    1 
ATOM   7112 N  N     . PRO B 1 435 ? -20.863 9.655   35.169 1.00 43.43  ? 1652 PRO B N     1 
ATOM   7113 C  CA    . PRO B 1 435 ? -21.508 9.375   33.880 1.00 46.37  ? 1652 PRO B CA    1 
ATOM   7114 C  C     . PRO B 1 435 ? -20.944 10.238  32.759 1.00 59.59  ? 1652 PRO B C     1 
ATOM   7115 O  O     . PRO B 1 435 ? -20.526 11.382  32.955 1.00 70.15  ? 1652 PRO B O     1 
ATOM   7116 C  CB    . PRO B 1 435 ? -22.990 9.705   34.129 1.00 49.85  ? 1652 PRO B CB    1 
ATOM   7117 C  CG    . PRO B 1 435 ? -23.045 10.447  35.439 1.00 48.45  ? 1652 PRO B CG    1 
ATOM   7118 C  CD    . PRO B 1 435 ? -21.820 10.047  36.222 1.00 44.31  ? 1652 PRO B CD    1 
ATOM   7119 N  N     . PHE B 1 436 ? -20.906 9.656   31.570 1.00 59.13  ? 1653 PHE B N     1 
ATOM   7120 C  CA    . PHE B 1 436 ? -20.257 10.280  30.434 1.00 42.60  ? 1653 PHE B CA    1 
ATOM   7121 C  C     . PHE B 1 436 ? -20.902 9.790   29.141 1.00 47.52  ? 1653 PHE B C     1 
ATOM   7122 O  O     . PHE B 1 436 ? -21.384 8.646   29.048 1.00 65.69  ? 1653 PHE B O     1 
ATOM   7123 C  CB    . PHE B 1 436 ? -18.770 9.967   30.485 1.00 43.79  ? 1653 PHE B CB    1 
ATOM   7124 C  CG    . PHE B 1 436 ? -17.981 10.627  29.430 1.00 47.65  ? 1653 PHE B CG    1 
ATOM   7125 C  CD1   . PHE B 1 436 ? -18.221 11.944  29.108 1.00 46.26  ? 1653 PHE B CD1   1 
ATOM   7126 C  CD2   . PHE B 1 436 ? -16.963 9.937   28.779 1.00 49.74  ? 1653 PHE B CD2   1 
ATOM   7127 C  CE1   . PHE B 1 436 ? -17.491 12.560  28.138 1.00 45.16  ? 1653 PHE B CE1   1 
ATOM   7128 C  CE2   . PHE B 1 436 ? -16.218 10.544  27.808 1.00 46.65  ? 1653 PHE B CE2   1 
ATOM   7129 C  CZ    . PHE B 1 436 ? -16.485 11.859  27.478 1.00 46.81  ? 1653 PHE B CZ    1 
ATOM   7130 N  N     . CYS B 1 437 ? -20.940 10.702  28.165 1.00 47.40  ? 1654 CYS B N     1 
ATOM   7131 C  CA    . CYS B 1 437 ? -21.468 10.465  26.825 1.00 45.07  ? 1654 CYS B CA    1 
ATOM   7132 C  C     . CYS B 1 437 ? -20.468 9.733   25.947 1.00 46.93  ? 1654 CYS B C     1 
ATOM   7133 O  O     . CYS B 1 437 ? -20.860 9.130   24.945 1.00 50.78  ? 1654 CYS B O     1 
ATOM   7134 C  CB    . CYS B 1 437 ? -21.884 11.786  26.172 1.00 47.42  ? 1654 CYS B CB    1 
ATOM   7135 S  SG    . CYS B 1 437 ? -20.511 12.977  25.872 1.00 48.84  ? 1654 CYS B SG    1 
ATOM   7136 N  N     . GLY B 1 438 ? -19.178 9.914   26.208 1.00 44.02  ? 1655 GLY B N     1 
ATOM   7137 C  CA    . GLY B 1 438 ? -18.138 9.282   25.433 1.00 49.53  ? 1655 GLY B CA    1 
ATOM   7138 C  C     . GLY B 1 438 ? -17.582 10.137  24.332 1.00 56.30  ? 1655 GLY B C     1 
ATOM   7139 O  O     . GLY B 1 438 ? -16.477 9.845   23.844 1.00 68.06  ? 1655 GLY B O     1 
ATOM   7140 N  N     . GLU B 1 439 ? -18.272 11.224  23.992 1.00 40.72  ? 1656 GLU B N     1 
ATOM   7141 C  CA    . GLU B 1 439 ? -17.934 12.006  22.822 1.00 48.34  ? 1656 GLU B CA    1 
ATOM   7142 C  C     . GLU B 1 439 ? -16.619 12.737  23.030 1.00 57.75  ? 1656 GLU B C     1 
ATOM   7143 O  O     . GLU B 1 439 ? -16.348 13.273  24.109 1.00 48.77  ? 1656 GLU B O     1 
ATOM   7144 C  CB    . GLU B 1 439 ? -19.055 12.996  22.535 1.00 64.24  ? 1656 GLU B CB    1 
ATOM   7145 C  CG    . GLU B 1 439 ? -20.324 12.329  22.058 1.00 79.65  ? 1656 GLU B CG    1 
ATOM   7146 C  CD    . GLU B 1 439 ? -20.157 11.764  20.663 1.00 91.39  ? 1656 GLU B CD    1 
ATOM   7147 O  OE1   . GLU B 1 439 ? -19.393 12.375  19.884 1.00 102.22 ? 1656 GLU B OE1   1 
ATOM   7148 O  OE2   . GLU B 1 439 ? -20.771 10.720  20.345 1.00 87.02  ? 1656 GLU B OE2   1 
ATOM   7149 N  N     . ILE B 1 440 ? -15.825 12.815  21.959 1.00 67.31  ? 1657 ILE B N     1 
ATOM   7150 C  CA    . ILE B 1 440 ? -14.446 13.273  22.102 1.00 60.84  ? 1657 ILE B CA    1 
ATOM   7151 C  C     . ILE B 1 440 ? -14.411 14.754  22.392 1.00 60.21  ? 1657 ILE B C     1 
ATOM   7152 O  O     . ILE B 1 440 ? -13.606 15.221  23.209 1.00 67.99  ? 1657 ILE B O     1 
ATOM   7153 C  CB    . ILE B 1 440 ? -13.635 12.959  20.834 1.00 51.56  ? 1657 ILE B CB    1 
ATOM   7154 C  CG1   . ILE B 1 440 ? -13.464 11.453  20.647 1.00 49.45  ? 1657 ILE B CG1   1 
ATOM   7155 C  CG2   . ILE B 1 440 ? -12.290 13.658  20.867 1.00 38.77  ? 1657 ILE B CG2   1 
ATOM   7156 C  CD1   . ILE B 1 440 ? -13.108 11.075  19.232 1.00 38.05  ? 1657 ILE B CD1   1 
ATOM   7157 N  N     . SER B 1 441 ? -15.295 15.515  21.751 1.00 59.63  ? 1658 SER B N     1 
ATOM   7158 C  CA    . SER B 1 441 ? -15.385 16.948  22.013 1.00 58.73  ? 1658 SER B CA    1 
ATOM   7159 C  C     . SER B 1 441 ? -15.600 17.219  23.496 1.00 69.28  ? 1658 SER B C     1 
ATOM   7160 O  O     . SER B 1 441 ? -14.926 18.064  24.106 1.00 76.27  ? 1658 SER B O     1 
ATOM   7161 C  CB    . SER B 1 441 ? -16.551 17.509  21.204 1.00 56.47  ? 1658 SER B CB    1 
ATOM   7162 O  OG    . SER B 1 441 ? -17.625 16.586  21.196 1.00 62.24  ? 1658 SER B OG    1 
ATOM   7163 N  N     . CYS B 1 442 ? -16.522 16.470  24.099 1.00 70.34  ? 1659 CYS B N     1 
ATOM   7164 C  CA    . CYS B 1 442 ? -16.825 16.633  25.507 1.00 59.96  ? 1659 CYS B CA    1 
ATOM   7165 C  C     . CYS B 1 442 ? -15.661 16.207  26.392 1.00 63.80  ? 1659 CYS B C     1 
ATOM   7166 O  O     . CYS B 1 442 ? -15.383 16.846  27.402 1.00 66.89  ? 1659 CYS B O     1 
ATOM   7167 C  CB    . CYS B 1 442 ? -18.068 15.826  25.852 1.00 57.53  ? 1659 CYS B CB    1 
ATOM   7168 S  SG    . CYS B 1 442 ? -18.511 15.917  27.566 1.00 69.53  ? 1659 CYS B SG    1 
ATOM   7169 N  N     . GLU B 1 443 ? -14.995 15.116  26.035 1.00 61.03  ? 1660 GLU B N     1 
ATOM   7170 C  CA    . GLU B 1 443 ? -13.837 14.677  26.802 1.00 59.56  ? 1660 GLU B CA    1 
ATOM   7171 C  C     . GLU B 1 443 ? -12.750 15.746  26.820 1.00 66.49  ? 1660 GLU B C     1 
ATOM   7172 O  O     . GLU B 1 443 ? -12.128 16.016  27.869 1.00 69.90  ? 1660 GLU B O     1 
ATOM   7173 C  CB    . GLU B 1 443 ? -13.323 13.368  26.202 1.00 60.05  ? 1660 GLU B CB    1 
ATOM   7174 C  CG    . GLU B 1 443 ? -12.669 12.428  27.191 1.00 67.19  ? 1660 GLU B CG    1 
ATOM   7175 C  CD    . GLU B 1 443 ? -12.239 11.125  26.540 1.00 80.99  ? 1660 GLU B CD    1 
ATOM   7176 O  OE1   . GLU B 1 443 ? -13.087 10.508  25.853 1.00 89.62  ? 1660 GLU B OE1   1 
ATOM   7177 O  OE2   . GLU B 1 443 ? -11.057 10.732  26.694 1.00 81.90  ? 1660 GLU B OE2   1 
ATOM   7178 N  N     . ASP B 1 444 ? -12.518 16.374  25.663 1.00 65.76  ? 1661 ASP B N     1 
ATOM   7179 C  CA    . ASP B 1 444 ? -11.610 17.516  25.607 1.00 64.55  ? 1661 ASP B CA    1 
ATOM   7180 C  C     . ASP B 1 444 ? -12.092 18.645  26.506 1.00 61.29  ? 1661 ASP B C     1 
ATOM   7181 O  O     . ASP B 1 444 ? -11.286 19.261  27.216 1.00 61.28  ? 1661 ASP B O     1 
ATOM   7182 C  CB    . ASP B 1 444 ? -11.480 18.030  24.180 1.00 55.99  ? 1661 ASP B CB    1 
ATOM   7183 C  CG    . ASP B 1 444 ? -10.813 17.052  23.267 1.00 59.33  ? 1661 ASP B CG    1 
ATOM   7184 O  OD1   . ASP B 1 444 ? -11.165 17.078  22.070 1.00 53.94  ? 1661 ASP B OD1   1 
ATOM   7185 O  OD2   . ASP B 1 444 ? -9.949  16.274  23.730 1.00 68.68  ? 1661 ASP B OD2   1 
ATOM   7186 N  N     . ARG B 1 445 ? -13.406 18.931  26.483 1.00 45.32  ? 1662 ARG B N     1 
ATOM   7187 C  CA    . ARG B 1 445 ? -13.933 20.032  27.284 1.00 63.75  ? 1662 ARG B CA    1 
ATOM   7188 C  C     . ARG B 1 445 ? -13.736 19.783  28.774 1.00 75.98  ? 1662 ARG B C     1 
ATOM   7189 O  O     . ARG B 1 445 ? -13.386 20.700  29.530 1.00 84.38  ? 1662 ARG B O     1 
ATOM   7190 C  CB    . ARG B 1 445 ? -15.411 20.249  26.973 1.00 62.82  ? 1662 ARG B CB    1 
ATOM   7191 N  N     . ILE B 1 446 ? -13.950 18.543  29.208 1.00 68.58  ? 1663 ILE B N     1 
ATOM   7192 C  CA    . ILE B 1 446 ? -13.717 18.171  30.602 1.00 66.31  ? 1663 ILE B CA    1 
ATOM   7193 C  C     . ILE B 1 446 ? -12.256 18.393  30.962 1.00 62.68  ? 1663 ILE B C     1 
ATOM   7194 O  O     . ILE B 1 446 ? -11.932 19.092  31.938 1.00 73.14  ? 1663 ILE B O     1 
ATOM   7195 C  CB    . ILE B 1 446 ? -14.144 16.710  30.852 1.00 67.13  ? 1663 ILE B CB    1 
ATOM   7196 C  CG1   . ILE B 1 446 ? -15.554 16.457  30.334 1.00 63.78  ? 1663 ILE B CG1   1 
ATOM   7197 C  CG2   . ILE B 1 446 ? -14.122 16.375  32.319 1.00 68.85  ? 1663 ILE B CG2   1 
ATOM   7198 C  CD1   . ILE B 1 446 ? -16.148 15.145  30.783 1.00 59.98  ? 1663 ILE B CD1   1 
ATOM   7199 N  N     . LYS B 1 447 ? -11.345 17.825  30.165 1.00 57.07  ? 1664 LYS B N     1 
ATOM   7200 C  CA    . LYS B 1 447 ? -9.931  18.012  30.479 1.00 73.99  ? 1664 LYS B CA    1 
ATOM   7201 C  C     . LYS B 1 447 ? -9.566  19.494  30.517 1.00 81.69  ? 1664 LYS B C     1 
ATOM   7202 O  O     . LYS B 1 447 ? -8.798  19.932  31.386 1.00 87.96  ? 1664 LYS B O     1 
ATOM   7203 C  CB    . LYS B 1 447 ? -9.052  17.283  29.472 1.00 73.99  ? 1664 LYS B CB    1 
ATOM   7204 C  CG    . LYS B 1 447 ? -7.571  17.366  29.817 1.00 73.05  ? 1664 LYS B CG    1 
ATOM   7205 C  CD    . LYS B 1 447 ? -6.849  18.459  29.019 1.00 72.80  ? 1664 LYS B CD    1 
ATOM   7206 C  CE    . LYS B 1 447 ? -5.337  18.399  29.249 1.00 72.55  ? 1664 LYS B CE    1 
ATOM   7207 N  NZ    . LYS B 1 447 ? -4.752  17.053  28.902 1.00 64.90  ? 1664 LYS B NZ    1 
ATOM   7208 N  N     . ALA B 1 448 ? -10.118 20.282  29.593 1.00 67.18  ? 1665 ALA B N     1 
ATOM   7209 C  CA    . ALA B 1 448 ? -9.816  21.702  29.545 1.00 57.47  ? 1665 ALA B CA    1 
ATOM   7210 C  C     . ALA B 1 448 ? -10.253 22.393  30.821 1.00 57.60  ? 1665 ALA B C     1 
ATOM   7211 O  O     . ALA B 1 448 ? -9.445  23.025  31.509 1.00 66.82  ? 1665 ALA B O     1 
ATOM   7212 C  CB    . ALA B 1 448 ? -10.515 22.335  28.341 1.00 58.40  ? 1665 ALA B CB    1 
ATOM   7213 N  N     . GLU B 1 449 ? -11.534 22.272  31.162 1.00 55.00  ? 1666 GLU B N     1 
ATOM   7214 C  CA    . GLU B 1 449 ? -12.100 23.036  32.263 1.00 54.85  ? 1666 GLU B CA    1 
ATOM   7215 C  C     . GLU B 1 449 ? -11.737 22.489  33.632 1.00 65.63  ? 1666 GLU B C     1 
ATOM   7216 O  O     . GLU B 1 449 ? -12.209 23.052  34.626 1.00 46.00  ? 1666 GLU B O     1 
ATOM   7217 C  CB    . GLU B 1 449 ? -13.619 23.132  32.119 1.00 63.76  ? 1666 GLU B CB    1 
ATOM   7218 C  CG    . GLU B 1 449 ? -14.038 24.174  31.085 1.00 70.51  ? 1666 GLU B CG    1 
ATOM   7219 C  CD    . GLU B 1 449 ? -15.517 24.147  30.754 1.00 66.82  ? 1666 GLU B CD    1 
ATOM   7220 O  OE1   . GLU B 1 449 ? -16.349 24.213  31.690 1.00 59.44  ? 1666 GLU B OE1   1 
ATOM   7221 O  OE2   . GLU B 1 449 ? -15.837 24.066  29.546 1.00 67.98  ? 1666 GLU B OE2   1 
ATOM   7222 N  N     . SER B 1 450 ? -10.900 21.427  33.702 1.00 79.82  ? 1667 SER B N     1 
ATOM   7223 C  CA    . SER B 1 450 ? -10.377 20.873  34.963 1.00 86.01  ? 1667 SER B CA    1 
ATOM   7224 C  C     . SER B 1 450 ? -8.993  21.377  35.395 1.00 84.19  ? 1667 SER B C     1 
ATOM   7225 O  O     . SER B 1 450 ? -8.640  21.215  36.571 1.00 81.78  ? 1667 SER B O     1 
ATOM   7226 C  CB    . SER B 1 450 ? -10.349 19.345  34.920 1.00 92.95  ? 1667 SER B CB    1 
ATOM   7227 O  OG    . SER B 1 450 ? -11.533 18.843  34.340 1.00 98.24  ? 1667 SER B OG    1 
ATOM   7228 N  N     . ALA B 1 451 ? -8.193  21.946  34.499 1.00 86.95  ? 1668 ALA B N     1 
ATOM   7229 C  CA    . ALA B 1 451 ? -6.874  22.476  34.868 1.00 86.67  ? 1668 ALA B CA    1 
ATOM   7230 C  C     . ALA B 1 451 ? -6.933  23.515  36.009 1.00 88.50  ? 1668 ALA B C     1 
ATOM   7231 O  O     . ALA B 1 451 ? -6.081  24.405  36.128 1.00 86.07  ? 1668 ALA B O     1 
ATOM   7232 C  CB    . ALA B 1 451 ? -6.225  23.090  33.635 1.00 87.93  ? 1668 ALA B CB    1 
ATOM   7233 N  N     . MET B 1 464 ? -2.350  18.023  34.028 1.00 82.20  ? 1681 MET B N     1 
ATOM   7234 C  CA    . MET B 1 464 ? -2.869  18.715  35.210 1.00 95.64  ? 1681 MET B CA    1 
ATOM   7235 C  C     . MET B 1 464 ? -4.409  18.827  35.256 1.00 86.28  ? 1681 MET B C     1 
ATOM   7236 O  O     . MET B 1 464 ? -5.004  19.024  36.325 1.00 85.25  ? 1681 MET B O     1 
ATOM   7237 C  CB    . MET B 1 464 ? -2.249  20.115  35.290 1.00 108.19 ? 1681 MET B CB    1 
ATOM   7238 C  CG    . MET B 1 464 ? -0.976  20.158  36.128 1.00 111.03 ? 1681 MET B CG    1 
ATOM   7239 S  SD    . MET B 1 464 ? -1.356  19.831  37.859 1.00 105.82 ? 1681 MET B SD    1 
ATOM   7240 C  CE    . MET B 1 464 ? -2.772  20.921  38.083 1.00 103.49 ? 1681 MET B CE    1 
ATOM   7241 N  N     . GLY B 1 465 ? -5.050  18.700  34.094 1.00 71.51  ? 1682 GLY B N     1 
ATOM   7242 C  CA    . GLY B 1 465 ? -6.486  18.564  34.026 1.00 69.91  ? 1682 GLY B CA    1 
ATOM   7243 C  C     . GLY B 1 465 ? -6.864  17.100  34.079 1.00 68.97  ? 1682 GLY B C     1 
ATOM   7244 O  O     . GLY B 1 465 ? -6.010  16.216  34.080 1.00 73.87  ? 1682 GLY B O     1 
ATOM   7245 N  N     . ALA B 1 466 ? -8.166  16.829  34.039 1.00 63.68  ? 1683 ALA B N     1 
ATOM   7246 C  CA    . ALA B 1 466 ? -8.642  15.467  34.261 1.00 59.05  ? 1683 ALA B CA    1 
ATOM   7247 C  C     . ALA B 1 466 ? -8.828  14.767  32.928 1.00 56.77  ? 1683 ALA B C     1 
ATOM   7248 O  O     . ALA B 1 466 ? -9.567  15.244  32.060 1.00 62.15  ? 1683 ALA B O     1 
ATOM   7249 C  CB    . ALA B 1 466 ? -9.944  15.437  35.056 1.00 55.20  ? 1683 ALA B CB    1 
ATOM   7250 N  N     . LYS B 1 467 ? -8.143  13.643  32.778 1.00 52.41  ? 1684 LYS B N     1 
ATOM   7251 C  CA    . LYS B 1 467 ? -8.188  12.794  31.601 1.00 49.50  ? 1684 LYS B CA    1 
ATOM   7252 C  C     . LYS B 1 467 ? -9.107  11.610  31.862 1.00 47.35  ? 1684 LYS B C     1 
ATOM   7253 O  O     . LYS B 1 467 ? -9.524  11.362  32.989 1.00 48.59  ? 1684 LYS B O     1 
ATOM   7254 C  CB    . LYS B 1 467 ? -6.779  12.313  31.223 1.00 47.72  ? 1684 LYS B CB    1 
ATOM   7255 N  N     . SER B 1 468 ? -9.477  10.919  30.787 1.00 54.49  ? 1685 SER B N     1 
ATOM   7256 C  CA    . SER B 1 468 ? -10.171 9.637   30.896 1.00 67.16  ? 1685 SER B CA    1 
ATOM   7257 C  C     . SER B 1 468 ? -9.184  8.498   31.133 1.00 67.57  ? 1685 SER B C     1 
ATOM   7258 O  O     . SER B 1 468 ? -8.154  8.400   30.457 1.00 76.88  ? 1685 SER B O     1 
ATOM   7259 C  CB    . SER B 1 468 ? -10.970 9.368   29.623 1.00 68.68  ? 1685 SER B CB    1 
ATOM   7260 O  OG    . SER B 1 468 ? -10.093 9.237   28.522 1.00 72.79  ? 1685 SER B OG    1 
ATOM   7261 N  N     . LEU B 1 469 ? -9.485  7.643   32.107 1.00 60.00  ? 1686 LEU B N     1 
ATOM   7262 C  CA    . LEU B 1 469 ? -8.659  6.455   32.347 1.00 53.75  ? 1686 LEU B CA    1 
ATOM   7263 C  C     . LEU B 1 469 ? -9.198  5.248   31.575 1.00 54.99  ? 1686 LEU B C     1 
ATOM   7264 O  O     . LEU B 1 469 ? -8.527  4.727   30.682 1.00 50.17  ? 1686 LEU B O     1 
ATOM   7265 C  CB    . LEU B 1 469 ? -8.593  6.185   33.850 1.00 36.75  ? 1686 LEU B CB    1 
ATOM   7266 C  CG    . LEU B 1 469 ? -8.466  7.516   34.591 1.00 45.96  ? 1686 LEU B CG    1 
ATOM   7267 C  CD1   . LEU B 1 469 ? -8.623  7.318   36.073 1.00 53.14  ? 1686 LEU B CD1   1 
ATOM   7268 C  CD2   . LEU B 1 469 ? -7.127  8.202   34.281 1.00 50.48  ? 1686 LEU B CD2   1 
ATOM   7269 N  N     . CYS B 1 470 ? -10.412 4.812   31.898 1.00 58.16  ? 1687 CYS B N     1 
ATOM   7270 C  CA    . CYS B 1 470 ? -11.106 3.817   31.093 1.00 47.26  ? 1687 CYS B CA    1 
ATOM   7271 C  C     . CYS B 1 470 ? -12.595 3.823   31.494 1.00 49.36  ? 1687 CYS B C     1 
ATOM   7272 O  O     . CYS B 1 470 ? -13.000 4.378   32.526 1.00 43.47  ? 1687 CYS B O     1 
ATOM   7273 C  CB    . CYS B 1 470 ? -10.483 2.415   31.235 1.00 43.76  ? 1687 CYS B CB    1 
ATOM   7274 S  SG    . CYS B 1 470 ? -10.973 1.682   32.796 1.00 36.39  ? 1687 CYS B SG    1 
ATOM   7275 N  N     . ILE B 1 471 ? -13.394 3.259   30.590 1.00 47.81  ? 1688 ILE B N     1 
ATOM   7276 C  CA    . ILE B 1 471 ? -14.767 2.871   30.890 1.00 52.17  ? 1688 ILE B CA    1 
ATOM   7277 C  C     . ILE B 1 471 ? -14.696 1.497   31.547 1.00 77.54  ? 1688 ILE B C     1 
ATOM   7278 O  O     . ILE B 1 471 ? -14.413 0.504   30.846 1.00 89.21  ? 1688 ILE B O     1 
ATOM   7279 C  CB    . ILE B 1 471 ? -15.615 2.806   29.620 1.00 51.32  ? 1688 ILE B CB    1 
ATOM   7280 C  CG1   . ILE B 1 471 ? -15.279 3.955   28.687 1.00 36.00  ? 1688 ILE B CG1   1 
ATOM   7281 C  CG2   . ILE B 1 471 ? -17.059 2.814   29.970 1.00 50.52  ? 1688 ILE B CG2   1 
ATOM   7282 C  CD1   . ILE B 1 471 ? -15.624 3.687   27.272 1.00 36.04  ? 1688 ILE B CD1   1 
ATOM   7283 N  N     . PRO B 1 472 ? -14.880 1.397   32.856 1.00 76.89  ? 1689 PRO B N     1 
ATOM   7284 C  CA    . PRO B 1 472 ? -14.605 0.141   33.546 1.00 71.43  ? 1689 PRO B CA    1 
ATOM   7285 C  C     . PRO B 1 472 ? -15.571 -0.952  33.133 1.00 73.94  ? 1689 PRO B C     1 
ATOM   7286 O  O     . PRO B 1 472 ? -16.732 -0.704  32.793 1.00 87.59  ? 1689 PRO B O     1 
ATOM   7287 C  CB    . PRO B 1 472 ? -14.783 0.505   35.025 1.00 71.77  ? 1689 PRO B CB    1 
ATOM   7288 C  CG    . PRO B 1 472 ? -14.789 1.993   35.075 1.00 72.28  ? 1689 PRO B CG    1 
ATOM   7289 C  CD    . PRO B 1 472 ? -15.390 2.418   33.773 1.00 75.99  ? 1689 PRO B CD    1 
ATOM   7290 N  N     . PHE B 1 473 ? -15.121 -2.177  33.278 1.00 59.49  ? 1690 PHE B N     1 
ATOM   7291 C  CA    . PHE B 1 473 ? -15.932 -3.304  32.996 1.00 40.41  ? 1690 PHE B CA    1 
ATOM   7292 C  C     . PHE B 1 473 ? -16.923 -3.468  34.098 1.00 44.74  ? 1690 PHE B C     1 
ATOM   7293 O  O     . PHE B 1 473 ? -17.967 -3.976  33.890 1.00 53.03  ? 1690 PHE B O     1 
ATOM   7294 C  CB    . PHE B 1 473 ? -15.088 -4.519  32.958 1.00 35.84  ? 1690 PHE B CB    1 
ATOM   7295 C  CG    . PHE B 1 473 ? -14.190 -4.569  31.818 1.00 38.39  ? 1690 PHE B CG    1 
ATOM   7296 C  CD1   . PHE B 1 473 ? -14.349 -3.739  30.804 1.00 43.25  ? 1690 PHE B CD1   1 
ATOM   7297 C  CD2   . PHE B 1 473 ? -13.223 -5.483  31.756 1.00 40.15  ? 1690 PHE B CD2   1 
ATOM   7298 C  CE1   . PHE B 1 473 ? -13.527 -3.796  29.732 1.00 41.53  ? 1690 PHE B CE1   1 
ATOM   7299 C  CE2   . PHE B 1 473 ? -12.390 -5.532  30.706 1.00 43.22  ? 1690 PHE B CE2   1 
ATOM   7300 C  CZ    . PHE B 1 473 ? -12.547 -4.692  29.689 1.00 41.60  ? 1690 PHE B CZ    1 
ATOM   7301 N  N     . GLU B 1 474 ? -16.592 -3.047  35.290 1.00 48.24  ? 1691 GLU B N     1 
ATOM   7302 C  CA    . GLU B 1 474 ? -17.526 -3.174  36.357 1.00 57.00  ? 1691 GLU B CA    1 
ATOM   7303 C  C     . GLU B 1 474 ? -18.165 -1.861  36.610 1.00 62.36  ? 1691 GLU B C     1 
ATOM   7304 O  O     . GLU B 1 474 ? -17.608 -1.023  37.239 1.00 64.90  ? 1691 GLU B O     1 
ATOM   7305 C  CB    . GLU B 1 474 ? -16.801 -3.551  37.610 1.00 77.29  ? 1691 GLU B CB    1 
ATOM   7306 C  CG    . GLU B 1 474 ? -15.551 -4.375  37.408 1.00 85.90  ? 1691 GLU B CG    1 
ATOM   7307 C  CD    . GLU B 1 474 ? -15.194 -5.160  38.653 1.00 91.93  ? 1691 GLU B CD    1 
ATOM   7308 O  OE1   . GLU B 1 474 ? -15.499 -4.699  39.770 1.00 86.11  ? 1691 GLU B OE1   1 
ATOM   7309 O  OE2   . GLU B 1 474 ? -14.610 -6.249  38.513 1.00 94.57  ? 1691 GLU B OE2   1 
ATOM   7310 N  N     . GLN B 1 475 ? -19.409 -1.743  36.231 1.00 64.72  ? 1692 GLN B N     1 
ATOM   7311 C  CA    . GLN B 1 475 ? -20.128 -0.529  36.367 1.00 56.62  ? 1692 GLN B CA    1 
ATOM   7312 C  C     . GLN B 1 475 ? -20.765 -0.421  37.655 1.00 57.95  ? 1692 GLN B C     1 
ATOM   7313 O  O     . GLN B 1 475 ? -21.254 -1.371  38.163 1.00 66.29  ? 1692 GLN B O     1 
ATOM   7314 C  CB    . GLN B 1 475 ? -21.224 -0.547  35.374 1.00 54.94  ? 1692 GLN B CB    1 
ATOM   7315 C  CG    . GLN B 1 475 ? -20.685 -0.546  34.003 1.00 61.64  ? 1692 GLN B CG    1 
ATOM   7316 C  CD    . GLN B 1 475 ? -20.422 0.827   33.556 1.00 64.52  ? 1692 GLN B CD    1 
ATOM   7317 O  OE1   . GLN B 1 475 ? -21.334 1.562   33.346 1.00 73.80  ? 1692 GLN B OE1   1 
ATOM   7318 N  NE2   . GLN B 1 475 ? -19.185 1.176   33.397 1.00 61.29  ? 1692 GLN B NE2   1 
ATOM   7319 N  N     . PRO B 1 476 ? -20.794 0.771   38.181 1.00 67.88  ? 1693 PRO B N     1 
ATOM   7320 C  CA    . PRO B 1 476 ? -21.407 1.127   39.444 1.00 80.66  ? 1693 PRO B CA    1 
ATOM   7321 C  C     . PRO B 1 476 ? -22.887 0.911   39.436 1.00 87.36  ? 1693 PRO B C     1 
ATOM   7322 O  O     . PRO B 1 476 ? -23.466 0.468   40.396 1.00 103.70 ? 1693 PRO B O     1 
ATOM   7323 C  CB    . PRO B 1 476 ? -21.116 2.596   39.543 1.00 79.29  ? 1693 PRO B CB    1 
ATOM   7324 C  CG    . PRO B 1 476 ? -19.893 2.750   38.779 1.00 72.59  ? 1693 PRO B CG    1 
ATOM   7325 C  CD    . PRO B 1 476 ? -20.151 1.926   37.593 1.00 70.15  ? 1693 PRO B CD    1 
ATOM   7326 N  N     . ALA B 1 477 ? -23.498 1.275   38.340 1.00 79.00  ? 1694 ALA B N     1 
ATOM   7327 C  CA    . ALA B 1 477 ? -24.891 1.094   38.180 1.00 86.78  ? 1694 ALA B CA    1 
ATOM   7328 C  C     . ALA B 1 477 ? -25.220 1.066   36.733 1.00 84.54  ? 1694 ALA B C     1 
ATOM   7329 O  O     . ALA B 1 477 ? -24.465 1.518   35.908 1.00 81.01  ? 1694 ALA B O     1 
ATOM   7330 C  CB    . ALA B 1 477 ? -25.607 2.243   38.803 1.00 95.73  ? 1694 ALA B CB    1 
ATOM   7331 N  N     . LYS B 1 478 ? -26.383 0.537   36.412 1.00 81.25  ? 1695 LYS B N     1 
ATOM   7332 C  CA    . LYS B 1 478 ? -26.841 0.534   35.047 1.00 72.22  ? 1695 LYS B CA    1 
ATOM   7333 C  C     . LYS B 1 478 ? -27.286 1.946   34.737 1.00 73.20  ? 1695 LYS B C     1 
ATOM   7334 O  O     . LYS B 1 478 ? -27.788 2.617   35.596 1.00 76.65  ? 1695 LYS B O     1 
ATOM   7335 C  CB    . LYS B 1 478 ? -27.956 -0.476  34.898 1.00 62.95  ? 1695 LYS B CB    1 
ATOM   7336 N  N     . ILE B 1 479 ? -27.112 2.414   33.524 1.00 70.09  ? 1696 ILE B N     1 
ATOM   7337 C  CA    . ILE B 1 479 ? -27.493 3.768   33.243 1.00 61.48  ? 1696 ILE B CA    1 
ATOM   7338 C  C     . ILE B 1 479 ? -28.942 3.803   32.948 1.00 67.37  ? 1696 ILE B C     1 
ATOM   7339 O  O     . ILE B 1 479 ? -29.394 3.010   32.175 1.00 74.95  ? 1696 ILE B O     1 
ATOM   7340 C  CB    . ILE B 1 479 ? -26.742 4.337   32.040 1.00 45.18  ? 1696 ILE B CB    1 
ATOM   7341 N  N     . ASP B 1 480 ? -29.664 4.723   33.586 1.00 64.07  ? 1697 ASP B N     1 
ATOM   7342 C  CA    . ASP B 1 480 ? -31.089 4.934   33.385 1.00 62.10  ? 1697 ASP B CA    1 
ATOM   7343 C  C     . ASP B 1 480 ? -31.132 5.981   32.341 1.00 63.80  ? 1697 ASP B C     1 
ATOM   7344 O  O     . ASP B 1 480 ? -30.703 7.060   32.560 1.00 62.29  ? 1697 ASP B O     1 
ATOM   7345 C  CB    . ASP B 1 480 ? -31.734 5.419   34.651 1.00 51.12  ? 1697 ASP B CB    1 
ATOM   7346 C  CG    . ASP B 1 480 ? -33.201 5.386   34.574 1.00 64.43  ? 1697 ASP B CG    1 
ATOM   7347 O  OD1   . ASP B 1 480 ? -33.863 5.259   35.587 1.00 62.85  ? 1697 ASP B OD1   1 
ATOM   7348 O  OD2   . ASP B 1 480 ? -33.700 5.487   33.474 1.00 63.15  ? 1697 ASP B OD2   1 
ATOM   7349 N  N     . PRO B 1 481 ? -31.656 5.657   31.191 1.00 68.50  ? 1698 PRO B N     1 
ATOM   7350 C  CA    . PRO B 1 481 ? -31.578 6.571   30.042 1.00 69.20  ? 1698 PRO B CA    1 
ATOM   7351 C  C     . PRO B 1 481 ? -32.564 7.725   30.129 1.00 69.83  ? 1698 PRO B C     1 
ATOM   7352 O  O     . PRO B 1 481 ? -32.277 8.825   29.642 1.00 76.47  ? 1698 PRO B O     1 
ATOM   7353 C  CB    . PRO B 1 481 ? -31.878 5.651   28.850 1.00 71.67  ? 1698 PRO B CB    1 
ATOM   7354 C  CG    . PRO B 1 481 ? -31.535 4.274   29.351 1.00 75.43  ? 1698 PRO B CG    1 
ATOM   7355 C  CD    . PRO B 1 481 ? -31.990 4.290   30.776 1.00 76.16  ? 1698 PRO B CD    1 
ATOM   7356 N  N     . LYS B 1 482 ? -33.664 7.544   30.808 1.00 59.95  ? 1699 LYS B N     1 
ATOM   7357 C  CA    . LYS B 1 482 ? -34.599 8.618   30.914 1.00 64.20  ? 1699 LYS B CA    1 
ATOM   7358 C  C     . LYS B 1 482 ? -34.097 9.675   31.878 1.00 76.33  ? 1699 LYS B C     1 
ATOM   7359 O  O     . LYS B 1 482 ? -34.418 10.823  31.754 1.00 55.12  ? 1699 LYS B O     1 
ATOM   7360 C  CB    . LYS B 1 482 ? -35.914 8.052   31.402 1.00 61.70  ? 1699 LYS B CB    1 
ATOM   7361 C  CG    . LYS B 1 482 ? -36.124 6.610   31.007 1.00 62.40  ? 1699 LYS B CG    1 
ATOM   7362 C  CD    . LYS B 1 482 ? -37.568 6.233   31.125 1.00 69.01  ? 1699 LYS B CD    1 
ATOM   7363 C  CE    . LYS B 1 482 ? -38.379 6.746   29.946 1.00 79.71  ? 1699 LYS B CE    1 
ATOM   7364 N  NZ    . LYS B 1 482 ? -39.801 7.126   30.254 1.00 77.88  ? 1699 LYS B NZ    1 
ATOM   7365 N  N     . VAL B 1 483 ? -33.227 9.279   32.796 1.00 80.64  ? 1700 VAL B N     1 
ATOM   7366 C  CA    . VAL B 1 483 ? -32.732 10.168  33.854 1.00 70.98  ? 1700 VAL B CA    1 
ATOM   7367 C  C     . VAL B 1 483 ? -31.287 10.624  33.623 1.00 75.34  ? 1700 VAL B C     1 
ATOM   7368 O  O     . VAL B 1 483 ? -31.017 11.822  33.508 1.00 88.50  ? 1700 VAL B O     1 
ATOM   7369 C  CB    . VAL B 1 483 ? -32.869 9.487   35.232 1.00 62.78  ? 1700 VAL B CB    1 
ATOM   7370 C  CG1   . VAL B 1 483 ? -32.251 10.356  36.303 1.00 74.43  ? 1700 VAL B CG1   1 
ATOM   7371 C  CG2   . VAL B 1 483 ? -34.322 9.159   35.553 1.00 64.27  ? 1700 VAL B CG2   1 
ATOM   7372 N  N     . ASP B 1 484 ? -30.347 9.678   33.549 1.00 63.14  ? 1701 ASP B N     1 
ATOM   7373 C  CA    . ASP B 1 484 ? -28.914 9.985   33.591 1.00 56.12  ? 1701 ASP B CA    1 
ATOM   7374 C  C     . ASP B 1 484 ? -28.448 10.890  32.458 1.00 64.95  ? 1701 ASP B C     1 
ATOM   7375 O  O     . ASP B 1 484 ? -28.839 10.725  31.302 1.00 71.14  ? 1701 ASP B O     1 
ATOM   7376 C  CB    . ASP B 1 484 ? -28.104 8.686   33.554 1.00 52.75  ? 1701 ASP B CB    1 
ATOM   7377 C  CG    . ASP B 1 484 ? -28.338 7.821   34.777 1.00 71.19  ? 1701 ASP B CG    1 
ATOM   7378 O  OD1   . ASP B 1 484 ? -28.300 6.577   34.660 1.00 76.20  ? 1701 ASP B OD1   1 
ATOM   7379 O  OD2   . ASP B 1 484 ? -28.575 8.387   35.864 1.00 76.95  ? 1701 ASP B OD2   1 
ATOM   7380 N  N     . LYS B 1 485 ? -27.591 11.824  32.800 1.00 74.73  ? 1702 LYS B N     1 
ATOM   7381 C  CA    . LYS B 1 485 ? -27.035 12.730  31.830 1.00 72.67  ? 1702 LYS B CA    1 
ATOM   7382 C  C     . LYS B 1 485 ? -25.522 12.788  31.996 1.00 69.22  ? 1702 LYS B C     1 
ATOM   7383 O  O     . LYS B 1 485 ? -25.017 12.385  32.992 1.00 69.02  ? 1702 LYS B O     1 
ATOM   7384 C  CB    . LYS B 1 485 ? -27.660 14.095  31.989 1.00 50.21  ? 1702 LYS B CB    1 
ATOM   7385 N  N     . CYS B 1 486 ? -24.797 13.379  31.060 1.00 59.64  ? 1703 CYS B N     1 
ATOM   7386 C  CA    . CYS B 1 486 ? -23.348 13.480  31.144 1.00 54.45  ? 1703 CYS B CA    1 
ATOM   7387 C  C     . CYS B 1 486 ? -22.906 14.418  32.211 1.00 61.20  ? 1703 CYS B C     1 
ATOM   7388 O  O     . CYS B 1 486 ? -23.628 15.248  32.683 1.00 74.19  ? 1703 CYS B O     1 
ATOM   7389 C  CB    . CYS B 1 486 ? -22.714 13.872  29.828 1.00 51.28  ? 1703 CYS B CB    1 
ATOM   7390 S  SG    . CYS B 1 486 ? -20.962 14.196  29.837 1.00 55.60  ? 1703 CYS B SG    1 
ATOM   7391 N  N     . VAL B 1 487 ? -21.656 14.340  32.589 1.00 55.68  ? 1704 VAL B N     1 
ATOM   7392 C  CA    . VAL B 1 487 ? -21.214 15.134  33.706 1.00 62.17  ? 1704 VAL B CA    1 
ATOM   7393 C  C     . VAL B 1 487 ? -20.896 16.585  33.388 1.00 68.87  ? 1704 VAL B C     1 
ATOM   7394 O  O     . VAL B 1 487 ? -20.626 17.369  34.239 1.00 63.98  ? 1704 VAL B O     1 
ATOM   7395 C  CB    . VAL B 1 487 ? -20.196 14.358  34.537 1.00 53.22  ? 1704 VAL B CB    1 
ATOM   7396 C  CG1   . VAL B 1 487 ? -18.960 14.043  33.772 1.00 49.26  ? 1704 VAL B CG1   1 
ATOM   7397 C  CG2   . VAL B 1 487 ? -19.863 15.099  35.781 1.00 53.03  ? 1704 VAL B CG2   1 
ATOM   7398 N  N     . HIS B 1 488 ? -21.080 16.957  32.149 1.00 75.56  ? 1705 HIS B N     1 
ATOM   7399 C  CA    . HIS B 1 488 ? -20.821 18.298  31.691 1.00 80.04  ? 1705 HIS B CA    1 
ATOM   7400 C  C     . HIS B 1 488 ? -22.072 18.942  31.083 1.00 78.31  ? 1705 HIS B C     1 
ATOM   7401 O  O     . HIS B 1 488 ? -23.094 18.304  30.970 1.00 58.18  ? 1705 HIS B O     1 
ATOM   7402 C  CB    . HIS B 1 488 ? -19.740 18.225  30.664 1.00 80.39  ? 1705 HIS B CB    1 
ATOM   7403 C  CG    . HIS B 1 488 ? -18.908 19.447  30.580 1.00 81.95  ? 1705 HIS B CG    1 
ATOM   7404 N  ND1   . HIS B 1 488 ? -18.539 20.165  31.682 1.00 81.29  ? 1705 HIS B ND1   1 
ATOM   7405 C  CD2   . HIS B 1 488 ? -18.358 20.070  29.526 1.00 85.66  ? 1705 HIS B CD2   1 
ATOM   7406 C  CE1   . HIS B 1 488 ? -17.790 21.176  31.315 1.00 88.30  ? 1705 HIS B CE1   1 
ATOM   7407 N  NE2   . HIS B 1 488 ? -17.672 21.145  30.009 1.00 88.48  ? 1705 HIS B NE2   1 
ATOM   7408 N  N     . PRO B 1 489 ? -22.033 20.249  30.830 1.00 86.06  ? 1706 PRO B N     1 
ATOM   7409 C  CA    . PRO B 1 489 ? -23.025 21.107  30.199 1.00 74.27  ? 1706 PRO B CA    1 
ATOM   7410 C  C     . PRO B 1 489 ? -23.505 20.909  28.783 1.00 71.76  ? 1706 PRO B C     1 
ATOM   7411 O  O     . PRO B 1 489 ? -24.691 20.938  28.720 1.00 83.16  ? 1706 PRO B O     1 
ATOM   7412 C  CB    . PRO B 1 489 ? -22.376 22.426  30.323 1.00 65.70  ? 1706 PRO B CB    1 
ATOM   7413 C  CG    . PRO B 1 489 ? -22.019 22.350  31.752 1.00 78.89  ? 1706 PRO B CG    1 
ATOM   7414 C  CD    . PRO B 1 489 ? -21.418 20.994  31.929 1.00 85.12  ? 1706 PRO B CD    1 
ATOM   7415 N  N     . ALA B 1 490 ? -22.756 20.665  27.733 1.00 61.03  ? 1707 ALA B N     1 
ATOM   7416 C  CA    . ALA B 1 490 ? -23.439 20.463  26.450 1.00 65.47  ? 1707 ALA B CA    1 
ATOM   7417 C  C     . ALA B 1 490 ? -23.616 18.978  26.104 1.00 76.06  ? 1707 ALA B C     1 
ATOM   7418 O  O     . ALA B 1 490 ? -24.633 18.379  26.365 1.00 55.39  ? 1707 ALA B O     1 
ATOM   7419 C  CB    . ALA B 1 490 ? -22.723 21.197  25.360 1.00 57.93  ? 1707 ALA B CB    1 
ATOM   7420 N  N     . CYS B 1 491 ? -22.462 18.327  25.800 1.00 97.53  ? 1708 CYS B N     1 
ATOM   7421 C  CA    . CYS B 1 491 ? -22.221 16.902  25.514 1.00 90.01  ? 1708 CYS B CA    1 
ATOM   7422 C  C     . CYS B 1 491 ? -23.069 16.243  24.435 1.00 90.55  ? 1708 CYS B C     1 
ATOM   7423 O  O     . CYS B 1 491 ? -23.580 16.893  23.521 1.00 94.31  ? 1708 CYS B O     1 
ATOM   7424 C  CB    . CYS B 1 491 ? -22.395 16.090  26.785 1.00 88.27  ? 1708 CYS B CB    1 
ATOM   7425 S  SG    . CYS B 1 491 ? -21.905 17.008  28.203 1.00 102.95 ? 1708 CYS B SG    1 
ATOM   7426 N  N     . GLY B 1 492 ? -23.127 14.919  24.505 1.00 91.28  ? 1709 GLY B N     1 
ATOM   7427 C  CA    . GLY B 1 492 ? -24.131 14.116  23.853 1.00 94.06  ? 1709 GLY B CA    1 
ATOM   7428 C  C     . GLY B 1 492 ? -25.389 14.057  24.686 1.00 95.42  ? 1709 GLY B C     1 
ATOM   7429 O  O     . GLY B 1 492 ? -26.337 13.343  24.346 1.00 103.27 ? 1709 GLY B O     1 
ATOM   7430 N  N     . ARG B 1 493 ? -25.404 14.816  25.786 1.00 87.57  ? 1710 ARG B N     1 
ATOM   7431 C  CA    . ARG B 1 493 ? -26.417 14.787  26.838 1.00 85.70  ? 1710 ARG B CA    1 
ATOM   7432 C  C     . ARG B 1 493 ? -26.660 13.416  27.477 1.00 80.62  ? 1710 ARG B C     1 
ATOM   7433 O  O     . ARG B 1 493 ? -26.386 13.245  28.667 1.00 78.20  ? 1710 ARG B O     1 
ATOM   7434 C  CB    . ARG B 1 493 ? -27.745 15.355  26.305 1.00 87.02  ? 1710 ARG B CB    1 
ATOM   7435 N  N     . VAL B 1 494 ? -27.190 12.445  26.730 1.00 80.98  ? 1711 VAL B N     1 
ATOM   7436 C  CA    . VAL B 1 494 ? -27.530 11.152  27.322 1.00 72.08  ? 1711 VAL B CA    1 
ATOM   7437 C  C     . VAL B 1 494 ? -26.259 10.435  27.755 1.00 70.77  ? 1711 VAL B C     1 
ATOM   7438 O  O     . VAL B 1 494 ? -25.262 10.403  27.025 1.00 68.91  ? 1711 VAL B O     1 
ATOM   7439 C  CB    . VAL B 1 494 ? -28.334 10.297  26.332 1.00 64.36  ? 1711 VAL B CB    1 
ATOM   7440 N  N     . ALA B 1 495 ? -26.273 9.891   28.963 1.00 67.46  ? 1712 ALA B N     1 
ATOM   7441 C  CA    . ALA B 1 495 ? -25.088 9.230   29.490 1.00 70.06  ? 1712 ALA B CA    1 
ATOM   7442 C  C     . ALA B 1 495 ? -24.975 7.833   28.890 1.00 64.97  ? 1712 ALA B C     1 
ATOM   7443 O  O     . ALA B 1 495 ? -25.857 6.984   29.091 1.00 62.55  ? 1712 ALA B O     1 
ATOM   7444 C  CB    . ALA B 1 495 ? -25.138 9.153   31.014 1.00 71.85  ? 1712 ALA B CB    1 
ATOM   7445 N  N     . LYS B 1 496 ? -23.883 7.551   28.215 1.00 55.35  ? 1713 LYS B N     1 
ATOM   7446 C  CA    . LYS B 1 496 ? -23.736 6.254   27.656 1.00 53.13  ? 1713 LYS B CA    1 
ATOM   7447 C  C     . LYS B 1 496 ? -23.244 5.270   28.687 1.00 59.89  ? 1713 LYS B C     1 
ATOM   7448 O  O     . LYS B 1 496 ? -23.641 4.141   28.663 1.00 51.06  ? 1713 LYS B O     1 
ATOM   7449 C  CB    . LYS B 1 496 ? -22.899 6.305   26.417 1.00 56.18  ? 1713 LYS B CB    1 
ATOM   7450 C  CG    . LYS B 1 496 ? -23.548 7.072   25.304 1.00 56.69  ? 1713 LYS B CG    1 
ATOM   7451 C  CD    . LYS B 1 496 ? -23.590 6.261   24.046 1.00 77.33  ? 1713 LYS B CD    1 
ATOM   7452 C  CE    . LYS B 1 496 ? -24.690 5.207   24.098 1.00 95.87  ? 1713 LYS B CE    1 
ATOM   7453 N  NZ    . LYS B 1 496 ? -24.476 3.919   23.353 1.00 98.97  ? 1713 LYS B NZ    1 
ATOM   7454 N  N     . PHE B 1 497 ? -22.391 5.677   29.615 1.00 62.70  ? 1714 PHE B N     1 
ATOM   7455 C  CA    . PHE B 1 497 ? -21.913 4.829   30.711 1.00 53.71  ? 1714 PHE B CA    1 
ATOM   7456 C  C     . PHE B 1 497 ? -21.203 5.637   31.739 1.00 59.33  ? 1714 PHE B C     1 
ATOM   7457 O  O     . PHE B 1 497 ? -21.233 6.812   31.685 1.00 52.34  ? 1714 PHE B O     1 
ATOM   7458 C  CB    . PHE B 1 497 ? -20.874 3.874   30.231 1.00 46.36  ? 1714 PHE B CB    1 
ATOM   7459 C  CG    . PHE B 1 497 ? -20.012 4.446   29.224 1.00 62.70  ? 1714 PHE B CG    1 
ATOM   7460 C  CD1   . PHE B 1 497 ? -19.356 5.575   29.478 1.00 87.10  ? 1714 PHE B CD1   1 
ATOM   7461 C  CD2   . PHE B 1 497 ? -19.938 3.898   28.023 1.00 54.36  ? 1714 PHE B CD2   1 
ATOM   7462 C  CE1   . PHE B 1 497 ? -18.573 6.144   28.551 1.00 91.18  ? 1714 PHE B CE1   1 
ATOM   7463 C  CE2   . PHE B 1 497 ? -19.187 4.450   27.066 1.00 71.48  ? 1714 PHE B CE2   1 
ATOM   7464 C  CZ    . PHE B 1 497 ? -18.495 5.581   27.328 1.00 87.23  ? 1714 PHE B CZ    1 
ATOM   7465 N  N     . TYR B 1 498 ? -20.601 4.975   32.712 1.00 40.62  ? 1715 TYR B N     1 
ATOM   7466 C  CA    . TYR B 1 498 ? -19.734 5.647   33.678 1.00 40.39  ? 1715 TYR B CA    1 
ATOM   7467 C  C     . TYR B 1 498 ? -18.283 5.478   33.270 1.00 42.30  ? 1715 TYR B C     1 
ATOM   7468 O  O     . TYR B 1 498 ? -17.844 4.360   32.975 1.00 47.92  ? 1715 TYR B O     1 
ATOM   7469 C  CB    . TYR B 1 498 ? -19.900 5.112   35.092 1.00 40.71  ? 1715 TYR B CB    1 
ATOM   7470 C  CG    . TYR B 1 498 ? -21.229 5.403   35.707 1.00 41.99  ? 1715 TYR B CG    1 
ATOM   7471 C  CD1   . TYR B 1 498 ? -21.399 6.453   36.595 1.00 46.44  ? 1715 TYR B CD1   1 
ATOM   7472 C  CD2   . TYR B 1 498 ? -22.314 4.608   35.426 1.00 50.25  ? 1715 TYR B CD2   1 
ATOM   7473 C  CE1   . TYR B 1 498 ? -22.640 6.708   37.169 1.00 43.99  ? 1715 TYR B CE1   1 
ATOM   7474 C  CE2   . TYR B 1 498 ? -23.543 4.848   35.989 1.00 59.48  ? 1715 TYR B CE2   1 
ATOM   7475 C  CZ    . TYR B 1 498 ? -23.709 5.895   36.856 1.00 56.27  ? 1715 TYR B CZ    1 
ATOM   7476 O  OH    . TYR B 1 498 ? -24.961 6.097   37.388 1.00 58.74  ? 1715 TYR B OH    1 
ATOM   7477 N  N     . THR B 1 499 ? -17.533 6.577   33.308 1.00 39.04  ? 1716 THR B N     1 
ATOM   7478 C  CA    . THR B 1 499 ? -16.101 6.584   33.062 1.00 38.04  ? 1716 THR B CA    1 
ATOM   7479 C  C     . THR B 1 499 ? -15.354 7.016   34.296 1.00 46.55  ? 1716 THR B C     1 
ATOM   7480 O  O     . THR B 1 499 ? -15.831 7.857   35.077 1.00 47.55  ? 1716 THR B O     1 
ATOM   7481 C  CB    . THR B 1 499 ? -15.686 7.520   31.942 1.00 50.83  ? 1716 THR B CB    1 
ATOM   7482 O  OG1   . THR B 1 499 ? -16.447 8.723   32.049 1.00 76.01  ? 1716 THR B OG1   1 
ATOM   7483 C  CG2   . THR B 1 499 ? -15.880 6.895   30.598 1.00 46.42  ? 1716 THR B CG2   1 
ATOM   7484 N  N     . LEU B 1 500 ? -14.184 6.412   34.453 1.00 49.35  ? 1717 LEU B N     1 
ATOM   7485 C  CA    . LEU B 1 500 ? -13.237 6.802   35.473 1.00 58.18  ? 1717 LEU B CA    1 
ATOM   7486 C  C     . LEU B 1 500 ? -12.335 7.891   34.913 1.00 61.59  ? 1717 LEU B C     1 
ATOM   7487 O  O     . LEU B 1 500 ? -11.806 7.762   33.802 1.00 71.47  ? 1717 LEU B O     1 
ATOM   7488 C  CB    . LEU B 1 500 ? -12.429 5.594   35.932 1.00 62.74  ? 1717 LEU B CB    1 
ATOM   7489 C  CG    . LEU B 1 500 ? -12.241 5.534   37.443 1.00 70.54  ? 1717 LEU B CG    1 
ATOM   7490 C  CD1   . LEU B 1 500 ? -13.454 6.094   38.137 1.00 72.95  ? 1717 LEU B CD1   1 
ATOM   7491 C  CD2   . LEU B 1 500 ? -12.044 4.114   37.874 1.00 78.07  ? 1717 LEU B CD2   1 
ATOM   7492 N  N     . PHE B 1 501 ? -12.222 8.987   35.649 1.00 52.52  ? 1718 PHE B N     1 
ATOM   7493 C  CA    . PHE B 1 501 ? -11.410 10.121  35.254 1.00 52.27  ? 1718 PHE B CA    1 
ATOM   7494 C  C     . PHE B 1 501 ? -10.402 10.466  36.338 1.00 59.62  ? 1718 PHE B C     1 
ATOM   7495 O  O     . PHE B 1 501 ? -10.656 10.271  37.528 1.00 61.48  ? 1718 PHE B O     1 
ATOM   7496 C  CB    . PHE B 1 501 ? -12.258 11.353  35.035 1.00 54.07  ? 1718 PHE B CB    1 
ATOM   7497 C  CG    . PHE B 1 501 ? -13.168 11.277  33.884 1.00 50.40  ? 1718 PHE B CG    1 
ATOM   7498 C  CD1   . PHE B 1 501 ? -14.545 11.279  34.086 1.00 39.27  ? 1718 PHE B CD1   1 
ATOM   7499 C  CD2   . PHE B 1 501 ? -12.663 11.288  32.604 1.00 40.94  ? 1718 PHE B CD2   1 
ATOM   7500 C  CE1   . PHE B 1 501 ? -15.396 11.258  33.031 1.00 39.56  ? 1718 PHE B CE1   1 
ATOM   7501 C  CE2   . PHE B 1 501 ? -13.508 11.262  31.534 1.00 49.78  ? 1718 PHE B CE2   1 
ATOM   7502 C  CZ    . PHE B 1 501 ? -14.883 11.247  31.741 1.00 50.49  ? 1718 PHE B CZ    1 
ATOM   7503 N  N     . GLY B 1 502 ? -9.314  11.108  35.931 1.00 65.41  ? 1719 GLY B N     1 
ATOM   7504 C  CA    . GLY B 1 502 ? -8.344  11.587  36.897 1.00 61.52  ? 1719 GLY B CA    1 
ATOM   7505 C  C     . GLY B 1 502 ? -7.068  12.036  36.226 1.00 59.76  ? 1719 GLY B C     1 
ATOM   7506 O  O     . GLY B 1 502 ? -6.902  11.932  35.006 1.00 58.42  ? 1719 GLY B O     1 
ATOM   7507 N  N     . ARG B 1 503 ? -6.177  12.588  37.050 1.00 58.01  ? 1720 ARG B N     1 
ATOM   7508 C  CA    . ARG B 1 503 ? -4.829  12.917  36.599 1.00 63.01  ? 1720 ARG B CA    1 
ATOM   7509 C  C     . ARG B 1 503 ? -4.056  11.634  36.299 1.00 51.45  ? 1720 ARG B C     1 
ATOM   7510 O  O     . ARG B 1 503 ? -4.243  10.619  36.964 1.00 42.03  ? 1720 ARG B O     1 
ATOM   7511 C  CB    . ARG B 1 503 ? -4.106  13.763  37.654 1.00 72.05  ? 1720 ARG B CB    1 
ATOM   7512 C  CG    . ARG B 1 503 ? -4.899  14.991  38.091 1.00 73.72  ? 1720 ARG B CG    1 
ATOM   7513 C  CD    . ARG B 1 503 ? -4.193  16.297  37.782 1.00 66.60  ? 1720 ARG B CD    1 
ATOM   7514 N  NE    . ARG B 1 503 ? -4.932  17.443  38.315 1.00 66.35  ? 1720 ARG B NE    1 
ATOM   7515 C  CZ    . ARG B 1 503 ? -5.025  17.743  39.610 1.00 70.03  ? 1720 ARG B CZ    1 
ATOM   7516 N  NH1   . ARG B 1 503 ? -4.432  16.980  40.521 1.00 72.04  ? 1720 ARG B NH1   1 
ATOM   7517 N  NH2   . ARG B 1 503 ? -5.715  18.808  40.000 1.00 68.81  ? 1720 ARG B NH2   1 
ATOM   7518 N  N     . SER B 1 504 ? -3.198  11.664  35.277 1.00 54.09  ? 1721 SER B N     1 
ATOM   7519 C  CA    . SER B 1 504 ? -2.477  10.457  34.894 1.00 52.90  ? 1721 SER B CA    1 
ATOM   7520 C  C     . SER B 1 504 ? -1.038  10.770  34.507 1.00 59.45  ? 1721 SER B C     1 
ATOM   7521 O  O     . SER B 1 504 ? -0.634  11.927  34.360 1.00 64.74  ? 1721 SER B O     1 
ATOM   7522 C  CB    . SER B 1 504 ? -3.145  9.731   33.716 1.00 47.01  ? 1721 SER B CB    1 
ATOM   7523 O  OG    . SER B 1 504 ? -2.663  10.242  32.481 1.00 43.34  ? 1721 SER B OG    1 
ATOM   7524 N  N     . TYR B 1 505 ? -0.265  9.695   34.375 1.00 64.70  ? 1722 TYR B N     1 
ATOM   7525 C  CA    . TYR B 1 505 ? 1.113   9.712   33.907 1.00 68.92  ? 1722 TYR B CA    1 
ATOM   7526 C  C     . TYR B 1 505 ? 1.203   9.640   32.392 1.00 76.29  ? 1722 TYR B C     1 
ATOM   7527 O  O     . TYR B 1 505 ? 0.237   9.270   31.711 1.00 71.64  ? 1722 TYR B O     1 
ATOM   7528 C  CB    . TYR B 1 505 ? 1.900   8.557   34.521 1.00 60.12  ? 1722 TYR B CB    1 
ATOM   7529 C  CG    . TYR B 1 505 ? 2.602   8.941   35.797 1.00 61.61  ? 1722 TYR B CG    1 
ATOM   7530 C  CD1   . TYR B 1 505 ? 3.935   9.347   35.788 1.00 57.85  ? 1722 TYR B CD1   1 
ATOM   7531 C  CD2   . TYR B 1 505 ? 1.924   8.914   37.022 1.00 69.15  ? 1722 TYR B CD2   1 
ATOM   7532 C  CE1   . TYR B 1 505 ? 4.583   9.714   36.973 1.00 68.91  ? 1722 TYR B CE1   1 
ATOM   7533 C  CE2   . TYR B 1 505 ? 2.553   9.281   38.212 1.00 72.99  ? 1722 TYR B CE2   1 
ATOM   7534 C  CZ    . TYR B 1 505 ? 3.884   9.681   38.189 1.00 77.97  ? 1722 TYR B CZ    1 
ATOM   7535 O  OH    . TYR B 1 505 ? 4.513   10.039  39.377 1.00 82.25  ? 1722 TYR B OH    1 
ATOM   7536 O  OXT   . TYR B 1 505 ? 2.268   9.948   31.846 1.00 79.25  ? 1722 TYR B OXT   1 
HETATM 7537 P  PG    . ANP C 2 .   ? 35.194  -11.232 13.380 1.00 91.93  ? 1801 ANP A PG    1 
HETATM 7538 O  O1G   . ANP C 2 .   ? 36.329  -11.530 12.443 1.00 86.86  ? 1801 ANP A O1G   1 
HETATM 7539 O  O2G   . ANP C 2 .   ? 34.950  -9.663  13.437 1.00 84.23  ? 1801 ANP A O2G   1 
HETATM 7540 O  O3G   . ANP C 2 .   ? 33.910  -11.979 12.830 1.00 84.48  ? 1801 ANP A O3G   1 
HETATM 7541 P  PB    . ANP C 2 .   ? 35.044  -10.925 16.253 1.00 72.11  ? 1801 ANP A PB    1 
HETATM 7542 O  O1B   . ANP C 2 .   ? 36.255  -10.339 16.908 1.00 66.27  ? 1801 ANP A O1B   1 
HETATM 7543 O  O2B   . ANP C 2 .   ? 34.211  -9.716  15.733 1.00 80.99  ? 1801 ANP A O2B   1 
HETATM 7544 N  N3B   . ANP C 2 .   ? 35.425  -11.908 14.928 1.00 85.22  ? 1801 ANP A N3B   1 
HETATM 7545 P  PA    . ANP C 2 .   ? 33.760  -11.094 18.609 1.00 43.63  ? 1801 ANP A PA    1 
HETATM 7546 O  O1A   . ANP C 2 .   ? 34.649  -11.295 19.762 1.00 37.83  ? 1801 ANP A O1A   1 
HETATM 7547 O  O2A   . ANP C 2 .   ? 33.697  -9.625  18.245 1.00 61.88  ? 1801 ANP A O2A   1 
HETATM 7548 O  O3A   . ANP C 2 .   ? 34.233  -11.768 17.274 1.00 59.51  ? 1801 ANP A O3A   1 
HETATM 7549 O  "O5'" . ANP C 2 .   ? 32.316  -11.646 18.897 1.00 49.89  ? 1801 ANP A "O5'" 1 
HETATM 7550 C  "C5'" . ANP C 2 .   ? 32.104  -12.674 19.887 1.00 63.46  ? 1801 ANP A "C5'" 1 
HETATM 7551 C  "C4'" . ANP C 2 .   ? 31.631  -13.905 19.145 1.00 59.16  ? 1801 ANP A "C4'" 1 
HETATM 7552 O  "O4'" . ANP C 2 .   ? 30.573  -13.510 18.262 1.00 42.81  ? 1801 ANP A "O4'" 1 
HETATM 7553 C  "C3'" . ANP C 2 .   ? 32.721  -14.553 18.293 1.00 53.85  ? 1801 ANP A "C3'" 1 
HETATM 7554 O  "O3'" . ANP C 2 .   ? 32.984  -15.821 18.870 1.00 52.56  ? 1801 ANP A "O3'" 1 
HETATM 7555 C  "C2'" . ANP C 2 .   ? 32.096  -14.733 16.901 1.00 46.25  ? 1801 ANP A "C2'" 1 
HETATM 7556 O  "O2'" . ANP C 2 .   ? 32.044  -16.089 16.489 1.00 44.84  ? 1801 ANP A "O2'" 1 
HETATM 7557 C  "C1'" . ANP C 2 .   ? 30.687  -14.146 17.015 1.00 45.98  ? 1801 ANP A "C1'" 1 
HETATM 7558 N  N9    . ANP C 2 .   ? 30.412  -13.122 16.034 1.00 54.63  ? 1801 ANP A N9    1 
HETATM 7559 C  C8    . ANP C 2 .   ? 31.192  -12.051 15.689 1.00 57.68  ? 1801 ANP A C8    1 
HETATM 7560 N  N7    . ANP C 2 .   ? 30.633  -11.247 14.809 1.00 62.15  ? 1801 ANP A N7    1 
HETATM 7561 C  C5    . ANP C 2 .   ? 29.384  -11.812 14.608 1.00 55.65  ? 1801 ANP A C5    1 
HETATM 7562 C  C6    . ANP C 2 .   ? 28.296  -11.445 13.785 1.00 49.02  ? 1801 ANP A C6    1 
HETATM 7563 N  N6    . ANP C 2 .   ? 28.288  -10.368 13.001 1.00 52.05  ? 1801 ANP A N6    1 
HETATM 7564 N  N1    . ANP C 2 .   ? 27.192  -12.214 13.829 1.00 49.21  ? 1801 ANP A N1    1 
HETATM 7565 C  C2    . ANP C 2 .   ? 27.186  -13.288 14.626 1.00 51.10  ? 1801 ANP A C2    1 
HETATM 7566 N  N3    . ANP C 2 .   ? 28.151  -13.745 15.427 1.00 42.63  ? 1801 ANP A N3    1 
HETATM 7567 C  C4    . ANP C 2 .   ? 29.220  -12.956 15.372 1.00 52.19  ? 1801 ANP A C4    1 
HETATM 7568 O  "O4'" . HFG D 3 .   ? 33.369  -7.701  21.472 0.91 30.31  ? 1802 HFG A "O4'" 1 
HETATM 7569 C  C21   . HFG D 3 .   ? 34.543  -7.995  21.525 0.91 39.78  ? 1802 HFG A C21   1 
HETATM 7570 C  "C3'" . HFG D 3 .   ? 35.162  -8.675  22.725 0.91 34.76  ? 1802 HFG A "C3'" 1 
HETATM 7571 C  "C2'" . HFG D 3 .   ? 34.177  -9.318  23.712 0.91 39.49  ? 1802 HFG A "C2'" 1 
HETATM 7572 N  "N1'" . HFG D 3 .   ? 33.201  -8.365  24.247 0.91 29.85  ? 1802 HFG A "N1'" 1 
HETATM 7573 C  "C6'" . HFG D 3 .   ? 32.421  -8.979  25.330 0.91 29.41  ? 1802 HFG A "C6'" 1 
HETATM 7574 C  "C5'" . HFG D 3 .   ? 31.645  -10.182 24.842 0.91 29.11  ? 1802 HFG A "C5'" 1 
HETATM 7575 C  "C4'" . HFG D 3 .   ? 32.587  -11.195 24.196 0.91 32.98  ? 1802 HFG A "C4'" 1 
HETATM 7576 C  C39   . HFG D 3 .   ? 33.451  -10.531 23.137 0.91 42.74  ? 1802 HFG A C39   1 
HETATM 7577 O  "O7'" . HFG D 3 .   ? 34.368  -11.466 22.563 0.91 43.50  ? 1802 HFG A "O7'" 1 
HETATM 7578 C  "C1'" . HFG D 3 .   ? 35.477  -7.718  20.377 0.91 41.65  ? 1802 HFG A "C1'" 1 
HETATM 7579 N  N3    . HFG D 3 .   ? 34.964  -6.649  19.531 0.91 46.00  ? 1802 HFG A N3    1 
HETATM 7580 C  C4    . HFG D 3 .   ? 34.942  -5.361  20.053 0.91 53.11  ? 1802 HFG A C4    1 
HETATM 7581 O  O11   . HFG D 3 .   ? 35.469  -5.098  21.124 0.91 61.84  ? 1802 HFG A O11   1 
HETATM 7582 C  C10   . HFG D 3 .   ? 34.295  -4.379  19.183 0.91 40.43  ? 1802 HFG A C10   1 
HETATM 7583 C  C5    . HFG D 3 .   ? 34.172  -3.062  19.593 0.91 41.17  ? 1802 HFG A C5    1 
HETATM 7584 C  C2    . HFG D 3 .   ? 34.475  -6.926  18.287 0.91 50.74  ? 1802 HFG A C2    1 
HETATM 7585 N  N1    . HFG D 3 .   ? 33.917  -6.092  17.486 0.91 55.93  ? 1802 HFG A N1    1 
HETATM 7586 C  C9    . HFG D 3 .   ? 33.802  -4.780  17.941 0.91 53.02  ? 1802 HFG A C9    1 
HETATM 7587 C  C8    . HFG D 3 .   ? 33.157  -3.849  17.128 0.91 62.48  ? 1802 HFG A C8    1 
HETATM 7588 C  C7    . HFG D 3 .   ? 33.031  -2.539  17.565 0.91 64.49  ? 1802 HFG A C7    1 
HETATM 7589 BR BR1   . HFG D 3 .   ? 32.045  -1.291  16.561 0.91 72.87  ? 1802 HFG A BR1   1 
HETATM 7590 C  C6    . HFG D 3 .   ? 33.559  -2.147  18.761 0.91 52.97  ? 1802 HFG A C6    1 
HETATM 7591 CL CL1   . HFG D 3 .   ? 33.506  -0.478  19.206 0.91 47.09  ? 1802 HFG A CL1   1 
HETATM 7592 MG MG    . MG  E 4 .   ? 33.687  -7.980  13.898 1.00 62.89  ? 1803 MG  A MG    1 
HETATM 7593 ZN ZN    . ZN  F 5 .   ? 57.012  -18.760 11.910 0.53 56.50  ? 1804 ZN  A ZN    1 
HETATM 7594 P  PG    . ANP G 2 .   ? 1.749   6.776   26.709 1.00 60.05  ? 1801 ANP B PG    1 
HETATM 7595 O  O1G   . ANP G 2 .   ? 0.775   7.547   27.558 1.00 62.06  ? 1801 ANP B O1G   1 
HETATM 7596 O  O2G   . ANP G 2 .   ? 2.002   7.563   25.344 1.00 54.23  ? 1801 ANP B O2G   1 
HETATM 7597 O  O3G   . ANP G 2 .   ? 3.144   6.726   27.418 1.00 68.53  ? 1801 ANP B O3G   1 
HETATM 7598 P  PB    . ANP G 2 .   ? 1.551   4.648   24.799 1.00 56.32  ? 1801 ANP B PB    1 
HETATM 7599 O  O1B   . ANP G 2 .   ? 0.430   4.818   23.821 1.00 47.74  ? 1801 ANP B O1B   1 
HETATM 7600 O  O2B   . ANP G 2 .   ? 2.755   5.429   24.196 1.00 60.54  ? 1801 ANP B O2B   1 
HETATM 7601 N  N3B   . ANP G 2 .   ? 1.181   5.213   26.358 1.00 46.61  ? 1801 ANP B N3B   1 
HETATM 7602 P  PA    . ANP G 2 .   ? 1.600   1.836   24.212 1.00 59.38  ? 1801 ANP B PA    1 
HETATM 7603 O  O1A   . ANP G 2 .   ? 0.184   1.400   24.412 1.00 45.31  ? 1801 ANP B O1A   1 
HETATM 7604 O  O2A   . ANP G 2 .   ? 2.193   1.993   22.814 1.00 60.78  ? 1801 ANP B O2A   1 
HETATM 7605 O  O3A   . ANP G 2 .   ? 1.827   3.138   25.122 1.00 56.10  ? 1801 ANP B O3A   1 
HETATM 7606 O  "O5'" . ANP G 2 .   ? 2.529   0.807   24.906 1.00 46.83  ? 1801 ANP B "O5'" 1 
HETATM 7607 C  "C5'" . ANP G 2 .   ? 1.965   -0.363  25.446 1.00 52.44  ? 1801 ANP B "C5'" 1 
HETATM 7608 C  "C4'" . ANP G 2 .   ? 2.197   -0.251  26.924 1.00 49.39  ? 1801 ANP B "C4'" 1 
HETATM 7609 O  "O4'" . ANP G 2 .   ? 3.569   0.087   27.172 1.00 48.27  ? 1801 ANP B "O4'" 1 
HETATM 7610 C  "C3'" . ANP G 2 .   ? 1.354   0.798   27.632 1.00 49.62  ? 1801 ANP B "C3'" 1 
HETATM 7611 O  "O3'" . ANP G 2 .   ? 0.217   0.182   28.215 1.00 69.84  ? 1801 ANP B "O3'" 1 
HETATM 7612 C  "C2'" . ANP G 2 .   ? 2.311   1.455   28.643 1.00 41.36  ? 1801 ANP B "C2'" 1 
HETATM 7613 O  "O2'" . ANP G 2 .   ? 1.975   1.080   29.973 1.00 41.60  ? 1801 ANP B "O2'" 1 
HETATM 7614 C  "C1'" . ANP G 2 .   ? 3.691   0.888   28.322 1.00 35.33  ? 1801 ANP B "C1'" 1 
HETATM 7615 N  N9    . ANP G 2 .   ? 4.662   1.911   27.996 1.00 46.28  ? 1801 ANP B N9    1 
HETATM 7616 C  C8    . ANP G 2 .   ? 4.484   2.879   27.046 1.00 58.31  ? 1801 ANP B C8    1 
HETATM 7617 N  N7    . ANP G 2 .   ? 5.491   3.715   26.929 1.00 66.67  ? 1801 ANP B N7    1 
HETATM 7618 C  C5    . ANP G 2 .   ? 6.394   3.261   27.883 1.00 53.01  ? 1801 ANP B C5    1 
HETATM 7619 C  C6    . ANP G 2 .   ? 7.671   3.721   28.261 1.00 47.62  ? 1801 ANP B C6    1 
HETATM 7620 N  N6    . ANP G 2 .   ? 8.272   4.770   27.698 1.00 46.81  ? 1801 ANP B N6    1 
HETATM 7621 N  N1    . ANP G 2 .   ? 8.307   3.052   29.248 1.00 45.19  ? 1801 ANP B N1    1 
HETATM 7622 C  C2    . ANP G 2 .   ? 7.698   2.004   29.809 1.00 49.44  ? 1801 ANP B C2    1 
HETATM 7623 N  N3    . ANP G 2 .   ? 6.499   1.479   29.532 1.00 48.45  ? 1801 ANP B N3    1 
HETATM 7624 C  C4    . ANP G 2 .   ? 5.897   2.159   28.550 1.00 51.12  ? 1801 ANP B C4    1 
HETATM 7625 O  "O4'" . HFG H 3 .   ? 2.684   0.538   19.900 0.85 57.94  ? 1802 HFG B "O4'" 1 
HETATM 7626 C  C21   . HFG H 3 .   ? 1.541   0.924   20.021 0.85 46.78  ? 1802 HFG B C21   1 
HETATM 7627 C  "C3'" . HFG H 3 .   ? 0.382   -0.044  20.100 0.85 37.54  ? 1802 HFG B "C3'" 1 
HETATM 7628 C  "C2'" . HFG H 3 .   ? 0.775   -1.471  20.501 0.85 31.66  ? 1802 HFG B "C2'" 1 
HETATM 7629 N  "N1'" . HFG H 3 .   ? 1.839   -2.009  19.644 0.85 27.60  ? 1802 HFG B "N1'" 1 
HETATM 7630 C  "C6'" . HFG H 3 .   ? 1.985   -3.443  19.925 0.85 31.22  ? 1802 HFG B "C6'" 1 
HETATM 7631 C  "C5'" . HFG H 3 .   ? 2.399   -3.717  21.359 0.85 30.92  ? 1802 HFG B "C5'" 1 
HETATM 7632 C  "C4'" . HFG H 3 .   ? 1.434   -3.050  22.333 0.85 28.97  ? 1802 HFG B "C4'" 1 
HETATM 7633 C  C39   . HFG H 3 .   ? 1.220   -1.593  21.956 0.85 36.24  ? 1802 HFG B C39   1 
HETATM 7634 O  "O7'" . HFG H 3 .   ? 0.252   -1.010  22.828 0.85 34.73  ? 1802 HFG B "O7'" 1 
HETATM 7635 C  "C1'" . HFG H 3 .   ? 1.167   2.458   20.028 0.85 35.71  ? 1802 HFG B "C1'" 1 
HETATM 7636 N  N3    . HFG H 3 .   ? 2.286   3.321   19.653 0.85 32.44  ? 1802 HFG B N3    1 
HETATM 7637 C  C4    . HFG H 3 .   ? 2.718   3.293   18.334 0.85 30.16  ? 1802 HFG B C4    1 
HETATM 7638 O  O11   . HFG H 3 .   ? 2.040   2.801   17.457 0.85 31.96  ? 1802 HFG B O11   1 
HETATM 7639 C  C10   . HFG H 3 .   ? 3.976   4.012   18.108 0.85 32.67  ? 1802 HFG B C10   1 
HETATM 7640 C  C5    . HFG H 3 .   ? 4.517   4.082   16.833 0.85 40.78  ? 1802 HFG B C5    1 
HETATM 7641 C  C2    . HFG H 3 .   ? 2.954   4.027   20.615 0.85 35.30  ? 1802 HFG B C2    1 
HETATM 7642 N  N1    . HFG H 3 .   ? 4.046   4.686   20.452 0.85 36.11  ? 1802 HFG B N1    1 
HETATM 7643 C  C9    . HFG H 3 .   ? 4.593   4.670   19.171 0.85 32.72  ? 1802 HFG B C9    1 
HETATM 7644 C  C8    . HFG H 3 .   ? 5.778   5.369   18.946 0.85 38.35  ? 1802 HFG B C8    1 
HETATM 7645 C  C7    . HFG H 3 .   ? 6.309   5.423   17.668 0.85 43.98  ? 1802 HFG B C7    1 
HETATM 7646 BR BR1   . HFG H 3 .   ? 7.965   6.301   17.388 0.85 56.17  ? 1802 HFG B BR1   1 
HETATM 7647 C  C6    . HFG H 3 .   ? 5.665   4.814   16.618 0.85 43.42  ? 1802 HFG B C6    1 
HETATM 7648 CL CL1   . HFG H 3 .   ? 6.206   5.052   14.990 0.85 53.20  ? 1802 HFG B CL1   1 
HETATM 7649 MG MG    . MG  I 4 .   ? 4.279   6.868   24.212 1.00 39.94  ? 1803 MG  B MG    1 
HETATM 7650 ZN ZN    . ZN  J 5 .   ? -20.583 14.914  27.238 0.84 64.51  ? 1804 ZN  B ZN    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     . LEU A 6   ? 0.9292 0.8695 0.8192 0.0195  -0.0606 -0.1811 1223 LEU A N     
2    C  CA    . LEU A 6   ? 0.9335 0.8843 0.8125 0.0228  -0.0522 -0.1784 1223 LEU A CA    
3    C  C     . LEU A 6   ? 1.1165 1.0801 0.9793 0.0262  -0.0520 -0.1903 1223 LEU A C     
4    O  O     . LEU A 6   ? 1.2686 1.2299 1.1336 0.0298  -0.0550 -0.2053 1223 LEU A O     
5    C  CB    . LEU A 6   ? 0.8204 0.7646 0.7111 0.0266  -0.0472 -0.1791 1223 LEU A CB    
6    C  CG    . LEU A 6   ? 0.7861 0.7291 0.6814 0.0251  -0.0412 -0.1638 1223 LEU A CG    
7    C  CD1   . LEU A 6   ? 0.7295 0.6608 0.6370 0.0204  -0.0448 -0.1536 1223 LEU A CD1   
8    C  CD2   . LEU A 6   ? 0.6714 0.6130 0.5738 0.0302  -0.0356 -0.1663 1223 LEU A CD2   
9    N  N     . GLU A 7   ? 1.1601 1.1370 1.0062 0.0251  -0.0481 -0.1837 1224 GLU A N     
10   C  CA    . GLU A 7   ? 1.2382 1.2289 1.0666 0.0280  -0.0477 -0.1936 1224 GLU A CA    
11   C  C     . GLU A 7   ? 1.2499 1.2484 1.0749 0.0332  -0.0395 -0.1997 1224 GLU A C     
12   O  O     . GLU A 7   ? 1.4322 1.4348 1.2536 0.0379  -0.0403 -0.2150 1224 GLU A O     
13   C  CB    . GLU A 7   ? 1.2290 1.2303 1.0404 0.0246  -0.0473 -0.1832 1224 GLU A CB    
14   N  N     . ALA A 8   ? 1.1515 1.1521 0.9791 0.0326  -0.0319 -0.1887 1225 ALA A N     
15   C  CA    . ALA A 8   ? 1.1609 1.1711 0.9860 0.0370  -0.0235 -0.1929 1225 ALA A CA    
16   C  C     . ALA A 8   ? 1.1476 1.1471 0.9914 0.0409  -0.0229 -0.1979 1225 ALA A C     
17   O  O     . ALA A 8   ? 1.1447 1.1294 1.0029 0.0390  -0.0271 -0.1933 1225 ALA A O     
18   C  CB    . ALA A 8   ? 1.1718 1.1913 0.9899 0.0338  -0.0156 -0.1783 1225 ALA A CB    
19   N  N     . THR A 9   ? 1.0779 1.0857 0.9212 0.0467  -0.0173 -0.2069 1226 THR A N     
20   C  CA    . THR A 9   ? 0.9684 0.9673 0.8285 0.0518  -0.0167 -0.2128 1226 THR A CA    
21   C  C     . THR A 9   ? 0.9437 0.9481 0.8089 0.0523  -0.0087 -0.2033 1226 THR A C     
22   O  O     . THR A 9   ? 0.9412 0.9598 0.7956 0.0502  -0.0023 -0.1967 1226 THR A O     
23   C  CB    . THR A 9   ? 0.8877 0.8907 0.7467 0.0592  -0.0168 -0.2315 1226 THR A CB    
24   O  OG1   . THR A 9   ? 0.8505 0.8706 0.7029 0.0629  -0.0078 -0.2334 1226 THR A OG1   
25   C  CG2   . THR A 9   ? 0.9883 0.9943 0.8348 0.0586  -0.0225 -0.2419 1226 THR A CG2   
26   N  N     . LYS A 10  ? 0.9050 0.8979 0.7869 0.0551  -0.0095 -0.2024 1227 LYS A N     
27   C  CA    . LYS A 10  ? 0.5745 0.5723 0.4629 0.0560  -0.0030 -0.1941 1227 LYS A CA    
28   C  C     . LYS A 10  ? 0.8782 0.8935 0.7615 0.0611  0.0043  -0.2022 1227 LYS A C     
29   O  O     . LYS A 10  ? 0.9634 0.9906 0.8441 0.0594  0.0111  -0.1945 1227 LYS A O     
30   C  CB    . LYS A 10  ? 0.5680 0.5499 0.4748 0.0589  -0.0061 -0.1926 1227 LYS A CB    
31   C  CG    . LYS A 10  ? 0.7862 0.7706 0.7002 0.0583  -0.0013 -0.1810 1227 LYS A CG    
32   C  CD    . LYS A 10  ? 0.8230 0.7912 0.7538 0.0610  -0.0049 -0.1782 1227 LYS A CD    
33   C  CE    . LYS A 10  ? 0.7551 0.7279 0.6928 0.0620  -0.0003 -0.1690 1227 LYS A CE    
34   N  NZ    . LYS A 10  ? 0.8496 0.8070 0.8024 0.0657  -0.0040 -0.1670 1227 LYS A NZ    
35   N  N     . GLU A 11  ? 1.0092 1.0272 0.8903 0.0671  0.0030  -0.2181 1228 GLU A N     
36   C  CA    . GLU A 11  ? 1.0787 1.1129 0.9578 0.0735  0.0099  -0.2279 1228 GLU A CA    
37   C  C     . GLU A 11  ? 1.0981 1.1525 0.9586 0.0704  0.0162  -0.2264 1228 GLU A C     
38   O  O     . GLU A 11  ? 1.0832 1.1531 0.9422 0.0708  0.0244  -0.2229 1228 GLU A O     
39   C  CB    . GLU A 11  ? 1.0471 1.0758 0.9309 0.0815  0.0059  -0.2463 1228 GLU A CB    
40   C  CG    . GLU A 11  ? 1.0426 1.0475 0.9395 0.0817  -0.0033 -0.2482 1228 GLU A CG    
41   C  CD    . GLU A 11  ? 1.1918 1.1842 1.1052 0.0816  -0.0039 -0.2372 1228 GLU A CD    
42   O  OE1   . GLU A 11  ? 1.2452 1.2471 1.1628 0.0838  0.0023  -0.2322 1228 GLU A OE1   
43   O  OE2   . GLU A 11  ? 1.2336 1.2073 1.1560 0.0792  -0.0106 -0.2335 1228 GLU A OE2   
44   N  N     . ASP A 12  ? 1.1863 1.2414 1.0327 0.0674  0.0125  -0.2288 1229 ASP A N     
45   C  CA    . ASP A 12  ? 1.2971 1.3690 1.1244 0.0634  0.0175  -0.2243 1229 ASP A CA    
46   C  C     . ASP A 12  ? 1.3859 1.4520 1.2091 0.0547  0.0158  -0.2067 1229 ASP A C     
47   O  O     . ASP A 12  ? 1.4859 1.5369 1.3127 0.0519  0.0079  -0.2038 1229 ASP A O     
48   C  CB    . ASP A 12  ? 1.3864 1.4633 1.1991 0.0657  0.0140  -0.2373 1229 ASP A CB    
49   C  CG    . ASP A 12  ? 1.5613 1.6377 1.3805 0.0745  0.0128  -0.2563 1229 ASP A CG    
50   O  OD1   . ASP A 12  ? 1.6656 1.7585 1.4812 0.0795  0.0203  -0.2637 1229 ASP A OD1   
51   O  OD2   . ASP A 12  ? 1.5826 1.6422 1.4115 0.0765  0.0045  -0.2639 1229 ASP A OD2   
52   N  N     . ASN A 13  ? 1.2582 1.3362 1.0750 0.0504  0.0232  -0.1952 1230 ASN A N     
53   C  CA    . ASN A 13  ? 1.1041 1.1772 0.9166 0.0425  0.0222  -0.1785 1230 ASN A CA    
54   C  C     . ASN A 13  ? 0.9386 0.9946 0.7683 0.0407  0.0181  -0.1704 1230 ASN A C     
55   O  O     . ASN A 13  ? 0.9019 0.9435 0.7353 0.0388  0.0106  -0.1681 1230 ASN A O     
56   C  CB    . ASN A 13  ? 1.0464 1.1178 0.8438 0.0397  0.0163  -0.1783 1230 ASN A CB    
57   C  CG    . ASN A 13  ? 1.1369 1.2102 0.9243 0.0324  0.0178  -0.1619 1230 ASN A CG    
58   O  OD1   . ASN A 13  ? 1.1447 1.2179 0.9379 0.0288  0.0225  -0.1503 1230 ASN A OD1   
59   N  ND2   . ASN A 13  ? 1.2464 1.3212 1.0189 0.0304  0.0135  -0.1610 1230 ASN A ND2   
60   N  N     . LEU A 14  ? 0.8184 0.8779 0.6587 0.0416  0.0236  -0.1665 1231 LEU A N     
61   C  CA    . LEU A 14  ? 0.6899 0.7358 0.5451 0.0401  0.0210  -0.1580 1231 LEU A CA    
62   C  C     . LEU A 14  ? 0.7380 0.7779 0.5894 0.0325  0.0195  -0.1428 1231 LEU A C     
63   O  O     . LEU A 14  ? 0.7265 0.7513 0.5861 0.0311  0.0135  -0.1385 1231 LEU A O     
64   C  CB    . LEU A 14  ? 0.5453 0.5988 0.4115 0.0429  0.0272  -0.1576 1231 LEU A CB    
65   C  CG    . LEU A 14  ? 0.6450 0.6839 0.5266 0.0429  0.0235  -0.1511 1231 LEU A CG    
66   C  CD1   . LEU A 14  ? 0.5721 0.5977 0.4618 0.0482  0.0168  -0.1610 1231 LEU A CD1   
67   C  CD2   . LEU A 14  ? 0.6863 0.7330 0.5782 0.0447  0.0290  -0.1485 1231 LEU A CD2   
68   N  N     . PRO A 15  ? 0.7789 0.8293 0.6189 0.0276  0.0246  -0.1342 1232 PRO A N     
69   C  CA    . PRO A 15  ? 0.7373 0.7806 0.5756 0.0210  0.0231  -0.1196 1232 PRO A CA    
70   C  C     . PRO A 15  ? 0.7915 0.8241 0.6248 0.0192  0.0151  -0.1184 1232 PRO A C     
71   O  O     . PRO A 15  ? 0.7506 0.7712 0.5900 0.0163  0.0109  -0.1102 1232 PRO A O     
72   C  CB    . PRO A 15  ? 0.6619 0.7196 0.4875 0.0168  0.0305  -0.1129 1232 PRO A CB    
73   C  CG    . PRO A 15  ? 0.5539 0.6252 0.3698 0.0207  0.0337  -0.1241 1232 PRO A CG    
74   C  CD    . PRO A 15  ? 0.7550 0.8241 0.5832 0.0276  0.0322  -0.1368 1232 PRO A CD    
75   N  N     . ASP A 16  ? 0.9442 0.9811 0.7676 0.0217  0.0126  -0.1279 1233 ASP A N     
76   C  CA    . ASP A 16  ? 1.0964 1.1265 0.9132 0.0200  0.0051  -0.1278 1233 ASP A CA    
77   C  C     . ASP A 16  ? 1.1270 1.1430 0.9574 0.0226  -0.0023 -0.1348 1233 ASP A C     
78   O  O     . ASP A 16  ? 1.2798 1.2856 1.1132 0.0198  -0.0085 -0.1301 1233 ASP A O     
79   C  CB    . ASP A 16  ? 1.2775 1.3199 1.0771 0.0217  0.0056  -0.1358 1233 ASP A CB    
80   C  CG    . ASP A 16  ? 1.4488 1.4884 1.2378 0.0195  -0.0016 -0.1342 1233 ASP A CG    
81   O  OD1   . ASP A 16  ? 1.5651 1.6162 1.3366 0.0186  0.0007  -0.1328 1233 ASP A OD1   
82   O  OD2   . ASP A 16  ? 1.4778 1.5050 1.2759 0.0194  -0.0093 -0.1361 1233 ASP A OD2   
83   N  N     . TRP A 17  ? 0.8750 0.8897 0.7156 0.0277  -0.0010 -0.1445 1234 TRP A N     
84   C  CA    . TRP A 17  ? 0.7915 0.7910 0.6479 0.0297  -0.0066 -0.1483 1234 TRP A CA    
85   C  C     . TRP A 17  ? 0.8109 0.8004 0.6783 0.0263  -0.0069 -0.1354 1234 TRP A C     
86   O  O     . TRP A 17  ? 0.7518 0.7289 0.6271 0.0246  -0.0129 -0.1329 1234 TRP A O     
87   C  CB    . TRP A 17  ? 0.8534 0.8542 0.7181 0.0364  -0.0044 -0.1602 1234 TRP A CB    
88   C  CG    . TRP A 17  ? 0.8139 0.7984 0.6960 0.0385  -0.0089 -0.1614 1234 TRP A CG    
89   C  CD1   . TRP A 17  ? 0.8307 0.8030 0.7194 0.0397  -0.0161 -0.1691 1234 TRP A CD1   
90   C  CD2   . TRP A 17  ? 0.7318 0.7105 0.6267 0.0392  -0.0067 -0.1540 1234 TRP A CD2   
91   N  NE1   . TRP A 17  ? 0.8570 0.8157 0.7617 0.0410  -0.0180 -0.1662 1234 TRP A NE1   
92   C  CE2   . TRP A 17  ? 0.7928 0.7555 0.7010 0.0410  -0.0124 -0.1569 1234 TRP A CE2   
93   C  CE3   . TRP A 17  ? 0.6966 0.6823 0.5931 0.0383  -0.0005 -0.1453 1234 TRP A CE3   
94   C  CZ2   . TRP A 17  ? 0.8285 0.7824 0.7501 0.0424  -0.0120 -0.1508 1234 TRP A CZ2   
95   C  CZ3   . TRP A 17  ? 0.7762 0.7538 0.6861 0.0398  -0.0006 -0.1403 1234 TRP A CZ3   
96   C  CH2   . TRP A 17  ? 0.8049 0.7668 0.7267 0.0421  -0.0062 -0.1428 1234 TRP A CH2   
97   N  N     . TYR A 18  ? 0.8321 0.8272 0.7014 0.0256  -0.0005 -0.1280 1235 TYR A N     
98   C  CA    . TYR A 18  ? 0.7570 0.7442 0.6356 0.0226  -0.0004 -0.1161 1235 TYR A CA    
99   C  C     . TYR A 18  ? 0.6903 0.6723 0.5639 0.0171  -0.0040 -0.1064 1235 TYR A C     
100  O  O     . TYR A 18  ? 0.6263 0.5971 0.5090 0.0155  -0.0078 -0.1009 1235 TYR A O     
101  C  CB    . TYR A 18  ? 0.7000 0.6968 0.5787 0.0219  0.0071  -0.1105 1235 TYR A CB    
102  C  CG    . TYR A 18  ? 0.6043 0.5944 0.4932 0.0200  0.0077  -0.1004 1235 TYR A CG    
103  C  CD1   . TYR A 18  ? 0.6487 0.6321 0.5512 0.0239  0.0067  -0.1024 1235 TYR A CD1   
104  C  CD2   . TYR A 18  ? 0.4803 0.4710 0.3648 0.0146  0.0093  -0.0890 1235 TYR A CD2   
105  C  CE1   . TYR A 18  ? 0.5580 0.5366 0.4686 0.0223  0.0074  -0.0930 1235 TYR A CE1   
106  C  CE2   . TYR A 18  ? 0.4883 0.4737 0.3813 0.0129  0.0099  -0.0806 1235 TYR A CE2   
107  C  CZ    . TYR A 18  ? 0.4925 0.4724 0.3980 0.0167  0.0090  -0.0826 1235 TYR A CZ    
108  O  OH    . TYR A 18  ? 0.5258 0.5016 0.4379 0.0150  0.0096  -0.0741 1235 TYR A OH    
109  N  N     . SER A 19  ? 0.6582 0.6487 0.5173 0.0144  -0.0028 -0.1040 1236 SER A N     
110  C  CA    . SER A 19  ? 0.7040 0.6901 0.5581 0.0099  -0.0067 -0.0951 1236 SER A CA    
111  C  C     . SER A 19  ? 0.9096 0.8864 0.7687 0.0104  -0.0149 -0.1001 1236 SER A C     
112  O  O     . SER A 19  ? 0.8636 0.8314 0.7297 0.0079  -0.0186 -0.0932 1236 SER A O     
113  C  CB    . SER A 19  ? 0.6743 0.6713 0.5111 0.0078  -0.0045 -0.0922 1236 SER A CB    
114  O  OG    . SER A 19  ? 0.7098 0.7026 0.5422 0.0039  -0.0080 -0.0824 1236 SER A OG    
115  N  N     . GLN A 20  ? 1.0752 1.0543 0.9315 0.0136  -0.0176 -0.1127 1237 GLN A N     
116  C  CA    . GLN A 20  ? 1.0509 1.0213 0.9130 0.0137  -0.0256 -0.1187 1237 GLN A CA    
117  C  C     . GLN A 20  ? 0.8697 0.8267 0.7498 0.0138  -0.0278 -0.1170 1237 GLN A C     
118  O  O     . GLN A 20  ? 0.7455 0.6946 0.6322 0.0110  -0.0328 -0.1127 1237 GLN A O     
119  C  CB    . GLN A 20  ? 1.1045 1.0797 0.9609 0.0174  -0.0279 -0.1337 1237 GLN A CB    
120  C  CG    . GLN A 20  ? 1.1432 1.1318 0.9805 0.0169  -0.0265 -0.1345 1237 GLN A CG    
121  C  CD    . GLN A 20  ? 1.3165 1.3062 1.1473 0.0174  -0.0339 -0.1440 1237 GLN A CD    
122  O  OE1   . GLN A 20  ? 1.3034 1.2843 1.1447 0.0183  -0.0399 -0.1524 1237 GLN A OE1   
123  N  NE2   . GLN A 20  ? 1.5026 1.5033 1.3158 0.0166  -0.0339 -0.1426 1237 GLN A NE2   
124  N  N     . VAL A 21  ? 0.7588 0.7135 0.6472 0.0172  -0.0240 -0.1197 1238 VAL A N     
125  C  CA    . VAL A 21  ? 0.7071 0.6487 0.6116 0.0175  -0.0263 -0.1174 1238 VAL A CA    
126  C  C     . VAL A 21  ? 0.6605 0.5985 0.5686 0.0135  -0.0255 -0.1034 1238 VAL A C     
127  O  O     . VAL A 21  ? 0.5575 0.4872 0.4724 0.0108  -0.0300 -0.0997 1238 VAL A O     
128  C  CB    . VAL A 21  ? 0.7160 0.6557 0.6289 0.0227  -0.0229 -0.1226 1238 VAL A CB    
129  C  CG1   . VAL A 21  ? 0.7537 0.7047 0.6606 0.0240  -0.0157 -0.1193 1238 VAL A CG1   
130  C  CG2   . VAL A 21  ? 0.5010 0.4275 0.4291 0.0226  -0.0246 -0.1167 1238 VAL A CG2   
131  N  N     . ILE A 22  ? 0.5807 0.5256 0.4834 0.0126  -0.0198 -0.0957 1239 ILE A N     
132  C  CA    . ILE A 22  ? 0.5663 0.5072 0.4730 0.0094  -0.0189 -0.0833 1239 ILE A CA    
133  C  C     . ILE A 22  ? 0.6024 0.5419 0.5049 0.0053  -0.0230 -0.0776 1239 ILE A C     
134  O  O     . ILE A 22  ? 0.4809 0.4146 0.3897 0.0030  -0.0239 -0.0691 1239 ILE A O     
135  C  CB    . ILE A 22  ? 0.6016 0.5503 0.5033 0.0088  -0.0123 -0.0770 1239 ILE A CB    
136  C  CG1   . ILE A 22  ? 0.5183 0.4768 0.4052 0.0065  -0.0107 -0.0757 1239 ILE A CG1   
137  C  CG2   . ILE A 22  ? 0.5174 0.4694 0.4240 0.0130  -0.0082 -0.0822 1239 ILE A CG2   
138  C  CD1   . ILE A 22  ? 0.5125 0.4778 0.3947 0.0046  -0.0045 -0.0685 1239 ILE A CD1   
139  N  N     . THR A 23  ? 0.5461 0.4911 0.4383 0.0046  -0.0258 -0.0822 1240 THR A N     
140  C  CA    . THR A 23  ? 0.5145 0.4581 0.4045 0.0014  -0.0306 -0.0769 1240 THR A CA    
141  C  C     . THR A 23  ? 0.7059 0.6423 0.6054 0.0011  -0.0373 -0.0828 1240 THR A C     
142  O  O     . THR A 23  ? 0.9678 0.8979 0.8767 -0.0011 -0.0399 -0.0770 1240 THR A O     
143  C  CB    . THR A 23  ? 0.4945 0.4475 0.3684 0.0005  -0.0312 -0.0769 1240 THR A CB    
144  O  OG1   . THR A 23  ? 0.5901 0.5465 0.4593 0.0025  -0.0347 -0.0888 1240 THR A OG1   
145  C  CG2   . THR A 23  ? 0.5498 0.5107 0.4136 0.0004  -0.0242 -0.0721 1240 THR A CG2   
146  N  N     . LYS A 24  ? 0.5576 0.4951 0.4557 0.0033  -0.0400 -0.0948 1241 LYS A N     
147  C  CA    . LYS A 24  ? 0.5245 0.4550 0.4324 0.0024  -0.0468 -0.1012 1241 LYS A CA    
148  C  C     . LYS A 24  ? 0.6752 0.5942 0.5997 0.0024  -0.0465 -0.0993 1241 LYS A C     
149  O  O     . LYS A 24  ? 0.7405 0.6526 0.6755 0.0002  -0.0516 -0.1008 1241 LYS A O     
150  C  CB    . LYS A 24  ? 0.5479 0.4815 0.4506 0.0048  -0.0500 -0.1156 1241 LYS A CB    
151  C  CG    . LYS A 24  ? 0.6721 0.6180 0.5566 0.0053  -0.0503 -0.1183 1241 LYS A CG    
152  C  CD    . LYS A 24  ? 0.7771 0.7260 0.6570 0.0076  -0.0549 -0.1335 1241 LYS A CD    
153  C  CE    . LYS A 24  ? 0.9618 0.9244 0.8216 0.0091  -0.0530 -0.1359 1241 LYS A CE    
154  N  NZ    . LYS A 24  ? 1.0077 0.9752 0.8602 0.0110  -0.0586 -0.1503 1241 LYS A NZ    
155  N  N     . GLY A 25  ? 0.4914 0.4086 0.4187 0.0045  -0.0407 -0.0953 1242 GLY A N     
156  C  CA    . GLY A 25  ? 0.4847 0.3917 0.4262 0.0047  -0.0400 -0.0912 1242 GLY A CA    
157  C  C     . GLY A 25  ? 0.8478 0.7531 0.7932 0.0016  -0.0388 -0.0787 1242 GLY A C     
158  O  O     . GLY A 25  ? 0.8847 0.7821 0.8410 0.0015  -0.0380 -0.0739 1242 GLY A O     
159  N  N     . GLU A 26  ? 0.8715 0.7839 0.8075 -0.0005 -0.0385 -0.0732 1243 GLU A N     
160  C  CA    . GLU A 26  ? 0.7380 0.6496 0.6768 -0.0034 -0.0384 -0.0623 1243 GLU A CA    
161  C  C     . GLU A 26  ? 0.6509 0.5610 0.5922 -0.0025 -0.0327 -0.0541 1243 GLU A C     
162  O  O     . GLU A 26  ? 0.6232 0.5285 0.5728 -0.0038 -0.0324 -0.0472 1243 GLU A O     
163  C  CB    . GLU A 26  ? 0.5569 0.4622 0.5079 -0.0060 -0.0433 -0.0620 1243 GLU A CB    
164  C  CG    . GLU A 26  ? 0.4940 0.4024 0.4421 -0.0074 -0.0495 -0.0697 1243 GLU A CG    
165  C  CD    . GLU A 26  ? 0.7451 0.6495 0.7054 -0.0108 -0.0544 -0.0681 1243 GLU A CD    
166  O  OE1   . GLU A 26  ? 0.9948 0.9011 0.9557 -0.0122 -0.0604 -0.0753 1243 GLU A OE1   
167  O  OE2   . GLU A 26  ? 0.6934 0.5936 0.6630 -0.0121 -0.0522 -0.0599 1243 GLU A OE2   
168  N  N     . MET A 27  ? 0.6102 0.5253 0.5440 -0.0004 -0.0282 -0.0550 1244 MET A N     
169  C  CA    . MET A 27  ? 0.7755 0.6907 0.7109 0.0001  -0.0233 -0.0477 1244 MET A CA    
170  C  C     . MET A 27  ? 0.8085 0.7306 0.7336 -0.0014 -0.0201 -0.0422 1244 MET A C     
171  O  O     . MET A 27  ? 0.6446 0.5658 0.5715 -0.0023 -0.0177 -0.0346 1244 MET A O     
172  C  CB    . MET A 27  ? 0.8724 0.7872 0.8109 0.0039  -0.0203 -0.0525 1244 MET A CB    
173  C  CG    . MET A 27  ? 0.7620 0.6689 0.7101 0.0058  -0.0234 -0.0585 1244 MET A CG    
174  S  SD    . MET A 27  ? 0.7424 0.6516 0.6911 0.0111  -0.0202 -0.0657 1244 MET A SD    
175  C  CE    . MET A 27  ? 0.4960 0.4015 0.4524 0.0126  -0.0170 -0.0570 1244 MET A CE    
176  N  N     . ILE A 28  ? 0.8645 0.7932 0.7789 -0.0018 -0.0203 -0.0457 1245 ILE A N     
177  C  CA    . ILE A 28  ? 0.6989 0.6340 0.6029 -0.0035 -0.0170 -0.0406 1245 ILE A CA    
178  C  C     . ILE A 28  ? 0.7019 0.6377 0.5997 -0.0056 -0.0211 -0.0375 1245 ILE A C     
179  O  O     . ILE A 28  ? 0.7219 0.6567 0.6208 -0.0055 -0.0262 -0.0424 1245 ILE A O     
180  C  CB    . ILE A 28  ? 0.6834 0.6267 0.5794 -0.0020 -0.0132 -0.0466 1245 ILE A CB    
181  C  CG1   . ILE A 28  ? 0.7135 0.6574 0.6161 0.0001  -0.0087 -0.0476 1245 ILE A CG1   
182  C  CG2   . ILE A 28  ? 0.5459 0.4965 0.4292 -0.0043 -0.0104 -0.0423 1245 ILE A CG2   
183  C  CD1   . ILE A 28  ? 0.7803 0.7206 0.6881 -0.0013 -0.0069 -0.0390 1245 ILE A CD1   
184  N  N     . GLU A 29  ? 0.7049 0.6419 0.5975 -0.0076 -0.0193 -0.0293 1246 GLU A N     
185  C  CA    . GLU A 29  ? 0.7217 0.6617 0.6044 -0.0090 -0.0222 -0.0262 1246 GLU A CA    
186  C  C     . GLU A 29  ? 0.7183 0.6630 0.5906 -0.0104 -0.0173 -0.0212 1246 GLU A C     
187  O  O     . GLU A 29  ? 0.6099 0.5522 0.4851 -0.0116 -0.0137 -0.0149 1246 GLU A O     
188  C  CB    . GLU A 29  ? 0.7250 0.6601 0.6136 -0.0099 -0.0263 -0.0202 1246 GLU A CB    
189  C  CG    . GLU A 29  ? 0.7123 0.6504 0.5932 -0.0103 -0.0312 -0.0194 1246 GLU A CG    
190  C  CD    . GLU A 29  ? 0.6827 0.6247 0.5601 -0.0093 -0.0349 -0.0290 1246 GLU A CD    
191  O  OE1   . GLU A 29  ? 0.7185 0.6576 0.6054 -0.0092 -0.0395 -0.0334 1246 GLU A OE1   
192  O  OE2   . GLU A 29  ? 0.6120 0.5602 0.4773 -0.0089 -0.0331 -0.0321 1246 GLU A OE2   
193  N  N     . TYR A 30  ? 0.7161 0.6677 0.5763 -0.0105 -0.0170 -0.0238 1247 TYR A N     
194  C  CA    . TYR A 30  ? 0.6955 0.6518 0.5461 -0.0124 -0.0117 -0.0186 1247 TYR A CA    
195  C  C     . TYR A 30  ? 0.6739 0.6255 0.5226 -0.0146 -0.0124 -0.0079 1247 TYR A C     
196  O  O     . TYR A 30  ? 0.4664 0.4131 0.3190 -0.0140 -0.0175 -0.0052 1247 TYR A O     
197  C  CB    . TYR A 30  ? 0.7281 0.6932 0.5649 -0.0121 -0.0111 -0.0228 1247 TYR A CB    
198  C  CG    . TYR A 30  ? 0.6731 0.6437 0.5115 -0.0098 -0.0086 -0.0332 1247 TYR A CG    
199  C  CD1   . TYR A 30  ? 0.6148 0.5891 0.4565 -0.0100 -0.0021 -0.0340 1247 TYR A CD1   
200  C  CD2   . TYR A 30  ? 0.7891 0.7614 0.6266 -0.0072 -0.0130 -0.0429 1247 TYR A CD2   
201  C  CE1   . TYR A 30  ? 0.7647 0.7446 0.6085 -0.0071 0.0002  -0.0440 1247 TYR A CE1   
202  C  CE2   . TYR A 30  ? 0.8147 0.7914 0.6541 -0.0044 -0.0108 -0.0533 1247 TYR A CE2   
203  C  CZ    . TYR A 30  ? 0.7694 0.7499 0.6119 -0.0041 -0.0041 -0.0536 1247 TYR A CZ    
204  O  OH    . TYR A 30  ? 0.7069 0.6921 0.5520 -0.0007 -0.0020 -0.0639 1247 TYR A OH    
205  N  N     . TYR A 31  ? 0.7041 0.6570 0.5486 -0.0170 -0.0071 -0.0020 1248 TYR A N     
206  C  CA    . TYR A 31  ? 0.5621 0.5084 0.4080 -0.0188 -0.0071 0.0076  1248 TYR A CA    
207  C  C     . TYR A 31  ? 0.7735 0.7226 0.6078 -0.0217 -0.0035 0.0144  1248 TYR A C     
208  O  O     . TYR A 31  ? 1.0145 0.9711 0.8426 -0.0230 0.0013  0.0121  1248 TYR A O     
209  C  CB    . TYR A 31  ? 0.5128 0.4549 0.3708 -0.0191 -0.0042 0.0079  1248 TYR A CB    
210  C  CG    . TYR A 31  ? 0.5461 0.4806 0.4083 -0.0200 -0.0052 0.0155  1248 TYR A CG    
211  C  CD1   . TYR A 31  ? 0.5418 0.4715 0.4072 -0.0182 -0.0106 0.0176  1248 TYR A CD1   
212  C  CD2   . TYR A 31  ? 0.6845 0.6169 0.5484 -0.0225 -0.0008 0.0200  1248 TYR A CD2   
213  C  CE1   . TYR A 31  ? 0.6174 0.5404 0.4870 -0.0184 -0.0114 0.0240  1248 TYR A CE1   
214  C  CE2   . TYR A 31  ? 0.6601 0.5850 0.5281 -0.0229 -0.0018 0.0261  1248 TYR A CE2   
215  C  CZ    . TYR A 31  ? 0.5999 0.5201 0.4704 -0.0206 -0.0070 0.0280  1248 TYR A CZ    
216  O  OH    . TYR A 31  ? 0.6839 0.5971 0.5588 -0.0203 -0.0081 0.0333  1248 TYR A OH    
217  N  N     . ASP A 32  ? 0.7642 0.7072 0.5959 -0.0227 -0.0056 0.0231  1249 ASP A N     
218  C  CA    . ASP A 32  ? 0.6987 0.6429 0.5182 -0.0254 -0.0031 0.0307  1249 ASP A CA    
219  C  C     . ASP A 32  ? 0.6209 0.5628 0.4431 -0.0293 0.0032  0.0358  1249 ASP A C     
220  O  O     . ASP A 32  ? 0.6657 0.6074 0.4790 -0.0323 0.0059  0.0432  1249 ASP A O     
221  C  CB    . ASP A 32  ? 0.7469 0.6856 0.5613 -0.0242 -0.0088 0.0380  1249 ASP A CB    
222  C  CG    . ASP A 32  ? 0.8197 0.7478 0.6432 -0.0243 -0.0100 0.0443  1249 ASP A CG    
223  O  OD1   . ASP A 32  ? 0.8449 0.7701 0.6807 -0.0239 -0.0088 0.0408  1249 ASP A OD1   
224  O  OD2   . ASP A 32  ? 0.6545 0.5775 0.4725 -0.0243 -0.0123 0.0527  1249 ASP A OD2   
225  N  N     . VAL A 33  ? 0.5720 0.5126 0.4061 -0.0295 0.0057  0.0320  1250 VAL A N     
226  C  CA    . VAL A 33  ? 0.6195 0.5607 0.4573 -0.0334 0.0118  0.0342  1250 VAL A CA    
227  C  C     . VAL A 33  ? 0.7600 0.7116 0.5999 -0.0333 0.0161  0.0261  1250 VAL A C     
228  O  O     . VAL A 33  ? 0.7265 0.6787 0.5756 -0.0304 0.0150  0.0192  1250 VAL A O     
229  C  CB    . VAL A 33  ? 0.5496 0.4822 0.3992 -0.0333 0.0109  0.0358  1250 VAL A CB    
230  C  CG1   . VAL A 33  ? 0.6195 0.5547 0.4751 -0.0367 0.0166  0.0350  1250 VAL A CG1   
231  C  CG2   . VAL A 33  ? 0.6681 0.5909 0.5155 -0.0337 0.0078  0.0441  1250 VAL A CG2   
232  N  N     . SER A 34  ? 0.7637 0.7235 0.5955 -0.0362 0.0212  0.0271  1251 SER A N     
233  C  CA    . SER A 34  ? 0.7268 0.6984 0.5585 -0.0354 0.0253  0.0191  1251 SER A CA    
234  C  C     . SER A 34  ? 0.6441 0.6168 0.4897 -0.0343 0.0268  0.0132  1251 SER A C     
235  O  O     . SER A 34  ? 0.6711 0.6413 0.5235 -0.0373 0.0293  0.0166  1251 SER A O     
236  C  CB    . SER A 34  ? 0.7466 0.7269 0.5696 -0.0399 0.0319  0.0229  1251 SER A CB    
237  O  OG    . SER A 34  ? 0.9313 0.9150 0.7632 -0.0434 0.0374  0.0230  1251 SER A OG    
238  N  N     . GLY A 35  ? 0.6601 0.6369 0.5099 -0.0298 0.0253  0.0040  1252 GLY A N     
239  C  CA    . GLY A 35  ? 0.5729 0.5520 0.4348 -0.0279 0.0266  -0.0018 1252 GLY A CA    
240  C  C     . GLY A 35  ? 0.6262 0.5955 0.4977 -0.0253 0.0219  -0.0020 1252 GLY A C     
241  O  O     . GLY A 35  ? 0.8767 0.8473 0.7580 -0.0234 0.0227  -0.0059 1252 GLY A O     
242  N  N     . CYS A 36  ? 0.5106 0.4711 0.3800 -0.0247 0.0171  0.0021  1253 CYS A N     
243  C  CA    . CYS A 36  ? 0.4545 0.4068 0.3323 -0.0219 0.0126  0.0016  1253 CYS A CA    
244  C  C     . CYS A 36  ? 0.5885 0.5392 0.4637 -0.0190 0.0078  -0.0021 1253 CYS A C     
245  O  O     . CYS A 36  ? 0.4463 0.4000 0.3117 -0.0195 0.0069  -0.0020 1253 CYS A O     
246  C  CB    . CYS A 36  ? 0.4670 0.4108 0.3462 -0.0238 0.0111  0.0094  1253 CYS A CB    
247  S  SG    . CYS A 36  ? 0.6931 0.6374 0.5720 -0.0291 0.0163  0.0152  1253 CYS A SG    
248  N  N     . TYR A 37  ? 0.4293 0.3757 0.3134 -0.0159 0.0047  -0.0055 1254 TYR A N     
249  C  CA    . TYR A 37  ? 0.4350 0.3803 0.3195 -0.0133 0.0004  -0.0109 1254 TYR A CA    
250  C  C     . TYR A 37  ? 0.5116 0.4490 0.4054 -0.0120 -0.0034 -0.0090 1254 TYR A C     
251  O  O     . TYR A 37  ? 0.5822 0.5171 0.4838 -0.0113 -0.0019 -0.0077 1254 TYR A O     
252  C  CB    . TYR A 37  ? 0.5027 0.4534 0.3893 -0.0106 0.0019  -0.0198 1254 TYR A CB    
253  C  CG    . TYR A 37  ? 0.4404 0.4009 0.3194 -0.0117 0.0068  -0.0221 1254 TYR A CG    
254  C  CD1   . TYR A 37  ? 0.4513 0.4172 0.3199 -0.0117 0.0064  -0.0252 1254 TYR A CD1   
255  C  CD2   . TYR A 37  ? 0.4366 0.4019 0.3187 -0.0128 0.0120  -0.0211 1254 TYR A CD2   
256  C  CE1   . TYR A 37  ? 0.4585 0.4344 0.3195 -0.0128 0.0115  -0.0269 1254 TYR A CE1   
257  C  CE2   . TYR A 37  ? 0.4431 0.4186 0.3190 -0.0143 0.0170  -0.0229 1254 TYR A CE2   
258  C  CZ    . TYR A 37  ? 0.4860 0.4668 0.3512 -0.0142 0.0170  -0.0256 1254 TYR A CZ    
259  O  OH    . TYR A 37  ? 0.6237 0.6157 0.4821 -0.0157 0.0226  -0.0272 1254 TYR A OH    
260  N  N     . ILE A 38  ? 0.5996 0.5341 0.4925 -0.0117 -0.0082 -0.0086 1255 ILE A N     
261  C  CA    . ILE A 38  ? 0.6735 0.6018 0.5757 -0.0107 -0.0115 -0.0067 1255 ILE A CA    
262  C  C     . ILE A 38  ? 0.6390 0.5657 0.5498 -0.0085 -0.0121 -0.0127 1255 ILE A C     
263  O  O     . ILE A 38  ? 0.9194 0.8476 0.8291 -0.0074 -0.0141 -0.0193 1255 ILE A O     
264  C  CB    . ILE A 38  ? 0.5995 0.5265 0.4994 -0.0112 -0.0167 -0.0050 1255 ILE A CB    
265  C  CG1   . ILE A 38  ? 0.7363 0.6645 0.6267 -0.0129 -0.0162 0.0012  1255 ILE A CG1   
266  C  CG2   . ILE A 38  ? 0.6128 0.5347 0.5228 -0.0107 -0.0191 -0.0019 1255 ILE A CG2   
267  C  CD1   . ILE A 38  ? 0.7313 0.6602 0.6170 -0.0127 -0.0216 0.0023  1255 ILE A CD1   
268  N  N     . LEU A 39  ? 0.4460 0.3691 0.3650 -0.0076 -0.0106 -0.0104 1256 LEU A N     
269  C  CA    . LEU A 39  ? 0.4080 0.3279 0.3358 -0.0053 -0.0113 -0.0142 1256 LEU A CA    
270  C  C     . LEU A 39  ? 0.5983 0.5133 0.5328 -0.0057 -0.0154 -0.0130 1256 LEU A C     
271  O  O     . LEU A 39  ? 0.4373 0.3495 0.3763 -0.0063 -0.0154 -0.0072 1256 LEU A O     
272  C  CB    . LEU A 39  ? 0.4009 0.3197 0.3340 -0.0040 -0.0081 -0.0115 1256 LEU A CB    
273  C  CG    . LEU A 39  ? 0.4464 0.3708 0.3751 -0.0039 -0.0040 -0.0124 1256 LEU A CG    
274  C  CD1   . LEU A 39  ? 0.3948 0.3184 0.3303 -0.0016 -0.0022 -0.0118 1256 LEU A CD1   
275  C  CD2   . LEU A 39  ? 0.4077 0.3372 0.3312 -0.0034 -0.0036 -0.0191 1256 LEU A CD2   
276  N  N     . ARG A 40  ? 0.5666 0.4807 0.5026 -0.0054 -0.0188 -0.0189 1257 ARG A N     
277  C  CA    . ARG A 40  ? 0.5437 0.4538 0.4876 -0.0064 -0.0229 -0.0186 1257 ARG A CA    
278  C  C     . ARG A 40  ? 0.6009 0.5053 0.5556 -0.0053 -0.0219 -0.0171 1257 ARG A C     
279  O  O     . ARG A 40  ? 0.6066 0.5102 0.5621 -0.0033 -0.0186 -0.0171 1257 ARG A O     
280  C  CB    . ARG A 40  ? 0.4866 0.3978 0.4286 -0.0068 -0.0272 -0.0261 1257 ARG A CB    
281  C  CG    . ARG A 40  ? 0.4882 0.4059 0.4173 -0.0072 -0.0274 -0.0275 1257 ARG A CG    
282  C  CD    . ARG A 40  ? 0.4486 0.3686 0.3745 -0.0076 -0.0325 -0.0345 1257 ARG A CD    
283  N  NE    . ARG A 40  ? 0.4730 0.3905 0.4070 -0.0093 -0.0376 -0.0339 1257 ARG A NE    
284  C  CZ    . ARG A 40  ? 0.5012 0.4198 0.4357 -0.0099 -0.0430 -0.0408 1257 ARG A CZ    
285  N  NH1   . ARG A 40  ? 0.5477 0.4696 0.4741 -0.0086 -0.0435 -0.0488 1257 ARG A NH1   
286  N  NH2   . ARG A 40  ? 0.5694 0.4867 0.5128 -0.0119 -0.0477 -0.0402 1257 ARG A NH2   
287  N  N     . HIS A 41  ? 0.6273 0.5283 0.5905 -0.0068 -0.0247 -0.0155 1258 HIS A N     
288  C  CA    . HIS A 41  ? 0.7030 0.5985 0.6762 -0.0064 -0.0235 -0.0122 1258 HIS A CA    
289  C  C     . HIS A 41  ? 0.7930 0.6842 0.7691 -0.0040 -0.0228 -0.0170 1258 HIS A C     
290  O  O     . HIS A 41  ? 0.8108 0.6992 0.7905 -0.0020 -0.0201 -0.0136 1258 HIS A O     
291  C  CB    . HIS A 41  ? 0.6708 0.5643 0.6531 -0.0091 -0.0268 -0.0107 1258 HIS A CB    
292  C  CG    . HIS A 41  ? 0.9380 0.8249 0.9313 -0.0093 -0.0267 -0.0100 1258 HIS A CG    
293  N  ND1   . HIS A 41  ? 1.0695 0.9538 1.0665 -0.0080 -0.0230 -0.0037 1258 HIS A ND1   
294  C  CD2   . HIS A 41  ? 1.0185 0.9003 1.0196 -0.0107 -0.0300 -0.0147 1258 HIS A CD2   
295  C  CE1   . HIS A 41  ? 1.0894 0.9671 1.0960 -0.0087 -0.0238 -0.0036 1258 HIS A CE1   
296  N  NE2   . HIS A 41  ? 1.0506 0.9262 1.0604 -0.0105 -0.0280 -0.0104 1258 HIS A NE2   
297  N  N     . TRP A 42  ? 0.6826 0.5736 0.6568 -0.0036 -0.0254 -0.0253 1259 TRP A N     
298  C  CA    . TRP A 42  ? 0.6835 0.5698 0.6614 -0.0008 -0.0254 -0.0311 1259 TRP A CA    
299  C  C     . TRP A 42  ? 0.7101 0.5992 0.6837 0.0028  -0.0212 -0.0306 1259 TRP A C     
300  O  O     . TRP A 42  ? 0.9277 0.8124 0.9068 0.0052  -0.0196 -0.0280 1259 TRP A O     
301  C  CB    . TRP A 42  ? 0.6864 0.5738 0.6613 -0.0010 -0.0290 -0.0410 1259 TRP A CB    
302  C  CG    . TRP A 42  ? 0.7646 0.6445 0.7470 0.0007  -0.0314 -0.0484 1259 TRP A CG    
303  C  CD1   . TRP A 42  ? 0.8577 0.7382 0.8368 0.0041  -0.0314 -0.0574 1259 TRP A CD1   
304  C  CD2   . TRP A 42  ? 0.7165 0.5870 0.7113 -0.0010 -0.0342 -0.0478 1259 TRP A CD2   
305  N  NE1   . TRP A 42  ? 0.7650 0.6361 0.7537 0.0051  -0.0343 -0.0627 1259 TRP A NE1   
306  C  CE2   . TRP A 42  ? 0.7513 0.6157 0.7498 0.0016  -0.0360 -0.0566 1259 TRP A CE2   
307  C  CE3   . TRP A 42  ? 0.7650 0.6318 0.7686 -0.0046 -0.0349 -0.0405 1259 TRP A CE3   
308  C  CZ2   . TRP A 42  ? 0.7916 0.6451 0.8025 0.0004  -0.0389 -0.0581 1259 TRP A CZ2   
309  C  CZ3   . TRP A 42  ? 0.8231 0.6801 0.8390 -0.0061 -0.0374 -0.0416 1259 TRP A CZ3   
310  C  CH2   . TRP A 42  ? 0.7493 0.5991 0.7688 -0.0038 -0.0395 -0.0502 1259 TRP A CH2   
311  N  N     . SER A 43  ? 0.6248 0.5217 0.5885 0.0030  -0.0194 -0.0326 1260 SER A N     
312  C  CA    . SER A 43  ? 0.4941 0.3951 0.4547 0.0059  -0.0154 -0.0326 1260 SER A CA    
313  C  C     . SER A 43  ? 0.4095 0.3096 0.3728 0.0060  -0.0130 -0.0242 1260 SER A C     
314  O  O     . SER A 43  ? 0.4142 0.3138 0.3806 0.0091  -0.0112 -0.0233 1260 SER A O     
315  C  CB    . SER A 43  ? 0.4182 0.3283 0.3681 0.0051  -0.0133 -0.0348 1260 SER A CB    
316  O  OG    . SER A 43  ? 0.4739 0.3859 0.4189 0.0016  -0.0141 -0.0301 1260 SER A OG    
317  N  N     . PHE A 44  ? 0.4048 0.3051 0.3672 0.0031  -0.0133 -0.0182 1261 PHE A N     
318  C  CA    . PHE A 44  ? 0.6184 0.5187 0.5824 0.0034  -0.0108 -0.0111 1261 PHE A CA    
319  C  C     . PHE A 44  ? 0.5643 0.4583 0.5368 0.0054  -0.0111 -0.0084 1261 PHE A C     
320  O  O     . PHE A 44  ? 0.4643 0.3589 0.4375 0.0075  -0.0089 -0.0046 1261 PHE A O     
321  C  CB    . PHE A 44  ? 0.3936 0.2952 0.3554 0.0005  -0.0111 -0.0057 1261 PHE A CB    
322  C  CG    . PHE A 44  ? 0.4169 0.3208 0.3770 0.0010  -0.0081 -0.0004 1261 PHE A CG    
323  C  CD1   . PHE A 44  ? 0.4683 0.3772 0.4222 0.0011  -0.0057 -0.0015 1261 PHE A CD1   
324  C  CD2   . PHE A 44  ? 0.4676 0.3690 0.4325 0.0013  -0.0075 0.0052  1261 PHE A CD2   
325  C  CE1   . PHE A 44  ? 0.4710 0.3818 0.4239 0.0014  -0.0035 0.0023  1261 PHE A CE1   
326  C  CE2   . PHE A 44  ? 0.5379 0.4416 0.5007 0.0021  -0.0050 0.0088  1261 PHE A CE2   
327  C  CZ    . PHE A 44  ? 0.5196 0.4277 0.4766 0.0021  -0.0033 0.0071  1261 PHE A CZ    
328  N  N     . ALA A 45  ? 0.5309 0.4187 0.5098 0.0047  -0.0139 -0.0102 1262 ALA A N     
329  C  CA    . ALA A 45  ? 0.5742 0.4551 0.5614 0.0064  -0.0139 -0.0070 1262 ALA A CA    
330  C  C     . ALA A 45  ? 0.5662 0.4464 0.5534 0.0111  -0.0129 -0.0101 1262 ALA A C     
331  O  O     . ALA A 45  ? 0.5303 0.4082 0.5203 0.0137  -0.0116 -0.0053 1262 ALA A O     
332  C  CB    . ALA A 45  ? 0.6284 0.5023 0.6235 0.0042  -0.0172 -0.0090 1262 ALA A CB    
333  N  N     . ILE A 46  ? 0.5644 0.4475 0.5482 0.0124  -0.0136 -0.0182 1263 ILE A N     
334  C  CA    . ILE A 46  ? 0.5924 0.4767 0.5767 0.0174  -0.0125 -0.0220 1263 ILE A CA    
335  C  C     . ILE A 46  ? 0.6542 0.5454 0.6347 0.0190  -0.0095 -0.0176 1263 ILE A C     
336  O  O     . ILE A 46  ? 0.7453 0.6354 0.7290 0.0230  -0.0089 -0.0155 1263 ILE A O     
337  C  CB    . ILE A 46  ? 0.4949 0.3835 0.4752 0.0184  -0.0130 -0.0318 1263 ILE A CB    
338  C  CG1   . ILE A 46  ? 0.4299 0.3114 0.4143 0.0174  -0.0167 -0.0376 1263 ILE A CG1   
339  C  CG2   . ILE A 46  ? 0.4224 0.3153 0.4030 0.0237  -0.0112 -0.0356 1263 ILE A CG2   
340  C  CD1   . ILE A 46  ? 0.4363 0.3224 0.4159 0.0186  -0.0173 -0.0479 1263 ILE A CD1   
341  N  N     . TRP A 47  ? 0.4130 0.3112 0.3868 0.0159  -0.0078 -0.0164 1264 TRP A N     
342  C  CA    . TRP A 47  ? 0.6916 0.5962 0.6622 0.0166  -0.0052 -0.0129 1264 TRP A CA    
343  C  C     . TRP A 47  ? 0.7244 0.6254 0.6983 0.0175  -0.0050 -0.0054 1264 TRP A C     
344  O  O     . TRP A 47  ? 0.8178 0.7219 0.7920 0.0206  -0.0039 -0.0036 1264 TRP A O     
345  C  CB    . TRP A 47  ? 0.7553 0.6659 0.7189 0.0125  -0.0037 -0.0123 1264 TRP A CB    
346  C  CG    . TRP A 47  ? 0.7201 0.6362 0.6812 0.0123  -0.0014 -0.0087 1264 TRP A CG    
347  C  CD1   . TRP A 47  ? 0.7943 0.7099 0.7539 0.0102  -0.0008 -0.0031 1264 TRP A CD1   
348  C  CD2   . TRP A 47  ? 0.6840 0.6072 0.6448 0.0145  0.0005  -0.0112 1264 TRP A CD2   
349  N  NE1   . TRP A 47  ? 0.7011 0.6223 0.6589 0.0107  0.0011  -0.0023 1264 TRP A NE1   
350  C  CE2   . TRP A 47  ? 0.6681 0.5944 0.6270 0.0131  0.0018  -0.0071 1264 TRP A CE2   
351  C  CE3   . TRP A 47  ? 0.6854 0.6132 0.6480 0.0176  0.0010  -0.0171 1264 TRP A CE3   
352  C  CZ2   . TRP A 47  ? 0.6899 0.6238 0.6489 0.0142  0.0034  -0.0086 1264 TRP A CZ2   
353  C  CZ3   . TRP A 47  ? 0.7298 0.6659 0.6927 0.0189  0.0028  -0.0182 1264 TRP A CZ3   
354  C  CH2   . TRP A 47  ? 0.7103 0.6494 0.6716 0.0169  0.0038  -0.0140 1264 TRP A CH2   
355  N  N     . LYS A 48  ? 0.6610 0.5564 0.6373 0.0150  -0.0060 -0.0011 1265 LYS A N     
356  C  CA    . LYS A 48  ? 0.6130 0.5060 0.5918 0.0156  -0.0052 0.0064  1265 LYS A CA    
357  C  C     . LYS A 48  ? 0.7372 0.6256 0.7206 0.0200  -0.0057 0.0082  1265 LYS A C     
358  O  O     . LYS A 48  ? 0.7810 0.6714 0.7634 0.0225  -0.0045 0.0128  1265 LYS A O     
359  C  CB    . LYS A 48  ? 0.5780 0.4667 0.5600 0.0119  -0.0060 0.0099  1265 LYS A CB    
360  C  CG    . LYS A 48  ? 0.6520 0.5415 0.6344 0.0114  -0.0043 0.0174  1265 LYS A CG    
361  C  CD    . LYS A 48  ? 0.8266 0.7121 0.8147 0.0081  -0.0050 0.0209  1265 LYS A CD    
362  C  CE    . LYS A 48  ? 0.8573 0.7453 0.8438 0.0045  -0.0064 0.0179  1265 LYS A CE    
363  N  NZ    . LYS A 48  ? 0.7621 0.6478 0.7557 0.0014  -0.0073 0.0213  1265 LYS A NZ    
364  N  N     . ALA A 49  ? 0.7380 0.6201 0.7264 0.0212  -0.0076 0.0045  1266 ALA A N     
365  C  CA    . ALA A 49  ? 0.6687 0.5453 0.6619 0.0259  -0.0084 0.0062  1266 ALA A CA    
366  C  C     . ALA A 49  ? 0.6895 0.5733 0.6797 0.0307  -0.0077 0.0040  1266 ALA A C     
367  O  O     . ALA A 49  ? 0.8071 0.6909 0.7978 0.0343  -0.0075 0.0091  1266 ALA A O     
368  C  CB    . ALA A 49  ? 0.7064 0.5744 0.7058 0.0265  -0.0110 0.0011  1266 ALA A CB    
369  N  N     . ILE A 50  ? 0.6054 0.4961 0.5927 0.0307  -0.0073 -0.0034 1267 ILE A N     
370  C  CA    . ILE A 50  ? 0.5845 0.4835 0.5704 0.0348  -0.0065 -0.0059 1267 ILE A CA    
371  C  C     . ILE A 50  ? 0.5765 0.4814 0.5586 0.0344  -0.0051 -0.0002 1267 ILE A C     
372  O  O     . ILE A 50  ? 0.4125 0.3207 0.3954 0.0388  -0.0054 0.0016  1267 ILE A O     
373  C  CB    . ILE A 50  ? 0.5420 0.4491 0.5249 0.0337  -0.0054 -0.0140 1267 ILE A CB    
374  C  CG1   . ILE A 50  ? 0.5593 0.4612 0.5449 0.0342  -0.0068 -0.0207 1267 ILE A CG1   
375  C  CG2   . ILE A 50  ? 0.4378 0.3548 0.4209 0.0375  -0.0043 -0.0166 1267 ILE A CG2   
376  C  CD1   . ILE A 50  ? 0.6159 0.5269 0.5974 0.0333  -0.0052 -0.0284 1267 ILE A CD1   
377  N  N     . ARG A 51  ? 0.5083 0.4150 0.4861 0.0295  -0.0037 0.0021  1268 ARG A N     
378  C  CA    . ARG A 51  ? 0.5336 0.4457 0.5077 0.0288  -0.0024 0.0063  1268 ARG A CA    
379  C  C     . ARG A 51  ? 0.5808 0.4889 0.5562 0.0317  -0.0029 0.0134  1268 ARG A C     
380  O  O     . ARG A 51  ? 0.5317 0.4451 0.5052 0.0347  -0.0029 0.0152  1268 ARG A O     
381  C  CB    . ARG A 51  ? 0.6202 0.5328 0.5904 0.0233  -0.0012 0.0074  1268 ARG A CB    
382  C  CG    . ARG A 51  ? 0.6721 0.5888 0.6387 0.0225  0.0000  0.0113  1268 ARG A CG    
383  C  CD    . ARG A 51  ? 0.8593 0.7722 0.8250 0.0193  0.0006  0.0155  1268 ARG A CD    
384  N  NE    . ARG A 51  ? 1.1525 1.0687 1.1151 0.0197  0.0018  0.0190  1268 ARG A NE    
385  C  CZ    . ARG A 51  ? 1.2174 1.1351 1.1771 0.0168  0.0028  0.0195  1268 ARG A CZ    
386  N  NH1   . ARG A 51  ? 1.3086 1.2248 1.2677 0.0132  0.0027  0.0177  1268 ARG A NH1   
387  N  NH2   . ARG A 51  ? 1.0714 0.9921 1.0284 0.0179  0.0037  0.0218  1268 ARG A NH2   
388  N  N     . ASN A 52  ? 0.3951 0.2945 0.3737 0.0308  -0.0033 0.0176  1269 ASN A N     
389  C  CA    . ASN A 52  ? 0.5737 0.4698 0.5529 0.0330  -0.0031 0.0254  1269 ASN A CA    
390  C  C     . ASN A 52  ? 0.5958 0.4909 0.5770 0.0392  -0.0047 0.0263  1269 ASN A C     
391  O  O     . ASN A 52  ? 0.5344 0.4320 0.5131 0.0425  -0.0046 0.0315  1269 ASN A O     
392  C  CB    . ASN A 52  ? 0.7742 0.6617 0.7577 0.0300  -0.0029 0.0298  1269 ASN A CB    
393  C  CG    . ASN A 52  ? 0.8590 0.7481 0.8412 0.0245  -0.0019 0.0285  1269 ASN A CG    
394  O  OD1   . ASN A 52  ? 1.0762 0.9601 1.0628 0.0214  -0.0028 0.0277  1269 ASN A OD1   
395  N  ND2   . ASN A 52  ? 0.7795 0.6759 0.7562 0.0235  -0.0006 0.0280  1269 ASN A ND2   
396  N  N     . TRP A 53  ? 0.6300 0.5213 0.6158 0.0413  -0.0064 0.0213  1270 TRP A N     
397  C  CA    . TRP A 53  ? 0.6518 0.5425 0.6402 0.0479  -0.0082 0.0213  1270 TRP A CA    
398  C  C     . TRP A 53  ? 0.6767 0.5794 0.6612 0.0509  -0.0082 0.0196  1270 TRP A C     
399  O  O     . TRP A 53  ? 0.8669 0.7715 0.8496 0.0551  -0.0091 0.0247  1270 TRP A O     
400  C  CB    . TRP A 53  ? 0.7993 0.6858 0.7931 0.0499  -0.0098 0.0140  1270 TRP A CB    
401  C  CG    . TRP A 53  ? 0.7624 0.6457 0.7604 0.0573  -0.0121 0.0149  1270 TRP A CG    
402  C  CD1   . TRP A 53  ? 0.6698 0.5413 0.6723 0.0601  -0.0136 0.0207  1270 TRP A CD1   
403  C  CD2   . TRP A 53  ? 0.7237 0.6160 0.7222 0.0629  -0.0132 0.0104  1270 TRP A CD2   
404  N  NE1   . TRP A 53  ? 0.5499 0.4217 0.5552 0.0677  -0.0159 0.0203  1270 TRP A NE1   
405  C  CE2   . TRP A 53  ? 0.5394 0.4246 0.5426 0.0698  -0.0157 0.0136  1270 TRP A CE2   
406  C  CE3   . TRP A 53  ? 0.7639 0.6699 0.7602 0.0628  -0.0122 0.0040  1270 TRP A CE3   
407  C  CZ2   . TRP A 53  ? 0.4539 0.3458 0.4597 0.0771  -0.0177 0.0104  1270 TRP A CZ2   
408  C  CZ3   . TRP A 53  ? 0.7268 0.6402 0.7262 0.0694  -0.0138 0.0006  1270 TRP A CZ3   
409  C  CH2   . TRP A 53  ? 0.5203 0.4269 0.5244 0.0768  -0.0167 0.0037  1270 TRP A CH2   
410  N  N     . PHE A 54  ? 0.6499 0.5611 0.6327 0.0485  -0.0073 0.0125  1271 PHE A N     
411  C  CA    . PHE A 54  ? 0.7173 0.6404 0.6980 0.0506  -0.0074 0.0098  1271 PHE A CA    
412  C  C     . PHE A 54  ? 0.7213 0.6484 0.6966 0.0495  -0.0068 0.0151  1271 PHE A C     
413  O  O     . PHE A 54  ? 0.7655 0.7001 0.7395 0.0532  -0.0081 0.0155  1271 PHE A O     
414  C  CB    . PHE A 54  ? 0.6442 0.5753 0.6245 0.0470  -0.0059 0.0020  1271 PHE A CB    
415  C  CG    . PHE A 54  ? 0.4574 0.4012 0.4383 0.0493  -0.0062 -0.0020 1271 PHE A CG    
416  C  CD1   . PHE A 54  ? 0.4827 0.4313 0.4689 0.0545  -0.0074 -0.0068 1271 PHE A CD1   
417  C  CD2   . PHE A 54  ? 0.4434 0.3948 0.4206 0.0463  -0.0053 -0.0015 1271 PHE A CD2   
418  C  CE1   . PHE A 54  ? 0.5473 0.5091 0.5354 0.0562  -0.0077 -0.0107 1271 PHE A CE1   
419  C  CE2   . PHE A 54  ? 0.3848 0.3484 0.3637 0.0476  -0.0058 -0.0056 1271 PHE A CE2   
420  C  CZ    . PHE A 54  ? 0.4367 0.4059 0.4211 0.0524  -0.0069 -0.0100 1271 PHE A CZ    
421  N  N     . ASP A 55  ? 0.3954 0.3182 0.3677 0.0449  -0.0051 0.0189  1272 ASP A N     
422  C  CA    . ASP A 55  ? 0.3934 0.3204 0.3604 0.0443  -0.0043 0.0230  1272 ASP A CA    
423  C  C     . ASP A 55  ? 0.4845 0.4086 0.4504 0.0492  -0.0053 0.0304  1272 ASP A C     
424  O  O     . ASP A 55  ? 0.5031 0.4339 0.4648 0.0519  -0.0060 0.0321  1272 ASP A O     
425  C  CB    . ASP A 55  ? 0.4357 0.3600 0.4001 0.0387  -0.0021 0.0246  1272 ASP A CB    
426  C  CG    . ASP A 55  ? 0.6579 0.5883 0.6169 0.0383  -0.0013 0.0263  1272 ASP A CG    
427  O  OD1   . ASP A 55  ? 0.6199 0.5580 0.5773 0.0375  -0.0016 0.0213  1272 ASP A OD1   
428  O  OD2   . ASP A 55  ? 0.7560 0.6838 0.7126 0.0390  -0.0003 0.0324  1272 ASP A OD2   
429  N  N     . ALA A 56  ? 0.5359 0.4499 0.5054 0.0502  -0.0055 0.0350  1273 ALA A N     
430  C  CA    . ALA A 56  ? 0.6265 0.5370 0.5951 0.0551  -0.0064 0.0429  1273 ALA A CA    
431  C  C     . ALA A 56  ? 0.4572 0.3743 0.4254 0.0617  -0.0093 0.0412  1273 ALA A C     
432  O  O     . ALA A 56  ? 0.4238 0.3460 0.3870 0.0654  -0.0102 0.0456  1273 ALA A O     
433  C  CB    . ALA A 56  ? 0.6970 0.5946 0.6715 0.0549  -0.0065 0.0471  1273 ALA A CB    
434  N  N     . GLU A 57  ? 0.4187 0.3374 0.3920 0.0632  -0.0109 0.0340  1274 GLU A N     
435  C  CA    . GLU A 57  ? 0.4562 0.3820 0.4310 0.0698  -0.0138 0.0315  1274 GLU A CA    
436  C  C     . GLU A 57  ? 0.5549 0.4944 0.5248 0.0699  -0.0143 0.0291  1274 GLU A C     
437  O  O     . GLU A 57  ? 0.5191 0.4636 0.4861 0.0753  -0.0167 0.0326  1274 GLU A O     
438  C  CB    . GLU A 57  ? 0.4210 0.3475 0.4026 0.0708  -0.0146 0.0232  1274 GLU A CB    
439  C  CG    . GLU A 57  ? 0.6974 0.6118 0.6849 0.0747  -0.0161 0.0252  1274 GLU A CG    
440  C  CD    . GLU A 57  ? 0.9218 0.8304 0.9080 0.0805  -0.0181 0.0349  1274 GLU A CD    
441  O  OE1   . GLU A 57  ? 1.0067 0.9231 0.9916 0.0865  -0.0207 0.0357  1274 GLU A OE1   
442  O  OE2   . GLU A 57  ? 0.9974 0.8939 0.9838 0.0789  -0.0172 0.0420  1274 GLU A OE2   
443  N  N     . ILE A 58  ? 0.6556 0.6006 0.6243 0.0639  -0.0123 0.0234  1275 ILE A N     
444  C  CA    . ILE A 58  ? 0.6606 0.6184 0.6265 0.0637  -0.0132 0.0195  1275 ILE A CA    
445  C  C     . ILE A 58  ? 0.6441 0.6033 0.6025 0.0635  -0.0129 0.0247  1275 ILE A C     
446  O  O     . ILE A 58  ? 0.7300 0.6991 0.6855 0.0660  -0.0150 0.0232  1275 ILE A O     
447  C  CB    . ILE A 58  ? 0.6613 0.6242 0.6289 0.0574  -0.0112 0.0120  1275 ILE A CB    
448  C  CG1   . ILE A 58  ? 0.6334 0.5884 0.5980 0.0510  -0.0081 0.0140  1275 ILE A CG1   
449  C  CG2   . ILE A 58  ? 0.6939 0.6590 0.6683 0.0586  -0.0114 0.0060  1275 ILE A CG2   
450  C  CD1   . ILE A 58  ? 0.5827 0.5431 0.5450 0.0453  -0.0065 0.0098  1275 ILE A CD1   
451  N  N     . THR A 59  ? 0.4885 0.4390 0.4437 0.0609  -0.0105 0.0306  1276 THR A N     
452  C  CA    . THR A 59  ? 0.5157 0.4692 0.4636 0.0619  -0.0101 0.0354  1276 THR A CA    
453  C  C     . THR A 59  ? 0.6448 0.5974 0.5900 0.0688  -0.0122 0.0427  1276 THR A C     
454  O  O     . THR A 59  ? 0.6501 0.6094 0.5885 0.0717  -0.0131 0.0451  1276 THR A O     
455  C  CB    . THR A 59  ? 0.4965 0.4437 0.4419 0.0567  -0.0064 0.0387  1276 THR A CB    
456  O  OG1   . THR A 59  ? 0.6761 0.6138 0.6228 0.0577  -0.0052 0.0466  1276 THR A OG1   
457  C  CG2   . THR A 59  ? 0.5101 0.4552 0.4591 0.0503  -0.0046 0.0329  1276 THR A CG2   
458  N  N     . ARG A 60  ? 0.7313 0.6757 0.6815 0.0718  -0.0131 0.0462  1277 ARG A N     
459  C  CA    . ARG A 60  ? 0.8334 0.7769 0.7816 0.0792  -0.0158 0.0531  1277 ARG A CA    
460  C  C     . ARG A 60  ? 0.7704 0.7262 0.7180 0.0847  -0.0200 0.0485  1277 ARG A C     
461  O  O     . ARG A 60  ? 0.9322 0.8924 0.8742 0.0904  -0.0224 0.0537  1277 ARG A O     
462  C  CB    . ARG A 60  ? 1.0179 0.9491 0.9729 0.0814  -0.0163 0.0567  1277 ARG A CB    
463  C  CG    . ARG A 60  ? 1.0886 1.0154 1.0410 0.0883  -0.0184 0.0666  1277 ARG A CG    
464  C  CD    . ARG A 60  ? 1.1846 1.1006 1.1452 0.0921  -0.0204 0.0678  1277 ARG A CD    
465  N  NE    . ARG A 60  ? 1.2340 1.1569 1.1973 0.0997  -0.0250 0.0641  1277 ARG A NE    
466  C  CZ    . ARG A 60  ? 1.2171 1.1445 1.1875 0.1003  -0.0264 0.0541  1277 ARG A CZ    
467  N  NH1   . ARG A 60  ? 1.1633 1.0887 1.1378 0.0936  -0.0236 0.0471  1277 ARG A NH1   
468  N  NH2   . ARG A 60  ? 1.2599 1.1947 1.2334 0.1077  -0.0305 0.0513  1277 ARG A NH2   
469  N  N     . LEU A 61  ? 0.4857 0.4479 0.4392 0.0832  -0.0210 0.0390  1278 LEU A N     
470  C  CA    . LEU A 61  ? 0.5609 0.5365 0.5151 0.0879  -0.0250 0.0343  1278 LEU A CA    
471  C  C     . LEU A 61  ? 0.6576 0.6437 0.6046 0.0860  -0.0254 0.0321  1278 LEU A C     
472  O  O     . LEU A 61  ? 0.6507 0.6473 0.5953 0.0910  -0.0293 0.0312  1278 LEU A O     
473  C  CB    . LEU A 61  ? 0.5773 0.5584 0.5404 0.0863  -0.0253 0.0247  1278 LEU A CB    
474  C  CG    . LEU A 61  ? 0.5525 0.5252 0.5234 0.0881  -0.0250 0.0237  1278 LEU A CG    
475  C  CD1   . LEU A 61  ? 0.4272 0.4082 0.4052 0.0851  -0.0242 0.0135  1278 LEU A CD1   
476  C  CD2   . LEU A 61  ? 0.5199 0.4909 0.4931 0.0975  -0.0290 0.0283  1278 LEU A CD2   
477  N  N     . GLY A 62  ? 0.7804 0.7636 0.7240 0.0792  -0.0217 0.0313  1279 GLY A N     
478  C  CA    . GLY A 62  ? 0.7340 0.7251 0.6710 0.0769  -0.0216 0.0286  1279 GLY A CA    
479  C  C     . GLY A 62  ? 0.5671 0.5611 0.5069 0.0694  -0.0196 0.0204  1279 GLY A C     
480  O  O     . GLY A 62  ? 0.4706 0.4700 0.4058 0.0672  -0.0195 0.0173  1279 GLY A O     
481  N  N     . VAL A 63  ? 0.5737 0.5628 0.5202 0.0652  -0.0175 0.0172  1280 VAL A N     
482  C  CA    . VAL A 63  ? 0.3955 0.3867 0.3440 0.0581  -0.0155 0.0106  1280 VAL A CA    
483  C  C     . VAL A 63  ? 0.6099 0.5934 0.5534 0.0539  -0.0122 0.0138  1280 VAL A C     
484  O  O     . VAL A 63  ? 0.4207 0.3948 0.3632 0.0541  -0.0102 0.0200  1280 VAL A O     
485  C  CB    . VAL A 63  ? 0.4584 0.4481 0.4146 0.0551  -0.0141 0.0064  1280 VAL A CB    
486  C  CG1   . VAL A 63  ? 0.4607 0.4532 0.4184 0.0477  -0.0121 0.0004  1280 VAL A CG1   
487  C  CG2   . VAL A 63  ? 0.3925 0.3902 0.3546 0.0601  -0.0171 0.0033  1280 VAL A CG2   
488  N  N     . LYS A 64  ? 0.6141 0.6017 0.5550 0.0502  -0.0118 0.0094  1281 LYS A N     
489  C  CA    . LYS A 64  ? 0.6229 0.6042 0.5599 0.0464  -0.0088 0.0111  1281 LYS A CA    
490  C  C     . LYS A 64  ? 0.6188 0.5955 0.5600 0.0397  -0.0064 0.0076  1281 LYS A C     
491  O  O     . LYS A 64  ? 0.6553 0.6359 0.6015 0.0371  -0.0070 0.0024  1281 LYS A O     
492  C  CB    . LYS A 64  ? 0.5170 0.5045 0.4482 0.0471  -0.0098 0.0085  1281 LYS A CB    
493  C  CG    . LYS A 64  ? 0.4003 0.3898 0.3245 0.0531  -0.0106 0.0142  1281 LYS A CG    
494  C  CD    . LYS A 64  ? 0.4410 0.4417 0.3616 0.0563  -0.0144 0.0096  1281 LYS A CD    
495  C  CE    . LYS A 64  ? 0.5612 0.5646 0.4731 0.0625  -0.0151 0.0157  1281 LYS A CE    
496  N  NZ    . LYS A 64  ? 0.8425 0.8570 0.7495 0.0648  -0.0187 0.0096  1281 LYS A NZ    
497  N  N     . GLU A 65  ? 0.5693 0.5386 0.5084 0.0370  -0.0038 0.0105  1282 GLU A N     
498  C  CA    . GLU A 65  ? 0.5975 0.5609 0.5395 0.0313  -0.0017 0.0089  1282 GLU A CA    
499  C  C     . GLU A 65  ? 0.5454 0.5079 0.4849 0.0279  -0.0007 0.0064  1282 GLU A C     
500  O  O     . GLU A 65  ? 0.5449 0.5077 0.4799 0.0302  -0.0004 0.0080  1282 GLU A O     
501  C  CB    . GLU A 65  ? 0.6358 0.5907 0.5789 0.0311  0.0001  0.0144  1282 GLU A CB    
502  C  CG    . GLU A 65  ? 0.6500 0.5991 0.5946 0.0259  0.0019  0.0135  1282 GLU A CG    
503  C  CD    . GLU A 65  ? 0.7972 0.7398 0.7447 0.0256  0.0025  0.0169  1282 GLU A CD    
504  O  OE1   . GLU A 65  ? 0.9025 0.8447 0.8515 0.0292  0.0016  0.0193  1282 GLU A OE1   
505  O  OE2   . GLU A 65  ? 0.8635 0.8013 0.8118 0.0219  0.0037  0.0170  1282 GLU A OE2   
506  N  N     . CYS A 66  ? 0.6366 0.5983 0.5788 0.0228  -0.0002 0.0022  1283 CYS A N     
507  C  CA    . CYS A 66  ? 0.7132 0.6724 0.6540 0.0193  0.0005  -0.0004 1283 CYS A CA    
508  C  C     . CYS A 66  ? 0.7200 0.6731 0.6633 0.0141  0.0022  -0.0003 1283 CYS A C     
509  O  O     . CYS A 66  ? 0.8930 0.8443 0.8383 0.0135  0.0028  0.0017  1283 CYS A O     
510  C  CB    . CYS A 66  ? 0.6707 0.6370 0.6120 0.0184  -0.0015 -0.0067 1283 CYS A CB    
511  S  SG    . CYS A 66  ? 0.6899 0.6626 0.6376 0.0150  -0.0022 -0.0109 1283 CYS A SG    
512  N  N     . TYR A 67  ? 0.5570 0.5067 0.5000 0.0104  0.0027  -0.0024 1284 TYR A N     
513  C  CA    . TYR A 67  ? 0.5045 0.4482 0.4489 0.0056  0.0041  -0.0015 1284 TYR A CA    
514  C  C     . TYR A 67  ? 0.5314 0.4731 0.4764 0.0013  0.0040  -0.0050 1284 TYR A C     
515  O  O     . TYR A 67  ? 0.6290 0.5663 0.5723 0.0019  0.0039  -0.0054 1284 TYR A O     
516  C  CB    . TYR A 67  ? 0.3697 0.3062 0.3125 0.0066  0.0051  0.0035  1284 TYR A CB    
517  C  CG    . TYR A 67  ? 0.6098 0.5409 0.5532 0.0022  0.0060  0.0047  1284 TYR A CG    
518  C  CD1   . TYR A 67  ? 0.5364 0.4689 0.4810 0.0005  0.0064  0.0050  1284 TYR A CD1   
519  C  CD2   . TYR A 67  ? 0.6406 0.5654 0.5831 0.0001  0.0062  0.0053  1284 TYR A CD2   
520  C  CE1   . TYR A 67  ? 0.5523 0.4807 0.4961 -0.0033 0.0071  0.0062  1284 TYR A CE1   
521  C  CE2   . TYR A 67  ? 0.5422 0.4621 0.4844 -0.0036 0.0067  0.0072  1284 TYR A CE2   
522  C  CZ    . TYR A 67  ? 0.5014 0.4235 0.4437 -0.0054 0.0072  0.0077  1284 TYR A CZ    
523  O  OH    . TYR A 67  ? 0.4586 0.3769 0.3994 -0.0089 0.0077  0.0096  1284 TYR A OH    
524  N  N     . PHE A 68  ? 0.4607 0.4052 0.4087 -0.0030 0.0044  -0.0075 1285 PHE A N     
525  C  CA    . PHE A 68  ? 0.5540 0.4957 0.5038 -0.0084 0.0047  -0.0101 1285 PHE A CA    
526  C  C     . PHE A 68  ? 0.6463 0.5792 0.5947 -0.0119 0.0063  -0.0061 1285 PHE A C     
527  O  O     . PHE A 68  ? 0.6883 0.6200 0.6353 -0.0110 0.0072  -0.0025 1285 PHE A O     
528  C  CB    . PHE A 68  ? 0.6437 0.5941 0.5981 -0.0119 0.0047  -0.0141 1285 PHE A CB    
529  C  CG    . PHE A 68  ? 0.6280 0.5872 0.5844 -0.0092 0.0022  -0.0192 1285 PHE A CG    
530  C  CD1   . PHE A 68  ? 0.5567 0.5215 0.5113 -0.0029 0.0007  -0.0186 1285 PHE A CD1   
531  C  CD2   . PHE A 68  ? 0.6108 0.5725 0.5708 -0.0131 0.0011  -0.0245 1285 PHE A CD2   
532  C  CE1   . PHE A 68  ? 0.5413 0.5147 0.4967 -0.0001 -0.0019 -0.0229 1285 PHE A CE1   
533  C  CE2   . PHE A 68  ? 0.5672 0.5379 0.5288 -0.0106 -0.0018 -0.0297 1285 PHE A CE2   
534  C  CZ    . PHE A 68  ? 0.6089 0.5858 0.5677 -0.0038 -0.0034 -0.0287 1285 PHE A CZ    
535  N  N     . PRO A 69  ? 0.6963 0.6228 0.6454 -0.0159 0.0065  -0.0066 1286 PRO A N     
536  C  CA    . PRO A 69  ? 0.6716 0.5894 0.6187 -0.0186 0.0076  -0.0020 1286 PRO A CA    
537  C  C     . PRO A 69  ? 0.6501 0.5711 0.5972 -0.0224 0.0095  0.0000  1286 PRO A C     
538  O  O     . PRO A 69  ? 0.7734 0.7026 0.7235 -0.0246 0.0103  -0.0029 1286 PRO A O     
539  C  CB    . PRO A 69  ? 0.6448 0.5554 0.5934 -0.0223 0.0073  -0.0036 1286 PRO A CB    
540  C  CG    . PRO A 69  ? 0.6504 0.5651 0.6010 -0.0199 0.0055  -0.0095 1286 PRO A CG    
541  C  CD    . PRO A 69  ? 0.6554 0.5816 0.6068 -0.0175 0.0052  -0.0116 1286 PRO A CD    
542  N  N     . ILE A 70  ? 0.4617 0.3772 0.4054 -0.0230 0.0101  0.0048  1287 ILE A N     
543  C  CA    . ILE A 70  ? 0.5543 0.4727 0.4965 -0.0265 0.0121  0.0066  1287 ILE A CA    
544  C  C     . ILE A 70  ? 0.6066 0.5241 0.5502 -0.0331 0.0139  0.0068  1287 ILE A C     
545  O  O     . ILE A 70  ? 0.6734 0.5958 0.6163 -0.0365 0.0163  0.0077  1287 ILE A O     
546  C  CB    . ILE A 70  ? 0.6062 0.5189 0.5436 -0.0259 0.0119  0.0116  1287 ILE A CB    
547  C  CG1   . ILE A 70  ? 0.3967 0.2990 0.3329 -0.0262 0.0107  0.0147  1287 ILE A CG1   
548  C  CG2   . ILE A 70  ? 0.4831 0.3988 0.4194 -0.0212 0.0109  0.0118  1287 ILE A CG2   
549  C  CD1   . ILE A 70  ? 0.5651 0.4628 0.4970 -0.0256 0.0100  0.0193  1287 ILE A CD1   
550  N  N     . PHE A 71  ? 0.5949 0.5054 0.5403 -0.0351 0.0131  0.0064  1288 PHE A N     
551  C  CA    . PHE A 71  ? 0.4100 0.3170 0.3573 -0.0419 0.0147  0.0075  1288 PHE A CA    
552  C  C     . PHE A 71  ? 0.4100 0.3241 0.3640 -0.0449 0.0149  0.0015  1288 PHE A C     
553  O  O     . PHE A 71  ? 0.4064 0.3232 0.3627 -0.0413 0.0126  -0.0033 1288 PHE A O     
554  C  CB    . PHE A 71  ? 0.6471 0.5405 0.5930 -0.0423 0.0133  0.0105  1288 PHE A CB    
555  C  CG    . PHE A 71  ? 0.5662 0.4527 0.5062 -0.0410 0.0132  0.0171  1288 PHE A CG    
556  C  CD1   . PHE A 71  ? 0.5354 0.4239 0.4713 -0.0445 0.0154  0.0215  1288 PHE A CD1   
557  C  CD2   . PHE A 71  ? 0.4209 0.2996 0.3593 -0.0360 0.0107  0.0186  1288 PHE A CD2   
558  C  CE1   . PHE A 71  ? 0.4276 0.3103 0.3576 -0.0430 0.0146  0.0273  1288 PHE A CE1   
559  C  CE2   . PHE A 71  ? 0.4237 0.2971 0.3574 -0.0345 0.0099  0.0243  1288 PHE A CE2   
560  C  CZ    . PHE A 71  ? 0.4408 0.3158 0.3700 -0.0380 0.0116  0.0287  1288 PHE A CZ    
561  N  N     . VAL A 72  ? 0.6139 0.5314 0.5708 -0.0518 0.0176  0.0020  1289 VAL A N     
562  C  CA    . VAL A 72  ? 0.5584 0.4840 0.5231 -0.0562 0.0180  -0.0034 1289 VAL A CA    
563  C  C     . VAL A 72  ? 0.6318 0.5491 0.5999 -0.0640 0.0193  -0.0016 1289 VAL A C     
564  O  O     . VAL A 72  ? 0.6869 0.5996 0.6521 -0.0685 0.0221  0.0046  1289 VAL A O     
565  C  CB    . VAL A 72  ? 0.5770 0.5172 0.5441 -0.0575 0.0207  -0.0047 1289 VAL A CB    
566  C  CG1   . VAL A 72  ? 0.4931 0.4437 0.4695 -0.0614 0.0207  -0.0109 1289 VAL A CG1   
567  C  CG2   . VAL A 72  ? 0.4020 0.3474 0.3653 -0.0495 0.0194  -0.0055 1289 VAL A CG2   
568  N  N     . SER A 73  ? 0.7152 0.6301 0.6892 -0.0656 0.0169  -0.0069 1290 SER A N     
569  C  CA    . SER A 73  ? 0.4421 0.3507 0.4220 -0.0740 0.0179  -0.0069 1290 SER A CA    
570  C  C     . SER A 73  ? 0.6676 0.5862 0.6520 -0.0816 0.0223  -0.0051 1290 SER A C     
571  O  O     . SER A 73  ? 0.8231 0.7570 0.8101 -0.0804 0.0233  -0.0085 1290 SER A O     
572  C  CB    . SER A 73  ? 0.4436 0.3534 0.4306 -0.0742 0.0144  -0.0156 1290 SER A CB    
573  O  OG    . SER A 73  ? 1.1006 1.0065 1.0954 -0.0833 0.0154  -0.0168 1290 SER A OG    
574  N  N     . ARG A 74  ? 0.6948 0.6051 0.6803 -0.0893 0.0250  0.0004  1291 ARG A N     
575  C  CA    . ARG A 74  ? 0.5865 0.5069 0.5775 -0.0976 0.0296  0.0018  1291 ARG A CA    
576  C  C     . ARG A 74  ? 0.5369 0.4704 0.5393 -0.1003 0.0285  -0.0071 1291 ARG A C     
577  O  O     . ARG A 74  ? 0.5450 0.4952 0.5511 -0.1008 0.0307  -0.0096 1291 ARG A O     
578  C  CB    . ARG A 74  ? 0.4749 0.3826 0.4664 -0.1062 0.0324  0.0091  1291 ARG A CB    
579  N  N     . ALA A 75  ? 0.6265 0.5533 0.6345 -0.1015 0.0247  -0.0127 1292 ALA A N     
580  C  CA    . ALA A 75  ? 0.7791 0.7185 0.7987 -0.1049 0.0231  -0.0216 1292 ALA A CA    
581  C  C     . ALA A 75  ? 0.7449 0.7006 0.7640 -0.0970 0.0209  -0.0273 1292 ALA A C     
582  O  O     . ALA A 75  ? 0.8083 0.7807 0.8353 -0.0995 0.0220  -0.0315 1292 ALA A O     
583  C  CB    . ALA A 75  ? 0.7938 0.7223 0.8185 -0.1067 0.0187  -0.0274 1292 ALA A CB    
584  N  N     . ALA A 76  ? 0.6609 0.6122 0.6711 -0.0874 0.0180  -0.0273 1293 ALA A N     
585  C  CA    . ALA A 76  ? 0.6862 0.6510 0.6950 -0.0794 0.0161  -0.0313 1293 ALA A CA    
586  C  C     . ALA A 76  ? 0.7497 0.7279 0.7597 -0.0803 0.0202  -0.0289 1293 ALA A C     
587  O  O     . ALA A 76  ? 0.7297 0.7239 0.7462 -0.0792 0.0196  -0.0341 1293 ALA A O     
588  C  CB    . ALA A 76  ? 0.7008 0.6571 0.6991 -0.0701 0.0138  -0.0290 1293 ALA A CB    
589  N  N     . LEU A 77  ? 0.7620 0.7340 0.7654 -0.0817 0.0241  -0.0212 1294 LEU A N     
590  C  CA    . LEU A 77  ? 0.5817 0.5654 0.5847 -0.0822 0.0285  -0.0189 1294 LEU A CA    
591  C  C     . LEU A 77  ? 0.5827 0.5785 0.5965 -0.0911 0.0321  -0.0208 1294 LEU A C     
592  O  O     . LEU A 77  ? 0.6302 0.6424 0.6484 -0.0902 0.0342  -0.0235 1294 LEU A O     
593  C  CB    . LEU A 77  ? 0.5087 0.4819 0.5013 -0.0821 0.0313  -0.0104 1294 LEU A CB    
594  C  CG    . LEU A 77  ? 0.5375 0.5184 0.5249 -0.0805 0.0354  -0.0070 1294 LEU A CG    
595  C  CD1   . LEU A 77  ? 0.5043 0.4944 0.4905 -0.0716 0.0333  -0.0113 1294 LEU A CD1   
596  C  CD2   . LEU A 77  ? 0.4274 0.3949 0.4039 -0.0809 0.0368  0.0012  1294 LEU A CD2   
597  N  N     . GLU A 78  ? 0.5716 0.5602 0.5908 -0.0997 0.0327  -0.0200 1295 GLU A N     
598  C  CA    . GLU A 78  ? 0.7064 0.7068 0.7372 -0.1092 0.0365  -0.0215 1295 GLU A CA    
599  C  C     . GLU A 78  ? 0.7924 0.8021 0.8351 -0.1102 0.0321  -0.0311 1295 GLU A C     
600  O  O     . GLU A 78  ? 0.9038 0.9091 0.9546 -0.1178 0.0312  -0.0333 1295 GLU A O     
601  C  CB    . GLU A 78  ? 0.8506 0.8378 0.8814 -0.1189 0.0400  -0.0144 1295 GLU A CB    
602  C  CG    . GLU A 78  ? 0.9573 0.9316 0.9748 -0.1175 0.0429  -0.0043 1295 GLU A CG    
603  C  CD    . GLU A 78  ? 1.0499 1.0078 1.0673 -0.1263 0.0449  0.0029  1295 GLU A CD    
604  O  OE1   . GLU A 78  ? 1.0873 1.0431 1.1155 -0.1336 0.0441  -0.0004 1295 GLU A OE1   
605  O  OE2   . GLU A 78  ? 0.9875 0.9343 0.9943 -0.1258 0.0469  0.0117  1295 GLU A OE2   
606  N  N     . ARG A 79  ? 0.9054 0.9291 0.9498 -0.1026 0.0294  -0.0370 1296 ARG A N     
607  C  CA    . ARG A 79  ? 0.9097 0.9436 0.9641 -0.1021 0.0244  -0.0463 1296 ARG A CA    
608  C  C     . ARG A 79  ? 1.0808 1.1334 1.1376 -0.0943 0.0229  -0.0509 1296 ARG A C     
609  O  O     . ARG A 79  ? 1.1039 1.1745 1.1719 -0.0978 0.0248  -0.0546 1296 ARG A O     
610  C  CB    . ARG A 79  ? 0.6730 0.6926 0.7223 -0.0979 0.0184  -0.0492 1296 ARG A CB    
611  C  CG    . ARG A 79  ? 0.6054 0.6359 0.6618 -0.0949 0.0123  -0.0591 1296 ARG A CG    
612  C  CD    . ARG A 79  ? 0.5913 0.6110 0.6401 -0.0879 0.0065  -0.0622 1296 ARG A CD    
613  N  NE    . ARG A 79  ? 0.7516 0.7859 0.8056 -0.0835 0.0010  -0.0711 1296 ARG A NE    
614  C  CZ    . ARG A 79  ? 0.8691 0.9007 0.9169 -0.0758 -0.0044 -0.0751 1296 ARG A CZ    
615  N  NH1   . ARG A 79  ? 0.8719 0.8869 0.9088 -0.0717 -0.0048 -0.0716 1296 ARG A NH1   
616  N  NH2   . ARG A 79  ? 0.8638 0.9101 0.9162 -0.0721 -0.0094 -0.0828 1296 ARG A NH2   
617  N  N     . ASP A 86  ? 0.5138 0.6172 0.5341 -0.1084 0.0792  -0.0121 1303 ASP A N     
618  C  CA    . ASP A 86  ? 0.7837 0.8982 0.8025 -0.0982 0.0785  -0.0184 1303 ASP A CA    
619  C  C     . ASP A 86  ? 0.9785 1.0789 0.9810 -0.0906 0.0760  -0.0154 1303 ASP A C     
620  O  O     . ASP A 86  ? 0.8645 0.9690 0.8583 -0.0895 0.0805  -0.0134 1303 ASP A O     
621  C  CB    . ASP A 86  ? 0.6089 0.7304 0.6392 -0.0921 0.0724  -0.0270 1303 ASP A CB    
622  N  N     . PHE A 87  ? 1.0363 1.1205 1.0347 -0.0857 0.0690  -0.0151 1304 PHE A N     
623  C  CA    . PHE A 87  ? 1.0008 1.0702 0.9850 -0.0802 0.0664  -0.0114 1304 PHE A CA    
624  C  C     . PHE A 87  ? 0.9599 1.0119 0.9356 -0.0860 0.0663  -0.0025 1304 PHE A C     
625  O  O     . PHE A 87  ? 0.9598 0.9980 0.9251 -0.0816 0.0629  0.0007  1304 PHE A O     
626  C  CB    . PHE A 87  ? 1.0382 1.1002 1.0226 -0.0710 0.0590  -0.0156 1304 PHE A CB    
627  C  CG    . PHE A 87  ? 1.0511 1.1273 1.0440 -0.0642 0.0576  -0.0237 1304 PHE A CG    
628  C  CD1   . PHE A 87  ? 1.0575 1.1348 1.0590 -0.0614 0.0526  -0.0280 1304 PHE A CD1   
629  C  CD2   . PHE A 87  ? 1.0483 1.1358 1.0398 -0.0598 0.0607  -0.0273 1304 PHE A CD2   
630  C  CE1   . PHE A 87  ? 1.0152 1.1049 1.0243 -0.0544 0.0507  -0.0349 1304 PHE A CE1   
631  C  CE2   . PHE A 87  ? 1.0710 1.1704 1.0709 -0.0527 0.0589  -0.0347 1304 PHE A CE2   
632  C  CZ    . PHE A 87  ? 1.0112 1.1115 1.0198 -0.0499 0.0537  -0.0381 1304 PHE A CZ    
633  N  N     . ALA A 88  ? 0.9777 1.0297 0.9583 -0.0956 0.0697  0.0016  1305 ALA A N     
634  C  CA    . ALA A 88  ? 1.0016 1.0353 0.9754 -0.1008 0.0690  0.0100  1305 ALA A CA    
635  C  C     . ALA A 88  ? 0.9495 0.9744 0.9076 -0.0988 0.0700  0.0169  1305 ALA A C     
636  O  O     . ALA A 88  ? 0.8645 0.8721 0.8158 -0.0970 0.0658  0.0214  1305 ALA A O     
637  C  CB    . ALA A 88  ? 1.0257 1.0623 1.0075 -0.1123 0.0737  0.0138  1305 ALA A CB    
638  N  N     . PRO A 89  ? 0.9740 1.0099 0.9258 -0.0986 0.0752  0.0179  1306 PRO A N     
639  C  CA    . PRO A 89  ? 0.9200 0.9475 0.8560 -0.0969 0.0757  0.0246  1306 PRO A CA    
640  C  C     . PRO A 89  ? 0.8964 0.9149 0.8250 -0.0873 0.0693  0.0220  1306 PRO A C     
641  O  O     . PRO A 89  ? 0.9177 0.9285 0.8338 -0.0858 0.0686  0.0273  1306 PRO A O     
642  C  CB    . PRO A 89  ? 0.8422 0.8873 0.7747 -0.0985 0.0829  0.0239  1306 PRO A CB    
643  C  CG    . PRO A 89  ? 0.8081 0.8672 0.7549 -0.1054 0.0877  0.0213  1306 PRO A CG    
644  C  CD    . PRO A 89  ? 0.9078 0.9650 0.8664 -0.1013 0.0817  0.0139  1306 PRO A CD    
645  N  N     . GLU A 90  ? 0.8404 0.8600 0.7763 -0.0810 0.0646  0.0145  1307 GLU A N     
646  C  CA    . GLU A 90  ? 0.7618 0.7736 0.6924 -0.0723 0.0589  0.0119  1307 GLU A CA    
647  C  C     . GLU A 90  ? 0.7088 0.7040 0.6399 -0.0709 0.0531  0.0144  1307 GLU A C     
648  O  O     . GLU A 90  ? 0.8042 0.7930 0.7324 -0.0641 0.0484  0.0125  1307 GLU A O     
649  C  CB    . GLU A 90  ? 0.8416 0.8648 0.7794 -0.0656 0.0577  0.0027  1307 GLU A CB    
650  C  CG    . GLU A 90  ? 0.9025 0.9407 0.8379 -0.0639 0.0623  -0.0012 1307 GLU A CG    
651  C  CD    . GLU A 90  ? 0.8988 0.9457 0.8408 -0.0560 0.0602  -0.0102 1307 GLU A CD    
652  O  OE1   . GLU A 90  ? 0.8803 0.9248 0.8306 -0.0529 0.0560  -0.0134 1307 GLU A OE1   
653  O  OE2   . GLU A 90  ? 0.8128 0.8689 0.7514 -0.0525 0.0627  -0.0141 1307 GLU A OE2   
654  N  N     . VAL A 91  ? 0.6636 0.6519 0.5989 -0.0771 0.0534  0.0183  1308 VAL A N     
655  C  CA    . VAL A 91  ? 0.5745 0.5481 0.5115 -0.0756 0.0481  0.0195  1308 VAL A CA    
656  C  C     . VAL A 91  ? 0.6056 0.5643 0.5326 -0.0763 0.0467  0.0276  1308 VAL A C     
657  O  O     . VAL A 91  ? 0.4597 0.4159 0.3828 -0.0825 0.0502  0.0343  1308 VAL A O     
658  C  CB    . VAL A 91  ? 0.5872 0.5611 0.5350 -0.0815 0.0486  0.0180  1308 VAL A CB    
659  C  CG1   . VAL A 91  ? 0.4979 0.4564 0.4467 -0.0799 0.0435  0.0188  1308 VAL A CG1   
660  C  CG2   . VAL A 91  ? 0.6043 0.5942 0.5623 -0.0802 0.0494  0.0097  1308 VAL A CG2   
661  N  N     . ALA A 92  ? 0.6122 0.5615 0.5356 -0.0699 0.0416  0.0275  1309 ALA A N     
662  C  CA    . ALA A 92  ? 0.5715 0.5069 0.4868 -0.0694 0.0392  0.0346  1309 ALA A CA    
663  C  C     . ALA A 92  ? 0.6520 0.5748 0.5725 -0.0711 0.0365  0.0362  1309 ALA A C     
664  O  O     . ALA A 92  ? 0.7240 0.6459 0.6509 -0.0676 0.0335  0.0307  1309 ALA A O     
665  C  CB    . ALA A 92  ? 0.5568 0.4896 0.4662 -0.0618 0.0351  0.0335  1309 ALA A CB    
666  N  N     . TRP A 93  ? 0.6917 0.6044 0.6088 -0.0760 0.0375  0.0436  1310 TRP A N     
667  C  CA    . TRP A 93  ? 0.6016 0.5018 0.5241 -0.0787 0.0357  0.0452  1310 TRP A CA    
668  C  C     . TRP A 93  ? 0.6560 0.5417 0.5724 -0.0745 0.0316  0.0506  1310 TRP A C     
669  O  O     . TRP A 93  ? 0.7100 0.5911 0.6178 -0.0756 0.0323  0.0582  1310 TRP A O     
670  C  CB    . TRP A 93  ? 0.5229 0.4218 0.4484 -0.0881 0.0401  0.0497  1310 TRP A CB    
671  C  CG    . TRP A 93  ? 0.5928 0.5060 0.5278 -0.0926 0.0436  0.0434  1310 TRP A CG    
672  C  CD1   . TRP A 93  ? 0.4789 0.4065 0.4137 -0.0966 0.0490  0.0436  1310 TRP A CD1   
673  C  CD2   . TRP A 93  ? 0.4709 0.3865 0.4171 -0.0931 0.0417  0.0357  1310 TRP A CD2   
674  N  NE1   . TRP A 93  ? 0.4730 0.4119 0.4192 -0.0994 0.0504  0.0365  1310 TRP A NE1   
675  C  CE2   . TRP A 93  ? 0.4682 0.3998 0.4213 -0.0974 0.0458  0.0317  1310 TRP A CE2   
676  C  CE3   . TRP A 93  ? 0.4676 0.3740 0.4186 -0.0900 0.0370  0.0316  1310 TRP A CE3   
677  C  CZ2   . TRP A 93  ? 0.4625 0.4010 0.4270 -0.0988 0.0447  0.0239  1310 TRP A CZ2   
678  C  CZ3   . TRP A 93  ? 0.4749 0.3881 0.4363 -0.0914 0.0360  0.0237  1310 TRP A CZ3   
679  C  CH2   . TRP A 93  ? 0.4746 0.4037 0.4427 -0.0958 0.0396  0.0200  1310 TRP A CH2   
680  N  N     . VAL A 94  ? 0.6889 0.5680 0.6095 -0.0696 0.0273  0.0467  1311 VAL A N     
681  C  CA    . VAL A 94  ? 0.7562 0.6207 0.6736 -0.0666 0.0237  0.0516  1311 VAL A CA    
682  C  C     . VAL A 94  ? 0.7033 0.5562 0.6247 -0.0727 0.0246  0.0552  1311 VAL A C     
683  O  O     . VAL A 94  ? 0.6756 0.5284 0.6057 -0.0755 0.0249  0.0498  1311 VAL A O     
684  C  CB    . VAL A 94  ? 0.6858 0.5480 0.6063 -0.0590 0.0194  0.0464  1311 VAL A CB    
685  C  CG1   . VAL A 94  ? 0.6304 0.4778 0.5492 -0.0559 0.0159  0.0509  1311 VAL A CG1   
686  C  CG2   . VAL A 94  ? 0.6601 0.5316 0.5766 -0.0535 0.0184  0.0442  1311 VAL A CG2   
687  N  N     . THR A 95  ? 0.6665 0.5096 0.5817 -0.0749 0.0249  0.0642  1312 THR A N     
688  C  CA    . THR A 95  ? 0.7017 0.5316 0.6205 -0.0806 0.0256  0.0688  1312 THR A CA    
689  C  C     . THR A 95  ? 0.8015 0.6146 0.7185 -0.0759 0.0211  0.0731  1312 THR A C     
690  O  O     . THR A 95  ? 1.0035 0.8036 0.9257 -0.0790 0.0204  0.0745  1312 THR A O     
691  C  CB    . THR A 95  ? 0.5798 0.4113 0.4936 -0.0884 0.0304  0.0771  1312 THR A CB    
692  O  OG1   . THR A 95  ? 0.6956 0.5221 0.5980 -0.0852 0.0291  0.0859  1312 THR A OG1   
693  C  CG2   . THR A 95  ? 0.5211 0.3711 0.4354 -0.0913 0.0349  0.0730  1312 THR A CG2   
694  N  N     . LYS A 96  ? 0.6281 0.4414 0.5393 -0.0683 0.0176  0.0743  1313 LYS A N     
695  C  CA    . LYS A 96  ? 0.5950 0.3940 0.5035 -0.0638 0.0136  0.0801  1313 LYS A CA    
696  C  C     . LYS A 96  ? 0.5179 0.3187 0.4283 -0.0548 0.0094  0.0745  1313 LYS A C     
697  O  O     . LYS A 96  ? 0.7764 0.5896 0.6847 -0.0516 0.0093  0.0707  1313 LYS A O     
698  C  CB    . LYS A 96  ? 0.5671 0.3645 0.4643 -0.0639 0.0136  0.0905  1313 LYS A CB    
699  C  CG    . LYS A 96  ? 0.7258 0.5094 0.6213 -0.0696 0.0149  0.1000  1313 LYS A CG    
700  C  CD    . LYS A 96  ? 0.7626 0.5429 0.6462 -0.0678 0.0135  0.1108  1313 LYS A CD    
701  C  CE    . LYS A 96  ? 0.7701 0.5651 0.6447 -0.0712 0.0175  0.1131  1313 LYS A CE    
702  N  NZ    . LYS A 96  ? 0.8704 0.6660 0.7334 -0.0660 0.0142  0.1198  1313 LYS A NZ    
703  N  N     . SER A 97  ? 0.5414 0.3299 0.4561 -0.0508 0.0060  0.0741  1314 SER A N     
704  C  CA    . SER A 97  ? 0.6171 0.4067 0.5334 -0.0421 0.0021  0.0705  1314 SER A CA    
705  C  C     . SER A 97  ? 0.6777 0.4579 0.5888 -0.0381 -0.0013 0.0791  1314 SER A C     
706  O  O     . SER A 97  ? 0.6940 0.4614 0.6086 -0.0349 -0.0040 0.0806  1314 SER A O     
707  C  CB    . SER A 97  ? 0.6449 0.4295 0.5699 -0.0395 0.0009  0.0629  1314 SER A CB    
708  O  OG    . SER A 97  ? 0.5637 0.3317 0.4910 -0.0386 -0.0012 0.0665  1314 SER A OG    
709  N  N     . GLY A 98  ? 0.8053 0.5927 0.7081 -0.0376 -0.0016 0.0841  1315 GLY A N     
710  C  CA    . GLY A 98  ? 0.8456 0.6263 0.7427 -0.0335 -0.0054 0.0921  1315 GLY A CA    
711  C  C     . GLY A 98  ? 0.9139 0.6834 0.8056 -0.0386 -0.0043 0.1020  1315 GLY A C     
712  O  O     . GLY A 98  ? 0.9148 0.6896 0.7983 -0.0435 -0.0015 0.1071  1315 GLY A O     
713  N  N     . ASP A 99  ? 0.9994 0.7529 0.8956 -0.0372 -0.0064 0.1048  1316 ASP A N     
714  C  CA    . ASP A 99  ? 0.8945 0.6335 0.7879 -0.0421 -0.0055 0.1143  1316 ASP A CA    
715  C  C     . ASP A 99  ? 0.9025 0.6370 0.8029 -0.0501 -0.0012 0.1106  1316 ASP A C     
716  O  O     . ASP A 99  ? 0.8182 0.5523 0.7151 -0.0583 0.0029  0.1160  1316 ASP A O     
717  C  CB    . ASP A 99  ? 0.8616 0.5844 0.7583 -0.0356 -0.0106 0.1180  1316 ASP A CB    
718  C  CG    . ASP A 99  ? 1.1162 0.8338 1.0034 -0.0329 -0.0137 0.1297  1316 ASP A CG    
719  O  OD1   . ASP A 99  ? 1.2652 0.9920 1.1423 -0.0363 -0.0118 0.1350  1316 ASP A OD1   
720  O  OD2   . ASP A 99  ? 1.1213 0.8253 1.0111 -0.0273 -0.0181 0.1337  1316 ASP A OD2   
721  N  N     . SER A 100 ? 0.8994 0.6328 0.8096 -0.0478 -0.0020 0.1006  1317 SER A N     
722  C  CA    . SER A 100 ? 0.9764 0.7038 0.8952 -0.0539 0.0004  0.0955  1317 SER A CA    
723  C  C     . SER A 100 ? 0.9771 0.7198 0.8967 -0.0607 0.0052  0.0903  1317 SER A C     
724  O  O     . SER A 100 ? 0.9327 0.6900 0.8526 -0.0575 0.0055  0.0831  1317 SER A O     
725  C  CB    . SER A 100 ? 1.0832 0.8055 1.0108 -0.0473 -0.0028 0.0862  1317 SER A CB    
726  O  OG    . SER A 100 ? 1.1568 0.8916 1.0827 -0.0396 -0.0047 0.0816  1317 SER A OG    
727  N  N     . GLU A 101 ? 1.0675 0.8067 0.9884 -0.0701 0.0091  0.0939  1318 GLU A N     
728  C  CA    . GLU A 101 ? 1.1269 0.8805 1.0508 -0.0768 0.0136  0.0884  1318 GLU A CA    
729  C  C     . GLU A 101 ? 1.1680 0.9214 1.1033 -0.0773 0.0129  0.0768  1318 GLU A C     
730  O  O     . GLU A 101 ? 1.1031 0.8417 1.0446 -0.0772 0.0106  0.0752  1318 GLU A O     
731  C  CB    . GLU A 101 ? 1.2307 0.9817 1.1525 -0.0870 0.0184  0.0970  1318 GLU A CB    
732  N  N     . LEU A 102 ? 1.3723 1.1426 1.3096 -0.0773 0.0145  0.0686  1319 LEU A N     
733  C  CA    . LEU A 102 ? 1.0097 0.7844 0.9554 -0.0753 0.0130  0.0568  1319 LEU A CA    
734  C  C     . LEU A 102 ? 0.8431 0.6159 0.7978 -0.0841 0.0151  0.0527  1319 LEU A C     
735  O  O     . LEU A 102 ? 0.8343 0.6107 0.7894 -0.0925 0.0191  0.0573  1319 LEU A O     
736  C  CB    . LEU A 102 ? 0.9633 0.7570 0.9071 -0.0715 0.0137  0.0508  1319 LEU A CB    
737  C  CG    . LEU A 102 ? 1.0069 0.8030 0.9453 -0.0618 0.0107  0.0508  1319 LEU A CG    
738  C  CD1   . LEU A 102 ? 1.0513 0.8644 0.9896 -0.0590 0.0115  0.0443  1319 LEU A CD1   
739  C  CD2   . LEU A 102 ? 1.0519 0.8368 0.9940 -0.0554 0.0068  0.0474  1319 LEU A CD2   
740  N  N     . ALA A 103 ? 0.7925 0.5608 0.7550 -0.0821 0.0123  0.0435  1320 ALA A N     
741  C  CA    . ALA A 103 ? 0.8711 0.6377 0.8435 -0.0901 0.0132  0.0378  1320 ALA A CA    
742  C  C     . ALA A 103 ? 0.8385 0.6228 0.8130 -0.0969 0.0173  0.0362  1320 ALA A C     
743  O  O     . ALA A 103 ? 0.7279 0.5118 0.7042 -0.1059 0.0210  0.0421  1320 ALA A O     
744  C  CB    . ALA A 103 ? 0.9056 0.6711 0.8841 -0.0853 0.0094  0.0258  1320 ALA A CB    
745  N  N     . GLU A 104 ? 0.8289 0.6292 0.8030 -0.0923 0.0168  0.0290  1321 GLU A N     
746  C  CA    . GLU A 104 ? 0.6155 0.4334 0.5903 -0.0969 0.0206  0.0284  1321 GLU A CA    
747  C  C     . GLU A 104 ? 0.6554 0.4820 0.6202 -0.0914 0.0218  0.0334  1321 GLU A C     
748  O  O     . GLU A 104 ? 0.5046 0.3281 0.4640 -0.0830 0.0189  0.0334  1321 GLU A O     
749  C  CB    . GLU A 104 ? 0.5093 0.3404 0.4914 -0.0960 0.0191  0.0166  1321 GLU A CB    
750  N  N     . PRO A 105 ? 0.6967 0.5337 0.6589 -0.0962 0.0262  0.0379  1322 PRO A N     
751  C  CA    . PRO A 105 ? 0.7569 0.6042 0.7102 -0.0908 0.0271  0.0404  1322 PRO A CA    
752  C  C     . PRO A 105 ? 0.6650 0.5267 0.6209 -0.0853 0.0258  0.0313  1322 PRO A C     
753  O  O     . PRO A 105 ? 0.7299 0.5991 0.6941 -0.0877 0.0257  0.0240  1322 PRO A O     
754  C  CB    . PRO A 105 ? 0.7548 0.6098 0.7058 -0.0981 0.0326  0.0466  1322 PRO A CB    
755  C  CG    . PRO A 105 ? 0.7874 0.6331 0.7451 -0.1074 0.0346  0.0496  1322 PRO A CG    
756  C  CD    . PRO A 105 ? 0.6894 0.5293 0.6567 -0.1068 0.0307  0.0410  1322 PRO A CD    
757  N  N     . ILE A 106 ? 0.5454 0.4110 0.4943 -0.0780 0.0244  0.0320  1323 ILE A N     
758  C  CA    . ILE A 106 ? 0.5637 0.4418 0.5141 -0.0724 0.0232  0.0248  1323 ILE A CA    
759  C  C     . ILE A 106 ? 0.6039 0.4939 0.5493 -0.0713 0.0258  0.0266  1323 ILE A C     
760  O  O     . ILE A 106 ? 0.6303 0.5174 0.5683 -0.0719 0.0271  0.0333  1323 ILE A O     
761  C  CB    . ILE A 106 ? 0.5269 0.3991 0.4755 -0.0640 0.0189  0.0223  1323 ILE A CB    
762  C  CG1   . ILE A 106 ? 0.5468 0.4131 0.4872 -0.0597 0.0179  0.0288  1323 ILE A CG1   
763  C  CG2   . ILE A 106 ? 0.5769 0.4368 0.5299 -0.0647 0.0165  0.0203  1323 ILE A CG2   
764  C  CD1   . ILE A 106 ? 0.6282 0.4860 0.5682 -0.0530 0.0141  0.0278  1323 ILE A CD1   
765  N  N     . ALA A 107 ? 0.6759 0.5794 0.6250 -0.0693 0.0261  0.0202  1324 ALA A N     
766  C  CA    . ALA A 107 ? 0.7148 0.6305 0.6606 -0.0680 0.0285  0.0201  1324 ALA A CA    
767  C  C     . ALA A 107 ? 0.6425 0.5606 0.5855 -0.0595 0.0255  0.0172  1324 ALA A C     
768  O  O     . ALA A 107 ? 0.5859 0.5022 0.5322 -0.0554 0.0225  0.0132  1324 ALA A O     
769  C  CB    . ALA A 107 ? 0.7428 0.6730 0.6962 -0.0720 0.0314  0.0151  1324 ALA A CB    
770  N  N     . VAL A 108 ? 0.6279 0.5495 0.5647 -0.0569 0.0263  0.0195  1325 VAL A N     
771  C  CA    . VAL A 108 ? 0.6200 0.5450 0.5554 -0.0496 0.0239  0.0165  1325 VAL A CA    
772  C  C     . VAL A 108 ? 0.5761 0.5143 0.5171 -0.0484 0.0250  0.0103  1325 VAL A C     
773  O  O     . VAL A 108 ? 0.6169 0.5642 0.5592 -0.0520 0.0284  0.0095  1325 VAL A O     
774  C  CB    . VAL A 108 ? 0.6000 0.5238 0.5274 -0.0473 0.0238  0.0202  1325 VAL A CB    
775  C  CG1   . VAL A 108 ? 0.6021 0.5245 0.5290 -0.0403 0.0204  0.0183  1325 VAL A CG1   
776  C  CG2   . VAL A 108 ? 0.5100 0.4238 0.4316 -0.0505 0.0240  0.0273  1325 VAL A CG2   
777  N  N     . ARG A 109 ? 0.5261 0.4660 0.4703 -0.0429 0.0221  0.0062  1326 ARG A N     
778  C  CA    . ARG A 109 ? 0.5442 0.4962 0.4945 -0.0413 0.0224  0.0004  1326 ARG A CA    
779  C  C     . ARG A 109 ? 0.5878 0.5490 0.5368 -0.0402 0.0247  -0.0007 1326 ARG A C     
780  O  O     . ARG A 109 ? 0.5713 0.5290 0.5143 -0.0377 0.0245  0.0016  1326 ARG A O     
781  C  CB    . ARG A 109 ? 0.3872 0.3388 0.3392 -0.0346 0.0188  -0.0025 1326 ARG A CB    
782  C  CG    . ARG A 109 ? 0.3832 0.3320 0.3310 -0.0289 0.0174  -0.0009 1326 ARG A CG    
783  C  CD    . ARG A 109 ? 0.4375 0.3856 0.3869 -0.0230 0.0144  -0.0026 1326 ARG A CD    
784  N  NE    . ARG A 109 ? 0.5624 0.5020 0.5076 -0.0197 0.0128  0.0011  1326 ARG A NE    
785  C  CZ    . ARG A 109 ? 0.6890 0.6248 0.6342 -0.0159 0.0108  0.0016  1326 ARG A CZ    
786  N  NH1   . ARG A 109 ? 0.7163 0.6558 0.6644 -0.0145 0.0098  -0.0015 1326 ARG A NH1   
787  N  NH2   . ARG A 109 ? 0.3743 0.3037 0.3169 -0.0134 0.0098  0.0049  1326 ARG A NH2   
788  N  N     . PRO A 110 ? 0.6122 0.5855 0.5668 -0.0422 0.0271  -0.0046 1327 PRO A N     
789  C  CA    . PRO A 110 ? 0.7587 0.7416 0.7129 -0.0397 0.0291  -0.0070 1327 PRO A CA    
790  C  C     . PRO A 110 ? 0.8165 0.8076 0.7767 -0.0337 0.0270  -0.0125 1327 PRO A C     
791  O  O     . PRO A 110 ? 0.8349 0.8322 0.7954 -0.0296 0.0275  -0.0152 1327 PRO A O     
792  C  CB    . PRO A 110 ? 0.6540 0.6455 0.6104 -0.0467 0.0340  -0.0067 1327 PRO A CB    
793  C  CG    . PRO A 110 ? 0.3980 0.3885 0.3609 -0.0517 0.0335  -0.0071 1327 PRO A CG    
794  C  CD    . PRO A 110 ? 0.3954 0.3738 0.3566 -0.0485 0.0289  -0.0061 1327 PRO A CD    
795  N  N     . THR A 111 ? 0.7093 0.7001 0.6743 -0.0330 0.0243  -0.0143 1328 THR A N     
796  C  CA    . THR A 111 ? 0.6110 0.6084 0.5814 -0.0274 0.0214  -0.0186 1328 THR A CA    
797  C  C     . THR A 111 ? 0.5638 0.5586 0.5370 -0.0294 0.0190  -0.0194 1328 THR A C     
798  O  O     . THR A 111 ? 0.7586 0.7484 0.7314 -0.0355 0.0203  -0.0176 1328 THR A O     
799  C  CB    . THR A 111 ? 0.5205 0.5331 0.4977 -0.0266 0.0232  -0.0234 1328 THR A CB    
800  O  OG1   . THR A 111 ? 0.4977 0.5160 0.4799 -0.0209 0.0197  -0.0270 1328 THR A OG1   
801  C  CG2   . THR A 111 ? 0.5076 0.5281 0.4898 -0.0346 0.0268  -0.0244 1328 THR A CG2   
802  N  N     . SER A 112 ? 0.3730 0.3708 0.3487 -0.0241 0.0155  -0.0221 1329 SER A N     
803  C  CA    . SER A 112 ? 0.3743 0.3676 0.3502 -0.0249 0.0129  -0.0229 1329 SER A CA    
804  C  C     . SER A 112 ? 0.5014 0.5061 0.4849 -0.0255 0.0109  -0.0286 1329 SER A C     
805  O  O     . SER A 112 ? 0.4119 0.4138 0.3953 -0.0252 0.0081  -0.0304 1329 SER A O     
806  C  CB    . SER A 112 ? 0.3720 0.3577 0.3425 -0.0183 0.0100  -0.0207 1329 SER A CB    
807  O  OG    . SER A 112 ? 0.4663 0.4448 0.4317 -0.0166 0.0112  -0.0165 1329 SER A OG    
808  N  N     . GLU A 113 ? 0.4704 0.4882 0.4609 -0.0269 0.0124  -0.0320 1330 GLU A N     
809  C  CA    . GLU A 113 ? 0.5698 0.5997 0.5685 -0.0277 0.0101  -0.0378 1330 GLU A CA    
810  C  C     . GLU A 113 ? 0.6290 0.6550 0.6302 -0.0347 0.0096  -0.0394 1330 GLU A C     
811  O  O     . GLU A 113 ? 0.5790 0.6066 0.5818 -0.0332 0.0056  -0.0432 1330 GLU A O     
812  C  CB    . GLU A 113 ? 0.6186 0.6635 0.6254 -0.0291 0.0126  -0.0409 1330 GLU A CB    
813  C  CG    . GLU A 113 ? 0.7756 0.8277 0.7832 -0.0203 0.0108  -0.0422 1330 GLU A CG    
814  C  CD    . GLU A 113 ? 0.7170 0.7655 0.7203 -0.0183 0.0141  -0.0392 1330 GLU A CD    
815  O  OE1   . GLU A 113 ? 0.6624 0.7188 0.6688 -0.0125 0.0138  -0.0414 1330 GLU A OE1   
816  O  OE2   . GLU A 113 ? 0.6783 0.7159 0.6752 -0.0225 0.0168  -0.0350 1330 GLU A OE2   
817  N  N     . THR A 114 ? 0.6517 0.6719 0.6528 -0.0424 0.0135  -0.0365 1331 THR A N     
818  C  CA    . THR A 114 ? 0.6840 0.6983 0.6881 -0.0501 0.0136  -0.0373 1331 THR A CA    
819  C  C     . THR A 114 ? 0.7160 0.7185 0.7151 -0.0474 0.0099  -0.0376 1331 THR A C     
820  O  O     . THR A 114 ? 0.6614 0.6607 0.6643 -0.0522 0.0085  -0.0407 1331 THR A O     
821  C  CB    . THR A 114 ? 0.7005 0.7064 0.7016 -0.0566 0.0184  -0.0314 1331 THR A CB    
822  O  OG1   . THR A 114 ? 0.8465 0.8436 0.8379 -0.0515 0.0191  -0.0261 1331 THR A OG1   
823  C  CG2   . THR A 114 ? 0.5872 0.6061 0.5952 -0.0620 0.0228  -0.0320 1331 THR A CG2   
824  N  N     . VAL A 115 ? 0.7064 0.7025 0.6974 -0.0400 0.0084  -0.0348 1332 VAL A N     
825  C  CA    . VAL A 115 ? 0.5757 0.5604 0.5609 -0.0371 0.0059  -0.0342 1332 VAL A CA    
826  C  C     . VAL A 115 ? 0.5886 0.5788 0.5719 -0.0293 0.0019  -0.0373 1332 VAL A C     
827  O  O     . VAL A 115 ? 0.6116 0.5988 0.5934 -0.0279 -0.0010 -0.0405 1332 VAL A O     
828  C  CB    . VAL A 115 ? 0.5116 0.4837 0.4891 -0.0358 0.0079  -0.0272 1332 VAL A CB    
829  C  CG1   . VAL A 115 ? 0.4960 0.4591 0.4678 -0.0308 0.0055  -0.0265 1332 VAL A CG1   
830  C  CG2   . VAL A 115 ? 0.4043 0.3694 0.3829 -0.0438 0.0112  -0.0240 1332 VAL A CG2   
831  N  N     . MET A 116 ? 0.5244 0.5223 0.5070 -0.0238 0.0016  -0.0363 1333 MET A N     
832  C  CA    . MET A 116 ? 0.4390 0.4420 0.4191 -0.0161 -0.0020 -0.0379 1333 MET A CA    
833  C  C     . MET A 116 ? 0.5503 0.5665 0.5370 -0.0163 -0.0054 -0.0449 1333 MET A C     
834  O  O     . MET A 116 ? 0.5339 0.5526 0.5176 -0.0114 -0.0091 -0.0473 1333 MET A O     
835  C  CB    . MET A 116 ? 0.4426 0.4481 0.4206 -0.0102 -0.0013 -0.0342 1333 MET A CB    
836  C  CG    . MET A 116 ? 0.6166 0.6099 0.5878 -0.0085 0.0008  -0.0278 1333 MET A CG    
837  S  SD    . MET A 116 ? 0.7386 0.7342 0.7083 -0.0012 0.0008  -0.0244 1333 MET A SD    
838  C  CE    . MET A 116 ? 0.7324 0.7326 0.6997 0.0063  -0.0035 -0.0253 1333 MET A CE    
839  N  N     . TYR A 117 ? 0.5548 0.5803 0.5504 -0.0219 -0.0042 -0.0482 1334 TYR A N     
840  C  CA    . TYR A 117 ? 0.6113 0.6513 0.6143 -0.0216 -0.0079 -0.0551 1334 TYR A CA    
841  C  C     . TYR A 117 ? 0.6870 0.7249 0.6917 -0.0258 -0.0107 -0.0605 1334 TYR A C     
842  O  O     . TYR A 117 ? 0.7983 0.8454 0.8046 -0.0225 -0.0154 -0.0661 1334 TYR A O     
843  C  CB    . TYR A 117 ? 0.5579 0.6108 0.5713 -0.0260 -0.0057 -0.0574 1334 TYR A CB    
844  C  CG    . TYR A 117 ? 0.5318 0.5888 0.5441 -0.0203 -0.0040 -0.0539 1334 TYR A CG    
845  C  CD1   . TYR A 117 ? 0.6675 0.7178 0.6712 -0.0121 -0.0053 -0.0497 1334 TYR A CD1   
846  C  CD2   . TYR A 117 ? 0.4815 0.5492 0.5017 -0.0230 -0.0009 -0.0551 1334 TYR A CD2   
847  C  CE1   . TYR A 117 ? 0.6573 0.7096 0.6603 -0.0070 -0.0041 -0.0469 1334 TYR A CE1   
848  C  CE2   . TYR A 117 ? 0.4765 0.5474 0.4957 -0.0172 0.0005  -0.0529 1334 TYR A CE2   
849  C  CZ    . TYR A 117 ? 0.5853 0.6476 0.5959 -0.0092 -0.0013 -0.0489 1334 TYR A CZ    
850  O  OH    . TYR A 117 ? 0.6153 0.6788 0.6252 -0.0035 -0.0002 -0.0468 1334 TYR A OH    
851  N  N     . PRO A 118 ? 0.6554 0.6816 0.6599 -0.0326 -0.0083 -0.0595 1335 PRO A N     
852  C  CA    . PRO A 118 ? 0.6640 0.6850 0.6685 -0.0349 -0.0114 -0.0648 1335 PRO A CA    
853  C  C     . PRO A 118 ? 0.6746 0.6915 0.6693 -0.0267 -0.0146 -0.0651 1335 PRO A C     
854  O  O     . PRO A 118 ? 0.6904 0.7121 0.6855 -0.0252 -0.0190 -0.0718 1335 PRO A O     
855  C  CB    . PRO A 118 ? 0.6257 0.6319 0.6302 -0.0423 -0.0076 -0.0613 1335 PRO A CB    
856  C  CG    . PRO A 118 ? 0.5798 0.5903 0.5890 -0.0469 -0.0032 -0.0572 1335 PRO A CG    
857  C  CD    . PRO A 118 ? 0.5798 0.5986 0.5858 -0.0394 -0.0031 -0.0546 1335 PRO A CD    
858  N  N     . ALA A 119 ? 0.6335 0.6420 0.6197 -0.0215 -0.0125 -0.0581 1336 ALA A N     
859  C  CA    . ALA A 119 ? 0.6052 0.6119 0.5823 -0.0134 -0.0148 -0.0574 1336 ALA A CA    
860  C  C     . ALA A 119 ? 0.6670 0.6880 0.6440 -0.0072 -0.0187 -0.0602 1336 ALA A C     
861  O  O     . ALA A 119 ? 0.6418 0.6656 0.6133 -0.0021 -0.0220 -0.0631 1336 ALA A O     
862  C  CB    . ALA A 119 ? 0.5384 0.5355 0.5084 -0.0096 -0.0115 -0.0490 1336 ALA A CB    
863  N  N     . TYR A 120 ? 0.6678 0.6983 0.6501 -0.0067 -0.0183 -0.0590 1337 TYR A N     
864  C  CA    . TYR A 120 ? 0.6045 0.6491 0.5877 -0.0005 -0.0225 -0.0616 1337 TYR A CA    
865  C  C     . TYR A 120 ? 0.6039 0.6587 0.5921 -0.0027 -0.0272 -0.0707 1337 TYR A C     
866  O  O     . TYR A 120 ? 0.4418 0.5036 0.4254 0.0034  -0.0318 -0.0735 1337 TYR A O     
867  C  CB    . TYR A 120 ? 0.5788 0.6315 0.5687 -0.0001 -0.0209 -0.0595 1337 TYR A CB    
868  C  CG    . TYR A 120 ? 0.6264 0.6722 0.6102 0.0054  -0.0184 -0.0516 1337 TYR A CG    
869  C  CD1   . TYR A 120 ? 0.5709 0.6034 0.5457 0.0073  -0.0166 -0.0463 1337 TYR A CD1   
870  C  CD2   . TYR A 120 ? 0.5271 0.5799 0.5152 0.0086  -0.0179 -0.0498 1337 TYR A CD2   
871  C  CE1   . TYR A 120 ? 0.5633 0.5898 0.5338 0.0116  -0.0146 -0.0395 1337 TYR A CE1   
872  C  CE2   . TYR A 120 ? 0.4395 0.4852 0.4228 0.0132  -0.0160 -0.0434 1337 TYR A CE2   
873  C  CZ    . TYR A 120 ? 0.5448 0.5773 0.5195 0.0144  -0.0144 -0.0381 1337 TYR A CZ    
874  O  OH    . TYR A 120 ? 0.6544 0.6796 0.6252 0.0185  -0.0126 -0.0318 1337 TYR A OH    
875  N  N     . ALA A 121 ? 0.5902 0.6457 0.5877 -0.0116 -0.0262 -0.0753 1338 ALA A N     
876  C  CA    . ALA A 121 ? 0.4578 0.5220 0.4615 -0.0151 -0.0308 -0.0847 1338 ALA A CA    
877  C  C     . ALA A 121 ? 0.4140 0.4711 0.4092 -0.0125 -0.0336 -0.0882 1338 ALA A C     
878  O  O     . ALA A 121 ? 0.4196 0.4863 0.4140 -0.0095 -0.0390 -0.0951 1338 ALA A O     
879  C  CB    . ALA A 121 ? 0.4475 0.5107 0.4628 -0.0262 -0.0281 -0.0876 1338 ALA A CB    
880  N  N     . LYS A 122 ? 0.5695 0.6106 0.5577 -0.0128 -0.0300 -0.0836 1339 LYS A N     
881  C  CA    . LYS A 122 ? 0.6685 0.7031 0.6483 -0.0094 -0.0321 -0.0868 1339 LYS A CA    
882  C  C     . LYS A 122 ? 0.6463 0.6867 0.6153 0.0010  -0.0342 -0.0841 1339 LYS A C     
883  O  O     . LYS A 122 ? 0.8166 0.8602 0.7797 0.0049  -0.0378 -0.0894 1339 LYS A O     
884  C  CB    . LYS A 122 ? 0.7042 0.7208 0.6804 -0.0121 -0.0276 -0.0824 1339 LYS A CB    
885  C  CG    . LYS A 122 ? 0.8827 0.8914 0.8682 -0.0223 -0.0259 -0.0850 1339 LYS A CG    
886  C  CD    . LYS A 122 ? 0.9517 0.9428 0.9330 -0.0236 -0.0238 -0.0837 1339 LYS A CD    
887  C  CE    . LYS A 122 ? 0.8812 0.8670 0.8696 -0.0307 -0.0260 -0.0924 1339 LYS A CE    
888  N  NZ    . LYS A 122 ? 0.7083 0.6868 0.6909 -0.0269 -0.0284 -0.0984 1339 LYS A NZ    
889  N  N     . TRP A 123 ? 0.5450 0.5872 0.5116 0.0055  -0.0322 -0.0761 1340 TRP A N     
890  C  CA    . TRP A 123 ? 0.5695 0.6140 0.5255 0.0148  -0.0332 -0.0714 1340 TRP A CA    
891  C  C     . TRP A 123 ? 0.4835 0.5441 0.4391 0.0205  -0.0386 -0.0744 1340 TRP A C     
892  O  O     . TRP A 123 ? 0.5132 0.5770 0.4588 0.0277  -0.0409 -0.0734 1340 TRP A O     
893  C  CB    . TRP A 123 ? 0.5957 0.6329 0.5494 0.0170  -0.0286 -0.0610 1340 TRP A CB    
894  C  CG    . TRP A 123 ? 0.5278 0.5500 0.4766 0.0156  -0.0242 -0.0564 1340 TRP A CG    
895  C  CD1   . TRP A 123 ? 0.5745 0.5906 0.5172 0.0166  -0.0241 -0.0587 1340 TRP A CD1   
896  C  CD2   . TRP A 123 ? 0.5162 0.5286 0.4661 0.0135  -0.0196 -0.0492 1340 TRP A CD2   
897  N  NE1   . TRP A 123 ? 0.4905 0.4939 0.4312 0.0153  -0.0197 -0.0530 1340 TRP A NE1   
898  C  CE2   . TRP A 123 ? 0.5650 0.5661 0.5099 0.0132  -0.0171 -0.0471 1340 TRP A CE2   
899  C  CE3   . TRP A 123 ? 0.5969 0.6097 0.5516 0.0120  -0.0175 -0.0448 1340 TRP A CE3   
900  C  CZ2   . TRP A 123 ? 0.6846 0.6751 0.6293 0.0115  -0.0130 -0.0405 1340 TRP A CZ2   
901  C  CZ3   . TRP A 123 ? 0.5270 0.5289 0.4806 0.0102  -0.0134 -0.0387 1340 TRP A CZ3   
902  C  CH2   . TRP A 123 ? 0.6195 0.6107 0.5684 0.0098  -0.0114 -0.0365 1340 TRP A CH2   
903  N  N     . ILE A 124 ? 0.4503 0.5219 0.4162 0.0177  -0.0408 -0.0781 1341 ILE A N     
904  C  CA    . ILE A 124 ? 0.5293 0.6174 0.4958 0.0235  -0.0468 -0.0814 1341 ILE A CA    
905  C  C     . ILE A 124 ? 0.7685 0.8638 0.7367 0.0209  -0.0519 -0.0924 1341 ILE A C     
906  O  O     . ILE A 124 ? 0.8402 0.9419 0.8200 0.0140  -0.0536 -0.0997 1341 ILE A O     
907  C  CB    . ILE A 124 ? 0.4442 0.5426 0.4219 0.0226  -0.0472 -0.0811 1341 ILE A CB    
908  C  CG1   . ILE A 124 ? 0.4744 0.5633 0.4545 0.0207  -0.0411 -0.0732 1341 ILE A CG1   
909  C  CG2   . ILE A 124 ? 0.4168 0.5285 0.3917 0.0319  -0.0525 -0.0801 1341 ILE A CG2   
910  C  CD1   . ILE A 124 ? 0.5090 0.5920 0.4799 0.0285  -0.0397 -0.0643 1341 ILE A CD1   
911  N  N     . GLN A 125 ? 0.7311 0.8258 0.6877 0.0264  -0.0542 -0.0939 1342 GLN A N     
912  C  CA    . GLN A 125 ? 0.7738 0.8766 0.7305 0.0253  -0.0599 -0.1051 1342 GLN A CA    
913  C  C     . GLN A 125 ? 0.8975 1.0192 0.8541 0.0315  -0.0669 -0.1085 1342 GLN A C     
914  O  O     . GLN A 125 ? 0.9667 1.0992 0.9285 0.0291  -0.0726 -0.1191 1342 GLN A O     
915  C  CB    . GLN A 125 ? 0.8441 0.9382 0.7881 0.0285  -0.0590 -0.1061 1342 GLN A CB    
916  N  N     . SER A 126 ? 0.8738 0.9996 0.8258 0.0391  -0.0669 -0.0998 1343 SER A N     
917  C  CA    . SER A 126 ? 0.7222 0.8650 0.6724 0.0466  -0.0737 -0.1013 1343 SER A CA    
918  C  C     . SER A 126 ? 0.7809 0.9265 0.7347 0.0512  -0.0725 -0.0923 1343 SER A C     
919  O  O     . SER A 126 ? 0.8225 0.9561 0.7774 0.0496  -0.0663 -0.0844 1343 SER A O     
920  C  CB    . SER A 126 ? 0.7174 0.8621 0.6506 0.0551  -0.0765 -0.1000 1343 SER A CB    
921  O  OG    . SER A 126 ? 0.8150 0.9703 0.7435 0.0644  -0.0804 -0.0943 1343 SER A OG    
922  N  N     . TYR A 127 ? 0.7878 0.9497 0.7436 0.0574  -0.0790 -0.0940 1344 TYR A N     
923  C  CA    . TYR A 127 ? 0.6649 0.8288 0.6214 0.0643  -0.0786 -0.0850 1344 TYR A CA    
924  C  C     . TYR A 127 ? 0.6347 0.7865 0.5762 0.0711  -0.0752 -0.0734 1344 TYR A C     
925  O  O     . TYR A 127 ? 0.8243 0.9698 0.7667 0.0744  -0.0721 -0.0645 1344 TYR A O     
926  C  CB    . TYR A 127 ? 0.5794 0.7634 0.5398 0.0708  -0.0870 -0.0890 1344 TYR A CB    
927  N  N     . ARG A 128 ? 0.5445 0.6929 0.4726 0.0733  -0.0756 -0.0737 1345 ARG A N     
928  C  CA    . ARG A 128 ? 0.6245 0.7633 0.5385 0.0797  -0.0723 -0.0627 1345 ARG A CA    
929  C  C     . ARG A 128 ? 0.5786 0.6995 0.4939 0.0750  -0.0640 -0.0555 1345 ARG A C     
930  O  O     . ARG A 128 ? 0.5230 0.6361 0.4315 0.0799  -0.0609 -0.0448 1345 ARG A O     
931  C  CB    . ARG A 128 ? 0.7741 0.9150 0.6738 0.0826  -0.0740 -0.0657 1345 ARG A CB    
932  N  N     . ASP A 129 ? 0.6657 0.7801 0.5902 0.0658  -0.0605 -0.0608 1346 ASP A N     
933  C  CA    . ASP A 129 ? 0.7472 0.8453 0.6727 0.0617  -0.0531 -0.0542 1346 ASP A CA    
934  C  C     . ASP A 129 ? 0.6104 0.7062 0.5443 0.0619  -0.0511 -0.0485 1346 ASP A C     
935  O  O     . ASP A 129 ? 0.4511 0.5346 0.3872 0.0581  -0.0455 -0.0439 1346 ASP A O     
936  C  CB    . ASP A 129 ? 0.8569 0.9473 0.7884 0.0519  -0.0498 -0.0608 1346 ASP A CB    
937  C  CG    . ASP A 129 ? 0.8883 0.9821 0.8152 0.0504  -0.0527 -0.0698 1346 ASP A CG    
938  O  OD1   . ASP A 129 ? 0.9881 1.0829 0.9027 0.0563  -0.0537 -0.0682 1346 ASP A OD1   
939  O  OD2   . ASP A 129 ? 0.8382 0.9326 0.7740 0.0429  -0.0534 -0.0783 1346 ASP A OD2   
940  N  N     . LEU A 130 ? 0.6426 0.7504 0.5816 0.0664  -0.0557 -0.0495 1347 LEU A N     
941  C  CA    . LEU A 130 ? 0.7433 0.8494 0.6916 0.0664  -0.0537 -0.0459 1347 LEU A CA    
942  C  C     . LEU A 130 ? 0.7662 0.8680 0.7085 0.0751  -0.0537 -0.0354 1347 LEU A C     
943  O  O     . LEU A 130 ? 0.8893 0.9965 0.8229 0.0826  -0.0578 -0.0323 1347 LEU A O     
944  C  CB    . LEU A 130 ? 0.7924 0.9145 0.7532 0.0654  -0.0581 -0.0538 1347 LEU A CB    
945  C  CG    . LEU A 130 ? 0.7351 0.8586 0.7052 0.0549  -0.0563 -0.0626 1347 LEU A CG    
946  C  CD1   . LEU A 130 ? 0.7044 0.8407 0.6895 0.0524  -0.0577 -0.0679 1347 LEU A CD1   
947  C  CD2   . LEU A 130 ? 0.7512 0.8576 0.7197 0.0488  -0.0490 -0.0583 1347 LEU A CD2   
948  N  N     . PRO A 131 ? 0.6303 0.7221 0.5769 0.0743  -0.0494 -0.0298 1348 PRO A N     
949  C  CA    . PRO A 131 ? 0.6286 0.7148 0.5848 0.0666  -0.0447 -0.0325 1348 PRO A CA    
950  C  C     . PRO A 131 ? 0.7089 0.7802 0.6606 0.0604  -0.0388 -0.0298 1348 PRO A C     
951  O  O     . PRO A 131 ? 0.8308 0.8937 0.7728 0.0633  -0.0373 -0.0234 1348 PRO A O     
952  C  CB    . PRO A 131 ? 0.6106 0.6945 0.5718 0.0714  -0.0441 -0.0274 1348 PRO A CB    
953  C  CG    . PRO A 131 ? 0.6720 0.7504 0.6231 0.0794  -0.0455 -0.0184 1348 PRO A CG    
954  C  CD    . PRO A 131 ? 0.6413 0.7285 0.5840 0.0825  -0.0499 -0.0204 1348 PRO A CD    
955  N  N     . ILE A 132 ? 0.6538 0.7222 0.6126 0.0522  -0.0354 -0.0342 1349 ILE A N     
956  C  CA    . ILE A 132 ? 0.6480 0.7020 0.6038 0.0468  -0.0300 -0.0310 1349 ILE A CA    
957  C  C     . ILE A 132 ? 0.6012 0.6489 0.5619 0.0463  -0.0266 -0.0270 1349 ILE A C     
958  O  O     . ILE A 132 ? 0.5258 0.5798 0.4956 0.0436  -0.0263 -0.0311 1349 ILE A O     
959  C  CB    . ILE A 132 ? 0.6732 0.7265 0.6324 0.0382  -0.0285 -0.0376 1349 ILE A CB    
960  C  CG1   . ILE A 132 ? 0.6411 0.6996 0.5951 0.0390  -0.0321 -0.0425 1349 ILE A CG1   
961  C  CG2   . ILE A 132 ? 0.6472 0.6858 0.6036 0.0334  -0.0233 -0.0338 1349 ILE A CG2   
962  C  CD1   . ILE A 132 ? 0.6147 0.6635 0.5576 0.0410  -0.0302 -0.0383 1349 ILE A CD1   
963  N  N     . ARG A 133 ? 0.5430 0.5791 0.4984 0.0484  -0.0240 -0.0195 1350 ARG A N     
964  C  CA    . ARG A 133 ? 0.4479 0.4776 0.4073 0.0489  -0.0215 -0.0160 1350 ARG A CA    
965  C  C     . ARG A 133 ? 0.5277 0.5438 0.4832 0.0447  -0.0171 -0.0118 1350 ARG A C     
966  O  O     . ARG A 133 ? 0.5275 0.5361 0.4768 0.0475  -0.0163 -0.0056 1350 ARG A O     
967  C  CB    . ARG A 133 ? 0.4905 0.5208 0.4489 0.0574  -0.0240 -0.0108 1350 ARG A CB    
968  C  CG    . ARG A 133 ? 0.6668 0.7105 0.6260 0.0632  -0.0294 -0.0135 1350 ARG A CG    
969  C  CD    . ARG A 133 ? 0.8220 0.8639 0.7792 0.0719  -0.0318 -0.0068 1350 ARG A CD    
970  N  NE    . ARG A 133 ? 0.8633 0.9045 0.8293 0.0733  -0.0312 -0.0078 1350 ARG A NE    
971  C  CZ    . ARG A 133 ? 0.8394 0.8702 0.8054 0.0769  -0.0300 -0.0018 1350 ARG A CZ    
972  N  NH1   . ARG A 133 ? 0.8663 0.8867 0.8245 0.0789  -0.0291 0.0064  1350 ARG A NH1   
973  N  NH2   . ARG A 133 ? 0.7896 0.8205 0.7639 0.0783  -0.0295 -0.0042 1350 ARG A NH2   
974  N  N     . LEU A 134 ? 0.6737 0.6873 0.6329 0.0378  -0.0143 -0.0151 1351 LEU A N     
975  C  CA    . LEU A 134 ? 0.6062 0.6083 0.5620 0.0335  -0.0108 -0.0121 1351 LEU A CA    
976  C  C     . LEU A 134 ? 0.5894 0.5861 0.5490 0.0311  -0.0080 -0.0109 1351 LEU A C     
977  O  O     . LEU A 134 ? 0.5397 0.5425 0.5052 0.0307  -0.0081 -0.0144 1351 LEU A O     
978  C  CB    . LEU A 134 ? 0.4334 0.4359 0.3888 0.0274  -0.0101 -0.0165 1351 LEU A CB    
979  C  CG    . LEU A 134 ? 0.4101 0.4158 0.3600 0.0302  -0.0125 -0.0176 1351 LEU A CG    
980  C  CD1   . LEU A 134 ? 0.4945 0.5016 0.4456 0.0246  -0.0127 -0.0237 1351 LEU A CD1   
981  C  CD2   . LEU A 134 ? 0.3831 0.3803 0.3259 0.0333  -0.0110 -0.0110 1351 LEU A CD2   
982  N  N     . ASN A 135 ? 0.4794 0.4653 0.4356 0.0299  -0.0058 -0.0062 1352 ASN A N     
983  C  CA    . ASN A 135 ? 0.4818 0.4618 0.4403 0.0275  -0.0035 -0.0053 1352 ASN A CA    
984  C  C     . ASN A 135 ? 0.4615 0.4329 0.4168 0.0226  -0.0012 -0.0032 1352 ASN A C     
985  O  O     . ASN A 135 ? 0.3697 0.3372 0.3208 0.0233  -0.0011 -0.0005 1352 ASN A O     
986  C  CB    . ASN A 135 ? 0.4553 0.4307 0.4144 0.0328  -0.0042 -0.0011 1352 ASN A CB    
987  C  CG    . ASN A 135 ? 0.4073 0.3736 0.3669 0.0303  -0.0021 0.0007  1352 ASN A CG    
988  O  OD1   . ASN A 135 ? 0.4006 0.3685 0.3633 0.0278  -0.0009 -0.0028 1352 ASN A OD1   
989  N  ND2   . ASN A 135 ? 0.3727 0.3306 0.3296 0.0309  -0.0015 0.0062  1352 ASN A ND2   
990  N  N     . GLN A 136 ? 0.4022 0.3713 0.3591 0.0181  0.0008  -0.0047 1353 GLN A N     
991  C  CA    . GLN A 136 ? 0.5289 0.4892 0.4829 0.0145  0.0025  -0.0020 1353 GLN A CA    
992  C  C     . GLN A 136 ? 0.6418 0.5983 0.5971 0.0134  0.0037  -0.0013 1353 GLN A C     
993  O  O     . GLN A 136 ? 0.7384 0.6998 0.6963 0.0124  0.0043  -0.0048 1353 GLN A O     
994  C  CB    . GLN A 136 ? 0.5909 0.5507 0.5439 0.0091  0.0035  -0.0040 1353 GLN A CB    
995  C  CG    . GLN A 136 ? 0.6237 0.5906 0.5800 0.0052  0.0040  -0.0087 1353 GLN A CG    
996  C  CD    . GLN A 136 ? 0.5612 0.5243 0.5163 0.0000  0.0049  -0.0093 1353 GLN A CD    
997  O  OE1   . GLN A 136 ? 0.4457 0.4021 0.3975 0.0006  0.0046  -0.0070 1353 GLN A OE1   
998  N  NE2   . GLN A 136 ? 0.5503 0.5174 0.5084 -0.0052 0.0061  -0.0123 1353 GLN A NE2   
999  N  N     . TRP A 137 ? 0.5700 0.5184 0.5234 0.0139  0.0039  0.0027  1354 TRP A N     
1000 C  CA    . TRP A 137 ? 0.6449 0.5886 0.5985 0.0119  0.0047  0.0031  1354 TRP A CA    
1001 C  C     . TRP A 137 ? 0.5940 0.5349 0.5448 0.0068  0.0059  0.0034  1354 TRP A C     
1002 O  O     . TRP A 137 ? 0.7279 0.6644 0.6769 0.0062  0.0058  0.0062  1354 TRP A O     
1003 C  CB    . TRP A 137 ? 0.6435 0.5803 0.5976 0.0143  0.0039  0.0071  1354 TRP A CB    
1004 C  CG    . TRP A 137 ? 0.5849 0.5222 0.5417 0.0193  0.0027  0.0081  1354 TRP A CG    
1005 C  CD1   . TRP A 137 ? 0.5867 0.5240 0.5430 0.0229  0.0020  0.0117  1354 TRP A CD1   
1006 C  CD2   . TRP A 137 ? 0.5996 0.5369 0.5597 0.0216  0.0019  0.0057  1354 TRP A CD2   
1007 N  NE1   . TRP A 137 ? 0.6375 0.5743 0.5966 0.0273  0.0007  0.0125  1354 TRP A NE1   
1008 C  CE2   . TRP A 137 ? 0.6454 0.5818 0.6073 0.0268  0.0005  0.0085  1354 TRP A CE2   
1009 C  CE3   . TRP A 137 ? 0.5869 0.5250 0.5483 0.0202  0.0024  0.0014  1354 TRP A CE3   
1010 C  CZ2   . TRP A 137 ? 0.6740 0.6093 0.6399 0.0306  -0.0007 0.0070  1354 TRP A CZ2   
1011 C  CZ3   . TRP A 137 ? 0.6784 0.6161 0.6435 0.0241  0.0013  -0.0008 1354 TRP A CZ3   
1012 C  CH2   . TRP A 137 ? 0.6954 0.6312 0.6632 0.0293  -0.0003 0.0019  1354 TRP A CH2   
1013 N  N     . ASN A 138 ? 0.4546 0.3981 0.4050 0.0034  0.0071  0.0008  1355 ASN A N     
1014 C  CA    . ASN A 138 ? 0.4312 0.3712 0.3785 -0.0013 0.0081  0.0021  1355 ASN A CA    
1015 C  C     . ASN A 138 ? 0.4847 0.4262 0.4304 -0.0041 0.0094  0.0006  1355 ASN A C     
1016 O  O     . ASN A 138 ? 0.7694 0.7149 0.7167 -0.0023 0.0096  -0.0022 1355 ASN A O     
1017 C  CB    . ASN A 138 ? 0.4779 0.4201 0.4254 -0.0038 0.0086  0.0011  1355 ASN A CB    
1018 C  CG    . ASN A 138 ? 0.5447 0.4958 0.4952 -0.0053 0.0095  -0.0031 1355 ASN A CG    
1019 O  OD1   . ASN A 138 ? 0.4857 0.4408 0.4367 -0.0074 0.0112  -0.0048 1355 ASN A OD1   
1020 N  ND2   . ASN A 138 ? 0.5186 0.4740 0.4714 -0.0042 0.0085  -0.0051 1355 ASN A ND2   
1021 N  N     . ASN A 139 ? 0.3709 0.3092 0.3131 -0.0083 0.0103  0.0025  1356 ASN A N     
1022 C  CA    . ASN A 139 ? 0.4778 0.4176 0.4166 -0.0113 0.0118  0.0020  1356 ASN A CA    
1023 C  C     . ASN A 139 ? 0.5460 0.4902 0.4846 -0.0160 0.0143  0.0013  1356 ASN A C     
1024 O  O     . ASN A 139 ? 0.4029 0.3453 0.3428 -0.0178 0.0142  0.0023  1356 ASN A O     
1025 C  CB    . ASN A 139 ? 0.4026 0.3352 0.3369 -0.0127 0.0107  0.0057  1356 ASN A CB    
1026 C  CG    . ASN A 139 ? 0.4626 0.3899 0.3960 -0.0148 0.0104  0.0092  1356 ASN A CG    
1027 O  OD1   . ASN A 139 ? 0.5178 0.4447 0.4542 -0.0136 0.0101  0.0088  1356 ASN A OD1   
1028 N  ND2   . ASN A 139 ? 0.4586 0.3817 0.3874 -0.0176 0.0104  0.0123  1356 ASN A ND2   
1029 N  N     . VAL A 140 ? 0.5255 0.4761 0.4629 -0.0180 0.0166  -0.0007 1357 VAL A N     
1030 C  CA    . VAL A 140 ? 0.3835 0.3394 0.3214 -0.0231 0.0196  -0.0011 1357 VAL A CA    
1031 C  C     . VAL A 140 ? 0.6131 0.5706 0.5450 -0.0263 0.0220  0.0003  1357 VAL A C     
1032 O  O     . VAL A 140 ? 0.6529 0.6099 0.5812 -0.0238 0.0213  -0.0004 1357 VAL A O     
1033 C  CB    . VAL A 140 ? 0.3807 0.3474 0.3253 -0.0223 0.0209  -0.0060 1357 VAL A CB    
1034 C  CG1   . VAL A 140 ? 0.3757 0.3411 0.3247 -0.0184 0.0179  -0.0071 1357 VAL A CG1   
1035 C  CG2   . VAL A 140 ? 0.4243 0.3985 0.3696 -0.0192 0.0219  -0.0099 1357 VAL A CG2   
1036 N  N     . VAL A 141 ? 0.4973 0.4561 0.4280 -0.0320 0.0249  0.0027  1358 VAL A N     
1037 C  CA    . VAL A 141 ? 0.5264 0.4863 0.4501 -0.0360 0.0276  0.0057  1358 VAL A CA    
1038 C  C     . VAL A 141 ? 0.4809 0.4522 0.4078 -0.0403 0.0323  0.0036  1358 VAL A C     
1039 O  O     . VAL A 141 ? 0.5606 0.5345 0.4942 -0.0430 0.0332  0.0026  1358 VAL A O     
1040 C  CB    . VAL A 141 ? 0.7080 0.6572 0.6268 -0.0394 0.0268  0.0124  1358 VAL A CB    
1041 C  CG1   . VAL A 141 ? 0.8185 0.7696 0.7295 -0.0437 0.0299  0.0163  1358 VAL A CG1   
1042 C  CG2   . VAL A 141 ? 0.4063 0.3461 0.3227 -0.0351 0.0223  0.0143  1358 VAL A CG2   
1043 N  N     . ARG A 142 ? 0.4101 0.3895 0.3331 -0.0404 0.0352  0.0019  1359 ARG A N     
1044 C  CA    . ARG A 142 ? 0.4358 0.4266 0.3608 -0.0453 0.0406  0.0011  1359 ARG A CA    
1045 C  C     . ARG A 142 ? 0.5915 0.5848 0.5063 -0.0474 0.0437  0.0039  1359 ARG A C     
1046 O  O     . ARG A 142 ? 0.5999 0.5950 0.5098 -0.0429 0.0426  0.0009  1359 ARG A O     
1047 C  CB    . ARG A 142 ? 0.5684 0.5719 0.5017 -0.0420 0.0417  -0.0063 1359 ARG A CB    
1048 C  CG    . ARG A 142 ? 0.5686 0.5694 0.5098 -0.0377 0.0376  -0.0094 1359 ARG A CG    
1049 C  CD    . ARG A 142 ? 0.5959 0.6084 0.5435 -0.0330 0.0381  -0.0162 1359 ARG A CD    
1050 N  NE    . ARG A 142 ? 0.5494 0.5624 0.5050 -0.0295 0.0348  -0.0189 1359 ARG A NE    
1051 C  CZ    . ARG A 142 ? 0.7009 0.7247 0.6638 -0.0253 0.0348  -0.0246 1359 ARG A CZ    
1052 N  NH1   . ARG A 142 ? 0.7562 0.7905 0.7196 -0.0245 0.0383  -0.0283 1359 ARG A NH1   
1053 N  NH2   . ARG A 142 ? 0.8544 0.8788 0.8237 -0.0218 0.0313  -0.0265 1359 ARG A NH2   
1054 N  N     . TRP A 143 ? 0.8005 0.7940 0.7120 -0.0543 0.0475  0.0097  1360 TRP A N     
1055 C  CA    . TRP A 143 ? 0.7858 0.7816 0.6862 -0.0568 0.0507  0.0138  1360 TRP A CA    
1056 C  C     . TRP A 143 ? 0.9058 0.9186 0.8071 -0.0572 0.0562  0.0088  1360 TRP A C     
1057 O  O     . TRP A 143 ? 1.0072 1.0280 0.9082 -0.0633 0.0620  0.0117  1360 TRP A O     
1058 C  CB    . TRP A 143 ? 0.7433 0.7319 0.6400 -0.0640 0.0526  0.0228  1360 TRP A CB    
1059 C  CG    . TRP A 143 ? 0.8306 0.8115 0.7144 -0.0636 0.0512  0.0291  1360 TRP A CG    
1060 C  CD1   . TRP A 143 ? 0.9184 0.9041 0.7919 -0.0670 0.0553  0.0340  1360 TRP A CD1   
1061 C  CD2   . TRP A 143 ? 0.8054 0.7734 0.6850 -0.0595 0.0450  0.0315  1360 TRP A CD2   
1062 N  NE1   . TRP A 143 ? 0.8970 0.8732 0.7596 -0.0649 0.0515  0.0393  1360 TRP A NE1   
1063 C  CE2   . TRP A 143 ? 0.8666 0.8320 0.7335 -0.0604 0.0451  0.0377  1360 TRP A CE2   
1064 C  CE3   . TRP A 143 ? 0.8025 0.7616 0.6879 -0.0551 0.0395  0.0293  1360 TRP A CE3   
1065 C  CZ2   . TRP A 143 ? 0.9227 0.8775 0.7837 -0.0569 0.0395  0.0411  1360 TRP A CZ2   
1066 C  CZ3   . TRP A 143 ? 0.8999 0.8488 0.7797 -0.0520 0.0347  0.0327  1360 TRP A CZ3   
1067 C  CH2   . TRP A 143 ? 0.9748 0.9217 0.8430 -0.0528 0.0345  0.0384  1360 TRP A CH2   
1068 N  N     . GLU A 144 ? 0.9389 0.9570 0.8412 -0.0504 0.0545  0.0012  1361 GLU A N     
1069 C  CA    . GLU A 144 ? 0.9651 0.9998 0.8711 -0.0492 0.0591  -0.0055 1361 GLU A CA    
1070 C  C     . GLU A 144 ? 0.7895 0.8326 0.6855 -0.0532 0.0650  -0.0025 1361 GLU A C     
1071 O  O     . GLU A 144 ? 0.6111 0.6474 0.4949 -0.0535 0.0638  0.0022  1361 GLU A O     
1072 C  CB    . GLU A 144 ? 1.0499 1.0866 0.9583 -0.0406 0.0557  -0.0140 1361 GLU A CB    
1073 C  CG    . GLU A 144 ? 1.0178 1.0449 0.9343 -0.0361 0.0496  -0.0158 1361 GLU A CG    
1074 C  CD    . GLU A 144 ? 1.0665 1.1032 0.9949 -0.0318 0.0497  -0.0232 1361 GLU A CD    
1075 O  OE1   . GLU A 144 ? 1.0897 1.1197 1.0238 -0.0274 0.0449  -0.0248 1361 GLU A OE1   
1076 O  OE2   . GLU A 144 ? 1.0738 1.1252 1.0058 -0.0326 0.0546  -0.0272 1361 GLU A OE2   
1077 N  N     . PHE A 145 ? 0.9276 0.9860 0.8289 -0.0564 0.0714  -0.0048 1362 PHE A N     
1078 C  CA    . PHE A 145 ? 1.0257 1.0962 0.9190 -0.0602 0.0784  -0.0029 1362 PHE A CA    
1079 C  C     . PHE A 145 ? 1.0183 1.0983 0.9058 -0.0534 0.0792  -0.0110 1362 PHE A C     
1080 O  O     . PHE A 145 ? 1.1203 1.2140 1.0024 -0.0553 0.0856  -0.0117 1362 PHE A O     
1081 C  CB    . PHE A 145 ? 1.2139 1.2984 1.1174 -0.0668 0.0853  -0.0024 1362 PHE A CB    
1082 C  CG    . PHE A 145 ? 1.5089 1.6020 1.4286 -0.0634 0.0842  -0.0109 1362 PHE A CG    
1083 C  CD1   . PHE A 145 ? 1.6690 1.7812 1.5946 -0.0607 0.0889  -0.0187 1362 PHE A CD1   
1084 C  CD2   . PHE A 145 ? 1.6245 1.7076 1.5535 -0.0627 0.0786  -0.0110 1362 PHE A CD2   
1085 C  CE1   . PHE A 145 ? 1.6543 1.7751 1.5951 -0.0570 0.0875  -0.0262 1362 PHE A CE1   
1086 C  CE2   . PHE A 145 ? 1.6706 1.7623 1.6137 -0.0592 0.0773  -0.0183 1362 PHE A CE2   
1087 C  CZ    . PHE A 145 ? 1.6475 1.7579 1.5966 -0.0563 0.0815  -0.0257 1362 PHE A CZ    
1088 N  N     . LYS A 146 ? 0.9702 1.0443 0.8602 -0.0456 0.0732  -0.0177 1363 LYS A N     
1089 C  CA    . LYS A 146 ? 0.8938 0.9746 0.7793 -0.0387 0.0729  -0.0264 1363 LYS A CA    
1090 C  C     . LYS A 146 ? 0.9976 1.0654 0.8720 -0.0353 0.0669  -0.0254 1363 LYS A C     
1091 O  O     . LYS A 146 ? 0.9921 1.0449 0.8672 -0.0355 0.0612  -0.0209 1363 LYS A O     
1092 C  CB    . LYS A 146 ? 0.8742 0.9589 0.7728 -0.0319 0.0706  -0.0358 1363 LYS A CB    
1093 C  CG    . LYS A 146 ? 0.9126 1.0082 0.8250 -0.0346 0.0743  -0.0368 1363 LYS A CG    
1094 C  CD    . LYS A 146 ? 0.9218 1.0267 0.8450 -0.0268 0.0736  -0.0474 1363 LYS A CD    
1095 C  CE    . LYS A 146 ? 0.9696 1.0786 0.9080 -0.0276 0.0729  -0.0479 1363 LYS A CE    
1096 N  NZ    . LYS A 146 ? 0.9609 1.0732 0.9095 -0.0186 0.0695  -0.0567 1363 LYS A NZ    
1097 N  N     . HIS A 147 ? 1.0205 1.0950 0.8852 -0.0320 0.0681  -0.0305 1364 HIS A N     
1098 C  CA    . HIS A 147 ? 0.8781 0.9424 0.7332 -0.0283 0.0620  -0.0317 1364 HIS A CA    
1099 C  C     . HIS A 147 ? 0.7911 0.8432 0.6561 -0.0233 0.0549  -0.0354 1364 HIS A C     
1100 O  O     . HIS A 147 ? 0.8910 0.9474 0.7663 -0.0186 0.0547  -0.0431 1364 HIS A O     
1101 C  CB    . HIS A 147 ? 0.9297 1.0045 0.7758 -0.0239 0.0639  -0.0402 1364 HIS A CB    
1102 C  CG    . HIS A 147 ? 1.0580 1.1466 0.8932 -0.0283 0.0715  -0.0368 1364 HIS A CG    
1103 N  ND1   . HIS A 147 ? 1.1191 1.2217 0.9471 -0.0249 0.0755  -0.0449 1364 HIS A ND1   
1104 C  CD2   . HIS A 147 ? 1.1060 1.1962 0.9361 -0.0359 0.0762  -0.0260 1364 HIS A CD2   
1105 C  CE1   . HIS A 147 ? 1.1621 1.2754 0.9805 -0.0303 0.0826  -0.0389 1364 HIS A CE1   
1106 N  NE2   . HIS A 147 ? 1.1258 1.2314 0.9455 -0.0373 0.0831  -0.0270 1364 HIS A NE2   
1107 N  N     . PRO A 148 ? 0.7116 0.7490 0.5744 -0.0241 0.0491  -0.0296 1365 PRO A N     
1108 C  CA    . PRO A 148 ? 0.6126 0.6389 0.4843 -0.0197 0.0428  -0.0323 1365 PRO A CA    
1109 C  C     . PRO A 148 ? 0.6450 0.6684 0.5133 -0.0142 0.0383  -0.0399 1365 PRO A C     
1110 O  O     . PRO A 148 ? 0.6725 0.6982 0.5292 -0.0142 0.0379  -0.0409 1365 PRO A O     
1111 C  CB    . PRO A 148 ? 0.5777 0.5912 0.4480 -0.0235 0.0393  -0.0227 1365 PRO A CB    
1112 C  CG    . PRO A 148 ? 0.6307 0.6458 0.4875 -0.0275 0.0412  -0.0167 1365 PRO A CG    
1113 C  CD    . PRO A 148 ? 0.7431 0.7737 0.5961 -0.0293 0.0485  -0.0193 1365 PRO A CD    
1114 N  N     . GLN A 149 ? 0.6797 0.6984 0.5584 -0.0092 0.0349  -0.0455 1366 GLN A N     
1115 C  CA    . GLN A 149 ? 0.7619 0.7752 0.6404 -0.0042 0.0299  -0.0527 1366 GLN A CA    
1116 C  C     . GLN A 149 ? 0.6976 0.6973 0.5850 -0.0029 0.0243  -0.0497 1366 GLN A C     
1117 O  O     . GLN A 149 ? 0.6265 0.6246 0.5226 -0.0033 0.0252  -0.0465 1366 GLN A O     
1118 C  CB    . GLN A 149 ? 0.9111 0.9334 0.7939 0.0013  0.0321  -0.0637 1366 GLN A CB    
1119 C  CG    . GLN A 149 ? 1.1760 1.1945 1.0561 0.0061  0.0276  -0.0727 1366 GLN A CG    
1120 C  CD    . GLN A 149 ? 1.3680 1.3993 1.2401 0.0086  0.0313  -0.0817 1366 GLN A CD    
1121 O  OE1   . GLN A 149 ? 1.4362 1.4750 1.2959 0.0051  0.0344  -0.0789 1366 GLN A OE1   
1122 N  NE2   . GLN A 149 ? 1.3240 1.3573 1.2027 0.0149  0.0307  -0.0925 1366 GLN A NE2   
1123 N  N     . PRO A 150 ? 0.6371 0.6278 0.5225 -0.0016 0.0187  -0.0508 1367 PRO A N     
1124 C  CA    . PRO A 150 ? 0.7340 0.7123 0.6251 -0.0023 0.0141  -0.0451 1367 PRO A CA    
1125 C  C     . PRO A 150 ? 0.8149 0.7878 0.7183 0.0001  0.0131  -0.0445 1367 PRO A C     
1126 O  O     . PRO A 150 ? 0.8663 0.8317 0.7729 -0.0016 0.0111  -0.0378 1367 PRO A O     
1127 C  CB    . PRO A 150 ? 0.7092 0.6818 0.5971 -0.0007 0.0086  -0.0491 1367 PRO A CB    
1128 C  CG    . PRO A 150 ? 0.7336 0.7158 0.6116 0.0002  0.0105  -0.0559 1367 PRO A CG    
1129 C  CD    . PRO A 150 ? 0.6000 0.5929 0.4736 -0.0022 0.0172  -0.0530 1367 PRO A CD    
1130 N  N     . PHE A 151 ? 0.7463 0.7221 0.6568 0.0045  0.0140  -0.0509 1368 PHE A N     
1131 C  CA    . PHE A 151 ? 0.5810 0.5523 0.5015 0.0060  0.0133  -0.0477 1368 PHE A CA    
1132 C  C     . PHE A 151 ? 0.6101 0.5913 0.5350 0.0069  0.0177  -0.0490 1368 PHE A C     
1133 O  O     . PHE A 151 ? 0.4125 0.3928 0.3425 0.0060  0.0182  -0.0443 1368 PHE A O     
1134 C  CB    . PHE A 151 ? 0.4778 0.4404 0.4060 0.0107  0.0092  -0.0516 1368 PHE A CB    
1135 C  CG    . PHE A 151 ? 0.4877 0.4395 0.4154 0.0093  0.0045  -0.0487 1368 PHE A CG    
1136 C  CD1   . PHE A 151 ? 0.4472 0.3915 0.3797 0.0081  0.0026  -0.0416 1368 PHE A CD1   
1137 C  CD2   . PHE A 151 ? 0.4707 0.4210 0.3939 0.0093  0.0018  -0.0537 1368 PHE A CD2   
1138 C  CE1   . PHE A 151 ? 0.4520 0.3877 0.3855 0.0068  -0.0014 -0.0391 1368 PHE A CE1   
1139 C  CE2   . PHE A 151 ? 0.4683 0.4097 0.3926 0.0078  -0.0029 -0.0515 1368 PHE A CE2   
1140 C  CZ    . PHE A 151 ? 0.4716 0.4060 0.4016 0.0064  -0.0042 -0.0439 1368 PHE A CZ    
1141 N  N     . LEU A 152 ? 0.6924 0.6841 0.6150 0.0084  0.0211  -0.0556 1369 LEU A N     
1142 C  CA    . LEU A 152 ? 0.6252 0.6285 0.5535 0.0099  0.0253  -0.0584 1369 LEU A CA    
1143 C  C     . LEU A 152 ? 0.6133 0.6225 0.5402 0.0040  0.0290  -0.0517 1369 LEU A C     
1144 O  O     . LEU A 152 ? 0.6295 0.6430 0.5641 0.0043  0.0302  -0.0507 1369 LEU A O     
1145 C  CB    . LEU A 152 ? 0.5667 0.5804 0.4921 0.0129  0.0283  -0.0674 1369 LEU A CB    
1146 C  CG    . LEU A 152 ? 0.4798 0.4850 0.4062 0.0182  0.0237  -0.0741 1369 LEU A CG    
1147 C  CD1   . LEU A 152 ? 0.4499 0.4638 0.3718 0.0214  0.0258  -0.0842 1369 LEU A CD1   
1148 C  CD2   . LEU A 152 ? 0.4340 0.4323 0.3722 0.0234  0.0205  -0.0751 1369 LEU A CD2   
1149 N  N     . ARG A 153 ? 0.5654 0.5744 0.4825 -0.0014 0.0305  -0.0471 1370 ARG A N     
1150 C  CA    . ARG A 153 ? 0.5413 0.5544 0.4570 -0.0076 0.0341  -0.0404 1370 ARG A CA    
1151 C  C     . ARG A 153 ? 0.5427 0.5466 0.4494 -0.0119 0.0322  -0.0332 1370 ARG A C     
1152 O  O     . ARG A 153 ? 0.6406 0.6468 0.5373 -0.0136 0.0333  -0.0329 1370 ARG A O     
1153 C  CB    . ARG A 153 ? 0.5729 0.6012 0.4865 -0.0099 0.0405  -0.0429 1370 ARG A CB    
1154 C  CG    . ARG A 153 ? 0.7101 0.7411 0.6235 -0.0170 0.0440  -0.0357 1370 ARG A CG    
1155 C  CD    . ARG A 153 ? 0.8634 0.9104 0.7757 -0.0201 0.0510  -0.0375 1370 ARG A CD    
1156 N  NE    . ARG A 153 ? 0.8950 0.9533 0.8141 -0.0144 0.0527  -0.0467 1370 ARG A NE    
1157 C  CZ    . ARG A 153 ? 1.0232 1.0867 0.9546 -0.0118 0.0524  -0.0499 1370 ARG A CZ    
1158 N  NH1   . ARG A 153 ? 1.1207 1.1944 1.0581 -0.0059 0.0538  -0.0584 1370 ARG A NH1   
1159 N  NH2   . ARG A 153 ? 1.0292 1.0876 0.9667 -0.0144 0.0505  -0.0451 1370 ARG A NH2   
1160 N  N     . THR A 154 ? 0.4278 0.4217 0.3378 -0.0130 0.0290  -0.0277 1371 THR A N     
1161 C  CA    . THR A 154 ? 0.5131 0.4982 0.4162 -0.0166 0.0270  -0.0206 1371 THR A CA    
1162 C  C     . THR A 154 ? 0.6299 0.6141 0.5350 -0.0215 0.0291  -0.0142 1371 THR A C     
1163 O  O     . THR A 154 ? 0.4304 0.4183 0.3436 -0.0214 0.0305  -0.0154 1371 THR A O     
1164 C  CB    . THR A 154 ? 0.4869 0.4608 0.3920 -0.0134 0.0212  -0.0201 1371 THR A CB    
1165 O  OG1   . THR A 154 ? 0.4558 0.4261 0.3706 -0.0108 0.0196  -0.0203 1371 THR A OG1   
1166 C  CG2   . THR A 154 ? 0.4210 0.3962 0.3242 -0.0095 0.0195  -0.0269 1371 THR A CG2   
1167 N  N     . ARG A 155 ? 0.6633 0.6428 0.5607 -0.0257 0.0292  -0.0076 1372 ARG A N     
1168 C  CA    . ARG A 155 ? 0.6262 0.6040 0.5247 -0.0310 0.0315  -0.0014 1372 ARG A CA    
1169 C  C     . ARG A 155 ? 0.5755 0.5436 0.4803 -0.0301 0.0279  0.0011  1372 ARG A C     
1170 O  O     . ARG A 155 ? 0.5145 0.4830 0.4247 -0.0328 0.0294  0.0026  1372 ARG A O     
1171 C  CB    . ARG A 155 ? 0.6186 0.5941 0.5064 -0.0354 0.0328  0.0051  1372 ARG A CB    
1172 C  CG    . ARG A 155 ? 0.7583 0.7461 0.6420 -0.0387 0.0389  0.0042  1372 ARG A CG    
1173 C  CD    . ARG A 155 ? 0.8207 0.8073 0.6945 -0.0443 0.0416  0.0122  1372 ARG A CD    
1174 N  NE    . ARG A 155 ? 0.8707 0.8707 0.7400 -0.0466 0.0477  0.0104  1372 ARG A NE    
1175 C  CZ    . ARG A 155 ? 1.0603 1.0631 0.9174 -0.0491 0.0501  0.0149  1372 ARG A CZ    
1176 N  NH1   . ARG A 155 ? 1.1966 1.1890 1.0452 -0.0493 0.0462  0.0214  1372 ARG A NH1   
1177 N  NH2   . ARG A 155 ? 1.0769 1.0934 0.9303 -0.0511 0.0563  0.0129  1372 ARG A NH2   
1178 N  N     . GLU A 156 ? 0.4118 0.3719 0.3164 -0.0265 0.0233  0.0014  1373 GLU A N     
1179 C  CA    . GLU A 156 ? 0.4035 0.3576 0.3154 -0.0239 0.0205  0.0015  1373 GLU A CA    
1180 C  C     . GLU A 156 ? 0.4587 0.4152 0.3752 -0.0187 0.0188  -0.0044 1373 GLU A C     
1181 O  O     . GLU A 156 ? 0.4198 0.3778 0.3329 -0.0168 0.0180  -0.0075 1373 GLU A O     
1182 C  CB    . GLU A 156 ? 0.4034 0.3469 0.3131 -0.0238 0.0169  0.0067  1373 GLU A CB    
1183 C  CG    . GLU A 156 ? 0.3955 0.3342 0.3124 -0.0210 0.0145  0.0067  1373 GLU A CG    
1184 C  CD    . GLU A 156 ? 0.5875 0.5178 0.5037 -0.0191 0.0108  0.0099  1373 GLU A CD    
1185 O  OE1   . GLU A 156 ? 0.6632 0.5916 0.5739 -0.0195 0.0092  0.0115  1373 GLU A OE1   
1186 O  OE2   . GLU A 156 ? 0.3892 0.3157 0.3105 -0.0170 0.0094  0.0106  1373 GLU A OE2   
1187 N  N     . PHE A 157 ? 0.4496 0.4071 0.3738 -0.0163 0.0184  -0.0062 1374 PHE A N     
1188 C  CA    . PHE A 157 ? 0.4079 0.3651 0.3369 -0.0110 0.0162  -0.0103 1374 PHE A CA    
1189 C  C     . PHE A 157 ? 0.5246 0.4777 0.4595 -0.0088 0.0143  -0.0085 1374 PHE A C     
1190 O  O     . PHE A 157 ? 0.8011 0.7551 0.7376 -0.0110 0.0153  -0.0064 1374 PHE A O     
1191 C  CB    . PHE A 157 ? 0.3909 0.3578 0.3227 -0.0088 0.0185  -0.0165 1374 PHE A CB    
1192 C  CG    . PHE A 157 ? 0.4188 0.3941 0.3555 -0.0100 0.0212  -0.0177 1374 PHE A CG    
1193 C  CD1   . PHE A 157 ? 0.5427 0.5183 0.4863 -0.0070 0.0196  -0.0183 1374 PHE A CD1   
1194 C  CD2   . PHE A 157 ? 0.4876 0.4718 0.4223 -0.0140 0.0254  -0.0185 1374 PHE A CD2   
1195 C  CE1   . PHE A 157 ? 0.5352 0.5199 0.4841 -0.0081 0.0216  -0.0202 1374 PHE A CE1   
1196 C  CE2   . PHE A 157 ? 0.4675 0.4608 0.4082 -0.0156 0.0278  -0.0202 1374 PHE A CE2   
1197 C  CZ    . PHE A 157 ? 0.4704 0.4641 0.4184 -0.0125 0.0257  -0.0213 1374 PHE A CZ    
1198 N  N     . LEU A 158 ? 0.4606 0.4090 0.3986 -0.0047 0.0116  -0.0091 1375 LEU A N     
1199 C  CA    . LEU A 158 ? 0.5213 0.4664 0.4640 -0.0020 0.0099  -0.0072 1375 LEU A CA    
1200 C  C     . LEU A 158 ? 0.5739 0.5247 0.5221 0.0021  0.0101  -0.0109 1375 LEU A C     
1201 O  O     . LEU A 158 ? 0.5786 0.5331 0.5282 0.0043  0.0105  -0.0154 1375 LEU A O     
1202 C  CB    . LEU A 158 ? 0.4492 0.3859 0.3926 -0.0002 0.0072  -0.0045 1375 LEU A CB    
1203 C  CG    . LEU A 158 ? 0.4805 0.4122 0.4194 -0.0031 0.0061  -0.0016 1375 LEU A CG    
1204 C  CD1   . LEU A 158 ? 0.5216 0.4477 0.4630 -0.0010 0.0034  -0.0014 1375 LEU A CD1   
1205 C  CD2   . LEU A 158 ? 0.4759 0.4047 0.4135 -0.0053 0.0063  0.0031  1375 LEU A CD2   
1206 N  N     . TRP A 159 ? 0.4698 0.4219 0.4211 0.0034  0.0096  -0.0095 1376 TRP A N     
1207 C  CA    . TRP A 159 ? 0.5344 0.4924 0.4909 0.0078  0.0092  -0.0125 1376 TRP A CA    
1208 C  C     . TRP A 159 ? 0.5975 0.5535 0.5559 0.0104  0.0074  -0.0094 1376 TRP A C     
1209 O  O     . TRP A 159 ? 0.6920 0.6421 0.6479 0.0090  0.0068  -0.0053 1376 TRP A O     
1210 C  CB    . TRP A 159 ? 0.5577 0.5268 0.5160 0.0059  0.0117  -0.0166 1376 TRP A CB    
1211 C  CG    . TRP A 159 ? 0.7398 0.7129 0.6984 0.0021  0.0127  -0.0155 1376 TRP A CG    
1212 C  CD1   . TRP A 159 ? 0.7743 0.7420 0.7312 0.0005  0.0116  -0.0118 1376 TRP A CD1   
1213 C  CD2   . TRP A 159 ? 0.8557 0.8395 0.8173 -0.0009 0.0151  -0.0187 1376 TRP A CD2   
1214 N  NE1   . TRP A 159 ? 0.7024 0.6757 0.6609 -0.0032 0.0127  -0.0129 1376 TRP A NE1   
1215 C  CE2   . TRP A 159 ? 0.6527 0.6359 0.6144 -0.0045 0.0149  -0.0169 1376 TRP A CE2   
1216 C  CE3   . TRP A 159 ? 0.8880 0.8823 0.8527 -0.0010 0.0176  -0.0233 1376 TRP A CE3   
1217 C  CZ2   . TRP A 159 ? 0.4977 0.4898 0.4630 -0.0087 0.0169  -0.0192 1376 TRP A CZ2   
1218 C  CZ3   . TRP A 159 ? 0.7619 0.7663 0.7304 -0.0051 0.0200  -0.0253 1376 TRP A CZ3   
1219 C  CH2   . TRP A 159 ? 0.6537 0.6565 0.6226 -0.0093 0.0195  -0.0231 1376 TRP A CH2   
1220 N  N     . GLN A 160 ? 0.5515 0.5130 0.5142 0.0147  0.0065  -0.0115 1377 GLN A N     
1221 C  CA    . GLN A 160 ? 0.5707 0.5349 0.5347 0.0169  0.0050  -0.0099 1377 GLN A CA    
1222 C  C     . GLN A 160 ? 0.5381 0.5140 0.5054 0.0161  0.0058  -0.0144 1377 GLN A C     
1223 O  O     . GLN A 160 ? 0.7403 0.7226 0.7109 0.0169  0.0069  -0.0186 1377 GLN A O     
1224 C  CB    . GLN A 160 ? 0.6600 0.6207 0.6260 0.0233  0.0026  -0.0075 1377 GLN A CB    
1225 C  CG    . GLN A 160 ? 0.4594 0.4236 0.4303 0.0285  0.0016  -0.0109 1377 GLN A CG    
1226 C  CD    . GLN A 160 ? 0.5702 0.5458 0.5448 0.0312  0.0007  -0.0140 1377 GLN A CD    
1227 O  OE1   . GLN A 160 ? 0.6330 0.6101 0.6073 0.0342  -0.0013 -0.0115 1377 GLN A OE1   
1228 N  NE2   . GLN A 160 ? 0.6611 0.6457 0.6394 0.0304  0.0022  -0.0196 1377 GLN A NE2   
1229 N  N     . GLU A 161 ? 0.5965 0.5755 0.5634 0.0140  0.0054  -0.0140 1378 GLU A N     
1230 C  CA    . GLU A 161 ? 0.6353 0.6260 0.6068 0.0136  0.0052  -0.0182 1378 GLU A CA    
1231 C  C     . GLU A 161 ? 0.6172 0.6096 0.5887 0.0177  0.0020  -0.0171 1378 GLU A C     
1232 O  O     . GLU A 161 ? 0.6663 0.6525 0.6334 0.0170  0.0014  -0.0139 1378 GLU A O     
1233 C  CB    . GLU A 161 ? 0.5927 0.5868 0.5643 0.0062  0.0076  -0.0199 1378 GLU A CB    
1234 C  CG    . GLU A 161 ? 0.6275 0.6128 0.5941 0.0023  0.0077  -0.0165 1378 GLU A CG    
1235 C  CD    . GLU A 161 ? 0.5800 0.5672 0.5473 -0.0052 0.0101  -0.0177 1378 GLU A CD    
1236 O  OE1   . GLU A 161 ? 0.4827 0.4801 0.4554 -0.0076 0.0109  -0.0216 1378 GLU A OE1   
1237 O  OE2   . GLU A 161 ? 0.5012 0.4796 0.4640 -0.0087 0.0113  -0.0145 1378 GLU A OE2   
1238 N  N     . GLY A 162 ? 0.5751 0.5762 0.5513 0.0227  0.0000  -0.0196 1379 GLY A N     
1239 C  CA    . GLY A 162 ? 0.4981 0.5033 0.4741 0.0271  -0.0034 -0.0190 1379 GLY A CA    
1240 C  C     . GLY A 162 ? 0.5188 0.5377 0.5005 0.0254  -0.0043 -0.0247 1379 GLY A C     
1241 O  O     . GLY A 162 ? 0.4993 0.5267 0.4872 0.0248  -0.0032 -0.0287 1379 GLY A O     
1242 N  N     . HIS A 163 ? 0.5833 0.6048 0.5631 0.0245  -0.0064 -0.0253 1380 HIS A N     
1243 C  CA    . HIS A 163 ? 0.6281 0.6623 0.6137 0.0220  -0.0078 -0.0311 1380 HIS A CA    
1244 C  C     . HIS A 163 ? 0.5928 0.6322 0.5765 0.0277  -0.0125 -0.0313 1380 HIS A C     
1245 O  O     . HIS A 163 ? 0.5457 0.5775 0.5220 0.0294  -0.0134 -0.0277 1380 HIS A O     
1246 C  CB    . HIS A 163 ? 0.6101 0.6421 0.5954 0.0133  -0.0056 -0.0330 1380 HIS A CB    
1247 C  CG    . HIS A 163 ? 0.5062 0.5324 0.4915 0.0076  -0.0011 -0.0317 1380 HIS A CG    
1248 N  ND1   . HIS A 163 ? 0.5152 0.5499 0.5070 0.0027  0.0015  -0.0353 1380 HIS A ND1   
1249 C  CD2   . HIS A 163 ? 0.5221 0.5359 0.5015 0.0062  0.0012  -0.0272 1380 HIS A CD2   
1250 C  CE1   . HIS A 163 ? 0.5399 0.5672 0.5287 -0.0014 0.0053  -0.0327 1380 HIS A CE1   
1251 N  NE2   . HIS A 163 ? 0.5458 0.5604 0.5272 0.0007  0.0049  -0.0279 1380 HIS A NE2   
1252 N  N     . THR A 164 ? 0.6424 0.6956 0.6328 0.0306  -0.0154 -0.0357 1381 THR A N     
1253 C  CA    . THR A 164 ? 0.5800 0.6393 0.5684 0.0379  -0.0205 -0.0354 1381 THR A CA    
1254 C  C     . THR A 164 ? 0.5784 0.6540 0.5742 0.0367  -0.0238 -0.0426 1381 THR A C     
1255 O  O     . THR A 164 ? 0.6879 0.7727 0.6931 0.0329  -0.0223 -0.0473 1381 THR A O     
1256 C  CB    . THR A 164 ? 0.5297 0.5881 0.5185 0.0465  -0.0221 -0.0315 1381 THR A CB    
1257 O  OG1   . THR A 164 ? 0.5047 0.5706 0.5027 0.0465  -0.0207 -0.0353 1381 THR A OG1   
1258 C  CG2   . THR A 164 ? 0.5941 0.6365 0.5759 0.0477  -0.0195 -0.0244 1381 THR A CG2   
1259 N  N     . ALA A 165 ? 0.4405 0.5203 0.4320 0.0400  -0.0283 -0.0434 1382 ALA A N     
1260 C  CA    . ALA A 165 ? 0.5022 0.5975 0.4998 0.0393  -0.0327 -0.0506 1382 ALA A CA    
1261 C  C     . ALA A 165 ? 0.4510 0.5533 0.4442 0.0487  -0.0387 -0.0493 1382 ALA A C     
1262 O  O     . ALA A 165 ? 0.3953 0.4894 0.3776 0.0525  -0.0396 -0.0443 1382 ALA A O     
1263 C  CB    . ALA A 165 ? 0.6152 0.7085 0.6115 0.0314  -0.0322 -0.0550 1382 ALA A CB    
1264 N  N     . PHE A 166 ? 0.4832 0.6017 0.4851 0.0520  -0.0428 -0.0541 1383 PHE A N     
1265 C  CA    . PHE A 166 ? 0.5911 0.7180 0.5910 0.0622  -0.0489 -0.0524 1383 PHE A CA    
1266 C  C     . PHE A 166 ? 0.6702 0.8163 0.6777 0.0619  -0.0546 -0.0609 1383 PHE A C     
1267 O  O     . PHE A 166 ? 0.5374 0.6933 0.5570 0.0557  -0.0534 -0.0676 1383 PHE A O     
1268 C  CB    . PHE A 166 ? 0.5650 0.6926 0.5702 0.0689  -0.0486 -0.0489 1383 PHE A CB    
1269 C  CG    . PHE A 166 ? 0.5022 0.6118 0.5011 0.0702  -0.0439 -0.0409 1383 PHE A CG    
1270 C  CD1   . PHE A 166 ? 0.4067 0.5104 0.4109 0.0652  -0.0383 -0.0415 1383 PHE A CD1   
1271 C  CD2   . PHE A 166 ? 0.5659 0.6654 0.5538 0.0764  -0.0453 -0.0328 1383 PHE A CD2   
1272 C  CE1   . PHE A 166 ? 0.4419 0.5298 0.4410 0.0662  -0.0347 -0.0350 1383 PHE A CE1   
1273 C  CE2   . PHE A 166 ? 0.6700 0.7534 0.6536 0.0770  -0.0412 -0.0258 1383 PHE A CE2   
1274 C  CZ    . PHE A 166 ? 0.6365 0.7140 0.6259 0.0719  -0.0362 -0.0273 1383 PHE A CZ    
1275 N  N     . ALA A 167 ? 0.7171 0.8696 0.7180 0.0693  -0.0609 -0.0602 1384 ALA A N     
1276 C  CA    . ALA A 167 ? 0.5099 0.6821 0.5177 0.0706  -0.0676 -0.0683 1384 ALA A CA    
1277 C  C     . ALA A 167 ? 0.4656 0.6520 0.4875 0.0741  -0.0694 -0.0711 1384 ALA A C     
1278 O  O     . ALA A 167 ? 0.4772 0.6778 0.5120 0.0687  -0.0703 -0.0794 1384 ALA A O     
1279 C  CB    . ALA A 167 ? 0.4237 0.5998 0.4198 0.0790  -0.0742 -0.0660 1384 ALA A CB    
1280 N  N     . THR A 168 ? 0.5865 0.7696 0.6071 0.0832  -0.0699 -0.0645 1385 THR A N     
1281 C  CA    . THR A 168 ? 0.7372 0.9344 0.7713 0.0882  -0.0721 -0.0674 1385 THR A CA    
1282 C  C     . THR A 168 ? 0.8019 0.9914 0.8427 0.0856  -0.0651 -0.0658 1385 THR A C     
1283 O  O     . THR A 168 ? 0.7987 0.9698 0.8314 0.0841  -0.0599 -0.0595 1385 THR A O     
1284 C  CB    . THR A 168 ? 0.7717 0.9723 0.8013 0.1016  -0.0786 -0.0620 1385 THR A CB    
1285 O  OG1   . THR A 168 ? 0.7976 0.9790 0.8180 0.1062  -0.0751 -0.0519 1385 THR A OG1   
1286 C  CG2   . THR A 168 ? 0.7819 0.9890 0.8019 0.1049  -0.0854 -0.0624 1385 THR A CG2   
1287 N  N     . GLN A 169 ? 0.8123 1.0173 0.8683 0.0856  -0.0651 -0.0720 1386 GLN A N     
1288 C  CA    . GLN A 169 ? 0.7868 0.9880 0.8501 0.0834  -0.0586 -0.0721 1386 GLN A CA    
1289 C  C     . GLN A 169 ? 0.7667 0.9560 0.8254 0.0934  -0.0585 -0.0648 1386 GLN A C     
1290 O  O     . GLN A 169 ? 0.7776 0.9553 0.8359 0.0912  -0.0525 -0.0626 1386 GLN A O     
1291 C  CB    . GLN A 169 ? 0.8014 1.0249 0.8825 0.0817  -0.0589 -0.0808 1386 GLN A CB    
1292 C  CG    . GLN A 169 ? 0.8240 1.0477 0.9137 0.0806  -0.0525 -0.0821 1386 GLN A CG    
1293 C  CD    . GLN A 169 ? 0.9036 1.1477 1.0095 0.0734  -0.0501 -0.0909 1386 GLN A CD    
1294 O  OE1   . GLN A 169 ? 0.9224 1.1643 1.0315 0.0649  -0.0427 -0.0924 1386 GLN A OE1   
1295 N  NE2   . GLN A 169 ? 0.9018 1.1666 1.0179 0.0766  -0.0564 -0.0967 1386 GLN A NE2   
1296 N  N     . LYS A 170 ? 0.6775 0.8691 0.7326 0.1043  -0.0653 -0.0610 1387 LYS A N     
1297 C  CA    . LYS A 170 ? 0.6108 0.7900 0.6621 0.1140  -0.0657 -0.0536 1387 LYS A CA    
1298 C  C     . LYS A 170 ? 0.6884 0.8440 0.7271 0.1103  -0.0605 -0.0459 1387 LYS A C     
1299 O  O     . LYS A 170 ? 0.7212 0.8657 0.7615 0.1106  -0.0560 -0.0439 1387 LYS A O     
1300 C  CB    . LYS A 170 ? 0.4495 0.6342 0.4970 0.1257  -0.0741 -0.0494 1387 LYS A CB    
1301 N  N     . GLU A 171 ? 0.6529 0.8013 0.6795 0.1067  -0.0610 -0.0422 1388 GLU A N     
1302 C  CA    . GLU A 171 ? 0.6550 0.7826 0.6701 0.1030  -0.0562 -0.0351 1388 GLU A CA    
1303 C  C     . GLU A 171 ? 0.6462 0.7665 0.6656 0.0946  -0.0490 -0.0378 1388 GLU A C     
1304 O  O     . GLU A 171 ? 0.6901 0.7946 0.7057 0.0949  -0.0453 -0.0326 1388 GLU A O     
1305 C  CB    . GLU A 171 ? 0.6553 0.7805 0.6593 0.0987  -0.0571 -0.0336 1388 GLU A CB    
1306 C  CG    . GLU A 171 ? 0.7218 0.8573 0.7207 0.1058  -0.0644 -0.0326 1388 GLU A CG    
1307 C  CD    . GLU A 171 ? 0.8793 1.0165 0.8694 0.1003  -0.0651 -0.0349 1388 GLU A CD    
1308 O  OE1   . GLU A 171 ? 0.9308 1.0538 0.9098 0.0980  -0.0618 -0.0291 1388 GLU A OE1   
1309 O  OE2   . GLU A 171 ? 0.8666 1.0197 0.8617 0.0984  -0.0691 -0.0428 1388 GLU A OE2   
1310 N  N     . ALA A 172 ? 0.5341 0.6661 0.5617 0.0869  -0.0469 -0.0458 1389 ALA A N     
1311 C  CA    . ALA A 172 ? 0.6956 0.8222 0.7265 0.0786  -0.0400 -0.0482 1389 ALA A CA    
1312 C  C     . ALA A 172 ? 0.7912 0.9168 0.8291 0.0832  -0.0378 -0.0487 1389 ALA A C     
1313 O  O     . ALA A 172 ? 0.8386 0.9502 0.8728 0.0810  -0.0333 -0.0458 1389 ALA A O     
1314 C  CB    . ALA A 172 ? 0.7858 0.9262 0.8245 0.0696  -0.0385 -0.0560 1389 ALA A CB    
1315 N  N     . ASP A 173 ? 0.7045 0.8453 0.7528 0.0901  -0.0413 -0.0530 1390 ASP A N     
1316 C  CA    . ASP A 173 ? 0.5728 0.7137 0.6286 0.0957  -0.0396 -0.0546 1390 ASP A CA    
1317 C  C     . ASP A 173 ? 0.5699 0.6906 0.6175 0.1018  -0.0398 -0.0467 1390 ASP A C     
1318 O  O     . ASP A 173 ? 0.5094 0.6207 0.5581 0.1015  -0.0357 -0.0469 1390 ASP A O     
1319 C  CB    . ASP A 173 ? 0.5864 0.7463 0.6541 0.1042  -0.0446 -0.0594 1390 ASP A CB    
1320 C  CG    . ASP A 173 ? 0.6384 0.8200 0.7172 0.0979  -0.0439 -0.0680 1390 ASP A CG    
1321 O  OD1   . ASP A 173 ? 0.5590 0.7423 0.6410 0.0886  -0.0375 -0.0717 1390 ASP A OD1   
1322 O  OD2   . ASP A 173 ? 0.6954 0.8929 0.7801 0.1021  -0.0499 -0.0709 1390 ASP A OD2   
1323 N  N     . GLU A 174 ? 0.4666 0.5807 0.5060 0.1070  -0.0445 -0.0399 1391 GLU A N     
1324 C  CA    . GLU A 174 ? 0.5416 0.6371 0.5742 0.1128  -0.0450 -0.0316 1391 GLU A CA    
1325 C  C     . GLU A 174 ? 0.5710 0.6493 0.5957 0.1049  -0.0394 -0.0281 1391 GLU A C     
1326 O  O     . GLU A 174 ? 0.6046 0.6698 0.6293 0.1066  -0.0372 -0.0258 1391 GLU A O     
1327 C  CB    . GLU A 174 ? 0.4452 0.5391 0.4703 0.1197  -0.0509 -0.0244 1391 GLU A CB    
1328 C  CG    . GLU A 174 ? 0.5564 0.6654 0.5896 0.1296  -0.0571 -0.0270 1391 GLU A CG    
1329 C  CD    . GLU A 174 ? 0.7408 0.8527 0.7659 0.1350  -0.0632 -0.0212 1391 GLU A CD    
1330 O  OE1   . GLU A 174 ? 0.7234 0.8223 0.7361 0.1325  -0.0620 -0.0138 1391 GLU A OE1   
1331 O  OE2   . GLU A 174 ? 0.8371 0.9651 0.8680 0.1417  -0.0690 -0.0242 1391 GLU A OE2   
1332 N  N     . GLU A 175 ? 0.5505 0.6288 0.5691 0.0964  -0.0373 -0.0281 1392 GLU A N     
1333 C  CA    . GLU A 175 ? 0.5697 0.6323 0.5812 0.0896  -0.0324 -0.0246 1392 GLU A CA    
1334 C  C     . GLU A 175 ? 0.5887 0.6507 0.6060 0.0849  -0.0275 -0.0299 1392 GLU A C     
1335 O  O     . GLU A 175 ? 0.6540 0.7019 0.6681 0.0833  -0.0246 -0.0271 1392 GLU A O     
1336 C  CB    . GLU A 175 ? 0.5204 0.5831 0.5247 0.0820  -0.0314 -0.0240 1392 GLU A CB    
1337 C  CG    . GLU A 175 ? 0.4808 0.5282 0.4785 0.0756  -0.0267 -0.0204 1392 GLU A CG    
1338 C  CD    . GLU A 175 ? 0.6172 0.6669 0.6111 0.0673  -0.0249 -0.0224 1392 GLU A CD    
1339 O  OE1   . GLU A 175 ? 0.7706 0.8161 0.7565 0.0675  -0.0262 -0.0183 1392 GLU A OE1   
1340 O  OE2   . GLU A 175 ? 0.4979 0.5535 0.4967 0.0609  -0.0220 -0.0281 1392 GLU A OE2   
1341 N  N     . VAL A 176 ? 0.5277 0.6056 0.5536 0.0824  -0.0265 -0.0377 1393 VAL A N     
1342 C  CA    . VAL A 176 ? 0.4747 0.5543 0.5060 0.0787  -0.0216 -0.0429 1393 VAL A CA    
1343 C  C     . VAL A 176 ? 0.5720 0.6420 0.6050 0.0858  -0.0217 -0.0418 1393 VAL A C     
1344 O  O     . VAL A 176 ? 0.5435 0.6020 0.5733 0.0826  -0.0180 -0.0412 1393 VAL A O     
1345 C  CB    . VAL A 176 ? 0.3861 0.4867 0.4284 0.0773  -0.0210 -0.0510 1393 VAL A CB    
1346 C  CG1   . VAL A 176 ? 0.4217 0.5246 0.4681 0.0734  -0.0152 -0.0559 1393 VAL A CG1   
1347 C  CG2   . VAL A 176 ? 0.3818 0.4911 0.4235 0.0700  -0.0213 -0.0525 1393 VAL A CG2   
1348 N  N     . LEU A 177 ? 0.5376 0.6116 0.5758 0.0960  -0.0264 -0.0415 1394 LEU A N     
1349 C  CA    . LEU A 177 ? 0.5482 0.6133 0.5900 0.1034  -0.0268 -0.0414 1394 LEU A CA    
1350 C  C     . LEU A 177 ? 0.6676 0.7108 0.7007 0.1041  -0.0272 -0.0332 1394 LEU A C     
1351 O  O     . LEU A 177 ? 0.6592 0.6910 0.6928 0.1044  -0.0250 -0.0339 1394 LEU A O     
1352 C  CB    . LEU A 177 ? 0.4595 0.5346 0.5099 0.1144  -0.0318 -0.0433 1394 LEU A CB    
1353 C  CG    . LEU A 177 ? 0.4829 0.5797 0.5455 0.1161  -0.0312 -0.0528 1394 LEU A CG    
1354 C  CD1   . LEU A 177 ? 0.4211 0.5251 0.4921 0.1285  -0.0369 -0.0536 1394 LEU A CD1   
1355 C  CD2   . LEU A 177 ? 0.4095 0.5085 0.4764 0.1121  -0.0251 -0.0599 1394 LEU A CD2   
1356 N  N     . THR A 178 ? 0.6143 0.6521 0.6398 0.1039  -0.0297 -0.0256 1395 THR A N     
1357 C  CA    . THR A 178 ? 0.5488 0.5674 0.5664 0.1034  -0.0294 -0.0172 1395 THR A CA    
1358 C  C     . THR A 178 ? 0.6885 0.6979 0.7025 0.0945  -0.0243 -0.0183 1395 THR A C     
1359 O  O     . THR A 178 ? 0.7199 0.7153 0.7335 0.0949  -0.0232 -0.0164 1395 THR A O     
1360 C  CB    . THR A 178 ? 0.4784 0.4970 0.4878 0.1031  -0.0319 -0.0101 1395 THR A CB    
1361 O  OG1   . THR A 178 ? 0.5955 0.6201 0.6070 0.1126  -0.0373 -0.0076 1395 THR A OG1   
1362 C  CG2   . THR A 178 ? 0.4234 0.4245 0.4245 0.1003  -0.0303 -0.0017 1395 THR A CG2   
1363 N  N     . ILE A 179 ? 0.6093 0.6263 0.6206 0.0863  -0.0215 -0.0212 1396 ILE A N     
1364 C  CA    . ILE A 179 ? 0.4301 0.4400 0.4375 0.0778  -0.0169 -0.0221 1396 ILE A CA    
1365 C  C     . ILE A 179 ? 0.4773 0.4864 0.4899 0.0783  -0.0145 -0.0281 1396 ILE A C     
1366 O  O     . ILE A 179 ? 0.4077 0.4046 0.4175 0.0757  -0.0127 -0.0270 1396 ILE A O     
1367 C  CB    . ILE A 179 ? 0.4732 0.4928 0.4782 0.0698  -0.0148 -0.0246 1396 ILE A CB    
1368 C  CG1   . ILE A 179 ? 0.4536 0.4712 0.4520 0.0693  -0.0170 -0.0189 1396 ILE A CG1   
1369 C  CG2   . ILE A 179 ? 0.3861 0.4003 0.3878 0.0614  -0.0101 -0.0261 1396 ILE A CG2   
1370 C  CD1   . ILE A 179 ? 0.4463 0.4480 0.4375 0.0669  -0.0156 -0.0122 1396 ILE A CD1   
1371 N  N     . LEU A 180 ? 0.4515 0.4744 0.4721 0.0819  -0.0147 -0.0350 1397 LEU A N     
1372 C  CA    . LEU A 180 ? 0.5421 0.5659 0.5674 0.0829  -0.0121 -0.0417 1397 LEU A CA    
1373 C  C     . LEU A 180 ? 0.6064 0.6149 0.6327 0.0893  -0.0141 -0.0397 1397 LEU A C     
1374 O  O     . LEU A 180 ? 0.5445 0.5456 0.5704 0.0877  -0.0119 -0.0429 1397 LEU A O     
1375 C  CB    . LEU A 180 ? 0.4479 0.4908 0.4827 0.0865  -0.0119 -0.0492 1397 LEU A CB    
1376 C  CG    . LEU A 180 ? 0.5421 0.5899 0.5812 0.0864  -0.0079 -0.0573 1397 LEU A CG    
1377 C  CD1   . LEU A 180 ? 0.5593 0.6103 0.5933 0.0759  -0.0025 -0.0592 1397 LEU A CD1   
1378 C  CD2   . LEU A 180 ? 0.4816 0.5469 0.5318 0.0929  -0.0086 -0.0642 1397 LEU A CD2   
1379 N  N     . ASP A 181 ? 0.5656 0.5691 0.5933 0.0967  -0.0186 -0.0344 1398 ASP A N     
1380 C  CA    . ASP A 181 ? 0.6665 0.6536 0.6954 0.1023  -0.0208 -0.0312 1398 ASP A CA    
1381 C  C     . ASP A 181 ? 0.7404 0.7112 0.7622 0.0959  -0.0191 -0.0258 1398 ASP A C     
1382 O  O     . ASP A 181 ? 0.6643 0.6229 0.6877 0.0965  -0.0188 -0.0272 1398 ASP A O     
1383 C  CB    . ASP A 181 ? 0.7761 0.7615 0.8068 0.1109  -0.0258 -0.0250 1398 ASP A CB    
1384 C  CG    . ASP A 181 ? 0.8347 0.8019 0.8671 0.1165  -0.0282 -0.0206 1398 ASP A CG    
1385 O  OD1   . ASP A 181 ? 0.8595 0.8166 0.8871 0.1175  -0.0302 -0.0109 1398 ASP A OD1   
1386 O  OD2   . ASP A 181 ? 0.8249 0.7876 0.8632 0.1197  -0.0277 -0.0268 1398 ASP A OD2   
1387 N  N     . LEU A 182 ? 0.7675 0.7380 0.7820 0.0898  -0.0183 -0.0201 1399 LEU A N     
1388 C  CA    . LEU A 182 ? 0.7948 0.7521 0.8032 0.0832  -0.0164 -0.0153 1399 LEU A CA    
1389 C  C     . LEU A 182 ? 0.7915 0.7483 0.7994 0.0771  -0.0129 -0.0217 1399 LEU A C     
1390 O  O     . LEU A 182 ? 0.7625 0.7068 0.7690 0.0745  -0.0124 -0.0204 1399 LEU A O     
1391 C  CB    . LEU A 182 ? 0.7875 0.7472 0.7889 0.0784  -0.0159 -0.0092 1399 LEU A CB    
1392 C  CG    . LEU A 182 ? 0.7319 0.6885 0.7306 0.0832  -0.0189 -0.0008 1399 LEU A CG    
1393 C  CD1   . LEU A 182 ? 0.7366 0.6974 0.7280 0.0779  -0.0177 0.0029  1399 LEU A CD1   
1394 C  CD2   . LEU A 182 ? 0.6558 0.5956 0.6547 0.0851  -0.0197 0.0057  1399 LEU A CD2   
1395 N  N     . TYR A 183 ? 0.6403 0.6109 0.6487 0.0740  -0.0104 -0.0281 1400 TYR A N     
1396 C  CA    . TYR A 183 ? 0.4851 0.4567 0.4923 0.0690  -0.0071 -0.0341 1400 TYR A CA    
1397 C  C     . TYR A 183 ? 0.5421 0.5075 0.5542 0.0741  -0.0078 -0.0395 1400 TYR A C     
1398 O  O     . TYR A 183 ? 0.4849 0.4402 0.4947 0.0713  -0.0072 -0.0406 1400 TYR A O     
1399 C  CB    . TYR A 183 ? 0.4585 0.4473 0.4667 0.0658  -0.0041 -0.0397 1400 TYR A CB    
1400 C  CG    . TYR A 183 ? 0.6157 0.6088 0.6185 0.0587  -0.0027 -0.0359 1400 TYR A CG    
1401 C  CD1   . TYR A 183 ? 0.5619 0.5439 0.5582 0.0542  -0.0029 -0.0295 1400 TYR A CD1   
1402 C  CD2   . TYR A 183 ? 0.5231 0.5316 0.5284 0.0564  -0.0013 -0.0389 1400 TYR A CD2   
1403 C  CE1   . TYR A 183 ? 0.5302 0.5152 0.5220 0.0484  -0.0018 -0.0266 1400 TYR A CE1   
1404 C  CE2   . TYR A 183 ? 0.4780 0.4889 0.4790 0.0500  -0.0004 -0.0359 1400 TYR A CE2   
1405 C  CZ    . TYR A 183 ? 0.5611 0.5597 0.5551 0.0463  -0.0006 -0.0298 1400 TYR A CZ    
1406 O  OH    . TYR A 183 ? 0.6164 0.6160 0.6060 0.0404  0.0002  -0.0270 1400 TYR A OH    
1407 N  N     . ALA A 184 ? 0.6760 0.6476 0.6953 0.0821  -0.0095 -0.0435 1401 ALA A N     
1408 C  CA    . ALA A 184 ? 0.5714 0.5370 0.5963 0.0881  -0.0105 -0.0494 1401 ALA A CA    
1409 C  C     . ALA A 184 ? 0.5605 0.5061 0.5850 0.0894  -0.0133 -0.0442 1401 ALA A C     
1410 O  O     . ALA A 184 ? 0.4444 0.3813 0.4707 0.0901  -0.0134 -0.0491 1401 ALA A O     
1411 C  CB    . ALA A 184 ? 0.4860 0.4614 0.5194 0.0973  -0.0125 -0.0534 1401 ALA A CB    
1412 N  N     . LYS A 185 ? 0.5200 0.4584 0.5423 0.0893  -0.0154 -0.0344 1402 LYS A N     
1413 C  CA    . LYS A 185 ? 0.5074 0.4273 0.5298 0.0894  -0.0174 -0.0285 1402 LYS A CA    
1414 C  C     . LYS A 185 ? 0.5718 0.4849 0.5892 0.0808  -0.0153 -0.0285 1402 LYS A C     
1415 O  O     . LYS A 185 ? 0.7547 0.6550 0.7745 0.0804  -0.0163 -0.0296 1402 LYS A O     
1416 C  CB    . LYS A 185 ? 0.4467 0.3624 0.4668 0.0910  -0.0194 -0.0175 1402 LYS A CB    
1417 C  CG    . LYS A 185 ? 0.7003 0.6156 0.7259 0.1008  -0.0230 -0.0156 1402 LYS A CG    
1418 C  CD    . LYS A 185 ? 0.7022 0.6119 0.7242 0.1023  -0.0250 -0.0039 1402 LYS A CD    
1419 C  CE    . LYS A 185 ? 0.7817 0.6825 0.8095 0.1117  -0.0289 -0.0003 1402 LYS A CE    
1420 N  NZ    . LYS A 185 ? 0.9663 0.8794 0.9940 0.1184  -0.0315 0.0018  1402 LYS A NZ    
1421 N  N     . VAL A 186 ? 0.5089 0.4304 0.5200 0.0739  -0.0126 -0.0274 1403 VAL A N     
1422 C  CA    . VAL A 186 ? 0.5807 0.4973 0.5873 0.0664  -0.0109 -0.0282 1403 VAL A CA    
1423 C  C     . VAL A 186 ? 0.6766 0.5921 0.6855 0.0672  -0.0105 -0.0378 1403 VAL A C     
1424 O  O     . VAL A 186 ? 0.6630 0.5686 0.6714 0.0641  -0.0112 -0.0389 1403 VAL A O     
1425 C  CB    . VAL A 186 ? 0.6883 0.6155 0.6882 0.0598  -0.0080 -0.0270 1403 VAL A CB    
1426 C  CG1   . VAL A 186 ? 0.6377 0.5636 0.6333 0.0534  -0.0062 -0.0307 1403 VAL A CG1   
1427 C  CG2   . VAL A 186 ? 0.7421 0.6667 0.7385 0.0576  -0.0084 -0.0177 1403 VAL A CG2   
1428 N  N     . TYR A 187 ? 0.8118 0.7385 0.8234 0.0714  -0.0095 -0.0451 1404 TYR A N     
1429 C  CA    . TYR A 187 ? 0.8430 0.7705 0.8558 0.0724  -0.0087 -0.0551 1404 TYR A CA    
1430 C  C     . TYR A 187 ? 0.8161 0.7301 0.8358 0.0786  -0.0120 -0.0582 1404 TYR A C     
1431 O  O     . TYR A 187 ? 0.7867 0.6930 0.8061 0.0767  -0.0126 -0.0632 1404 TYR A O     
1432 C  CB    . TYR A 187 ? 0.8138 0.7590 0.8274 0.0744  -0.0057 -0.0623 1404 TYR A CB    
1433 C  CG    . TYR A 187 ? 0.6572 0.6123 0.6630 0.0663  -0.0019 -0.0623 1404 TYR A CG    
1434 C  CD1   . TYR A 187 ? 0.6603 0.6234 0.6634 0.0625  -0.0005 -0.0565 1404 TYR A CD1   
1435 C  CD2   . TYR A 187 ? 0.5193 0.4748 0.5201 0.0624  0.0000  -0.0679 1404 TYR A CD2   
1436 C  CE1   . TYR A 187 ? 0.6845 0.6550 0.6810 0.0550  0.0028  -0.0560 1404 TYR A CE1   
1437 C  CE2   . TYR A 187 ? 0.4552 0.4188 0.4484 0.0552  0.0033  -0.0669 1404 TYR A CE2   
1438 C  CZ    . TYR A 187 ? 0.6175 0.5879 0.6089 0.0515  0.0048  -0.0607 1404 TYR A CZ    
1439 O  OH    . TYR A 187 ? 0.6731 0.6500 0.6576 0.0444  0.0079  -0.0593 1404 TYR A OH    
1440 N  N     . THR A 188 ? 0.8250 0.7355 0.8511 0.0859  -0.0145 -0.0552 1405 THR A N     
1441 C  CA    . THR A 188 ? 0.6983 0.5959 0.7320 0.0927  -0.0177 -0.0589 1405 THR A CA    
1442 C  C     . THR A 188 ? 0.5241 0.4025 0.5596 0.0911  -0.0206 -0.0507 1405 THR A C     
1443 O  O     . THR A 188 ? 0.6645 0.5299 0.7047 0.0926  -0.0226 -0.0550 1405 THR A O     
1444 C  CB    . THR A 188 ? 0.6719 0.5748 0.7128 0.1028  -0.0194 -0.0607 1405 THR A CB    
1445 O  OG1   . THR A 188 ? 0.4741 0.3771 0.5147 0.1045  -0.0210 -0.0501 1405 THR A OG1   
1446 C  CG2   . THR A 188 ? 0.8035 0.7262 0.8446 0.1046  -0.0163 -0.0696 1405 THR A CG2   
1447 N  N     . ASP A 189 ? 0.5594 0.4358 0.5916 0.0878  -0.0206 -0.0394 1406 ASP A N     
1448 C  CA    . ASP A 189 ? 0.6264 0.4865 0.6599 0.0854  -0.0224 -0.0301 1406 ASP A CA    
1449 C  C     . ASP A 189 ? 0.6943 0.5507 0.7233 0.0759  -0.0209 -0.0284 1406 ASP A C     
1450 O  O     . ASP A 189 ? 0.7356 0.5778 0.7681 0.0733  -0.0224 -0.0245 1406 ASP A O     
1451 C  CB    . ASP A 189 ? 0.5616 0.4231 0.5927 0.0869  -0.0227 -0.0184 1406 ASP A CB    
1452 C  CG    . ASP A 189 ? 0.7541 0.6206 0.7890 0.0963  -0.0247 -0.0184 1406 ASP A CG    
1453 O  OD1   . ASP A 189 ? 0.7383 0.6070 0.7786 0.1019  -0.0256 -0.0276 1406 ASP A OD1   
1454 O  OD2   . ASP A 189 ? 0.9634 0.8321 0.9959 0.0984  -0.0254 -0.0094 1406 ASP A OD2   
1455 N  N     . LEU A 190 ? 0.6862 0.5552 0.7082 0.0706  -0.0181 -0.0305 1407 LEU A N     
1456 C  CA    . LEU A 190 ? 0.6438 0.5107 0.6615 0.0622  -0.0170 -0.0293 1407 LEU A CA    
1457 C  C     . LEU A 190 ? 0.6617 0.5302 0.6784 0.0601  -0.0169 -0.0401 1407 LEU A C     
1458 O  O     . LEU A 190 ? 0.5917 0.4510 0.6100 0.0562  -0.0184 -0.0414 1407 LEU A O     
1459 C  CB    . LEU A 190 ? 0.5263 0.4041 0.5366 0.0576  -0.0144 -0.0238 1407 LEU A CB    
1460 C  CG    . LEU A 190 ? 0.5154 0.3896 0.5252 0.0578  -0.0145 -0.0123 1407 LEU A CG    
1461 C  CD1   . LEU A 190 ? 0.5253 0.4098 0.5281 0.0538  -0.0122 -0.0079 1407 LEU A CD1   
1462 C  CD2   . LEU A 190 ? 0.4902 0.3502 0.5036 0.0545  -0.0157 -0.0068 1407 LEU A CD2   
1463 N  N     . LEU A 191 ? 0.8026 0.6836 0.8168 0.0624  -0.0151 -0.0479 1408 LEU A N     
1464 C  CA    . LEU A 191 ? 0.7538 0.6386 0.7647 0.0599  -0.0144 -0.0576 1408 LEU A CA    
1465 C  C     . LEU A 191 ? 0.6685 0.5497 0.6850 0.0662  -0.0160 -0.0679 1408 LEU A C     
1466 O  O     . LEU A 191 ? 0.5715 0.4545 0.5853 0.0647  -0.0159 -0.0767 1408 LEU A O     
1467 C  CB    . LEU A 191 ? 0.7315 0.6331 0.7348 0.0572  -0.0106 -0.0599 1408 LEU A CB    
1468 C  CG    . LEU A 191 ? 0.6824 0.5880 0.6800 0.0510  -0.0089 -0.0509 1408 LEU A CG    
1469 C  CD1   . LEU A 191 ? 0.7320 0.6508 0.7219 0.0468  -0.0056 -0.0541 1408 LEU A CD1   
1470 C  CD2   . LEU A 191 ? 0.5043 0.3981 0.5017 0.0461  -0.0109 -0.0446 1408 LEU A CD2   
1471 N  N     . ALA A 192 ? 0.6761 0.5518 0.7002 0.0735  -0.0178 -0.0671 1409 ALA A N     
1472 C  CA    . ALA A 192 ? 0.5741 0.4449 0.6048 0.0806  -0.0197 -0.0770 1409 ALA A CA    
1473 C  C     . ALA A 192 ? 0.7031 0.5899 0.7306 0.0831  -0.0168 -0.0881 1409 ALA A C     
1474 O  O     . ALA A 192 ? 0.7301 0.6153 0.7583 0.0849  -0.0173 -0.0987 1409 ALA A O     
1475 C  CB    . ALA A 192 ? 0.4993 0.3540 0.5334 0.0782  -0.0229 -0.0805 1409 ALA A CB    
1476 N  N     . ILE A 193 ? 0.8324 0.7351 0.8565 0.0830  -0.0135 -0.0858 1410 ILE A N     
1477 C  CA    . ILE A 193 ? 0.9273 0.8472 0.9492 0.0852  -0.0099 -0.0948 1410 ILE A CA    
1478 C  C     . ILE A 193 ? 0.9039 0.8321 0.9329 0.0930  -0.0097 -0.0949 1410 ILE A C     
1479 O  O     . ILE A 193 ? 0.9697 0.8990 0.9995 0.0928  -0.0103 -0.0857 1410 ILE A O     
1480 C  CB    . ILE A 193 ? 0.9717 0.9048 0.9838 0.0771  -0.0058 -0.0924 1410 ILE A CB    
1481 C  CG1   . ILE A 193 ? 1.0193 0.9434 1.0248 0.0692  -0.0068 -0.0887 1410 ILE A CG1   
1482 C  CG2   . ILE A 193 ? 0.9712 0.9202 0.9804 0.0782  -0.0018 -0.1025 1410 ILE A CG2   
1483 C  CD1   . ILE A 193 ? 0.9130 0.8473 0.9092 0.0613  -0.0035 -0.0839 1410 ILE A CD1   
1484 N  N     . PRO A 194 ? 0.6997 0.6352 0.7337 0.1003  -0.0089 -0.1053 1411 PRO A N     
1485 C  CA    . PRO A 194 ? 0.7072 0.6535 0.7485 0.1079  -0.0087 -0.1057 1411 PRO A CA    
1486 C  C     . PRO A 194 ? 0.6473 0.6154 0.6850 0.1041  -0.0038 -0.1057 1411 PRO A C     
1487 O  O     . PRO A 194 ? 0.6192 0.5974 0.6508 0.0994  0.0003  -0.1112 1411 PRO A O     
1488 C  CB    . PRO A 194 ? 0.5993 0.5449 0.6477 0.1169  -0.0094 -0.1180 1411 PRO A CB    
1489 C  CG    . PRO A 194 ? 0.6209 0.5679 0.6622 0.1121  -0.0070 -0.1262 1411 PRO A CG    
1490 C  CD    . PRO A 194 ? 0.6603 0.5949 0.6941 0.1026  -0.0084 -0.1177 1411 PRO A CD    
1491 N  N     . VAL A 195 ? 0.4649 0.4404 0.5065 0.1063  -0.0045 -0.0997 1412 VAL A N     
1492 C  CA    . VAL A 195 ? 0.5259 0.5205 0.5650 0.1015  -0.0005 -0.0984 1412 VAL A CA    
1493 C  C     . VAL A 195 ? 0.4971 0.5058 0.5458 0.1091  -0.0009 -0.1007 1412 VAL A C     
1494 O  O     . VAL A 195 ? 0.6760 0.6778 0.7309 0.1162  -0.0054 -0.0971 1412 VAL A O     
1495 C  CB    . VAL A 195 ? 0.5625 0.5535 0.5949 0.0932  -0.0008 -0.0872 1412 VAL A CB    
1496 C  CG1   . VAL A 195 ? 0.4794 0.4625 0.5017 0.0842  0.0009  -0.0856 1412 VAL A CG1   
1497 C  CG2   . VAL A 195 ? 0.4453 0.4238 0.4810 0.0973  -0.0058 -0.0786 1412 VAL A CG2   
1498 N  N     . VAL A 196 ? 0.4732 0.5024 0.5228 0.1069  0.0037  -0.1054 1413 VAL A N     
1499 C  CA    . VAL A 196 ? 0.5877 0.6342 0.6473 0.1131  0.0038  -0.1086 1413 VAL A CA    
1500 C  C     . VAL A 196 ? 0.6071 0.6617 0.6655 0.1076  0.0036  -0.1005 1413 VAL A C     
1501 O  O     . VAL A 196 ? 0.6603 0.7220 0.7126 0.0981  0.0076  -0.0987 1413 VAL A O     
1502 C  CB    . VAL A 196 ? 0.4490 0.5150 0.5118 0.1139  0.0096  -0.1193 1413 VAL A CB    
1503 C  CG1   . VAL A 196 ? 0.4493 0.5331 0.5246 0.1217  0.0092  -0.1235 1413 VAL A CG1   
1504 C  CG2   . VAL A 196 ? 0.4596 0.5176 0.5205 0.1175  0.0104  -0.1278 1413 VAL A CG2   
1505 N  N     . LYS A 197 ? 0.5676 0.6208 0.6318 0.1136  -0.0013 -0.0958 1414 LYS A N     
1506 C  CA    . LYS A 197 ? 0.6266 0.6896 0.6910 0.1099  -0.0022 -0.0899 1414 LYS A CA    
1507 C  C     . LYS A 197 ? 0.7055 0.7933 0.7787 0.1109  0.0008  -0.0967 1414 LYS A C     
1508 O  O     . LYS A 197 ? 0.7262 0.8227 0.8088 0.1195  0.0006  -0.1041 1414 LYS A O     
1509 C  CB    . LYS A 197 ? 0.6193 0.6734 0.6861 0.1166  -0.0087 -0.0827 1414 LYS A CB    
1510 C  CG    . LYS A 197 ? 0.6823 0.7148 0.7402 0.1134  -0.0112 -0.0734 1414 LYS A CG    
1511 C  CD    . LYS A 197 ? 0.7310 0.7552 0.7920 0.1219  -0.0173 -0.0669 1414 LYS A CD    
1512 C  CE    . LYS A 197 ? 0.7655 0.7711 0.8180 0.1182  -0.0193 -0.0566 1414 LYS A CE    
1513 N  NZ    . LYS A 197 ? 0.7670 0.7716 0.8196 0.1233  -0.0242 -0.0485 1414 LYS A NZ    
1514 N  N     . GLY A 198 ? 0.6813 0.7808 0.7523 0.1020  0.0037  -0.0945 1415 GLY A N     
1515 C  CA    . GLY A 198 ? 0.7114 0.8352 0.7920 0.1021  0.0066  -0.1006 1415 GLY A CA    
1516 C  C     . GLY A 198 ? 0.6534 0.7876 0.7331 0.0930  0.0077  -0.0967 1415 GLY A C     
1517 O  O     . GLY A 198 ? 0.6184 0.7411 0.6893 0.0864  0.0066  -0.0895 1415 GLY A O     
1518 N  N     . ARG A 199 ? 0.6739 0.8308 0.7640 0.0928  0.0100  -0.1021 1416 ARG A N     
1519 C  CA    . ARG A 199 ? 0.6179 0.7882 0.7096 0.0832  0.0123  -0.1006 1416 ARG A CA    
1520 C  C     . ARG A 199 ? 0.6022 0.7820 0.6921 0.0743  0.0205  -0.1040 1416 ARG A C     
1521 O  O     . ARG A 199 ? 0.5785 0.7676 0.6726 0.0778  0.0246  -0.1108 1416 ARG A O     
1522 C  CB    . ARG A 199 ? 0.6075 0.7981 0.7132 0.0881  0.0092  -0.1043 1416 ARG A CB    
1523 C  CG    . ARG A 199 ? 0.6117 0.8153 0.7205 0.0785  0.0103  -0.1030 1416 ARG A CG    
1524 C  CD    . ARG A 199 ? 0.5396 0.7650 0.6635 0.0840  0.0070  -0.1078 1416 ARG A CD    
1525 N  NE    . ARG A 199 ? 0.5900 0.8311 0.7194 0.0737  0.0092  -0.1086 1416 ARG A NE    
1526 C  CZ    . ARG A 199 ? 0.5538 0.8016 0.6876 0.0728  0.0038  -0.1074 1416 ARG A CZ    
1527 N  NH1   . ARG A 199 ? 0.4008 0.6418 0.5333 0.0820  -0.0042 -0.1046 1416 ARG A NH1   
1528 N  NH2   . ARG A 199 ? 0.6562 0.9174 0.7956 0.0625  0.0063  -0.1088 1416 ARG A NH2   
1529 N  N     . LYS A 200 ? 0.6408 0.8189 0.7245 0.0630  0.0231  -0.0993 1417 LYS A N     
1530 C  CA    . LYS A 200 ? 0.7037 0.8910 0.7854 0.0542  0.0310  -0.1013 1417 LYS A CA    
1531 C  C     . LYS A 200 ? 0.7097 0.9229 0.8050 0.0518  0.0343  -0.1063 1417 LYS A C     
1532 O  O     . LYS A 200 ? 0.7698 0.9915 0.8736 0.0522  0.0302  -0.1060 1417 LYS A O     
1533 C  CB    . LYS A 200 ? 0.6378 0.8118 0.7076 0.0432  0.0324  -0.0938 1417 LYS A CB    
1534 C  CG    . LYS A 200 ? 0.5712 0.7225 0.6274 0.0441  0.0313  -0.0899 1417 LYS A CG    
1535 C  CD    . LYS A 200 ? 0.6371 0.7915 0.6882 0.0417  0.0378  -0.0934 1417 LYS A CD    
1536 C  CE    . LYS A 200 ? 0.6063 0.7402 0.6437 0.0405  0.0371  -0.0897 1417 LYS A CE    
1537 N  NZ    . LYS A 200 ? 0.5723 0.7094 0.6017 0.0347  0.0436  -0.0910 1417 LYS A NZ    
1538 N  N     . THR A 201 ? 0.6316 0.8584 0.7293 0.0491  0.0417  -0.1111 1418 THR A N     
1539 C  CA    . THR A 201 ? 0.7081 0.9609 0.8193 0.0457  0.0460  -0.1158 1418 THR A CA    
1540 C  C     . THR A 201 ? 0.7461 1.0012 0.8576 0.0333  0.0469  -0.1105 1418 THR A C     
1541 O  O     . THR A 201 ? 0.7717 1.0087 0.8719 0.0273  0.0454  -0.1035 1418 THR A O     
1542 C  CB    . THR A 201 ? 0.7826 1.0488 0.8942 0.0441  0.0549  -0.1210 1418 THR A CB    
1543 O  OG1   . THR A 201 ? 0.8559 1.1089 0.9522 0.0357  0.0593  -0.1158 1418 THR A OG1   
1544 C  CG2   . THR A 201 ? 0.7102 0.9779 0.8247 0.0572  0.0540  -0.1285 1418 THR A CG2   
1545 N  N     . GLU A 202 ? 0.7120 0.9902 0.8378 0.0297  0.0494  -0.1142 1419 GLU A N     
1546 C  CA    . GLU A 202 ? 0.7078 0.9891 0.8354 0.0172  0.0508  -0.1101 1419 GLU A CA    
1547 C  C     . GLU A 202 ? 0.7405 1.0125 0.8559 0.0064  0.0578  -0.1046 1419 GLU A C     
1548 O  O     . GLU A 202 ? 0.8439 1.1041 0.9532 -0.0024 0.0569  -0.0984 1419 GLU A O     
1549 C  CB    . GLU A 202 ? 0.6803 0.9899 0.8267 0.0145  0.0533  -0.1157 1419 GLU A CB    
1550 C  CG    . GLU A 202 ? 0.7115 1.0302 0.8701 0.0238  0.0451  -0.1200 1419 GLU A CG    
1551 C  CD    . GLU A 202 ? 0.8040 1.1037 0.9549 0.0251  0.0364  -0.1148 1419 GLU A CD    
1552 O  OE1   . GLU A 202 ? 0.8860 1.1689 1.0281 0.0344  0.0314  -0.1129 1419 GLU A OE1   
1553 O  OE2   . GLU A 202 ? 0.8124 1.1139 0.9662 0.0166  0.0346  -0.1129 1419 GLU A OE2   
1554 N  N     . LYS A 203 ? 0.6760 0.9516 0.7865 0.0078  0.0643  -0.1068 1420 LYS A N     
1555 C  CA    . LYS A 203 ? 0.6256 0.8935 0.7236 -0.0019 0.0709  -0.1014 1420 LYS A CA    
1556 C  C     . LYS A 203 ? 0.6137 0.8540 0.6949 -0.0014 0.0667  -0.0950 1420 LYS A C     
1557 O  O     . LYS A 203 ? 0.7439 0.9732 0.8162 -0.0107 0.0685  -0.0881 1420 LYS A O     
1558 C  CB    . LYS A 203 ? 0.5744 0.8555 0.6710 -0.0001 0.0790  -0.1060 1420 LYS A CB    
1559 C  CG    . LYS A 203 ? 0.6080 0.8770 0.6879 -0.0072 0.0841  -0.1000 1420 LYS A CG    
1560 C  CD    . LYS A 203 ? 0.6183 0.9041 0.6970 -0.0086 0.0935  -0.1035 1420 LYS A CD    
1561 C  CE    . LYS A 203 ? 0.6742 0.9463 0.7347 -0.0158 0.0975  -0.0964 1420 LYS A CE    
1562 N  NZ    . LYS A 203 ? 0.7540 1.0407 0.8093 -0.0172 0.1068  -0.0990 1420 LYS A NZ    
1563 N  N     . GLU A 204 ? 0.6112 0.8397 0.6887 0.0092  0.0609  -0.0970 1421 GLU A N     
1564 C  CA    . GLU A 204 ? 0.6427 0.8468 0.7050 0.0098  0.0578  -0.0916 1421 GLU A CA    
1565 C  C     . GLU A 204 ? 0.5399 0.7287 0.6007 0.0112  0.0499  -0.0871 1421 GLU A C     
1566 O  O     . GLU A 204 ? 0.6241 0.7929 0.6732 0.0108  0.0473  -0.0820 1421 GLU A O     
1567 C  CB    . GLU A 204 ? 0.7951 0.9939 0.8524 0.0195  0.0573  -0.0963 1421 GLU A CB    
1568 C  CG    . GLU A 204 ? 0.8379 1.0537 0.8967 0.0196  0.0651  -0.1022 1421 GLU A CG    
1569 C  CD    . GLU A 204 ? 0.8767 1.0845 0.9206 0.0130  0.0701  -0.0983 1421 GLU A CD    
1570 O  OE1   . GLU A 204 ? 0.9149 1.1366 0.9577 0.0117  0.0772  -0.1021 1421 GLU A OE1   
1571 O  OE2   . GLU A 204 ? 0.8367 1.0250 0.8698 0.0093  0.0668  -0.0913 1421 GLU A OE2   
1572 N  N     . LYS A 205 ? 0.4241 0.6224 0.4963 0.0126  0.0462  -0.0889 1422 LYS A N     
1573 C  CA    . LYS A 205 ? 0.4680 0.6531 0.5379 0.0136  0.0390  -0.0846 1422 LYS A CA    
1574 C  C     . LYS A 205 ? 0.5852 0.7600 0.6477 0.0025  0.0403  -0.0781 1422 LYS A C     
1575 O  O     . LYS A 205 ? 0.7643 0.9444 0.8259 -0.0064 0.0464  -0.0767 1422 LYS A O     
1576 C  CB    . LYS A 205 ? 0.4723 0.6718 0.5558 0.0181  0.0345  -0.0886 1422 LYS A CB    
1577 C  CG    . LYS A 205 ? 0.5598 0.7765 0.6538 0.0092  0.0371  -0.0902 1422 LYS A CG    
1578 C  CD    . LYS A 205 ? 0.6670 0.8942 0.7723 0.0139  0.0303  -0.0934 1422 LYS A CD    
1579 C  CE    . LYS A 205 ? 0.6588 0.9073 0.7780 0.0059  0.0329  -0.0971 1422 LYS A CE    
1580 N  NZ    . LYS A 205 ? 0.6174 0.8659 0.7405 0.0033  0.0265  -0.0966 1422 LYS A NZ    
1581 N  N     . PHE A 206 ? 0.5050 0.6645 0.5620 0.0033  0.0345  -0.0737 1423 PHE A N     
1582 C  CA    . PHE A 206 ? 0.4345 0.5834 0.4852 -0.0061 0.0350  -0.0681 1423 PHE A CA    
1583 C  C     . PHE A 206 ? 0.5611 0.7242 0.6229 -0.0131 0.0355  -0.0702 1423 PHE A C     
1584 O  O     . PHE A 206 ? 0.7313 0.9041 0.8023 -0.0089 0.0310  -0.0741 1423 PHE A O     
1585 C  CB    . PHE A 206 ? 0.3700 0.4998 0.4121 -0.0023 0.0289  -0.0636 1423 PHE A CB    
1586 C  CG    . PHE A 206 ? 0.5234 0.6437 0.5614 -0.0101 0.0278  -0.0592 1423 PHE A CG    
1587 C  CD1   . PHE A 206 ? 0.6190 0.7357 0.6531 -0.0198 0.0327  -0.0559 1423 PHE A CD1   
1588 C  CD2   . PHE A 206 ? 0.5342 0.6488 0.5719 -0.0075 0.0219  -0.0583 1423 PHE A CD2   
1589 C  CE1   . PHE A 206 ? 0.5631 0.6700 0.5941 -0.0264 0.0314  -0.0522 1423 PHE A CE1   
1590 C  CE2   . PHE A 206 ? 0.4793 0.5850 0.5134 -0.0141 0.0208  -0.0552 1423 PHE A CE2   
1591 C  CZ    . PHE A 206 ? 0.3701 0.4716 0.4014 -0.0234 0.0254  -0.0523 1423 PHE A CZ    
1592 N  N     . ALA A 207 ? 0.5847 0.7489 0.6457 -0.0238 0.0409  -0.0676 1424 ALA A N     
1593 C  CA    . ALA A 207 ? 0.4450 0.6251 0.5185 -0.0318 0.0430  -0.0702 1424 ALA A CA    
1594 C  C     . ALA A 207 ? 0.4458 0.6248 0.5245 -0.0317 0.0362  -0.0716 1424 ALA A C     
1595 O  O     . ALA A 207 ? 0.4017 0.5980 0.4937 -0.0319 0.0345  -0.0770 1424 ALA A O     
1596 C  CB    . ALA A 207 ? 0.3806 0.5569 0.4504 -0.0437 0.0493  -0.0653 1424 ALA A CB    
1597 N  N     . GLY A 208 ? 0.6136 0.7736 0.6823 -0.0318 0.0323  -0.0673 1425 GLY A N     
1598 C  CA    . GLY A 208 ? 0.8284 0.9889 0.9017 -0.0319 0.0261  -0.0694 1425 GLY A CA    
1599 C  C     . GLY A 208 ? 0.8763 1.0425 0.9526 -0.0208 0.0196  -0.0730 1425 GLY A C     
1600 O  O     . GLY A 208 ? 0.8303 0.9993 0.9104 -0.0200 0.0141  -0.0754 1425 GLY A O     
1601 N  N     . GLY A 209 ? 1.0205 1.1891 1.0956 -0.0121 0.0200  -0.0737 1426 GLY A N     
1602 C  CA    . GLY A 209 ? 1.0931 1.2643 1.1699 -0.0009 0.0137  -0.0759 1426 GLY A CA    
1603 C  C     . GLY A 209 ? 1.0429 1.2372 1.1348 0.0029  0.0121  -0.0827 1426 GLY A C     
1604 O  O     . GLY A 209 ? 1.0726 1.2831 1.1753 -0.0036 0.0161  -0.0864 1426 GLY A O     
1605 N  N     . ASP A 210 ? 0.8363 1.0321 0.9290 0.0139  0.0062  -0.0838 1427 ASP A N     
1606 C  CA    . ASP A 210 ? 0.7763 0.9930 0.8827 0.0206  0.0036  -0.0899 1427 ASP A CA    
1607 C  C     . ASP A 210 ? 0.7710 0.9894 0.8783 0.0279  0.0069  -0.0912 1427 ASP A C     
1608 O  O     . ASP A 210 ? 0.8407 1.0738 0.9567 0.0253  0.0124  -0.0954 1427 ASP A O     
1609 C  CB    . ASP A 210 ? 0.8063 1.0229 0.9122 0.0290  -0.0053 -0.0899 1427 ASP A CB    
1610 C  CG    . ASP A 210 ? 0.7792 1.0190 0.9001 0.0302  -0.0092 -0.0964 1427 ASP A CG    
1611 O  OD1   . ASP A 210 ? 0.7313 0.9815 0.8599 0.0201  -0.0069 -0.0997 1427 ASP A OD1   
1612 O  OD2   . ASP A 210 ? 0.7655 1.0129 0.8908 0.0413  -0.0146 -0.0982 1427 ASP A OD2   
1613 N  N     . TYR A 211 ? 0.6711 0.8747 0.7697 0.0368  0.0037  -0.0878 1428 TYR A N     
1614 C  CA    . TYR A 211 ? 0.6582 0.8582 0.7553 0.0429  0.0070  -0.0887 1428 TYR A CA    
1615 C  C     . TYR A 211 ? 0.6867 0.8625 0.7684 0.0417  0.0080  -0.0823 1428 TYR A C     
1616 O  O     . TYR A 211 ? 0.3690 0.5313 0.4421 0.0391  0.0051  -0.0771 1428 TYR A O     
1617 C  CB    . TYR A 211 ? 0.5620 0.7681 0.6658 0.0562  0.0017  -0.0915 1428 TYR A CB    
1618 C  CG    . TYR A 211 ? 0.5611 0.7546 0.6583 0.0630  -0.0060 -0.0864 1428 TYR A CG    
1619 C  CD1   . TYR A 211 ? 0.5359 0.7072 0.6209 0.0662  -0.0070 -0.0804 1428 TYR A CD1   
1620 C  CD2   . TYR A 211 ? 0.5228 0.7273 0.6260 0.0661  -0.0123 -0.0876 1428 TYR A CD2   
1621 C  CE1   . TYR A 211 ? 0.4672 0.6274 0.5459 0.0722  -0.0134 -0.0750 1428 TYR A CE1   
1622 C  CE2   . TYR A 211 ? 0.5037 0.6973 0.5995 0.0726  -0.0191 -0.0824 1428 TYR A CE2   
1623 C  CZ    . TYR A 211 ? 0.5087 0.6802 0.5922 0.0755  -0.0193 -0.0758 1428 TYR A CZ    
1624 O  OH    . TYR A 211 ? 0.5690 0.7301 0.6450 0.0816  -0.0252 -0.0700 1428 TYR A OH    
1625 N  N     . THR A 212 ? 0.7364 0.9076 0.8152 0.0443  0.0119  -0.0833 1429 THR A N     
1626 C  CA    . THR A 212 ? 0.7814 0.9314 0.8472 0.0434  0.0130  -0.0783 1429 THR A CA    
1627 C  C     . THR A 212 ? 0.6861 0.8302 0.7520 0.0539  0.0113  -0.0801 1429 THR A C     
1628 O  O     . THR A 212 ? 0.5892 0.7446 0.6620 0.0577  0.0142  -0.0861 1429 THR A O     
1629 C  CB    . THR A 212 ? 0.8554 1.0040 0.9158 0.0338  0.0200  -0.0777 1429 THR A CB    
1630 O  OG1   . THR A 212 ? 0.9181 1.0649 0.9757 0.0240  0.0208  -0.0741 1429 THR A OG1   
1631 C  CG2   . THR A 212 ? 0.8554 0.9855 0.9043 0.0352  0.0210  -0.0746 1429 THR A CG2   
1632 N  N     . THR A 213 ? 0.6433 0.7699 0.7020 0.0585  0.0069  -0.0749 1430 THR A N     
1633 C  CA    . THR A 213 ? 0.6372 0.7530 0.6943 0.0669  0.0054  -0.0754 1430 THR A CA    
1634 C  C     . THR A 213 ? 0.7540 0.8565 0.8015 0.0618  0.0094  -0.0740 1430 THR A C     
1635 O  O     . THR A 213 ? 0.9170 1.0143 0.9571 0.0530  0.0118  -0.0702 1430 THR A O     
1636 C  CB    . THR A 213 ? 0.5377 0.6397 0.5913 0.0733  -0.0009 -0.0695 1430 THR A CB    
1637 O  OG1   . THR A 213 ? 0.7227 0.8113 0.7658 0.0663  -0.0008 -0.0629 1430 THR A OG1   
1638 C  CG2   . THR A 213 ? 0.5178 0.6327 0.5794 0.0786  -0.0056 -0.0705 1430 THR A CG2   
1639 N  N     . THR A 214 ? 0.6763 0.7732 0.7241 0.0680  0.0097  -0.0773 1431 THR A N     
1640 C  CA    . THR A 214 ? 0.5838 0.6673 0.6226 0.0646  0.0123  -0.0766 1431 THR A CA    
1641 C  C     . THR A 214 ? 0.6153 0.6867 0.6548 0.0734  0.0094  -0.0784 1431 THR A C     
1642 O  O     . THR A 214 ? 0.6654 0.7392 0.7127 0.0825  0.0059  -0.0806 1431 THR A O     
1643 C  CB    . THR A 214 ? 0.6124 0.7073 0.6501 0.0588  0.0190  -0.0816 1431 THR A CB    
1644 O  OG1   . THR A 214 ? 0.7621 0.8441 0.7901 0.0558  0.0206  -0.0807 1431 THR A OG1   
1645 C  CG2   . THR A 214 ? 0.4330 0.5440 0.4805 0.0653  0.0211  -0.0904 1431 THR A CG2   
1646 N  N     . VAL A 215 ? 0.6141 0.6714 0.6453 0.0703  0.0103  -0.0770 1432 VAL A N     
1647 C  CA    . VAL A 215 ? 0.4118 0.4553 0.4426 0.0764  0.0080  -0.0790 1432 VAL A CA    
1648 C  C     . VAL A 215 ? 0.5544 0.5984 0.5796 0.0723  0.0124  -0.0843 1432 VAL A C     
1649 O  O     . VAL A 215 ? 0.5610 0.5978 0.5771 0.0647  0.0138  -0.0804 1432 VAL A O     
1650 C  CB    . VAL A 215 ? 0.4121 0.4363 0.4381 0.0762  0.0038  -0.0708 1432 VAL A CB    
1651 C  CG1   . VAL A 215 ? 0.6075 0.6165 0.6303 0.0774  0.0029  -0.0722 1432 VAL A CG1   
1652 C  CG2   . VAL A 215 ? 0.4549 0.4778 0.4871 0.0838  -0.0010 -0.0673 1432 VAL A CG2   
1653 N  N     . GLU A 216 ? 0.5547 0.6085 0.5849 0.0774  0.0147  -0.0933 1433 GLU A N     
1654 C  CA    . GLU A 216 ? 0.5812 0.6387 0.6057 0.0743  0.0192  -0.0993 1433 GLU A CA    
1655 C  C     . GLU A 216 ? 0.6167 0.6590 0.6395 0.0793  0.0165  -0.1035 1433 GLU A C     
1656 O  O     . GLU A 216 ? 0.5507 0.5840 0.5800 0.0872  0.0121  -0.1042 1433 GLU A O     
1657 C  CB    . GLU A 216 ? 0.6977 0.7769 0.7282 0.0764  0.0243  -0.1075 1433 GLU A CB    
1658 C  CG    . GLU A 216 ? 0.9065 1.0024 0.9422 0.0724  0.0266  -0.1048 1433 GLU A CG    
1659 C  CD    . GLU A 216 ? 1.0337 1.1313 1.0607 0.0606  0.0302  -0.0987 1433 GLU A CD    
1660 O  OE1   . GLU A 216 ? 1.0923 1.1818 1.1170 0.0565  0.0274  -0.0909 1433 GLU A OE1   
1661 O  OE2   . GLU A 216 ? 1.0380 1.1449 1.0604 0.0557  0.0360  -0.1016 1433 GLU A OE2   
1662 N  N     . ALA A 217 ? 0.6697 0.7082 0.6834 0.0744  0.0187  -0.1057 1434 ALA A N     
1663 C  CA    . ALA A 217 ? 0.5445 0.5697 0.5562 0.0781  0.0162  -0.1109 1434 ALA A CA    
1664 C  C     . ALA A 217 ? 0.5436 0.5788 0.5493 0.0767  0.0209  -0.1196 1434 ALA A C     
1665 O  O     . ALA A 217 ? 0.5932 0.6419 0.5936 0.0706  0.0259  -0.1185 1434 ALA A O     
1666 C  CB    . ALA A 217 ? 0.4741 0.4804 0.4797 0.0732  0.0124  -0.1032 1434 ALA A CB    
1667 N  N     . TYR A 218 ? 0.6302 0.6589 0.6365 0.0822  0.0192  -0.1282 1435 TYR A N     
1668 C  CA    . TYR A 218 ? 0.7584 0.7985 0.7594 0.0826  0.0237  -0.1381 1435 TYR A CA    
1669 C  C     . TYR A 218 ? 0.6709 0.6980 0.6628 0.0800  0.0213  -0.1408 1435 TYR A C     
1670 O  O     . TYR A 218 ? 0.7950 0.8048 0.7903 0.0833  0.0158  -0.1417 1435 TYR A O     
1671 C  CB    . TYR A 218 ? 0.8724 0.9208 0.8829 0.0930  0.0245  -0.1493 1435 TYR A CB    
1672 C  CG    . TYR A 218 ? 0.9572 1.0208 0.9622 0.0936  0.0301  -0.1598 1435 TYR A CG    
1673 C  CD1   . TYR A 218 ? 1.0741 1.1568 1.0737 0.0874  0.0369  -0.1579 1435 TYR A CD1   
1674 C  CD2   . TYR A 218 ? 1.0375 1.0965 1.0428 0.1004  0.0287  -0.1715 1435 TYR A CD2   
1675 C  CE1   . TYR A 218 ? 1.1496 1.2471 1.1432 0.0879  0.0427  -0.1668 1435 TYR A CE1   
1676 C  CE2   . TYR A 218 ? 1.1962 1.2703 1.1955 0.1014  0.0341  -0.1816 1435 TYR A CE2   
1677 C  CZ    . TYR A 218 ? 1.2856 1.3794 1.2786 0.0951  0.0413  -0.1788 1435 TYR A CZ    
1678 O  OH    . TYR A 218 ? 1.3604 1.4703 1.3466 0.0960  0.0473  -0.1881 1435 TYR A OH    
1679 N  N     . ILE A 219 ? 0.6057 0.6409 0.5861 0.0738  0.0252  -0.1416 1436 ILE A N     
1680 C  CA    . ILE A 219 ? 0.8983 0.9245 0.8694 0.0718  0.0230  -0.1458 1436 ILE A CA    
1681 C  C     . ILE A 219 ? 0.9323 0.9718 0.8995 0.0761  0.0270  -0.1586 1436 ILE A C     
1682 O  O     . ILE A 219 ? 0.8927 0.9500 0.8537 0.0731  0.0333  -0.1593 1436 ILE A O     
1683 C  CB    . ILE A 219 ? 1.0315 1.0547 0.9913 0.0619  0.0231  -0.1362 1436 ILE A CB    
1684 C  CG1   . ILE A 219 ? 1.0908 1.1318 1.0409 0.0567  0.0299  -0.1353 1436 ILE A CG1   
1685 C  CG2   . ILE A 219 ? 0.9671 0.9819 0.9315 0.0581  0.0208  -0.1237 1436 ILE A CG2   
1686 C  CD1   . ILE A 219 ? 1.1166 1.1532 1.0546 0.0487  0.0293  -0.1282 1436 ILE A CD1   
1687 N  N     . SER A 220 ? 0.8497 0.8806 0.8209 0.0831  0.0233  -0.1690 1437 SER A N     
1688 C  CA    . SER A 220 ? 0.6520 0.6951 0.6203 0.0886  0.0268  -0.1828 1437 SER A CA    
1689 C  C     . SER A 220 ? 0.6317 0.6799 0.5840 0.0831  0.0287  -0.1855 1437 SER A C     
1690 O  O     . SER A 220 ? 0.7214 0.7868 0.6675 0.0847  0.0344  -0.1931 1437 SER A O     
1691 C  CB    . SER A 220 ? 0.6505 0.6812 0.6283 0.0980  0.0218  -0.1935 1437 SER A CB    
1692 O  OG    . SER A 220 ? 0.6813 0.6896 0.6613 0.0959  0.0147  -0.1886 1437 SER A OG    
1693 N  N     . ALA A 221 ? 0.6043 0.6386 0.5498 0.0770  0.0240  -0.1796 1438 ALA A N     
1694 C  CA    . ALA A 221 ? 0.6819 0.7209 0.6117 0.0719  0.0250  -0.1814 1438 ALA A CA    
1695 C  C     . ALA A 221 ? 0.7293 0.7893 0.6497 0.0678  0.0332  -0.1779 1438 ALA A C     
1696 O  O     . ALA A 221 ? 0.7606 0.8344 0.6725 0.0697  0.0375  -0.1866 1438 ALA A O     
1697 C  CB    . ALA A 221 ? 0.6661 0.6895 0.5917 0.0649  0.0193  -0.1718 1438 ALA A CB    
1698 N  N     . SER A 222 ? 0.6604 0.7230 0.5824 0.0619  0.0356  -0.1651 1439 SER A N     
1699 C  CA    . SER A 222 ? 0.6912 0.7728 0.6072 0.0574  0.0436  -0.1605 1439 SER A CA    
1700 C  C     . SER A 222 ? 0.8018 0.8988 0.7286 0.0628  0.0490  -0.1658 1439 SER A C     
1701 O  O     . SER A 222 ? 0.7703 0.8851 0.6939 0.0593  0.0563  -0.1634 1439 SER A O     
1702 C  CB    . SER A 222 ? 0.7542 0.8315 0.6681 0.0487  0.0436  -0.1455 1439 SER A CB    
1703 O  OG    . SER A 222 ? 0.8899 0.9688 0.8169 0.0497  0.0446  -0.1409 1439 SER A OG    
1704 N  N     . GLY A 223 ? 0.8773 0.9678 0.8174 0.0710  0.0454  -0.1723 1440 GLY A N     
1705 C  CA    . GLY A 223 ? 0.8170 0.9219 0.7691 0.0770  0.0496  -0.1774 1440 GLY A CA    
1706 C  C     . GLY A 223 ? 0.8948 1.0073 0.8540 0.0726  0.0525  -0.1669 1440 GLY A C     
1707 O  O     . GLY A 223 ? 0.9543 1.0852 0.9202 0.0748  0.0581  -0.1701 1440 GLY A O     
1708 N  N     . ARG A 224 ? 0.8741 0.9735 0.8327 0.0664  0.0486  -0.1551 1441 ARG A N     
1709 C  CA    . ARG A 224 ? 0.7415 0.8479 0.7043 0.0605  0.0513  -0.1448 1441 ARG A CA    
1710 C  C     . ARG A 224 ? 0.5959 0.6878 0.5687 0.0623  0.0451  -0.1386 1441 ARG A C     
1711 O  O     . ARG A 224 ? 0.5424 0.6160 0.5152 0.0645  0.0388  -0.1380 1441 ARG A O     
1712 C  CB    . ARG A 224 ? 0.7097 0.8159 0.6595 0.0498  0.0538  -0.1349 1441 ARG A CB    
1713 C  CG    . ARG A 224 ? 0.8828 1.0052 0.8215 0.0467  0.0609  -0.1383 1441 ARG A CG    
1714 C  CD    . ARG A 224 ? 0.9391 1.0618 0.8668 0.0361  0.0636  -0.1267 1441 ARG A CD    
1715 N  NE    . ARG A 224 ? 0.9461 1.0897 0.8698 0.0321  0.0725  -0.1266 1441 ARG A NE    
1716 C  CZ    . ARG A 224 ? 0.9250 1.0774 0.8355 0.0308  0.0769  -0.1299 1441 ARG A CZ    
1717 N  NH1   . ARG A 224 ? 0.9452 1.0872 0.8452 0.0334  0.0724  -0.1342 1441 ARG A NH1   
1718 N  NH2   . ARG A 224 ? 0.7654 0.9374 0.6732 0.0268  0.0856  -0.1288 1441 ARG A NH2   
1719 N  N     . ALA A 225 ? 0.5890 0.6899 0.5705 0.0611  0.0469  -0.1338 1442 ALA A N     
1720 C  CA    . ALA A 225 ? 0.5725 0.6615 0.5620 0.0623  0.0413  -0.1270 1442 ALA A CA    
1721 C  C     . ALA A 225 ? 0.7916 0.8747 0.7746 0.0526  0.0410  -0.1152 1442 ALA A C     
1722 O  O     . ALA A 225 ? 0.9432 1.0333 0.9176 0.0452  0.0455  -0.1121 1442 ALA A O     
1723 C  CB    . ALA A 225 ? 0.4504 0.5524 0.4538 0.0678  0.0422  -0.1295 1442 ALA A CB    
1724 N  N     . ILE A 226 ? 0.7891 0.8588 0.7762 0.0529  0.0356  -0.1085 1443 ILE A N     
1725 C  CA    . ILE A 226 ? 0.7296 0.7926 0.7114 0.0447  0.0348  -0.0980 1443 ILE A CA    
1726 C  C     . ILE A 226 ? 0.7139 0.7719 0.7043 0.0469  0.0308  -0.0928 1443 ILE A C     
1727 O  O     . ILE A 226 ? 0.7148 0.7658 0.7121 0.0543  0.0266  -0.0951 1443 ILE A O     
1728 C  CB    . ILE A 226 ? 0.7276 0.7747 0.6989 0.0411  0.0320  -0.0946 1443 ILE A CB    
1729 C  CG1   . ILE A 226 ? 0.7662 0.8080 0.7323 0.0329  0.0317  -0.0840 1443 ILE A CG1   
1730 C  CG2   . ILE A 226 ? 0.7050 0.7363 0.6804 0.0473  0.0259  -0.0965 1443 ILE A CG2   
1731 C  CD1   . ILE A 226 ? 0.7210 0.7569 0.6748 0.0269  0.0321  -0.0808 1443 ILE A CD1   
1732 N  N     . GLN A 227 ? 0.6406 0.7027 0.6307 0.0404  0.0321  -0.0859 1444 GLN A N     
1733 C  CA    . GLN A 227 ? 0.6279 0.6860 0.6241 0.0415  0.0284  -0.0806 1444 GLN A CA    
1734 C  C     . GLN A 227 ? 0.5891 0.6281 0.5801 0.0403  0.0237  -0.0739 1444 GLN A C     
1735 O  O     . GLN A 227 ? 0.5668 0.5999 0.5494 0.0336  0.0246  -0.0691 1444 GLN A O     
1736 C  CB    . GLN A 227 ? 0.7298 0.7994 0.7273 0.0346  0.0317  -0.0768 1444 GLN A CB    
1737 C  CG    . GLN A 227 ? 0.7964 0.8675 0.8013 0.0359  0.0284  -0.0735 1444 GLN A CG    
1738 C  CD    . GLN A 227 ? 0.8756 0.9599 0.8830 0.0287  0.0321  -0.0718 1444 GLN A CD    
1739 O  OE1   . GLN A 227 ? 1.1032 1.1876 1.1037 0.0208  0.0358  -0.0688 1444 GLN A OE1   
1740 N  NE2   . GLN A 227 ? 0.8310 0.9267 0.8485 0.0313  0.0310  -0.0737 1444 GLN A NE2   
1741 N  N     . GLY A 228 ? 0.6451 0.6746 0.6411 0.0466  0.0189  -0.0730 1445 GLY A N     
1742 C  CA    . GLY A 228 ? 0.5078 0.5198 0.4998 0.0457  0.0149  -0.0668 1445 GLY A CA    
1743 C  C     . GLY A 228 ? 0.5130 0.5223 0.5049 0.0427  0.0132  -0.0588 1445 GLY A C     
1744 O  O     . GLY A 228 ? 0.5742 0.5714 0.5614 0.0398  0.0112  -0.0529 1445 GLY A O     
1745 N  N     . ALA A 229 ? 0.4324 0.4533 0.4301 0.0437  0.0137  -0.0590 1446 ALA A N     
1746 C  CA    . ALA A 229 ? 0.4466 0.4665 0.4440 0.0411  0.0120  -0.0527 1446 ALA A CA    
1747 C  C     . ALA A 229 ? 0.4663 0.5029 0.4710 0.0418  0.0131  -0.0557 1446 ALA A C     
1748 O  O     . ALA A 229 ? 0.4092 0.4575 0.4195 0.0449  0.0152  -0.0622 1446 ALA A O     
1749 C  CB    . ALA A 229 ? 0.3895 0.3970 0.3877 0.0460  0.0072  -0.0477 1446 ALA A CB    
1750 N  N     . THR A 230 ? 0.4380 0.4765 0.4427 0.0388  0.0119  -0.0515 1447 THR A N     
1751 C  CA    . THR A 230 ? 0.6503 0.7046 0.6628 0.0393  0.0119  -0.0543 1447 THR A CA    
1752 C  C     . THR A 230 ? 0.6850 0.7367 0.6981 0.0413  0.0074  -0.0500 1447 THR A C     
1753 O  O     . THR A 230 ? 0.7655 0.8059 0.7718 0.0383  0.0061  -0.0444 1447 THR A O     
1754 C  CB    . THR A 230 ? 0.7221 0.7876 0.7349 0.0306  0.0164  -0.0557 1447 THR A CB    
1755 O  OG1   . THR A 230 ? 0.7969 0.8515 0.8008 0.0233  0.0176  -0.0504 1447 THR A OG1   
1756 C  CG2   . THR A 230 ? 0.7834 0.8604 0.7993 0.0302  0.0212  -0.0616 1447 THR A CG2   
1757 N  N     . SER A 231 ? 0.4819 0.5458 0.5033 0.0464  0.0051  -0.0531 1448 SER A N     
1758 C  CA    . SER A 231 ? 0.5287 0.5949 0.5514 0.0486  0.0007  -0.0504 1448 SER A CA    
1759 C  C     . SER A 231 ? 0.5547 0.6405 0.5865 0.0468  0.0015  -0.0558 1448 SER A C     
1760 O  O     . SER A 231 ? 0.4778 0.5753 0.5179 0.0514  0.0020  -0.0611 1448 SER A O     
1761 C  CB    . SER A 231 ? 0.4029 0.4635 0.4271 0.0587  -0.0042 -0.0482 1448 SER A CB    
1762 O  OG    . SER A 231 ? 0.5361 0.5937 0.5568 0.0600  -0.0082 -0.0433 1448 SER A OG    
1763 N  N     . HIS A 232 ? 0.5501 0.6396 0.5808 0.0395  0.0019  -0.0549 1449 HIS A N     
1764 C  CA    . HIS A 232 ? 0.5184 0.6263 0.5584 0.0362  0.0027  -0.0600 1449 HIS A CA    
1765 C  C     . HIS A 232 ? 0.5562 0.6700 0.5992 0.0399  -0.0032 -0.0599 1449 HIS A C     
1766 O  O     . HIS A 232 ? 0.6391 0.7417 0.6746 0.0417  -0.0066 -0.0551 1449 HIS A O     
1767 C  CB    . HIS A 232 ? 0.6063 0.7151 0.6445 0.0247  0.0072  -0.0597 1449 HIS A CB    
1768 C  CG    . HIS A 232 ? 0.7209 0.8190 0.7515 0.0204  0.0120  -0.0572 1449 HIS A CG    
1769 N  ND1   . HIS A 232 ? 0.8016 0.9064 0.8347 0.0200  0.0167  -0.0606 1449 HIS A ND1   
1770 C  CD2   . HIS A 232 ? 0.7900 0.8721 0.8105 0.0163  0.0128  -0.0519 1449 HIS A CD2   
1771 C  CE1   . HIS A 232 ? 0.8174 0.9106 0.8415 0.0159  0.0198  -0.0574 1449 HIS A CE1   
1772 N  NE2   . HIS A 232 ? 0.7810 0.8603 0.7978 0.0136  0.0174  -0.0520 1449 HIS A NE2   
1773 N  N     . HIS A 233 ? 0.5232 0.6558 0.5774 0.0413  -0.0045 -0.0655 1450 HIS A N     
1774 C  CA    . HIS A 233 ? 0.5583 0.6997 0.6160 0.0422  -0.0098 -0.0668 1450 HIS A CA    
1775 C  C     . HIS A 233 ? 0.6750 0.8267 0.7382 0.0316  -0.0071 -0.0704 1450 HIS A C     
1776 O  O     . HIS A 233 ? 0.7221 0.8893 0.7958 0.0287  -0.0040 -0.0755 1450 HIS A O     
1777 C  CB    . HIS A 233 ? 0.4986 0.6545 0.5658 0.0519  -0.0144 -0.0705 1450 HIS A CB    
1778 C  CG    . HIS A 233 ? 0.4615 0.6274 0.5317 0.0531  -0.0205 -0.0720 1450 HIS A CG    
1779 N  ND1   . HIS A 233 ? 0.5070 0.6621 0.5670 0.0531  -0.0242 -0.0676 1450 HIS A ND1   
1780 C  CD2   . HIS A 233 ? 0.4515 0.6378 0.5335 0.0541  -0.0236 -0.0781 1450 HIS A CD2   
1781 C  CE1   . HIS A 233 ? 0.4461 0.6144 0.5108 0.0543  -0.0295 -0.0710 1450 HIS A CE1   
1782 N  NE2   . HIS A 233 ? 0.4319 0.6192 0.5103 0.0548  -0.0295 -0.0774 1450 HIS A NE2   
1783 N  N     . LEU A 234 ? 0.6697 0.8130 0.7264 0.0259  -0.0082 -0.0680 1451 LEU A N     
1784 C  CA    . LEU A 234 ? 0.6541 0.8046 0.7161 0.0153  -0.0060 -0.0711 1451 LEU A CA    
1785 C  C     . LEU A 234 ? 0.6319 0.8003 0.7044 0.0160  -0.0108 -0.0770 1451 LEU A C     
1786 O  O     . LEU A 234 ? 0.6393 0.8180 0.7203 0.0075  -0.0090 -0.0811 1451 LEU A O     
1787 C  CB    . LEU A 234 ? 0.5361 0.6696 0.5876 0.0090  -0.0051 -0.0668 1451 LEU A CB    
1788 C  CG    . LEU A 234 ? 0.5385 0.6561 0.5805 0.0091  -0.0009 -0.0613 1451 LEU A CG    
1789 C  CD1   . LEU A 234 ? 0.3650 0.4655 0.3967 0.0041  -0.0002 -0.0566 1451 LEU A CD1   
1790 C  CD2   . LEU A 234 ? 0.3642 0.4887 0.4114 0.0050  0.0054  -0.0630 1451 LEU A CD2   
1791 N  N     . GLY A 235 ? 0.4030 0.5747 0.4748 0.0257  -0.0173 -0.0772 1452 GLY A N     
1792 C  CA    . GLY A 235 ? 0.4014 0.5910 0.4829 0.0266  -0.0227 -0.0830 1452 GLY A CA    
1793 C  C     . GLY A 235 ? 0.5126 0.6990 0.5915 0.0184  -0.0243 -0.0845 1452 GLY A C     
1794 O  O     . GLY A 235 ? 0.6848 0.8550 0.7515 0.0181  -0.0252 -0.0802 1452 GLY A O     
1795 N  N     . GLN A 236 ? 0.4526 0.6547 0.5439 0.0115  -0.0245 -0.0910 1453 GLN A N     
1796 C  CA    . GLN A 236 ? 0.5162 0.7163 0.6073 0.0031  -0.0264 -0.0938 1453 GLN A CA    
1797 C  C     . GLN A 236 ? 0.5944 0.7916 0.6903 -0.0099 -0.0196 -0.0943 1453 GLN A C     
1798 O  O     . GLN A 236 ? 0.5460 0.7434 0.6451 -0.0178 -0.0210 -0.0978 1453 GLN A O     
1799 C  CB    . GLN A 236 ? 0.4261 0.6461 0.5280 0.0044  -0.0332 -0.1015 1453 GLN A CB    
1800 C  CG    . GLN A 236 ? 0.3804 0.5998 0.4743 0.0137  -0.0412 -0.1014 1453 GLN A CG    
1801 C  CD    . GLN A 236 ? 0.5389 0.7809 0.6454 0.0149  -0.0478 -0.1095 1453 GLN A CD    
1802 O  OE1   . GLN A 236 ? 0.3811 0.6398 0.5029 0.0116  -0.0459 -0.1140 1453 GLN A OE1   
1803 N  NE2   . GLN A 236 ? 0.6045 0.8484 0.7049 0.0199  -0.0555 -0.1115 1453 GLN A NE2   
1804 N  N     . ASN A 237 ? 0.6223 0.8168 0.7187 -0.0123 -0.0125 -0.0910 1454 ASN A N     
1805 C  CA    . ASN A 237 ? 0.5363 0.7279 0.6363 -0.0246 -0.0060 -0.0904 1454 ASN A CA    
1806 C  C     . ASN A 237 ? 0.6180 0.7890 0.7068 -0.0298 -0.0058 -0.0865 1454 ASN A C     
1807 O  O     . ASN A 237 ? 0.6900 0.8603 0.7835 -0.0390 -0.0058 -0.0891 1454 ASN A O     
1808 C  CB    . ASN A 237 ? 0.5176 0.7081 0.6167 -0.0252 0.0015  -0.0867 1454 ASN A CB    
1809 C  CG    . ASN A 237 ? 0.6118 0.8175 0.7177 -0.0164 0.0010  -0.0894 1454 ASN A CG    
1810 O  OD1   . ASN A 237 ? 0.6455 0.8708 0.7653 -0.0190 0.0031  -0.0943 1454 ASN A OD1   
1811 N  ND2   . ASN A 237 ? 0.6349 0.8317 0.7317 -0.0058 -0.0015 -0.0863 1454 ASN A ND2   
1812 N  N     . PHE A 238 ? 0.5716 0.7255 0.6463 -0.0239 -0.0058 -0.0806 1455 PHE A N     
1813 C  CA    . PHE A 238 ? 0.6178 0.7523 0.6822 -0.0283 -0.0050 -0.0766 1455 PHE A CA    
1814 C  C     . PHE A 238 ? 0.5640 0.6967 0.6264 -0.0272 -0.0115 -0.0803 1455 PHE A C     
1815 O  O     . PHE A 238 ? 0.5569 0.6797 0.6173 -0.0341 -0.0112 -0.0806 1455 PHE A O     
1816 C  CB    . PHE A 238 ? 0.6498 0.7685 0.7012 -0.0225 -0.0030 -0.0695 1455 PHE A CB    
1817 C  CG    . PHE A 238 ? 0.5711 0.6861 0.6215 -0.0268 0.0041  -0.0655 1455 PHE A CG    
1818 C  CD1   . PHE A 238 ? 0.5130 0.6380 0.5674 -0.0224 0.0065  -0.0661 1455 PHE A CD1   
1819 C  CD2   . PHE A 238 ? 0.3965 0.4980 0.4417 -0.0346 0.0081  -0.0614 1455 PHE A CD2   
1820 C  CE1   . PHE A 238 ? 0.4414 0.5638 0.4938 -0.0258 0.0129  -0.0631 1455 PHE A CE1   
1821 C  CE2   . PHE A 238 ? 0.3743 0.4730 0.4174 -0.0380 0.0142  -0.0576 1455 PHE A CE2   
1822 C  CZ    . PHE A 238 ? 0.4876 0.5972 0.5340 -0.0338 0.0167  -0.0586 1455 PHE A CZ    
1823 N  N     . SER A 239 ? 0.5579 0.6999 0.6204 -0.0185 -0.0175 -0.0831 1456 SER A N     
1824 C  CA    . SER A 239 ? 0.5040 0.6467 0.5644 -0.0173 -0.0239 -0.0875 1456 SER A CA    
1825 C  C     . SER A 239 ? 0.4677 0.6202 0.5403 -0.0269 -0.0250 -0.0949 1456 SER A C     
1826 O  O     . SER A 239 ? 0.3980 0.5465 0.4686 -0.0294 -0.0288 -0.0988 1456 SER A O     
1827 C  CB    . SER A 239 ? 0.5386 0.6924 0.5979 -0.0062 -0.0303 -0.0892 1456 SER A CB    
1828 O  OG    . SER A 239 ? 0.5792 0.7527 0.6519 -0.0054 -0.0311 -0.0935 1456 SER A OG    
1829 N  N     . ARG A 240 ? 0.4267 0.5928 0.5126 -0.0324 -0.0218 -0.0973 1457 ARG A N     
1830 C  CA    . ARG A 240 ? 0.5102 0.6860 0.6096 -0.0429 -0.0220 -0.1038 1457 ARG A CA    
1831 C  C     . ARG A 240 ? 0.6777 0.8381 0.7760 -0.0541 -0.0162 -0.1006 1457 ARG A C     
1832 O  O     . ARG A 240 ? 0.8353 0.9930 0.9383 -0.0617 -0.0182 -0.1051 1457 ARG A O     
1833 C  CB    . ARG A 240 ? 0.4607 0.6591 0.5757 -0.0439 -0.0206 -0.1075 1457 ARG A CB    
1834 C  CG    . ARG A 240 ? 0.4875 0.7039 0.6079 -0.0353 -0.0285 -0.1136 1457 ARG A CG    
1835 C  CD    . ARG A 240 ? 0.6515 0.8929 0.7910 -0.0385 -0.0284 -0.1198 1457 ARG A CD    
1836 N  NE    . ARG A 240 ? 0.7935 1.0520 0.9401 -0.0336 -0.0375 -0.1276 1457 ARG A NE    
1837 C  CZ    . ARG A 240 ? 0.7917 1.0640 0.9401 -0.0223 -0.0422 -0.1288 1457 ARG A CZ    
1838 N  NH1   . ARG A 240 ? 0.9230 1.1931 1.0672 -0.0147 -0.0385 -0.1231 1457 ARG A NH1   
1839 N  NH2   . ARG A 240 ? 0.6745 0.9626 0.8290 -0.0183 -0.0508 -0.1359 1457 ARG A NH2   
1840 N  N     . MET A 241 ? 0.7221 0.8726 0.8146 -0.0553 -0.0094 -0.0931 1458 MET A N     
1841 C  CA    . MET A 241 ? 0.6253 0.7601 0.7152 -0.0649 -0.0042 -0.0887 1458 MET A CA    
1842 C  C     . MET A 241 ? 0.7770 0.8943 0.8577 -0.0648 -0.0078 -0.0888 1458 MET A C     
1843 O  O     . MET A 241 ? 0.9569 1.0678 1.0420 -0.0736 -0.0078 -0.0912 1458 MET A O     
1844 C  CB    . MET A 241 ? 0.6150 0.7405 0.6963 -0.0635 0.0023  -0.0803 1458 MET A CB    
1845 C  CG    . MET A 241 ? 0.8353 0.9747 0.9260 -0.0679 0.0083  -0.0797 1458 MET A CG    
1846 S  SD    . MET A 241 ? 0.9465 1.0741 1.0257 -0.0669 0.0157  -0.0705 1458 MET A SD    
1847 C  CE    . MET A 241 ? 0.9904 1.1005 1.0667 -0.0791 0.0198  -0.0653 1458 MET A CE    
1848 N  N     . PHE A 242 ? 0.6662 0.7756 0.7344 -0.0549 -0.0108 -0.0865 1459 PHE A N     
1849 C  CA    . PHE A 242 ? 0.6014 0.6939 0.6592 -0.0534 -0.0133 -0.0857 1459 PHE A CA    
1850 C  C     . PHE A 242 ? 0.7004 0.7997 0.7580 -0.0486 -0.0208 -0.0931 1459 PHE A C     
1851 O  O     . PHE A 242 ? 0.8201 0.9076 0.8684 -0.0457 -0.0233 -0.0934 1459 PHE A O     
1852 C  CB    . PHE A 242 ? 0.5267 0.6058 0.5705 -0.0460 -0.0112 -0.0777 1459 PHE A CB    
1853 C  CG    . PHE A 242 ? 0.4361 0.5065 0.4779 -0.0505 -0.0045 -0.0707 1459 PHE A CG    
1854 C  CD1   . PHE A 242 ? 0.3977 0.4504 0.4337 -0.0551 -0.0019 -0.0664 1459 PHE A CD1   
1855 C  CD2   . PHE A 242 ? 0.3889 0.4696 0.4349 -0.0500 -0.0008 -0.0687 1459 PHE A CD2   
1856 C  CE1   . PHE A 242 ? 0.4921 0.5374 0.5255 -0.0590 0.0038  -0.0598 1459 PHE A CE1   
1857 C  CE2   . PHE A 242 ? 0.4964 0.5701 0.5396 -0.0540 0.0052  -0.0626 1459 PHE A CE2   
1858 C  CZ    . PHE A 242 ? 0.5953 0.6514 0.6319 -0.0585 0.0074  -0.0578 1459 PHE A CZ    
1859 N  N     . ASP A 243 ? 0.7250 0.8439 0.7926 -0.0474 -0.0245 -0.0992 1460 ASP A N     
1860 C  CA    . ASP A 243 ? 0.7646 0.8926 0.8335 -0.0440 -0.0322 -0.1074 1460 ASP A CA    
1861 C  C     . ASP A 243 ? 0.6851 0.8063 0.7386 -0.0327 -0.0356 -0.1046 1460 ASP A C     
1862 O  O     . ASP A 243 ? 0.7213 0.8367 0.7683 -0.0311 -0.0395 -0.1083 1460 ASP A O     
1863 C  CB    . ASP A 243 ? 0.8353 0.9583 0.9102 -0.0536 -0.0338 -0.1141 1460 ASP A CB    
1864 C  CG    . ASP A 243 ? 0.8710 1.0068 0.9638 -0.0642 -0.0322 -0.1185 1460 ASP A CG    
1865 O  OD1   . ASP A 243 ? 0.8846 1.0107 0.9820 -0.0741 -0.0268 -0.1158 1460 ASP A OD1   
1866 O  OD2   . ASP A 243 ? 0.8844 1.0405 0.9871 -0.0625 -0.0363 -0.1246 1460 ASP A OD2   
1867 N  N     . ILE A 244 ? 0.5544 0.6764 0.6025 -0.0250 -0.0337 -0.0980 1461 ILE A N     
1868 C  CA    . ILE A 244 ? 0.5597 0.6775 0.5946 -0.0141 -0.0365 -0.0941 1461 ILE A CA    
1869 C  C     . ILE A 244 ? 0.6293 0.7655 0.6675 -0.0074 -0.0436 -0.0996 1461 ILE A C     
1870 O  O     . ILE A 244 ? 0.6992 0.8479 0.7436 -0.0034 -0.0441 -0.0988 1461 ILE A O     
1871 C  CB    . ILE A 244 ? 0.4801 0.5902 0.5089 -0.0093 -0.0318 -0.0849 1461 ILE A CB    
1872 C  CG1   . ILE A 244 ? 0.3905 0.4882 0.4207 -0.0178 -0.0250 -0.0810 1461 ILE A CG1   
1873 C  CG2   . ILE A 244 ? 0.4223 0.5225 0.4366 -0.0005 -0.0334 -0.0798 1461 ILE A CG2   
1874 C  CD1   . ILE A 244 ? 0.4644 0.5552 0.4900 -0.0147 -0.0202 -0.0732 1461 ILE A CD1   
1875 N  N     . VAL A 245 ? 0.6628 0.8011 0.6973 -0.0062 -0.0491 -0.1056 1462 VAL A N     
1876 C  CA    . VAL A 245 ? 0.5630 0.7202 0.6023 -0.0020 -0.0567 -0.1128 1462 VAL A CA    
1877 C  C     . VAL A 245 ? 0.4738 0.6292 0.4984 0.0072  -0.0618 -0.1127 1462 VAL A C     
1878 O  O     . VAL A 245 ? 0.4915 0.6318 0.5043 0.0083  -0.0596 -0.1092 1462 VAL A O     
1879 C  CB    . VAL A 245 ? 0.4410 0.6069 0.4936 -0.0119 -0.0592 -0.1232 1462 VAL A CB    
1880 C  CG1   . VAL A 245 ? 0.4381 0.6102 0.5061 -0.0203 -0.0543 -0.1231 1462 VAL A CG1   
1881 C  CG2   . VAL A 245 ? 0.4230 0.5725 0.4704 -0.0181 -0.0578 -0.1255 1462 VAL A CG2   
1882 N  N     . TYR A 246 ? 0.4230 0.5955 0.4490 0.0137  -0.0688 -0.1169 1463 TYR A N     
1883 C  CA    . TYR A 246 ? 0.5680 0.7427 0.5807 0.0223  -0.0746 -0.1179 1463 TYR A CA    
1884 C  C     . TYR A 246 ? 0.5641 0.7604 0.5845 0.0240  -0.0831 -0.1274 1463 TYR A C     
1885 O  O     . TYR A 246 ? 0.4336 0.6433 0.4693 0.0204  -0.0842 -0.1313 1463 TYR A O     
1886 C  CB    . TYR A 246 ? 0.6781 0.8481 0.6782 0.0333  -0.0736 -0.1071 1463 TYR A CB    
1887 C  CG    . TYR A 246 ? 0.7794 0.9613 0.7874 0.0386  -0.0749 -0.1037 1463 TYR A CG    
1888 C  CD1   . TYR A 246 ? 0.7658 0.9626 0.7714 0.0482  -0.0822 -0.1044 1463 TYR A CD1   
1889 C  CD2   . TYR A 246 ? 0.7444 0.9229 0.7618 0.0345  -0.0690 -0.1002 1463 TYR A CD2   
1890 C  CE1   . TYR A 246 ? 0.7745 0.9818 0.7883 0.0536  -0.0836 -0.1017 1463 TYR A CE1   
1891 C  CE2   . TYR A 246 ? 0.8256 1.0149 0.8507 0.0397  -0.0700 -0.0980 1463 TYR A CE2   
1892 C  CZ    . TYR A 246 ? 0.7928 0.9961 0.8166 0.0493  -0.0773 -0.0988 1463 TYR A CZ    
1893 O  OH    . TYR A 246 ? 0.6903 0.9038 0.7229 0.0547  -0.0782 -0.0969 1463 TYR A OH    
1894 N  N     . GLU A 247 ? 0.7179 0.9181 0.7278 0.0293  -0.0892 -0.1317 1464 GLU A N     
1895 C  CA    . GLU A 247 ? 0.8088 1.0302 0.8241 0.0322  -0.0983 -0.1407 1464 GLU A CA    
1896 C  C     . GLU A 247 ? 0.8592 1.0905 0.8685 0.0446  -0.1020 -0.1338 1464 GLU A C     
1897 O  O     . GLU A 247 ? 0.9970 1.2185 0.9910 0.0524  -0.1001 -0.1246 1464 GLU A O     
1898 C  CB    . GLU A 247 ? 0.9031 1.1257 0.9098 0.0323  -0.1039 -0.1498 1464 GLU A CB    
1899 C  CG    . GLU A 247 ? 1.0310 1.2762 1.0462 0.0330  -0.1136 -0.1612 1464 GLU A CG    
1900 C  CD    . GLU A 247 ? 1.0904 1.3381 1.0947 0.0351  -0.1199 -0.1703 1464 GLU A CD    
1901 O  OE1   . GLU A 247 ? 1.1422 1.3832 1.1512 0.0260  -0.1193 -0.1791 1464 GLU A OE1   
1902 O  OE2   . GLU A 247 ? 1.0219 1.2780 1.0126 0.0459  -0.1254 -0.1685 1464 GLU A OE2   
1903 N  N     . HIS A 248 ? 0.8592 1.1098 0.8813 0.0463  -0.1071 -0.1380 1465 HIS A N     
1904 C  CA    . HIS A 248 ? 0.9342 1.1950 0.9528 0.0582  -0.1112 -0.1318 1465 HIS A CA    
1905 C  C     . HIS A 248 ? 0.9031 1.1692 0.9052 0.0680  -0.1186 -0.1320 1465 HIS A C     
1906 O  O     . HIS A 248 ? 0.9324 1.2039 0.9316 0.0652  -0.1234 -0.1415 1465 HIS A O     
1907 C  CB    . HIS A 248 ? 0.9606 1.2428 0.9982 0.0578  -0.1156 -0.1377 1465 HIS A CB    
1908 C  CG    . HIS A 248 ? 0.9217 1.2122 0.9582 0.0700  -0.1187 -0.1303 1465 HIS A CG    
1909 N  ND1   . HIS A 248 ? 0.9088 1.2159 0.9414 0.0800  -0.1284 -0.1324 1465 HIS A ND1   
1910 C  CD2   . HIS A 248 ? 0.8889 1.1721 0.9267 0.0743  -0.1135 -0.1208 1465 HIS A CD2   
1911 C  CE1   . HIS A 248 ? 0.9105 1.2199 0.9428 0.0899  -0.1291 -0.1240 1465 HIS A CE1   
1912 N  NE2   . HIS A 248 ? 0.8964 1.1913 0.9321 0.0867  -0.1201 -0.1172 1465 HIS A NE2   
1913 N  N     . PRO A 249 ? 0.9130 1.1769 0.9032 0.0794  -0.1193 -0.1213 1466 PRO A N     
1914 C  CA    . PRO A 249 ? 1.0423 1.3120 1.0155 0.0890  -0.1261 -0.1204 1466 PRO A CA    
1915 C  C     . PRO A 249 ? 1.1210 1.4146 1.1007 0.0911  -0.1368 -0.1317 1466 PRO A C     
1916 O  O     . PRO A 249 ? 1.0481 1.3461 1.0242 0.0874  -0.1407 -0.1417 1466 PRO A O     
1917 C  CB    . PRO A 249 ? 1.0003 1.2655 0.9651 0.1002  -0.1251 -0.1064 1466 PRO A CB    
1918 C  CG    . PRO A 249 ? 0.8652 1.1137 0.8367 0.0950  -0.1154 -0.0994 1466 PRO A CG    
1919 C  CD    . PRO A 249 ? 0.8171 1.0710 0.8076 0.0837  -0.1136 -0.1093 1466 PRO A CD    
1920 N  N     . GLU A 250 ? 1.1971 1.5064 1.1880 0.0965  -0.1417 -0.1312 1467 GLU A N     
1921 C  CA    . GLU A 250 ? 1.2356 1.5696 1.2354 0.0984  -0.1522 -0.1422 1467 GLU A CA    
1922 C  C     . GLU A 250 ? 1.2487 1.5887 1.2652 0.0848  -0.1521 -0.1561 1467 GLU A C     
1923 O  O     . GLU A 250 ? 1.2603 1.6032 1.2720 0.0811  -0.1563 -0.1657 1467 GLU A O     
1924 C  CB    . GLU A 250 ? 1.2133 1.5621 1.2243 0.1065  -0.1564 -0.1384 1467 GLU A CB    
1925 N  N     . THR A 251 ? 1.2291 1.5705 1.2650 0.0771  -0.1472 -0.1574 1468 THR A N     
1926 C  CA    . THR A 251 ? 1.2403 1.5873 1.2937 0.0635  -0.1465 -0.1695 1468 THR A CA    
1927 C  C     . THR A 251 ? 1.2503 1.5767 1.2955 0.0543  -0.1405 -0.1712 1468 THR A C     
1928 O  O     . THR A 251 ? 1.2017 1.5139 1.2535 0.0454  -0.1315 -0.1682 1468 THR A O     
1929 C  CB    . THR A 251 ? 1.2909 1.6426 1.3652 0.0574  -0.1410 -0.1687 1468 THR A CB    
1930 O  OG1   . THR A 251 ? 1.3760 1.7054 1.4481 0.0506  -0.1298 -0.1616 1468 THR A OG1   
1931 C  CG2   . THR A 251 ? 1.2496 1.6130 1.3270 0.0692  -0.1438 -0.1620 1468 THR A CG2   
1932 N  N     . LYS A 252 ? 1.2960 1.6204 1.3259 0.0574  -0.1452 -0.1753 1469 LYS A N     
1933 C  CA    . LYS A 252 ? 1.3000 1.6049 1.3197 0.0512  -0.1402 -0.1768 1469 LYS A CA    
1934 C  C     . LYS A 252 ? 1.3037 1.6028 1.3400 0.0361  -0.1360 -0.1850 1469 LYS A C     
1935 O  O     . LYS A 252 ? 1.2949 1.6097 1.3491 0.0296  -0.1404 -0.1948 1469 LYS A O     
1936 C  CB    . LYS A 252 ? 1.2352 1.5455 1.2393 0.0567  -0.1480 -0.1839 1469 LYS A CB    
1937 N  N     . GLU A 253 ? 1.0449 1.3443 1.1146 0.0239  -0.1229 -0.1762 1470 GLU A N     
1938 C  CA    . GLU A 253 ? 0.8790 1.1790 0.9676 0.0130  -0.1166 -0.1769 1470 GLU A CA    
1939 C  C     . GLU A 253 ? 0.8268 1.1054 0.9089 0.0117  -0.1060 -0.1651 1470 GLU A C     
1940 O  O     . GLU A 253 ? 0.7403 1.0110 0.8086 0.0215  -0.1044 -0.1555 1470 GLU A O     
1941 C  CB    . GLU A 253 ? 0.9763 1.3000 1.0813 0.0160  -0.1201 -0.1788 1470 GLU A CB    
1942 C  CG    . GLU A 253 ? 1.0451 1.3782 1.1734 0.0033  -0.1166 -0.1846 1470 GLU A CG    
1943 C  CD    . GLU A 253 ? 1.1225 1.4835 1.2674 0.0070  -0.1223 -0.1895 1470 GLU A CD    
1944 O  OE1   . GLU A 253 ? 1.1381 1.5056 1.2786 0.0191  -0.1241 -0.1832 1470 GLU A OE1   
1945 O  OE2   . GLU A 253 ? 1.1444 1.5210 1.3076 -0.0021 -0.1253 -0.1998 1470 GLU A OE2   
1946 N  N     . LYS A 254 ? 0.9756 1.2456 1.0683 -0.0005 -0.0990 -0.1658 1471 LYS A N     
1947 C  CA    . LYS A 254 ? 0.8178 1.0663 0.9035 -0.0029 -0.0892 -0.1555 1471 LYS A CA    
1948 C  C     . LYS A 254 ? 0.6739 0.9268 0.7622 0.0031  -0.0854 -0.1471 1471 LYS A C     
1949 O  O     . LYS A 254 ? 0.6390 0.9064 0.7436 -0.0004 -0.0843 -0.1496 1471 LYS A O     
1950 C  CB    . LYS A 254 ? 0.6724 0.9115 0.7688 -0.0174 -0.0830 -0.1580 1471 LYS A CB    
1951 N  N     . GLU A 255 ? 0.6355 0.8761 0.7083 0.0123  -0.0833 -0.1375 1472 GLU A N     
1952 C  CA    . GLU A 255 ? 0.6112 0.8520 0.6850 0.0182  -0.0793 -0.1292 1472 GLU A CA    
1953 C  C     . GLU A 255 ? 0.6396 0.8587 0.7071 0.0136  -0.0700 -0.1212 1472 GLU A C     
1954 O  O     . GLU A 255 ? 0.6410 0.8433 0.6963 0.0121  -0.0682 -0.1187 1472 GLU A O     
1955 C  CB    . GLU A 255 ? 0.6622 0.9060 0.7245 0.0324  -0.0844 -0.1239 1472 GLU A CB    
1956 C  CG    . GLU A 255 ? 0.7683 1.0363 0.8391 0.0386  -0.0934 -0.1303 1472 GLU A CG    
1957 C  CD    . GLU A 255 ? 0.8741 1.1595 0.9662 0.0340  -0.0922 -0.1352 1472 GLU A CD    
1958 O  OE1   . GLU A 255 ? 0.8901 1.1695 0.9874 0.0311  -0.0845 -0.1304 1472 GLU A OE1   
1959 O  OE2   . GLU A 255 ? 0.8195 1.1257 0.9230 0.0337  -0.0991 -0.1440 1472 GLU A OE2   
1960 N  N     . TYR A 256 ? 0.7577 0.9784 0.8341 0.0110  -0.0643 -0.1180 1473 TYR A N     
1961 C  CA    . TYR A 256 ? 0.7588 0.9610 0.8297 0.0073  -0.0558 -0.1103 1473 TYR A CA    
1962 C  C     . TYR A 256 ? 0.7536 0.9489 0.8148 0.0181  -0.0546 -0.1016 1473 TYR A C     
1963 O  O     . TYR A 256 ? 0.6861 0.8938 0.7510 0.0265  -0.0581 -0.1014 1473 TYR A O     
1964 C  CB    . TYR A 256 ? 0.6647 0.8724 0.7501 -0.0024 -0.0496 -0.1121 1473 TYR A CB    
1965 C  CG    . TYR A 256 ? 0.6373 0.8478 0.7325 -0.0148 -0.0494 -0.1192 1473 TYR A CG    
1966 C  CD1   . TYR A 256 ? 0.5268 0.7217 0.6206 -0.0246 -0.0428 -0.1164 1473 TYR A CD1   
1967 C  CD2   . TYR A 256 ? 0.6777 0.9064 0.7842 -0.0168 -0.0558 -0.1286 1473 TYR A CD2   
1968 C  CE1   . TYR A 256 ? 0.6426 0.8385 0.7458 -0.0361 -0.0425 -0.1223 1473 TYR A CE1   
1969 C  CE2   . TYR A 256 ? 0.6426 0.8733 0.7593 -0.0288 -0.0557 -0.1354 1473 TYR A CE2   
1970 C  CZ    . TYR A 256 ? 0.7219 0.9355 0.8370 -0.0385 -0.0488 -0.1320 1473 TYR A CZ    
1971 O  OH    . TYR A 256 ? 0.8189 1.0328 0.9445 -0.0506 -0.0486 -0.1381 1473 TYR A OH    
1972 N  N     . VAL A 257 ? 0.6578 0.8331 0.7067 0.0180  -0.0500 -0.0944 1474 VAL A N     
1973 C  CA    . VAL A 257 ? 0.5233 0.6899 0.5628 0.0272  -0.0489 -0.0860 1474 VAL A CA    
1974 C  C     . VAL A 257 ? 0.4858 0.6540 0.5330 0.0270  -0.0437 -0.0835 1474 VAL A C     
1975 O  O     . VAL A 257 ? 0.4653 0.6382 0.5226 0.0187  -0.0396 -0.0867 1474 VAL A O     
1976 C  CB    . VAL A 257 ? 0.4913 0.6371 0.5162 0.0269  -0.0458 -0.0796 1474 VAL A CB    
1977 C  CG1   . VAL A 257 ? 0.5587 0.7032 0.5757 0.0273  -0.0502 -0.0828 1474 VAL A CG1   
1978 C  CG2   . VAL A 257 ? 0.4845 0.6191 0.5117 0.0174  -0.0387 -0.0782 1474 VAL A CG2   
1979 N  N     . PHE A 258 ? 0.5370 0.7013 0.5793 0.0362  -0.0440 -0.0775 1475 PHE A N     
1980 C  CA    . PHE A 258 ? 0.5449 0.7087 0.5925 0.0376  -0.0394 -0.0751 1475 PHE A CA    
1981 C  C     . PHE A 258 ? 0.5359 0.6788 0.5725 0.0370  -0.0344 -0.0675 1475 PHE A C     
1982 O  O     . PHE A 258 ? 0.5618 0.6933 0.5868 0.0409  -0.0360 -0.0625 1475 PHE A O     
1983 C  CB    . PHE A 258 ? 0.5146 0.6892 0.5666 0.0486  -0.0437 -0.0748 1475 PHE A CB    
1984 C  CG    . PHE A 258 ? 0.4564 0.6532 0.5208 0.0493  -0.0488 -0.0825 1475 PHE A CG    
1985 C  CD1   . PHE A 258 ? 0.3822 0.5938 0.4615 0.0466  -0.0463 -0.0877 1475 PHE A CD1   
1986 C  CD2   . PHE A 258 ? 0.4110 0.6149 0.4722 0.0523  -0.0559 -0.0852 1475 PHE A CD2   
1987 C  CE1   . PHE A 258 ? 0.3837 0.6173 0.4759 0.0470  -0.0511 -0.0952 1475 PHE A CE1   
1988 C  CE2   . PHE A 258 ? 0.3976 0.6229 0.4707 0.0527  -0.0612 -0.0929 1475 PHE A CE2   
1989 C  CZ    . PHE A 258 ? 0.3891 0.6295 0.4784 0.0499  -0.0589 -0.0979 1475 PHE A CZ    
1990 N  N     . GLN A 259 ? 0.3752 0.5139 0.4152 0.0316  -0.0281 -0.0669 1476 GLN A N     
1991 C  CA    . GLN A 259 ? 0.4480 0.5678 0.4784 0.0294  -0.0235 -0.0607 1476 GLN A CA    
1992 C  C     . GLN A 259 ? 0.4606 0.5781 0.4933 0.0324  -0.0198 -0.0585 1476 GLN A C     
1993 O  O     . GLN A 259 ? 0.3938 0.5241 0.4367 0.0321  -0.0182 -0.0629 1476 GLN A O     
1994 C  CB    . GLN A 259 ? 0.4250 0.5383 0.4547 0.0183  -0.0192 -0.0616 1476 GLN A CB    
1995 C  CG    . GLN A 259 ? 0.4176 0.5279 0.4429 0.0150  -0.0222 -0.0633 1476 GLN A CG    
1996 C  CD    . GLN A 259 ? 0.5438 0.6507 0.5723 0.0038  -0.0184 -0.0656 1476 GLN A CD    
1997 O  OE1   . GLN A 259 ? 0.4419 0.5611 0.4811 -0.0019 -0.0182 -0.0711 1476 GLN A OE1   
1998 N  NE2   . GLN A 259 ? 0.7260 0.8162 0.7458 0.0005  -0.0154 -0.0610 1476 GLN A NE2   
1999 N  N     . ASN A 260 ? 0.3713 0.4724 0.3945 0.0349  -0.0181 -0.0522 1477 ASN A N     
2000 C  CA    . ASN A 260 ? 0.5485 0.6427 0.5714 0.0352  -0.0136 -0.0502 1477 ASN A CA    
2001 C  C     . ASN A 260 ? 0.5669 0.6456 0.5816 0.0285  -0.0095 -0.0461 1477 ASN A C     
2002 O  O     . ASN A 260 ? 0.6379 0.7094 0.6464 0.0253  -0.0103 -0.0441 1477 ASN A O     
2003 C  CB    . ASN A 260 ? 0.4267 0.5155 0.4475 0.0452  -0.0159 -0.0466 1477 ASN A CB    
2004 C  CG    . ASN A 260 ? 0.5763 0.6769 0.6020 0.0535  -0.0216 -0.0483 1477 ASN A CG    
2005 O  OD1   . ASN A 260 ? 0.6758 0.7931 0.7111 0.0531  -0.0230 -0.0543 1477 ASN A OD1   
2006 N  ND2   . ASN A 260 ? 0.5678 0.6602 0.5872 0.0612  -0.0251 -0.0428 1477 ASN A ND2   
2007 N  N     . SER A 261 ? 0.5184 0.5931 0.5333 0.0266  -0.0051 -0.0456 1478 SER A N     
2008 C  CA    . SER A 261 ? 0.5704 0.6295 0.5770 0.0229  -0.0019 -0.0410 1478 SER A CA    
2009 C  C     . SER A 261 ? 0.7140 0.7699 0.7210 0.0265  0.0002  -0.0407 1478 SER A C     
2010 O  O     . SER A 261 ? 0.7423 0.8093 0.7566 0.0290  0.0010  -0.0451 1478 SER A O     
2011 C  CB    . SER A 261 ? 0.6047 0.6627 0.6105 0.0128  0.0018  -0.0416 1478 SER A CB    
2012 O  OG    . SER A 261 ? 0.6443 0.7130 0.6569 0.0084  0.0056  -0.0455 1478 SER A OG    
2013 N  N     . TRP A 262 ? 0.7870 0.8282 0.7865 0.0272  0.0008  -0.0360 1479 TRP A N     
2014 C  CA    . TRP A 262 ? 0.7795 0.8158 0.7789 0.0307  0.0022  -0.0361 1479 TRP A CA    
2015 C  C     . TRP A 262 ? 0.8534 0.8753 0.8448 0.0267  0.0042  -0.0319 1479 TRP A C     
2016 O  O     . TRP A 262 ? 0.7796 0.7940 0.7659 0.0239  0.0035  -0.0278 1479 TRP A O     
2017 C  CB    . TRP A 262 ? 0.5137 0.5478 0.5151 0.0402  -0.0017 -0.0349 1479 TRP A CB    
2018 C  CG    . TRP A 262 ? 0.4439 0.4759 0.4424 0.0432  -0.0056 -0.0310 1479 TRP A CG    
2019 C  CD1   . TRP A 262 ? 0.4185 0.4620 0.4212 0.0461  -0.0088 -0.0331 1479 TRP A CD1   
2020 C  CD2   . TRP A 262 ? 0.4263 0.4453 0.4172 0.0435  -0.0068 -0.0245 1479 TRP A CD2   
2021 N  NE1   . TRP A 262 ? 0.5053 0.5437 0.5023 0.0486  -0.0119 -0.0284 1479 TRP A NE1   
2022 C  CE2   . TRP A 262 ? 0.4922 0.5158 0.4820 0.0469  -0.0104 -0.0229 1479 TRP A CE2   
2023 C  CE3   . TRP A 262 ? 0.4344 0.4396 0.4196 0.0413  -0.0051 -0.0200 1479 TRP A CE3   
2024 C  CZ2   . TRP A 262 ? 0.4912 0.5060 0.4739 0.0483  -0.0118 -0.0169 1479 TRP A CZ2   
2025 C  CZ3   . TRP A 262 ? 0.5448 0.5415 0.5241 0.0424  -0.0065 -0.0141 1479 TRP A CZ3   
2026 C  CH2   . TRP A 262 ? 0.5707 0.5723 0.5486 0.0459  -0.0096 -0.0125 1479 TRP A CH2   
2027 N  N     . GLY A 263 ? 0.7487 0.7674 0.7396 0.0270  0.0063  -0.0332 1480 GLY A N     
2028 C  CA    . GLY A 263 ? 0.6520 0.6585 0.6358 0.0232  0.0077  -0.0297 1480 GLY A CA    
2029 C  C     . GLY A 263 ? 0.6568 0.6590 0.6402 0.0259  0.0085  -0.0317 1480 GLY A C     
2030 O  O     . GLY A 263 ? 0.7937 0.8040 0.7818 0.0289  0.0096  -0.0369 1480 GLY A O     
2031 N  N     . ILE A 264 ? 0.5982 0.5878 0.5763 0.0248  0.0080  -0.0280 1481 ILE A N     
2032 C  CA    . ILE A 264 ? 0.6074 0.5918 0.5845 0.0263  0.0084  -0.0303 1481 ILE A CA    
2033 C  C     . ILE A 264 ? 0.6420 0.6175 0.6122 0.0210  0.0091  -0.0269 1481 ILE A C     
2034 O  O     . ILE A 264 ? 0.8307 0.8001 0.7980 0.0187  0.0082  -0.0217 1481 ILE A O     
2035 C  CB    . ILE A 264 ? 0.6075 0.5847 0.5883 0.0335  0.0052  -0.0301 1481 ILE A CB    
2036 C  CG1   . ILE A 264 ? 0.6212 0.5977 0.6033 0.0358  0.0059  -0.0359 1481 ILE A CG1   
2037 C  CG2   . ILE A 264 ? 0.3826 0.3468 0.3604 0.0332  0.0031  -0.0238 1481 ILE A CG2   
2038 C  CD1   . ILE A 264 ? 0.5389 0.5064 0.5251 0.0423  0.0029  -0.0363 1481 ILE A CD1   
2039 N  N     . THR A 265 ? 0.4968 0.4725 0.4643 0.0194  0.0108  -0.0303 1482 THR A N     
2040 C  CA    . THR A 265 ? 0.5542 0.5246 0.5148 0.0140  0.0117  -0.0277 1482 THR A CA    
2041 C  C     . THR A 265 ? 0.6952 0.6576 0.6539 0.0156  0.0100  -0.0293 1482 THR A C     
2042 O  O     . THR A 265 ? 0.6479 0.6073 0.6110 0.0206  0.0081  -0.0321 1482 THR A O     
2043 C  CB    . THR A 265 ? 0.5421 0.5216 0.4992 0.0091  0.0155  -0.0295 1482 THR A CB    
2044 O  OG1   . THR A 265 ? 0.5459 0.5311 0.5026 0.0108  0.0172  -0.0355 1482 THR A OG1   
2045 C  CG2   . THR A 265 ? 0.5501 0.5393 0.5116 0.0078  0.0172  -0.0298 1482 THR A CG2   
2046 N  N     . THR A 266 ? 0.8541 0.8133 0.8065 0.0112  0.0104  -0.0277 1483 THR A N     
2047 C  CA    . THR A 266 ? 0.8904 0.8430 0.8407 0.0119  0.0084  -0.0297 1483 THR A CA    
2048 C  C     . THR A 266 ? 0.9001 0.8584 0.8502 0.0144  0.0095  -0.0376 1483 THR A C     
2049 O  O     . THR A 266 ? 0.9045 0.8574 0.8538 0.0158  0.0073  -0.0409 1483 THR A O     
2050 C  CB    . THR A 266 ? 0.7908 0.7398 0.7342 0.0068  0.0081  -0.0258 1483 THR A CB    
2051 O  OG1   . THR A 266 ? 0.7014 0.6584 0.6392 0.0031  0.0115  -0.0261 1483 THR A OG1   
2052 C  CG2   . THR A 266 ? 0.7134 0.6567 0.6579 0.0053  0.0069  -0.0190 1483 THR A CG2   
2053 N  N     . ARG A 267 ? 0.7673 0.7368 0.7187 0.0152  0.0127  -0.0410 1484 ARG A N     
2054 C  CA    . ARG A 267 ? 0.6585 0.6351 0.6102 0.0182  0.0144  -0.0491 1484 ARG A CA    
2055 C  C     . ARG A 267 ? 0.6730 0.6428 0.6308 0.0246  0.0111  -0.0536 1484 ARG A C     
2056 O  O     . ARG A 267 ? 0.7102 0.6811 0.6671 0.0271  0.0110  -0.0607 1484 ARG A O     
2057 C  CB    . ARG A 267 ? 0.4584 0.4489 0.4132 0.0185  0.0184  -0.0516 1484 ARG A CB    
2058 C  CG    . ARG A 267 ? 0.4109 0.4114 0.3657 0.0213  0.0212  -0.0600 1484 ARG A CG    
2059 C  CD    . ARG A 267 ? 0.4292 0.4443 0.3892 0.0216  0.0250  -0.0619 1484 ARG A CD    
2060 N  NE    . ARG A 267 ? 0.6689 0.6930 0.6230 0.0148  0.0297  -0.0597 1484 ARG A NE    
2061 C  CZ    . ARG A 267 ? 0.9010 0.9392 0.8589 0.0130  0.0341  -0.0610 1484 ARG A CZ    
2062 N  NH1   . ARG A 267 ? 0.9473 0.9935 0.9153 0.0179  0.0340  -0.0650 1484 ARG A NH1   
2063 N  NH2   . ARG A 267 ? 0.9319 0.9766 0.8840 0.0061  0.0385  -0.0579 1484 ARG A NH2   
2064 N  N     . THR A 268 ? 0.5711 0.5334 0.5349 0.0273  0.0083  -0.0496 1485 THR A N     
2065 C  CA    . THR A 268 ? 0.6281 0.5816 0.5980 0.0328  0.0050  -0.0523 1485 THR A CA    
2066 C  C     . THR A 268 ? 0.7412 0.6872 0.7080 0.0318  0.0030  -0.0560 1485 THR A C     
2067 O  O     . THR A 268 ? 0.8145 0.7598 0.7838 0.0359  0.0022  -0.0636 1485 THR A O     
2068 C  CB    . THR A 268 ? 0.5987 0.5432 0.5725 0.0337  0.0024  -0.0447 1485 THR A CB    
2069 O  OG1   . THR A 268 ? 0.4038 0.3428 0.3727 0.0281  0.0019  -0.0388 1485 THR A OG1   
2070 C  CG2   . THR A 268 ? 0.5719 0.5241 0.5487 0.0354  0.0035  -0.0420 1485 THR A CG2   
2071 N  N     . ILE A 269 ? 0.4158 0.3569 0.3775 0.0265  0.0020  -0.0512 1486 ILE A N     
2072 C  CA    . ILE A 269 ? 0.5311 0.4651 0.4908 0.0254  -0.0007 -0.0547 1486 ILE A CA    
2073 C  C     . ILE A 269 ? 0.5197 0.4615 0.4743 0.0263  0.0008  -0.0636 1486 ILE A C     
2074 O  O     . ILE A 269 ? 0.4651 0.4027 0.4217 0.0293  -0.0015 -0.0709 1486 ILE A O     
2075 C  CB    . ILE A 269 ? 0.5203 0.4498 0.4755 0.0198  -0.0020 -0.0480 1486 ILE A CB    
2076 C  CG1   . ILE A 269 ? 0.4123 0.3349 0.3732 0.0199  -0.0032 -0.0400 1486 ILE A CG1   
2077 C  CG2   . ILE A 269 ? 0.4255 0.3496 0.3791 0.0186  -0.0053 -0.0522 1486 ILE A CG2   
2078 C  CD1   . ILE A 269 ? 0.4436 0.3611 0.4024 0.0154  -0.0047 -0.0339 1486 ILE A CD1   
2079 N  N     . GLY A 270 ? 0.4277 0.3812 0.3761 0.0240  0.0049  -0.0635 1487 GLY A N     
2080 C  CA    . GLY A 270 ? 0.4725 0.4351 0.4151 0.0248  0.0072  -0.0715 1487 GLY A CA    
2081 C  C     . GLY A 270 ? 0.5277 0.4926 0.4768 0.0316  0.0073  -0.0806 1487 GLY A C     
2082 O  O     . GLY A 270 ? 0.4989 0.4632 0.4459 0.0339  0.0061  -0.0890 1487 GLY A O     
2083 N  N     . VAL A 271 ? 0.4374 0.4044 0.3946 0.0354  0.0083  -0.0794 1488 VAL A N     
2084 C  CA    . VAL A 271 ? 0.6994 0.6688 0.6635 0.0427  0.0082  -0.0882 1488 VAL A CA    
2085 C  C     . VAL A 271 ? 0.7319 0.6864 0.7009 0.0461  0.0031  -0.0916 1488 VAL A C     
2086 O  O     . VAL A 271 ? 0.5182 0.4724 0.4885 0.0505  0.0023  -0.1014 1488 VAL A O     
2087 C  CB    . VAL A 271 ? 0.7251 0.7012 0.6972 0.0465  0.0098  -0.0862 1488 VAL A CB    
2088 C  CG1   . VAL A 271 ? 0.8196 0.7878 0.7951 0.0449  0.0075  -0.0765 1488 VAL A CG1   
2089 C  CG2   . VAL A 271 ? 0.7493 0.7252 0.7300 0.0552  0.0087  -0.0946 1488 VAL A CG2   
2090 N  N     . MET A 272 ? 0.7637 0.7057 0.7351 0.0436  -0.0003 -0.0838 1489 MET A N     
2091 C  CA    . MET A 272 ? 0.6728 0.6003 0.6488 0.0451  -0.0050 -0.0862 1489 MET A CA    
2092 C  C     . MET A 272 ? 0.7530 0.6812 0.7230 0.0436  -0.0061 -0.0947 1489 MET A C     
2093 O  O     . MET A 272 ? 0.8040 0.7292 0.7774 0.0483  -0.0077 -0.1044 1489 MET A O     
2094 C  CB    . MET A 272 ? 0.6062 0.5233 0.5838 0.0407  -0.0074 -0.0759 1489 MET A CB    
2095 C  CG    . MET A 272 ? 0.6733 0.5755 0.6571 0.0412  -0.0120 -0.0771 1489 MET A CG    
2096 S  SD    . MET A 272 ? 0.6714 0.5651 0.6551 0.0343  -0.0141 -0.0667 1489 MET A SD    
2097 C  CE    . MET A 272 ? 0.4511 0.3516 0.4243 0.0290  -0.0143 -0.0710 1489 MET A CE    
2098 N  N     . ILE A 273 ? 0.8313 0.7647 0.7917 0.0376  -0.0050 -0.0918 1490 ILE A N     
2099 C  CA    . ILE A 273 ? 0.8346 0.7697 0.7877 0.0361  -0.0064 -0.0994 1490 ILE A CA    
2100 C  C     . ILE A 273 ? 0.7349 0.6793 0.6863 0.0413  -0.0039 -0.1108 1490 ILE A C     
2101 O  O     . ILE A 273 ? 0.4894 0.4295 0.4419 0.0444  -0.0067 -0.1206 1490 ILE A O     
2102 C  CB    . ILE A 273 ? 0.6713 0.6125 0.6135 0.0296  -0.0052 -0.0935 1490 ILE A CB    
2103 C  CG1   . ILE A 273 ? 0.7516 0.6829 0.6971 0.0254  -0.0081 -0.0836 1490 ILE A CG1   
2104 C  CG2   . ILE A 273 ? 0.4753 0.4194 0.4087 0.0285  -0.0070 -0.1014 1490 ILE A CG2   
2105 C  CD1   . ILE A 273 ? 0.8977 0.8338 0.8342 0.0196  -0.0069 -0.0762 1490 ILE A CD1   
2106 N  N     . MET A 274 ? 0.5804 0.5381 0.5300 0.0425  0.0015  -0.1100 1491 MET A N     
2107 C  CA    . MET A 274 ? 0.6343 0.6041 0.5812 0.0469  0.0049  -0.1205 1491 MET A CA    
2108 C  C     . MET A 274 ? 0.6697 0.6335 0.6268 0.0548  0.0027  -0.1295 1491 MET A C     
2109 O  O     . MET A 274 ? 0.7480 0.7164 0.7030 0.0589  0.0032  -0.1411 1491 MET A O     
2110 C  CB    . MET A 274 ? 0.8138 0.7993 0.7591 0.0463  0.0113  -0.1174 1491 MET A CB    
2111 C  CG    . MET A 274 ? 0.8054 0.7991 0.7403 0.0389  0.0147  -0.1097 1491 MET A CG    
2112 S  SD    . MET A 274 ? 0.8920 0.8899 0.8118 0.0355  0.0147  -0.1142 1491 MET A SD    
2113 C  CE    . MET A 274 ? 0.8542 0.8684 0.7711 0.0410  0.0198  -0.1270 1491 MET A CE    
2114 N  N     . VAL A 275 ? 0.6137 0.5670 0.5815 0.0574  0.0001  -0.1245 1492 VAL A N     
2115 C  CA    . VAL A 275 ? 0.6896 0.6373 0.6678 0.0657  -0.0017 -0.1321 1492 VAL A CA    
2116 C  C     . VAL A 275 ? 0.6785 0.6093 0.6608 0.0669  -0.0076 -0.1374 1492 VAL A C     
2117 O  O     . VAL A 275 ? 0.5686 0.4974 0.5546 0.0730  -0.0088 -0.1488 1492 VAL A O     
2118 C  CB    . VAL A 275 ? 0.6639 0.6098 0.6515 0.0688  -0.0016 -0.1243 1492 VAL A CB    
2119 C  CG1   . VAL A 275 ? 0.6319 0.5660 0.6309 0.0768  -0.0053 -0.1291 1492 VAL A CG1   
2120 C  CG2   . VAL A 275 ? 0.5503 0.5151 0.5367 0.0699  0.0040  -0.1241 1492 VAL A CG2   
2121 N  N     . HIS A 276 ? 0.6789 0.5985 0.6603 0.0609  -0.0111 -0.1303 1493 HIS A N     
2122 C  CA    . HIS A 276 ? 0.6235 0.5255 0.6120 0.0614  -0.0168 -0.1330 1493 HIS A CA    
2123 C  C     . HIS A 276 ? 0.7463 0.6462 0.7287 0.0573  -0.0198 -0.1398 1493 HIS A C     
2124 O  O     . HIS A 276 ? 0.7133 0.6024 0.7012 0.0597  -0.0240 -0.1484 1493 HIS A O     
2125 C  CB    . HIS A 276 ? 0.6140 0.5043 0.6085 0.0577  -0.0189 -0.1201 1493 HIS A CB    
2126 C  CG    . HIS A 276 ? 0.7214 0.6091 0.7242 0.0628  -0.0180 -0.1143 1493 HIS A CG    
2127 N  ND1   . HIS A 276 ? 0.8061 0.6912 0.8164 0.0712  -0.0186 -0.1214 1493 HIS A ND1   
2128 C  CD2   . HIS A 276 ? 0.7287 0.6162 0.7331 0.0613  -0.0169 -0.1023 1493 HIS A CD2   
2129 C  CE1   . HIS A 276 ? 0.8130 0.6966 0.8291 0.0745  -0.0181 -0.1135 1493 HIS A CE1   
2130 N  NE2   . HIS A 276 ? 0.7568 0.6420 0.7691 0.0685  -0.0170 -0.1020 1493 HIS A NE2   
2131 N  N     . ALA A 277 ? 0.7431 0.6521 0.7144 0.0513  -0.0183 -0.1363 1494 ALA A N     
2132 C  CA    . ALA A 277 ? 0.7184 0.6251 0.6840 0.0473  -0.0221 -0.1415 1494 ALA A CA    
2133 C  C     . ALA A 277 ? 0.7406 0.6528 0.7019 0.0520  -0.0223 -0.1570 1494 ALA A C     
2134 O  O     . ALA A 277 ? 0.7271 0.6516 0.6844 0.0563  -0.0176 -0.1618 1494 ALA A O     
2135 C  CB    . ALA A 277 ? 0.7382 0.6541 0.6923 0.0406  -0.0204 -0.1338 1494 ALA A CB    
2136 N  N     . ASP A 278 ? 0.7979 0.7014 0.7608 0.0512  -0.0279 -0.1652 1495 ASP A N     
2137 C  CA    . ASP A 278 ? 0.8015 0.7093 0.7599 0.0554  -0.0291 -0.1811 1495 ASP A CA    
2138 C  C     . ASP A 278 ? 0.7312 0.6486 0.6752 0.0505  -0.0302 -0.1836 1495 ASP A C     
2139 O  O     . ASP A 278 ? 0.6875 0.6115 0.6238 0.0451  -0.0284 -0.1729 1495 ASP A O     
2140 C  CB    . ASP A 278 ? 0.7818 0.6725 0.7526 0.0585  -0.0349 -0.1904 1495 ASP A CB    
2141 C  CG    . ASP A 278 ? 0.7610 0.6372 0.7391 0.0521  -0.0407 -0.1840 1495 ASP A CG    
2142 O  OD1   . ASP A 278 ? 0.7963 0.6770 0.7667 0.0459  -0.0426 -0.1811 1495 ASP A OD1   
2143 O  OD2   . ASP A 278 ? 0.8176 0.6782 0.8095 0.0533  -0.0432 -0.1815 1495 ASP A OD2   
2144 N  N     . ASN A 279 ? 0.6009 0.5192 0.5409 0.0529  -0.0335 -0.1981 1496 ASN A N     
2145 C  CA    . ASN A 279 ? 0.6193 0.5476 0.5447 0.0493  -0.0351 -0.2017 1496 ASN A CA    
2146 C  C     . ASN A 279 ? 0.7774 0.6952 0.7062 0.0434  -0.0427 -0.2000 1496 ASN A C     
2147 O  O     . ASN A 279 ? 0.9297 0.8533 0.8487 0.0414  -0.0463 -0.2066 1496 ASN A O     
2148 C  CB    . ASN A 279 ? 0.6034 0.5404 0.5209 0.0550  -0.0346 -0.2186 1496 ASN A CB    
2149 C  CG    . ASN A 279 ? 0.8933 0.8421 0.8088 0.0610  -0.0269 -0.2207 1496 ASN A CG    
2150 O  OD1   . ASN A 279 ? 0.8749 0.8404 0.7772 0.0603  -0.0212 -0.2183 1496 ASN A OD1   
2151 N  ND2   . ASN A 279 ? 0.9390 0.8792 0.8682 0.0668  -0.0265 -0.2246 1496 ASN A ND2   
2152 N  N     . GLN A 280 ? 0.7486 0.6520 0.6916 0.0408  -0.0452 -0.1919 1497 GLN A N     
2153 C  CA    . GLN A 280 ? 0.7562 0.6509 0.7042 0.0344  -0.0515 -0.1880 1497 GLN A CA    
2154 C  C     . GLN A 280 ? 0.7718 0.6651 0.7227 0.0294  -0.0494 -0.1706 1497 GLN A C     
2155 O  O     . GLN A 280 ? 0.7815 0.6686 0.7377 0.0240  -0.0538 -0.1654 1497 GLN A O     
2156 C  CB    . GLN A 280 ? 0.7481 0.6253 0.7121 0.0353  -0.0571 -0.1954 1497 GLN A CB    
2157 C  CG    . GLN A 280 ? 0.9839 0.8611 0.9453 0.0388  -0.0612 -0.2137 1497 GLN A CG    
2158 C  CD    . GLN A 280 ? 1.2746 1.1524 1.2373 0.0473  -0.0573 -0.2230 1497 GLN A CD    
2159 O  OE1   . GLN A 280 ? 1.4332 1.3233 1.3843 0.0515  -0.0553 -0.2336 1497 GLN A OE1   
2160 N  NE2   . GLN A 280 ? 1.3146 1.1796 1.2914 0.0501  -0.0562 -0.2188 1497 GLN A NE2   
2161 N  N     . GLY A 281 ? 0.7815 0.6811 0.7293 0.0311  -0.0429 -0.1620 1498 GLY A N     
2162 C  CA    . GLY A 281 ? 0.8496 0.7490 0.7986 0.0267  -0.0408 -0.1466 1498 GLY A CA    
2163 C  C     . GLY A 281 ? 0.9597 0.8541 0.9175 0.0297  -0.0367 -0.1398 1498 GLY A C     
2164 O  O     . GLY A 281 ? 0.9864 0.8808 0.9471 0.0356  -0.0345 -0.1464 1498 GLY A O     
2165 N  N     . LEU A 282 ? 0.9361 0.8267 0.8982 0.0259  -0.0359 -0.1267 1499 LEU A N     
2166 C  CA    . LEU A 282 ? 0.8377 0.7238 0.8076 0.0282  -0.0325 -0.1186 1499 LEU A CA    
2167 C  C     . LEU A 282 ? 0.8119 0.6840 0.7951 0.0319  -0.0352 -0.1232 1499 LEU A C     
2168 O  O     . LEU A 282 ? 0.7306 0.5945 0.7188 0.0315  -0.0400 -0.1314 1499 LEU A O     
2169 C  CB    . LEU A 282 ? 0.7876 0.6713 0.7597 0.0231  -0.0321 -0.1047 1499 LEU A CB    
2170 C  CG    . LEU A 282 ? 0.6613 0.5559 0.6227 0.0193  -0.0293 -0.0970 1499 LEU A CG    
2171 C  CD1   . LEU A 282 ? 0.5712 0.4598 0.5379 0.0143  -0.0316 -0.0875 1499 LEU A CD1   
2172 C  CD2   . LEU A 282 ? 0.4745 0.3768 0.4323 0.0215  -0.0234 -0.0916 1499 LEU A CD2   
2173 N  N     . VAL A 283 ? 0.8060 0.6757 0.7948 0.0359  -0.0321 -0.1181 1500 VAL A N     
2174 C  CA    . VAL A 283 ? 0.6962 0.5513 0.6981 0.0391  -0.0341 -0.1173 1500 VAL A CA    
2175 C  C     . VAL A 283 ? 0.6728 0.5273 0.6777 0.0393  -0.0310 -0.1040 1500 VAL A C     
2176 O  O     . VAL A 283 ? 0.6775 0.5381 0.6815 0.0442  -0.0276 -0.1031 1500 VAL A O     
2177 C  CB    . VAL A 283 ? 0.7246 0.5781 0.7299 0.0470  -0.0341 -0.1290 1500 VAL A CB    
2178 C  CG1   . VAL A 283 ? 0.7475 0.5832 0.7668 0.0498  -0.0374 -0.1284 1500 VAL A CG1   
2179 C  CG2   . VAL A 283 ? 0.7489 0.6076 0.7478 0.0476  -0.0360 -0.1432 1500 VAL A CG2   
2180 N  N     . LEU A 284 ? 0.6692 0.5172 0.6781 0.0340  -0.0322 -0.0937 1501 LEU A N     
2181 C  CA    . LEU A 284 ? 0.6652 0.5150 0.6746 0.0339  -0.0289 -0.0813 1501 LEU A CA    
2182 C  C     . LEU A 284 ? 0.7636 0.6024 0.7828 0.0389  -0.0294 -0.0780 1501 LEU A C     
2183 O  O     . LEU A 284 ? 0.7801 0.6053 0.8085 0.0391  -0.0328 -0.0801 1501 LEU A O     
2184 C  CB    . LEU A 284 ? 0.6394 0.4880 0.6485 0.0270  -0.0293 -0.0714 1501 LEU A CB    
2185 C  CG    . LEU A 284 ? 0.6881 0.5432 0.6905 0.0211  -0.0307 -0.0728 1501 LEU A CG    
2186 C  CD1   . LEU A 284 ? 0.8187 0.6722 0.8235 0.0158  -0.0306 -0.0617 1501 LEU A CD1   
2187 C  CD2   . LEU A 284 ? 0.5427 0.4122 0.5324 0.0214  -0.0280 -0.0762 1501 LEU A CD2   
2188 N  N     . PRO A 285 ? 0.8678 0.7121 0.8856 0.0428  -0.0262 -0.0726 1502 PRO A N     
2189 C  CA    . PRO A 285 ? 1.0261 0.8606 1.0523 0.0477  -0.0269 -0.0674 1502 PRO A CA    
2190 C  C     . PRO A 285 ? 1.1014 0.9255 1.1329 0.0432  -0.0279 -0.0562 1502 PRO A C     
2191 O  O     . PRO A 285 ? 1.2568 1.0863 1.2839 0.0378  -0.0263 -0.0492 1502 PRO A O     
2192 C  CB    . PRO A 285 ? 0.9985 0.8452 1.0202 0.0518  -0.0233 -0.0637 1502 PRO A CB    
2193 C  CG    . PRO A 285 ? 0.9007 0.7620 0.9133 0.0504  -0.0209 -0.0708 1502 PRO A CG    
2194 C  CD    . PRO A 285 ? 0.8778 0.7378 0.8866 0.0432  -0.0222 -0.0713 1502 PRO A CD    
2195 N  N     . PRO A 286 ? 0.9561 0.7654 0.9974 0.0454  -0.0303 -0.0542 1503 PRO A N     
2196 C  CA    . PRO A 286 ? 0.8480 0.6471 0.8951 0.0402  -0.0311 -0.0440 1503 PRO A CA    
2197 C  C     . PRO A 286 ? 0.6257 0.4309 0.6686 0.0388  -0.0278 -0.0312 1503 PRO A C     
2198 O  O     . PRO A 286 ? 0.5751 0.3787 0.6191 0.0327  -0.0273 -0.0240 1503 PRO A O     
2199 C  CB    . PRO A 286 ? 0.8892 0.6714 0.9473 0.0443  -0.0338 -0.0438 1503 PRO A CB    
2200 C  CG    . PRO A 286 ? 0.9201 0.7025 0.9787 0.0507  -0.0354 -0.0570 1503 PRO A CG    
2201 C  CD    . PRO A 286 ? 0.9561 0.7570 1.0040 0.0528  -0.0324 -0.0612 1503 PRO A CD    
2202 N  N     . ARG A 287 ? 0.7094 0.5220 0.7479 0.0442  -0.0257 -0.0286 1504 ARG A N     
2203 C  CA    . ARG A 287 ? 0.6926 0.5087 0.7281 0.0437  -0.0233 -0.0164 1504 ARG A CA    
2204 C  C     . ARG A 287 ? 0.7180 0.5470 0.7449 0.0389  -0.0206 -0.0142 1504 ARG A C     
2205 O  O     . ARG A 287 ? 0.8271 0.6585 0.8518 0.0371  -0.0187 -0.0047 1504 ARG A O     
2206 C  CB    . ARG A 287 ? 0.7546 0.5732 0.7895 0.0516  -0.0228 -0.0141 1504 ARG A CB    
2207 C  CG    . ARG A 287 ? 0.7416 0.5458 0.7854 0.0569  -0.0256 -0.0139 1504 ARG A CG    
2208 C  CD    . ARG A 287 ? 0.8559 0.6618 0.8991 0.0640  -0.0253 -0.0072 1504 ARG A CD    
2209 N  NE    . ARG A 287 ? 1.0404 0.8436 1.0881 0.0722  -0.0275 -0.0149 1504 ARG A NE    
2210 C  CZ    . ARG A 287 ? 1.2526 1.0402 1.3091 0.0752  -0.0305 -0.0174 1504 ARG A CZ    
2211 N  NH1   . ARG A 287 ? 1.3507 1.1239 1.4127 0.0701  -0.0315 -0.0123 1504 ARG A NH1   
2212 N  NH2   . ARG A 287 ? 1.2617 1.0485 1.3223 0.0834  -0.0323 -0.0253 1504 ARG A NH2   
2213 N  N     . VAL A 288 ? 0.6975 0.5343 0.7197 0.0367  -0.0206 -0.0228 1505 VAL A N     
2214 C  CA    . VAL A 288 ? 0.5202 0.3677 0.5346 0.0318  -0.0185 -0.0213 1505 VAL A CA    
2215 C  C     . VAL A 288 ? 0.6745 0.5203 0.6893 0.0259  -0.0203 -0.0252 1505 VAL A C     
2216 O  O     . VAL A 288 ? 0.5953 0.4491 0.6040 0.0218  -0.0191 -0.0238 1505 VAL A O     
2217 C  CB    . VAL A 288 ? 0.4421 0.3026 0.4490 0.0342  -0.0165 -0.0269 1505 VAL A CB    
2218 C  CG1   . VAL A 288 ? 0.6489 0.5120 0.6568 0.0406  -0.0155 -0.0248 1505 VAL A CG1   
2219 C  CG2   . VAL A 288 ? 0.4474 0.3097 0.4530 0.0345  -0.0178 -0.0383 1505 VAL A CG2   
2220 N  N     . ALA A 289 ? 0.7858 0.6220 0.8075 0.0256  -0.0235 -0.0308 1506 ALA A N     
2221 C  CA    . ALA A 289 ? 0.7934 0.6283 0.8162 0.0202  -0.0260 -0.0354 1506 ALA A CA    
2222 C  C     . ALA A 289 ? 0.9369 0.7715 0.9618 0.0145  -0.0255 -0.0262 1506 ALA A C     
2223 O  O     . ALA A 289 ? 1.1335 0.9617 1.1643 0.0142  -0.0245 -0.0176 1506 ALA A O     
2224 C  CB    . ALA A 289 ? 0.6523 0.4751 0.6839 0.0209  -0.0298 -0.0426 1506 ALA A CB    
2225 N  N     . CYS A 290 ? 0.7705 0.6127 0.7906 0.0102  -0.0259 -0.0277 1507 CYS A N     
2226 C  CA    . CYS A 290 ? 0.6154 0.4592 0.6375 0.0054  -0.0251 -0.0194 1507 CYS A CA    
2227 C  C     . CYS A 290 ? 0.6035 0.4379 0.6374 0.0014  -0.0278 -0.0181 1507 CYS A C     
2228 O  O     . CYS A 290 ? 0.6610 0.4915 0.7009 -0.0002 -0.0260 -0.0090 1507 CYS A O     
2229 C  CB    . CYS A 290 ? 0.6578 0.5118 0.6720 0.0025  -0.0255 -0.0216 1507 CYS A CB    
2230 S  SG    . CYS A 290 ? 0.8288 0.6854 0.8472 -0.0030 -0.0254 -0.0133 1507 CYS A SG    
2231 N  N     . ILE A 291 ? 0.6827 0.5130 0.7203 0.0000  -0.0318 -0.0273 1508 ILE A N     
2232 C  CA    . ILE A 291 ? 0.7851 0.6040 0.8355 -0.0031 -0.0349 -0.0283 1508 ILE A CA    
2233 C  C     . ILE A 291 ? 0.6984 0.5073 0.7520 0.0018  -0.0362 -0.0344 1508 ILE A C     
2234 O  O     . ILE A 291 ? 0.7096 0.5212 0.7575 0.0051  -0.0377 -0.0446 1508 ILE A O     
2235 C  CB    . ILE A 291 ? 0.7994 0.6206 0.8528 -0.0083 -0.0394 -0.0354 1508 ILE A CB    
2236 C  CG1   . ILE A 291 ? 0.6969 0.5292 0.7462 -0.0120 -0.0385 -0.0303 1508 ILE A CG1   
2237 C  CG2   . ILE A 291 ? 0.7592 0.5688 0.8273 -0.0126 -0.0426 -0.0362 1508 ILE A CG2   
2238 C  CD1   . ILE A 291 ? 0.4897 0.3255 0.5424 -0.0168 -0.0435 -0.0366 1508 ILE A CD1   
2239 N  N     . GLN A 292 ? 0.5669 0.3643 0.6293 0.0025  -0.0355 -0.0281 1509 GLN A N     
2240 C  CA    . GLN A 292 ? 0.6029 0.3896 0.6694 0.0077  -0.0372 -0.0340 1509 GLN A CA    
2241 C  C     . GLN A 292 ? 0.6871 0.4632 0.7637 0.0045  -0.0421 -0.0427 1509 GLN A C     
2242 O  O     . GLN A 292 ? 0.8034 0.5753 0.8799 0.0085  -0.0448 -0.0539 1509 GLN A O     
2243 C  CB    . GLN A 292 ? 0.5639 0.3417 0.6350 0.0108  -0.0348 -0.0233 1509 GLN A CB    
2244 C  CG    . GLN A 292 ? 0.6921 0.4788 0.7539 0.0155  -0.0307 -0.0163 1509 GLN A CG    
2245 C  CD    . GLN A 292 ? 0.7984 0.5762 0.8650 0.0179  -0.0289 -0.0049 1509 GLN A CD    
2246 O  OE1   . GLN A 292 ? 0.8262 0.5968 0.9007 0.0132  -0.0286 0.0029  1509 GLN A OE1   
2247 N  NE2   . GLN A 292 ? 0.8136 0.5926 0.8757 0.0252  -0.0278 -0.0038 1509 GLN A NE2   
2248 N  N     . VAL A 293 ? 0.6863 0.4584 0.7721 -0.0026 -0.0434 -0.0382 1510 VAL A N     
2249 C  CA    . VAL A 293 ? 0.7179 0.4801 0.8152 -0.0070 -0.0483 -0.0459 1510 VAL A CA    
2250 C  C     . VAL A 293 ? 0.9202 0.6921 1.0181 -0.0141 -0.0503 -0.0476 1510 VAL A C     
2251 O  O     . VAL A 293 ? 1.0113 0.7900 1.1096 -0.0178 -0.0475 -0.0374 1510 VAL A O     
2252 C  CB    . VAL A 293 ? 0.5433 0.2891 0.6549 -0.0094 -0.0483 -0.0381 1510 VAL A CB    
2253 C  CG1   . VAL A 293 ? 0.5590 0.2931 0.6822 -0.0129 -0.0538 -0.0484 1510 VAL A CG1   
2254 C  CG2   . VAL A 293 ? 0.5476 0.2856 0.6574 -0.0020 -0.0457 -0.0329 1510 VAL A CG2   
2255 N  N     . VAL A 294 ? 0.8827 0.6554 0.9814 -0.0157 -0.0555 -0.0605 1511 VAL A N     
2256 C  CA    . VAL A 294 ? 0.8215 0.6017 0.9235 -0.0226 -0.0588 -0.0630 1511 VAL A CA    
2257 C  C     . VAL A 294 ? 0.8529 0.6209 0.9701 -0.0275 -0.0642 -0.0701 1511 VAL A C     
2258 O  O     . VAL A 294 ? 0.8126 0.5713 0.9317 -0.0245 -0.0674 -0.0809 1511 VAL A O     
2259 C  CB    . VAL A 294 ? 0.6817 0.4763 0.7696 -0.0208 -0.0606 -0.0716 1511 VAL A CB    
2260 C  CG1   . VAL A 294 ? 0.6166 0.4088 0.6977 -0.0150 -0.0629 -0.0851 1511 VAL A CG1   
2261 C  CG2   . VAL A 294 ? 0.5232 0.3248 0.6158 -0.0275 -0.0654 -0.0751 1511 VAL A CG2   
2262 N  N     . ILE A 295 ? 0.8294 0.5975 0.9585 -0.0351 -0.0649 -0.0639 1512 ILE A N     
2263 C  CA    . ILE A 295 ? 0.7502 0.5080 0.8962 -0.0418 -0.0698 -0.0688 1512 ILE A CA    
2264 C  C     . ILE A 295 ? 0.8044 0.5725 0.9495 -0.0455 -0.0760 -0.0804 1512 ILE A C     
2265 O  O     . ILE A 295 ? 0.9646 0.7476 1.1042 -0.0473 -0.0755 -0.0768 1512 ILE A O     
2266 C  CB    . ILE A 295 ? 0.6122 0.3664 0.7717 -0.0483 -0.0663 -0.0546 1512 ILE A CB    
2267 C  CG1   . ILE A 295 ? 0.5626 0.3035 0.7242 -0.0445 -0.0615 -0.0446 1512 ILE A CG1   
2268 C  CG2   . ILE A 295 ? 0.5790 0.3289 0.7565 -0.0573 -0.0713 -0.0587 1512 ILE A CG2   
2269 C  CD1   . ILE A 295 ? 0.5637 0.3003 0.7377 -0.0506 -0.0574 -0.0297 1512 ILE A CD1   
2270 N  N     . VAL A 296 ? 0.7616 0.5219 0.9122 -0.0463 -0.0823 -0.0945 1513 VAL A N     
2271 C  CA    . VAL A 296 ? 0.7223 0.4918 0.8714 -0.0492 -0.0892 -0.1074 1513 VAL A CA    
2272 C  C     . VAL A 296 ? 0.8351 0.5944 1.0032 -0.0565 -0.0956 -0.1151 1513 VAL A C     
2273 O  O     . VAL A 296 ? 0.9317 0.6773 1.1043 -0.0547 -0.0987 -0.1252 1513 VAL A O     
2274 C  CB    . VAL A 296 ? 0.7987 0.5721 0.9315 -0.0417 -0.0912 -0.1205 1513 VAL A CB    
2275 C  CG1   . VAL A 296 ? 0.8877 0.6715 1.0171 -0.0442 -0.0985 -0.1335 1513 VAL A CG1   
2276 C  CG2   . VAL A 296 ? 0.7591 0.5426 0.8743 -0.0351 -0.0848 -0.1130 1513 VAL A CG2   
2277 N  N     . PRO A 297 ? 0.8646 0.6303 1.0447 -0.0648 -0.0980 -0.1117 1514 PRO A N     
2278 C  CA    . PRO A 297 ? 0.7603 0.5166 0.9603 -0.0728 -0.1043 -0.1193 1514 PRO A CA    
2279 C  C     . PRO A 297 ? 0.9055 0.6631 1.1022 -0.0719 -0.1130 -0.1391 1514 PRO A C     
2280 O  O     . PRO A 297 ? 1.1142 0.8826 1.2927 -0.0658 -0.1141 -0.1463 1514 PRO A O     
2281 C  CB    . PRO A 297 ? 0.6174 0.3855 0.8286 -0.0810 -0.1040 -0.1103 1514 PRO A CB    
2282 C  CG    . PRO A 297 ? 0.6268 0.4121 0.8212 -0.0763 -0.0997 -0.1023 1514 PRO A CG    
2283 C  CD    . PRO A 297 ? 0.7653 0.5452 0.9440 -0.0674 -0.0938 -0.0985 1514 PRO A CD    
2284 N  N     . CYS A 298 ? 0.9586 0.7043 1.1731 -0.0782 -0.1191 -0.1484 1515 CYS A N     
2285 C  CA    . CYS A 298 ? 1.0220 0.7653 1.2333 -0.0762 -0.1272 -0.1686 1515 CYS A CA    
2286 C  C     . CYS A 298 ? 1.1552 0.8993 1.3834 -0.0854 -0.1362 -0.1794 1515 CYS A C     
2287 O  O     . CYS A 298 ? 0.9397 0.6733 1.1734 -0.0857 -0.1427 -0.1952 1515 CYS A O     
2288 C  CB    . CYS A 298 ? 1.1103 0.8330 1.3233 -0.0710 -0.1264 -0.1747 1515 CYS A CB    
2289 S  SG    . CYS A 298 ? 1.1053 0.8289 1.2967 -0.0586 -0.1181 -0.1683 1515 CYS A SG    
2290 N  N     . GLY A 299 ? 1.4624 1.2194 1.6991 -0.0926 -0.1374 -0.1727 1516 GLY A N     
2291 C  CA    . GLY A 299 ? 1.4393 1.2002 1.6921 -0.1014 -0.1464 -0.1833 1516 GLY A CA    
2292 C  C     . GLY A 299 ? 1.2401 1.0250 1.4832 -0.1014 -0.1504 -0.1854 1516 GLY A C     
2293 O  O     . GLY A 299 ? 1.0517 0.8490 1.2879 -0.1000 -0.1448 -0.1717 1516 GLY A O     
2294 N  N     . ILE A 300 ? 1.1821 0.9733 1.4253 -0.1031 -0.1604 -0.2027 1517 ILE A N     
2295 C  CA    . ILE A 300 ? 1.0950 0.9090 1.3243 -0.1008 -0.1645 -0.2052 1517 ILE A CA    
2296 C  C     . ILE A 300 ? 0.9348 0.7582 1.1714 -0.1058 -0.1765 -0.2215 1517 ILE A C     
2297 O  O     . ILE A 300 ? 0.7743 0.5860 1.0274 -0.1115 -0.1825 -0.2332 1517 ILE A O     
2298 C  CB    . ILE A 300 ? 0.9932 0.8123 1.1939 -0.0895 -0.1613 -0.2074 1517 ILE A CB    
2299 N  N     . THR A 301 ? 0.8560 0.7008 1.0800 -0.1036 -0.1802 -0.2217 1518 THR A N     
2300 C  CA    . THR A 301 ? 0.9000 0.7602 1.1237 -0.1058 -0.1916 -0.2353 1518 THR A CA    
2301 C  C     . THR A 301 ? 1.0560 0.9210 1.3070 -0.1170 -0.1977 -0.2359 1518 THR A C     
2302 O  O     . THR A 301 ? 1.1099 0.9824 1.3717 -0.1210 -0.1933 -0.2212 1518 THR A O     
2303 C  CB    . THR A 301 ? 0.9351 0.7892 1.1490 -0.1021 -0.1986 -0.2560 1518 THR A CB    
2304 N  N     . ALA A 302 ? 1.1713 1.0339 1.4331 -0.1219 -0.2081 -0.2538 1519 ALA A N     
2305 C  CA    . ALA A 302 ? 1.1687 1.0354 1.4585 -0.1333 -0.2147 -0.2566 1519 ALA A CA    
2306 C  C     . ALA A 302 ? 1.2447 1.0938 1.5590 -0.1413 -0.2078 -0.2460 1519 ALA A C     
2307 O  O     . ALA A 302 ? 1.2082 1.0640 1.5439 -0.1500 -0.2075 -0.2377 1519 ALA A O     
2308 C  CB    . ALA A 302 ? 1.1072 0.9737 1.4017 -0.1362 -0.2277 -0.2796 1519 ALA A CB    
2309 N  N     . THR A 303 ? 1.4447 1.2717 1.7561 -0.1383 -0.2022 -0.2458 1520 THR A N     
2310 C  CA    . THR A 303 ? 1.5752 1.3829 1.9083 -0.1453 -0.1958 -0.2360 1520 THR A CA    
2311 C  C     . THR A 303 ? 1.4909 1.3024 1.8212 -0.1437 -0.1839 -0.2129 1520 THR A C     
2312 O  O     . THR A 303 ? 1.3639 1.1631 1.6839 -0.1377 -0.1750 -0.2035 1520 THR A O     
2313 C  CB    . THR A 303 ? 1.6515 1.4346 1.9817 -0.1415 -0.1948 -0.2443 1520 THR A CB    
2314 N  N     . THR A 304 ? 1.5005 1.3317 1.8378 -0.1478 -0.1842 -0.2048 1521 THR A N     
2315 C  CA    . THR A 304 ? 1.4942 1.3321 1.8297 -0.1466 -0.1737 -0.1841 1521 THR A CA    
2316 C  C     . THR A 304 ? 1.4154 1.2596 1.7790 -0.1581 -0.1727 -0.1754 1521 THR A C     
2317 O  O     . THR A 304 ? 1.5073 1.3719 1.8729 -0.1590 -0.1726 -0.1688 1521 THR A O     
2318 C  CB    . THR A 304 ? 1.4455 1.3035 1.7577 -0.1379 -0.1733 -0.1808 1521 THR A CB    
2319 N  N     . THR A 305 ? 1.2084 1.0354 1.5944 -0.1668 -0.1717 -0.1749 1522 THR A N     
2320 C  CA    . THR A 305 ? 1.0778 0.9111 1.4890 -0.1773 -0.1681 -0.1631 1522 THR A CA    
2321 C  C     . THR A 305 ? 1.2775 1.1133 1.6778 -0.1720 -0.1555 -0.1428 1522 THR A C     
2322 O  O     . THR A 305 ? 1.4737 1.2911 1.8707 -0.1700 -0.1477 -0.1341 1522 THR A O     
2323 C  CB    . THR A 305 ? 0.8703 0.6835 1.3076 -0.1882 -0.1685 -0.1645 1522 THR A CB    
2324 N  N     . ASP A 306 ? 1.2523 1.1106 1.6472 -0.1695 -0.1537 -0.1355 1523 ASP A N     
2325 C  CA    . ASP A 306 ? 1.1402 1.0027 1.5194 -0.1622 -0.1429 -0.1190 1523 ASP A CA    
2326 C  C     . ASP A 306 ? 1.0751 0.9243 1.4661 -0.1667 -0.1323 -0.1033 1523 ASP A C     
2327 O  O     . ASP A 306 ? 0.7346 0.5817 1.1111 -0.1600 -0.1231 -0.0907 1523 ASP A O     
2328 C  CB    . ASP A 306 ? 1.1076 0.9959 1.4855 -0.1608 -0.1430 -0.1135 1523 ASP A CB    
2329 C  CG    . ASP A 306 ? 0.9881 0.8884 1.3433 -0.1517 -0.1498 -0.1231 1523 ASP A CG    
2330 O  OD1   . ASP A 306 ? 0.7760 0.6809 1.1102 -0.1426 -0.1442 -0.1153 1523 ASP A OD1   
2331 O  OD2   . ASP A 306 ? 1.0405 0.9456 1.3990 -0.1538 -0.1608 -0.1385 1523 ASP A OD2   
2332 N  N     . ASP A 307 ? 1.3556 1.1972 1.7731 -0.1781 -0.1334 -0.1034 1524 ASP A N     
2333 C  CA    . ASP A 307 ? 1.4375 1.2623 1.8662 -0.1828 -0.1241 -0.0896 1524 ASP A CA    
2334 C  C     . ASP A 307 ? 1.4614 1.2626 1.8738 -0.1754 -0.1216 -0.0905 1524 ASP A C     
2335 O  O     . ASP A 307 ? 1.5393 1.3324 1.9434 -0.1713 -0.1119 -0.0763 1524 ASP A O     
2336 C  CB    . ASP A 307 ? 1.4597 1.2792 1.9199 -0.1970 -0.1278 -0.0928 1524 ASP A CB    
2337 C  CG    . ASP A 307 ? 1.5547 1.3533 2.0277 -0.2027 -0.1196 -0.0800 1524 ASP A CG    
2338 O  OD1   . ASP A 307 ? 1.5779 1.3537 2.0418 -0.1983 -0.1189 -0.0819 1524 ASP A OD1   
2339 O  OD2   . ASP A 307 ? 1.6030 1.4083 2.0956 -0.2118 -0.1138 -0.0679 1524 ASP A OD2   
2340 N  N     . GLU A 308 ? 1.2936 1.0842 1.7009 -0.1731 -0.1303 -0.1077 1525 GLU A N     
2341 C  CA    . GLU A 308 ? 1.1222 0.8921 1.5139 -0.1650 -0.1285 -0.1102 1525 GLU A CA    
2342 C  C     . GLU A 308 ? 1.1638 0.9416 1.5264 -0.1522 -0.1239 -0.1060 1525 GLU A C     
2343 O  O     . GLU A 308 ? 1.2630 1.0274 1.6140 -0.1457 -0.1176 -0.0989 1525 GLU A O     
2344 C  CB    . GLU A 308 ? 0.9864 0.7444 1.3805 -0.1655 -0.1390 -0.1308 1525 GLU A CB    
2345 N  N     . ARG A 309 ? 1.0846 0.8840 1.4355 -0.1484 -0.1272 -0.1100 1526 ARG A N     
2346 C  CA    . ARG A 309 ? 1.0176 0.8244 1.3418 -0.1370 -0.1227 -0.1054 1526 ARG A CA    
2347 C  C     . ARG A 309 ? 1.0443 0.8537 1.3664 -0.1356 -0.1114 -0.0856 1526 ARG A C     
2348 O  O     . ARG A 309 ? 0.9794 0.7832 1.2836 -0.1272 -0.1053 -0.0794 1526 ARG A O     
2349 C  CB    . ARG A 309 ? 0.9592 0.7877 1.2725 -0.1338 -0.1290 -0.1133 1526 ARG A CB    
2350 N  N     . ARG A 310 ? 1.1824 1.0005 1.5230 -0.1438 -0.1083 -0.0760 1527 ARG A N     
2351 C  CA    . ARG A 310 ? 1.1371 0.9577 1.4770 -0.1430 -0.0974 -0.0575 1527 ARG A CA    
2352 C  C     . ARG A 310 ? 1.0011 0.7994 1.3444 -0.1437 -0.0913 -0.0493 1527 ARG A C     
2353 O  O     . ARG A 310 ? 0.9951 0.7904 1.3262 -0.1378 -0.0831 -0.0373 1527 ARG A O     
2354 C  CB    . ARG A 310 ? 1.1830 1.0199 1.5430 -0.1517 -0.0956 -0.0501 1527 ARG A CB    
2355 N  N     . ARG A 311 ? 0.8922 0.6743 1.2523 -0.1506 -0.0957 -0.0558 1528 ARG A N     
2356 C  CA    . ARG A 311 ? 0.9161 0.6751 1.2796 -0.1508 -0.0908 -0.0484 1528 ARG A CA    
2357 C  C     . ARG A 311 ? 1.0227 0.7711 1.3628 -0.1388 -0.0899 -0.0516 1528 ARG A C     
2358 O  O     . ARG A 311 ? 1.1200 0.8591 1.4522 -0.1341 -0.0824 -0.0395 1528 ARG A O     
2359 C  CB    . ARG A 311 ? 0.8271 0.5700 1.2133 -0.1604 -0.0969 -0.0568 1528 ARG A CB    
2360 N  N     . LEU A 312 ? 1.0004 0.7518 1.3286 -0.1336 -0.0974 -0.0678 1529 LEU A N     
2361 C  CA    . LEU A 312 ? 0.9812 0.7259 1.2873 -0.1222 -0.0967 -0.0721 1529 LEU A CA    
2362 C  C     . LEU A 312 ? 0.8487 0.6054 1.1364 -0.1147 -0.0890 -0.0599 1529 LEU A C     
2363 O  O     . LEU A 312 ? 0.8894 0.6367 1.1659 -0.1079 -0.0835 -0.0530 1529 LEU A O     
2364 C  CB    . LEU A 312 ? 1.0482 0.7984 1.3449 -0.1186 -0.1058 -0.0913 1529 LEU A CB    
2365 C  CG    . LEU A 312 ? 1.0141 0.7586 1.2886 -0.1071 -0.1050 -0.0968 1529 LEU A CG    
2366 C  CD1   . LEU A 312 ? 0.9459 0.6668 1.2266 -0.1060 -0.1025 -0.0941 1529 LEU A CD1   
2367 C  CD2   . LEU A 312 ? 1.0861 0.8350 1.3527 -0.1044 -0.1139 -0.1161 1529 LEU A CD2   
2368 N  N     . TYR A 313 ? 0.8740 0.6515 1.1585 -0.1156 -0.0888 -0.0577 1530 TYR A N     
2369 C  CA    . TYR A 313 ? 0.9539 0.7426 1.2208 -0.1084 -0.0820 -0.0474 1530 TYR A CA    
2370 C  C     . TYR A 313 ? 0.9860 0.7693 1.2574 -0.1095 -0.0725 -0.0297 1530 TYR A C     
2371 O  O     . TYR A 313 ? 0.8313 0.6123 1.0874 -0.1020 -0.0668 -0.0225 1530 TYR A O     
2372 C  CB    . TYR A 313 ? 0.8985 0.7097 1.1627 -0.1091 -0.0840 -0.0484 1530 TYR A CB    
2373 N  N     . GLU A 314 ? 1.1487 0.9300 1.4411 -0.1189 -0.0707 -0.0227 1531 GLU A N     
2374 C  CA    . GLU A 314 ? 1.0669 0.8450 1.3631 -0.1204 -0.0613 -0.0052 1531 GLU A CA    
2375 C  C     . GLU A 314 ? 0.9182 0.6746 1.2098 -0.1162 -0.0584 -0.0008 1531 GLU A C     
2376 O  O     . GLU A 314 ? 0.8738 0.6291 1.1545 -0.1108 -0.0512 0.0112  1531 GLU A O     
2377 C  CB    . GLU A 314 ? 1.1591 0.9406 1.4800 -0.1322 -0.0602 0.0006  1531 GLU A CB    
2378 C  CG    . GLU A 314 ? 1.3521 1.1356 1.6779 -0.1348 -0.0500 0.0193  1531 GLU A CG    
2379 C  CD    . GLU A 314 ? 1.4810 1.2579 1.8328 -0.1470 -0.0487 0.0252  1531 GLU A CD    
2380 O  OE1   . GLU A 314 ? 1.5266 1.2942 1.8820 -0.1488 -0.0412 0.0395  1531 GLU A OE1   
2381 O  OE2   . GLU A 314 ? 1.4980 1.2792 1.8667 -0.1550 -0.0551 0.0158  1531 GLU A OE2   
2382 N  N     . SER A 315 ? 0.7247 0.4642 1.0224 -0.1173 -0.0646 -0.0117 1532 SER A N     
2383 C  CA    . SER A 315 ? 0.6924 0.4112 0.9852 -0.1120 -0.0625 -0.0085 1532 SER A CA    
2384 C  C     . SER A 315 ? 0.7190 0.4401 0.9878 -0.0998 -0.0619 -0.0123 1532 SER A C     
2385 O  O     . SER A 315 ? 0.8069 0.5193 1.0670 -0.0936 -0.0570 -0.0036 1532 SER A O     
2386 C  CB    . SER A 315 ? 0.8029 0.5026 1.1103 -0.1165 -0.0695 -0.0197 1532 SER A CB    
2387 O  OG    . SER A 315 ? 0.7296 0.4105 1.0295 -0.1090 -0.0695 -0.0213 1532 SER A OG    
2388 N  N     . CYS A 316 ? 0.7285 0.4623 0.9862 -0.0961 -0.0666 -0.0245 1533 CYS A N     
2389 C  CA    . CYS A 316 ? 0.7496 0.4872 0.9852 -0.0853 -0.0653 -0.0272 1533 CYS A CA    
2390 C  C     . CYS A 316 ? 0.8720 0.6215 1.0964 -0.0816 -0.0574 -0.0131 1533 CYS A C     
2391 O  O     . CYS A 316 ? 0.9504 0.6972 1.1605 -0.0736 -0.0538 -0.0093 1533 CYS A O     
2392 C  CB    . CYS A 316 ? 0.8211 0.5703 1.0473 -0.0829 -0.0717 -0.0423 1533 CYS A CB    
2393 S  SG    . CYS A 316 ? 0.9280 0.6622 1.1597 -0.0829 -0.0803 -0.0608 1533 CYS A SG    
2394 N  N     . ARG A 317 ? 0.9053 0.6685 1.1362 -0.0872 -0.0549 -0.0059 1534 ARG A N     
2395 C  CA    . ARG A 317 ? 0.9005 0.6743 1.1215 -0.0837 -0.0473 0.0072  1534 ARG A CA    
2396 C  C     . ARG A 317 ? 0.7763 0.5377 1.0004 -0.0833 -0.0409 0.0208  1534 ARG A C     
2397 O  O     . ARG A 317 ? 0.6287 0.3919 0.8389 -0.0765 -0.0358 0.0284  1534 ARG A O     
2398 C  CB    . ARG A 317 ? 0.9591 0.7508 1.1872 -0.0893 -0.0460 0.0112  1534 ARG A CB    
2399 C  CG    . ARG A 317 ? 1.0723 0.8797 1.2894 -0.0860 -0.0503 0.0016  1534 ARG A CG    
2400 C  CD    . ARG A 317 ? 1.1614 0.9867 1.3873 -0.0911 -0.0499 0.0049  1534 ARG A CD    
2401 N  NE    . ARG A 317 ? 1.1447 0.9779 1.3754 -0.0941 -0.0583 -0.0078 1534 ARG A NE    
2402 C  CZ    . ARG A 317 ? 1.1202 0.9601 1.3694 -0.1024 -0.0616 -0.0097 1534 ARG A CZ    
2403 N  NH1   . ARG A 317 ? 1.0545 0.8944 1.3200 -0.1091 -0.0565 0.0007  1534 ARG A NH1   
2404 N  NH2   . ARG A 317 ? 1.0582 0.9057 1.3095 -0.1040 -0.0699 -0.0219 1534 ARG A NH2   
2405 N  N     . GLU A 318 ? 0.7233 0.4710 0.9649 -0.0903 -0.0416 0.0235  1535 GLU A N     
2406 C  CA    . GLU A 318 ? 0.7019 0.4358 0.9461 -0.0896 -0.0360 0.0368  1535 GLU A CA    
2407 C  C     . GLU A 318 ? 0.7138 0.4349 0.9445 -0.0799 -0.0369 0.0341  1535 GLU A C     
2408 O  O     . GLU A 318 ? 0.8527 0.5719 1.0742 -0.0745 -0.0314 0.0452  1535 GLU A O     
2409 C  CB    . GLU A 318 ? 0.7765 0.4967 1.0429 -0.0994 -0.0373 0.0394  1535 GLU A CB    
2410 C  CG    . GLU A 318 ? 0.8740 0.5729 1.1438 -0.0980 -0.0345 0.0489  1535 GLU A CG    
2411 C  CD    . GLU A 318 ? 0.9424 0.6269 1.2356 -0.1086 -0.0363 0.0506  1535 GLU A CD    
2412 O  OE1   . GLU A 318 ? 0.8928 0.5625 1.1917 -0.1100 -0.0322 0.0632  1535 GLU A OE1   
2413 O  OE2   . GLU A 318 ? 0.9310 0.6185 1.2371 -0.1157 -0.0420 0.0395  1535 GLU A OE2   
2414 N  N     . LEU A 319 ? 0.6317 0.3453 0.8612 -0.0771 -0.0437 0.0191  1536 LEU A N     
2415 C  CA    . LEU A 319 ? 0.6191 0.3222 0.8366 -0.0674 -0.0446 0.0154  1536 LEU A CA    
2416 C  C     . LEU A 319 ? 0.8576 0.5750 1.0546 -0.0589 -0.0413 0.0168  1536 LEU A C     
2417 O  O     . LEU A 319 ? 0.8833 0.5962 1.0709 -0.0518 -0.0379 0.0236  1536 LEU A O     
2418 C  CB    . LEU A 319 ? 0.6037 0.2974 0.8242 -0.0662 -0.0523 -0.0020 1536 LEU A CB    
2419 C  CG    . LEU A 319 ? 0.6889 0.3694 0.9010 -0.0565 -0.0533 -0.0061 1536 LEU A CG    
2420 C  CD1   . LEU A 319 ? 0.6318 0.2902 0.8564 -0.0578 -0.0527 0.0012  1536 LEU A CD1   
2421 C  CD2   . LEU A 319 ? 0.6445 0.3249 0.8516 -0.0526 -0.0599 -0.0253 1536 LEU A CD2   
2422 N  N     . GLU A 320 ? 0.9908 0.7255 1.1808 -0.0594 -0.0427 0.0105  1537 GLU A N     
2423 C  CA    . GLU A 320 ? 0.9498 0.6978 1.1215 -0.0522 -0.0395 0.0123  1537 GLU A CA    
2424 C  C     . GLU A 320 ? 0.9129 0.6661 1.0812 -0.0515 -0.0321 0.0284  1537 GLU A C     
2425 O  O     . GLU A 320 ? 0.8561 0.6123 1.0108 -0.0443 -0.0289 0.0325  1537 GLU A O     
2426 C  CB    . GLU A 320 ? 0.8423 0.6069 1.0082 -0.0534 -0.0424 0.0037  1537 GLU A CB    
2427 C  CG    . GLU A 320 ? 0.8489 0.6287 1.0160 -0.0574 -0.0387 0.0121  1537 GLU A CG    
2428 C  CD    . GLU A 320 ? 0.8443 0.6399 1.0010 -0.0556 -0.0411 0.0047  1537 GLU A CD    
2429 O  OE1   . GLU A 320 ? 0.8013 0.6021 0.9424 -0.0489 -0.0392 0.0045  1537 GLU A OE1   
2430 O  OE2   . GLU A 320 ? 0.8584 0.6611 1.0229 -0.0610 -0.0451 -0.0007 1537 GLU A OE2   
2431 N  N     . GLN A 321 ? 0.8998 0.6544 1.0806 -0.0590 -0.0292 0.0376  1538 GLN A N     
2432 C  CA    . GLN A 321 ? 0.7392 0.5002 0.9162 -0.0583 -0.0219 0.0526  1538 GLN A CA    
2433 C  C     . GLN A 321 ? 0.6592 0.4061 0.8335 -0.0538 -0.0190 0.0616  1538 GLN A C     
2434 O  O     . GLN A 321 ? 0.5400 0.2915 0.7011 -0.0473 -0.0149 0.0684  1538 GLN A O     
2435 C  CB    . GLN A 321 ? 0.7464 0.5130 0.9386 -0.0677 -0.0192 0.0599  1538 GLN A CB    
2436 C  CG    . GLN A 321 ? 1.0133 0.8003 1.2028 -0.0694 -0.0179 0.0589  1538 GLN A CG    
2437 C  CD    . GLN A 321 ? 1.2432 1.0414 1.4138 -0.0614 -0.0142 0.0618  1538 GLN A CD    
2438 O  OE1   . GLN A 321 ? 1.2853 1.0843 1.4500 -0.0584 -0.0083 0.0730  1538 GLN A OE1   
2439 N  NE2   . GLN A 321 ? 1.2926 1.0996 1.4537 -0.0580 -0.0179 0.0517  1538 GLN A NE2   
2440 N  N     . THR A 322 ? 0.6965 0.4257 0.8830 -0.0568 -0.0216 0.0610  1539 THR A N     
2441 C  CA    . THR A 322 ? 0.8002 0.5141 0.9850 -0.0519 -0.0198 0.0692  1539 THR A CA    
2442 C  C     . THR A 322 ? 0.7967 0.5092 0.9665 -0.0413 -0.0220 0.0623  1539 THR A C     
2443 O  O     . THR A 322 ? 0.6539 0.3607 0.8168 -0.0350 -0.0194 0.0705  1539 THR A O     
2444 C  CB    . THR A 322 ? 0.7850 0.4792 0.9870 -0.0575 -0.0230 0.0683  1539 THR A CB    
2445 O  OG1   . THR A 322 ? 0.8870 0.5786 1.0936 -0.0588 -0.0301 0.0512  1539 THR A OG1   
2446 C  CG2   . THR A 322 ? 0.6893 0.3852 0.9065 -0.0681 -0.0195 0.0783  1539 THR A CG2   
2447 N  N     . PHE A 323 ? 0.8274 0.5464 0.9918 -0.0391 -0.0264 0.0476  1540 PHE A N     
2448 C  CA    . PHE A 323 ? 0.8854 0.6068 1.0351 -0.0294 -0.0275 0.0414  1540 PHE A CA    
2449 C  C     . PHE A 323 ? 0.9056 0.6430 1.0406 -0.0252 -0.0228 0.0478  1540 PHE A C     
2450 O  O     . PHE A 323 ? 0.9888 0.7258 1.1137 -0.0175 -0.0214 0.0505  1540 PHE A O     
2451 C  CB    . PHE A 323 ? 0.8139 0.5380 0.9619 -0.0286 -0.0332 0.0243  1540 PHE A CB    
2452 C  CG    . PHE A 323 ? 0.8114 0.5186 0.9669 -0.0267 -0.0380 0.0156  1540 PHE A CG    
2453 C  CD1   . PHE A 323 ? 0.8418 0.5356 0.9970 -0.0205 -0.0373 0.0205  1540 PHE A CD1   
2454 C  CD2   . PHE A 323 ? 0.9010 0.6053 1.0640 -0.0309 -0.0436 0.0023  1540 PHE A CD2   
2455 C  CE1   . PHE A 323 ? 0.9774 0.6544 1.1404 -0.0181 -0.0420 0.0119  1540 PHE A CE1   
2456 C  CE2   . PHE A 323 ? 0.9784 0.6664 1.1486 -0.0289 -0.0482 -0.0069 1540 PHE A CE2   
2457 C  CZ    . PHE A 323 ? 0.9843 0.6581 1.1549 -0.0224 -0.0473 -0.0022 1540 PHE A CZ    
2458 N  N     . VAL A 324 ? 0.7711 0.5233 0.9047 -0.0297 -0.0208 0.0493  1541 VAL A N     
2459 C  CA    . VAL A 324 ? 0.8447 0.6111 0.9645 -0.0254 -0.0166 0.0544  1541 VAL A CA    
2460 C  C     . VAL A 324 ? 0.9840 0.7478 1.1019 -0.0235 -0.0113 0.0692  1541 VAL A C     
2461 O  O     . VAL A 324 ? 0.9946 0.7632 1.1002 -0.0167 -0.0092 0.0724  1541 VAL A O     
2462 C  CB    . VAL A 324 ? 0.8909 0.6732 1.0097 -0.0299 -0.0157 0.0525  1541 VAL A CB    
2463 C  CG1   . VAL A 324 ? 0.7864 0.5714 0.9062 -0.0316 -0.0214 0.0383  1541 VAL A CG1   
2464 C  CG2   . VAL A 324 ? 1.0421 0.8267 1.1722 -0.0372 -0.0123 0.0623  1541 VAL A CG2   
2465 N  N     . LYS A 325 ? 0.9940 0.7503 1.1239 -0.0294 -0.0092 0.0784  1542 LYS A N     
2466 C  CA    . LYS A 325 ? 0.9308 0.6851 1.0580 -0.0276 -0.0038 0.0935  1542 LYS A CA    
2467 C  C     . LYS A 325 ? 0.9337 0.6766 1.0547 -0.0195 -0.0052 0.0954  1542 LYS A C     
2468 O  O     . LYS A 325 ? 0.9075 0.6539 1.0188 -0.0143 -0.0017 0.1046  1542 LYS A O     
2469 C  CB    . LYS A 325 ? 0.8537 0.6010 0.9960 -0.0360 -0.0012 0.1033  1542 LYS A CB    
2470 C  CG    . LYS A 325 ? 0.9085 0.6594 1.0468 -0.0356 0.0057  0.1198  1542 LYS A CG    
2471 C  CD    . LYS A 325 ? 1.0908 0.8247 1.2295 -0.0319 0.0061  0.1292  1542 LYS A CD    
2472 C  CE    . LYS A 325 ? 1.1771 0.9172 1.3031 -0.0265 0.0116  0.1428  1542 LYS A CE    
2473 N  NZ    . LYS A 325 ? 1.1424 0.8894 1.2517 -0.0164 0.0100  0.1378  1542 LYS A NZ    
2474 N  N     . ALA A 326 ? 1.0046 0.7348 1.1307 -0.0177 -0.0105 0.0861  1543 ALA A N     
2475 C  CA    . ALA A 326 ? 0.9609 0.6820 1.0810 -0.0088 -0.0125 0.0852  1543 ALA A CA    
2476 C  C     . ALA A 326 ? 1.0052 0.7383 1.1118 -0.0017 -0.0140 0.0755  1543 ALA A C     
2477 O  O     . ALA A 326 ? 1.0873 0.8142 1.1914 0.0050  -0.0173 0.0689  1543 ALA A O     
2478 C  CB    . ALA A 326 ? 0.7308 0.4326 0.8629 -0.0093 -0.0174 0.0791  1543 ALA A CB    
2479 N  N     . GLY A 327 ? 0.8534 0.6034 0.9524 -0.0034 -0.0116 0.0744  1544 GLY A N     
2480 C  CA    . GLY A 327 ? 0.9053 0.6672 0.9912 0.0026  -0.0120 0.0677  1544 GLY A CA    
2481 C  C     . GLY A 327 ? 0.9854 0.7473 1.0706 0.0043  -0.0165 0.0527  1544 GLY A C     
2482 O  O     . GLY A 327 ? 1.1068 0.8750 1.1826 0.0104  -0.0171 0.0473  1544 GLY A O     
2483 N  N     . ILE A 328 ? 0.9431 0.6986 1.0383 -0.0010 -0.0197 0.0455  1545 ILE A N     
2484 C  CA    . ILE A 328 ? 0.8772 0.6331 0.9712 0.0006  -0.0240 0.0307  1545 ILE A CA    
2485 C  C     . ILE A 328 ? 0.7842 0.5531 0.8753 -0.0045 -0.0243 0.0251  1545 ILE A C     
2486 O  O     . ILE A 328 ? 0.7054 0.4756 0.8039 -0.0115 -0.0238 0.0286  1545 ILE A O     
2487 C  CB    . ILE A 328 ? 0.8096 0.5489 0.9158 -0.0009 -0.0283 0.0245  1545 ILE A CB    
2488 C  CG1   . ILE A 328 ? 0.6971 0.4230 0.8052 0.0058  -0.0286 0.0288  1545 ILE A CG1   
2489 C  CG2   . ILE A 328 ? 0.8035 0.5454 0.9077 0.0002  -0.0326 0.0085  1545 ILE A CG2   
2490 C  CD1   . ILE A 328 ? 0.6803 0.3889 0.8001 0.0054  -0.0332 0.0214  1545 ILE A CD1   
2491 N  N     . ARG A 329 ? 0.8162 0.5949 0.8970 -0.0009 -0.0251 0.0168  1546 ARG A N     
2492 C  CA    . ARG A 329 ? 0.8657 0.6565 0.9426 -0.0050 -0.0256 0.0122  1546 ARG A CA    
2493 C  C     . ARG A 329 ? 0.7727 0.5583 0.8576 -0.0092 -0.0305 0.0019  1546 ARG A C     
2494 O  O     . ARG A 329 ? 0.7048 0.4893 0.7866 -0.0063 -0.0336 -0.0092 1546 ARG A O     
2495 C  CB    . ARG A 329 ? 0.8301 0.6327 0.8933 -0.0003 -0.0245 0.0078  1546 ARG A CB    
2496 C  CG    . ARG A 329 ? 0.7099 0.5169 0.7657 0.0045  -0.0203 0.0166  1546 ARG A CG    
2497 C  CD    . ARG A 329 ? 0.7193 0.5390 0.7627 0.0077  -0.0191 0.0127  1546 ARG A CD    
2498 N  NE    . ARG A 329 ? 0.7092 0.5290 0.7485 0.0124  -0.0209 0.0029  1546 ARG A NE    
2499 C  CZ    . ARG A 329 ? 0.7219 0.5381 0.7605 0.0186  -0.0208 0.0028  1546 ARG A CZ    
2500 N  NH1   . ARG A 329 ? 0.7391 0.5505 0.7800 0.0210  -0.0191 0.0123  1546 ARG A NH1   
2501 N  NH2   . ARG A 329 ? 0.6672 0.4853 0.7029 0.0227  -0.0222 -0.0068 1546 ARG A NH2   
2502 N  N     . CYS A 330 ? 0.7459 0.5284 0.8420 -0.0162 -0.0312 0.0054  1547 CYS A N     
2503 C  CA    . CYS A 330 ? 0.7968 0.5750 0.9020 -0.0212 -0.0364 -0.0041 1547 CYS A CA    
2504 C  C     . CYS A 330 ? 0.8678 0.6572 0.9756 -0.0275 -0.0368 -0.0030 1547 CYS A C     
2505 O  O     . CYS A 330 ? 0.9691 0.7634 1.0797 -0.0303 -0.0329 0.0076  1547 CYS A O     
2506 C  CB    . CYS A 330 ? 0.8064 0.5679 0.9265 -0.0242 -0.0380 -0.0022 1547 CYS A CB    
2507 S  SG    . CYS A 330 ? 0.7892 0.5458 0.9230 -0.0319 -0.0447 -0.0137 1547 CYS A SG    
2508 N  N     . GLU A 331 ? 0.7928 0.5871 0.8995 -0.0293 -0.0415 -0.0141 1548 GLU A N     
2509 C  CA    . GLU A 331 ? 0.8031 0.6069 0.9145 -0.0354 -0.0435 -0.0149 1548 GLU A CA    
2510 C  C     . GLU A 331 ? 0.7933 0.5922 0.9128 -0.0390 -0.0503 -0.0270 1548 GLU A C     
2511 O  O     . GLU A 331 ? 0.7617 0.5538 0.8779 -0.0354 -0.0532 -0.0367 1548 GLU A O     
2512 C  CB    . GLU A 331 ? 0.7293 0.5486 0.8270 -0.0330 -0.0426 -0.0154 1548 GLU A CB    
2513 N  N     . GLY A 332 ? 0.7456 0.5485 0.8762 -0.0459 -0.0529 -0.0270 1549 GLY A N     
2514 C  CA    . GLY A 332 ? 0.6629 0.4631 0.8014 -0.0499 -0.0599 -0.0390 1549 GLY A CA    
2515 C  C     . GLY A 332 ? 0.6768 0.4919 0.8061 -0.0496 -0.0635 -0.0457 1549 GLY A C     
2516 O  O     . GLY A 332 ? 0.8654 0.6923 0.9883 -0.0489 -0.0606 -0.0389 1549 GLY A O     
2517 N  N     . ASP A 333 ? 0.5158 0.3302 0.6444 -0.0499 -0.0700 -0.0591 1550 ASP A N     
2518 C  CA    . ASP A 333 ? 0.5388 0.3666 0.6585 -0.0497 -0.0745 -0.0665 1550 ASP A CA    
2519 C  C     . ASP A 333 ? 0.7346 0.5638 0.8695 -0.0570 -0.0810 -0.0723 1550 ASP A C     
2520 O  O     . ASP A 333 ? 0.8372 0.6589 0.9778 -0.0586 -0.0865 -0.0836 1550 ASP A O     
2521 C  CB    . ASP A 333 ? 0.6238 0.4510 0.7288 -0.0436 -0.0766 -0.0777 1550 ASP A CB    
2522 C  CG    . ASP A 333 ? 0.6847 0.5249 0.7795 -0.0432 -0.0816 -0.0857 1550 ASP A CG    
2523 O  OD1   . ASP A 333 ? 0.6939 0.5383 0.7973 -0.0483 -0.0877 -0.0908 1550 ASP A OD1   
2524 O  OD2   . ASP A 333 ? 0.6912 0.5375 0.7692 -0.0378 -0.0797 -0.0872 1550 ASP A OD2   
2525 N  N     . TYR A 334 ? 0.8088 0.6482 0.9507 -0.0613 -0.0807 -0.0653 1551 TYR A N     
2526 C  CA    . TYR A 334 ? 0.9036 0.7451 1.0632 -0.0691 -0.0863 -0.0692 1551 TYR A CA    
2527 C  C     . TYR A 334 ? 0.9603 0.8169 1.1162 -0.0700 -0.0928 -0.0759 1551 TYR A C     
2528 O  O     . TYR A 334 ? 1.1894 1.0496 1.3601 -0.0764 -0.0984 -0.0803 1551 TYR A O     
2529 C  CB    . TYR A 334 ? 0.9048 0.7470 1.0795 -0.0743 -0.0812 -0.0561 1551 TYR A CB    
2530 C  CG    . TYR A 334 ? 0.8824 0.7117 1.0596 -0.0732 -0.0741 -0.0465 1551 TYR A CG    
2531 C  CD1   . TYR A 334 ? 0.8829 0.6956 1.0683 -0.0748 -0.0753 -0.0504 1551 TYR A CD1   
2532 C  CD2   . TYR A 334 ? 1.0102 0.8439 1.1816 -0.0705 -0.0665 -0.0335 1551 TYR A CD2   
2533 C  CE1   . TYR A 334 ? 0.9745 0.7753 1.1621 -0.0734 -0.0691 -0.0407 1551 TYR A CE1   
2534 C  CE2   . TYR A 334 ? 1.0608 0.8836 1.2338 -0.0692 -0.0603 -0.0243 1551 TYR A CE2   
2535 C  CZ    . TYR A 334 ? 1.0300 0.8364 1.2110 -0.0706 -0.0617 -0.0276 1551 TYR A CZ    
2536 O  OH    . TYR A 334 ? 1.1358 0.9310 1.3180 -0.0689 -0.0560 -0.0179 1551 TYR A OH    
2537 N  N     . ARG A 335 ? 0.8766 0.7422 1.0138 -0.0640 -0.0926 -0.0768 1552 ARG A N     
2538 C  CA    . ARG A 335 ? 0.8616 0.7419 0.9933 -0.0639 -0.0985 -0.0813 1552 ARG A CA    
2539 C  C     . ARG A 335 ? 0.9259 0.8068 1.0653 -0.0679 -0.1080 -0.0954 1552 ARG A C     
2540 O  O     . ARG A 335 ? 0.8160 0.6877 0.9525 -0.0667 -0.1106 -0.1057 1552 ARG A O     
2541 C  CB    . ARG A 335 ? 0.8040 0.6893 0.9125 -0.0564 -0.0965 -0.0815 1552 ARG A CB    
2542 C  CG    . ARG A 335 ? 0.7294 0.6115 0.8321 -0.0528 -0.0870 -0.0687 1552 ARG A CG    
2543 C  CD    . ARG A 335 ? 0.7670 0.6511 0.8487 -0.0459 -0.0834 -0.0677 1552 ARG A CD    
2544 N  NE    . ARG A 335 ? 0.7972 0.6787 0.8674 -0.0426 -0.0866 -0.0792 1552 ARG A NE    
2545 C  CZ    . ARG A 335 ? 0.8525 0.7300 0.9100 -0.0374 -0.0820 -0.0795 1552 ARG A CZ    
2546 N  NH1   . ARG A 335 ? 0.9022 0.7773 0.9572 -0.0351 -0.0748 -0.0692 1552 ARG A NH1   
2547 N  NH2   . ARG A 335 ? 0.7714 0.6482 0.8189 -0.0344 -0.0847 -0.0904 1552 ARG A NH2   
2548 N  N     . ASP A 336 ? 1.1342 1.0267 1.2847 -0.0727 -0.1136 -0.0964 1553 ASP A N     
2549 C  CA    . ASP A 336 ? 1.2497 1.1422 1.4114 -0.0778 -0.1229 -0.1096 1553 ASP A CA    
2550 C  C     . ASP A 336 ? 1.2099 1.1092 1.3536 -0.0730 -0.1294 -0.1212 1553 ASP A C     
2551 O  O     . ASP A 336 ? 1.1117 1.0107 1.2595 -0.0755 -0.1375 -0.1347 1553 ASP A O     
2552 C  CB    . ASP A 336 ? 1.3662 1.2716 1.5445 -0.0841 -0.1286 -0.1096 1553 ASP A CB    
2553 C  CG    . ASP A 336 ? 1.5235 1.4452 1.6941 -0.0807 -0.1273 -0.1005 1553 ASP A CG    
2554 O  OD1   . ASP A 336 ? 1.5593 1.4836 1.7085 -0.0734 -0.1252 -0.0987 1553 ASP A OD1   
2555 O  OD2   . ASP A 336 ? 1.6067 1.5378 1.7928 -0.0851 -0.1277 -0.0947 1553 ASP A OD2   
2556 N  N     . ASN A 337 ? 1.2231 1.1287 1.3468 -0.0663 -0.1258 -0.1160 1554 ASN A N     
2557 C  CA    . ASN A 337 ? 1.2319 1.1475 1.3373 -0.0618 -0.1314 -0.1238 1554 ASN A CA    
2558 C  C     . ASN A 337 ? 1.2324 1.1397 1.3267 -0.0585 -0.1328 -0.1361 1554 ASN A C     
2559 O  O     . ASN A 337 ? 1.2156 1.1279 1.3050 -0.0584 -0.1408 -0.1489 1554 ASN A O     
2560 C  CB    . ASN A 337 ? 1.2442 1.1677 1.3333 -0.0562 -0.1260 -0.1125 1554 ASN A CB    
2561 C  CG    . ASN A 337 ? 1.3996 1.3300 1.4649 -0.0502 -0.1286 -0.1181 1554 ASN A CG    
2562 O  OD1   . ASN A 337 ? 1.4000 1.3312 1.4593 -0.0496 -0.1347 -0.1309 1554 ASN A OD1   
2563 N  ND2   . ASN A 337 ? 1.4609 1.3962 1.5122 -0.0456 -0.1235 -0.1080 1554 ASN A ND2   
2564 N  N     . TYR A 338 ? 1.2258 1.1202 1.3190 -0.0564 -0.1258 -0.1333 1555 TYR A N     
2565 C  CA    . TYR A 338 ? 1.2221 1.1103 1.3018 -0.0514 -0.1252 -0.1430 1555 TYR A CA    
2566 C  C     . TYR A 338 ? 1.2480 1.1217 1.3425 -0.0546 -0.1277 -0.1526 1555 TYR A C     
2567 O  O     . TYR A 338 ? 1.2836 1.1488 1.3972 -0.0599 -0.1263 -0.1473 1555 TYR A O     
2568 C  CB    . TYR A 338 ? 1.2341 1.1187 1.3011 -0.0457 -0.1157 -0.1336 1555 TYR A CB    
2569 C  CG    . TYR A 338 ? 1.2525 1.1494 1.3043 -0.0423 -0.1127 -0.1241 1555 TYR A CG    
2570 C  CD1   . TYR A 338 ? 1.2843 1.1832 1.3413 -0.0435 -0.1075 -0.1098 1555 TYR A CD1   
2571 C  CD2   . TYR A 338 ? 1.3193 1.2254 1.3513 -0.0379 -0.1147 -0.1294 1555 TYR A CD2   
2572 C  CE1   . TYR A 338 ? 1.3447 1.2534 1.3884 -0.0403 -0.1050 -0.1015 1555 TYR A CE1   
2573 C  CE2   . TYR A 338 ? 1.3640 1.2799 1.3824 -0.0350 -0.1120 -0.1201 1555 TYR A CE2   
2574 C  CZ    . TYR A 338 ? 1.3222 1.2388 1.3470 -0.0362 -0.1073 -0.1064 1555 TYR A CZ    
2575 O  OH    . TYR A 338 ? 1.1761 1.1010 1.1883 -0.0333 -0.1048 -0.0975 1555 TYR A OH    
2576 N  N     . SER A 339 ? 1.1593 1.0305 1.2449 -0.0513 -0.1315 -0.1671 1556 SER A N     
2577 C  CA    . SER A 339 ? 1.1363 0.9929 1.2341 -0.0532 -0.1344 -0.1783 1556 SER A CA    
2578 C  C     . SER A 339 ? 1.1587 1.0011 1.2567 -0.0493 -0.1262 -0.1728 1556 SER A C     
2579 O  O     . SER A 339 ? 1.2808 1.1266 1.3649 -0.0439 -0.1193 -0.1646 1556 SER A O     
2580 C  CB    . SER A 339 ? 1.1902 1.0502 1.2774 -0.0502 -0.1415 -0.1967 1556 SER A CB    
2581 O  OG    . SER A 339 ? 1.2305 1.1020 1.2934 -0.0433 -0.1393 -0.1975 1556 SER A OG    
2582 N  N     . PRO A 340 ? 1.0564 0.8824 1.1708 -0.0521 -0.1272 -0.1771 1557 PRO A N     
2583 C  CA    . PRO A 340 ? 0.8999 0.7117 1.0146 -0.0477 -0.1204 -0.1731 1557 PRO A CA    
2584 C  C     . PRO A 340 ? 0.9256 0.7394 1.0213 -0.0388 -0.1181 -0.1810 1557 PRO A C     
2585 O  O     . PRO A 340 ? 0.8802 0.6903 0.9699 -0.0337 -0.1109 -0.1734 1557 PRO A O     
2586 C  CB    . PRO A 340 ? 0.8888 0.6831 1.0241 -0.0525 -0.1244 -0.1799 1557 PRO A CB    
2587 C  CG    . PRO A 340 ? 0.9931 0.7930 1.1434 -0.0615 -0.1295 -0.1780 1557 PRO A CG    
2588 C  CD    . PRO A 340 ? 1.0493 0.8693 1.1855 -0.0606 -0.1335 -0.1814 1557 PRO A CD    
2589 N  N     . GLY A 341 ? 0.9781 0.7985 1.0643 -0.0367 -0.1241 -0.1965 1558 GLY A N     
2590 C  CA    . GLY A 341 ? 0.9702 0.7941 1.0384 -0.0283 -0.1214 -0.2041 1558 GLY A CA    
2591 C  C     . GLY A 341 ? 0.9560 0.7945 1.0057 -0.0246 -0.1155 -0.1938 1558 GLY A C     
2592 O  O     . GLY A 341 ? 0.9243 0.7631 0.9633 -0.0183 -0.1092 -0.1919 1558 GLY A O     
2593 N  N     . TRP A 342 ? 0.9393 0.7902 0.9856 -0.0284 -0.1176 -0.1873 1559 TRP A N     
2594 C  CA    . TRP A 342 ? 0.8522 0.7151 0.8834 -0.0257 -0.1120 -0.1754 1559 TRP A CA    
2595 C  C     . TRP A 342 ? 0.7539 0.6096 0.7899 -0.0247 -0.1036 -0.1610 1559 TRP A C     
2596 O  O     . TRP A 342 ? 0.6591 0.5174 0.6830 -0.0194 -0.0974 -0.1574 1559 TRP A O     
2597 C  CB    . TRP A 342 ? 0.9082 0.7834 0.9386 -0.0301 -0.1163 -0.1701 1559 TRP A CB    
2598 C  CG    . TRP A 342 ? 0.9740 0.8614 0.9879 -0.0272 -0.1114 -0.1589 1559 TRP A CG    
2599 C  CD1   . TRP A 342 ? 1.0214 0.9216 1.0159 -0.0239 -0.1129 -0.1622 1559 TRP A CD1   
2600 C  CD2   . TRP A 342 ? 0.8175 0.7046 0.8330 -0.0275 -0.1045 -0.1427 1559 TRP A CD2   
2601 N  NE1   . TRP A 342 ? 0.9486 0.8556 0.9337 -0.0224 -0.1073 -0.1488 1559 TRP A NE1   
2602 C  CE2   . TRP A 342 ? 0.8178 0.7170 0.8156 -0.0245 -0.1023 -0.1374 1559 TRP A CE2   
2603 C  CE3   . TRP A 342 ? 0.7307 0.6087 0.7606 -0.0299 -0.1000 -0.1324 1559 TRP A CE3   
2604 C  CZ2   . TRP A 342 ? 0.7510 0.6525 0.7459 -0.0239 -0.0961 -0.1230 1559 TRP A CZ2   
2605 C  CZ3   . TRP A 342 ? 0.7184 0.5998 0.7444 -0.0290 -0.0938 -0.1185 1559 TRP A CZ3   
2606 C  CH2   . TRP A 342 ? 0.7644 0.6572 0.7736 -0.0261 -0.0920 -0.1143 1559 TRP A CH2   
2607 N  N     . LYS A 343 ? 0.7461 0.5931 0.8001 -0.0298 -0.1033 -0.1530 1560 LYS A N     
2608 C  CA    . LYS A 343 ? 0.7767 0.6171 0.8353 -0.0289 -0.0956 -0.1391 1560 LYS A CA    
2609 C  C     . LYS A 343 ? 0.8061 0.6371 0.8616 -0.0229 -0.0915 -0.1428 1560 LYS A C     
2610 O  O     . LYS A 343 ? 0.7994 0.6314 0.8481 -0.0190 -0.0847 -0.1341 1560 LYS A O     
2611 C  CB    . LYS A 343 ? 0.7480 0.5794 0.8271 -0.0355 -0.0964 -0.1319 1560 LYS A CB    
2612 C  CG    . LYS A 343 ? 0.7838 0.6251 0.8692 -0.0417 -0.1011 -0.1297 1560 LYS A CG    
2613 C  CD    . LYS A 343 ? 0.7563 0.5891 0.8637 -0.0489 -0.1019 -0.1241 1560 LYS A CD    
2614 C  CE    . LYS A 343 ? 0.6114 0.4555 0.7265 -0.0550 -0.1067 -0.1225 1560 LYS A CE    
2615 N  NZ    . LYS A 343 ? 0.5493 0.3886 0.6838 -0.0613 -0.1043 -0.1120 1560 LYS A NZ    
2616 N  N     . TYR A 344 ? 0.9378 0.7597 0.9986 -0.0218 -0.0957 -0.1563 1561 TYR A N     
2617 C  CA    . TYR A 344 ? 0.9385 0.7533 0.9953 -0.0149 -0.0927 -0.1625 1561 TYR A CA    
2618 C  C     . TYR A 344 ? 0.9036 0.7317 0.9406 -0.0090 -0.0879 -0.1620 1561 TYR A C     
2619 O  O     . TYR A 344 ? 1.0895 0.9170 1.1229 -0.0050 -0.0814 -0.1540 1561 TYR A O     
2620 C  CB    . TYR A 344 ? 0.9971 0.8044 1.0587 -0.0141 -0.0992 -0.1803 1561 TYR A CB    
2621 C  CG    . TYR A 344 ? 1.1358 0.9265 1.2184 -0.0194 -0.1032 -0.1817 1561 TYR A CG    
2622 C  CD1   . TYR A 344 ? 1.1652 0.9480 1.2608 -0.0236 -0.1000 -0.1669 1561 TYR A CD1   
2623 C  CD2   . TYR A 344 ? 1.2274 1.0104 1.3172 -0.0203 -0.1102 -0.1979 1561 TYR A CD2   
2624 C  CE1   . TYR A 344 ? 1.1911 0.9586 1.3064 -0.0290 -0.1032 -0.1672 1561 TYR A CE1   
2625 C  CE2   . TYR A 344 ? 1.2156 0.9824 1.3259 -0.0258 -0.1140 -0.1991 1561 TYR A CE2   
2626 C  CZ    . TYR A 344 ? 1.1986 0.9576 1.3217 -0.0304 -0.1102 -0.1831 1561 TYR A CZ    
2627 O  OH    . TYR A 344 ? 1.1689 0.9117 1.3126 -0.0364 -0.1134 -0.1831 1561 TYR A OH    
2628 N  N     . ASN A 345 ? 0.5828 0.4237 0.6068 -0.0087 -0.0912 -0.1699 1562 ASN A N     
2629 C  CA    . ASN A 345 ? 0.6118 0.4650 0.6168 -0.0032 -0.0867 -0.1706 1562 ASN A CA    
2630 C  C     . ASN A 345 ? 0.6327 0.4928 0.6318 -0.0037 -0.0805 -0.1544 1562 ASN A C     
2631 O  O     . ASN A 345 ? 0.6186 0.4831 0.6086 0.0008  -0.0743 -0.1509 1562 ASN A O     
2632 C  CB    . ASN A 345 ? 0.6811 0.5468 0.6726 -0.0030 -0.0914 -0.1811 1562 ASN A CB    
2633 C  CG    . ASN A 345 ? 0.8384 0.7184 0.8103 0.0009  -0.0861 -0.1775 1562 ASN A CG    
2634 O  OD1   . ASN A 345 ? 0.8430 0.7332 0.8062 -0.0015 -0.0860 -0.1695 1562 ASN A OD1   
2635 N  ND2   . ASN A 345 ? 0.8892 0.7698 0.8549 0.0068  -0.0813 -0.1826 1562 ASN A ND2   
2636 N  N     . HIS A 346 ? 0.7203 0.5827 0.7245 -0.0092 -0.0822 -0.1451 1563 HIS A N     
2637 C  CA    . HIS A 346 ? 0.7958 0.6637 0.7959 -0.0101 -0.0770 -0.1301 1563 HIS A CA    
2638 C  C     . HIS A 346 ? 0.8263 0.6866 0.8313 -0.0073 -0.0705 -0.1223 1563 HIS A C     
2639 O  O     . HIS A 346 ? 0.9315 0.7975 0.9261 -0.0036 -0.0649 -0.1180 1563 HIS A O     
2640 C  CB    . HIS A 346 ? 0.8917 0.7603 0.9018 -0.0163 -0.0804 -0.1227 1563 HIS A CB    
2641 C  CG    . HIS A 346 ? 0.9286 0.8023 0.9357 -0.0171 -0.0754 -0.1079 1563 HIS A CG    
2642 N  ND1   . HIS A 346 ? 0.9386 0.8234 0.9302 -0.0150 -0.0730 -0.1039 1563 HIS A ND1   
2643 C  CD2   . HIS A 346 ? 0.9576 0.8268 0.9755 -0.0197 -0.0726 -0.0965 1563 HIS A CD2   
2644 C  CE1   . HIS A 346 ? 0.9757 0.8619 0.9690 -0.0162 -0.0691 -0.0913 1563 HIS A CE1   
2645 N  NE2   . HIS A 346 ? 0.9482 0.8257 0.9570 -0.0189 -0.0687 -0.0868 1563 HIS A NE2   
2646 N  N     . TRP A 347 ? 0.7205 0.5677 0.7413 -0.0090 -0.0712 -0.1205 1564 TRP A N     
2647 C  CA    . TRP A 347 ? 0.6827 0.5231 0.7077 -0.0063 -0.0654 -0.1117 1564 TRP A CA    
2648 C  C     . TRP A 347 ? 0.7053 0.5437 0.7249 0.0006  -0.0628 -0.1191 1564 TRP A C     
2649 O  O     . TRP A 347 ? 0.5225 0.3606 0.5405 0.0041  -0.0574 -0.1121 1564 TRP A O     
2650 C  CB    . TRP A 347 ? 0.5265 0.3536 0.5691 -0.0100 -0.0665 -0.1064 1564 TRP A CB    
2651 C  CG    . TRP A 347 ? 0.7100 0.5407 0.7588 -0.0165 -0.0680 -0.0981 1564 TRP A CG    
2652 C  CD1   . TRP A 347 ? 0.8652 0.6944 0.9239 -0.0221 -0.0738 -0.1023 1564 TRP A CD1   
2653 C  CD2   . TRP A 347 ? 0.7391 0.5763 0.7853 -0.0178 -0.0636 -0.0848 1564 TRP A CD2   
2654 N  NE1   . TRP A 347 ? 0.8786 0.7136 0.9416 -0.0267 -0.0730 -0.0921 1564 TRP A NE1   
2655 C  CE2   . TRP A 347 ? 0.7162 0.5558 0.7712 -0.0239 -0.0668 -0.0814 1564 TRP A CE2   
2656 C  CE3   . TRP A 347 ? 0.7060 0.5475 0.7438 -0.0143 -0.0574 -0.0759 1564 TRP A CE3   
2657 C  CZ2   . TRP A 347 ? 0.7496 0.5956 0.8051 -0.0261 -0.0637 -0.0697 1564 TRP A CZ2   
2658 C  CZ3   . TRP A 347 ? 0.7244 0.5714 0.7622 -0.0167 -0.0547 -0.0647 1564 TRP A CZ3   
2659 C  CH2   . TRP A 347 ? 0.8292 0.6784 0.8756 -0.0223 -0.0577 -0.0616 1564 TRP A CH2   
2660 N  N     . GLU A 348 ? 0.7964 0.6347 0.8132 0.0028  -0.0665 -0.1335 1565 GLU A N     
2661 C  CA    . GLU A 348 ? 0.9012 0.7402 0.9122 0.0099  -0.0637 -0.1414 1565 GLU A CA    
2662 C  C     . GLU A 348 ? 0.8790 0.7334 0.8735 0.0125  -0.0587 -0.1386 1565 GLU A C     
2663 O  O     . GLU A 348 ? 0.8062 0.6631 0.7971 0.0179  -0.0540 -0.1393 1565 GLU A O     
2664 C  CB    . GLU A 348 ? 1.0097 0.8445 1.0223 0.0117  -0.0690 -0.1583 1565 GLU A CB    
2665 C  CG    . GLU A 348 ? 1.1800 0.9967 1.2110 0.0097  -0.0731 -0.1606 1565 GLU A CG    
2666 C  CD    . GLU A 348 ? 1.1766 0.9855 1.2113 0.0134  -0.0774 -0.1776 1565 GLU A CD    
2667 O  OE1   . GLU A 348 ? 1.2182 1.0371 1.2415 0.0156  -0.0792 -0.1895 1565 GLU A OE1   
2668 O  OE2   . GLU A 348 ? 1.0996 0.8921 1.1486 0.0141  -0.0790 -0.1788 1565 GLU A OE2   
2669 N  N     . LEU A 349 ? 0.7913 0.6563 0.7765 0.0088  -0.0597 -0.1355 1566 LEU A N     
2670 C  CA    . LEU A 349 ? 0.7519 0.6300 0.7229 0.0102  -0.0545 -0.1298 1566 LEU A CA    
2671 C  C     . LEU A 349 ? 0.8808 0.7573 0.8553 0.0097  -0.0494 -0.1158 1566 LEU A C     
2672 O  O     . LEU A 349 ? 0.9288 0.8122 0.8959 0.0126  -0.0440 -0.1123 1566 LEU A O     
2673 C  CB    . LEU A 349 ? 0.6384 0.5264 0.5993 0.0063  -0.0573 -0.1286 1566 LEU A CB    
2674 C  CG    . LEU A 349 ? 0.6448 0.5378 0.5986 0.0067  -0.0625 -0.1417 1566 LEU A CG    
2675 C  CD1   . LEU A 349 ? 0.6037 0.4996 0.5575 0.0014  -0.0683 -0.1389 1566 LEU A CD1   
2676 C  CD2   . LEU A 349 ? 0.5432 0.4489 0.4799 0.0105  -0.0584 -0.1455 1566 LEU A CD2   
2677 N  N     . LYS A 350 ? 0.8034 0.6718 0.7892 0.0059  -0.0510 -0.1077 1567 LYS A N     
2678 C  CA    . LYS A 350 ? 0.7354 0.6019 0.7248 0.0055  -0.0465 -0.0948 1567 LYS A CA    
2679 C  C     . LYS A 350 ? 0.7629 0.6212 0.7596 0.0100  -0.0438 -0.0943 1567 LYS A C     
2680 O  O     . LYS A 350 ? 0.7841 0.6414 0.7830 0.0106  -0.0401 -0.0842 1567 LYS A O     
2681 C  CB    . LYS A 350 ? 0.6398 0.5017 0.6384 0.0000  -0.0489 -0.0866 1567 LYS A CB    
2682 C  CG    . LYS A 350 ? 0.7760 0.6475 0.7673 -0.0037 -0.0502 -0.0828 1567 LYS A CG    
2683 C  CD    . LYS A 350 ? 0.8220 0.6913 0.8217 -0.0076 -0.0498 -0.0716 1567 LYS A CD    
2684 C  CE    . LYS A 350 ? 0.8424 0.7206 0.8368 -0.0108 -0.0520 -0.0684 1567 LYS A CE    
2685 N  NZ    . LYS A 350 ? 0.8840 0.7593 0.8908 -0.0154 -0.0542 -0.0625 1567 LYS A NZ    
2686 N  N     . GLY A 351 ? 0.6410 0.4934 0.6414 0.0137  -0.0458 -0.1051 1568 GLY A N     
2687 C  CA    . GLY A 351 ? 0.6317 0.4774 0.6379 0.0191  -0.0434 -0.1053 1568 GLY A CA    
2688 C  C     . GLY A 351 ? 0.6548 0.4880 0.6736 0.0179  -0.0436 -0.0960 1568 GLY A C     
2689 O  O     . GLY A 351 ? 0.6018 0.4323 0.6231 0.0221  -0.0404 -0.0909 1568 GLY A O     
2690 N  N     . VAL A 352 ? 0.6395 0.4656 0.6665 0.0123  -0.0471 -0.0934 1569 VAL A N     
2691 C  CA    . VAL A 352 ? 0.6575 0.4710 0.6970 0.0108  -0.0471 -0.0847 1569 VAL A CA    
2692 C  C     . VAL A 352 ? 0.6209 0.4218 0.6684 0.0159  -0.0484 -0.0906 1569 VAL A C     
2693 O  O     . VAL A 352 ? 0.6825 0.4782 0.7333 0.0165  -0.0524 -0.1026 1569 VAL A O     
2694 C  CB    . VAL A 352 ? 0.6059 0.4148 0.6542 0.0034  -0.0508 -0.0824 1569 VAL A CB    
2695 C  CG1   . VAL A 352 ? 0.5201 0.3151 0.5821 0.0019  -0.0505 -0.0742 1569 VAL A CG1   
2696 C  CG2   . VAL A 352 ? 0.5481 0.3691 0.5896 -0.0008 -0.0493 -0.0753 1569 VAL A CG2   
2697 N  N     . PRO A 353 ? 0.6618 0.4574 0.7129 0.0200  -0.0454 -0.0828 1570 PRO A N     
2698 C  CA    . PRO A 353 ? 0.7442 0.5287 0.8019 0.0264  -0.0465 -0.0886 1570 PRO A CA    
2699 C  C     . PRO A 353 ? 0.7064 0.4752 0.7762 0.0244  -0.0516 -0.0957 1570 PRO A C     
2700 O  O     . PRO A 353 ? 0.7478 0.5125 0.8189 0.0288  -0.0542 -0.1085 1570 PRO A O     
2701 C  CB    . PRO A 353 ? 0.7601 0.5405 0.8207 0.0291  -0.0432 -0.0754 1570 PRO A CB    
2702 C  CG    . PRO A 353 ? 0.6639 0.4598 0.7138 0.0273  -0.0391 -0.0678 1570 PRO A CG    
2703 C  CD    . PRO A 353 ? 0.6143 0.4157 0.6615 0.0200  -0.0408 -0.0696 1570 PRO A CD    
2704 N  N     . VAL A 354 ? 0.5740 0.3341 0.6532 0.0177  -0.0532 -0.0881 1571 VAL A N     
2705 C  CA    . VAL A 354 ? 0.6510 0.3958 0.7432 0.0146  -0.0582 -0.0944 1571 VAL A CA    
2706 C  C     . VAL A 354 ? 0.5683 0.3167 0.6638 0.0054  -0.0608 -0.0940 1571 VAL A C     
2707 O  O     . VAL A 354 ? 0.6655 0.4183 0.7618 0.0006  -0.0583 -0.0818 1571 VAL A O     
2708 C  CB    . VAL A 354 ? 0.8464 0.5736 0.9511 0.0157  -0.0578 -0.0854 1571 VAL A CB    
2709 C  CG1   . VAL A 354 ? 0.9625 0.6916 1.0685 0.0111  -0.0540 -0.0683 1571 VAL A CG1   
2710 C  CG2   . VAL A 354 ? 0.8294 0.5397 0.9484 0.0120  -0.0631 -0.0925 1571 VAL A CG2   
2711 N  N     . ARG A 355 ? 0.6534 0.4001 0.7512 0.0033  -0.0660 -0.1075 1572 ARG A N     
2712 C  CA    . ARG A 355 ? 0.6568 0.4053 0.7607 -0.0053 -0.0699 -0.1089 1572 ARG A CA    
2713 C  C     . ARG A 355 ? 0.8082 0.5382 0.9304 -0.0098 -0.0732 -0.1082 1572 ARG A C     
2714 O  O     . ARG A 355 ? 0.9450 0.6612 1.0736 -0.0061 -0.0756 -0.1161 1572 ARG A O     
2715 C  CB    . ARG A 355 ? 0.6236 0.3814 0.7196 -0.0053 -0.0743 -0.1244 1572 ARG A CB    
2716 C  CG    . ARG A 355 ? 0.6401 0.3974 0.7446 -0.0134 -0.0804 -0.1301 1572 ARG A CG    
2717 C  CD    . ARG A 355 ? 0.6969 0.4656 0.7902 -0.0120 -0.0846 -0.1449 1572 ARG A CD    
2718 N  NE    . ARG A 355 ? 0.8036 0.5626 0.9008 -0.0089 -0.0893 -0.1611 1572 ARG A NE    
2719 C  CZ    . ARG A 355 ? 1.0233 0.7836 1.1113 -0.0008 -0.0879 -0.1704 1572 ARG A CZ    
2720 N  NH1   . ARG A 355 ? 1.0136 0.7846 1.0883 0.0047  -0.0819 -0.1647 1572 ARG A NH1   
2721 N  NH2   . ARG A 355 ? 1.1311 0.8819 1.2239 0.0019  -0.0925 -0.1860 1572 ARG A NH2   
2722 N  N     . ILE A 356 ? 0.6684 0.3981 0.7996 -0.0179 -0.0731 -0.0990 1573 ILE A N     
2723 C  CA    . ILE A 356 ? 0.6502 0.3637 0.7998 -0.0240 -0.0762 -0.0980 1573 ILE A CA    
2724 C  C     . ILE A 356 ? 0.7946 0.5113 0.9498 -0.0304 -0.0829 -0.1101 1573 ILE A C     
2725 O  O     . ILE A 356 ? 0.7794 0.5119 0.9286 -0.0339 -0.0835 -0.1099 1573 ILE A O     
2726 C  CB    . ILE A 356 ? 0.7507 0.4623 0.9082 -0.0293 -0.0718 -0.0800 1573 ILE A CB    
2727 C  CG1   . ILE A 356 ? 0.8396 0.5416 0.9963 -0.0234 -0.0669 -0.0691 1573 ILE A CG1   
2728 C  CG2   . ILE A 356 ? 0.8163 0.5173 0.9930 -0.0388 -0.0753 -0.0793 1573 ILE A CG2   
2729 C  CD1   . ILE A 356 ? 0.9109 0.6095 1.0761 -0.0289 -0.0627 -0.0519 1573 ILE A CD1   
2730 N  N     . GLU A 357 ? 0.8425 0.5442 1.0094 -0.0317 -0.0882 -0.1211 1574 GLU A N     
2731 C  CA    . GLU A 357 ? 0.8212 0.5233 0.9973 -0.0389 -0.0953 -0.1325 1574 GLU A CA    
2732 C  C     . GLU A 357 ? 0.7958 0.4818 0.9937 -0.0472 -0.0966 -0.1261 1574 GLU A C     
2733 O  O     . GLU A 357 ? 0.9509 0.6179 1.1578 -0.0451 -0.0961 -0.1247 1574 GLU A O     
2734 C  CB    . GLU A 357 ? 0.8476 0.5470 1.0189 -0.0340 -0.1010 -0.1527 1574 GLU A CB    
2735 C  CG    . GLU A 357 ? 0.9469 0.6578 1.0975 -0.0239 -0.0978 -0.1576 1574 GLU A CG    
2736 C  CD    . GLU A 357 ? 1.0483 0.7592 1.1930 -0.0190 -0.1030 -0.1781 1574 GLU A CD    
2737 O  OE1   . GLU A 357 ? 1.1439 0.8404 1.3015 -0.0212 -0.1086 -0.1887 1574 GLU A OE1   
2738 O  OE2   . GLU A 357 ? 1.0379 0.7630 1.1652 -0.0128 -0.1013 -0.1838 1574 GLU A OE2   
2739 N  N     . LEU A 358 ? 0.6467 0.3408 0.8531 -0.0564 -0.0977 -0.1210 1575 LEU A N     
2740 C  CA    . LEU A 358 ? 0.7028 0.3849 0.9306 -0.0658 -0.0984 -0.1138 1575 LEU A CA    
2741 C  C     . LEU A 358 ? 0.7886 0.4776 1.0268 -0.0745 -0.1056 -0.1243 1575 LEU A C     
2742 O  O     . LEU A 358 ? 0.7556 0.4627 0.9903 -0.0780 -0.1055 -0.1210 1575 LEU A O     
2743 C  CB    . LEU A 358 ? 0.6434 0.3297 0.8732 -0.0686 -0.0907 -0.0931 1575 LEU A CB    
2744 C  CG    . LEU A 358 ? 0.6883 0.3615 0.9402 -0.0781 -0.0899 -0.0835 1575 LEU A CG    
2745 C  CD1   . LEU A 358 ? 0.7397 0.4067 0.9918 -0.0767 -0.0817 -0.0641 1575 LEU A CD1   
2746 C  CD2   . LEU A 358 ? 0.7026 0.3885 0.9654 -0.0883 -0.0921 -0.0828 1575 LEU A CD2   
2747 N  N     . GLY A 359 ? 0.9330 0.6074 1.1840 -0.0776 -0.1122 -0.1375 1576 GLY A N     
2748 C  CA    . GLY A 359 ? 1.0222 0.7010 1.2856 -0.0863 -0.1199 -0.1485 1576 GLY A CA    
2749 C  C     . GLY A 359 ? 1.0607 0.7263 1.3493 -0.0973 -0.1203 -0.1412 1576 GLY A C     
2750 O  O     . GLY A 359 ? 1.1245 0.7796 1.4198 -0.0984 -0.1139 -0.1254 1576 GLY A O     
2751 N  N     . PHE A 360 ? 1.0156 0.6825 1.3185 -0.1057 -0.1282 -0.1528 1577 PHE A N     
2752 C  CA    . PHE A 360 ? 0.9932 0.6478 1.3221 -0.1173 -0.1292 -0.1476 1577 PHE A CA    
2753 C  C     . PHE A 360 ? 0.9707 0.5966 1.3108 -0.1165 -0.1296 -0.1493 1577 PHE A C     
2754 O  O     . PHE A 360 ? 0.9499 0.5640 1.3056 -0.1231 -0.1256 -0.1364 1577 PHE A O     
2755 C  CB    . PHE A 360 ? 0.9737 0.6376 1.3158 -0.1264 -0.1385 -0.1615 1577 PHE A CB    
2756 C  CG    . PHE A 360 ? 0.9660 0.6570 1.3009 -0.1282 -0.1385 -0.1580 1577 PHE A CG    
2757 C  CD1   . PHE A 360 ? 0.9477 0.6486 1.2877 -0.1326 -0.1312 -0.1393 1577 PHE A CD1   
2758 C  CD2   . PHE A 360 ? 0.9852 0.6922 1.3078 -0.1250 -0.1455 -0.1731 1577 PHE A CD2   
2759 C  CE1   . PHE A 360 ? 0.7873 0.5130 1.1209 -0.1334 -0.1312 -0.1360 1577 PHE A CE1   
2760 C  CE2   . PHE A 360 ? 0.8497 0.5812 1.1655 -0.1260 -0.1456 -0.1690 1577 PHE A CE2   
2761 C  CZ    . PHE A 360 ? 0.6872 0.4275 1.0091 -0.1301 -0.1386 -0.1507 1577 PHE A CZ    
2762 N  N     . LYS A 361 ? 0.8417 0.4579 1.1724 -0.1079 -0.1335 -0.1643 1578 LYS A N     
2763 C  CA    . LYS A 361 ? 0.9262 0.5206 1.2619 -0.1048 -0.1320 -0.1640 1578 LYS A CA    
2764 C  C     . LYS A 361 ? 0.9686 0.5514 1.3017 -0.1000 -0.1235 -0.1453 1578 LYS A C     
2765 O  O     . LYS A 361 ? 1.0049 0.5743 1.3494 -0.1042 -0.1195 -0.1328 1578 LYS A O     
2766 C  CB    . LYS A 361 ? 0.9816 0.5720 1.3056 -0.0954 -0.1373 -0.1841 1578 LYS A CB    
2767 N  N     . ASP A 362 ? 1.0248 0.6161 1.3404 -0.0911 -0.1198 -0.1415 1579 ASP A N     
2768 C  CA    . ASP A 362 ? 1.0421 0.6268 1.3530 -0.0863 -0.1113 -0.1225 1579 ASP A CA    
2769 C  C     . ASP A 362 ? 0.9699 0.5571 1.2933 -0.0963 -0.1060 -0.1034 1579 ASP A C     
2770 O  O     . ASP A 362 ? 0.9980 0.5701 1.3286 -0.0969 -0.1011 -0.0887 1579 ASP A O     
2771 C  CB    . ASP A 362 ? 1.0859 0.6879 1.3721 -0.0755 -0.1066 -0.1200 1579 ASP A CB    
2772 C  CG    . ASP A 362 ? 1.2532 0.8620 1.5258 -0.0679 -0.1119 -0.1402 1579 ASP A CG    
2773 O  OD1   . ASP A 362 ? 1.2942 0.8866 1.5692 -0.0624 -0.1153 -0.1516 1579 ASP A OD1   
2774 O  OD2   . ASP A 362 ? 1.2967 0.9272 1.5563 -0.0673 -0.1125 -0.1446 1579 ASP A OD2   
2775 N  N     . LEU A 363 ? 0.9336 0.5394 1.2605 -0.1042 -0.1073 -0.1038 1580 LEU A N     
2776 C  CA    . LEU A 363 ? 0.8791 0.4891 1.2199 -0.1145 -0.1026 -0.0872 1580 LEU A CA    
2777 C  C     . LEU A 363 ? 0.8553 0.4448 1.2173 -0.1226 -0.1033 -0.0838 1580 LEU A C     
2778 O  O     . LEU A 363 ? 0.8155 0.3980 1.1828 -0.1253 -0.0962 -0.0657 1580 LEU A O     
2779 C  CB    . LEU A 363 ? 0.8101 0.4441 1.1525 -0.1211 -0.1054 -0.0917 1580 LEU A CB    
2780 C  CG    . LEU A 363 ? 0.8110 0.4594 1.1600 -0.1284 -0.0989 -0.0744 1580 LEU A CG    
2781 C  CD1   . LEU A 363 ? 0.7085 0.3844 1.0423 -0.1254 -0.0985 -0.0758 1580 LEU A CD1   
2782 C  CD2   . LEU A 363 ? 0.9012 0.5440 1.2778 -0.1425 -0.1016 -0.0736 1580 LEU A CD2   
2783 N  N     . GLN A 364 ? 0.9102 0.4945 1.2782 -0.1247 -0.1103 -0.1000 1581 GLN A N     
2784 C  CA    . GLN A 364 ? 0.9262 0.4950 1.3086 -0.1309 -0.1098 -0.0965 1581 GLN A CA    
2785 C  C     . GLN A 364 ? 1.0152 0.5634 1.3929 -0.1234 -0.1049 -0.0866 1581 GLN A C     
2786 O  O     . GLN A 364 ? 1.1138 0.6503 1.5020 -0.1288 -0.1009 -0.0741 1581 GLN A O     
2787 C  CB    . GLN A 364 ? 0.9492 0.5156 1.3373 -0.1332 -0.1187 -0.1174 1581 GLN A CB    
2788 N  N     . ASN A 365 ? 1.0316 0.5761 1.3934 -0.1111 -0.1048 -0.0908 1582 ASN A N     
2789 C  CA    . ASN A 365 ? 0.9725 0.4976 1.3298 -0.1029 -0.1013 -0.0835 1582 ASN A CA    
2790 C  C     . ASN A 365 ? 0.9743 0.5010 1.3219 -0.0973 -0.0937 -0.0651 1582 ASN A C     
2791 O  O     . ASN A 365 ? 1.0086 0.5218 1.3497 -0.0884 -0.0914 -0.0599 1582 ASN A O     
2792 C  CB    . ASN A 365 ? 0.8526 0.3703 1.2002 -0.0919 -0.1066 -0.1017 1582 ASN A CB    
2793 C  CG    . ASN A 365 ? 0.8540 0.3704 1.2088 -0.0959 -0.1145 -0.1216 1582 ASN A CG    
2794 O  OD1   . ASN A 365 ? 0.9287 0.4537 1.2748 -0.0910 -0.1197 -0.1393 1582 ASN A OD1   
2795 N  ND2   . ASN A 365 ? 0.8652 0.3713 1.2356 -0.1049 -0.1152 -0.1188 1582 ASN A ND2   
2796 N  N     . ASP A 366 ? 0.9400 0.4830 1.2873 -0.1024 -0.0898 -0.0545 1583 ASP A N     
2797 C  CA    . ASP A 366 ? 0.9406 0.4869 1.2786 -0.0977 -0.0823 -0.0364 1583 ASP A CA    
2798 C  C     . ASP A 366 ? 0.8132 0.3567 1.1348 -0.0838 -0.0829 -0.0415 1583 ASP A C     
2799 O  O     . ASP A 366 ? 0.7643 0.2981 1.0797 -0.0767 -0.0786 -0.0301 1583 ASP A O     
2800 C  CB    . ASP A 366 ? 1.0864 0.6205 1.4304 -0.1006 -0.0759 -0.0169 1583 ASP A CB    
2801 C  CG    . ASP A 366 ? 1.2218 0.7668 1.5617 -0.1021 -0.0677 0.0032  1583 ASP A CG    
2802 O  OD1   . ASP A 366 ? 1.3694 0.9167 1.6952 -0.0924 -0.0654 0.0074  1583 ASP A OD1   
2803 O  OD2   . ASP A 366 ? 1.2251 0.7757 1.5756 -0.1124 -0.0635 0.0148  1583 ASP A OD2   
2804 N  N     . GLN A 367 ? 0.8344 0.3926 1.1442 -0.0793 -0.0869 -0.0577 1584 GLN A N     
2805 C  CA    . GLN A 367 ? 0.8561 0.4174 1.1474 -0.0660 -0.0869 -0.0648 1584 GLN A CA    
2806 C  C     . GLN A 367 ? 0.9215 0.5087 1.1968 -0.0638 -0.0877 -0.0742 1584 GLN A C     
2807 O  O     . GLN A 367 ? 0.8945 0.4967 1.1728 -0.0719 -0.0881 -0.0737 1584 GLN A O     
2808 C  CB    . GLN A 367 ? 0.7979 0.3382 1.0956 -0.0610 -0.0933 -0.0804 1584 GLN A CB    
2809 C  CG    . GLN A 367 ? 0.9344 0.4735 1.2434 -0.0686 -0.1007 -0.0977 1584 GLN A CG    
2810 C  CD    . GLN A 367 ? 1.0516 0.5848 1.3551 -0.0604 -0.1064 -0.1180 1584 GLN A CD    
2811 O  OE1   . GLN A 367 ? 1.0170 0.5620 1.3097 -0.0556 -0.1097 -0.1322 1584 GLN A OE1   
2812 N  NE2   . GLN A 367 ? 1.1198 0.6351 1.4307 -0.0591 -0.1075 -0.1199 1584 GLN A NE2   
2813 N  N     . PHE A 368 ? 0.8336 0.4259 1.0924 -0.0526 -0.0879 -0.0824 1585 PHE A N     
2814 C  CA    . PHE A 368 ? 0.7329 0.3472 0.9750 -0.0488 -0.0889 -0.0926 1585 PHE A CA    
2815 C  C     . PHE A 368 ? 0.8128 0.4234 1.0434 -0.0368 -0.0902 -0.1040 1585 PHE A C     
2816 O  O     . PHE A 368 ? 0.9388 0.5329 1.1727 -0.0309 -0.0890 -0.1002 1585 PHE A O     
2817 C  CB    . PHE A 368 ? 0.6731 0.3073 0.9030 -0.0488 -0.0823 -0.0784 1585 PHE A CB    
2818 C  CG    . PHE A 368 ? 0.7040 0.3341 0.9270 -0.0420 -0.0758 -0.0634 1585 PHE A CG    
2819 C  CD1   . PHE A 368 ? 0.7672 0.3877 1.0002 -0.0465 -0.0716 -0.0462 1585 PHE A CD1   
2820 C  CD2   . PHE A 368 ? 0.6608 0.2972 0.8673 -0.0310 -0.0739 -0.0666 1585 PHE A CD2   
2821 C  CE1   . PHE A 368 ? 0.9855 0.6028 1.2110 -0.0396 -0.0661 -0.0326 1585 PHE A CE1   
2822 C  CE2   . PHE A 368 ? 0.7370 0.3705 0.9374 -0.0245 -0.0686 -0.0535 1585 PHE A CE2   
2823 C  CZ    . PHE A 368 ? 0.8929 0.5168 1.1021 -0.0285 -0.0649 -0.0365 1585 PHE A CZ    
2824 N  N     . VAL A 369 ? 0.7951 0.4209 1.0126 -0.0330 -0.0926 -0.1179 1586 VAL A N     
2825 C  CA    . VAL A 369 ? 0.7791 0.4044 0.9851 -0.0215 -0.0930 -0.1285 1586 VAL A CA    
2826 C  C     . VAL A 369 ? 0.8029 0.4500 0.9888 -0.0159 -0.0879 -0.1242 1586 VAL A C     
2827 O  O     . VAL A 369 ? 0.8065 0.4715 0.9846 -0.0198 -0.0880 -0.1254 1586 VAL A O     
2828 C  CB    . VAL A 369 ? 0.7722 0.3938 0.9803 -0.0205 -0.1003 -0.1507 1586 VAL A CB    
2829 C  CG1   . VAL A 369 ? 0.7057 0.3430 0.9117 -0.0281 -0.1043 -0.1588 1586 VAL A CG1   
2830 C  CG2   . VAL A 369 ? 0.9068 0.5332 1.1008 -0.0085 -0.0994 -0.1612 1586 VAL A CG2   
2831 N  N     . ALA A 370 ? 0.8819 0.5275 1.0601 -0.0065 -0.0839 -0.1196 1587 ALA A N     
2832 C  CA    . ALA A 370 ? 0.7887 0.4534 0.9492 -0.0008 -0.0790 -0.1155 1587 ALA A CA    
2833 C  C     . ALA A 370 ? 0.8753 0.5465 1.0249 0.0078  -0.0805 -0.1317 1587 ALA A C     
2834 O  O     . ALA A 370 ? 0.8805 0.5385 1.0354 0.0140  -0.0828 -0.1406 1587 ALA A O     
2835 C  CB    . ALA A 370 ? 0.7104 0.3713 0.8698 0.0034  -0.0733 -0.0988 1587 ALA A CB    
2836 N  N     . VAL A 371 ? 0.8817 0.5736 1.0163 0.0085  -0.0789 -0.1353 1588 VAL A N     
2837 C  CA    . VAL A 371 ? 0.8416 0.5433 0.9640 0.0160  -0.0793 -0.1498 1588 VAL A CA    
2838 C  C     . VAL A 371 ? 0.8045 0.5212 0.9130 0.0215  -0.0730 -0.1417 1588 VAL A C     
2839 O  O     . VAL A 371 ? 0.8423 0.5704 0.9448 0.0173  -0.0698 -0.1304 1588 VAL A O     
2840 C  CB    . VAL A 371 ? 0.7794 0.4929 0.8955 0.0116  -0.0835 -0.1624 1588 VAL A CB    
2841 C  CG1   . VAL A 371 ? 0.8387 0.5594 0.9440 0.0197  -0.0843 -0.1790 1588 VAL A CG1   
2842 C  CG2   . VAL A 371 ? 0.7233 0.4246 0.8541 0.0036  -0.0898 -0.1675 1588 VAL A CG2   
2843 N  N     . ARG A 372 ? 0.8206 0.5380 0.9246 0.0309  -0.0714 -0.1480 1589 ARG A N     
2844 C  CA    . ARG A 372 ? 0.9155 0.6470 1.0079 0.0363  -0.0655 -0.1410 1589 ARG A CA    
2845 C  C     . ARG A 372 ? 0.9119 0.6636 0.9889 0.0369  -0.0642 -0.1494 1589 ARG A C     
2846 O  O     . ARG A 372 ? 0.9381 0.6917 1.0123 0.0385  -0.0673 -0.1647 1589 ARG A O     
2847 C  CB    . ARG A 372 ? 1.0404 0.7646 1.1361 0.0464  -0.0642 -0.1433 1589 ARG A CB    
2848 C  CG    . ARG A 372 ? 1.0223 0.7276 1.1311 0.0469  -0.0648 -0.1322 1589 ARG A CG    
2849 C  CD    . ARG A 372 ? 0.9443 0.6398 1.0584 0.0573  -0.0654 -0.1378 1589 ARG A CD    
2850 N  NE    . ARG A 372 ? 0.8259 0.5379 0.9291 0.0653  -0.0616 -0.1415 1589 ARG A NE    
2851 C  CZ    . ARG A 372 ? 0.8064 0.5153 0.9124 0.0748  -0.0603 -0.1404 1589 ARG A CZ    
2852 N  NH1   . ARG A 372 ? 0.8221 0.5109 0.9405 0.0778  -0.0627 -0.1353 1589 ARG A NH1   
2853 N  NH2   . ARG A 372 ? 0.7917 0.5176 0.8888 0.0813  -0.0568 -0.1443 1589 ARG A NH2   
2854 N  N     . ARG A 373 ? 0.7798 0.5462 0.8465 0.0357  -0.0595 -0.1393 1590 ARG A N     
2855 C  CA    . ARG A 373 ? 0.7133 0.4985 0.7651 0.0360  -0.0577 -0.1455 1590 ARG A CA    
2856 C  C     . ARG A 373 ? 0.7524 0.5449 0.7979 0.0450  -0.0550 -0.1548 1590 ARG A C     
2857 O  O     . ARG A 373 ? 0.7895 0.5940 0.8247 0.0462  -0.0548 -0.1654 1590 ARG A O     
2858 C  CB    . ARG A 373 ? 0.6835 0.4811 0.7270 0.0316  -0.0537 -0.1321 1590 ARG A CB    
2859 C  CG    . ARG A 373 ? 0.6119 0.4284 0.6396 0.0317  -0.0513 -0.1362 1590 ARG A CG    
2860 C  CD    . ARG A 373 ? 0.7181 0.5379 0.7414 0.0291  -0.0559 -0.1488 1590 ARG A CD    
2861 N  NE    . ARG A 373 ? 0.8335 0.6712 0.8409 0.0291  -0.0534 -0.1513 1590 ARG A NE    
2862 C  CZ    . ARG A 373 ? 0.7840 0.6316 0.7824 0.0349  -0.0503 -0.1592 1590 ARG A CZ    
2863 N  NH1   . ARG A 373 ? 0.7165 0.5582 0.7208 0.0418  -0.0496 -0.1663 1590 ARG A NH1   
2864 N  NH2   . ARG A 373 ? 0.7266 0.5902 0.7104 0.0340  -0.0477 -0.1598 1590 ARG A NH2   
2865 N  N     . ASP A 374 ? 0.8164 0.6024 0.8681 0.0515  -0.0530 -0.1515 1591 ASP A N     
2866 C  CA    . ASP A 374 ? 0.8228 0.6178 0.8694 0.0603  -0.0502 -0.1603 1591 ASP A CA    
2867 C  C     . ASP A 374 ? 0.8749 0.6632 0.9254 0.0653  -0.0539 -0.1779 1591 ASP A C     
2868 O  O     . ASP A 374 ? 1.0291 0.8307 1.0704 0.0690  -0.0522 -0.1892 1591 ASP A O     
2869 C  CB    . ASP A 374 ? 0.8260 0.6188 0.8775 0.0662  -0.0470 -0.1509 1591 ASP A CB    
2870 C  CG    . ASP A 374 ? 0.7832 0.5546 0.8492 0.0684  -0.0504 -0.1473 1591 ASP A CG    
2871 O  OD1   . ASP A 374 ? 0.7906 0.5483 0.8641 0.0637  -0.0548 -0.1499 1591 ASP A OD1   
2872 O  OD2   . ASP A 374 ? 0.7166 0.4853 0.7869 0.0746  -0.0486 -0.1411 1591 ASP A OD2   
2873 N  N     . ASN A 375 ? 0.7941 0.5623 0.8580 0.0656  -0.0588 -0.1812 1592 ASN A N     
2874 C  CA    . ASN A 375 ? 0.7651 0.5269 0.8323 0.0697  -0.0628 -0.1994 1592 ASN A CA    
2875 C  C     . ASN A 375 ? 0.9358 0.6918 1.0048 0.0621  -0.0684 -0.2065 1592 ASN A C     
2876 O  O     . ASN A 375 ? 0.9496 0.7030 1.0190 0.0649  -0.0720 -0.2231 1592 ASN A O     
2877 C  CB    . ASN A 375 ? 0.6582 0.3999 0.7402 0.0763  -0.0656 -0.2027 1592 ASN A CB    
2878 C  CG    . ASN A 375 ? 0.7268 0.4671 0.8123 0.0818  -0.0620 -0.1910 1592 ASN A CG    
2879 O  OD1   . ASN A 375 ? 0.8125 0.5446 0.9033 0.0775  -0.0617 -0.1757 1592 ASN A OD1   
2880 N  ND2   . ASN A 375 ? 0.8038 0.5520 0.8873 0.0918  -0.0594 -0.1982 1592 ASN A ND2   
2881 N  N     . GLY A 376 ? 1.0279 0.7820 1.0985 0.0529  -0.0695 -0.1950 1593 GLY A N     
2882 C  CA    . GLY A 376 ? 1.0576 0.8027 1.1346 0.0460  -0.0757 -0.2016 1593 GLY A CA    
2883 C  C     . GLY A 376 ? 0.9020 0.6233 0.9965 0.0469  -0.0802 -0.2053 1593 GLY A C     
2884 O  O     . GLY A 376 ? 0.9266 0.6393 1.0278 0.0426  -0.0861 -0.2151 1593 GLY A O     
2885 N  N     . ALA A 377 ? 0.7606 0.4712 0.8627 0.0526  -0.0779 -0.1977 1594 ALA A N     
2886 C  CA    . ALA A 377 ? 0.7474 0.4338 0.8664 0.0539  -0.0819 -0.1993 1594 ALA A CA    
2887 C  C     . ALA A 377 ? 0.8087 0.4837 0.9381 0.0436  -0.0837 -0.1863 1594 ALA A C     
2888 O  O     . ALA A 377 ? 0.7360 0.4185 0.8617 0.0394  -0.0797 -0.1703 1594 ALA A O     
2889 C  CB    . ALA A 377 ? 0.7560 0.4348 0.8794 0.0636  -0.0790 -0.1940 1594 ALA A CB    
2890 N  N     . LYS A 378 ? 0.9031 0.5608 1.0459 0.0395  -0.0895 -0.1939 1595 LYS A N     
2891 C  CA    . LYS A 378 ? 0.9589 0.6040 1.1146 0.0294  -0.0917 -0.1833 1595 LYS A CA    
2892 C  C     . LYS A 378 ? 0.8957 0.5173 1.0665 0.0316  -0.0918 -0.1744 1595 LYS A C     
2893 O  O     . LYS A 378 ? 1.0039 0.6142 1.1786 0.0405  -0.0929 -0.1814 1595 LYS A O     
2894 C  CB    . LYS A 378 ? 1.1209 0.7620 1.2832 0.0219  -0.0985 -0.1971 1595 LYS A CB    
2895 N  N     . GLN A 379 ? 0.9247 0.5395 1.1040 0.0233  -0.0907 -0.1585 1596 GLN A N     
2896 C  CA    . GLN A 379 ? 1.0142 0.6070 1.2073 0.0238  -0.0904 -0.1468 1596 GLN A CA    
2897 C  C     . GLN A 379 ? 1.0647 0.6520 1.2682 0.0115  -0.0902 -0.1335 1596 GLN A C     
2898 O  O     . GLN A 379 ? 1.0351 0.6384 1.2312 0.0062  -0.0865 -0.1231 1596 GLN A O     
2899 C  CB    . GLN A 379 ? 1.0447 0.6414 1.2300 0.0326  -0.0848 -0.1342 1596 GLN A CB    
2900 C  CG    . GLN A 379 ? 1.0761 0.6566 1.2713 0.0314  -0.0828 -0.1156 1596 GLN A CG    
2901 C  CD    . GLN A 379 ? 1.1888 0.7798 1.3731 0.0387  -0.0772 -0.1026 1596 GLN A CD    
2902 O  OE1   . GLN A 379 ? 1.2298 0.8405 1.4002 0.0435  -0.0748 -0.1073 1596 GLN A OE1   
2903 N  NE2   . GLN A 379 ? 1.2586 0.8368 1.4490 0.0394  -0.0753 -0.0862 1596 GLN A NE2   
2904 N  N     . THR A 380 ? 1.0194 0.5841 1.2405 0.0069  -0.0942 -0.1342 1597 THR A N     
2905 C  CA    . THR A 380 ? 0.8462 0.4052 1.0795 -0.0055 -0.0942 -0.1231 1597 THR A CA    
2906 C  C     . THR A 380 ? 0.8496 0.3984 1.0881 -0.0062 -0.0892 -0.1011 1597 THR A C     
2907 O  O     . THR A 380 ? 0.8430 0.3775 1.0837 0.0018  -0.0885 -0.0967 1597 THR A O     
2908 C  CB    . THR A 380 ? 0.7735 0.3149 1.0240 -0.0120 -0.1012 -0.1357 1597 THR A CB    
2909 O  OG1   . THR A 380 ? 0.7732 0.3259 1.0164 -0.0100 -0.1058 -0.1565 1597 THR A OG1   
2910 C  CG2   . THR A 380 ? 0.7716 0.3128 1.0342 -0.0258 -0.1012 -0.1259 1597 THR A CG2   
2911 N  N     . ILE A 381 ? 0.8668 0.4244 1.1067 -0.0154 -0.0858 -0.0873 1598 ILE A N     
2912 C  CA    . ILE A 381 ? 0.8596 0.4137 1.1002 -0.0161 -0.0799 -0.0656 1598 ILE A CA    
2913 C  C     . ILE A 381 ? 0.9507 0.4999 1.2058 -0.0293 -0.0792 -0.0553 1598 ILE A C     
2914 O  O     . ILE A 381 ? 1.0190 0.5825 1.2747 -0.0374 -0.0800 -0.0590 1598 ILE A O     
2915 C  CB    . ILE A 381 ? 0.7570 0.3343 0.9789 -0.0113 -0.0742 -0.0576 1598 ILE A CB    
2916 C  CG1   . ILE A 381 ? 0.7062 0.2906 0.9149 0.0007  -0.0751 -0.0699 1598 ILE A CG1   
2917 C  CG2   . ILE A 381 ? 0.7448 0.3191 0.9663 -0.0114 -0.0685 -0.0364 1598 ILE A CG2   
2918 C  CD1   . ILE A 381 ? 0.6883 0.2880 0.8813 0.0077  -0.0697 -0.0605 1598 ILE A CD1   
2919 N  N     . LYS A 382 ? 0.9676 0.4963 1.2352 -0.0315 -0.0780 -0.0427 1599 LYS A N     
2920 C  CA    . LYS A 382 ? 1.0148 0.5387 1.2967 -0.0440 -0.0760 -0.0302 1599 LYS A CA    
2921 C  C     . LYS A 382 ? 0.9307 0.4732 1.2025 -0.0460 -0.0685 -0.0126 1599 LYS A C     
2922 O  O     . LYS A 382 ? 0.9077 0.4595 1.1640 -0.0371 -0.0647 -0.0064 1599 LYS A O     
2923 C  CB    . LYS A 382 ? 1.0327 0.5332 1.3261 -0.0451 -0.0756 -0.0215 1599 LYS A CB    
2924 N  N     . ARG A 383 ? 0.8440 0.3931 1.1253 -0.0578 -0.0665 -0.0053 1600 ARG A N     
2925 C  CA    . ARG A 383 ? 0.9305 0.5010 1.2015 -0.0597 -0.0599 0.0075  1600 ARG A CA    
2926 C  C     . ARG A 383 ? 1.0168 0.5823 1.2846 -0.0572 -0.0531 0.0288  1600 ARG A C     
2927 O  O     . ARG A 383 ? 1.1187 0.7020 1.3739 -0.0554 -0.0476 0.0383  1600 ARG A O     
2928 C  CB    . ARG A 383 ? 0.8505 0.4324 1.1325 -0.0722 -0.0601 0.0070  1600 ARG A CB    
2929 C  CG    . ARG A 383 ? 1.0165 0.6091 1.2962 -0.0728 -0.0666 -0.0135 1600 ARG A CG    
2930 C  CD    . ARG A 383 ? 1.1264 0.7396 1.4088 -0.0815 -0.0662 -0.0141 1600 ARG A CD    
2931 N  NE    . ARG A 383 ? 1.0964 0.7254 1.3708 -0.0819 -0.0585 0.0021  1600 ARG A NE    
2932 C  CZ    . ARG A 383 ? 1.0803 0.7292 1.3547 -0.0876 -0.0572 0.0033  1600 ARG A CZ    
2933 N  NH1   . ARG A 383 ? 1.0328 0.6885 1.3145 -0.0932 -0.0632 -0.0102 1600 ARG A NH1   
2934 N  NH2   . ARG A 383 ? 1.1116 0.7738 1.3788 -0.0872 -0.0500 0.0177  1600 ARG A NH2   
2935 N  N     . ALA A 384 ? 1.0407 0.5828 1.3185 -0.0567 -0.0534 0.0363  1601 ALA A N     
2936 C  CA    . ALA A 384 ? 1.0930 0.6307 1.3653 -0.0530 -0.0472 0.0565  1601 ALA A CA    
2937 C  C     . ALA A 384 ? 1.1831 0.7272 1.4365 -0.0390 -0.0466 0.0556  1601 ALA A C     
2938 O  O     . ALA A 384 ? 1.2764 0.8347 1.5165 -0.0355 -0.0411 0.0672  1601 ALA A O     
2939 C  CB    . ALA A 384 ? 1.1526 0.6665 1.4368 -0.0554 -0.0474 0.0647  1601 ALA A CB    
2940 N  N     . GLN A 385 ? 1.1609 0.6959 1.4129 -0.0310 -0.0522 0.0407  1602 GLN A N     
2941 C  CA    . GLN A 385 ? 1.1016 0.6409 1.3384 -0.0175 -0.0523 0.0382  1602 GLN A CA    
2942 C  C     . GLN A 385 ? 0.8702 0.4355 1.0910 -0.0142 -0.0514 0.0290  1602 GLN A C     
2943 O  O     . GLN A 385 ? 0.7027 0.2744 0.9109 -0.0036 -0.0513 0.0259  1602 GLN A O     
2944 C  CB    . GLN A 385 ? 1.1102 0.6302 1.3534 -0.0104 -0.0586 0.0248  1602 GLN A CB    
2945 C  CG    . GLN A 385 ? 1.2279 0.7556 1.4709 -0.0110 -0.0637 0.0024  1602 GLN A CG    
2946 C  CD    . GLN A 385 ? 1.2967 0.8046 1.5490 -0.0061 -0.0702 -0.0129 1602 GLN A CD    
2947 O  OE1   . GLN A 385 ? 1.2971 0.8098 1.5410 0.0036  -0.0726 -0.0262 1602 GLN A OE1   
2948 N  NE2   . GLN A 385 ? 1.3132 0.8015 1.5820 -0.0132 -0.0726 -0.0119 1602 GLN A NE2   
2949 N  N     . ALA A 386 ? 0.7182 0.2983 0.9398 -0.0230 -0.0508 0.0250  1603 ALA A N     
2950 C  CA    . ALA A 386 ? 0.7158 0.3197 0.9228 -0.0206 -0.0499 0.0170  1603 ALA A CA    
2951 C  C     . ALA A 386 ? 0.8072 0.4241 0.9984 -0.0136 -0.0446 0.0284  1603 ALA A C     
2952 O  O     . ALA A 386 ? 0.6462 0.2746 0.8243 -0.0057 -0.0449 0.0210  1603 ALA A O     
2953 C  CB    . ALA A 386 ? 0.6846 0.3012 0.8967 -0.0316 -0.0496 0.0150  1603 ALA A CB    
2954 N  N     . THR A 387 ? 0.9857 0.6005 1.1784 -0.0164 -0.0396 0.0465  1604 THR A N     
2955 C  CA    . THR A 387 ? 0.8854 0.5121 1.0638 -0.0106 -0.0346 0.0584  1604 THR A CA    
2956 C  C     . THR A 387 ? 0.9089 0.5304 1.0790 0.0017  -0.0361 0.0568  1604 THR A C     
2957 O  O     . THR A 387 ? 0.8810 0.5165 1.0372 0.0079  -0.0335 0.0602  1604 THR A O     
2958 C  CB    . THR A 387 ? 1.0298 0.6508 1.2132 -0.0154 -0.0295 0.0780  1604 THR A CB    
2959 O  OG1   . THR A 387 ? 1.2616 0.8795 1.4595 -0.0274 -0.0292 0.0793  1604 THR A OG1   
2960 C  CG2   . THR A 387 ? 0.9797 0.6187 1.1487 -0.0128 -0.0237 0.0891  1604 THR A CG2   
2961 N  N     . VAL A 388 ? 0.9555 0.5580 1.1344 0.0055  -0.0407 0.0505  1605 VAL A N     
2962 C  CA    . VAL A 388 ? 0.9927 0.5898 1.1657 0.0178  -0.0427 0.0479  1605 VAL A CA    
2963 C  C     . VAL A 388 ? 0.9492 0.5514 1.1193 0.0230  -0.0469 0.0279  1605 VAL A C     
2964 O  O     . VAL A 388 ? 1.0250 0.6400 1.1833 0.0311  -0.0464 0.0235  1605 VAL A O     
2965 C  CB    . VAL A 388 ? 0.9799 0.5512 1.1643 0.0203  -0.0447 0.0558  1605 VAL A CB    
2966 C  CG1   . VAL A 388 ? 0.7139 0.2776 0.8964 0.0327  -0.0488 0.0469  1605 VAL A CG1   
2967 C  CG2   . VAL A 388 ? 1.0282 0.5968 1.2102 0.0197  -0.0400 0.0775  1605 VAL A CG2   
2968 N  N     . GLU A 389 ? 0.8436 0.4369 1.0243 0.0178  -0.0510 0.0154  1606 GLU A N     
2969 C  CA    . GLU A 389 ? 0.7757 0.3716 0.9544 0.0230  -0.0552 -0.0041 1606 GLU A CA    
2970 C  C     . GLU A 389 ? 0.8415 0.4625 1.0059 0.0237  -0.0533 -0.0112 1606 GLU A C     
2971 O  O     . GLU A 389 ? 0.7440 0.3723 0.9009 0.0316  -0.0545 -0.0222 1606 GLU A O     
2972 C  CB    . GLU A 389 ? 0.7077 0.2894 0.9006 0.0165  -0.0601 -0.0158 1606 GLU A CB    
2973 C  CG    . GLU A 389 ? 0.7232 0.2771 0.9313 0.0173  -0.0629 -0.0114 1606 GLU A CG    
2974 C  CD    . GLU A 389 ? 0.9129 0.4570 1.1188 0.0306  -0.0645 -0.0132 1606 GLU A CD    
2975 O  OE1   . GLU A 389 ? 0.9794 0.5272 1.1819 0.0378  -0.0675 -0.0295 1606 GLU A OE1   
2976 O  OE2   . GLU A 389 ? 0.9734 0.5066 1.1812 0.0340  -0.0628 0.0020  1606 GLU A OE2   
2977 N  N     . MET A 390 ? 1.0382 0.6725 1.1992 0.0153  -0.0503 -0.0056 1607 MET A N     
2978 C  CA    . MET A 390 ? 1.0028 0.6593 1.1505 0.0158  -0.0489 -0.0126 1607 MET A CA    
2979 C  C     . MET A 390 ? 1.0582 0.7267 1.1925 0.0248  -0.0459 -0.0090 1607 MET A C     
2980 O  O     . MET A 390 ? 1.1844 0.8628 1.3111 0.0301  -0.0469 -0.0208 1607 MET A O     
2981 C  CB    . MET A 390 ? 0.9024 0.5703 1.0497 0.0059  -0.0464 -0.0065 1607 MET A CB    
2982 C  CG    . MET A 390 ? 0.8107 0.4977 0.9474 0.0052  -0.0465 -0.0164 1607 MET A CG    
2983 S  SD    . MET A 390 ? 0.7926 0.4770 0.9287 0.0102  -0.0519 -0.0374 1607 MET A SD    
2984 C  CE    . MET A 390 ? 0.6090 0.2910 0.7552 -0.0003 -0.0565 -0.0466 1607 MET A CE    
2985 N  N     . PRO A 391 ? 1.0090 0.6781 1.1399 0.0269  -0.0422 0.0064  1608 PRO A N     
2986 C  CA    . PRO A 391 ? 1.0821 0.7635 1.2007 0.0356  -0.0401 0.0084  1608 PRO A CA    
2987 C  C     . PRO A 391 ? 1.1071 0.7827 1.2264 0.0459  -0.0430 -0.0006 1608 PRO A C     
2988 O  O     . PRO A 391 ? 1.2165 0.9061 1.3264 0.0519  -0.0422 -0.0066 1608 PRO A O     
2989 C  CB    . PRO A 391 ? 1.0063 0.6860 1.1233 0.0355  -0.0365 0.0267  1608 PRO A CB    
2990 C  CG    . PRO A 391 ? 0.9188 0.5940 1.0435 0.0247  -0.0351 0.0336  1608 PRO A CG    
2991 C  CD    . PRO A 391 ? 0.8659 0.5278 1.0027 0.0209  -0.0395 0.0225  1608 PRO A CD    
2992 N  N     . LYS A 392 ? 0.8944 0.5495 1.0251 0.0483  -0.0463 -0.0012 1609 LYS A N     
2993 C  CA    . LYS A 392 ? 0.7247 0.3736 0.8575 0.0584  -0.0495 -0.0117 1609 LYS A CA    
2994 C  C     . LYS A 392 ? 0.6315 0.2911 0.7606 0.0589  -0.0511 -0.0302 1609 LYS A C     
2995 O  O     . LYS A 392 ? 0.6480 0.3159 0.7720 0.0673  -0.0514 -0.0386 1609 LYS A O     
2996 C  CB    . LYS A 392 ? 0.6634 0.2867 0.8104 0.0597  -0.0532 -0.0107 1609 LYS A CB    
2997 N  N     . LEU A 393 ? 0.6537 0.3126 0.7863 0.0502  -0.0525 -0.0370 1610 LEU A N     
2998 C  CA    . LEU A 393 ? 0.7062 0.3762 0.8339 0.0503  -0.0540 -0.0539 1610 LEU A CA    
2999 C  C     . LEU A 393 ? 0.6517 0.3449 0.7648 0.0515  -0.0501 -0.0538 1610 LEU A C     
3000 O  O     . LEU A 393 ? 0.7503 0.4543 0.8571 0.0562  -0.0503 -0.0658 1610 LEU A O     
3001 C  CB    . LEU A 393 ? 0.8691 0.5350 1.0028 0.0404  -0.0566 -0.0603 1610 LEU A CB    
3002 C  CG    . LEU A 393 ? 0.8407 0.5126 0.9715 0.0416  -0.0596 -0.0797 1610 LEU A CG    
3003 C  CD1   . LEU A 393 ? 0.8542 0.5110 0.9931 0.0490  -0.0636 -0.0917 1610 LEU A CD1   
3004 C  CD2   . LEU A 393 ? 0.7597 0.4340 0.8929 0.0314  -0.0618 -0.0843 1610 LEU A CD2   
3005 N  N     . LEU A 394 ? 0.6828 0.3845 0.7907 0.0468  -0.0466 -0.0407 1611 LEU A N     
3006 C  CA    . LEU A 394 ? 0.6082 0.3308 0.7029 0.0478  -0.0431 -0.0402 1611 LEU A CA    
3007 C  C     . LEU A 394 ? 0.7220 0.4503 0.8123 0.0580  -0.0421 -0.0414 1611 LEU A C     
3008 O  O     . LEU A 394 ? 0.9243 0.6670 1.0068 0.0612  -0.0409 -0.0502 1611 LEU A O     
3009 C  CB    . LEU A 394 ? 0.5677 0.2968 0.6586 0.0415  -0.0396 -0.0260 1611 LEU A CB    
3010 C  CG    . LEU A 394 ? 0.6415 0.3700 0.7362 0.0315  -0.0407 -0.0276 1611 LEU A CG    
3011 C  CD1   . LEU A 394 ? 0.7224 0.4578 0.8146 0.0249  -0.0373 -0.0149 1611 LEU A CD1   
3012 C  CD2   . LEU A 394 ? 0.6258 0.3651 0.7146 0.0303  -0.0422 -0.0418 1611 LEU A CD2   
3013 N  N     . GLU A 395 ? 0.6083 0.3253 0.7039 0.0634  -0.0426 -0.0329 1612 GLU A N     
3014 C  CA    . GLU A 395 ? 0.6282 0.3509 0.7209 0.0738  -0.0424 -0.0345 1612 GLU A CA    
3015 C  C     . GLU A 395 ? 0.6376 0.3590 0.7335 0.0800  -0.0449 -0.0509 1612 GLU A C     
3016 O  O     . GLU A 395 ? 0.7504 0.4865 0.8404 0.0856  -0.0435 -0.0579 1612 GLU A O     
3017 C  CB    . GLU A 395 ? 0.5922 0.3024 0.6898 0.0787  -0.0431 -0.0215 1612 GLU A CB    
3018 C  CG    . GLU A 395 ? 0.6291 0.3485 0.7191 0.0765  -0.0397 -0.0068 1612 GLU A CG    
3019 C  CD    . GLU A 395 ? 0.6423 0.3463 0.7378 0.0752  -0.0399 0.0082  1612 GLU A CD    
3020 N  N     . THR A 396 ? 0.6125 0.3167 0.7182 0.0790  -0.0485 -0.0574 1613 THR A N     
3021 C  CA    . THR A 396 ? 0.8072 0.5084 0.9168 0.0848  -0.0512 -0.0742 1613 THR A CA    
3022 C  C     . THR A 396 ? 0.8406 0.5612 0.9404 0.0830  -0.0493 -0.0862 1613 THR A C     
3023 O  O     . THR A 396 ? 0.7785 0.5085 0.8756 0.0902  -0.0488 -0.0969 1613 THR A O     
3024 C  CB    . THR A 396 ? 0.6776 0.3574 0.7989 0.0810  -0.0555 -0.0789 1613 THR A CB    
3025 O  OG1   . THR A 396 ? 0.7037 0.3642 0.8346 0.0844  -0.0572 -0.0686 1613 THR A OG1   
3026 C  CG2   . THR A 396 ? 0.6471 0.3245 0.7715 0.0856  -0.0584 -0.0980 1613 THR A CG2   
3027 N  N     . ILE A 397 ? 0.8096 0.5369 0.9041 0.0733  -0.0482 -0.0840 1614 ILE A N     
3028 C  CA    . ILE A 397 ? 0.8328 0.5776 0.9173 0.0707  -0.0465 -0.0937 1614 ILE A CA    
3029 C  C     . ILE A 397 ? 0.9096 0.6734 0.9843 0.0745  -0.0422 -0.0903 1614 ILE A C     
3030 O  O     . ILE A 397 ? 0.9749 0.7520 1.0437 0.0782  -0.0407 -0.1007 1614 ILE A O     
3031 C  CB    . ILE A 397 ? 0.6791 0.4251 0.7613 0.0597  -0.0469 -0.0905 1614 ILE A CB    
3032 C  CG1   . ILE A 397 ? 0.6018 0.3327 0.6933 0.0564  -0.0517 -0.0994 1614 ILE A CG1   
3033 C  CG2   . ILE A 397 ? 0.7128 0.4790 0.7822 0.0565  -0.0442 -0.0945 1614 ILE A CG2   
3034 C  CD1   . ILE A 397 ? 0.7030 0.4375 0.7925 0.0462  -0.0528 -0.0997 1614 ILE A CD1   
3035 N  N     . HIS A 398 ? 0.7543 0.5202 0.8272 0.0734  -0.0400 -0.0759 1615 HIS A N     
3036 C  CA    . HIS A 398 ? 0.7939 0.5772 0.8589 0.0769  -0.0364 -0.0729 1615 HIS A CA    
3037 C  C     . HIS A 398 ? 0.8816 0.6689 0.9491 0.0873  -0.0367 -0.0817 1615 HIS A C     
3038 O  O     . HIS A 398 ? 0.9145 0.7183 0.9758 0.0894  -0.0342 -0.0894 1615 HIS A O     
3039 C  CB    . HIS A 398 ? 0.6913 0.4738 0.7555 0.0761  -0.0350 -0.0570 1615 HIS A CB    
3040 C  CG    . HIS A 398 ? 0.8218 0.6207 0.8796 0.0806  -0.0321 -0.0546 1615 HIS A CG    
3041 N  ND1   . HIS A 398 ? 0.9019 0.7045 0.9627 0.0900  -0.0326 -0.0594 1615 HIS A ND1   
3042 C  CD2   . HIS A 398 ? 0.9067 0.7200 0.9560 0.0767  -0.0289 -0.0489 1615 HIS A CD2   
3043 C  CE1   . HIS A 398 ? 0.9135 0.7325 0.9682 0.0915  -0.0299 -0.0565 1615 HIS A CE1   
3044 N  NE2   . HIS A 398 ? 0.9175 0.7425 0.9650 0.0834  -0.0277 -0.0501 1615 HIS A NE2   
3045 N  N     . THR A 399 ? 0.7882 0.5611 0.8650 0.0940  -0.0394 -0.0796 1616 THR A N     
3046 C  CA    . THR A 399 ? 0.8474 0.6247 0.9276 0.1047  -0.0398 -0.0871 1616 THR A CA    
3047 C  C     . THR A 399 ? 0.7653 0.5452 0.8463 0.1072  -0.0405 -0.1045 1616 THR A C     
3048 O  O     . THR A 399 ? 0.6531 0.4461 0.7328 0.1139  -0.0388 -0.1130 1616 THR A O     
3049 C  CB    . THR A 399 ? 0.8516 0.6129 0.9414 0.1123  -0.0429 -0.0803 1616 THR A CB    
3050 O  OG1   . THR A 399 ? 0.7369 0.4768 0.8336 0.1078  -0.0459 -0.0762 1616 THR A OG1   
3051 C  CG2   . THR A 399 ? 0.9335 0.7019 1.0197 0.1139  -0.0414 -0.0658 1616 THR A CG2   
3052 N  N     . SER A 400 ? 0.7979 0.5668 0.8810 0.1020  -0.0428 -0.1105 1617 SER A N     
3053 C  CA    . SER A 400 ? 0.8756 0.6499 0.9573 0.1047  -0.0431 -0.1277 1617 SER A CA    
3054 C  C     . SER A 400 ? 0.8257 0.6236 0.8950 0.1014  -0.0386 -0.1316 1617 SER A C     
3055 O  O     . SER A 400 ? 0.8642 0.6745 0.9311 0.1072  -0.0367 -0.1429 1617 SER A O     
3056 C  CB    . SER A 400 ? 0.9060 0.6644 0.9924 0.0994  -0.0471 -0.1342 1617 SER A CB    
3057 O  OG    . SER A 400 ? 0.9718 0.7403 1.0516 0.0978  -0.0468 -0.1485 1617 SER A OG    
3058 N  N     . MET A 401 ? 0.7205 0.5258 0.7822 0.0932  -0.0363 -0.1211 1618 MET A N     
3059 C  CA    . MET A 401 ? 0.6914 0.5179 0.7416 0.0899  -0.0319 -0.1228 1618 MET A CA    
3060 C  C     . MET A 401 ? 0.7848 0.6259 0.8342 0.0968  -0.0285 -0.1223 1618 MET A C     
3061 O  O     . MET A 401 ? 0.6779 0.5343 0.7231 0.0997  -0.0256 -0.1319 1618 MET A O     
3062 C  CB    . MET A 401 ? 0.6110 0.4402 0.6547 0.0804  -0.0306 -0.1109 1618 MET A CB    
3063 C  CG    . MET A 401 ? 0.7428 0.5667 0.7838 0.0725  -0.0328 -0.1139 1618 MET A CG    
3064 S  SD    . MET A 401 ? 0.8304 0.6598 0.8642 0.0625  -0.0309 -0.1001 1618 MET A SD    
3065 C  CE    . MET A 401 ? 0.8214 0.6359 0.8603 0.0552  -0.0354 -0.1005 1618 MET A CE    
3066 N  N     . TYR A 402 ? 0.8630 0.7010 0.9165 0.0992  -0.0288 -0.1108 1619 TYR A N     
3067 C  CA    . TYR A 402 ? 0.7879 0.6401 0.8419 0.1057  -0.0263 -0.1099 1619 TYR A CA    
3068 C  C     . TYR A 402 ? 0.8371 0.6917 0.8976 0.1157  -0.0269 -0.1228 1619 TYR A C     
3069 O  O     . TYR A 402 ? 0.8168 0.6896 0.8750 0.1191  -0.0234 -0.1290 1619 TYR A O     
3070 C  CB    . TYR A 402 ? 0.8218 0.6682 0.8799 0.1080  -0.0277 -0.0965 1619 TYR A CB    
3071 C  CG    . TYR A 402 ? 0.9659 0.8293 1.0243 0.1141  -0.0255 -0.0961 1619 TYR A CG    
3072 C  CD1   . TYR A 402 ? 0.9806 0.8588 1.0320 0.1093  -0.0224 -0.0894 1619 TYR A CD1   
3073 C  CD2   . TYR A 402 ? 1.0694 0.9349 1.1358 0.1248  -0.0267 -0.1034 1619 TYR A CD2   
3074 C  CE1   . TYR A 402 ? 0.8897 0.7843 0.9424 0.1141  -0.0206 -0.0898 1619 TYR A CE1   
3075 C  CE2   . TYR A 402 ? 1.0690 0.9520 1.1367 0.1301  -0.0249 -0.1037 1619 TYR A CE2   
3076 C  CZ    . TYR A 402 ? 0.8836 0.7812 0.9445 0.1244  -0.0219 -0.0968 1619 TYR A CZ    
3077 O  OH    . TYR A 402 ? 0.9109 0.8262 0.9741 0.1291  -0.0203 -0.0975 1619 TYR A OH    
3078 N  N     . GLU A 403 ? 0.7802 0.6163 0.8497 0.1209  -0.0311 -0.1265 1620 GLU A N     
3079 C  CA    . GLU A 403 ? 0.6600 0.4968 0.7369 0.1316  -0.0321 -0.1388 1620 GLU A CA    
3080 C  C     . GLU A 403 ? 0.6410 0.4910 0.7123 0.1313  -0.0293 -0.1539 1620 GLU A C     
3081 O  O     . GLU A 403 ? 0.5780 0.4427 0.6508 0.1385  -0.0267 -0.1625 1620 GLU A O     
3082 C  CB    . GLU A 403 ? 0.5939 0.4060 0.6815 0.1362  -0.0375 -0.1397 1620 GLU A CB    
3083 C  CG    . GLU A 403 ? 0.5943 0.3938 0.6867 0.1371  -0.0399 -0.1238 1620 GLU A CG    
3084 C  CD    . GLU A 403 ? 0.8821 0.6695 0.9860 0.1487  -0.0436 -0.1246 1620 GLU A CD    
3085 O  OE1   . GLU A 403 ? 0.8969 0.6847 1.0026 0.1523  -0.0442 -0.1129 1620 GLU A OE1   
3086 O  OE2   . GLU A 403 ? 0.9472 0.7248 1.0580 0.1545  -0.0460 -0.1368 1620 GLU A OE2   
3087 N  N     . ARG A 404 ? 0.5774 0.4234 0.6423 0.1233  -0.0297 -0.1575 1621 ARG A N     
3088 C  CA    . ARG A 404 ? 0.5980 0.4579 0.6555 0.1227  -0.0269 -0.1711 1621 ARG A CA    
3089 C  C     . ARG A 404 ? 0.7366 0.6210 0.7854 0.1206  -0.0208 -0.1689 1621 ARG A C     
3090 O  O     . ARG A 404 ? 0.9293 0.8295 0.9767 0.1256  -0.0173 -0.1794 1621 ARG A O     
3091 C  CB    . ARG A 404 ? 0.6196 0.4715 0.6709 0.1140  -0.0289 -0.1738 1621 ARG A CB    
3092 C  CG    . ARG A 404 ? 0.6710 0.5322 0.7157 0.1149  -0.0277 -0.1897 1621 ARG A CG    
3093 C  CD    . ARG A 404 ? 0.8063 0.6606 0.8446 0.1057  -0.0305 -0.1910 1621 ARG A CD    
3094 N  NE    . ARG A 404 ? 0.9351 0.7657 0.9832 0.1047  -0.0367 -0.1910 1621 ARG A NE    
3095 C  CZ    . ARG A 404 ? 1.0274 0.8448 1.0799 0.0987  -0.0391 -0.1778 1621 ARG A CZ    
3096 N  NH1   . ARG A 404 ? 1.0817 0.9068 1.1291 0.0935  -0.0362 -0.1636 1621 ARG A NH1   
3097 N  NH2   . ARG A 404 ? 0.9642 0.7604 1.0263 0.0977  -0.0444 -0.1789 1621 ARG A NH2   
3098 N  N     . ALA A 405 ? 0.6087 0.4969 0.6527 0.1134  -0.0193 -0.1553 1622 ALA A N     
3099 C  CA    . ALA A 405 ? 0.6508 0.5609 0.6872 0.1104  -0.0137 -0.1526 1622 ALA A CA    
3100 C  C     . ALA A 405 ? 0.7739 0.6965 0.8173 0.1191  -0.0116 -0.1548 1622 ALA A C     
3101 O  O     . ALA A 405 ? 0.8189 0.7615 0.8586 0.1197  -0.0066 -0.1599 1622 ALA A O     
3102 C  CB    . ALA A 405 ? 0.6266 0.5361 0.6577 0.1017  -0.0132 -0.1378 1622 ALA A CB    
3103 N  N     . GLU A 406 ? 0.8991 0.8104 0.9529 0.1260  -0.0153 -0.1508 1623 GLU A N     
3104 C  CA    . GLU A 406 ? 0.9743 0.8969 1.0359 0.1352  -0.0143 -0.1525 1623 GLU A CA    
3105 C  C     . GLU A 406 ? 0.8867 0.8157 0.9531 0.1440  -0.0132 -0.1685 1623 GLU A C     
3106 O  O     . GLU A 406 ? 0.9223 0.8711 0.9911 0.1486  -0.0093 -0.1736 1623 GLU A O     
3107 C  CB    . GLU A 406 ? 1.0759 0.9837 1.1464 0.1404  -0.0191 -0.1430 1623 GLU A CB    
3108 C  CG    . GLU A 406 ? 1.1993 1.1192 1.2779 0.1498  -0.0189 -0.1433 1623 GLU A CG    
3109 C  CD    . GLU A 406 ? 1.2842 1.1874 1.3714 0.1566  -0.0244 -0.1352 1623 GLU A CD    
3110 O  OE1   . GLU A 406 ? 1.2247 1.1062 1.3123 0.1541  -0.0279 -0.1303 1623 GLU A OE1   
3111 O  OE2   . GLU A 406 ? 1.3617 1.2741 1.4556 0.1645  -0.0252 -0.1335 1623 GLU A OE2   
3112 N  N     . ARG A 407 ? 0.7416 0.6545 0.8105 0.1466  -0.0165 -0.1769 1624 ARG A N     
3113 C  CA    . ARG A 407 ? 0.7242 0.6437 0.7964 0.1547  -0.0153 -0.1934 1624 ARG A CA    
3114 C  C     . ARG A 407 ? 0.8764 0.8186 0.9378 0.1500  -0.0088 -0.2005 1624 ARG A C     
3115 O  O     . ARG A 407 ? 1.0622 1.0215 1.1260 0.1567  -0.0049 -0.2108 1624 ARG A O     
3116 C  CB    . ARG A 407 ? 0.6817 0.5791 0.7572 0.1567  -0.0203 -0.2014 1624 ARG A CB    
3117 N  N     . ASP A 408 ? 0.8340 0.7774 0.8837 0.1388  -0.0073 -0.1945 1625 ASP A N     
3118 C  CA    . ASP A 408 ? 0.8433 0.8078 0.8817 0.1336  -0.0011 -0.1989 1625 ASP A CA    
3119 C  C     . ASP A 408 ? 0.7996 0.7861 0.8391 0.1339  0.0044  -0.1943 1625 ASP A C     
3120 O  O     . ASP A 408 ? 0.7782 0.7848 0.8160 0.1366  0.0099  -0.2029 1625 ASP A O     
3121 C  CB    . ASP A 408 ? 0.8365 0.7958 0.8628 0.1218  -0.0015 -0.1917 1625 ASP A CB    
3122 C  CG    . ASP A 408 ? 0.9916 0.9660 1.0053 0.1177  0.0031  -0.1996 1625 ASP A CG    
3123 O  OD1   . ASP A 408 ? 1.0849 1.0709 1.0990 0.1242  0.0061  -0.2125 1625 ASP A OD1   
3124 O  OD2   . ASP A 408 ? 1.0444 1.0191 1.0475 0.1082  0.0037  -0.1928 1625 ASP A OD2   
3125 N  N     . LEU A 409 ? 0.7102 0.6940 0.7525 0.1308  0.0031  -0.1809 1626 LEU A N     
3126 C  CA    . LEU A 409 ? 0.5282 0.5319 0.5729 0.1307  0.0074  -0.1763 1626 LEU A CA    
3127 C  C     . LEU A 409 ? 0.7419 0.7569 0.7981 0.1424  0.0085  -0.1859 1626 LEU A C     
3128 O  O     . LEU A 409 ? 0.8098 0.8475 0.8662 0.1432  0.0143  -0.1911 1626 LEU A O     
3129 C  CB    . LEU A 409 ? 0.5300 0.5260 0.5768 0.1269  0.0044  -0.1614 1626 LEU A CB    
3130 C  CG    . LEU A 409 ? 0.6986 0.7120 0.7503 0.1275  0.0069  -0.1557 1626 LEU A CG    
3131 C  CD1   . LEU A 409 ? 0.4890 0.5171 0.5314 0.1170  0.0122  -0.1505 1626 LEU A CD1   
3132 C  CD2   . LEU A 409 ? 0.8464 0.8475 0.9040 0.1298  0.0016  -0.1450 1626 LEU A CD2   
3133 N  N     . GLN A 410 ? 0.8150 0.8145 0.8814 0.1516  0.0030  -0.1887 1627 GLN A N     
3134 C  CA    . GLN A 410 ? 0.7754 0.7845 0.8540 0.1639  0.0032  -0.1973 1627 GLN A CA    
3135 C  C     . GLN A 410 ? 0.6737 0.6961 0.7508 0.1682  0.0078  -0.2134 1627 GLN A C     
3136 O  O     . GLN A 410 ? 0.6367 0.6801 0.7203 0.1743  0.0119  -0.2201 1627 GLN A O     
3137 C  CB    . GLN A 410 ? 0.8026 0.7892 0.8918 0.1729  -0.0042 -0.1959 1627 GLN A CB    
3138 C  CG    . GLN A 410 ? 0.9246 0.9068 1.0189 0.1732  -0.0077 -0.1814 1627 GLN A CG    
3139 C  CD    . GLN A 410 ? 1.0940 1.0484 1.1933 0.1769  -0.0149 -0.1749 1627 GLN A CD    
3140 O  OE1   . GLN A 410 ? 1.1632 1.1007 1.2646 0.1801  -0.0178 -0.1820 1627 GLN A OE1   
3141 N  NE2   . GLN A 410 ? 1.1585 1.1081 1.2594 0.1758  -0.0179 -0.1612 1627 GLN A NE2   
3142 N  N     . SER A 411 ? 0.6109 0.6245 0.6788 0.1641  0.0077  -0.2195 1628 SER A N     
3143 C  CA    . SER A 411 ? 0.6603 0.6868 0.7251 0.1682  0.0120  -0.2352 1628 SER A CA    
3144 C  C     . SER A 411 ? 0.7459 0.7977 0.8005 0.1606  0.0202  -0.2347 1628 SER A C     
3145 O  O     . SER A 411 ? 0.6589 0.7281 0.7117 0.1644  0.0256  -0.2468 1628 SER A O     
3146 C  CB    . SER A 411 ? 0.7681 0.7754 0.8268 0.1670  0.0081  -0.2427 1628 SER A CB    
3147 O  OG    . SER A 411 ? 0.8920 0.9135 0.9397 0.1646  0.0132  -0.2533 1628 SER A OG    
3148 N  N     . HIS A 412 ? 0.8755 0.9305 0.9240 0.1502  0.0216  -0.2210 1629 HIS A N     
3149 C  CA    . HIS A 412 ? 0.8709 0.9498 0.9118 0.1431  0.0295  -0.2189 1629 HIS A CA    
3150 C  C     . HIS A 412 ? 0.8809 0.9769 0.9314 0.1441  0.0323  -0.2129 1629 HIS A C     
3151 O  O     . HIS A 412 ? 0.9521 1.0687 0.9985 0.1381  0.0390  -0.2109 1629 HIS A O     
3152 C  CB    . HIS A 412 ? 0.9012 0.9737 0.9279 0.1302  0.0297  -0.2086 1629 HIS A CB    
3153 C  CG    . HIS A 412 ? 0.9508 1.0157 0.9655 0.1275  0.0291  -0.2156 1629 HIS A CG    
3154 N  ND1   . HIS A 412 ? 0.9427 1.0190 0.9430 0.1193  0.0342  -0.2146 1629 HIS A ND1   
3155 C  CD2   . HIS A 412 ? 0.9713 1.0182 0.9862 0.1318  0.0237  -0.2234 1629 HIS A CD2   
3156 C  CE1   . HIS A 412 ? 0.9349 1.0016 0.9266 0.1190  0.0316  -0.2219 1629 HIS A CE1   
3157 N  NE2   . HIS A 412 ? 0.9705 1.0194 0.9712 0.1263  0.0252  -0.2277 1629 HIS A NE2   
3158 N  N     . THR A 413 ? 0.7594 0.8480 0.8228 0.1514  0.0273  -0.2098 1630 THR A N     
3159 C  CA    . THR A 413 ? 0.7148 0.8211 0.7883 0.1534  0.0292  -0.2056 1630 THR A CA    
3160 C  C     . THR A 413 ? 0.9892 1.1108 1.0748 0.1656  0.0314  -0.2188 1630 THR A C     
3161 O  O     . THR A 413 ? 1.1399 1.2483 1.2334 0.1763  0.0263  -0.2251 1630 THR A O     
3162 C  CB    . THR A 413 ? 0.6335 0.7251 0.7135 0.1545  0.0224  -0.1940 1630 THR A CB    
3163 O  OG1   . THR A 413 ? 0.5698 0.6411 0.6396 0.1458  0.0190  -0.1842 1630 THR A OG1   
3164 C  CG2   . THR A 413 ? 0.5941 0.7047 0.6799 0.1518  0.0247  -0.1873 1630 THR A CG2   
3165 N  N     . LYS A 414 ? 0.9455 1.0945 1.0327 0.1641  0.0390  -0.2230 1631 LYS A N     
3166 C  CA    . LYS A 414 ? 0.7743 0.9426 0.8732 0.1752  0.0424  -0.2358 1631 LYS A CA    
3167 C  C     . LYS A 414 ? 0.7485 0.9407 0.8586 0.1748  0.0456  -0.2317 1631 LYS A C     
3168 O  O     . LYS A 414 ? 0.8140 1.0146 0.9192 0.1637  0.0486  -0.2221 1631 LYS A O     
3169 C  CB    . LYS A 414 ? 0.5470 0.7283 0.6368 0.1741  0.0498  -0.2473 1631 LYS A CB    
3170 N  N     . LEU A 415 ? 0.7196 0.9230 0.8455 0.1872  0.0446  -0.2395 1632 LEU A N     
3171 C  CA    . LEU A 415 ? 0.7287 0.9548 0.8680 0.1887  0.0461  -0.2368 1632 LEU A CA    
3172 C  C     . LEU A 415 ? 0.8598 1.1160 1.0078 0.1943  0.0541  -0.2497 1632 LEU A C     
3173 O  O     . LEU A 415 ? 1.0669 1.3228 1.2169 0.2040  0.0551  -0.2624 1632 LEU A O     
3174 C  CB    . LEU A 415 ? 0.7060 0.9202 0.8582 0.1990  0.0369  -0.2330 1632 LEU A CB    
3175 C  CG    . LEU A 415 ? 0.7776 1.0146 0.9478 0.2067  0.0363  -0.2346 1632 LEU A CG    
3176 C  CD1   . LEU A 415 ? 0.8450 1.0924 1.0159 0.1966  0.0363  -0.2227 1632 LEU A CD1   
3177 C  CD2   . LEU A 415 ? 0.7961 1.0188 0.9779 0.2213  0.0274  -0.2359 1632 LEU A CD2   
3178 N  N     . THR A 416 ? 0.7833 1.0659 0.9368 0.1880  0.0600  -0.2467 1633 THR A N     
3179 C  CA    . THR A 416 ? 0.6860 1.0002 0.8487 0.1921  0.0685  -0.2578 1633 THR A CA    
3180 C  C     . THR A 416 ? 0.6671 1.0070 0.8421 0.1873  0.0715  -0.2527 1633 THR A C     
3181 O  O     . THR A 416 ? 0.6874 1.0218 0.8595 0.1776  0.0687  -0.2403 1633 THR A O     
3182 C  CB    . THR A 416 ? 0.6475 0.9714 0.7959 0.1845  0.0781  -0.2628 1633 THR A CB    
3183 O  OG1   . THR A 416 ? 0.7314 1.0878 0.8903 0.1889  0.0867  -0.2731 1633 THR A OG1   
3184 C  CG2   . THR A 416 ? 0.5199 0.8437 0.6553 0.1674  0.0817  -0.2500 1633 THR A CG2   
3185 N  N     . LYS A 417 ? 0.5812 0.9501 0.7708 0.1946  0.0770  -0.2631 1634 LYS A N     
3186 C  CA    . LYS A 417 ? 0.5452 0.9446 0.7478 0.1897  0.0819  -0.2610 1634 LYS A CA    
3187 C  C     . LYS A 417 ? 0.6620 1.0905 0.8638 0.1843  0.0947  -0.2680 1634 LYS A C     
3188 O  O     . LYS A 417 ? 0.7210 1.1759 0.9332 0.1781  0.1001  -0.2659 1634 LYS A O     
3189 C  CB    . LYS A 417 ? 0.6240 1.0356 0.8488 0.2034  0.0764  -0.2660 1634 LYS A CB    
3190 C  CG    . LYS A 417 ? 0.7352 1.1196 0.9613 0.2098  0.0639  -0.2588 1634 LYS A CG    
3191 C  CD    . LYS A 417 ? 0.8289 1.2251 1.0764 0.2246  0.0580  -0.2638 1634 LYS A CD    
3192 C  CE    . LYS A 417 ? 0.8858 1.2545 1.1327 0.2298  0.0456  -0.2544 1634 LYS A CE    
3193 N  NZ    . LYS A 417 ? 0.8754 1.2082 1.1032 0.2253  0.0419  -0.2480 1634 LYS A NZ    
3194 N  N     . GLN A 418 ? 0.7299 1.1548 0.9196 0.1862  0.0998  -0.2760 1635 GLN A N     
3195 C  CA    . GLN A 418 ? 0.8364 1.2879 1.0221 0.1805  0.1124  -0.2816 1635 GLN A CA    
3196 C  C     . GLN A 418 ? 0.8602 1.2996 1.0236 0.1651  0.1162  -0.2721 1635 GLN A C     
3197 O  O     . GLN A 418 ? 0.9219 1.3352 1.0695 0.1654  0.1120  -0.2715 1635 GLN A O     
3198 C  CB    . GLN A 418 ? 0.9271 1.3867 1.1146 0.1939  0.1161  -0.2982 1635 GLN A CB    
3199 C  CG    . GLN A 418 ? 1.0347 1.5306 1.2258 0.1917  0.1294  -0.3059 1635 GLN A CG    
3200 C  CD    . GLN A 418 ? 1.1302 1.6539 1.3380 0.1852  0.1335  -0.3003 1635 GLN A CD    
3201 O  OE1   . GLN A 418 ? 1.1700 1.7097 1.3725 0.1713  0.1422  -0.2937 1635 GLN A OE1   
3202 N  NE2   . GLN A 418 ? 1.1219 1.6512 1.3504 0.1951  0.1269  -0.3027 1635 GLN A NE2   
3203 N  N     . TRP A 419 ? 0.8323 1.2911 0.9951 0.1519  0.1240  -0.2648 1636 TRP A N     
3204 C  CA    . TRP A 419 ? 0.7886 1.2388 0.9314 0.1368  0.1283  -0.2547 1636 TRP A CA    
3205 C  C     . TRP A 419 ? 0.8078 1.2511 0.9323 0.1388  0.1323  -0.2617 1636 TRP A C     
3206 O  O     . TRP A 419 ? 0.8458 1.2670 0.9518 0.1316  0.1298  -0.2547 1636 TRP A O     
3207 C  CB    . TRP A 419 ? 0.8234 1.3019 0.9719 0.1246  0.1381  -0.2492 1636 TRP A CB    
3208 C  CG    . TRP A 419 ? 0.8365 1.3113 0.9663 0.1094  0.1443  -0.2393 1636 TRP A CG    
3209 C  CD1   . TRP A 419 ? 0.8825 1.3767 1.0035 0.1036  0.1560  -0.2413 1636 TRP A CD1   
3210 C  CD2   . TRP A 419 ? 0.8214 1.2725 0.9392 0.0980  0.1393  -0.2253 1636 TRP A CD2   
3211 N  NE1   . TRP A 419 ? 0.9037 1.3867 1.0076 0.0895  0.1582  -0.2289 1636 TRP A NE1   
3212 C  CE2   . TRP A 419 ? 0.8537 1.3102 0.9558 0.0859  0.1480  -0.2193 1636 TRP A CE2   
3213 C  CE3   . TRP A 419 ? 0.8961 1.3221 1.0146 0.0972  0.1284  -0.2173 1636 TRP A CE3   
3214 C  CZ2   . TRP A 419 ? 0.9406 1.3777 1.0283 0.0736  0.1458  -0.2058 1636 TRP A CZ2   
3215 C  CZ3   . TRP A 419 ? 0.9484 1.3561 1.0527 0.0848  0.1266  -0.2045 1636 TRP A CZ3   
3216 C  CH2   . TRP A 419 ? 0.9897 1.4027 1.0793 0.0734  0.1351  -0.1990 1636 TRP A CH2   
3217 N  N     . ALA A 420 ? 0.7897 1.2530 0.9190 0.1484  0.1386  -0.2758 1637 ALA A N     
3218 C  CA    . ALA A 420 ? 0.7198 1.1797 0.8316 0.1509  0.1428  -0.2841 1637 ALA A CA    
3219 C  C     . ALA A 420 ? 0.7494 1.1735 0.8497 0.1557  0.1322  -0.2848 1637 ALA A C     
3220 O  O     . ALA A 420 ? 0.8038 1.2132 0.8840 0.1488  0.1323  -0.2810 1637 ALA A O     
3221 C  CB    . ALA A 420 ? 0.6947 1.1801 0.8166 0.1635  0.1494  -0.3009 1637 ALA A CB    
3222 N  N     . GLU A 421 ? 0.6855 1.0952 0.7986 0.1675  0.1229  -0.2895 1638 GLU A N     
3223 C  CA    . GLU A 421 ? 0.8017 1.1777 0.9044 0.1712  0.1134  -0.2900 1638 GLU A CA    
3224 C  C     . GLU A 421 ? 0.8024 1.1541 0.8971 0.1603  0.1066  -0.2737 1638 GLU A C     
3225 O  O     . GLU A 421 ? 0.9403 1.2659 1.0222 0.1591  0.1007  -0.2719 1638 GLU A O     
3226 C  CB    . GLU A 421 ? 0.9231 1.2893 1.0406 0.1878  0.1059  -0.3005 1638 GLU A CB    
3227 C  CG    . GLU A 421 ? 0.9644 1.3374 1.1028 0.1932  0.1017  -0.2972 1638 GLU A CG    
3228 C  CD    . GLU A 421 ? 1.0875 1.4403 1.2360 0.2081  0.0918  -0.3039 1638 GLU A CD    
3229 O  OE1   . GLU A 421 ? 1.1583 1.5016 1.3016 0.2161  0.0911  -0.3156 1638 GLU A OE1   
3230 O  OE2   . GLU A 421 ? 1.1252 1.4709 1.2864 0.2117  0.0846  -0.2974 1638 GLU A OE2   
3231 N  N     . PHE A 422 ? 0.6922 1.0525 0.7944 0.1522  0.1073  -0.2624 1639 PHE A N     
3232 C  CA    . PHE A 422 ? 0.8093 1.1508 0.9014 0.1398  0.1032  -0.2470 1639 PHE A CA    
3233 C  C     . PHE A 422 ? 0.8878 1.2253 0.9584 0.1295  0.1082  -0.2436 1639 PHE A C     
3234 O  O     . PHE A 422 ? 0.9521 1.2644 1.0096 0.1256  0.1024  -0.2379 1639 PHE A O     
3235 C  CB    . PHE A 422 ? 0.9538 1.3111 1.0575 0.1323  0.1052  -0.2377 1639 PHE A CB    
3236 C  CG    . PHE A 422 ? 0.9311 1.2745 1.0245 0.1182  0.1032  -0.2223 1639 PHE A CG    
3237 C  CD1   . PHE A 422 ? 0.9121 1.2359 1.0096 0.1179  0.0938  -0.2139 1639 PHE A CD1   
3238 C  CD2   . PHE A 422 ? 0.8528 1.2037 0.9331 0.1055  0.1109  -0.2162 1639 PHE A CD2   
3239 C  CE1   . PHE A 422 ? 0.8467 1.1584 0.9354 0.1055  0.0922  -0.2006 1639 PHE A CE1   
3240 C  CE2   . PHE A 422 ? 0.7897 1.1276 0.8616 0.0932  0.1089  -0.2025 1639 PHE A CE2   
3241 C  CZ    . PHE A 422 ? 0.7683 1.0868 0.8446 0.0934  0.0996  -0.1952 1639 PHE A CZ    
3242 N  N     . LEU A 423 ? 0.9227 1.2858 0.9894 0.1254  0.1191  -0.2470 1640 LEU A N     
3243 C  CA    . LEU A 423 ? 0.8277 1.1894 0.8732 0.1161  0.1244  -0.2435 1640 LEU A CA    
3244 C  C     . LEU A 423 ? 0.8749 1.2209 0.9077 0.1234  0.1208  -0.2535 1640 LEU A C     
3245 O  O     . LEU A 423 ? 0.9484 1.2778 0.9638 0.1169  0.1186  -0.2480 1640 LEU A O     
3246 C  CB    . LEU A 423 ? 0.6390 1.0330 0.6837 0.1110  0.1373  -0.2453 1640 LEU A CB    
3247 C  CG    . LEU A 423 ? 0.5460 0.9554 0.5977 0.0989  0.1426  -0.2333 1640 LEU A CG    
3248 C  CD1   . LEU A 423 ? 0.5442 0.9848 0.5932 0.0940  0.1561  -0.2358 1640 LEU A CD1   
3249 C  CD2   . LEU A 423 ? 0.5518 0.9396 0.5920 0.0865  0.1382  -0.2177 1640 LEU A CD2   
3250 N  N     . GLN A 424 ? 0.8274 1.1784 0.8690 0.1372  0.1201  -0.2685 1641 GLN A N     
3251 C  CA    . GLN A 424 ? 0.8261 1.1600 0.8575 0.1446  0.1155  -0.2790 1641 GLN A CA    
3252 C  C     . GLN A 424 ? 0.9818 1.2811 1.0088 0.1427  0.1040  -0.2715 1641 GLN A C     
3253 O  O     . GLN A 424 ? 0.9933 1.2774 1.0033 0.1377  0.1016  -0.2695 1641 GLN A O     
3254 C  CB    . GLN A 424 ? 0.7694 1.1116 0.8144 0.1605  0.1153  -0.2960 1641 GLN A CB    
3255 N  N     . PHE A 425 ? 1.1732 1.4606 1.2153 0.1468  0.0967  -0.2672 1642 PHE A N     
3256 C  CA    . PHE A 425 ? 1.1838 1.4396 1.2232 0.1452  0.0863  -0.2595 1642 PHE A CA    
3257 C  C     . PHE A 425 ? 1.1172 1.3637 1.1410 0.1310  0.0864  -0.2457 1642 PHE A C     
3258 O  O     . PHE A 425 ? 1.1569 1.3829 1.1687 0.1284  0.0815  -0.2443 1642 PHE A O     
3259 C  CB    . PHE A 425 ? 1.0908 1.3397 1.1477 0.1498  0.0800  -0.2539 1642 PHE A CB    
3260 C  CG    . PHE A 425 ? 1.0729 1.3248 1.1456 0.1649  0.0775  -0.2662 1642 PHE A CG    
3261 C  CD1   . PHE A 425 ? 1.0428 1.2976 1.1134 0.1739  0.0794  -0.2817 1642 PHE A CD1   
3262 C  CD2   . PHE A 425 ? 1.1475 1.3994 1.2371 0.1705  0.0730  -0.2625 1642 PHE A CD2   
3263 C  CE1   . PHE A 425 ? 1.0720 1.3288 1.1577 0.1883  0.0769  -0.2933 1642 PHE A CE1   
3264 C  CE2   . PHE A 425 ? 1.1666 1.4208 1.2711 0.1851  0.0703  -0.2734 1642 PHE A CE2   
3265 C  CZ    . PHE A 425 ? 1.1420 1.3983 1.2449 0.1941  0.0723  -0.2889 1642 PHE A CZ    
3266 N  N     . LEU A 426 ? 1.0017 1.2633 1.0262 0.1216  0.0919  -0.2356 1643 LEU A N     
3267 C  CA    . LEU A 426 ? 1.0265 1.2792 1.0370 0.1084  0.0921  -0.2222 1643 LEU A CA    
3268 C  C     . LEU A 426 ? 1.0998 1.3528 1.0908 0.1046  0.0957  -0.2256 1643 LEU A C     
3269 O  O     . LEU A 426 ? 1.1710 1.4045 1.1497 0.0994  0.0907  -0.2198 1643 LEU A O     
3270 C  CB    . LEU A 426 ? 0.9881 1.2588 1.0033 0.0991  0.0982  -0.2123 1643 LEU A CB    
3271 C  CG    . LEU A 426 ? 0.9614 1.2226 0.9623 0.0856  0.0986  -0.1984 1643 LEU A CG    
3272 C  CD1   . LEU A 426 ? 1.0173 1.2489 1.0156 0.0845  0.0883  -0.1910 1643 LEU A CD1   
3273 C  CD2   . LEU A 426 ? 0.8826 1.1604 0.8898 0.0766  0.1043  -0.1894 1643 LEU A CD2   
3274 N  N     . GLU A 427 ? 1.0378 1.3134 1.0257 0.1077  0.1040  -0.2354 1644 GLU A N     
3275 C  CA    . GLU A 427 ? 0.9986 1.2768 0.9666 0.1042  0.1078  -0.2385 1644 GLU A CA    
3276 C  C     . GLU A 427 ? 1.0831 1.3378 1.0434 0.1095  0.0993  -0.2455 1644 GLU A C     
3277 O  O     . GLU A 427 ? 1.1183 1.3649 1.0613 0.1037  0.0982  -0.2424 1644 GLU A O     
3278 C  CB    . GLU A 427 ? 0.8913 1.1984 0.8584 0.1085  0.1182  -0.2496 1644 GLU A CB    
3279 N  N     . THR A 428 ? 1.0252 1.2688 0.9982 0.1204  0.0930  -0.2548 1645 THR A N     
3280 C  CA    . THR A 428 ? 0.8768 1.0951 0.8446 0.1244  0.0840  -0.2602 1645 THR A CA    
3281 C  C     . THR A 428 ? 0.8029 0.9953 0.7765 0.1211  0.0747  -0.2488 1645 THR A C     
3282 O  O     . THR A 428 ? 0.8276 1.0017 0.8097 0.1283  0.0671  -0.2538 1645 THR A O     
3283 C  CB    . THR A 428 ? 0.8191 1.0377 0.7949 0.1381  0.0823  -0.2782 1645 THR A CB    
3284 O  OG1   . THR A 428 ? 0.8574 1.0652 0.8524 0.1456  0.0765  -0.2782 1645 THR A OG1   
3285 C  CG2   . THR A 428 ? 0.7185 0.9675 0.6932 0.1425  0.0927  -0.2890 1645 THR A CG2   
3286 N  N     . LYS A 429 ? 0.7848 0.9757 0.7545 0.1103  0.0755  -0.2334 1646 LYS A N     
3287 C  CA    . LYS A 429 ? 0.8285 0.9949 0.7964 0.1047  0.0675  -0.2221 1646 LYS A CA    
3288 C  C     . LYS A 429 ? 0.7480 0.8998 0.7324 0.1101  0.0606  -0.2193 1646 LYS A C     
3289 O  O     . LYS A 429 ? 0.7489 0.8777 0.7334 0.1098  0.0529  -0.2155 1646 LYS A O     
3290 C  CB    . LYS A 429 ? 0.7484 0.8984 0.7033 0.1042  0.0623  -0.2268 1646 LYS A CB    
3291 C  CG    . LYS A 429 ? 0.7107 0.8400 0.6585 0.0957  0.0561  -0.2146 1646 LYS A CG    
3292 C  CD    . LYS A 429 ? 0.7226 0.8345 0.6635 0.0981  0.0494  -0.2224 1646 LYS A CD    
3293 C  CE    . LYS A 429 ? 0.7716 0.8784 0.6960 0.0885  0.0481  -0.2147 1646 LYS A CE    
3294 N  NZ    . LYS A 429 ? 0.7365 0.8625 0.6450 0.0861  0.0549  -0.2191 1646 LYS A NZ    
3295 N  N     . ASN A 430 ? 0.6273 0.7924 0.6257 0.1145  0.0633  -0.2196 1647 ASN A N     
3296 C  CA    . ASN A 430 ? 0.7649 0.9154 0.7768 0.1187  0.0563  -0.2146 1647 ASN A CA    
3297 C  C     . ASN A 430 ? 0.7660 0.9325 0.7881 0.1165  0.0597  -0.2074 1647 ASN A C     
3298 O  O     . ASN A 430 ? 0.8092 0.9981 0.8297 0.1122  0.0676  -0.2074 1647 ASN A O     
3299 C  CB    . ASN A 430 ? 0.7835 0.9235 0.8057 0.1318  0.0511  -0.2265 1647 ASN A CB    
3300 C  CG    . ASN A 430 ? 0.6468 0.8078 0.6792 0.1416  0.0561  -0.2388 1647 ASN A CG    
3301 O  OD1   . ASN A 430 ? 0.7362 0.9106 0.7626 0.1440  0.0615  -0.2497 1647 ASN A OD1   
3302 N  ND2   . ASN A 430 ? 0.5531 0.7169 0.6014 0.1483  0.0539  -0.2375 1647 ASN A ND2   
3303 N  N     . ILE A 431 ? 0.6622 0.8170 0.6945 0.1188  0.0536  -0.2007 1648 ILE A N     
3304 C  CA    . ILE A 431 ? 0.7059 0.8723 0.7466 0.1152  0.0550  -0.1922 1648 ILE A CA    
3305 C  C     . ILE A 431 ? 0.7159 0.8941 0.7739 0.1262  0.0544  -0.1990 1648 ILE A C     
3306 O  O     . ILE A 431 ? 0.8028 0.9735 0.8673 0.1371  0.0507  -0.2077 1648 ILE A O     
3307 C  CB    . ILE A 431 ? 0.6669 0.8136 0.7055 0.1092  0.0487  -0.1788 1648 ILE A CB    
3308 C  CG1   . ILE A 431 ? 0.5805 0.7050 0.6251 0.1175  0.0402  -0.1795 1648 ILE A CG1   
3309 C  CG2   . ILE A 431 ? 0.4850 0.6221 0.5075 0.0987  0.0496  -0.1724 1648 ILE A CG2   
3310 C  CD1   . ILE A 431 ? 0.4806 0.5940 0.5296 0.1155  0.0348  -0.1677 1648 ILE A CD1   
3311 N  N     . ILE A 432 ? 0.6100 0.8072 0.6763 0.1233  0.0579  -0.1949 1649 ILE A N     
3312 C  CA    . ILE A 432 ? 0.6110 0.8287 0.6932 0.1325  0.0600  -0.2031 1649 ILE A CA    
3313 C  C     . ILE A 432 ? 0.6312 0.8532 0.7254 0.1325  0.0563  -0.1955 1649 ILE A C     
3314 O  O     . ILE A 432 ? 0.5753 0.8038 0.6673 0.1222  0.0584  -0.1866 1649 ILE A O     
3315 C  CB    . ILE A 432 ? 0.6239 0.8698 0.7055 0.1292  0.0704  -0.2094 1649 ILE A CB    
3316 C  CG1   . ILE A 432 ? 0.6647 0.9067 0.7301 0.1261  0.0745  -0.2143 1649 ILE A CG1   
3317 C  CG2   . ILE A 432 ? 0.6573 0.9229 0.7554 0.1410  0.0723  -0.2205 1649 ILE A CG2   
3318 C  CD1   . ILE A 432 ? 0.6395 0.9032 0.6976 0.1168  0.0844  -0.2131 1649 ILE A CD1   
3319 N  N     . MET A 433 ? 0.7703 0.9906 0.8779 0.1445  0.0510  -0.1996 1650 MET A N     
3320 C  CA    . MET A 433 ? 0.7441 0.9720 0.8643 0.1465  0.0472  -0.1942 1650 MET A CA    
3321 C  C     . MET A 433 ? 0.7469 1.0043 0.8821 0.1530  0.0521  -0.2037 1650 MET A C     
3322 O  O     . MET A 433 ? 0.6897 0.9502 0.8320 0.1648  0.0519  -0.2144 1650 MET A O     
3323 C  CB    . MET A 433 ? 0.7833 0.9885 0.9076 0.1553  0.0373  -0.1906 1650 MET A CB    
3324 C  CG    . MET A 433 ? 0.9893 1.1997 1.1232 0.1562  0.0325  -0.1831 1650 MET A CG    
3325 S  SD    . MET A 433 ? 1.1408 1.3198 1.2719 0.1607  0.0217  -0.1733 1650 MET A SD    
3326 C  CE    . MET A 433 ? 1.1166 1.2718 1.2397 0.1653  0.0207  -0.1795 1650 MET A CE    
3327 N  N     . ALA A 434 ? 0.7751 1.0544 0.9155 0.1453  0.0567  -0.2002 1651 ALA A N     
3328 C  CA    . ALA A 434 ? 0.6380 0.9485 0.7930 0.1492  0.0626  -0.2087 1651 ALA A CA    
3329 C  C     . ALA A 434 ? 0.7036 1.0289 0.8716 0.1467  0.0602  -0.2032 1651 ALA A C     
3330 O  O     . ALA A 434 ? 0.7137 1.0285 0.8761 0.1380  0.0567  -0.1925 1651 ALA A O     
3331 C  CB    . ALA A 434 ? 0.4733 0.8022 0.6214 0.1404  0.0738  -0.2123 1651 ALA A CB    
3332 N  N     . PRO A 435 ? 0.6006 0.9511 0.7865 0.1545  0.0617  -0.2108 1652 PRO A N     
3333 C  CA    . PRO A 435 ? 0.6379 1.0051 0.8369 0.1515  0.0593  -0.2064 1652 PRO A CA    
3334 C  C     . PRO A 435 ? 0.6300 1.0117 0.8256 0.1351  0.0667  -0.2010 1652 PRO A C     
3335 O  O     . PRO A 435 ? 0.5607 0.9563 0.7528 0.1292  0.0764  -0.2048 1652 PRO A O     
3336 C  CB    . PRO A 435 ? 0.5827 0.9749 0.8018 0.1644  0.0601  -0.2175 1652 PRO A CB    
3337 C  CG    . PRO A 435 ? 0.4965 0.8899 0.7124 0.1713  0.0655  -0.2280 1652 PRO A CG    
3338 C  CD    . PRO A 435 ? 0.5182 0.8799 0.7141 0.1684  0.0635  -0.2240 1652 PRO A CD    
3339 N  N     . PHE A 436 ? 0.5255 0.9052 0.7232 0.1281  0.0622  -0.1923 1653 PHE A N     
3340 C  CA    . PHE A 436 ? 0.5718 0.9583 0.7645 0.1118  0.0677  -0.1856 1653 PHE A CA    
3341 C  C     . PHE A 436 ? 0.7931 1.1941 0.9995 0.1079  0.0639  -0.1822 1653 PHE A C     
3342 O  O     . PHE A 436 ? 0.7920 1.1863 1.0042 0.1155  0.0545  -0.1805 1653 PHE A O     
3343 C  CB    . PHE A 436 ? 0.5173 0.8751 0.6895 0.1032  0.0661  -0.1761 1653 PHE A CB    
3344 C  CG    . PHE A 436 ? 0.5532 0.9164 0.7188 0.0869  0.0728  -0.1697 1653 PHE A CG    
3345 C  CD1   . PHE A 436 ? 0.5037 0.8900 0.6728 0.0810  0.0833  -0.1738 1653 PHE A CD1   
3346 C  CD2   . PHE A 436 ? 0.5788 0.9242 0.7350 0.0777  0.0688  -0.1594 1653 PHE A CD2   
3347 C  CE1   . PHE A 436 ? 0.6088 0.9992 0.7720 0.0658  0.0895  -0.1670 1653 PHE A CE1   
3348 C  CE2   . PHE A 436 ? 0.6147 0.9638 0.7654 0.0631  0.0747  -0.1534 1653 PHE A CE2   
3349 C  CZ    . PHE A 436 ? 0.6533 1.0244 0.8075 0.0569  0.0850  -0.1568 1653 PHE A CZ    
3350 N  N     . CYS A 437 ? 0.8247 1.2459 1.0359 0.0958  0.0715  -0.1813 1654 CYS A N     
3351 C  CA    . CYS A 437 ? 0.7976 1.2356 1.0226 0.0897  0.0693  -0.1791 1654 CYS A CA    
3352 C  C     . CYS A 437 ? 0.9467 1.3646 1.1616 0.0801  0.0637  -0.1686 1654 CYS A C     
3353 O  O     . CYS A 437 ? 1.1867 1.6097 1.4111 0.0804  0.0570  -0.1671 1654 CYS A O     
3354 C  CB    . CYS A 437 ? 0.7201 1.1872 0.9549 0.0798  0.0802  -0.1823 1654 CYS A CB    
3355 S  SG    . CYS A 437 ? 0.7625 1.2197 0.9795 0.0615  0.0893  -0.1737 1654 CYS A SG    
3356 N  N     . GLY A 438 ? 0.8536 1.2494 1.0496 0.0721  0.0661  -0.1618 1655 GLY A N     
3357 C  CA    . GLY A 438 ? 0.7954 1.1724 0.9816 0.0631  0.0616  -0.1523 1655 GLY A CA    
3358 C  C     . GLY A 438 ? 0.8171 1.2005 1.0012 0.0466  0.0684  -0.1474 1655 GLY A C     
3359 O  O     . GLY A 438 ? 0.8690 1.2339 1.0423 0.0385  0.0658  -0.1395 1655 GLY A O     
3360 N  N     . GLU A 439 ? 0.8016 1.2102 0.9959 0.0416  0.0772  -0.1518 1656 GLU A N     
3361 C  CA    . GLU A 439 ? 0.9025 1.3197 1.0975 0.0257  0.0843  -0.1471 1656 GLU A CA    
3362 C  C     . GLU A 439 ? 0.9632 1.3634 1.1384 0.0176  0.0904  -0.1407 1656 GLU A C     
3363 O  O     . GLU A 439 ? 1.0196 1.4131 1.1842 0.0235  0.0933  -0.1429 1656 GLU A O     
3364 C  CB    . GLU A 439 ? 0.8629 1.3142 1.0760 0.0233  0.0923  -0.1537 1656 GLU A CB    
3365 C  CG    . GLU A 439 ? 0.8571 1.3290 1.0916 0.0316  0.0864  -0.1608 1656 GLU A CG    
3366 C  CD    . GLU A 439 ? 0.8261 1.2965 1.0679 0.0252  0.0790  -0.1571 1656 GLU A CD    
3367 O  OE1   . GLU A 439 ? 0.8279 1.2962 1.0675 0.0107  0.0824  -0.1513 1656 GLU A OE1   
3368 O  OE2   . GLU A 439 ? 0.7837 1.2545 1.0330 0.0350  0.0694  -0.1600 1656 GLU A OE2   
3369 N  N     . ILE A 440 ? 0.8916 1.2843 1.0619 0.0040  0.0919  -0.1327 1657 ILE A N     
3370 C  CA    . ILE A 440 ? 0.7385 1.1123 0.8894 -0.0036 0.0961  -0.1252 1657 ILE A CA    
3371 C  C     . ILE A 440 ? 0.7424 1.1326 0.8916 -0.0102 0.1081  -0.1257 1657 ILE A C     
3372 O  O     . ILE A 440 ? 0.7936 1.1731 0.9268 -0.0100 0.1119  -0.1235 1657 ILE A O     
3373 C  CB    . ILE A 440 ? 0.6383 0.9957 0.7837 -0.0149 0.0930  -0.1162 1657 ILE A CB    
3374 C  CG1   . ILE A 440 ? 0.6244 0.9682 0.7718 -0.0089 0.0816  -0.1159 1657 ILE A CG1   
3375 C  CG2   . ILE A 440 ? 0.6160 0.9526 0.7411 -0.0208 0.0962  -0.1085 1657 ILE A CG2   
3376 C  CD1   . ILE A 440 ? 0.5444 0.8813 0.6932 -0.0200 0.0790  -0.1100 1657 ILE A CD1   
3377 N  N     . SER A 441 ? 0.7429 1.1593 0.9082 -0.0169 0.1142  -0.1279 1658 SER A N     
3378 C  CA    . SER A 441 ? 0.7541 1.1882 0.9181 -0.0227 0.1264  -0.1283 1658 SER A CA    
3379 C  C     . SER A 441 ? 0.8088 1.2500 0.9689 -0.0100 0.1291  -0.1367 1658 SER A C     
3380 O  O     . SER A 441 ? 0.8338 1.2741 0.9803 -0.0116 0.1364  -0.1356 1658 SER A O     
3381 C  CB    . SER A 441 ? 0.7434 1.2063 0.9281 -0.0315 0.1323  -0.1301 1658 SER A CB    
3382 O  OG    . SER A 441 ? 0.8155 1.3052 1.0160 -0.0223 0.1349  -0.1405 1658 SER A OG    
3383 N  N     . CYS A 442 ? 0.7969 1.2446 0.9686 0.0031  0.1230  -0.1453 1659 CYS A N     
3384 C  CA    . CYS A 442 ? 0.7155 1.1677 0.8845 0.0163  0.1245  -0.1542 1659 CYS A CA    
3385 C  C     . CYS A 442 ? 0.6745 1.0974 0.8217 0.0208  0.1206  -0.1514 1659 CYS A C     
3386 O  O     . CYS A 442 ? 0.7315 1.1555 0.8683 0.0244  0.1260  -0.1551 1659 CYS A O     
3387 C  CB    . CYS A 442 ? 0.6498 1.1122 0.8363 0.0296  0.1174  -0.1629 1659 CYS A CB    
3388 S  SG    . CYS A 442 ? 0.6080 1.0740 0.7943 0.0476  0.1173  -0.1747 1659 CYS A SG    
3389 N  N     . GLU A 443 ? 0.5671 0.9643 0.7070 0.0201  0.1115  -0.1450 1660 GLU A N     
3390 C  CA    . GLU A 443 ? 0.5738 0.9432 0.6939 0.0229  0.1078  -0.1415 1660 GLU A CA    
3391 C  C     . GLU A 443 ? 0.6884 1.0541 0.7921 0.0128  0.1158  -0.1356 1660 GLU A C     
3392 O  O     . GLU A 443 ? 0.8183 1.1742 0.9078 0.0171  0.1170  -0.1376 1660 GLU A O     
3393 C  CB    . GLU A 443 ? 0.5153 0.8609 0.6321 0.0221  0.0976  -0.1347 1660 GLU A CB    
3394 C  CG    . GLU A 443 ? 0.5371 0.8557 0.6396 0.0295  0.0910  -0.1336 1660 GLU A CG    
3395 C  CD    . GLU A 443 ? 0.6477 0.9465 0.7493 0.0295  0.0814  -0.1274 1660 GLU A CD    
3396 O  OE1   . GLU A 443 ? 0.7193 1.0266 0.8346 0.0321  0.0770  -0.1289 1660 GLU A OE1   
3397 O  OE2   . GLU A 443 ? 0.7135 0.9892 0.8006 0.0272  0.0783  -0.1213 1660 GLU A OE2   
3398 N  N     . ASP A 444 ? 0.6887 1.0619 0.7942 -0.0006 0.1211  -0.1285 1661 ASP A N     
3399 C  CA    . ASP A 444 ? 0.6914 1.0637 0.7824 -0.0106 0.1294  -0.1221 1661 ASP A CA    
3400 C  C     . ASP A 444 ? 0.7601 1.1526 0.8493 -0.0065 0.1385  -0.1294 1661 ASP A C     
3401 O  O     . ASP A 444 ? 0.8530 1.2384 0.9248 -0.0071 0.1422  -0.1277 1661 ASP A O     
3402 C  CB    . ASP A 444 ? 0.7686 1.1487 0.8659 -0.0254 0.1340  -0.1140 1661 ASP A CB    
3403 C  CG    . ASP A 444 ? 0.9165 1.2748 1.0123 -0.0307 0.1258  -0.1063 1661 ASP A CG    
3404 O  OD1   . ASP A 444 ? 0.9087 1.2753 1.0176 -0.0386 0.1259  -0.1038 1661 ASP A OD1   
3405 O  OD2   . ASP A 444 ? 1.0564 1.3899 1.1385 -0.0269 0.1193  -0.1032 1661 ASP A OD2   
3406 N  N     . ARG A 445 ? 0.7402 1.1593 0.8475 -0.0021 0.1423  -0.1378 1662 ARG A N     
3407 C  CA    . ARG A 445 ? 0.6872 1.1275 0.7939 0.0028  0.1513  -0.1459 1662 ARG A CA    
3408 C  C     . ARG A 445 ? 0.8191 1.2460 0.9147 0.0161  0.1469  -0.1535 1662 ARG A C     
3409 O  O     . ARG A 445 ? 0.8262 1.2573 0.9091 0.0177  0.1531  -0.1566 1662 ARG A O     
3410 C  CB    . ARG A 445 ? 0.5359 1.0073 0.6662 0.0062  0.1552  -0.1542 1662 ARG A CB    
3411 N  N     . ILE A 446 ? 0.9135 1.3238 1.0134 0.0255  0.1360  -0.1564 1663 ILE A N     
3412 C  CA    . ILE A 446 ? 0.9308 1.3249 1.0207 0.0375  0.1309  -0.1629 1663 ILE A CA    
3413 C  C     . ILE A 446 ? 0.9594 1.3324 1.0261 0.0320  0.1311  -0.1563 1663 ILE A C     
3414 O  O     . ILE A 446 ? 0.9169 1.2904 0.9719 0.0363  0.1345  -0.1618 1663 ILE A O     
3415 C  CB    . ILE A 446 ? 0.8737 1.2512 0.9717 0.0468  0.1191  -0.1645 1663 ILE A CB    
3416 C  CG1   . ILE A 446 ? 0.8022 1.2008 0.9227 0.0549  0.1181  -0.1725 1663 ILE A CG1   
3417 C  CG2   . ILE A 446 ? 0.9421 1.2991 1.0290 0.0570  0.1136  -0.1695 1663 ILE A CG2   
3418 C  CD1   . ILE A 446 ? 0.6017 0.9841 0.7292 0.0658  0.1063  -0.1743 1663 ILE A CD1   
3419 N  N     . LYS A 447 ? 0.8636 1.2181 0.9235 0.0228  0.1270  -0.1449 1664 LYS A N     
3420 C  CA    . LYS A 447 ? 0.7921 1.1262 0.8310 0.0179  0.1261  -0.1381 1664 LYS A CA    
3421 C  C     . LYS A 447 ? 0.8166 1.1651 0.8440 0.0116  0.1368  -0.1370 1664 LYS A C     
3422 O  O     . LYS A 447 ? 0.8731 1.2134 0.8841 0.0141  0.1375  -0.1387 1664 LYS A O     
3423 C  CB    . LYS A 447 ? 0.6980 1.0132 0.7336 0.0086  0.1210  -0.1260 1664 LYS A CB    
3424 N  N     . ALA A 448 ? 0.7286 1.0993 0.7646 0.0035  0.1454  -0.1343 1665 ALA A N     
3425 C  CA    . ALA A 448 ? 0.6274 1.0134 0.6526 -0.0029 0.1564  -0.1323 1665 ALA A CA    
3426 C  C     . ALA A 448 ? 0.6287 1.0291 0.6506 0.0077  0.1608  -0.1449 1665 ALA A C     
3427 O  O     . ALA A 448 ? 0.5904 0.9884 0.5940 0.0074  0.1645  -0.1449 1665 ALA A O     
3428 C  CB    . ALA A 448 ? 0.5413 0.9493 0.5790 -0.0138 0.1649  -0.1272 1665 ALA A CB    
3429 N  N     . GLU A 449 ? 0.6914 1.1075 0.7308 0.0174  0.1605  -0.1561 1666 GLU A N     
3430 C  CA    . GLU A 449 ? 0.6938 1.1278 0.7333 0.0276  0.1659  -0.1692 1666 GLU A CA    
3431 C  C     . GLU A 449 ? 0.8043 1.2190 0.8313 0.0386  0.1591  -0.1768 1666 GLU A C     
3432 O  O     . GLU A 449 ? 0.8639 1.2915 0.8907 0.0480  0.1627  -0.1890 1666 GLU A O     
3433 C  CB    . GLU A 449 ? 0.6912 1.1474 0.7549 0.0352  0.1669  -0.1787 1666 GLU A CB    
3434 N  N     . SER A 450 ? 0.8455 1.2308 0.8626 0.0375  0.1497  -0.1706 1667 SER A N     
3435 C  CA    . SER A 450 ? 0.6965 1.0628 0.7005 0.0459  0.1436  -0.1768 1667 SER A CA    
3436 C  C     . SER A 450 ? 0.7738 1.1333 0.7545 0.0393  0.1469  -0.1714 1667 SER A C     
3437 O  O     . SER A 450 ? 0.7668 1.1253 0.7361 0.0459  0.1472  -0.1801 1667 SER A O     
3438 C  CB    . SER A 450 ? 0.6351 0.9735 0.6424 0.0490  0.1313  -0.1732 1667 SER A CB    
3439 O  OG    . SER A 450 ? 0.7026 1.0463 0.7299 0.0511  0.1281  -0.1730 1667 SER A OG    
3440 N  N     . ALA A 451 ? 0.9225 1.2788 0.8964 0.0265  0.1495  -0.1577 1668 ALA A N     
3441 C  CA    . ALA A 451 ? 1.0488 1.4001 1.0008 0.0190  0.1531  -0.1502 1668 ALA A CA    
3442 C  C     . ALA A 451 ? 1.1294 1.5057 1.0729 0.0189  0.1645  -0.1554 1668 ALA A C     
3443 O  O     . ALA A 451 ? 1.1707 1.5550 1.1037 0.0088  0.1720  -0.1459 1668 ALA A O     
3444 C  CB    . ALA A 451 ? 1.0637 1.4075 1.0138 0.0057  0.1537  -0.1344 1668 ALA A CB    
3445 N  N     . PRO A 462 ? 0.9372 1.0762 0.8338 0.0001  0.0805  -0.0877 1679 PRO A N     
3446 C  CA    . PRO A 462 ? 1.0073 1.1625 0.8945 -0.0049 0.0890  -0.0856 1679 PRO A CA    
3447 C  C     . PRO A 462 ? 1.0859 1.2616 0.9846 -0.0060 0.0967  -0.0883 1679 PRO A C     
3448 O  O     . PRO A 462 ? 1.2168 1.4063 1.1101 -0.0121 0.1046  -0.0842 1679 PRO A O     
3449 C  CB    . PRO A 462 ? 0.9683 1.1136 0.8467 -0.0139 0.0886  -0.0721 1679 PRO A CB    
3450 C  CG    . PRO A 462 ? 1.0432 1.1675 0.9182 -0.0111 0.0792  -0.0709 1679 PRO A CG    
3451 C  CD    . PRO A 462 ? 0.9820 1.1018 0.8704 -0.0028 0.0741  -0.0801 1679 PRO A CD    
3452 N  N     . ALA A 463 ? 0.9929 1.1708 0.9074 -0.0002 0.0945  -0.0949 1680 ALA A N     
3453 C  CA    . ALA A 463 ? 0.9564 1.1553 0.8838 0.0006  0.1009  -0.0996 1680 ALA A CA    
3454 C  C     . ALA A 463 ? 0.9362 1.1464 0.8650 0.0104  0.1026  -0.1132 1680 ALA A C     
3455 O  O     . ALA A 463 ? 0.8745 1.0751 0.8089 0.0190  0.0962  -0.1205 1680 ALA A O     
3456 C  CB    . ALA A 463 ? 0.8938 1.0896 0.8383 0.0012  0.0970  -0.0981 1680 ALA A CB    
3457 N  N     . MET A 464 ? 0.9626 1.1930 0.8865 0.0091  0.1115  -0.1166 1681 MET A N     
3458 C  CA    . MET A 464 ? 0.9479 1.1913 0.8719 0.0182  0.1143  -0.1301 1681 MET A CA    
3459 C  C     . MET A 464 ? 0.9714 1.2325 0.9144 0.0237  0.1175  -0.1380 1681 MET A C     
3460 O  O     . MET A 464 ? 0.9109 1.1802 0.8572 0.0332  0.1182  -0.1505 1681 MET A O     
3461 C  CB    . MET A 464 ? 0.9353 1.1929 0.8431 0.0149  0.1224  -0.1305 1681 MET A CB    
3462 C  CG    . MET A 464 ? 0.9914 1.2436 0.8866 0.0227  0.1192  -0.1405 1681 MET A CG    
3463 S  SD    . MET A 464 ? 1.0914 1.3119 0.9840 0.0264  0.1057  -0.1398 1681 MET A SD    
3464 C  CE    . MET A 464 ? 1.0928 1.3003 0.9720 0.0143  0.1044  -0.1224 1681 MET A CE    
3465 N  N     . GLY A 465 ? 1.1165 1.3839 1.0723 0.0181  0.1192  -0.1317 1682 GLY A N     
3466 C  CA    . GLY A 465 ? 1.1429 1.4259 1.1182 0.0236  0.1206  -0.1388 1682 GLY A CA    
3467 C  C     . GLY A 465 ? 1.0479 1.3149 1.0343 0.0313  0.1106  -0.1415 1682 GLY A C     
3468 O  O     . GLY A 465 ? 1.1171 1.3613 1.0962 0.0329  0.1029  -0.1389 1682 GLY A O     
3469 N  N     . ALA A 466 ? 0.9431 1.2233 0.9474 0.0367  0.1108  -0.1471 1683 ALA A N     
3470 C  CA    . ALA A 466 ? 0.8533 1.1217 0.8693 0.0454  0.1019  -0.1504 1683 ALA A CA    
3471 C  C     . ALA A 466 ? 0.7757 1.0407 0.8018 0.0399  0.0983  -0.1417 1683 ALA A C     
3472 O  O     . ALA A 466 ? 0.7974 1.0814 0.8345 0.0355  0.1031  -0.1407 1683 ALA A O     
3473 C  CB    . ALA A 466 ? 0.8464 1.1310 0.8757 0.0570  0.1033  -0.1631 1683 ALA A CB    
3474 N  N     . LYS A 467 ? 0.7117 0.9535 0.7350 0.0405  0.0897  -0.1363 1684 LYS A N     
3475 C  CA    . LYS A 467 ? 0.6521 0.8881 0.6833 0.0365  0.0851  -0.1287 1684 LYS A CA    
3476 C  C     . LYS A 467 ? 0.5782 0.8129 0.6233 0.0470  0.0785  -0.1338 1684 LYS A C     
3477 O  O     . LYS A 467 ? 0.4954 0.7257 0.5419 0.0573  0.0757  -0.1414 1684 LYS A O     
3478 C  CB    . LYS A 467 ? 0.5275 0.7393 0.5463 0.0306  0.0801  -0.1190 1684 LYS A CB    
3479 N  N     . SER A 468 ? 0.6665 0.9046 0.7220 0.0446  0.0757  -0.1295 1685 SER A N     
3480 C  CA    . SER A 468 ? 0.7416 0.9748 0.8077 0.0542  0.0681  -0.1321 1685 SER A CA    
3481 C  C     . SER A 468 ? 0.8879 1.0938 0.9444 0.0548  0.0607  -0.1257 1685 SER A C     
3482 O  O     . SER A 468 ? 0.9814 1.1768 1.0297 0.0458  0.0601  -0.1171 1685 SER A O     
3483 C  CB    . SER A 468 ? 0.7807 1.0287 0.8613 0.0520  0.0672  -0.1305 1685 SER A CB    
3484 O  OG    . SER A 468 ? 0.8271 1.0606 0.9049 0.0469  0.0616  -0.1218 1685 SER A OG    
3485 N  N     . LEU A 469 ? 0.9039 1.0980 0.9614 0.0651  0.0554  -0.1298 1686 LEU A N     
3486 C  CA    . LEU A 469 ? 0.8933 1.0622 0.9432 0.0659  0.0485  -0.1237 1686 LEU A CA    
3487 C  C     . LEU A 469 ? 0.8730 1.0388 0.9317 0.0690  0.0422  -0.1194 1686 LEU A C     
3488 O  O     . LEU A 469 ? 0.8757 1.0317 0.9298 0.0628  0.0395  -0.1111 1686 LEU A O     
3489 C  CB    . LEU A 469 ? 0.8973 1.0532 0.9434 0.0743  0.0459  -0.1295 1686 LEU A CB    
3490 C  CG    . LEU A 469 ? 1.0367 1.1980 1.0732 0.0710  0.0522  -0.1343 1686 LEU A CG    
3491 C  CD1   . LEU A 469 ? 1.0410 1.1916 1.0744 0.0793  0.0499  -0.1423 1686 LEU A CD1   
3492 C  CD2   . LEU A 469 ? 1.1085 1.2619 1.1316 0.0593  0.0540  -0.1256 1686 LEU A CD2   
3493 N  N     . CYS A 470 ? 0.8756 1.0496 0.9464 0.0791  0.0395  -0.1252 1687 CYS A N     
3494 C  CA    . CYS A 470 ? 0.7794 0.9534 0.8584 0.0821  0.0336  -0.1210 1687 CYS A CA    
3495 C  C     . CYS A 470 ? 0.7595 0.9481 0.8532 0.0933  0.0319  -0.1286 1687 CYS A C     
3496 O  O     . CYS A 470 ? 0.7745 0.9671 0.8713 0.1004  0.0340  -0.1366 1687 CYS A O     
3497 C  CB    . CYS A 470 ? 0.7001 0.8496 0.7721 0.0840  0.0267  -0.1138 1687 CYS A CB    
3498 S  SG    . CYS A 470 ? 0.8282 0.9630 0.9021 0.0968  0.0221  -0.1183 1687 CYS A SG    
3499 N  N     . ILE A 471 ? 0.6835 0.8798 0.7862 0.0953  0.0277  -0.1261 1688 ILE A N     
3500 C  CA    . ILE A 471 ? 0.6156 0.8216 0.7320 0.1074  0.0235  -0.1312 1688 ILE A CA    
3501 C  C     . ILE A 471 ? 0.6149 0.7980 0.7278 0.1158  0.0157  -0.1268 1688 ILE A C     
3502 O  O     . ILE A 471 ? 0.4207 0.5941 0.5296 0.1134  0.0108  -0.1186 1688 ILE A O     
3503 C  CB    . ILE A 471 ? 0.5158 0.7420 0.6436 0.1059  0.0221  -0.1308 1688 ILE A CB    
3504 C  CG1   . ILE A 471 ? 0.5218 0.7673 0.6516 0.0944  0.0300  -0.1327 1688 ILE A CG1   
3505 C  CG2   . ILE A 471 ? 0.4149 0.6549 0.5578 0.1187  0.0187  -0.1375 1688 ILE A CG2   
3506 C  CD1   . ILE A 471 ? 0.3977 0.6554 0.5340 0.0877  0.0283  -0.1293 1688 ILE A CD1   
3507 N  N     . PRO A 472 ? 0.6958 0.8697 0.8099 0.1253  0.0144  -0.1318 1689 PRO A N     
3508 C  CA    . PRO A 472 ? 0.6691 0.8184 0.7788 0.1315  0.0076  -0.1265 1689 PRO A CA    
3509 C  C     . PRO A 472 ? 0.6289 0.7794 0.7462 0.1391  0.0004  -0.1221 1689 PRO A C     
3510 O  O     . PRO A 472 ? 0.5279 0.6985 0.6572 0.1441  -0.0002 -0.1265 1689 PRO A O     
3511 C  CB    . PRO A 472 ? 0.6833 0.8270 0.7958 0.1405  0.0083  -0.1351 1689 PRO A CB    
3512 C  CG    . PRO A 472 ? 0.6998 0.8617 0.8128 0.1360  0.0165  -0.1436 1689 PRO A CG    
3513 C  CD    . PRO A 472 ? 0.7016 0.8868 0.8211 0.1306  0.0192  -0.1427 1689 PRO A CD    
3514 N  N     . PHE A 473 ? 0.7573 0.8869 0.8673 0.1395  -0.0049 -0.1131 1690 PHE A N     
3515 C  CA    . PHE A 473 ? 0.8167 0.9448 0.9320 0.1478  -0.0122 -0.1081 1690 PHE A CA    
3516 C  C     . PHE A 473 ? 0.8477 0.9719 0.9722 0.1619  -0.0159 -0.1127 1690 PHE A C     
3517 O  O     . PHE A 473 ? 0.9173 1.0492 1.0505 0.1708  -0.0211 -0.1119 1690 PHE A O     
3518 C  CB    . PHE A 473 ? 0.8887 0.9961 0.9928 0.1441  -0.0161 -0.0967 1690 PHE A CB    
3519 C  CG    . PHE A 473 ? 0.8378 0.9513 0.9353 0.1328  -0.0144 -0.0917 1690 PHE A CG    
3520 C  CD1   . PHE A 473 ? 0.7197 0.8558 0.8227 0.1273  -0.0106 -0.0967 1690 PHE A CD1   
3521 C  CD2   . PHE A 473 ? 0.7896 0.8864 0.8761 0.1276  -0.0164 -0.0822 1690 PHE A CD2   
3522 C  CE1   . PHE A 473 ? 0.6808 0.8211 0.7784 0.1169  -0.0093 -0.0926 1690 PHE A CE1   
3523 C  CE2   . PHE A 473 ? 0.6851 0.7871 0.7659 0.1177  -0.0150 -0.0784 1690 PHE A CE2   
3524 C  CZ    . PHE A 473 ? 0.6648 0.7877 0.7511 0.1124  -0.0116 -0.0837 1690 PHE A CZ    
3525 N  N     . GLU A 474 ? 0.7872 0.8985 0.9098 0.1643  -0.0139 -0.1174 1691 GLU A N     
3526 C  CA    . GLU A 474 ? 0.6672 0.7744 0.7992 0.1776  -0.0167 -0.1237 1691 GLU A CA    
3527 C  C     . GLU A 474 ? 0.6810 0.8109 0.8217 0.1795  -0.0110 -0.1363 1691 GLU A C     
3528 O  O     . GLU A 474 ? 0.6077 0.7355 0.7446 0.1766  -0.0058 -0.1431 1691 GLU A O     
3529 C  CB    . GLU A 474 ? 0.7750 0.8550 0.9008 0.1793  -0.0182 -0.1224 1691 GLU A CB    
3530 C  CG    . GLU A 474 ? 0.9656 1.0234 1.0835 0.1774  -0.0234 -0.1095 1691 GLU A CG    
3531 C  CD    . GLU A 474 ? 1.0403 1.0718 1.1530 0.1773  -0.0243 -0.1084 1691 GLU A CD    
3532 O  OE1   . GLU A 474 ? 1.0751 1.1050 1.1905 0.1798  -0.0217 -0.1183 1691 GLU A OE1   
3533 O  OE2   . GLU A 474 ? 1.0442 1.0574 1.1502 0.1744  -0.0275 -0.0978 1691 GLU A OE2   
3534 N  N     . GLN A 475 ? 0.7843 0.9373 0.9365 0.1842  -0.0117 -0.1394 1692 GLN A N     
3535 C  CA    . GLN A 475 ? 0.9178 1.0939 1.0805 0.1876  -0.0064 -0.1516 1692 GLN A CA    
3536 C  C     . GLN A 475 ? 1.0002 1.1681 1.1704 0.2014  -0.0085 -0.1595 1692 GLN A C     
3537 O  O     . GLN A 475 ? 0.8171 0.9682 0.9897 0.2108  -0.0157 -0.1552 1692 GLN A O     
3538 C  CB    . GLN A 475 ? 0.9123 1.1158 1.0872 0.1893  -0.0071 -0.1530 1692 GLN A CB    
3539 C  CG    . GLN A 475 ? 0.8550 1.0700 1.0244 0.1749  -0.0036 -0.1480 1692 GLN A CG    
3540 C  CD    . GLN A 475 ? 0.7730 1.0053 0.9421 0.1658  0.0061  -0.1549 1692 GLN A CD    
3541 O  OE1   . GLN A 475 ? 0.7963 1.0522 0.9778 0.1697  0.0098  -0.1638 1692 GLN A OE1   
3542 N  NE2   . GLN A 475 ? 0.6714 0.8927 0.8265 0.1536  0.0103  -0.1505 1692 GLN A NE2   
3543 N  N     . PRO A 476 ? 1.1695 1.3486 1.3432 0.2031  -0.0023 -0.1712 1693 PRO A N     
3544 C  CA    . PRO A 476 ? 1.2374 1.4084 1.4185 0.2166  -0.0043 -0.1801 1693 PRO A CA    
3545 C  C     . PRO A 476 ? 1.3330 1.5226 1.5319 0.2301  -0.0073 -0.1859 1693 PRO A C     
3546 O  O     . PRO A 476 ? 1.4396 1.6160 1.6451 0.2429  -0.0139 -0.1861 1693 PRO A O     
3547 C  CB    . PRO A 476 ? 1.1866 1.3640 1.3629 0.2121  0.0041  -0.1907 1693 PRO A CB    
3548 C  CG    . PRO A 476 ? 1.1797 1.3809 1.3534 0.1998  0.0111  -0.1896 1693 PRO A CG    
3549 C  CD    . PRO A 476 ? 1.1792 1.3771 1.3493 0.1925  0.0070  -0.1766 1693 PRO A CD    
3550 N  N     . ALA A 477 ? 1.2647 1.4847 1.4717 0.2274  -0.0028 -0.1901 1694 ALA A N     
3551 C  CA    . ALA A 477 ? 1.1738 1.4163 1.3991 0.2395  -0.0048 -0.1968 1694 ALA A CA    
3552 C  C     . ALA A 477 ? 1.1809 1.4454 1.4113 0.2332  -0.0055 -0.1914 1694 ALA A C     
3553 O  O     . ALA A 477 ? 1.2151 1.4811 1.4356 0.2188  -0.0021 -0.1852 1694 ALA A O     
3554 C  CB    . ALA A 477 ? 1.0932 1.3563 1.3272 0.2440  0.0028  -0.2117 1694 ALA A CB    
3555 N  N     . LYS A 478 ? 1.0943 1.3756 1.3405 0.2442  -0.0103 -0.1939 1695 LYS A N     
3556 C  CA    . LYS A 478 ? 1.0141 1.3194 1.2672 0.2386  -0.0111 -0.1907 1695 LYS A CA    
3557 C  C     . LYS A 478 ? 0.9027 1.2381 1.1632 0.2314  -0.0011 -0.2000 1695 LYS A C     
3558 O  O     . LYS A 478 ? 0.7853 1.1344 1.0558 0.2392  0.0033  -0.2113 1695 LYS A O     
3559 C  CB    . LYS A 478 ? 1.0421 1.3570 1.3102 0.2530  -0.0201 -0.1905 1695 LYS A CB    
3560 N  N     . ILE A 479 ? 0.8959 1.2405 1.1507 0.2161  0.0029  -0.1951 1696 ILE A N     
3561 C  CA    . ILE A 479 ? 0.8342 1.2074 1.0957 0.2075  0.0127  -0.2020 1696 ILE A CA    
3562 C  C     . ILE A 479 ? 0.9299 1.3321 1.2113 0.2132  0.0092  -0.2054 1696 ILE A C     
3563 O  O     . ILE A 479 ? 1.0177 1.4340 1.3022 0.2035  0.0090  -0.2013 1696 ILE A O     
3564 C  CB    . ILE A 479 ? 0.6183 0.9876 0.8658 0.1887  0.0183  -0.1951 1696 ILE A CB    
3565 N  N     . ASP A 480 ? 0.9770 1.3883 1.2727 0.2293  0.0062  -0.2133 1697 ASP A N     
3566 C  CA    . ASP A 480 ? 1.0812 1.5191 1.3969 0.2373  0.0013  -0.2167 1697 ASP A CA    
3567 C  C     . ASP A 480 ? 1.0794 1.5542 1.4097 0.2316  0.0107  -0.2259 1697 ASP A C     
3568 O  O     . ASP A 480 ? 1.0019 1.4871 1.3376 0.2365  0.0179  -0.2359 1697 ASP A O     
3569 C  CB    . ASP A 480 ? 1.1212 1.5529 1.4465 0.2574  -0.0060 -0.2210 1697 ASP A CB    
3570 N  N     . PRO A 481 ? 1.0590 1.5551 1.3968 0.2216  0.0108  -0.2234 1698 PRO A N     
3571 C  CA    . PRO A 481 ? 0.9744 1.5026 1.3232 0.2119  0.0213  -0.2301 1698 PRO A CA    
3572 C  C     . PRO A 481 ? 0.9871 1.5471 1.3592 0.2240  0.0233  -0.2420 1698 PRO A C     
3573 O  O     . PRO A 481 ? 0.9767 1.5685 1.3629 0.2166  0.0294  -0.2465 1698 PRO A O     
3574 C  CB    . PRO A 481 ? 0.8983 1.4366 1.2493 0.1987  0.0186  -0.2232 1698 PRO A CB    
3575 C  CG    . PRO A 481 ? 0.9276 1.4333 1.2614 0.1980  0.0094  -0.2121 1698 PRO A CG    
3576 C  CD    . PRO A 481 ? 1.0453 1.5341 1.3790 0.2165  0.0021  -0.2134 1698 PRO A CD    
3577 N  N     . LYS A 482 ? 1.0750 1.6277 1.4521 0.2420  0.0187  -0.2475 1699 LYS A N     
3578 C  CA    . LYS A 482 ? 1.0764 1.6606 1.4767 0.2543  0.0207  -0.2596 1699 LYS A CA    
3579 C  C     . LYS A 482 ? 0.9938 1.6021 1.3984 0.2460  0.0351  -0.2681 1699 LYS A C     
3580 O  O     . LYS A 482 ? 1.0256 1.6698 1.4493 0.2440  0.0397  -0.2742 1699 LYS A O     
3581 C  CB    . LYS A 482 ? 1.0910 1.6594 1.4938 0.2746  0.0147  -0.2645 1699 LYS A CB    
3582 N  N     . VAL A 483 ? 0.9311 1.5203 1.3171 0.2396  0.0425  -0.2675 1700 VAL A N     
3583 C  CA    . VAL A 483 ? 0.9295 1.5375 1.3144 0.2302  0.0566  -0.2736 1700 VAL A CA    
3584 C  C     . VAL A 483 ? 0.9246 1.5028 1.2832 0.2191  0.0608  -0.2671 1700 VAL A C     
3585 O  O     . VAL A 483 ? 0.9333 1.5190 1.2851 0.2125  0.0720  -0.2713 1700 VAL A O     
3586 C  CB    . VAL A 483 ? 0.8784 1.5062 1.2766 0.2442  0.0623  -0.2880 1700 VAL A CB    
3587 N  N     . ASP A 484 ? 0.8296 1.3743 1.1729 0.2174  0.0520  -0.2567 1701 ASP A N     
3588 C  CA    . ASP A 484 ? 0.8063 1.3227 1.1254 0.2071  0.0552  -0.2502 1701 ASP A CA    
3589 C  C     . ASP A 484 ? 0.8348 1.3646 1.1485 0.1877  0.0644  -0.2455 1701 ASP A C     
3590 O  O     . ASP A 484 ? 0.8961 1.4401 1.2184 0.1794  0.0628  -0.2407 1701 ASP A O     
3591 C  CB    . ASP A 484 ? 0.7430 1.2246 1.0490 0.2076  0.0442  -0.2392 1701 ASP A CB    
3592 C  CG    . ASP A 484 ? 0.7533 1.2067 1.0512 0.2205  0.0392  -0.2415 1701 ASP A CG    
3593 O  OD1   . ASP A 484 ? 0.8458 1.3002 1.1413 0.2249  0.0455  -0.2505 1701 ASP A OD1   
3594 O  OD2   . ASP A 484 ? 0.6673 1.0970 0.9606 0.2257  0.0290  -0.2340 1701 ASP A OD2   
3595 N  N     . LYS A 485 ? 0.7343 1.2585 1.0334 0.1802  0.0736  -0.2465 1702 LYS A N     
3596 C  CA    . LYS A 485 ? 0.5568 1.0934 0.8504 0.1622  0.0830  -0.2418 1702 LYS A CA    
3597 C  C     . LYS A 485 ? 0.7469 1.2547 1.0152 0.1524  0.0852  -0.2343 1702 LYS A C     
3598 O  O     . LYS A 485 ? 0.8648 1.3500 1.1211 0.1598  0.0828  -0.2365 1702 LYS A O     
3599 C  CB    . LYS A 485 ? 0.5026 1.0730 0.8073 0.1620  0.0951  -0.2519 1702 LYS A CB    
3600 N  N     . CYS A 486 ? 0.7413 1.2511 1.0026 0.1355  0.0898  -0.2259 1703 CYS A N     
3601 C  CA    . CYS A 486 ? 0.7251 1.2093 0.9632 0.1254  0.0918  -0.2180 1703 CYS A CA    
3602 C  C     . CYS A 486 ? 0.7121 1.1981 0.9401 0.1277  0.1004  -0.2250 1703 CYS A C     
3603 O  O     . CYS A 486 ? 0.7837 1.2971 1.0221 0.1308  0.1085  -0.2339 1703 CYS A O     
3604 C  CB    . CYS A 486 ? 0.7404 1.2299 0.9752 0.1072  0.0960  -0.2085 1703 CYS A CB    
3605 S  SG    . CYS A 486 ? 0.6616 1.1242 0.8689 0.0931  0.0999  -0.1982 1703 CYS A SG    
3606 N  N     . VAL A 487 ? 0.6523 1.1102 0.8598 0.1257  0.0989  -0.2210 1704 VAL A N     
3607 C  CA    . VAL A 487 ? 0.6285 1.0852 0.8253 0.1299  0.1051  -0.2288 1704 VAL A CA    
3608 C  C     . VAL A 487 ? 0.7241 1.1995 0.9140 0.1177  0.1177  -0.2279 1704 VAL A C     
3609 O  O     . VAL A 487 ? 0.7873 1.2730 0.9726 0.1218  0.1249  -0.2364 1704 VAL A O     
3610 C  CB    . VAL A 487 ? 0.6004 1.0211 0.7781 0.1314  0.0987  -0.2248 1704 VAL A CB    
3611 C  CG1   . VAL A 487 ? 0.4619 0.8655 0.6269 0.1169  0.0967  -0.2109 1704 VAL A CG1   
3612 C  CG2   . VAL A 487 ? 0.5149 0.9326 0.6797 0.1348  0.1045  -0.2329 1704 VAL A CG2   
3613 N  N     . HIS A 488 ? 0.6926 1.1754 0.8834 0.1034  0.1207  -0.2183 1705 HIS A N     
3614 C  CA    . HIS A 488 ? 0.6624 1.1624 0.8464 0.0920  0.1329  -0.2169 1705 HIS A CA    
3615 C  C     . HIS A 488 ? 0.6969 1.2349 0.9011 0.0937  0.1410  -0.2246 1705 HIS A C     
3616 O  O     . HIS A 488 ? 0.8160 1.3671 1.0397 0.0964  0.1369  -0.2258 1705 HIS A O     
3617 C  CB    . HIS A 488 ? 0.7576 1.2481 0.9332 0.0751  0.1335  -0.2031 1705 HIS A CB    
3618 C  CG    . HIS A 488 ? 0.8291 1.3299 0.9931 0.0627  0.1452  -0.1989 1705 HIS A CG    
3619 N  ND1   . HIS A 488 ? 0.8740 1.3669 1.0191 0.0637  0.1498  -0.2008 1705 HIS A ND1   
3620 C  CD2   . HIS A 488 ? 0.8522 1.3700 1.0206 0.0487  0.1529  -0.1922 1705 HIS A CD2   
3621 C  CE1   . HIS A 488 ? 0.8621 1.3668 0.9995 0.0513  0.1599  -0.1951 1705 HIS A CE1   
3622 N  NE2   . HIS A 488 ? 0.8473 1.3670 0.9990 0.0418  0.1622  -0.1896 1705 HIS A NE2   
3623 N  N     . PRO A 489 ? 0.6576 1.2143 0.8571 0.0921  0.1525  -0.2299 1706 PRO A N     
3624 C  CA    . PRO A 489 ? 0.6928 1.2876 0.9118 0.0944  0.1613  -0.2382 1706 PRO A CA    
3625 C  C     . PRO A 489 ? 0.7316 1.3465 0.9662 0.0819  0.1644  -0.2314 1706 PRO A C     
3626 O  O     . PRO A 489 ? 0.9026 1.5454 1.1599 0.0867  0.1662  -0.2384 1706 PRO A O     
3627 C  CB    . PRO A 489 ? 0.7157 1.3218 0.9207 0.0922  0.1734  -0.2423 1706 PRO A CB    
3628 C  CG    . PRO A 489 ? 0.6963 1.2709 0.8807 0.0992  0.1672  -0.2439 1706 PRO A CG    
3629 C  CD    . PRO A 489 ? 0.6945 1.2383 0.8717 0.0926  0.1567  -0.2316 1706 PRO A CD    
3630 N  N     . ALA A 490 ? 0.6963 1.2989 0.9206 0.0662  0.1651  -0.2186 1707 ALA A N     
3631 C  CA    . ALA A 490 ? 0.8201 1.4410 1.0589 0.0530  0.1685  -0.2123 1707 ALA A CA    
3632 C  C     . ALA A 490 ? 0.8931 1.5001 1.1408 0.0512  0.1566  -0.2066 1707 ALA A C     
3633 O  O     . ALA A 490 ? 0.9117 1.5319 1.1716 0.0398  0.1582  -0.2017 1707 ALA A O     
3634 C  CB    . ALA A 490 ? 0.8508 1.4696 1.0745 0.0359  0.1780  -0.2017 1707 ALA A CB    
3635 N  N     . CYS A 491 ? 0.9295 1.5115 1.1721 0.0621  0.1447  -0.2077 1708 CYS A N     
3636 C  CA    . CYS A 491 ? 0.9435 1.5121 1.1919 0.0595  0.1340  -0.2014 1708 CYS A CA    
3637 C  C     . CYS A 491 ? 1.1201 1.7140 1.3950 0.0650  0.1303  -0.2076 1708 CYS A C     
3638 O  O     . CYS A 491 ? 1.0463 1.6630 1.3354 0.0758  0.1330  -0.2181 1708 CYS A O     
3639 C  CB    . CYS A 491 ? 0.7659 1.3004 1.0007 0.0688  0.1227  -0.1995 1708 CYS A CB    
3640 S  SG    . CYS A 491 ? 0.7465 1.2699 0.9897 0.0672  0.1103  -0.1932 1708 CYS A SG    
3641 N  N     . GLY A 492 ? 1.3444 1.9325 1.6253 0.0583  0.1229  -0.2012 1709 GLY A N     
3642 C  CA    . GLY A 492 ? 1.3097 1.9150 1.6130 0.0637  0.1158  -0.2055 1709 GLY A CA    
3643 C  C     . GLY A 492 ? 1.1575 1.7430 1.4575 0.0801  0.1039  -0.2082 1709 GLY A C     
3644 O  O     . GLY A 492 ? 1.0458 1.6064 1.3368 0.0798  0.0944  -0.2015 1709 GLY A O     
3645 N  N     . ARG A 493 ? 1.1100 1.7076 1.4179 0.0946  0.1051  -0.2182 1710 ARG A N     
3646 C  CA    . ARG A 493 ? 1.1307 1.7073 1.4318 0.1110  0.0969  -0.2216 1710 ARG A CA    
3647 C  C     . ARG A 493 ? 1.1204 1.6870 1.4288 0.1190  0.0833  -0.2193 1710 ARG A C     
3648 O  O     . ARG A 493 ? 1.1920 1.7695 1.5150 0.1333  0.0778  -0.2263 1710 ARG A O     
3649 C  CB    . ARG A 493 ? 1.1264 1.7230 1.4377 0.1240  0.1023  -0.2339 1710 ARG A CB    
3650 N  N     . VAL A 494 ? 1.0535 1.5979 1.3501 0.1102  0.0775  -0.2092 1711 VAL A N     
3651 C  CA    . VAL A 494 ? 1.1435 1.6766 1.4438 0.1175  0.0646  -0.2061 1711 VAL A CA    
3652 C  C     . VAL A 494 ? 1.1325 1.6426 1.4247 0.1333  0.0578  -0.2077 1711 VAL A C     
3653 O  O     . VAL A 494 ? 1.2202 1.7336 1.5235 0.1466  0.0494  -0.2109 1711 VAL A O     
3654 C  CB    . VAL A 494 ? 1.2060 1.7203 1.4946 0.1044  0.0606  -0.1952 1711 VAL A CB    
3655 N  N     . ALA A 495 ? 0.9889 1.4766 1.2627 0.1323  0.0614  -0.2059 1712 ALA A N     
3656 C  CA    . ALA A 495 ? 0.8676 1.3274 1.1309 0.1444  0.0545  -0.2054 1712 ALA A CA    
3657 C  C     . ALA A 495 ? 0.7916 1.2331 1.0520 0.1463  0.0428  -0.1970 1712 ALA A C     
3658 O  O     . ALA A 495 ? 0.7622 1.2020 1.0309 0.1594  0.0343  -0.1987 1712 ALA A O     
3659 C  CB    . ALA A 495 ? 0.8062 1.2768 1.0817 0.1613  0.0541  -0.2164 1712 ALA A CB    
3660 N  N     . LYS A 496 ? 0.7028 1.1306 0.9507 0.1328  0.0427  -0.1877 1713 LYS A N     
3661 C  CA    . LYS A 496 ? 0.7382 1.1494 0.9815 0.1331  0.0326  -0.1796 1713 LYS A CA    
3662 C  C     . LYS A 496 ? 0.8612 1.2405 1.0907 0.1417  0.0264  -0.1754 1713 LYS A C     
3663 O  O     . LYS A 496 ? 0.8558 1.2251 1.0864 0.1494  0.0169  -0.1714 1713 LYS A O     
3664 C  CB    . LYS A 496 ? 0.6557 1.0628 0.8907 0.1164  0.0346  -0.1718 1713 LYS A CB    
3665 N  N     . PHE A 497 ? 0.9416 1.3053 1.1586 0.1407  0.0314  -0.1762 1714 PHE A N     
3666 C  CA    . PHE A 497 ? 1.0235 1.3567 1.2284 0.1480  0.0256  -0.1724 1714 PHE A CA    
3667 C  C     . PHE A 497 ? 1.1224 1.4467 1.3180 0.1480  0.0322  -0.1772 1714 PHE A C     
3668 O  O     . PHE A 497 ? 1.2697 1.6133 1.4697 0.1456  0.0406  -0.1844 1714 PHE A O     
3669 C  CB    . PHE A 497 ? 0.9623 1.2732 1.1534 0.1399  0.0207  -0.1608 1714 PHE A CB    
3670 C  CG    . PHE A 497 ? 0.9205 1.2360 1.1048 0.1236  0.0266  -0.1566 1714 PHE A CG    
3671 C  CD1   . PHE A 497 ? 0.9388 1.2554 1.1155 0.1157  0.0356  -0.1587 1714 PHE A CD1   
3672 C  CD2   . PHE A 497 ? 0.8883 1.2077 1.0741 0.1163  0.0232  -0.1508 1714 PHE A CD2   
3673 C  CE1   . PHE A 497 ? 0.9255 1.2457 1.0962 0.1009  0.0410  -0.1541 1714 PHE A CE1   
3674 C  CE2   . PHE A 497 ? 0.9054 1.2281 1.0859 0.1014  0.0286  -0.1471 1714 PHE A CE2   
3675 C  CZ    . PHE A 497 ? 0.8869 1.2096 1.0600 0.0937  0.0375  -0.1483 1714 PHE A CZ    
3676 N  N     . TYR A 498 ? 1.0062 1.3019 1.1891 0.1510  0.0284  -0.1734 1715 TYR A N     
3677 C  CA    . TYR A 498 ? 0.8436 1.1272 1.0147 0.1490  0.0337  -0.1767 1715 TYR A CA    
3678 C  C     . TYR A 498 ? 0.6634 0.9311 0.8177 0.1350  0.0354  -0.1674 1715 TYR A C     
3679 O  O     . TYR A 498 ? 0.5418 0.7946 0.6909 0.1318  0.0296  -0.1582 1715 TYR A O     
3680 C  CB    . TYR A 498 ? 0.8400 1.1025 1.0096 0.1617  0.0282  -0.1798 1715 TYR A CB    
3681 C  CG    . TYR A 498 ? 0.8619 1.1393 1.0470 0.1761  0.0281  -0.1910 1715 TYR A CG    
3682 C  CD1   . TYR A 498 ? 0.7580 1.0453 0.9439 0.1791  0.0351  -0.2021 1715 TYR A CD1   
3683 C  CD2   . TYR A 498 ? 0.9190 1.2012 1.1175 0.1871  0.0208  -0.1908 1715 TYR A CD2   
3684 C  CE1   . TYR A 498 ? 0.6429 0.9444 0.8434 0.1926  0.0352  -0.2130 1715 TYR A CE1   
3685 C  CE2   . TYR A 498 ? 0.8657 1.1617 1.0791 0.2008  0.0204  -0.2012 1715 TYR A CE2   
3686 C  CZ    . TYR A 498 ? 0.7878 1.0934 1.0025 0.2035  0.0278  -0.2124 1715 TYR A CZ    
3687 O  OH    . TYR A 498 ? 0.9038 1.2236 1.1339 0.2178  0.0275  -0.2233 1715 TYR A OH    
3688 N  N     . THR A 499 ? 0.5255 0.7982 0.6717 0.1266  0.0436  -0.1696 1716 THR A N     
3689 C  CA    . THR A 499 ? 0.4749 0.7312 0.6046 0.1146  0.0451  -0.1613 1716 THR A CA    
3690 C  C     . THR A 499 ? 0.5995 0.8416 0.7170 0.1156  0.0477  -0.1650 1716 THR A C     
3691 O  O     . THR A 499 ? 0.4990 0.7532 0.6190 0.1202  0.0529  -0.1746 1716 THR A O     
3692 C  CB    . THR A 499 ? 0.4938 0.7673 0.6229 0.1015  0.0521  -0.1583 1716 THR A CB    
3693 O  OG1   . THR A 499 ? 0.4287 0.7160 0.5703 0.1007  0.0491  -0.1561 1716 THR A OG1   
3694 C  CG2   . THR A 499 ? 0.5101 0.7648 0.6222 0.0898  0.0528  -0.1491 1716 THR A CG2   
3695 N  N     . LEU A 500 ? 0.7625 0.9798 0.8668 0.1113  0.0440  -0.1576 1717 LEU A N     
3696 C  CA    . LEU A 500 ? 0.7963 0.9986 0.8877 0.1100  0.0457  -0.1595 1717 LEU A CA    
3697 C  C     . LEU A 500 ? 0.9398 1.1483 1.0200 0.0970  0.0527  -0.1559 1717 LEU A C     
3698 O  O     . LEU A 500 ? 1.1140 1.3189 1.1900 0.0876  0.0522  -0.1465 1717 LEU A O     
3699 C  CB    . LEU A 500 ? 0.8288 1.0023 0.9130 0.1116  0.0380  -0.1530 1717 LEU A CB    
3700 C  CG    . LEU A 500 ? 0.9277 1.0825 1.0011 0.1127  0.0372  -0.1559 1717 LEU A CG    
3701 C  CD1   . LEU A 500 ? 0.9753 1.1267 1.0565 0.1259  0.0346  -0.1659 1717 LEU A CD1   
3702 C  CD2   . LEU A 500 ? 0.9290 1.0592 0.9935 0.1080  0.0317  -0.1458 1717 LEU A CD2   
3703 N  N     . PHE A 501 ? 0.7843 1.0017 0.8597 0.0972  0.0590  -0.1634 1718 PHE A N     
3704 C  CA    . PHE A 501 ? 0.7013 0.9272 0.7657 0.0869  0.0668  -0.1619 1718 PHE A CA    
3705 C  C     . PHE A 501 ? 0.8661 1.0770 0.9160 0.0876  0.0667  -0.1649 1718 PHE A C     
3706 O  O     . PHE A 501 ? 1.0398 1.2404 1.0910 0.0972  0.0627  -0.1720 1718 PHE A O     
3707 C  CB    . PHE A 501 ? 0.6000 0.8552 0.6720 0.0876  0.0755  -0.1696 1718 PHE A CB    
3708 C  CG    . PHE A 501 ? 0.6734 0.9480 0.7592 0.0840  0.0774  -0.1668 1718 PHE A CG    
3709 C  CD1   . PHE A 501 ? 0.6382 0.9255 0.7413 0.0939  0.0748  -0.1730 1718 PHE A CD1   
3710 C  CD2   . PHE A 501 ? 0.7254 1.0061 0.8077 0.0710  0.0815  -0.1584 1718 PHE A CD2   
3711 C  CE1   . PHE A 501 ? 0.5820 0.8886 0.6985 0.0906  0.0761  -0.1712 1718 PHE A CE1   
3712 C  CE2   . PHE A 501 ? 0.6749 0.9738 0.7709 0.0672  0.0830  -0.1566 1718 PHE A CE2   
3713 C  CZ    . PHE A 501 ? 0.6321 0.9445 0.7453 0.0770  0.0802  -0.1632 1718 PHE A CZ    
3714 N  N     . GLY A 502 ? 0.8716 1.0818 0.9080 0.0774  0.0711  -0.1598 1719 GLY A N     
3715 C  CA    . GLY A 502 ? 0.8203 1.0212 0.8423 0.0770  0.0720  -0.1631 1719 GLY A CA    
3716 C  C     . GLY A 502 ? 0.7662 0.9628 0.7743 0.0646  0.0747  -0.1532 1719 GLY A C     
3717 O  O     . GLY A 502 ? 0.6990 0.8947 0.7088 0.0571  0.0744  -0.1436 1719 GLY A O     
3718 N  N     . ARG A 503 ? 0.8320 1.0241 0.8259 0.0630  0.0765  -0.1557 1720 ARG A N     
3719 C  CA    . ARG A 503 ? 0.7981 0.9825 0.7778 0.0524  0.0775  -0.1457 1720 ARG A CA    
3720 C  C     . ARG A 503 ? 0.7759 0.9368 0.7551 0.0507  0.0692  -0.1375 1720 ARG A C     
3721 O  O     . ARG A 503 ? 0.8761 1.0231 0.8597 0.0580  0.0627  -0.1411 1720 ARG A O     
3722 C  CB    . ARG A 503 ? 0.9160 1.0992 0.8800 0.0523  0.0797  -0.1505 1720 ARG A CB    
3723 C  CG    . ARG A 503 ? 0.8957 1.1028 0.8584 0.0545  0.0884  -0.1592 1720 ARG A CG    
3724 C  CD    . ARG A 503 ? 0.7905 0.9995 0.7345 0.0500  0.0922  -0.1591 1720 ARG A CD    
3725 N  NE    . ARG A 503 ? 0.8203 1.0536 0.7626 0.0519  0.1012  -0.1670 1720 ARG A NE    
3726 C  CZ    . ARG A 503 ? 0.9023 1.1416 0.8436 0.0611  0.1020  -0.1806 1720 ARG A CZ    
3727 N  NH1   . ARG A 503 ? 0.9966 1.2180 0.9390 0.0688  0.0939  -0.1876 1720 ARG A NH1   
3728 N  NH2   . ARG A 503 ? 0.8464 1.1096 0.7859 0.0626  0.1111  -0.1875 1720 ARG A NH2   
3729 N  N     . SER A 504 ? 0.8100 0.9668 0.7845 0.0411  0.0697  -0.1264 1721 SER A N     
3730 C  CA    . SER A 504 ? 0.8753 1.0117 0.8493 0.0391  0.0625  -0.1183 1721 SER A CA    
3731 C  C     . SER A 504 ? 0.9016 1.0304 0.8626 0.0293  0.0634  -0.1088 1721 SER A C     
3732 O  O     . SER A 504 ? 0.7947 0.9346 0.7480 0.0234  0.0697  -0.1070 1721 SER A O     
3733 C  CB    . SER A 504 ? 0.8446 0.9833 0.8322 0.0396  0.0603  -0.1145 1721 SER A CB    
3734 O  OG    . SER A 504 ? 0.9090 1.0326 0.8941 0.0344  0.0558  -0.1046 1721 SER A OG    
3735 N  N     . TYR A 505 ? 0.9844 1.0943 0.9432 0.0278  0.0571  -0.1023 1722 TYR A N     
3736 C  CA    . TYR A 505 ? 0.9916 1.0919 0.9398 0.0195  0.0566  -0.0927 1722 TYR A CA    
3737 C  C     . TYR A 505 ? 1.1137 1.2196 1.0674 0.0129  0.0589  -0.0852 1722 TYR A C     
3738 O  O     . TYR A 505 ? 1.1519 1.2657 1.1178 0.0155  0.0590  -0.0873 1722 TYR A O     
3739 C  CB    . TYR A 505 ? 0.8983 0.9775 0.8438 0.0211  0.0490  -0.0895 1722 TYR A CB    
3740 C  CG    . TYR A 505 ? 0.8888 0.9610 0.8261 0.0245  0.0466  -0.0952 1722 TYR A CG    
3741 C  CD1   . TYR A 505 ? 0.9084 0.9760 0.8325 0.0194  0.0466  -0.0913 1722 TYR A CD1   
3742 C  CD2   . TYR A 505 ? 0.9041 0.9741 0.8470 0.0330  0.0440  -0.1047 1722 TYR A CD2   
3743 C  CE1   . TYR A 505 ? 0.8558 0.9177 0.7724 0.0223  0.0439  -0.0971 1722 TYR A CE1   
3744 C  CE2   . TYR A 505 ? 0.8643 0.9275 0.8002 0.0358  0.0414  -0.1107 1722 TYR A CE2   
3745 C  CZ    . TYR A 505 ? 0.7535 0.8132 0.6761 0.0303  0.0413  -0.1071 1722 TYR A CZ    
3746 O  OH    . TYR A 505 ? 0.7064 0.7605 0.6220 0.0327  0.0383  -0.1135 1722 TYR A OH    
3747 O  OXT   . TYR A 505 ? 1.1524 1.2551 1.0987 0.0050  0.0605  -0.0772 1722 TYR A OXT   
3748 N  N     . LEU B 6   ? 0.5335 0.5599 0.3764 0.0772  -0.0182 -0.1230 1223 LEU B N     
3749 C  CA    . LEU B 6   ? 0.7528 0.7653 0.6042 0.0752  -0.0137 -0.1205 1223 LEU B CA    
3750 C  C     . LEU B 6   ? 0.9107 0.9170 0.7639 0.0764  -0.0156 -0.1351 1223 LEU B C     
3751 O  O     . LEU B 6   ? 1.0212 1.0357 0.8648 0.0833  -0.0148 -0.1425 1223 LEU B O     
3752 C  CB    . LEU B 6   ? 0.7950 0.8107 0.6416 0.0801  -0.0064 -0.1093 1223 LEU B CB    
3753 C  CG    . LEU B 6   ? 0.7571 0.7599 0.6145 0.0761  -0.0023 -0.1001 1223 LEU B CG    
3754 C  CD1   . LEU B 6   ? 0.6873 0.6846 0.5527 0.0688  -0.0043 -0.0921 1223 LEU B CD1   
3755 C  CD2   . LEU B 6   ? 0.6661 0.6734 0.5197 0.0808  0.0046  -0.0904 1223 LEU B CD2   
3756 N  N     . GLU B 7   ? 0.9170 0.9083 0.7825 0.0699  -0.0176 -0.1387 1224 GLU B N     
3757 C  CA    . GLU B 7   ? 0.9965 0.9798 0.8661 0.0694  -0.0208 -0.1534 1224 GLU B CA    
3758 C  C     . GLU B 7   ? 1.1105 1.0857 0.9811 0.0743  -0.0164 -0.1555 1224 GLU B C     
3759 O  O     . GLU B 7   ? 1.1420 1.1190 1.0082 0.0795  -0.0174 -0.1679 1224 GLU B O     
3760 C  CB    . GLU B 7   ? 1.0459 1.0162 0.9286 0.0598  -0.0250 -0.1558 1224 GLU B CB    
3761 C  CG    . GLU B 7   ? 1.1871 1.1664 1.0704 0.0551  -0.0304 -0.1579 1224 GLU B CG    
3762 C  CD    . GLU B 7   ? 1.2806 1.2483 1.1778 0.0451  -0.0340 -0.1608 1224 GLU B CD    
3763 O  OE1   . GLU B 7   ? 1.2731 1.2251 1.1782 0.0421  -0.0336 -0.1646 1224 GLU B OE1   
3764 O  OE2   . GLU B 7   ? 1.2834 1.2578 1.1836 0.0403  -0.0371 -0.1590 1224 GLU B OE2   
3765 N  N     . ALA B 8   ? 1.0151 0.9819 0.8920 0.0727  -0.0118 -0.1442 1225 ALA B N     
3766 C  CA    . ALA B 8   ? 0.8838 0.8421 0.7645 0.0767  -0.0079 -0.1447 1225 ALA B CA    
3767 C  C     . ALA B 8   ? 0.8774 0.8470 0.7505 0.0840  -0.0014 -0.1370 1225 ALA B C     
3768 O  O     . ALA B 8   ? 0.9082 0.8890 0.7751 0.0845  0.0008  -0.1275 1225 ALA B O     
3769 C  CB    . ALA B 8   ? 0.8524 0.7941 0.7455 0.0701  -0.0076 -0.1372 1225 ALA B CB    
3770 N  N     . THR B 9   ? 0.7819 0.7484 0.6566 0.0897  0.0019  -0.1411 1226 THR B N     
3771 C  CA    . THR B 9   ? 0.7725 0.7496 0.6421 0.0963  0.0088  -0.1341 1226 THR B CA    
3772 C  C     . THR B 9   ? 0.8116 0.7794 0.6917 0.0948  0.0123  -0.1242 1226 THR B C     
3773 O  O     . THR B 9   ? 0.7312 0.6835 0.6213 0.0917  0.0099  -0.1265 1226 THR B O     
3774 C  CB    . THR B 9   ? 0.6968 0.6817 0.5596 0.1053  0.0110  -0.1457 1226 THR B CB    
3775 O  OG1   . THR B 9   ? 0.6516 0.6233 0.5208 0.1056  0.0070  -0.1592 1226 THR B OG1   
3776 C  CG2   . THR B 9   ? 0.7424 0.7440 0.5907 0.1090  0.0103  -0.1498 1226 THR B CG2   
3777 N  N     . LYS B 10  ? 0.8475 0.8254 0.7251 0.0972  0.0180  -0.1131 1227 LYS B N     
3778 C  CA    . LYS B 10  ? 0.8448 0.8163 0.7322 0.0956  0.0211  -0.1029 1227 LYS B CA    
3779 C  C     . LYS B 10  ? 0.9538 0.9186 0.8481 0.1007  0.0226  -0.1093 1227 LYS B C     
3780 O  O     . LYS B 10  ? 0.9308 0.8839 0.8354 0.0981  0.0219  -0.1048 1227 LYS B O     
3781 C  CB    . LYS B 10  ? 0.6932 0.6780 0.5767 0.0970  0.0268  -0.0906 1227 LYS B CB    
3782 C  CG    . LYS B 10  ? 0.5734 0.5525 0.4667 0.0929  0.0287  -0.0781 1227 LYS B CG    
3783 C  CD    . LYS B 10  ? 0.5829 0.5750 0.4725 0.0936  0.0340  -0.0666 1227 LYS B CD    
3784 C  CE    . LYS B 10  ? 0.6753 0.6630 0.5752 0.0901  0.0359  -0.0556 1227 LYS B CE    
3785 N  NZ    . LYS B 10  ? 0.6693 0.6677 0.5665 0.0891  0.0402  -0.0439 1227 LYS B NZ    
3786 N  N     . GLU B 11  ? 1.1036 1.0759 0.9923 0.1083  0.0244  -0.1199 1228 GLU B N     
3787 C  CA    . GLU B 11  ? 1.2112 1.1791 1.1067 0.1144  0.0265  -0.1258 1228 GLU B CA    
3788 C  C     . GLU B 11  ? 1.1872 1.1364 1.0899 0.1129  0.0207  -0.1361 1228 GLU B C     
3789 O  O     . GLU B 11  ? 1.2181 1.1553 1.1314 0.1131  0.0202  -0.1343 1228 GLU B O     
3790 C  CB    . GLU B 11  ? 1.2187 1.2028 1.1054 0.1237  0.0313  -0.1333 1228 GLU B CB    
3791 C  CG    . GLU B 11  ? 1.1218 1.1245 1.0002 0.1248  0.0371  -0.1229 1228 GLU B CG    
3792 C  CD    . GLU B 11  ? 1.1517 1.1647 1.0159 0.1249  0.0355  -0.1265 1228 GLU B CD    
3793 O  OE1   . GLU B 11  ? 1.1728 1.1816 1.0330 0.1257  0.0305  -0.1395 1228 GLU B OE1   
3794 O  OE2   . GLU B 11  ? 1.2289 1.2541 1.0861 0.1241  0.0389  -0.1163 1228 GLU B OE2   
3795 N  N     . ASP B 12  ? 1.0654 1.0122 0.9629 0.1114  0.0160  -0.1469 1229 ASP B N     
3796 C  CA    . ASP B 12  ? 1.0446 0.9729 0.9493 0.1082  0.0101  -0.1561 1229 ASP B CA    
3797 C  C     . ASP B 12  ? 1.1134 1.0331 1.0211 0.0977  0.0058  -0.1494 1229 ASP B C     
3798 O  O     . ASP B 12  ? 1.2978 1.2269 1.1983 0.0944  0.0044  -0.1484 1229 ASP B O     
3799 C  CB    . ASP B 12  ? 1.2129 1.1443 1.1110 0.1129  0.0076  -0.1732 1229 ASP B CB    
3800 C  CG    . ASP B 12  ? 1.4335 1.3808 1.3239 0.1234  0.0131  -0.1783 1229 ASP B CG    
3801 O  OD1   . ASP B 12  ? 1.4787 1.4208 1.3743 0.1300  0.0144  -0.1860 1229 ASP B OD1   
3802 O  OD2   . ASP B 12  ? 1.4895 1.4550 1.3691 0.1252  0.0166  -0.1738 1229 ASP B OD2   
3803 N  N     . ASN B 13  ? 1.0176 0.9202 0.9361 0.0927  0.0036  -0.1449 1230 ASN B N     
3804 C  CA    . ASN B 13  ? 1.0668 0.9602 0.9895 0.0826  0.0001  -0.1379 1230 ASN B CA    
3805 C  C     . ASN B 13  ? 0.8994 0.8036 0.8189 0.0792  0.0030  -0.1237 1230 ASN B C     
3806 O  O     . ASN B 13  ? 0.7866 0.6991 0.7005 0.0754  0.0017  -0.1220 1230 ASN B O     
3807 C  CB    . ASN B 13  ? 1.0829 0.9736 1.0038 0.0778  -0.0052 -0.1483 1230 ASN B CB    
3808 C  CG    . ASN B 13  ? 1.1768 1.0546 1.1053 0.0674  -0.0088 -0.1430 1230 ASN B CG    
3809 O  OD1   . ASN B 13  ? 1.2240 1.0928 1.1587 0.0642  -0.0076 -0.1325 1230 ASN B OD1   
3810 N  ND2   . ASN B 13  ? 1.2671 1.1452 1.1949 0.0620  -0.0131 -0.1500 1230 ASN B ND2   
3811 N  N     . LEU B 14  ? 0.7961 0.6987 0.7203 0.0804  0.0063  -0.1134 1231 LEU B N     
3812 C  CA    . LEU B 14  ? 0.7412 0.6511 0.6647 0.0772  0.0090  -0.0997 1231 LEU B CA    
3813 C  C     . LEU B 14  ? 0.8934 0.7956 0.8198 0.0678  0.0058  -0.0933 1231 LEU B C     
3814 O  O     . LEU B 14  ? 1.0237 0.9352 0.9458 0.0650  0.0066  -0.0869 1231 LEU B O     
3815 C  CB    . LEU B 14  ? 0.6633 0.5722 0.5928 0.0807  0.0125  -0.0919 1231 LEU B CB    
3816 C  CG    . LEU B 14  ? 0.7042 0.6233 0.6328 0.0789  0.0160  -0.0789 1231 LEU B CG    
3817 C  CD1   . LEU B 14  ? 0.7785 0.7153 0.6982 0.0835  0.0201  -0.0793 1231 LEU B CD1   
3818 C  CD2   . LEU B 14  ? 0.5618 0.4781 0.4984 0.0807  0.0182  -0.0714 1231 LEU B CD2   
3819 N  N     . PRO B 15  ? 0.9213 0.8074 0.8550 0.0630  0.0025  -0.0941 1232 PRO B N     
3820 C  CA    . PRO B 15  ? 0.8269 0.7078 0.7632 0.0542  0.0005  -0.0868 1232 PRO B CA    
3821 C  C     . PRO B 15  ? 0.7377 0.6261 0.6693 0.0500  -0.0017 -0.0906 1232 PRO B C     
3822 O  O     . PRO B 15  ? 0.7245 0.6169 0.6554 0.0450  -0.0017 -0.0831 1232 PRO B O     
3823 C  CB    . PRO B 15  ? 0.8707 0.7329 0.8151 0.0506  -0.0024 -0.0884 1232 PRO B CB    
3824 C  CG    . PRO B 15  ? 0.9335 0.7910 0.8787 0.0566  -0.0034 -0.1001 1232 PRO B CG    
3825 C  CD    . PRO B 15  ? 0.9939 0.8654 0.9340 0.0653  0.0007  -0.1007 1232 PRO B CD    
3826 N  N     . ASP B 16  ? 0.7572 0.6488 0.6852 0.0527  -0.0037 -0.1025 1233 ASP B N     
3827 C  CA    . ASP B 16  ? 0.8912 0.7907 0.8153 0.0491  -0.0066 -0.1069 1233 ASP B CA    
3828 C  C     . ASP B 16  ? 0.9156 0.8331 0.8297 0.0542  -0.0045 -0.1056 1233 ASP B C     
3829 O  O     . ASP B 16  ? 0.9241 0.8499 0.8350 0.0512  -0.0061 -0.1039 1233 ASP B O     
3830 C  CB    . ASP B 16  ? 0.9700 0.8629 0.8963 0.0478  -0.0108 -0.1206 1233 ASP B CB    
3831 C  CG    . ASP B 16  ? 1.1114 0.9868 1.0476 0.0411  -0.0130 -0.1198 1233 ASP B CG    
3832 O  OD1   . ASP B 16  ? 1.1199 0.9888 1.0596 0.0397  -0.0106 -0.1092 1233 ASP B OD1   
3833 O  OD2   . ASP B 16  ? 1.2416 1.1106 1.1818 0.0364  -0.0169 -0.1285 1233 ASP B OD2   
3834 N  N     . TRP B 17  ? 0.8879 0.8117 0.7979 0.0617  -0.0005 -0.1046 1234 TRP B N     
3835 C  CA    . TRP B 17  ? 0.7385 0.6780 0.6400 0.0655  0.0028  -0.0984 1234 TRP B CA    
3836 C  C     . TRP B 17  ? 0.5752 0.5155 0.4792 0.0608  0.0042  -0.0850 1234 TRP B C     
3837 O  O     . TRP B 17  ? 0.6668 0.6162 0.5659 0.0596  0.0036  -0.0814 1234 TRP B O     
3838 C  CB    . TRP B 17  ? 0.8096 0.7552 0.7080 0.0736  0.0076  -0.0986 1234 TRP B CB    
3839 C  CG    . TRP B 17  ? 0.8887 0.8489 0.7798 0.0767  0.0118  -0.0899 1234 TRP B CG    
3840 C  CD1   . TRP B 17  ? 0.9728 0.9470 0.8530 0.0806  0.0123  -0.0923 1234 TRP B CD1   
3841 C  CD2   . TRP B 17  ? 0.9280 0.8901 0.8222 0.0761  0.0159  -0.0772 1234 TRP B CD2   
3842 N  NE1   . TRP B 17  ? 1.0102 0.9941 0.8867 0.0822  0.0168  -0.0810 1234 TRP B NE1   
3843 C  CE2   . TRP B 17  ? 0.9787 0.9554 0.8642 0.0793  0.0191  -0.0720 1234 TRP B CE2   
3844 C  CE3   . TRP B 17  ? 0.8743 0.8273 0.7778 0.0731  0.0170  -0.0697 1234 TRP B CE3   
3845 C  CZ2   . TRP B 17  ? 0.9056 0.8871 0.7924 0.0791  0.0234  -0.0599 1234 TRP B CZ2   
3846 C  CZ3   . TRP B 17  ? 0.8039 0.7627 0.7085 0.0731  0.0210  -0.0586 1234 TRP B CZ3   
3847 C  CH2   . TRP B 17  ? 0.8909 0.8634 0.7878 0.0758  0.0242  -0.0538 1234 TRP B CH2   
3848 N  N     . TYR B 18  ? 0.5093 0.4399 0.4208 0.0585  0.0057  -0.0780 1235 TYR B N     
3849 C  CA    . TYR B 18  ? 0.6485 0.5788 0.5626 0.0538  0.0067  -0.0664 1235 TYR B CA    
3850 C  C     . TYR B 18  ? 0.7167 0.6455 0.6319 0.0471  0.0030  -0.0667 1235 TYR B C     
3851 O  O     . TYR B 18  ? 0.7413 0.6771 0.6541 0.0455  0.0033  -0.0604 1235 TYR B O     
3852 C  CB    . TYR B 18  ? 0.6421 0.5616 0.5643 0.0524  0.0079  -0.0606 1235 TYR B CB    
3853 C  CG    . TYR B 18  ? 0.7465 0.6648 0.6719 0.0481  0.0089  -0.0491 1235 TYR B CG    
3854 C  CD1   . TYR B 18  ? 0.7653 0.6934 0.6882 0.0500  0.0121  -0.0412 1235 TYR B CD1   
3855 C  CD2   . TYR B 18  ? 0.8259 0.7328 0.7570 0.0421  0.0068  -0.0462 1235 TYR B CD2   
3856 C  CE1   . TYR B 18  ? 0.8094 0.7354 0.7357 0.0460  0.0127  -0.0317 1235 TYR B CE1   
3857 C  CE2   . TYR B 18  ? 0.8776 0.7836 0.8112 0.0385  0.0075  -0.0367 1235 TYR B CE2   
3858 C  CZ    . TYR B 18  ? 0.8597 0.7750 0.7911 0.0404  0.0102  -0.0300 1235 TYR B CZ    
3859 O  OH    . TYR B 18  ? 0.6599 0.5733 0.5943 0.0366  0.0104  -0.0218 1235 TYR B OH    
3860 N  N     . SER B 19  ? 0.7324 0.6521 0.6518 0.0432  -0.0006 -0.0742 1236 SER B N     
3861 C  CA    . SER B 19  ? 0.7316 0.6510 0.6531 0.0365  -0.0038 -0.0749 1236 SER B CA    
3862 C  C     . SER B 19  ? 0.7516 0.6853 0.6663 0.0385  -0.0053 -0.0782 1236 SER B C     
3863 O  O     . SER B 19  ? 0.7407 0.6804 0.6547 0.0360  -0.0058 -0.0729 1236 SER B O     
3864 C  CB    . SER B 19  ? 0.5713 0.4791 0.4990 0.0319  -0.0071 -0.0830 1236 SER B CB    
3865 O  OG    . SER B 19  ? 0.5456 0.4572 0.4748 0.0264  -0.0104 -0.0867 1236 SER B OG    
3866 N  N     . GLN B 20  ? 0.7452 0.6845 0.6541 0.0439  -0.0061 -0.0869 1237 GLN B N     
3867 C  CA    . GLN B 20  ? 0.7721 0.7255 0.6732 0.0468  -0.0079 -0.0904 1237 GLN B CA    
3868 C  C     . GLN B 20  ? 0.8217 0.7847 0.7173 0.0496  -0.0049 -0.0795 1237 GLN B C     
3869 O  O     . GLN B 20  ? 0.9284 0.9001 0.8208 0.0490  -0.0069 -0.0778 1237 GLN B O     
3870 C  CB    . GLN B 20  ? 0.7159 0.6739 0.6102 0.0533  -0.0083 -0.1008 1237 GLN B CB    
3871 C  CG    . GLN B 20  ? 0.7707 0.7236 0.6686 0.0504  -0.0133 -0.1139 1237 GLN B CG    
3872 C  CD    . GLN B 20  ? 0.8606 0.8251 0.7543 0.0496  -0.0178 -0.1194 1237 GLN B CD    
3873 O  OE1   . GLN B 20  ? 1.0001 0.9771 0.8838 0.0558  -0.0183 -0.1232 1237 GLN B OE1   
3874 N  NE2   . GLN B 20  ? 0.8398 0.8015 0.7410 0.0421  -0.0211 -0.1195 1237 GLN B NE2   
3875 N  N     . VAL B 21  ? 0.6677 0.6296 0.5626 0.0529  -0.0002 -0.0724 1238 VAL B N     
3876 C  CA    . VAL B 21  ? 0.6675 0.6378 0.5577 0.0554  0.0029  -0.0621 1238 VAL B CA    
3877 C  C     . VAL B 21  ? 0.6392 0.6063 0.5348 0.0497  0.0020  -0.0541 1238 VAL B C     
3878 O  O     . VAL B 21  ? 0.5896 0.5644 0.4817 0.0502  0.0012  -0.0499 1238 VAL B O     
3879 C  CB    . VAL B 21  ? 0.6845 0.6549 0.5744 0.0596  0.0082  -0.0568 1238 VAL B CB    
3880 C  CG1   . VAL B 21  ? 0.7067 0.6819 0.5956 0.0597  0.0114  -0.0446 1238 VAL B CG1   
3881 C  CG2   . VAL B 21  ? 0.6661 0.6447 0.5481 0.0665  0.0097  -0.0639 1238 VAL B CG2   
3882 N  N     . ILE B 22  ? 0.6176 0.5734 0.5216 0.0446  0.0020  -0.0521 1239 ILE B N     
3883 C  CA    . ILE B 22  ? 0.6924 0.6460 0.6008 0.0398  0.0017  -0.0447 1239 ILE B CA    
3884 C  C     . ILE B 22  ? 0.7620 0.7195 0.6712 0.0362  -0.0023 -0.0487 1239 ILE B C     
3885 O  O     . ILE B 22  ? 0.9634 0.9226 0.8747 0.0336  -0.0026 -0.0432 1239 ILE B O     
3886 C  CB    . ILE B 22  ? 0.5879 0.5293 0.5039 0.0353  0.0027  -0.0412 1239 ILE B CB    
3887 C  CG1   . ILE B 22  ? 0.6816 0.6142 0.6021 0.0314  0.0000  -0.0491 1239 ILE B CG1   
3888 C  CG2   . ILE B 22  ? 0.4314 0.3712 0.3474 0.0392  0.0063  -0.0368 1239 ILE B CG2   
3889 C  CD1   . ILE B 22  ? 0.7211 0.6418 0.6484 0.0265  0.0004  -0.0450 1239 ILE B CD1   
3890 N  N     . THR B 23  ? 0.5718 0.5310 0.4802 0.0360  -0.0055 -0.0587 1240 THR B N     
3891 C  CA    . THR B 23  ? 0.5309 0.4957 0.4410 0.0327  -0.0096 -0.0630 1240 THR B CA    
3892 C  C     . THR B 23  ? 0.5979 0.5766 0.4999 0.0380  -0.0116 -0.0649 1240 THR B C     
3893 O  O     . THR B 23  ? 0.5573 0.5430 0.4597 0.0373  -0.0134 -0.0620 1240 THR B O     
3894 C  CB    . THR B 23  ? 0.4955 0.4541 0.4112 0.0281  -0.0126 -0.0729 1240 THR B CB    
3895 O  OG1   . THR B 23  ? 0.5631 0.5209 0.4744 0.0326  -0.0129 -0.0804 1240 THR B OG1   
3896 C  CG2   . THR B 23  ? 0.4478 0.3931 0.3718 0.0218  -0.0111 -0.0693 1240 THR B CG2   
3897 N  N     . LYS B 24  ? 0.5599 0.5432 0.4545 0.0435  -0.0117 -0.0704 1241 LYS B N     
3898 C  CA    . LYS B 24  ? 0.5717 0.5686 0.4570 0.0491  -0.0135 -0.0712 1241 LYS B CA    
3899 C  C     . LYS B 24  ? 0.6802 0.6813 0.5606 0.0529  -0.0099 -0.0592 1241 LYS B C     
3900 O  O     . LYS B 24  ? 0.7637 0.7753 0.6371 0.0570  -0.0115 -0.0571 1241 LYS B O     
3901 C  CB    . LYS B 24  ? 0.4759 0.4773 0.3536 0.0542  -0.0142 -0.0805 1241 LYS B CB    
3902 C  CG    . LYS B 24  ? 0.6794 0.6758 0.5626 0.0502  -0.0183 -0.0932 1241 LYS B CG    
3903 C  CD    . LYS B 24  ? 0.8117 0.8182 0.6872 0.0545  -0.0224 -0.1047 1241 LYS B CD    
3904 C  CE    . LYS B 24  ? 0.9604 0.9583 0.8425 0.0506  -0.0255 -0.1176 1241 LYS B CE    
3905 N  NZ    . LYS B 24  ? 1.0619 1.0687 0.9393 0.0527  -0.0311 -0.1311 1241 LYS B NZ    
3906 N  N     . GLY B 25  ? 0.6830 0.6761 0.5673 0.0515  -0.0055 -0.0512 1242 GLY B N     
3907 C  CA    . GLY B 25  ? 0.6445 0.6396 0.5269 0.0535  -0.0022 -0.0396 1242 GLY B CA    
3908 C  C     . GLY B 25  ? 0.7858 0.7779 0.6747 0.0493  -0.0033 -0.0338 1242 GLY B C     
3909 O  O     . GLY B 25  ? 0.8398 0.8326 0.7279 0.0507  -0.0011 -0.0246 1242 GLY B O     
3910 N  N     . GLU B 26  ? 0.9569 0.9456 0.8526 0.0440  -0.0064 -0.0392 1243 GLU B N     
3911 C  CA    . GLU B 26  ? 0.8835 0.8720 0.7850 0.0404  -0.0078 -0.0354 1243 GLU B CA    
3912 C  C     . GLU B 26  ? 0.9160 0.8961 0.8221 0.0380  -0.0042 -0.0269 1243 GLU B C     
3913 O  O     . GLU B 26  ? 1.0764 1.0580 0.9834 0.0386  -0.0038 -0.0204 1243 GLU B O     
3914 C  CB    . GLU B 26  ? 0.8491 0.8482 0.7458 0.0448  -0.0101 -0.0326 1243 GLU B CB    
3915 C  CG    . GLU B 26  ? 0.9040 0.9131 0.7956 0.0477  -0.0143 -0.0407 1243 GLU B CG    
3916 C  CD    . GLU B 26  ? 1.0102 1.0294 0.8976 0.0523  -0.0170 -0.0370 1243 GLU B CD    
3917 O  OE1   . GLU B 26  ? 1.0535 1.0826 0.9343 0.0563  -0.0205 -0.0420 1243 GLU B OE1   
3918 O  OE2   . GLU B 26  ? 1.0622 1.0792 0.9527 0.0521  -0.0158 -0.0290 1243 GLU B OE2   
3919 N  N     . MET B 27  ? 0.7979 0.7691 0.7071 0.0355  -0.0019 -0.0272 1244 MET B N     
3920 C  CA    . MET B 27  ? 0.5695 0.5328 0.4834 0.0328  0.0008  -0.0201 1244 MET B CA    
3921 C  C     . MET B 27  ? 0.5513 0.5066 0.4720 0.0265  0.0001  -0.0224 1244 MET B C     
3922 O  O     . MET B 27  ? 0.6540 0.6050 0.5785 0.0237  0.0013  -0.0172 1244 MET B O     
3923 C  CB    . MET B 27  ? 0.5361 0.4964 0.4482 0.0356  0.0043  -0.0167 1244 MET B CB    
3924 C  CG    . MET B 27  ? 0.6302 0.5979 0.5363 0.0409  0.0061  -0.0116 1244 MET B CG    
3925 S  SD    . MET B 27  ? 0.7545 0.7216 0.6586 0.0444  0.0103  -0.0100 1244 MET B SD    
3926 C  CE    . MET B 27  ? 0.6992 0.6597 0.6100 0.0416  0.0130  -0.0006 1244 MET B CE    
3927 N  N     . ILE B 28  ? 0.5505 0.5037 0.4727 0.0242  -0.0017 -0.0299 1245 ILE B N     
3928 C  CA    . ILE B 28  ? 0.4982 0.4431 0.4265 0.0181  -0.0022 -0.0323 1245 ILE B CA    
3929 C  C     . ILE B 28  ? 0.5455 0.4949 0.4767 0.0145  -0.0054 -0.0390 1245 ILE B C     
3930 O  O     . ILE B 28  ? 0.6282 0.5860 0.5563 0.0173  -0.0078 -0.0443 1245 ILE B O     
3931 C  CB    . ILE B 28  ? 0.6339 0.5704 0.5622 0.0188  -0.0014 -0.0352 1245 ILE B CB    
3932 C  CG1   . ILE B 28  ? 0.6682 0.6005 0.5960 0.0212  0.0017  -0.0279 1245 ILE B CG1   
3933 C  CG2   . ILE B 28  ? 0.4939 0.4213 0.4278 0.0129  -0.0029 -0.0400 1245 ILE B CG2   
3934 C  CD1   . ILE B 28  ? 0.6108 0.5429 0.5409 0.0187  0.0026  -0.0207 1245 ILE B CD1   
3935 N  N     . GLU B 29  ? 0.4662 0.4112 0.4034 0.0081  -0.0054 -0.0386 1246 GLU B N     
3936 C  CA    . GLU B 29  ? 0.5015 0.4471 0.4438 0.0029  -0.0077 -0.0457 1246 GLU B CA    
3937 C  C     . GLU B 29  ? 0.5713 0.5043 0.5180 -0.0027 -0.0063 -0.0444 1246 GLU B C     
3938 O  O     . GLU B 29  ? 0.6372 0.5653 0.5844 -0.0042 -0.0039 -0.0374 1246 GLU B O     
3939 C  CB    . GLU B 29  ? 0.6683 0.6237 0.6144 0.0003  -0.0091 -0.0465 1246 GLU B CB    
3940 C  CG    . GLU B 29  ? 0.6532 0.6170 0.6017 -0.0008 -0.0131 -0.0558 1246 GLU B CG    
3941 C  CD    . GLU B 29  ? 0.7376 0.7099 0.6789 0.0066  -0.0154 -0.0590 1246 GLU B CD    
3942 O  OE1   . GLU B 29  ? 0.7752 0.7454 0.7136 0.0084  -0.0168 -0.0650 1246 GLU B OE1   
3943 O  OE2   . GLU B 29  ? 0.7495 0.7305 0.6876 0.0111  -0.0158 -0.0552 1246 GLU B OE2   
3944 N  N     . TYR B 30  ? 0.5290 0.4562 0.4782 -0.0052 -0.0079 -0.0508 1247 TYR B N     
3945 C  CA    . TYR B 30  ? 0.5288 0.4428 0.4822 -0.0104 -0.0068 -0.0490 1247 TYR B CA    
3946 C  C     . TYR B 30  ? 0.5848 0.4997 0.5436 -0.0178 -0.0059 -0.0461 1247 TYR B C     
3947 O  O     . TYR B 30  ? 0.5795 0.5050 0.5411 -0.0199 -0.0070 -0.0490 1247 TYR B O     
3948 C  CB    . TYR B 30  ? 0.4424 0.3488 0.3983 -0.0117 -0.0089 -0.0570 1247 TYR B CB    
3949 C  CG    . TYR B 30  ? 0.4468 0.3491 0.3978 -0.0046 -0.0088 -0.0590 1247 TYR B CG    
3950 C  CD1   . TYR B 30  ? 0.5833 0.4770 0.5328 -0.0021 -0.0065 -0.0527 1247 TYR B CD1   
3951 C  CD2   . TYR B 30  ? 0.4526 0.3609 0.4005 -0.0002 -0.0111 -0.0676 1247 TYR B CD2   
3952 C  CE1   . TYR B 30  ? 0.5399 0.4316 0.4860 0.0046  -0.0061 -0.0547 1247 TYR B CE1   
3953 C  CE2   . TYR B 30  ? 0.4570 0.3632 0.4004 0.0065  -0.0105 -0.0697 1247 TYR B CE2   
3954 C  CZ    . TYR B 30  ? 0.5424 0.4404 0.4853 0.0089  -0.0078 -0.0632 1247 TYR B CZ    
3955 O  OH    . TYR B 30  ? 0.6774 0.5744 0.6166 0.0158  -0.0068 -0.0655 1247 TYR B OH    
3956 N  N     . TYR B 31  ? 0.6766 0.5812 0.6370 -0.0217 -0.0038 -0.0405 1248 TYR B N     
3957 C  CA    . TYR B 31  ? 0.6876 0.5940 0.6511 -0.0276 -0.0019 -0.0359 1248 TYR B CA    
3958 C  C     . TYR B 31  ? 0.6822 0.5765 0.6499 -0.0346 -0.0012 -0.0345 1248 TYR B C     
3959 O  O     . TYR B 31  ? 0.7363 0.6186 0.7031 -0.0334 -0.0017 -0.0341 1248 TYR B O     
3960 C  CB    . TYR B 31  ? 0.6132 0.5210 0.5722 -0.0245 0.0003  -0.0280 1248 TYR B CB    
3961 C  CG    . TYR B 31  ? 0.5900 0.5026 0.5510 -0.0291 0.0023  -0.0241 1248 TYR B CG    
3962 C  CD1   . TYR B 31  ? 0.4094 0.3349 0.3729 -0.0295 0.0021  -0.0269 1248 TYR B CD1   
3963 C  CD2   . TYR B 31  ? 0.6223 0.5272 0.5823 -0.0326 0.0045  -0.0177 1248 TYR B CD2   
3964 C  CE1   . TYR B 31  ? 0.4047 0.3354 0.3702 -0.0332 0.0043  -0.0240 1248 TYR B CE1   
3965 C  CE2   . TYR B 31  ? 0.5867 0.4970 0.5476 -0.0365 0.0067  -0.0145 1248 TYR B CE2   
3966 C  CZ    . TYR B 31  ? 0.5064 0.4296 0.4703 -0.0368 0.0068  -0.0179 1248 TYR B CZ    
3967 O  OH    . TYR B 31  ? 0.6001 0.5294 0.5653 -0.0403 0.0093  -0.0154 1248 TYR B OH    
3968 N  N     . ASP B 32  ? 0.5726 0.4705 0.5452 -0.0418 0.0001  -0.0336 1249 ASP B N     
3969 C  CA    . ASP B 32  ? 0.5221 0.4098 0.4998 -0.0495 0.0009  -0.0329 1249 ASP B CA    
3970 C  C     . ASP B 32  ? 0.5584 0.4363 0.5331 -0.0518 0.0036  -0.0233 1249 ASP B C     
3971 O  O     . ASP B 32  ? 0.7391 0.6089 0.7175 -0.0588 0.0048  -0.0208 1249 ASP B O     
3972 C  CB    . ASP B 32  ? 0.6502 0.5472 0.6357 -0.0570 0.0012  -0.0368 1249 ASP B CB    
3973 C  CG    . ASP B 32  ? 0.7916 0.6992 0.7770 -0.0592 0.0043  -0.0318 1249 ASP B CG    
3974 O  OD1   . ASP B 32  ? 0.9275 0.8381 0.9066 -0.0534 0.0052  -0.0276 1249 ASP B OD1   
3975 O  OD2   . ASP B 32  ? 0.7968 0.7101 0.7888 -0.0665 0.0060  -0.0324 1249 ASP B OD2   
3976 N  N     . VAL B 33  ? 0.5725 0.4511 0.5406 -0.0463 0.0045  -0.0178 1250 VAL B N     
3977 C  CA    . VAL B 33  ? 0.6979 0.5655 0.6622 -0.0467 0.0059  -0.0096 1250 VAL B CA    
3978 C  C     . VAL B 33  ? 0.7973 0.6569 0.7586 -0.0395 0.0039  -0.0099 1250 VAL B C     
3979 O  O     . VAL B 33  ? 0.8611 0.7273 0.8193 -0.0330 0.0032  -0.0112 1250 VAL B O     
3980 C  CB    . VAL B 33  ? 0.6802 0.5544 0.6403 -0.0467 0.0083  -0.0032 1250 VAL B CB    
3981 C  CG1   . VAL B 33  ? 0.5505 0.4367 0.5141 -0.0519 0.0103  -0.0050 1250 VAL B CG1   
3982 C  CG2   . VAL B 33  ? 0.8054 0.6844 0.7608 -0.0391 0.0075  -0.0024 1250 VAL B CG2   
3983 N  N     . SER B 34  ? 0.8312 0.6768 0.7941 -0.0408 0.0029  -0.0092 1251 SER B N     
3984 C  CA    . SER B 34  ? 0.9263 0.7644 0.8884 -0.0342 0.0008  -0.0119 1251 SER B CA    
3985 C  C     . SER B 34  ? 0.8590 0.7010 0.8159 -0.0269 0.0010  -0.0079 1251 SER B C     
3986 O  O     . SER B 34  ? 0.8429 0.6842 0.7968 -0.0273 0.0021  -0.0006 1251 SER B O     
3987 C  CB    . SER B 34  ? 1.0961 0.9172 1.0605 -0.0367 0.0000  -0.0090 1251 SER B CB    
3988 O  OG    . SER B 34  ? 1.1634 0.9802 1.1256 -0.0410 0.0018  0.0003  1251 SER B OG    
3989 N  N     . GLY B 35  ? 0.7268 0.5739 0.6829 -0.0204 0.0001  -0.0130 1252 GLY B N     
3990 C  CA    . GLY B 35  ? 0.7083 0.5575 0.6610 -0.0139 0.0004  -0.0093 1252 GLY B CA    
3991 C  C     . GLY B 35  ? 0.8200 0.6812 0.7698 -0.0126 0.0017  -0.0063 1252 GLY B C     
3992 O  O     . GLY B 35  ? 0.8990 0.7617 0.8468 -0.0081 0.0020  -0.0025 1252 GLY B O     
3993 N  N     . CYS B 36  ? 0.8115 0.6810 0.7617 -0.0163 0.0024  -0.0080 1253 CYS B N     
3994 C  CA    . CYS B 36  ? 0.6282 0.5091 0.5762 -0.0142 0.0032  -0.0070 1253 CYS B CA    
3995 C  C     . CYS B 36  ? 0.6252 0.5151 0.5740 -0.0129 0.0025  -0.0136 1253 CYS B C     
3996 O  O     . CYS B 36  ? 0.7199 0.6088 0.6717 -0.0163 0.0014  -0.0189 1253 CYS B O     
3997 C  CB    . CYS B 36  ? 0.5753 0.4593 0.5230 -0.0189 0.0046  -0.0029 1253 CYS B CB    
3998 S  SG    . CYS B 36  ? 0.7100 0.5827 0.6569 -0.0234 0.0052  0.0035  1253 CYS B SG    
3999 N  N     . TYR B 37  ? 0.5502 0.4488 0.4966 -0.0082 0.0027  -0.0133 1254 TYR B N     
4000 C  CA    . TYR B 37  ? 0.5241 0.4311 0.4698 -0.0054 0.0015  -0.0191 1254 TYR B CA    
4001 C  C     . TYR B 37  ? 0.6553 0.5726 0.5997 -0.0036 0.0018  -0.0174 1254 TYR B C     
4002 O  O     . TYR B 37  ? 0.6834 0.6015 0.6260 -0.0010 0.0030  -0.0122 1254 TYR B O     
4003 C  CB    . TYR B 37  ? 0.4154 0.3216 0.3584 0.0008  0.0013  -0.0213 1254 TYR B CB    
4004 C  CG    . TYR B 37  ? 0.5225 0.4177 0.4670 0.0007  0.0010  -0.0223 1254 TYR B CG    
4005 C  CD1   . TYR B 37  ? 0.5379 0.4296 0.4838 0.0003  -0.0006 -0.0297 1254 TYR B CD1   
4006 C  CD2   . TYR B 37  ? 0.4994 0.3874 0.4442 0.0011  0.0020  -0.0163 1254 TYR B CD2   
4007 C  CE1   . TYR B 37  ? 0.5318 0.4123 0.4795 0.0006  -0.0010 -0.0307 1254 TYR B CE1   
4008 C  CE2   . TYR B 37  ? 0.6284 0.5061 0.5749 0.0016  0.0015  -0.0169 1254 TYR B CE2   
4009 C  CZ    . TYR B 37  ? 0.6911 0.5645 0.6392 0.0015  0.0001  -0.0239 1254 TYR B CZ    
4010 O  OH    . TYR B 37  ? 0.7925 0.6544 0.7428 0.0026  -0.0006 -0.0241 1254 TYR B OH    
4011 N  N     . ILE B 38  ? 0.7330 0.6584 0.6790 -0.0047 0.0005  -0.0222 1255 ILE B N     
4012 C  CA    . ILE B 38  ? 0.6278 0.5631 0.5732 -0.0025 0.0003  -0.0211 1255 ILE B CA    
4013 C  C     . ILE B 38  ? 0.6294 0.5677 0.5700 0.0043  0.0003  -0.0190 1255 ILE B C     
4014 O  O     . ILE B 38  ? 0.7723 0.7119 0.7103 0.0076  -0.0006 -0.0226 1255 ILE B O     
4015 C  CB    . ILE B 38  ? 0.5279 0.4720 0.4763 -0.0043 -0.0018 -0.0273 1255 ILE B CB    
4016 C  CG1   . ILE B 38  ? 0.4680 0.4120 0.4221 -0.0115 -0.0011 -0.0281 1255 ILE B CG1   
4017 C  CG2   . ILE B 38  ? 0.6398 0.5944 0.5864 0.0006  -0.0029 -0.0267 1255 ILE B CG2   
4018 C  CD1   . ILE B 38  ? 0.3988 0.3504 0.3578 -0.0146 -0.0034 -0.0354 1255 ILE B CD1   
4019 N  N     . LEU B 39  ? 0.5453 0.4845 0.4849 0.0064  0.0016  -0.0132 1256 LEU B N     
4020 C  CA    . LEU B 39  ? 0.6383 0.5802 0.5742 0.0122  0.0022  -0.0098 1256 LEU B CA    
4021 C  C     . LEU B 39  ? 0.5940 0.5454 0.5285 0.0155  0.0007  -0.0106 1256 LEU B C     
4022 O  O     . LEU B 39  ? 0.6211 0.5751 0.5576 0.0152  0.0006  -0.0084 1256 LEU B O     
4023 C  CB    . LEU B 39  ? 0.6671 0.6042 0.6036 0.0123  0.0041  -0.0033 1256 LEU B CB    
4024 C  CG    . LEU B 39  ? 0.4755 0.4047 0.4124 0.0114  0.0052  -0.0018 1256 LEU B CG    
4025 C  CD1   . LEU B 39  ? 0.3781 0.3034 0.3165 0.0104  0.0062  0.0038  1256 LEU B CD1   
4026 C  CD2   . LEU B 39  ? 0.4182 0.3491 0.3523 0.0162  0.0059  -0.0023 1256 LEU B CD2   
4027 N  N     . ARG B 40  ? 0.3891 0.3456 0.3196 0.0194  -0.0004 -0.0135 1257 ARG B N     
4028 C  CA    . ARG B 40  ? 0.7132 0.6789 0.6413 0.0234  -0.0023 -0.0137 1257 ARG B CA    
4029 C  C     . ARG B 40  ? 0.6009 0.5667 0.5263 0.0278  -0.0007 -0.0061 1257 ARG B C     
4030 O  O     . ARG B 40  ? 0.3869 0.3467 0.3125 0.0276  0.0018  -0.0013 1257 ARG B O     
4031 C  CB    . ARG B 40  ? 0.5359 0.5077 0.4599 0.0261  -0.0044 -0.0197 1257 ARG B CB    
4032 C  CG    . ARG B 40  ? 0.4250 0.3943 0.3523 0.0215  -0.0058 -0.0271 1257 ARG B CG    
4033 C  CD    . ARG B 40  ? 0.5142 0.4911 0.4382 0.0240  -0.0089 -0.0346 1257 ARG B CD    
4034 N  NE    . ARG B 40  ? 0.5709 0.5587 0.4949 0.0260  -0.0120 -0.0360 1257 ARG B NE    
4035 C  CZ    . ARG B 40  ? 0.5564 0.5532 0.4768 0.0291  -0.0155 -0.0418 1257 ARG B CZ    
4036 N  NH1   . ARG B 40  ? 0.6914 0.6876 0.6077 0.0303  -0.0161 -0.0474 1257 ARG B NH1   
4037 N  NH2   . ARG B 40  ? 0.4139 0.4209 0.3349 0.0313  -0.0186 -0.0424 1257 ARG B NH2   
4038 N  N     . HIS B 41  ? 0.5064 0.4795 0.4298 0.0317  -0.0025 -0.0049 1258 HIS B N     
4039 C  CA    . HIS B 41  ? 0.5280 0.5008 0.4495 0.0356  -0.0014 0.0027  1258 HIS B CA    
4040 C  C     . HIS B 41  ? 0.6489 0.6198 0.5655 0.0383  0.0014  0.0069  1258 HIS B C     
4041 O  O     . HIS B 41  ? 0.9209 0.8870 0.8388 0.0384  0.0038  0.0134  1258 HIS B O     
4042 C  CB    . HIS B 41  ? 0.6901 0.6712 0.6097 0.0401  -0.0044 0.0027  1258 HIS B CB    
4043 C  CG    . HIS B 41  ? 1.0152 0.9957 0.9319 0.0448  -0.0035 0.0109  1258 HIS B CG    
4044 N  ND1   . HIS B 41  ? 1.1090 1.0945 1.0182 0.0499  -0.0037 0.0141  1258 HIS B ND1   
4045 C  CD2   . HIS B 41  ? 1.0949 1.0703 1.0153 0.0450  -0.0026 0.0166  1258 HIS B CD2   
4046 C  CE1   . HIS B 41  ? 1.1404 1.1233 1.0490 0.0529  -0.0026 0.0222  1258 HIS B CE1   
4047 N  NE2   . HIS B 41  ? 1.0951 1.0714 1.0108 0.0499  -0.0021 0.0236  1258 HIS B NE2   
4048 N  N     . TRP B 42  ? 0.5196 0.4946 0.4312 0.0402  0.0011  0.0028  1259 TRP B N     
4049 C  CA    . TRP B 42  ? 0.5713 0.5470 0.4776 0.0436  0.0040  0.0063  1259 TRP B CA    
4050 C  C     . TRP B 42  ? 0.6301 0.5979 0.5407 0.0408  0.0073  0.0094  1259 TRP B C     
4051 O  O     . TRP B 42  ? 0.6784 0.6450 0.5889 0.0421  0.0101  0.0164  1259 TRP B O     
4052 C  CB    . TRP B 42  ? 0.5914 0.5728 0.4918 0.0460  0.0029  -0.0006 1259 TRP B CB    
4053 C  CG    . TRP B 42  ? 0.7269 0.7144 0.6190 0.0516  0.0051  0.0030  1259 TRP B CG    
4054 C  CD1   . TRP B 42  ? 0.8055 0.7939 0.6942 0.0534  0.0079  0.0013  1259 TRP B CD1   
4055 C  CD2   . TRP B 42  ? 0.6591 0.6532 0.5450 0.0563  0.0048  0.0090  1259 TRP B CD2   
4056 N  NE1   . TRP B 42  ? 0.7179 0.7136 0.5984 0.0586  0.0099  0.0059  1259 TRP B NE1   
4057 C  CE2   . TRP B 42  ? 0.7662 0.7651 0.6446 0.0604  0.0079  0.0111  1259 TRP B CE2   
4058 C  CE3   . TRP B 42  ? 0.6273 0.6234 0.5134 0.0578  0.0023  0.0131  1259 TRP B CE3   
4059 C  CZ2   . TRP B 42  ? 0.9743 0.9799 0.8446 0.0655  0.0088  0.0178  1259 TRP B CZ2   
4060 C  CZ3   . TRP B 42  ? 0.7668 0.7686 0.6455 0.0632  0.0027  0.0197  1259 TRP B CZ3   
4061 C  CH2   . TRP B 42  ? 0.9123 0.9188 0.7827 0.0668  0.0059  0.0224  1259 TRP B CH2   
4062 N  N     . SER B 43  ? 0.7098 0.6723 0.6244 0.0367  0.0069  0.0045  1260 SER B N     
4063 C  CA    . SER B 43  ? 0.7691 0.7245 0.6880 0.0343  0.0093  0.0071  1260 SER B CA    
4064 C  C     . SER B 43  ? 0.6760 0.6272 0.5995 0.0320  0.0099  0.0131  1260 SER B C     
4065 O  O     . SER B 43  ? 0.6554 0.6039 0.5811 0.0321  0.0122  0.0182  1260 SER B O     
4066 C  CB    . SER B 43  ? 0.8169 0.7668 0.7389 0.0305  0.0081  0.0011  1260 SER B CB    
4067 O  OG    . SER B 43  ? 0.8638 0.8139 0.7878 0.0272  0.0054  -0.0027 1260 SER B OG    
4068 N  N     . PHE B 44  ? 0.5674 0.5185 0.4930 0.0300  0.0077  0.0120  1261 PHE B N     
4069 C  CA    . PHE B 44  ? 0.4953 0.4416 0.4255 0.0275  0.0079  0.0158  1261 PHE B CA    
4070 C  C     . PHE B 44  ? 0.7220 0.6688 0.6522 0.0302  0.0093  0.0226  1261 PHE B C     
4071 O  O     . PHE B 44  ? 0.6765 0.6184 0.6108 0.0283  0.0103  0.0264  1261 PHE B O     
4072 C  CB    . PHE B 44  ? 0.3777 0.3250 0.3101 0.0254  0.0057  0.0126  1261 PHE B CB    
4073 C  CG    . PHE B 44  ? 0.5450 0.4870 0.4817 0.0220  0.0060  0.0143  1261 PHE B CG    
4074 C  CD1   . PHE B 44  ? 0.6717 0.6087 0.6102 0.0180  0.0065  0.0129  1261 PHE B CD1   
4075 C  CD2   . PHE B 44  ? 0.6452 0.5870 0.5840 0.0232  0.0057  0.0173  1261 PHE B CD2   
4076 C  CE1   . PHE B 44  ? 0.7310 0.6640 0.6724 0.0152  0.0066  0.0144  1261 PHE B CE1   
4077 C  CE2   . PHE B 44  ? 0.7104 0.6477 0.6528 0.0203  0.0058  0.0180  1261 PHE B CE2   
4078 C  CZ    . PHE B 44  ? 0.6930 0.6264 0.6362 0.0163  0.0062  0.0165  1261 PHE B CZ    
4079 N  N     . ALA B 45  ? 0.8035 0.7559 0.7291 0.0345  0.0093  0.0245  1262 ALA B N     
4080 C  CA    . ALA B 45  ? 0.7383 0.6903 0.6637 0.0369  0.0110  0.0322  1262 ALA B CA    
4081 C  C     . ALA B 45  ? 0.7946 0.7451 0.7213 0.0364  0.0145  0.0361  1262 ALA B C     
4082 O  O     . ALA B 45  ? 0.8007 0.7477 0.7314 0.0354  0.0161  0.0419  1262 ALA B O     
4083 C  CB    . ALA B 45  ? 0.5950 0.5536 0.5140 0.0419  0.0102  0.0340  1262 ALA B CB    
4084 N  N     . ILE B 46  ? 0.8022 0.7553 0.7262 0.0370  0.0156  0.0325  1263 ILE B N     
4085 C  CA    . ILE B 46  ? 0.6959 0.6486 0.6222 0.0368  0.0189  0.0353  1263 ILE B CA    
4086 C  C     . ILE B 46  ? 0.6407 0.5867 0.5747 0.0325  0.0186  0.0362  1263 ILE B C     
4087 O  O     . ILE B 46  ? 0.6520 0.5968 0.5906 0.0315  0.0206  0.0414  1263 ILE B O     
4088 C  CB    . ILE B 46  ? 0.6938 0.6499 0.6167 0.0386  0.0197  0.0296  1263 ILE B CB    
4089 C  CG1   . ILE B 46  ? 0.6504 0.6135 0.5650 0.0427  0.0190  0.0269  1263 ILE B CG1   
4090 C  CG2   . ILE B 46  ? 0.7051 0.6630 0.6303 0.0396  0.0236  0.0327  1263 ILE B CG2   
4091 C  CD1   . ILE B 46  ? 0.5672 0.5344 0.4778 0.0453  0.0203  0.0216  1263 ILE B CD1   
4092 N  N     . TRP B 47  ? 0.5763 0.5182 0.5117 0.0297  0.0160  0.0311  1264 TRP B N     
4093 C  CA    . TRP B 47  ? 0.6390 0.5750 0.5803 0.0258  0.0152  0.0319  1264 TRP B CA    
4094 C  C     . TRP B 47  ? 0.6957 0.6295 0.6406 0.0248  0.0150  0.0365  1264 TRP B C     
4095 O  O     . TRP B 47  ? 0.6005 0.5314 0.5507 0.0226  0.0154  0.0393  1264 TRP B O     
4096 C  CB    . TRP B 47  ? 0.4562 0.3887 0.3973 0.0230  0.0128  0.0265  1264 TRP B CB    
4097 C  CG    . TRP B 47  ? 0.4310 0.3582 0.3764 0.0193  0.0117  0.0273  1264 TRP B CG    
4098 C  CD1   . TRP B 47  ? 0.6343 0.5594 0.5805 0.0169  0.0100  0.0261  1264 TRP B CD1   
4099 C  CD2   . TRP B 47  ? 0.4493 0.3737 0.3986 0.0179  0.0120  0.0291  1264 TRP B CD2   
4100 N  NE1   . TRP B 47  ? 0.6786 0.5996 0.6280 0.0141  0.0092  0.0270  1264 TRP B NE1   
4101 C  CE2   . TRP B 47  ? 0.5600 0.4805 0.5115 0.0146  0.0101  0.0290  1264 TRP B CE2   
4102 C  CE3   . TRP B 47  ? 0.4280 0.3537 0.3793 0.0195  0.0136  0.0306  1264 TRP B CE3   
4103 C  CZ2   . TRP B 47  ? 0.5661 0.4838 0.5210 0.0129  0.0093  0.0304  1264 TRP B CZ2   
4104 C  CZ3   . TRP B 47  ? 0.4508 0.3739 0.4068 0.0178  0.0129  0.0321  1264 TRP B CZ3   
4105 C  CH2   . TRP B 47  ? 0.5353 0.4543 0.4928 0.0145  0.0105  0.0320  1264 TRP B CH2   
4106 N  N     . LYS B 48  ? 0.6429 0.5780 0.5854 0.0264  0.0139  0.0371  1265 LYS B N     
4107 C  CA    . LYS B 48  ? 0.4999 0.4317 0.4461 0.0259  0.0134  0.0411  1265 LYS B CA    
4108 C  C     . LYS B 48  ? 0.3810 0.3127 0.3302 0.0264  0.0161  0.0479  1265 LYS B C     
4109 O  O     . LYS B 48  ? 0.4741 0.4014 0.4293 0.0239  0.0160  0.0504  1265 LYS B O     
4110 C  CB    . LYS B 48  ? 0.3806 0.3144 0.3238 0.0287  0.0118  0.0407  1265 LYS B CB    
4111 C  CG    . LYS B 48  ? 0.3773 0.3107 0.3209 0.0273  0.0092  0.0349  1265 LYS B CG    
4112 C  CD    . LYS B 48  ? 0.5514 0.4877 0.4932 0.0308  0.0076  0.0350  1265 LYS B CD    
4113 C  CE    . LYS B 48  ? 0.6735 0.6103 0.6173 0.0295  0.0054  0.0295  1265 LYS B CE    
4114 N  NZ    . LYS B 48  ? 0.7561 0.6939 0.7010 0.0331  0.0037  0.0306  1265 LYS B NZ    
4115 N  N     . ALA B 49  ? 0.3854 0.3224 0.3304 0.0294  0.0186  0.0507  1266 ALA B N     
4116 C  CA    . ALA B 49  ? 0.3892 0.3276 0.3370 0.0296  0.0220  0.0577  1266 ALA B CA    
4117 C  C     . ALA B 49  ? 0.6062 0.5432 0.5610 0.0263  0.0231  0.0576  1266 ALA B C     
4118 O  O     . ALA B 49  ? 0.6549 0.5893 0.6168 0.0237  0.0239  0.0620  1266 ALA B O     
4119 C  CB    . ALA B 49  ? 0.3950 0.3409 0.3357 0.0337  0.0249  0.0597  1266 ALA B CB    
4120 N  N     . ILE B 50  ? 0.5272 0.4658 0.4809 0.0262  0.0227  0.0524  1267 ILE B N     
4121 C  CA    . ILE B 50  ? 0.6146 0.5525 0.5751 0.0237  0.0230  0.0521  1267 ILE B CA    
4122 C  C     . ILE B 50  ? 0.5450 0.4766 0.5113 0.0198  0.0201  0.0518  1267 ILE B C     
4123 O  O     . ILE B 50  ? 0.3751 0.3061 0.3488 0.0174  0.0206  0.0551  1267 ILE B O     
4124 C  CB    . ILE B 50  ? 0.4353 0.3743 0.3931 0.0248  0.0224  0.0465  1267 ILE B CB    
4125 C  CG1   . ILE B 50  ? 0.4879 0.4339 0.4415 0.0288  0.0258  0.0466  1267 ILE B CG1   
4126 C  CG2   . ILE B 50  ? 0.3736 0.3106 0.3381 0.0224  0.0215  0.0459  1267 ILE B CG2   
4127 C  CD1   . ILE B 50  ? 0.5483 0.4946 0.4981 0.0306  0.0249  0.0398  1267 ILE B CD1   
4128 N  N     . ARG B 51  ? 0.5189 0.4466 0.4821 0.0190  0.0171  0.0477  1268 ARG B N     
4129 C  CA    . ARG B 51  ? 0.5769 0.4994 0.5440 0.0157  0.0143  0.0461  1268 ARG B CA    
4130 C  C     . ARG B 51  ? 0.5741 0.4938 0.5466 0.0146  0.0144  0.0503  1268 ARG B C     
4131 O  O     . ARG B 51  ? 0.5563 0.4734 0.5352 0.0116  0.0132  0.0507  1268 ARG B O     
4132 C  CB    . ARG B 51  ? 0.5450 0.4656 0.5071 0.0157  0.0119  0.0410  1268 ARG B CB    
4133 C  CG    . ARG B 51  ? 0.4833 0.3993 0.4477 0.0130  0.0093  0.0387  1268 ARG B CG    
4134 C  CD    . ARG B 51  ? 0.6668 0.5830 0.6266 0.0133  0.0079  0.0341  1268 ARG B CD    
4135 N  NE    . ARG B 51  ? 0.9604 0.8775 0.9193 0.0159  0.0080  0.0349  1268 ARG B NE    
4136 C  CZ    . ARG B 51  ? 1.1280 1.0475 1.0835 0.0171  0.0071  0.0314  1268 ARG B CZ    
4137 N  NH1   . ARG B 51  ? 1.0330 0.9540 0.9859 0.0154  0.0067  0.0271  1268 ARG B NH1   
4138 N  NH2   . ARG B 51  ? 1.2845 1.2051 1.2397 0.0202  0.0068  0.0325  1268 ARG B NH2   
4139 N  N     . ASN B 52  ? 0.4338 0.3537 0.4038 0.0170  0.0155  0.0535  1269 ASN B N     
4140 C  CA    . ASN B 52  ? 0.4163 0.3320 0.3913 0.0162  0.0155  0.0578  1269 ASN B CA    
4141 C  C     . ASN B 52  ? 0.4976 0.4143 0.4799 0.0140  0.0180  0.0633  1269 ASN B C     
4142 O  O     . ASN B 52  ? 0.5513 0.4636 0.5413 0.0107  0.0167  0.0641  1269 ASN B O     
4143 C  CB    . ASN B 52  ? 0.6100 0.5262 0.5799 0.0200  0.0162  0.0608  1269 ASN B CB    
4144 C  CG    . ASN B 52  ? 0.6318 0.5467 0.5978 0.0217  0.0133  0.0556  1269 ASN B CG    
4145 O  OD1   . ASN B 52  ? 0.5994 0.5119 0.5668 0.0195  0.0110  0.0503  1269 ASN B OD1   
4146 N  ND2   . ASN B 52  ? 0.5919 0.5091 0.5527 0.0256  0.0133  0.0572  1269 ASN B ND2   
4147 N  N     . TRP B 53  ? 0.5034 0.4265 0.4839 0.0156  0.0216  0.0666  1270 TRP B N     
4148 C  CA    . TRP B 53  ? 0.3873 0.3132 0.3758 0.0132  0.0244  0.0715  1270 TRP B CA    
4149 C  C     . TRP B 53  ? 0.4464 0.3712 0.4426 0.0095  0.0219  0.0679  1270 TRP B C     
4150 O  O     . TRP B 53  ? 0.5960 0.5182 0.6011 0.0058  0.0213  0.0701  1270 TRP B O     
4151 C  CB    . TRP B 53  ? 0.3886 0.3233 0.3735 0.0160  0.0287  0.0739  1270 TRP B CB    
4152 C  CG    . TRP B 53  ? 0.4814 0.4212 0.4743 0.0140  0.0327  0.0797  1270 TRP B CG    
4153 C  CD1   . TRP B 53  ? 0.5414 0.4834 0.5356 0.0140  0.0368  0.0877  1270 TRP B CD1   
4154 C  CD2   . TRP B 53  ? 0.6013 0.5455 0.6026 0.0118  0.0332  0.0784  1270 TRP B CD2   
4155 N  NE1   . TRP B 53  ? 0.5741 0.5222 0.5775 0.0113  0.0403  0.0913  1270 TRP B NE1   
4156 C  CE2   . TRP B 53  ? 0.5553 0.5052 0.5636 0.0102  0.0379  0.0854  1270 TRP B CE2   
4157 C  CE3   . TRP B 53  ? 0.5064 0.4507 0.5102 0.0111  0.0300  0.0723  1270 TRP B CE3   
4158 C  CZ2   . TRP B 53  ? 0.5396 0.4961 0.5582 0.0079  0.0395  0.0859  1270 TRP B CZ2   
4159 C  CZ3   . TRP B 53  ? 0.5377 0.4879 0.5510 0.0094  0.0311  0.0730  1270 TRP B CZ3   
4160 C  CH2   . TRP B 53  ? 0.6283 0.5851 0.6493 0.0079  0.0358  0.0794  1270 TRP B CH2   
4161 N  N     . PHE B 54  ? 0.4591 0.3854 0.4517 0.0103  0.0201  0.0623  1271 PHE B N     
4162 C  CA    . PHE B 54  ? 0.5849 0.5113 0.5840 0.0074  0.0176  0.0596  1271 PHE B CA    
4163 C  C     . PHE B 54  ? 0.6698 0.5895 0.6723 0.0042  0.0136  0.0572  1271 PHE B C     
4164 O  O     . PHE B 54  ? 0.7253 0.6451 0.7361 0.0010  0.0119  0.0571  1271 PHE B O     
4165 C  CB    . PHE B 54  ? 0.4725 0.4004 0.4665 0.0091  0.0162  0.0547  1271 PHE B CB    
4166 C  CG    . PHE B 54  ? 0.4638 0.3924 0.4638 0.0070  0.0135  0.0529  1271 PHE B CG    
4167 C  CD1   . PHE B 54  ? 0.3898 0.3248 0.3969 0.0072  0.0153  0.0551  1271 PHE B CD1   
4168 C  CD2   . PHE B 54  ? 0.4761 0.4001 0.4749 0.0050  0.0092  0.0490  1271 PHE B CD2   
4169 C  CE1   . PHE B 54  ? 0.3662 0.3026 0.3794 0.0057  0.0122  0.0534  1271 PHE B CE1   
4170 C  CE2   . PHE B 54  ? 0.3656 0.2908 0.3693 0.0034  0.0063  0.0476  1271 PHE B CE2   
4171 C  CZ    . PHE B 54  ? 0.3654 0.2967 0.3764 0.0038  0.0075  0.0498  1271 PHE B CZ    
4172 N  N     . ASP B 55  ? 0.5939 0.5087 0.5906 0.0052  0.0120  0.0547  1272 ASP B N     
4173 C  CA    . ASP B 55  ? 0.5718 0.4809 0.5715 0.0027  0.0083  0.0514  1272 ASP B CA    
4174 C  C     . ASP B 55  ? 0.5663 0.4717 0.5743 0.0005  0.0087  0.0552  1272 ASP B C     
4175 O  O     . ASP B 55  ? 0.4979 0.4005 0.5126 -0.0028 0.0059  0.0531  1272 ASP B O     
4176 C  CB    . ASP B 55  ? 0.5509 0.4568 0.5430 0.0045  0.0067  0.0471  1272 ASP B CB    
4177 C  CG    . ASP B 55  ? 0.6287 0.5297 0.6229 0.0024  0.0031  0.0425  1272 ASP B CG    
4178 O  OD1   . ASP B 55  ? 0.6112 0.5130 0.6042 0.0008  0.0007  0.0385  1272 ASP B OD1   
4179 O  OD2   . ASP B 55  ? 0.8266 0.7229 0.8234 0.0027  0.0026  0.0430  1272 ASP B OD2   
4180 N  N     . ALA B 56  ? 0.6746 0.5798 0.6823 0.0021  0.0119  0.0609  1273 ALA B N     
4181 C  CA    . ALA B 56  ? 0.7692 0.6703 0.7858 -0.0005 0.0127  0.0659  1273 ALA B CA    
4182 C  C     . ALA B 56  ? 0.7579 0.6631 0.7845 -0.0046 0.0131  0.0672  1273 ALA B C     
4183 O  O     . ALA B 56  ? 0.7361 0.6372 0.7719 -0.0085 0.0108  0.0664  1273 ALA B O     
4184 C  CB    . ALA B 56  ? 0.7270 0.6288 0.7408 0.0021  0.0168  0.0734  1273 ALA B CB    
4185 N  N     . GLU B 57  ? 0.5447 0.4583 0.5701 -0.0035 0.0155  0.0683  1274 GLU B N     
4186 C  CA    . GLU B 57  ? 0.4649 0.3843 0.5005 -0.0067 0.0162  0.0697  1274 GLU B CA    
4187 C  C     . GLU B 57  ? 0.5059 0.4235 0.5463 -0.0096 0.0108  0.0636  1274 GLU B C     
4188 O  O     . GLU B 57  ? 0.5239 0.4419 0.5755 -0.0139 0.0094  0.0642  1274 GLU B O     
4189 C  CB    . GLU B 57  ? 0.4686 0.3973 0.5009 -0.0037 0.0195  0.0708  1274 GLU B CB    
4190 C  CG    . GLU B 57  ? 0.6268 0.5598 0.6585 -0.0022 0.0254  0.0779  1274 GLU B CG    
4191 C  CD    . GLU B 57  ? 0.8186 0.7499 0.8610 -0.0066 0.0272  0.0841  1274 GLU B CD    
4192 O  OE1   . GLU B 57  ? 0.8063 0.7408 0.8605 -0.0108 0.0264  0.0840  1274 GLU B OE1   
4193 O  OE2   . GLU B 57  ? 0.8678 0.7944 0.9071 -0.0060 0.0292  0.0891  1274 GLU B OE2   
4194 N  N     . ILE B 58  ? 0.5303 0.4467 0.5624 -0.0076 0.0077  0.0578  1275 ILE B N     
4195 C  CA    . ILE B 58  ? 0.5609 0.4771 0.5962 -0.0099 0.0028  0.0525  1275 ILE B CA    
4196 C  C     . ILE B 58  ? 0.5053 0.4140 0.5424 -0.0123 -0.0009 0.0488  1275 ILE B C     
4197 O  O     . ILE B 58  ? 0.4017 0.3105 0.4436 -0.0150 -0.0052 0.0448  1275 ILE B O     
4198 C  CB    . ILE B 58  ? 0.5664 0.4845 0.5926 -0.0072 0.0009  0.0485  1275 ILE B CB    
4199 C  CG1   . ILE B 58  ? 0.5791 0.4918 0.5943 -0.0050 0.0005  0.0456  1275 ILE B CG1   
4200 C  CG2   . ILE B 58  ? 0.3707 0.2955 0.3963 -0.0046 0.0042  0.0514  1275 ILE B CG2   
4201 C  CD1   . ILE B 58  ? 0.5850 0.4962 0.5950 -0.0055 -0.0036 0.0400  1275 ILE B CD1   
4202 N  N     . THR B 59  ? 0.5135 0.4158 0.5463 -0.0108 0.0002  0.0495  1276 THR B N     
4203 C  CA    . THR B 59  ? 0.6228 0.5174 0.6585 -0.0126 -0.0030 0.0457  1276 THR B CA    
4204 C  C     . THR B 59  ? 0.6036 0.4952 0.6520 -0.0167 -0.0027 0.0493  1276 THR B C     
4205 O  O     . THR B 59  ? 0.6334 0.5206 0.6881 -0.0197 -0.0067 0.0449  1276 THR B O     
4206 C  CB    . THR B 59  ? 0.6156 0.5048 0.6432 -0.0090 -0.0021 0.0451  1276 THR B CB    
4207 O  OG1   . THR B 59  ? 0.5638 0.4552 0.5815 -0.0067 -0.0035 0.0399  1276 THR B OG1   
4208 C  CG2   . THR B 59  ? 0.3996 0.2801 0.4322 -0.0102 -0.0045 0.0426  1276 THR B CG2   
4209 N  N     . ARG B 60  ? 0.4751 0.3698 0.5277 -0.0170 0.0019  0.0570  1277 ARG B N     
4210 C  CA    . ARG B 60  ? 0.4037 0.2975 0.4700 -0.0218 0.0028  0.0612  1277 ARG B CA    
4211 C  C     . ARG B 60  ? 0.4532 0.3527 0.5288 -0.0259 -0.0006 0.0575  1277 ARG B C     
4212 O  O     . ARG B 60  ? 0.6755 0.5718 0.7627 -0.0307 -0.0028 0.0567  1277 ARG B O     
4213 C  CB    . ARG B 60  ? 0.6427 0.5415 0.7102 -0.0211 0.0091  0.0705  1277 ARG B CB    
4214 C  CG    . ARG B 60  ? 0.7350 0.6303 0.8141 -0.0255 0.0116  0.0773  1277 ARG B CG    
4215 C  CD    . ARG B 60  ? 0.8681 0.7698 0.9455 -0.0239 0.0184  0.0866  1277 ARG B CD    
4216 N  NE    . ARG B 60  ? 1.0133 0.9278 1.0906 -0.0229 0.0206  0.0862  1277 ARG B NE    
4217 C  CZ    . ARG B 60  ? 1.0132 0.9353 1.1025 -0.0270 0.0206  0.0862  1277 ARG B CZ    
4218 N  NH1   . ARG B 60  ? 1.0625 0.9811 1.1653 -0.0331 0.0185  0.0863  1277 ARG B NH1   
4219 N  NH2   . ARG B 60  ? 0.9479 0.8814 1.0365 -0.0250 0.0224  0.0855  1277 ARG B NH2   
4220 N  N     . LEU B 61  ? 0.6233 0.5309 0.6944 -0.0240 -0.0014 0.0551  1278 LEU B N     
4221 C  CA    . LEU B 61  ? 0.6843 0.5987 0.7631 -0.0267 -0.0050 0.0517  1278 LEU B CA    
4222 C  C     . LEU B 61  ? 0.6558 0.5664 0.7337 -0.0282 -0.0117 0.0434  1278 LEU B C     
4223 O  O     . LEU B 61  ? 0.6719 0.5877 0.7575 -0.0310 -0.0156 0.0403  1278 LEU B O     
4224 C  CB    . LEU B 61  ? 0.6879 0.6113 0.7611 -0.0230 -0.0036 0.0523  1278 LEU B CB    
4225 C  CG    . LEU B 61  ? 0.5622 0.4917 0.6383 -0.0219 0.0029  0.0597  1278 LEU B CG    
4226 C  CD1   . LEU B 61  ? 0.4145 0.3522 0.4857 -0.0178 0.0041  0.0594  1278 LEU B CD1   
4227 C  CD2   . LEU B 61  ? 0.4952 0.4287 0.5878 -0.0273 0.0043  0.0636  1278 LEU B CD2   
4228 N  N     . GLY B 62  ? 0.6547 0.5581 0.7222 -0.0257 -0.0133 0.0393  1279 GLY B N     
4229 C  CA    . GLY B 62  ? 0.6742 0.5747 0.7394 -0.0266 -0.0192 0.0311  1279 GLY B CA    
4230 C  C     . GLY B 62  ? 0.6977 0.6007 0.7494 -0.0230 -0.0208 0.0272  1279 GLY B C     
4231 O  O     . GLY B 62  ? 0.8102 0.7132 0.8590 -0.0236 -0.0257 0.0208  1279 GLY B O     
4232 N  N     . VAL B 63  ? 0.6258 0.5312 0.6693 -0.0194 -0.0171 0.0309  1280 VAL B N     
4233 C  CA    . VAL B 63  ? 0.6054 0.5122 0.6367 -0.0165 -0.0183 0.0278  1280 VAL B CA    
4234 C  C     . VAL B 63  ? 0.5801 0.4806 0.6029 -0.0146 -0.0176 0.0247  1280 VAL B C     
4235 O  O     . VAL B 63  ? 0.5581 0.4556 0.5797 -0.0129 -0.0139 0.0279  1280 VAL B O     
4236 C  CB    . VAL B 63  ? 0.5595 0.4713 0.5866 -0.0136 -0.0148 0.0324  1280 VAL B CB    
4237 C  CG1   . VAL B 63  ? 0.4881 0.4013 0.5050 -0.0118 -0.0171 0.0295  1280 VAL B CG1   
4238 C  CG2   . VAL B 63  ? 0.4252 0.3435 0.4632 -0.0151 -0.0141 0.0363  1280 VAL B CG2   
4239 N  N     . LYS B 64  ? 0.5525 0.4521 0.5689 -0.0145 -0.0211 0.0186  1281 LYS B N     
4240 C  CA    . LYS B 64  ? 0.5563 0.4517 0.5650 -0.0125 -0.0205 0.0149  1281 LYS B CA    
4241 C  C     . LYS B 64  ? 0.6372 0.5355 0.6347 -0.0099 -0.0184 0.0156  1281 LYS B C     
4242 O  O     . LYS B 64  ? 0.7008 0.6033 0.6958 -0.0098 -0.0184 0.0180  1281 LYS B O     
4243 C  CB    . LYS B 64  ? 0.4479 0.3412 0.4557 -0.0137 -0.0249 0.0071  1281 LYS B CB    
4244 C  CG    . LYS B 64  ? 0.6415 0.5310 0.6608 -0.0168 -0.0280 0.0047  1281 LYS B CG    
4245 C  CD    . LYS B 64  ? 0.8621 0.7548 0.8811 -0.0189 -0.0337 -0.0020 1281 LYS B CD    
4246 C  CE    . LYS B 64  ? 1.0126 0.9008 1.0433 -0.0223 -0.0374 -0.0064 1281 LYS B CE    
4247 N  NZ    . LYS B 64  ? 1.0967 0.9874 1.1254 -0.0237 -0.0435 -0.0149 1281 LYS B NZ    
4248 N  N     . GLU B 65  ? 0.6402 0.5362 0.6317 -0.0079 -0.0166 0.0135  1282 GLU B N     
4249 C  CA    . GLU B 65  ? 0.3840 0.2824 0.3665 -0.0058 -0.0140 0.0144  1282 GLU B CA    
4250 C  C     . GLU B 65  ? 0.5834 0.4828 0.5576 -0.0056 -0.0151 0.0088  1282 GLU B C     
4251 O  O     . GLU B 65  ? 0.6218 0.5190 0.5966 -0.0052 -0.0163 0.0039  1282 GLU B O     
4252 C  CB    . GLU B 65  ? 0.3819 0.2786 0.3651 -0.0035 -0.0105 0.0173  1282 GLU B CB    
4253 C  CG    . GLU B 65  ? 0.4955 0.3946 0.4706 -0.0016 -0.0082 0.0166  1282 GLU B CG    
4254 C  CD    . GLU B 65  ? 0.6339 0.5335 0.6095 0.0006  -0.0051 0.0210  1282 GLU B CD    
4255 O  OE1   . GLU B 65  ? 0.8407 0.7388 0.8224 0.0007  -0.0043 0.0251  1282 GLU B OE1   
4256 O  OE2   . GLU B 65  ? 0.5120 0.4141 0.4819 0.0019  -0.0034 0.0206  1282 GLU B OE2   
4257 N  N     . CYS B 66  ? 0.6477 0.5504 0.6142 -0.0057 -0.0146 0.0096  1283 CYS B N     
4258 C  CA    . CYS B 66  ? 0.6689 0.5738 0.6267 -0.0059 -0.0148 0.0054  1283 CYS B CA    
4259 C  C     . CYS B 66  ? 0.6995 0.6065 0.6512 -0.0055 -0.0116 0.0083  1283 CYS B C     
4260 O  O     . CYS B 66  ? 0.5824 0.4887 0.5366 -0.0046 -0.0095 0.0123  1283 CYS B O     
4261 C  CB    . CYS B 66  ? 0.5974 0.5042 0.5520 -0.0076 -0.0187 0.0033  1283 CYS B CB    
4262 S  SG    . CYS B 66  ? 0.7682 0.6763 0.7239 -0.0084 -0.0203 0.0091  1283 CYS B SG    
4263 N  N     . TYR B 67  ? 0.7748 0.6844 0.7184 -0.0062 -0.0111 0.0061  1284 TYR B N     
4264 C  CA    . TYR B 67  ? 0.6861 0.5973 0.6244 -0.0067 -0.0082 0.0087  1284 TYR B CA    
4265 C  C     . TYR B 67  ? 0.6001 0.5139 0.5296 -0.0086 -0.0084 0.0080  1284 TYR B C     
4266 O  O     . TYR B 67  ? 0.5544 0.4713 0.4800 -0.0087 -0.0078 0.0035  1284 TYR B O     
4267 C  CB    . TYR B 67  ? 0.7332 0.6459 0.6727 -0.0054 -0.0051 0.0069  1284 TYR B CB    
4268 C  CG    . TYR B 67  ? 0.8513 0.7662 0.7863 -0.0066 -0.0023 0.0087  1284 TYR B CG    
4269 C  CD1   . TYR B 67  ? 0.9407 0.8536 0.8771 -0.0065 -0.0014 0.0127  1284 TYR B CD1   
4270 C  CD2   . TYR B 67  ? 0.8661 0.7851 0.7955 -0.0080 -0.0005 0.0061  1284 TYR B CD2   
4271 C  CE1   . TYR B 67  ? 1.0360 0.9501 0.9691 -0.0081 0.0008  0.0138  1284 TYR B CE1   
4272 C  CE2   . TYR B 67  ? 1.0084 0.9293 0.9348 -0.0100 0.0022  0.0079  1284 TYR B CE2   
4273 C  CZ    . TYR B 67  ? 1.0664 0.9842 0.9949 -0.0101 0.0025  0.0116  1284 TYR B CZ    
4274 O  OH    . TYR B 67  ? 1.0213 0.9401 0.9476 -0.0125 0.0048  0.0129  1284 TYR B OH    
4275 N  N     . PHE B 68  ? 0.5115 0.4240 0.4376 -0.0097 -0.0091 0.0125  1285 PHE B N     
4276 C  CA    . PHE B 68  ? 0.5035 0.4178 0.4203 -0.0116 -0.0090 0.0136  1285 PHE B CA    
4277 C  C     . PHE B 68  ? 0.4862 0.4010 0.4000 -0.0131 -0.0049 0.0154  1285 PHE B C     
4278 O  O     . PHE B 68  ? 0.4991 0.4122 0.4179 -0.0124 -0.0032 0.0165  1285 PHE B O     
4279 C  CB    . PHE B 68  ? 0.5592 0.4712 0.4742 -0.0117 -0.0123 0.0180  1285 PHE B CB    
4280 C  CG    . PHE B 68  ? 0.6753 0.5887 0.5916 -0.0110 -0.0169 0.0156  1285 PHE B CG    
4281 C  CD1   . PHE B 68  ? 0.6421 0.5552 0.5670 -0.0100 -0.0182 0.0122  1285 PHE B CD1   
4282 C  CD2   . PHE B 68  ? 0.7701 0.6850 0.6793 -0.0115 -0.0201 0.0169  1285 PHE B CD2   
4283 C  CE1   . PHE B 68  ? 0.5749 0.4892 0.5022 -0.0100 -0.0226 0.0095  1285 PHE B CE1   
4284 C  CE2   . PHE B 68  ? 0.8098 0.7268 0.7207 -0.0110 -0.0249 0.0140  1285 PHE B CE2   
4285 C  CZ    . PHE B 68  ? 0.6766 0.5933 0.5970 -0.0105 -0.0262 0.0099  1285 PHE B CZ    
4286 N  N     . PRO B 69  ? 0.5559 0.4737 0.4618 -0.0153 -0.0031 0.0155  1286 PRO B N     
4287 C  CA    . PRO B 69  ? 0.4409 0.3601 0.3452 -0.0175 0.0011  0.0168  1286 PRO B CA    
4288 C  C     . PRO B 69  ? 0.4634 0.3769 0.3690 -0.0185 0.0012  0.0221  1286 PRO B C     
4289 O  O     . PRO B 69  ? 0.5975 0.5065 0.5026 -0.0176 -0.0018 0.0257  1286 PRO B O     
4290 C  CB    . PRO B 69  ? 0.4499 0.3735 0.3448 -0.0200 0.0027  0.0168  1286 PRO B CB    
4291 C  CG    . PRO B 69  ? 0.4914 0.4167 0.3827 -0.0184 -0.0008 0.0143  1286 PRO B CG    
4292 C  CD    . PRO B 69  ? 0.5601 0.4802 0.4576 -0.0161 -0.0050 0.0153  1286 PRO B CD    
4293 N  N     . ILE B 70  ? 0.4244 0.3382 0.3321 -0.0201 0.0044  0.0222  1287 ILE B N     
4294 C  CA    . ILE B 70  ? 0.6084 0.5163 0.5172 -0.0214 0.0046  0.0264  1287 ILE B CA    
4295 C  C     . ILE B 70  ? 0.6245 0.5288 0.5263 -0.0242 0.0046  0.0316  1287 ILE B C     
4296 O  O     . ILE B 70  ? 0.5923 0.4898 0.4948 -0.0246 0.0039  0.0356  1287 ILE B O     
4297 C  CB    . ILE B 70  ? 0.6400 0.5492 0.5527 -0.0232 0.0077  0.0248  1287 ILE B CB    
4298 C  CG1   . ILE B 70  ? 0.6324 0.5490 0.5430 -0.0259 0.0111  0.0221  1287 ILE B CG1   
4299 C  CG2   . ILE B 70  ? 0.7604 0.6698 0.6801 -0.0199 0.0071  0.0220  1287 ILE B CG2   
4300 C  CD1   . ILE B 70  ? 0.8107 0.7289 0.7252 -0.0286 0.0137  0.0211  1287 ILE B CD1   
4301 N  N     . PHE B 71  ? 0.4213 0.3299 0.3161 -0.0261 0.0057  0.0318  1288 PHE B N     
4302 C  CA    . PHE B 71  ? 0.4324 0.3382 0.3193 -0.0291 0.0062  0.0376  1288 PHE B CA    
4303 C  C     . PHE B 71  ? 0.4380 0.3419 0.3192 -0.0268 0.0019  0.0405  1288 PHE B C     
4304 O  O     . PHE B 71  ? 0.5396 0.4481 0.4201 -0.0246 -0.0003 0.0366  1288 PHE B O     
4305 C  CB    . PHE B 71  ? 0.6251 0.5382 0.5068 -0.0328 0.0106  0.0367  1288 PHE B CB    
4306 C  CG    . PHE B 71  ? 0.6767 0.5920 0.5640 -0.0357 0.0146  0.0348  1288 PHE B CG    
4307 C  CD1   . PHE B 71  ? 0.6248 0.5330 0.5175 -0.0368 0.0145  0.0370  1288 PHE B CD1   
4308 C  CD2   . PHE B 71  ? 0.7002 0.6254 0.5880 -0.0372 0.0184  0.0303  1288 PHE B CD2   
4309 C  CE1   . PHE B 71  ? 0.5830 0.4939 0.4815 -0.0397 0.0176  0.0346  1288 PHE B CE1   
4310 C  CE2   . PHE B 71  ? 0.6525 0.5810 0.5466 -0.0400 0.0217  0.0283  1288 PHE B CE2   
4311 C  CZ    . PHE B 71  ? 0.6400 0.5614 0.5395 -0.0414 0.0211  0.0304  1288 PHE B CZ    
4312 N  N     . VAL B 72  ? 0.5297 0.4267 0.4073 -0.0274 0.0003  0.0471  1289 VAL B N     
4313 C  CA    . VAL B 72  ? 0.5103 0.4053 0.3821 -0.0252 -0.0043 0.0510  1289 VAL B CA    
4314 C  C     . VAL B 72  ? 0.5032 0.3964 0.3646 -0.0285 -0.0028 0.0578  1289 VAL B C     
4315 O  O     . VAL B 72  ? 0.6998 0.5865 0.5619 -0.0311 -0.0005 0.0624  1289 VAL B O     
4316 C  CB    . VAL B 72  ? 0.4961 0.3841 0.3744 -0.0217 -0.0082 0.0534  1289 VAL B CB    
4317 C  CG1   . VAL B 72  ? 0.4563 0.3450 0.3305 -0.0188 -0.0136 0.0557  1289 VAL B CG1   
4318 C  CG2   . VAL B 72  ? 0.5463 0.4359 0.4352 -0.0195 -0.0080 0.0476  1289 VAL B CG2   
4319 N  N     . SER B 73  ? 0.4754 0.3743 0.3271 -0.0284 -0.0039 0.0583  1290 SER B N     
4320 C  CA    . SER B 73  ? 0.5280 0.4252 0.3682 -0.0310 -0.0029 0.0661  1290 SER B CA    
4321 C  C     . SER B 73  ? 0.5971 0.4832 0.4369 -0.0297 -0.0063 0.0744  1290 SER B C     
4322 O  O     . SER B 73  ? 0.4937 0.3757 0.3400 -0.0256 -0.0109 0.0738  1290 SER B O     
4323 C  CB    . SER B 73  ? 0.5373 0.4426 0.3665 -0.0297 -0.0050 0.0649  1290 SER B CB    
4324 O  OG    . SER B 73  ? 0.5146 0.4172 0.3422 -0.0257 -0.0118 0.0673  1290 SER B OG    
4325 N  N     . ARG B 74  ? 0.6014 0.4824 0.4342 -0.0332 -0.0038 0.0825  1291 ARG B N     
4326 C  CA    . ARG B 74  ? 0.6765 0.5469 0.5070 -0.0313 -0.0077 0.0911  1291 ARG B CA    
4327 C  C     . ARG B 74  ? 0.5664 0.4399 0.3915 -0.0261 -0.0145 0.0919  1291 ARG B C     
4328 O  O     . ARG B 74  ? 0.6017 0.4701 0.4328 -0.0217 -0.0195 0.0928  1291 ARG B O     
4329 C  CB    . ARG B 74  ? 0.7255 0.5904 0.5473 -0.0362 -0.0041 0.1006  1291 ARG B CB    
4330 N  N     . ALA B 75  ? 0.5338 0.4169 0.3484 -0.0265 -0.0147 0.0907  1292 ALA B N     
4331 C  CA    . ALA B 75  ? 0.5979 0.4849 0.4066 -0.0219 -0.0216 0.0912  1292 ALA B CA    
4332 C  C     . ALA B 75  ? 0.5871 0.4765 0.4075 -0.0177 -0.0262 0.0835  1292 ALA B C     
4333 O  O     . ALA B 75  ? 0.7941 0.6820 0.6162 -0.0134 -0.0326 0.0855  1292 ALA B O     
4334 C  CB    . ALA B 75  ? 0.7830 0.6808 0.5783 -0.0233 -0.0205 0.0894  1292 ALA B CB    
4335 N  N     . ALA B 76  ? 0.5092 0.4029 0.3381 -0.0188 -0.0231 0.0749  1293 ALA B N     
4336 C  CA    . ALA B 76  ? 0.6416 0.5369 0.4825 -0.0154 -0.0266 0.0685  1293 ALA B CA    
4337 C  C     . ALA B 76  ? 0.7101 0.5968 0.5600 -0.0126 -0.0290 0.0725  1293 ALA B C     
4338 O  O     . ALA B 76  ? 0.8163 0.7037 0.6703 -0.0086 -0.0347 0.0727  1293 ALA B O     
4339 C  CB    . ALA B 76  ? 0.6543 0.5532 0.5031 -0.0173 -0.0220 0.0605  1293 ALA B CB    
4340 N  N     . LEU B 77  ? 0.7627 0.6417 0.6160 -0.0147 -0.0248 0.0754  1294 LEU B N     
4341 C  CA    . LEU B 77  ? 0.7425 0.6132 0.6050 -0.0119 -0.0263 0.0777  1294 LEU B CA    
4342 C  C     . LEU B 77  ? 0.8871 0.7522 0.7455 -0.0085 -0.0315 0.0855  1294 LEU B C     
4343 O  O     . LEU B 77  ? 0.9159 0.7780 0.7826 -0.0041 -0.0351 0.0858  1294 LEU B O     
4344 C  CB    . LEU B 77  ? 0.6708 0.5346 0.5364 -0.0155 -0.0207 0.0785  1294 LEU B CB    
4345 C  CG    . LEU B 77  ? 0.7608 0.6186 0.6381 -0.0133 -0.0203 0.0764  1294 LEU B CG    
4346 C  CD1   . LEU B 77  ? 0.6921 0.5567 0.5785 -0.0105 -0.0213 0.0692  1294 LEU B CD1   
4347 C  CD2   . LEU B 77  ? 0.7563 0.6096 0.6353 -0.0178 -0.0148 0.0756  1294 LEU B CD2   
4348 N  N     . GLU B 78  ? 0.9061 0.7703 0.7517 -0.0102 -0.0319 0.0919  1295 GLU B N     
4349 C  CA    . GLU B 78  ? 0.9603 0.8181 0.8001 -0.0071 -0.0366 0.1010  1295 GLU B CA    
4350 C  C     . GLU B 78  ? 1.0571 0.9234 0.8909 -0.0035 -0.0432 0.1009  1295 GLU B C     
4351 O  O     . GLU B 78  ? 1.0477 0.9190 0.8685 -0.0051 -0.0436 0.1034  1295 GLU B O     
4352 C  CB    . GLU B 78  ? 1.0950 0.9456 0.9243 -0.0114 -0.0328 0.1094  1295 GLU B CB    
4353 C  CG    . GLU B 78  ? 1.2150 1.0582 1.0514 -0.0157 -0.0265 0.1082  1295 GLU B CG    
4354 C  CD    . GLU B 78  ? 1.3814 1.2133 1.2115 -0.0195 -0.0236 0.1179  1295 GLU B CD    
4355 O  OE1   . GLU B 78  ? 1.3433 1.1677 1.1806 -0.0227 -0.0195 0.1171  1295 GLU B OE1   
4356 O  OE2   . GLU B 78  ? 1.4520 1.2827 1.2702 -0.0195 -0.0255 0.1263  1295 GLU B OE2   
4357 N  N     . ARG B 79  ? 1.1340 1.0038 0.9779 0.0011  -0.0482 0.0969  1296 ARG B N     
4358 C  CA    . ARG B 79  ? 1.1052 0.9829 0.9458 0.0050  -0.0555 0.0967  1296 ARG B CA    
4359 C  C     . ARG B 79  ? 1.0295 0.9088 0.8841 0.0101  -0.0605 0.0941  1296 ARG B C     
4360 O  O     . ARG B 79  ? 1.0196 0.8915 0.8780 0.0140  -0.0629 0.0997  1296 ARG B O     
4361 C  CB    . ARG B 79  ? 1.2198 1.1089 1.0539 0.0023  -0.0553 0.0899  1296 ARG B CB    
4362 C  CG    . ARG B 79  ? 1.3855 1.2851 1.2234 0.0055  -0.0624 0.0842  1296 ARG B CG    
4363 C  CD    . ARG B 79  ? 1.4539 1.3627 1.2877 0.0022  -0.0606 0.0756  1296 ARG B CD    
4364 N  NE    . ARG B 79  ? 1.5123 1.4309 1.3473 0.0045  -0.0678 0.0701  1296 ARG B NE    
4365 C  CZ    . ARG B 79  ? 1.4527 1.3781 1.2934 0.0030  -0.0680 0.0604  1296 ARG B CZ    
4366 N  NH1   . ARG B 79  ? 1.3062 1.2302 1.1500 -0.0004 -0.0612 0.0556  1296 ARG B NH1   
4367 N  NH2   . ARG B 79  ? 1.4899 1.4237 1.3328 0.0047  -0.0750 0.0554  1296 ARG B NH2   
4368 N  N     . ASP B 86  ? 1.0317 0.8478 0.9577 0.0301  -0.0470 0.0921  1303 ASP B N     
4369 C  CA    . ASP B 86  ? 0.9897 0.7976 0.9075 0.0232  -0.0427 0.0939  1303 ASP B CA    
4370 C  C     . ASP B 86  ? 1.1843 0.9883 1.1085 0.0216  -0.0376 0.0875  1303 ASP B C     
4371 O  O     . ASP B 86  ? 1.2244 1.0197 1.1549 0.0255  -0.0379 0.0865  1303 ASP B O     
4372 C  CB    . ASP B 86  ? 0.6398 0.4338 0.5502 0.0232  -0.0450 0.1032  1303 ASP B CB    
4373 N  N     . PHE B 87  ? 1.1831 0.9943 1.1058 0.0162  -0.0332 0.0825  1304 PHE B N     
4374 C  CA    . PHE B 87  ? 1.0553 0.8634 0.9810 0.0129  -0.0282 0.0771  1304 PHE B CA    
4375 C  C     . PHE B 87  ? 0.9967 0.7983 0.9145 0.0057  -0.0253 0.0802  1304 PHE B C     
4376 O  O     . PHE B 87  ? 0.9614 0.7646 0.8803 0.0013  -0.0211 0.0754  1304 PHE B O     
4377 C  CB    . PHE B 87  ? 1.0218 0.8424 0.9514 0.0118  -0.0253 0.0697  1304 PHE B CB    
4378 C  CG    . PHE B 87  ? 0.8782 0.7084 0.8150 0.0173  -0.0274 0.0670  1304 PHE B CG    
4379 C  CD1   . PHE B 87  ? 0.9739 0.8056 0.9195 0.0215  -0.0260 0.0620  1304 PHE B CD1   
4380 C  CD2   . PHE B 87  ? 0.6284 0.4671 0.5636 0.0179  -0.0305 0.0690  1304 PHE B CD2   
4381 C  CE1   . PHE B 87  ? 0.8975 0.7390 0.8505 0.0260  -0.0273 0.0599  1304 PHE B CE1   
4382 C  CE2   . PHE B 87  ? 0.6482 0.4961 0.5914 0.0222  -0.0324 0.0666  1304 PHE B CE2   
4383 C  CZ    . PHE B 87  ? 0.7844 0.6340 0.7368 0.0261  -0.0305 0.0623  1304 PHE B CZ    
4384 N  N     . ALA B 88  ? 1.0001 0.7957 0.9101 0.0042  -0.0273 0.0884  1305 ALA B N     
4385 C  CA    . ALA B 88  ? 0.8465 0.6385 0.7481 -0.0032 -0.0241 0.0925  1305 ALA B CA    
4386 C  C     . ALA B 88  ? 0.8032 0.5881 0.7089 -0.0079 -0.0198 0.0889  1305 ALA B C     
4387 O  O     . ALA B 88  ? 0.7388 0.5284 0.6415 -0.0142 -0.0157 0.0872  1305 ALA B O     
4388 C  CB    . ALA B 88  ? 0.6653 0.4484 0.5588 -0.0030 -0.0271 0.1030  1305 ALA B CB    
4389 N  N     . PRO B 89  ? 0.7862 0.5607 0.6992 -0.0048 -0.0206 0.0870  1306 PRO B N     
4390 C  CA    . PRO B 89  ? 0.7920 0.5601 0.7091 -0.0096 -0.0170 0.0827  1306 PRO B CA    
4391 C  C     . PRO B 89  ? 0.8533 0.6329 0.7743 -0.0115 -0.0136 0.0734  1306 PRO B C     
4392 O  O     . PRO B 89  ? 0.8051 0.5814 0.7286 -0.0163 -0.0107 0.0698  1306 PRO B O     
4393 C  CB    . PRO B 89  ? 0.7632 0.5184 0.6874 -0.0042 -0.0196 0.0817  1306 PRO B CB    
4394 C  CG    . PRO B 89  ? 0.8224 0.5723 0.7430 0.0007  -0.0241 0.0901  1306 PRO B CG    
4395 C  CD    . PRO B 89  ? 0.8401 0.6059 0.7571 0.0025  -0.0252 0.0898  1306 PRO B CD    
4396 N  N     . GLU B 90  ? 0.7689 0.5617 0.6904 -0.0082 -0.0141 0.0698  1307 GLU B N     
4397 C  CA    . GLU B 90  ? 0.5053 0.3087 0.4303 -0.0089 -0.0113 0.0617  1307 GLU B CA    
4398 C  C     . GLU B 90  ? 0.4762 0.2897 0.3961 -0.0142 -0.0086 0.0615  1307 GLU B C     
4399 O  O     . GLU B 90  ? 0.5675 0.3898 0.4899 -0.0148 -0.0065 0.0554  1307 GLU B O     
4400 C  CB    . GLU B 90  ? 0.5149 0.3259 0.4449 -0.0021 -0.0131 0.0579  1307 GLU B CB    
4401 C  CG    . GLU B 90  ? 0.8307 0.6350 0.7678 0.0036  -0.0144 0.0548  1307 GLU B CG    
4402 C  CD    . GLU B 90  ? 1.0183 0.8326 0.9612 0.0090  -0.0140 0.0490  1307 GLU B CD    
4403 O  OE1   . GLU B 90  ? 1.0263 0.8515 0.9685 0.0092  -0.0139 0.0490  1307 GLU B OE1   
4404 O  OE2   . GLU B 90  ? 0.9931 0.8043 0.9413 0.0128  -0.0136 0.0443  1307 GLU B OE2   
4405 N  N     . VAL B 91  ? 0.5151 0.3278 0.4277 -0.0178 -0.0085 0.0677  1308 VAL B N     
4406 C  CA    . VAL B 91  ? 0.6011 0.4243 0.5085 -0.0219 -0.0060 0.0671  1308 VAL B CA    
4407 C  C     . VAL B 91  ? 0.6278 0.4505 0.5349 -0.0289 -0.0017 0.0660  1308 VAL B C     
4408 O  O     . VAL B 91  ? 0.6766 0.4901 0.5818 -0.0329 -0.0008 0.0711  1308 VAL B O     
4409 C  CB    . VAL B 91  ? 0.6344 0.4587 0.5330 -0.0218 -0.0081 0.0740  1308 VAL B CB    
4410 C  CG1   . VAL B 91  ? 0.6330 0.4683 0.5259 -0.0257 -0.0054 0.0726  1308 VAL B CG1   
4411 C  CG2   . VAL B 91  ? 0.6972 0.5234 0.5976 -0.0151 -0.0128 0.0744  1308 VAL B CG2   
4412 N  N     . ALA B 92  ? 0.6455 0.4784 0.5547 -0.0306 0.0009  0.0599  1309 ALA B N     
4413 C  CA    . ALA B 92  ? 0.5455 0.3809 0.4554 -0.0372 0.0049  0.0583  1309 ALA B CA    
4414 C  C     . ALA B 92  ? 0.6608 0.5031 0.5629 -0.0409 0.0071  0.0621  1309 ALA B C     
4415 O  O     . ALA B 92  ? 0.7478 0.5987 0.6467 -0.0382 0.0063  0.0606  1309 ALA B O     
4416 C  CB    . ALA B 92  ? 0.4580 0.3018 0.3741 -0.0367 0.0064  0.0499  1309 ALA B CB    
4417 N  N     . TRP B 93  ? 0.4852 0.3236 0.3844 -0.0471 0.0098  0.0670  1310 TRP B N     
4418 C  CA    . TRP B 93  ? 0.5260 0.3704 0.4165 -0.0506 0.0123  0.0718  1310 TRP B CA    
4419 C  C     . TRP B 93  ? 0.6887 0.5423 0.5811 -0.0568 0.0175  0.0688  1310 TRP B C     
4420 O  O     . TRP B 93  ? 0.7717 0.6208 0.6688 -0.0623 0.0200  0.0695  1310 TRP B O     
4421 C  CB    . TRP B 93  ? 0.5310 0.3645 0.4149 -0.0526 0.0116  0.0819  1310 TRP B CB    
4422 C  CG    . TRP B 93  ? 0.7980 0.6270 0.6781 -0.0461 0.0065  0.0851  1310 TRP B CG    
4423 C  CD1   . TRP B 93  ? 0.9006 0.7186 0.7850 -0.0417 0.0025  0.0865  1310 TRP B CD1   
4424 C  CD2   . TRP B 93  ? 0.8317 0.6683 0.7038 -0.0429 0.0044  0.0866  1310 TRP B CD2   
4425 N  NE1   . TRP B 93  ? 0.9055 0.7242 0.7853 -0.0359 -0.0019 0.0892  1310 TRP B NE1   
4426 C  CE2   . TRP B 93  ? 0.8000 0.6300 0.6722 -0.0368 -0.0011 0.0892  1310 TRP B CE2   
4427 C  CE3   . TRP B 93  ? 0.8393 0.6879 0.7043 -0.0444 0.0065  0.0854  1310 TRP B CE3   
4428 C  CZ2   . TRP B 93  ? 0.6816 0.5170 0.5475 -0.0326 -0.0048 0.0906  1310 TRP B CZ2   
4429 C  CZ3   . TRP B 93  ? 0.7640 0.6170 0.6221 -0.0402 0.0028  0.0865  1310 TRP B CZ3   
4430 C  CH2   . TRP B 93  ? 0.6653 0.5119 0.5240 -0.0346 -0.0029 0.0892  1310 TRP B CH2   
4431 N  N     . VAL B 94  ? 0.7071 0.5735 0.5964 -0.0561 0.0191  0.0652  1311 VAL B N     
4432 C  CA    . VAL B 94  ? 0.7561 0.6324 0.6452 -0.0620 0.0245  0.0641  1311 VAL B CA    
4433 C  C     . VAL B 94  ? 0.7532 0.6276 0.6325 -0.0661 0.0268  0.0731  1311 VAL B C     
4434 O  O     . VAL B 94  ? 0.8366 0.7111 0.7066 -0.0628 0.0246  0.0768  1311 VAL B O     
4435 C  CB    . VAL B 94  ? 0.6916 0.5821 0.5809 -0.0591 0.0254  0.0569  1311 VAL B CB    
4436 C  CG1   . VAL B 94  ? 0.6277 0.5294 0.5170 -0.0648 0.0312  0.0558  1311 VAL B CG1   
4437 C  CG2   . VAL B 94  ? 0.5258 0.4176 0.4240 -0.0547 0.0229  0.0492  1311 VAL B CG2   
4438 N  N     . THR B 95  ? 0.7453 0.6178 0.6267 -0.0734 0.0311  0.0767  1312 THR B N     
4439 C  CA    . THR B 95  ? 0.7606 0.6310 0.6331 -0.0784 0.0342  0.0863  1312 THR B CA    
4440 C  C     . THR B 95  ? 0.7600 0.6442 0.6320 -0.0847 0.0411  0.0854  1312 THR B C     
4441 O  O     . THR B 95  ? 0.7293 0.6157 0.5918 -0.0884 0.0445  0.0930  1312 THR B O     
4442 C  CB    . THR B 95  ? 0.7521 0.6059 0.6276 -0.0824 0.0336  0.0934  1312 THR B CB    
4443 O  OG1   . THR B 95  ? 0.7240 0.5790 0.6102 -0.0890 0.0373  0.0900  1312 THR B OG1   
4444 C  CG2   . THR B 95  ? 0.6658 0.5077 0.5453 -0.0757 0.0272  0.0916  1312 THR B CG2   
4445 N  N     . LYS B 96  ? 0.7797 0.6740 0.6615 -0.0857 0.0431  0.0766  1313 LYS B N     
4446 C  CA    . LYS B 96  ? 0.7526 0.6596 0.6385 -0.0924 0.0496  0.0749  1313 LYS B CA    
4447 C  C     . LYS B 96  ? 0.8263 0.7488 0.7178 -0.0887 0.0502  0.0640  1313 LYS B C     
4448 O  O     . LYS B 96  ? 0.8347 0.7555 0.7329 -0.0838 0.0461  0.0572  1313 LYS B O     
4449 C  CB    . LYS B 96  ? 0.5216 0.4212 0.4181 -0.0995 0.0512  0.0762  1313 LYS B CB    
4450 C  CG    . LYS B 96  ? 0.6208 0.5280 0.5198 -0.1090 0.0583  0.0799  1313 LYS B CG    
4451 C  CD    . LYS B 96  ? 0.7405 0.6462 0.6546 -0.1146 0.0589  0.0752  1313 LYS B CD    
4452 C  CE    . LYS B 96  ? 0.7122 0.5983 0.6290 -0.1186 0.0569  0.0816  1313 LYS B CE    
4453 N  NZ    . LYS B 96  ? 0.7961 0.6833 0.7196 -0.1299 0.0627  0.0861  1313 LYS B NZ    
4454 N  N     . SER B 97  ? 0.6925 0.6300 0.5811 -0.0908 0.0554  0.0626  1314 SER B N     
4455 C  CA    . SER B 97  ? 0.6481 0.6009 0.5433 -0.0879 0.0567  0.0526  1314 SER B CA    
4456 C  C     . SER B 97  ? 0.6948 0.6579 0.5995 -0.0956 0.0626  0.0513  1314 SER B C     
4457 O  O     . SER B 97  ? 0.7335 0.7069 0.6346 -0.1002 0.0687  0.0542  1314 SER B O     
4458 C  CB    . SER B 97  ? 0.7309 0.6941 0.6167 -0.0829 0.0575  0.0499  1314 SER B CB    
4459 O  OG    . SER B 97  ? 0.8548 0.8325 0.7383 -0.0872 0.0644  0.0501  1314 SER B OG    
4460 N  N     . GLY B 98  ? 0.7059 0.6660 0.6226 -0.0974 0.0608  0.0473  1315 GLY B N     
4461 C  CA    . GLY B 98  ? 0.6572 0.6274 0.5851 -0.1046 0.0655  0.0450  1315 GLY B CA    
4462 C  C     . GLY B 98  ? 0.7038 0.6648 0.6313 -0.1138 0.0686  0.0543  1315 GLY B C     
4463 O  O     . GLY B 98  ? 0.6692 0.6142 0.5990 -0.1150 0.0649  0.0571  1315 GLY B O     
4464 N  N     . ASP B 99  ? 0.8235 0.7942 0.7481 -0.1203 0.0757  0.0593  1316 ASP B N     
4465 C  CA    . ASP B 99  ? 0.7180 0.6792 0.6392 -0.1289 0.0794  0.0705  1316 ASP B CA    
4466 C  C     . ASP B 99  ? 0.8039 0.7607 0.7079 -0.1271 0.0805  0.0797  1316 ASP B C     
4467 O  O     . ASP B 99  ? 0.8800 0.8247 0.7789 -0.1324 0.0818  0.0903  1316 ASP B O     
4468 C  CB    . ASP B 99  ? 0.7528 0.7274 0.6837 -0.1391 0.0870  0.0712  1316 ASP B CB    
4469 C  CG    . ASP B 99  ? 0.9308 0.8960 0.8756 -0.1465 0.0858  0.0711  1316 ASP B CG    
4470 O  OD1   . ASP B 99  ? 1.0393 1.0156 0.9952 -0.1551 0.0912  0.0702  1316 ASP B OD1   
4471 O  OD2   . ASP B 99  ? 0.8383 0.7855 0.7833 -0.1435 0.0794  0.0714  1316 ASP B OD2   
4472 N  N     . SER B 100 ? 0.9792 0.9462 0.8742 -0.1201 0.0803  0.0759  1317 SER B N     
4473 C  CA    . SER B 100 ? 1.0663 1.0308 0.9443 -0.1178 0.0808  0.0835  1317 SER B CA    
4474 C  C     . SER B 100 ? 0.9861 0.9319 0.8579 -0.1118 0.0729  0.0868  1317 SER B C     
4475 O  O     . SER B 100 ? 0.8408 0.7836 0.7163 -0.1046 0.0670  0.0793  1317 SER B O     
4476 C  CB    . SER B 100 ? 1.2224 1.2042 1.0939 -0.1121 0.0827  0.0767  1317 SER B CB    
4477 O  OG    . SER B 100 ? 1.3658 1.3423 1.2222 -0.1059 0.0789  0.0798  1317 SER B OG    
4478 N  N     . GLU B 101 ? 1.0111 0.9443 0.8736 -0.1147 0.0728  0.0984  1318 GLU B N     
4479 C  CA    . GLU B 101 ? 0.9176 0.8339 0.7741 -0.1089 0.0655  0.1023  1318 GLU B CA    
4480 C  C     . GLU B 101 ? 0.7924 0.7139 0.6352 -0.1013 0.0627  0.1016  1318 GLU B C     
4481 O  O     . GLU B 101 ? 0.7561 0.6887 0.5884 -0.1027 0.0671  0.1044  1318 GLU B O     
4482 C  CB    . GLU B 101 ? 0.9574 0.8576 0.8102 -0.1144 0.0660  0.1152  1318 GLU B CB    
4483 C  CG    . GLU B 101 ? 1.0747 0.9558 0.9311 -0.1100 0.0585  0.1160  1318 GLU B CG    
4484 C  CD    . GLU B 101 ? 1.1965 1.0612 1.0446 -0.1117 0.0570  0.1291  1318 GLU B CD    
4485 O  OE1   . GLU B 101 ? 1.2436 1.0956 1.0897 -0.1051 0.0502  0.1303  1318 GLU B OE1   
4486 O  OE2   . GLU B 101 ? 1.2050 1.0696 1.0492 -0.1194 0.0628  0.1384  1318 GLU B OE2   
4487 N  N     . LEU B 102 ? 0.7603 0.6740 0.6034 -0.0935 0.0552  0.0977  1319 LEU B N     
4488 C  CA    . LEU B 102 ? 0.7652 0.6847 0.5988 -0.0859 0.0515  0.0939  1319 LEU B CA    
4489 C  C     . LEU B 102 ? 0.8177 0.7312 0.6360 -0.0847 0.0495  0.1040  1319 LEU B C     
4490 O  O     . LEU B 102 ? 0.8194 0.7180 0.6364 -0.0858 0.0470  0.1127  1319 LEU B O     
4491 C  CB    . LEU B 102 ? 0.6583 0.5716 0.4990 -0.0787 0.0444  0.0868  1319 LEU B CB    
4492 C  CG    . LEU B 102 ? 0.7348 0.6556 0.5874 -0.0761 0.0441  0.0752  1319 LEU B CG    
4493 C  CD1   . LEU B 102 ? 0.6983 0.6103 0.5551 -0.0692 0.0370  0.0716  1319 LEU B CD1   
4494 C  CD2   . LEU B 102 ? 0.8399 0.7774 0.6890 -0.0742 0.0471  0.0684  1319 LEU B CD2   
4495 N  N     . ALA B 103 ? 0.8697 0.7945 0.6764 -0.0816 0.0500  0.1023  1320 ALA B N     
4496 C  CA    . ALA B 103 ? 0.8854 0.8066 0.6762 -0.0795 0.0474  0.1110  1320 ALA B CA    
4497 C  C     . ALA B 103 ? 0.9429 0.8483 0.7352 -0.0745 0.0392  0.1142  1320 ALA B C     
4498 O  O     . ALA B 103 ? 1.0210 0.9136 0.8101 -0.0766 0.0381  0.1248  1320 ALA B O     
4499 C  CB    . ALA B 103 ? 0.8366 0.7725 0.6165 -0.0751 0.0472  0.1051  1320 ALA B CB    
4500 N  N     . GLU B 104 ? 0.9393 0.8455 0.7368 -0.0678 0.0335  0.1053  1321 GLU B N     
4501 C  CA    . GLU B 104 ? 0.8937 0.7869 0.6966 -0.0630 0.0263  0.1061  1321 GLU B CA    
4502 C  C     . GLU B 104 ? 0.8857 0.7762 0.7049 -0.0623 0.0258  0.0978  1321 GLU B C     
4503 O  O     . GLU B 104 ? 0.9941 0.8951 0.8189 -0.0625 0.0285  0.0889  1321 GLU B O     
4504 C  CB    . GLU B 104 ? 0.9060 0.8024 0.7020 -0.0558 0.0197  0.1032  1321 GLU B CB    
4505 N  N     . PRO B 105 ? 0.8704 0.7473 0.6970 -0.0611 0.0223  0.1004  1322 PRO B N     
4506 C  CA    . PRO B 105 ? 0.8586 0.7336 0.6993 -0.0596 0.0213  0.0921  1322 PRO B CA    
4507 C  C     . PRO B 105 ? 0.7658 0.6458 0.6093 -0.0526 0.0166  0.0841  1322 PRO B C     
4508 O  O     . PRO B 105 ? 0.7609 0.6411 0.5977 -0.0482 0.0122  0.0857  1322 PRO B O     
4509 C  CB    . PRO B 105 ? 0.6934 0.5521 0.5392 -0.0597 0.0186  0.0977  1322 PRO B CB    
4510 C  CG    . PRO B 105 ? 0.8437 0.6953 0.6792 -0.0624 0.0192  0.1094  1322 PRO B CG    
4511 C  CD    . PRO B 105 ? 0.9115 0.7741 0.7339 -0.0611 0.0194  0.1109  1322 PRO B CD    
4512 N  N     . ILE B 106 ? 0.5489 0.4329 0.4028 -0.0518 0.0175  0.0756  1323 ILE B N     
4513 C  CA    . ILE B 106 ? 0.5729 0.4602 0.4312 -0.0458 0.0134  0.0686  1323 ILE B CA    
4514 C  C     . ILE B 106 ? 0.5842 0.4630 0.4530 -0.0437 0.0112  0.0668  1323 ILE B C     
4515 O  O     . ILE B 106 ? 0.6276 0.5018 0.5019 -0.0473 0.0137  0.0674  1323 ILE B O     
4516 C  CB    . ILE B 106 ? 0.5412 0.4412 0.4018 -0.0452 0.0158  0.0600  1323 ILE B CB    
4517 C  CG1   . ILE B 106 ? 0.6253 0.5292 0.4929 -0.0496 0.0209  0.0569  1323 ILE B CG1   
4518 C  CG2   . ILE B 106 ? 0.4843 0.3934 0.3341 -0.0455 0.0171  0.0601  1323 ILE B CG2   
4519 C  CD1   . ILE B 106 ? 0.6369 0.5539 0.5051 -0.0495 0.0239  0.0499  1323 ILE B CD1   
4520 N  N     . ALA B 107 ? 0.4873 0.3645 0.3592 -0.0381 0.0065  0.0644  1324 ALA B N     
4521 C  CA    . ALA B 107 ? 0.4868 0.3564 0.3674 -0.0353 0.0042  0.0632  1324 ALA B CA    
4522 C  C     . ALA B 107 ? 0.4521 0.3278 0.3405 -0.0327 0.0043  0.0551  1324 ALA B C     
4523 O  O     . ALA B 107 ? 0.4462 0.3289 0.3337 -0.0302 0.0031  0.0516  1324 ALA B O     
4524 C  CB    . ALA B 107 ? 0.4714 0.3345 0.3503 -0.0307 -0.0010 0.0674  1324 ALA B CB    
4525 N  N     . VAL B 108 ? 0.4471 0.3196 0.3432 -0.0328 0.0053  0.0523  1325 VAL B N     
4526 C  CA    . VAL B 108 ? 0.4863 0.3638 0.3892 -0.0297 0.0050  0.0458  1325 VAL B CA    
4527 C  C     . VAL B 108 ? 0.5551 0.4296 0.4608 -0.0242 0.0010  0.0462  1325 VAL B C     
4528 O  O     . VAL B 108 ? 0.7477 0.6142 0.6548 -0.0226 -0.0009 0.0493  1325 VAL B O     
4529 C  CB    . VAL B 108 ? 0.5521 0.4284 0.4614 -0.0315 0.0073  0.0424  1325 VAL B CB    
4530 C  CG1   . VAL B 108 ? 0.4198 0.3018 0.3348 -0.0280 0.0069  0.0365  1325 VAL B CG1   
4531 C  CG2   . VAL B 108 ? 0.5052 0.3858 0.4131 -0.0374 0.0112  0.0421  1325 VAL B CG2   
4532 N  N     . ARG B 109 ? 0.5266 0.4075 0.4338 -0.0214 -0.0002 0.0428  1326 ARG B N     
4533 C  CA    . ARG B 109 ? 0.5841 0.4640 0.4936 -0.0171 -0.0040 0.0437  1326 ARG B CA    
4534 C  C     . ARG B 109 ? 0.5446 0.4200 0.4609 -0.0141 -0.0046 0.0432  1326 ARG B C     
4535 O  O     . ARG B 109 ? 0.6220 0.4984 0.5425 -0.0142 -0.0024 0.0397  1326 ARG B O     
4536 C  CB    . ARG B 109 ? 0.6970 0.5843 0.6084 -0.0155 -0.0048 0.0396  1326 ARG B CB    
4537 C  CG    . ARG B 109 ? 0.5979 0.4891 0.5148 -0.0150 -0.0023 0.0347  1326 ARG B CG    
4538 C  CD    . ARG B 109 ? 0.5379 0.4329 0.4602 -0.0118 -0.0039 0.0321  1326 ARG B CD    
4539 N  NE    . ARG B 109 ? 0.5830 0.4817 0.5084 -0.0117 -0.0014 0.0282  1326 ARG B NE    
4540 C  CZ    . ARG B 109 ? 0.6046 0.5080 0.5289 -0.0124 -0.0005 0.0250  1326 ARG B CZ    
4541 N  NH1   . ARG B 109 ? 0.6808 0.5860 0.6005 -0.0135 -0.0017 0.0247  1326 ARG B NH1   
4542 N  NH2   . ARG B 109 ? 0.5131 0.4197 0.4408 -0.0116 0.0014  0.0219  1326 ARG B NH2   
4543 N  N     . PRO B 110 ? 0.5851 0.4563 0.5027 -0.0110 -0.0077 0.0464  1327 PRO B N     
4544 C  CA    . PRO B 110 ? 0.6361 0.5049 0.5607 -0.0072 -0.0081 0.0451  1327 PRO B CA    
4545 C  C     . PRO B 110 ? 0.5855 0.4602 0.5153 -0.0037 -0.0099 0.0437  1327 PRO B C     
4546 O  O     . PRO B 110 ? 0.6290 0.5046 0.5649 -0.0006 -0.0094 0.0419  1327 PRO B O     
4547 C  CB    . PRO B 110 ? 0.6332 0.4932 0.5566 -0.0060 -0.0103 0.0498  1327 PRO B CB    
4548 C  CG    . PRO B 110 ? 0.6326 0.4934 0.5493 -0.0071 -0.0128 0.0541  1327 PRO B CG    
4549 C  CD    . PRO B 110 ? 0.6223 0.4897 0.5343 -0.0111 -0.0105 0.0519  1327 PRO B CD    
4550 N  N     . THR B 111 ? 0.4639 0.3429 0.3913 -0.0043 -0.0119 0.0443  1328 THR B N     
4551 C  CA    . THR B 111 ? 0.4508 0.3358 0.3831 -0.0022 -0.0140 0.0430  1328 THR B CA    
4552 C  C     . THR B 111 ? 0.5410 0.4287 0.4672 -0.0042 -0.0164 0.0435  1328 THR B C     
4553 O  O     . THR B 111 ? 0.6633 0.5482 0.5817 -0.0063 -0.0164 0.0459  1328 THR B O     
4554 C  CB    . THR B 111 ? 0.5918 0.4764 0.5307 0.0019  -0.0165 0.0448  1328 THR B CB    
4555 O  OG1   . THR B 111 ? 0.6257 0.5170 0.5716 0.0032  -0.0172 0.0429  1328 THR B OG1   
4556 C  CG2   . THR B 111 ? 0.6906 0.5720 0.6261 0.0032  -0.0206 0.0492  1328 THR B CG2   
4557 N  N     . SER B 112 ? 0.5581 0.4514 0.4879 -0.0037 -0.0182 0.0411  1329 SER B N     
4558 C  CA    . SER B 112 ? 0.6049 0.5017 0.5290 -0.0057 -0.0199 0.0394  1329 SER B CA    
4559 C  C     . SER B 112 ? 0.6402 0.5398 0.5644 -0.0044 -0.0252 0.0404  1329 SER B C     
4560 O  O     . SER B 112 ? 0.7685 0.6717 0.6885 -0.0058 -0.0270 0.0378  1329 SER B O     
4561 C  CB    . SER B 112 ? 0.5140 0.4147 0.4412 -0.0068 -0.0180 0.0343  1329 SER B CB    
4562 O  OG    . SER B 112 ? 0.3964 0.2959 0.3263 -0.0069 -0.0138 0.0331  1329 SER B OG    
4563 N  N     . GLU B 113 ? 0.5307 0.4291 0.4590 -0.0017 -0.0279 0.0438  1330 GLU B N     
4564 C  CA    . GLU B 113 ? 0.5216 0.4238 0.4505 -0.0002 -0.0336 0.0446  1330 GLU B CA    
4565 C  C     . GLU B 113 ? 0.5821 0.4847 0.4990 -0.0018 -0.0359 0.0457  1330 GLU B C     
4566 O  O     . GLU B 113 ? 0.6390 0.5469 0.5542 -0.0025 -0.0391 0.0426  1330 GLU B O     
4567 C  CB    . GLU B 113 ? 0.5127 0.4131 0.4466 0.0035  -0.0362 0.0488  1330 GLU B CB    
4568 C  CG    . GLU B 113 ? 0.5667 0.4709 0.5137 0.0057  -0.0358 0.0473  1330 GLU B CG    
4569 C  CD    . GLU B 113 ? 0.6178 0.5182 0.5678 0.0062  -0.0304 0.0469  1330 GLU B CD    
4570 O  OE1   . GLU B 113 ? 0.5217 0.4171 0.4644 0.0041  -0.0273 0.0470  1330 GLU B OE1   
4571 O  OE2   . GLU B 113 ? 0.7245 0.6276 0.6841 0.0085  -0.0292 0.0464  1330 GLU B OE2   
4572 N  N     . THR B 114 ? 0.6588 0.5558 0.5673 -0.0025 -0.0340 0.0500  1331 THR B N     
4573 C  CA    . THR B 114 ? 0.6876 0.5847 0.5834 -0.0042 -0.0351 0.0525  1331 THR B CA    
4574 C  C     . THR B 114 ? 0.5984 0.5009 0.4890 -0.0070 -0.0334 0.0471  1331 THR B C     
4575 O  O     . THR B 114 ? 0.5521 0.4573 0.4322 -0.0079 -0.0350 0.0478  1331 THR B O     
4576 C  CB    . THR B 114 ? 0.7236 0.6131 0.6134 -0.0056 -0.0316 0.0579  1331 THR B CB    
4577 O  OG1   . THR B 114 ? 0.8298 0.7163 0.7260 -0.0067 -0.0266 0.0555  1331 THR B OG1   
4578 C  CG2   . THR B 114 ? 0.5095 0.3933 0.3992 -0.0024 -0.0352 0.0644  1331 THR B CG2   
4579 N  N     . VAL B 115 ? 0.7566 0.6606 0.6535 -0.0081 -0.0300 0.0419  1332 VAL B N     
4580 C  CA    . VAL B 115 ? 0.8074 0.7160 0.7004 -0.0102 -0.0281 0.0364  1332 VAL B CA    
4581 C  C     . VAL B 115 ? 0.7103 0.6232 0.6108 -0.0093 -0.0311 0.0304  1332 VAL B C     
4582 O  O     . VAL B 115 ? 0.7387 0.6559 0.6346 -0.0099 -0.0330 0.0259  1332 VAL B O     
4583 C  CB    . VAL B 115 ? 0.7749 0.6818 0.6686 -0.0121 -0.0219 0.0350  1332 VAL B CB    
4584 C  CG1   . VAL B 115 ? 0.8185 0.7302 0.7053 -0.0140 -0.0198 0.0307  1332 VAL B CG1   
4585 C  CG2   . VAL B 115 ? 0.9241 0.8255 0.8141 -0.0132 -0.0194 0.0409  1332 VAL B CG2   
4586 N  N     . MET B 116 ? 0.5460 0.4577 0.4579 -0.0080 -0.0316 0.0302  1333 MET B N     
4587 C  CA    . MET B 116 ? 0.4928 0.4079 0.4134 -0.0078 -0.0341 0.0254  1333 MET B CA    
4588 C  C     . MET B 116 ? 0.4928 0.4120 0.4140 -0.0070 -0.0406 0.0250  1333 MET B C     
4589 O  O     . MET B 116 ? 0.5555 0.4781 0.4795 -0.0078 -0.0435 0.0195  1333 MET B O     
4590 C  CB    . MET B 116 ? 0.6239 0.5372 0.5564 -0.0070 -0.0319 0.0263  1333 MET B CB    
4591 C  CG    . MET B 116 ? 0.7616 0.6729 0.6956 -0.0077 -0.0266 0.0243  1333 MET B CG    
4592 S  SD    . MET B 116 ? 0.9281 0.8386 0.8751 -0.0066 -0.0245 0.0253  1333 MET B SD    
4593 C  CE    . MET B 116 ? 0.8633 0.7774 0.8189 -0.0074 -0.0290 0.0219  1333 MET B CE    
4594 N  N     . TYR B 117 ? 0.5901 0.5088 0.5088 -0.0052 -0.0435 0.0302  1334 TYR B N     
4595 C  CA    . TYR B 117 ? 0.6587 0.5827 0.5802 -0.0041 -0.0503 0.0293  1334 TYR B CA    
4596 C  C     . TYR B 117 ? 0.8080 0.7359 0.7177 -0.0048 -0.0539 0.0263  1334 TYR B C     
4597 O  O     . TYR B 117 ? 0.9447 0.8779 0.8578 -0.0051 -0.0590 0.0214  1334 TYR B O     
4598 C  CB    . TYR B 117 ? 0.4742 0.3975 0.3983 -0.0011 -0.0531 0.0355  1334 TYR B CB    
4599 C  CG    . TYR B 117 ? 0.6050 0.5267 0.5420 0.0001  -0.0502 0.0368  1334 TYR B CG    
4600 C  CD1   . TYR B 117 ? 0.6608 0.5829 0.6062 -0.0017 -0.0467 0.0329  1334 TYR B CD1   
4601 C  CD2   . TYR B 117 ? 0.6467 0.5663 0.5868 0.0032  -0.0507 0.0420  1334 TYR B CD2   
4602 C  CE1   . TYR B 117 ? 0.6600 0.5815 0.6159 -0.0006 -0.0435 0.0345  1334 TYR B CE1   
4603 C  CE2   . TYR B 117 ? 0.6738 0.5928 0.6249 0.0046  -0.0476 0.0427  1334 TYR B CE2   
4604 C  CZ    . TYR B 117 ? 0.6654 0.5858 0.6239 0.0025  -0.0439 0.0390  1334 TYR B CZ    
4605 O  OH    . TYR B 117 ? 0.6999 0.6206 0.6682 0.0040  -0.0405 0.0401  1334 TYR B OH    
4606 N  N     . PRO B 118 ? 0.7333 0.6593 0.6294 -0.0054 -0.0514 0.0289  1335 PRO B N     
4607 C  CA    . PRO B 118 ? 0.5931 0.5239 0.4777 -0.0062 -0.0538 0.0249  1335 PRO B CA    
4608 C  C     . PRO B 118 ? 0.5667 0.5001 0.4554 -0.0078 -0.0529 0.0158  1335 PRO B C     
4609 O  O     . PRO B 118 ? 0.4652 0.4037 0.3517 -0.0078 -0.0578 0.0099  1335 PRO B O     
4610 C  CB    . PRO B 118 ? 0.4687 0.3967 0.3401 -0.0072 -0.0489 0.0297  1335 PRO B CB    
4611 C  CG    . PRO B 118 ? 0.4661 0.3880 0.3407 -0.0062 -0.0473 0.0371  1335 PRO B CG    
4612 C  CD    . PRO B 118 ? 0.4535 0.3735 0.3438 -0.0054 -0.0468 0.0354  1335 PRO B CD    
4613 N  N     . ALA B 119 ? 0.5913 0.5210 0.4862 -0.0089 -0.0473 0.0142  1336 ALA B N     
4614 C  CA    . ALA B 119 ? 0.6513 0.5820 0.5518 -0.0099 -0.0468 0.0060  1336 ALA B CA    
4615 C  C     . ALA B 119 ? 0.6397 0.5725 0.5514 -0.0099 -0.0525 0.0023  1336 ALA B C     
4616 O  O     . ALA B 119 ? 0.5537 0.4897 0.4650 -0.0105 -0.0560 -0.0049 1336 ALA B O     
4617 C  CB    . ALA B 119 ? 0.5772 0.5034 0.4844 -0.0104 -0.0405 0.0062  1336 ALA B CB    
4618 N  N     . TYR B 120 ? 0.6732 0.6051 0.5948 -0.0093 -0.0537 0.0071  1337 TYR B N     
4619 C  CA    . TYR B 120 ? 0.6111 0.5461 0.5451 -0.0098 -0.0588 0.0044  1337 TYR B CA    
4620 C  C     . TYR B 120 ? 0.5876 0.5289 0.5164 -0.0095 -0.0663 0.0009  1337 TYR B C     
4621 O  O     . TYR B 120 ? 0.6740 0.6185 0.6106 -0.0109 -0.0708 -0.0054 1337 TYR B O     
4622 C  CB    . TYR B 120 ? 0.4939 0.4286 0.4383 -0.0087 -0.0584 0.0106  1337 TYR B CB    
4623 C  CG    . TYR B 120 ? 0.5348 0.4652 0.4887 -0.0093 -0.0526 0.0121  1337 TYR B CG    
4624 C  CD1   . TYR B 120 ? 0.5582 0.4841 0.5085 -0.0101 -0.0473 0.0102  1337 TYR B CD1   
4625 C  CD2   . TYR B 120 ? 0.5813 0.5129 0.5476 -0.0087 -0.0523 0.0156  1337 TYR B CD2   
4626 C  CE1   . TYR B 120 ? 0.7424 0.6649 0.7006 -0.0102 -0.0424 0.0121  1337 TYR B CE1   
4627 C  CE2   . TYR B 120 ? 0.6561 0.5846 0.6298 -0.0090 -0.0468 0.0174  1337 TYR B CE2   
4628 C  CZ    . TYR B 120 ? 0.7242 0.6479 0.6935 -0.0097 -0.0421 0.0158  1337 TYR B CZ    
4629 O  OH    . TYR B 120 ? 0.6375 0.5585 0.6134 -0.0096 -0.0371 0.0179  1337 TYR B OH    
4630 N  N     . ALA B 121 ? 0.5181 0.4613 0.4345 -0.0077 -0.0681 0.0052  1338 ALA B N     
4631 C  CA    . ALA B 121 ? 0.5015 0.4514 0.4107 -0.0070 -0.0755 0.0019  1338 ALA B CA    
4632 C  C     . ALA B 121 ? 0.5379 0.4897 0.4399 -0.0083 -0.0758 -0.0071 1338 ALA B C     
4633 O  O     . ALA B 121 ? 0.6062 0.5635 0.5087 -0.0086 -0.0823 -0.0138 1338 ALA B O     
4634 C  CB    . ALA B 121 ? 0.5035 0.4544 0.3992 -0.0045 -0.0769 0.0094  1338 ALA B CB    
4635 N  N     . LYS B 122 ? 0.5974 0.5454 0.4932 -0.0090 -0.0691 -0.0080 1339 LYS B N     
4636 C  CA    . LYS B 122 ? 0.6629 0.6128 0.5521 -0.0096 -0.0687 -0.0170 1339 LYS B CA    
4637 C  C     . LYS B 122 ? 0.6951 0.6429 0.5984 -0.0112 -0.0699 -0.0252 1339 LYS B C     
4638 O  O     . LYS B 122 ? 0.7504 0.7008 0.6515 -0.0115 -0.0731 -0.0345 1339 LYS B O     
4639 C  CB    . LYS B 122 ? 0.6058 0.5532 0.4857 -0.0096 -0.0610 -0.0155 1339 LYS B CB    
4640 N  N     . TRP B 123 ? 0.5808 0.5235 0.4982 -0.0121 -0.0673 -0.0220 1340 TRP B N     
4641 C  CA    . TRP B 123 ? 0.5860 0.5251 0.5165 -0.0138 -0.0671 -0.0282 1340 TRP B CA    
4642 C  C     . TRP B 123 ? 0.7664 0.7086 0.7087 -0.0155 -0.0742 -0.0317 1340 TRP B C     
4643 O  O     . TRP B 123 ? 0.8001 0.7401 0.7511 -0.0174 -0.0763 -0.0393 1340 TRP B O     
4644 C  CB    . TRP B 123 ? 0.4479 0.3806 0.3869 -0.0141 -0.0605 -0.0227 1340 TRP B CB    
4645 C  CG    . TRP B 123 ? 0.5396 0.4697 0.4692 -0.0129 -0.0540 -0.0221 1340 TRP B CG    
4646 C  CD1   . TRP B 123 ? 0.5128 0.4451 0.4310 -0.0120 -0.0532 -0.0278 1340 TRP B CD1   
4647 C  CD2   . TRP B 123 ? 0.5983 0.5243 0.5294 -0.0123 -0.0476 -0.0158 1340 TRP B CD2   
4648 N  NE1   . TRP B 123 ? 0.5041 0.4344 0.4178 -0.0112 -0.0465 -0.0253 1340 TRP B NE1   
4649 C  CE2   . TRP B 123 ? 0.5965 0.5227 0.5178 -0.0115 -0.0433 -0.0181 1340 TRP B CE2   
4650 C  CE3   . TRP B 123 ? 0.5273 0.4505 0.4669 -0.0124 -0.0451 -0.0090 1340 TRP B CE3   
4651 C  CZ2   . TRP B 123 ? 0.4644 0.3881 0.3850 -0.0109 -0.0372 -0.0137 1340 TRP B CZ2   
4652 C  CZ3   . TRP B 123 ? 0.5350 0.4551 0.4728 -0.0116 -0.0391 -0.0050 1340 TRP B CZ3   
4653 C  CH2   . TRP B 123 ? 0.5280 0.4483 0.4567 -0.0110 -0.0354 -0.0074 1340 TRP B CH2   
4654 N  N     . ILE B 124 ? 0.8243 0.7715 0.7676 -0.0150 -0.0783 -0.0268 1341 ILE B N     
4655 C  CA    . ILE B 124 ? 0.9225 0.8745 0.8777 -0.0166 -0.0854 -0.0301 1341 ILE B CA    
4656 C  C     . ILE B 124 ? 0.9568 0.9155 0.9017 -0.0160 -0.0927 -0.0372 1341 ILE B C     
4657 O  O     . ILE B 124 ? 1.0224 0.9872 0.9586 -0.0139 -0.0968 -0.0338 1341 ILE B O     
4658 C  CB    . ILE B 124 ? 0.8247 0.7798 0.7880 -0.0158 -0.0862 -0.0217 1341 ILE B CB    
4659 C  CG1   . ILE B 124 ? 0.8024 0.7511 0.7747 -0.0163 -0.0786 -0.0157 1341 ILE B CG1   
4660 C  CG2   . ILE B 124 ? 0.7364 0.6986 0.7124 -0.0176 -0.0940 -0.0253 1341 ILE B CG2   
4661 C  CD1   . ILE B 124 ? 0.8240 0.7758 0.8111 -0.0167 -0.0791 -0.0106 1341 ILE B CD1   
4662 N  N     . GLN B 125 ? 0.8702 0.8277 0.8160 -0.0176 -0.0946 -0.0475 1342 GLN B N     
4663 C  CA    . GLN B 125 ? 0.7243 0.6887 0.6616 -0.0171 -0.1021 -0.0560 1342 GLN B CA    
4664 C  C     . GLN B 125 ? 0.6016 0.5715 0.5532 -0.0196 -0.1106 -0.0608 1342 GLN B C     
4665 O  O     . GLN B 125 ? 0.5136 0.4913 0.4583 -0.0188 -0.1183 -0.0664 1342 GLN B O     
4666 C  CB    . GLN B 125 ? 0.5061 0.4672 0.4361 -0.0170 -0.1002 -0.0659 1342 GLN B CB    
4667 N  N     . SER B 126 ? 0.5706 0.5371 0.5417 -0.0226 -0.1095 -0.0589 1343 SER B N     
4668 C  CA    . SER B 126 ? 0.6874 0.6595 0.6749 -0.0259 -0.1170 -0.0634 1343 SER B CA    
4669 C  C     . SER B 126 ? 0.7544 0.7249 0.7597 -0.0279 -0.1134 -0.0552 1343 SER B C     
4670 O  O     . SER B 126 ? 0.6790 0.6430 0.6843 -0.0270 -0.1052 -0.0479 1343 SER B O     
4671 C  CB    . SER B 126 ? 0.6597 0.6285 0.6545 -0.0293 -0.1207 -0.0761 1343 SER B CB    
4672 O  OG    . SER B 126 ? 0.6105 0.5680 0.6106 -0.0307 -0.1137 -0.0767 1343 SER B OG    
4673 N  N     . TYR B 127 ? 0.9726 0.9501 0.9941 -0.0308 -0.1194 -0.0571 1344 TYR B N     
4674 C  CA    . TYR B 127 ? 1.0819 1.0586 1.1226 -0.0336 -0.1156 -0.0508 1344 TYR B CA    
4675 C  C     . TYR B 127 ? 1.1177 1.0830 1.1665 -0.0368 -0.1089 -0.0517 1344 TYR B C     
4676 O  O     . TYR B 127 ? 1.2125 1.1745 1.2705 -0.0376 -0.1025 -0.0439 1344 TYR B O     
4677 C  CB    . TYR B 127 ? 1.1970 1.1837 1.2553 -0.0372 -0.1234 -0.0546 1344 TYR B CB    
4678 C  CG    . TYR B 127 ? 1.3925 1.3775 1.4599 -0.0422 -0.1289 -0.0665 1344 TYR B CG    
4679 C  CD1   . TYR B 127 ? 1.4135 1.3931 1.5006 -0.0480 -0.1264 -0.0676 1344 TYR B CD1   
4680 C  CD2   . TYR B 127 ? 1.4178 1.4064 1.4739 -0.0412 -0.1367 -0.0768 1344 TYR B CD2   
4681 C  CE1   . TYR B 127 ? 1.3632 1.3398 1.4596 -0.0528 -0.1316 -0.0787 1344 TYR B CE1   
4682 C  CE2   . TYR B 127 ? 1.3324 1.3189 1.3972 -0.0457 -0.1421 -0.0887 1344 TYR B CE2   
4683 C  CZ    . TYR B 127 ? 1.3290 1.3089 1.4144 -0.0516 -0.1395 -0.0896 1344 TYR B CZ    
4684 O  OH    . TYR B 127 ? 1.3473 1.3236 1.4423 -0.0563 -0.1448 -0.1014 1344 TYR B OH    
4685 N  N     . ARG B 128 ? 1.0061 0.9652 1.0509 -0.0380 -0.1103 -0.0609 1345 ARG B N     
4686 C  CA    . ARG B 128 ? 1.0326 0.9802 1.0856 -0.0406 -0.1048 -0.0618 1345 ARG B CA    
4687 C  C     . ARG B 128 ? 0.9416 0.8819 0.9855 -0.0373 -0.0954 -0.0536 1345 ARG B C     
4688 O  O     . ARG B 128 ? 0.8867 0.8184 0.9388 -0.0389 -0.0901 -0.0514 1345 ARG B O     
4689 C  CB    . ARG B 128 ? 1.0970 1.0394 1.1469 -0.0417 -0.1089 -0.0744 1345 ARG B CB    
4690 N  N     . ASP B 129 ? 0.7880 0.7314 0.8152 -0.0327 -0.0934 -0.0493 1346 ASP B N     
4691 C  CA    . ASP B 129 ? 0.7534 0.6905 0.7726 -0.0299 -0.0850 -0.0425 1346 ASP B CA    
4692 C  C     . ASP B 129 ? 0.7380 0.6759 0.7647 -0.0297 -0.0799 -0.0317 1346 ASP B C     
4693 O  O     . ASP B 129 ? 0.7208 0.6536 0.7423 -0.0276 -0.0731 -0.0262 1346 ASP B O     
4694 C  CB    . ASP B 129 ? 0.7592 0.6984 0.7578 -0.0258 -0.0844 -0.0425 1346 ASP B CB    
4695 C  CG    . ASP B 129 ? 0.8722 0.8124 0.8614 -0.0254 -0.0892 -0.0535 1346 ASP B CG    
4696 O  OD1   . ASP B 129 ? 0.8553 0.7888 0.8452 -0.0258 -0.0872 -0.0597 1346 ASP B OD1   
4697 O  OD2   . ASP B 129 ? 0.8614 0.8095 0.8427 -0.0244 -0.0951 -0.0561 1346 ASP B OD2   
4698 N  N     . LEU B 130 ? 0.6604 0.6052 0.7000 -0.0316 -0.0831 -0.0292 1347 LEU B N     
4699 C  CA    . LEU B 130 ? 0.5637 0.5106 0.6096 -0.0307 -0.0782 -0.0195 1347 LEU B CA    
4700 C  C     . LEU B 130 ? 0.4962 0.4397 0.5591 -0.0346 -0.0745 -0.0174 1347 LEU B C     
4701 O  O     . LEU B 130 ? 0.6986 0.6432 0.7742 -0.0389 -0.0786 -0.0224 1347 LEU B O     
4702 C  CB    . LEU B 130 ? 0.6458 0.6037 0.6957 -0.0296 -0.0832 -0.0171 1347 LEU B CB    
4703 C  CG    . LEU B 130 ? 0.6701 0.6319 0.7044 -0.0247 -0.0853 -0.0143 1347 LEU B CG    
4704 C  CD1   . LEU B 130 ? 0.5969 0.5696 0.6355 -0.0245 -0.0941 -0.0168 1347 LEU B CD1   
4705 C  CD2   . LEU B 130 ? 0.6660 0.6263 0.6976 -0.0213 -0.0789 -0.0050 1347 LEU B CD2   
4706 N  N     . PRO B 131 ? 0.5713 0.5117 0.6364 -0.0336 -0.0671 -0.0097 1348 PRO B N     
4707 C  CA    . PRO B 131 ? 0.6575 0.5982 0.7121 -0.0290 -0.0621 -0.0028 1348 PRO B CA    
4708 C  C     . PRO B 131 ? 0.7342 0.6670 0.7736 -0.0261 -0.0578 -0.0026 1348 PRO B C     
4709 O  O     . PRO B 131 ? 0.8474 0.7729 0.8861 -0.0272 -0.0559 -0.0057 1348 PRO B O     
4710 C  CB    . PRO B 131 ? 0.6708 0.6128 0.7377 -0.0300 -0.0564 0.0043  1348 PRO B CB    
4711 C  CG    . PRO B 131 ? 0.6399 0.5771 0.7196 -0.0349 -0.0559 0.0021  1348 PRO B CG    
4712 C  CD    . PRO B 131 ? 0.5251 0.4630 0.6066 -0.0376 -0.0637 -0.0069 1348 PRO B CD    
4713 N  N     . ILE B 132 ? 0.7158 0.6502 0.7438 -0.0224 -0.0561 0.0012  1349 ILE B N     
4714 C  CA    . ILE B 132 ? 0.5624 0.4908 0.5777 -0.0198 -0.0512 0.0029  1349 ILE B CA    
4715 C  C     . ILE B 132 ? 0.4820 0.4095 0.5004 -0.0183 -0.0449 0.0101  1349 ILE B C     
4716 O  O     . ILE B 132 ? 0.5939 0.5264 0.6160 -0.0169 -0.0450 0.0143  1349 ILE B O     
4717 C  CB    . ILE B 132 ? 0.4108 0.3409 0.4109 -0.0172 -0.0533 0.0023  1349 ILE B CB    
4718 C  CG1   . ILE B 132 ? 0.4199 0.3527 0.4168 -0.0185 -0.0599 -0.0050 1349 ILE B CG1   
4719 C  CG2   . ILE B 132 ? 0.4535 0.3781 0.4423 -0.0155 -0.0481 0.0030  1349 ILE B CG2   
4720 C  CD1   . ILE B 132 ? 0.6163 0.5441 0.6151 -0.0204 -0.0596 -0.0118 1349 ILE B CD1   
4721 N  N     . ARG B 133 ? 0.3966 0.3181 0.4143 -0.0182 -0.0399 0.0111  1350 ARG B N     
4722 C  CA    . ARG B 133 ? 0.4086 0.3296 0.4287 -0.0166 -0.0341 0.0174  1350 ARG B CA    
4723 C  C     . ARG B 133 ? 0.5010 0.4162 0.5110 -0.0147 -0.0299 0.0174  1350 ARG B C     
4724 O  O     . ARG B 133 ? 0.5942 0.5047 0.6067 -0.0153 -0.0278 0.0166  1350 ARG B O     
4725 C  CB    . ARG B 133 ? 0.3889 0.3104 0.4232 -0.0191 -0.0321 0.0200  1350 ARG B CB    
4726 C  CG    . ARG B 133 ? 0.5323 0.4617 0.5780 -0.0207 -0.0350 0.0212  1350 ARG B CG    
4727 C  CD    . ARG B 133 ? 0.7554 0.6852 0.8158 -0.0243 -0.0331 0.0232  1350 ARG B CD    
4728 N  NE    . ARG B 133 ? 0.8454 0.7813 0.9134 -0.0236 -0.0289 0.0294  1350 ARG B NE    
4729 C  CZ    . ARG B 133 ? 1.0308 0.9670 1.1092 -0.0261 -0.0248 0.0335  1350 ARG B CZ    
4730 N  NH1   . ARG B 133 ? 1.1232 1.0523 1.2057 -0.0294 -0.0247 0.0324  1350 ARG B NH1   
4731 N  NH2   . ARG B 133 ? 0.9927 0.9362 1.0775 -0.0251 -0.0207 0.0388  1350 ARG B NH2   
4732 N  N     . LEU B 134 ? 0.5340 0.4497 0.5335 -0.0123 -0.0289 0.0186  1351 LEU B N     
4733 C  CA    . LEU B 134 ? 0.6171 0.5287 0.6074 -0.0108 -0.0255 0.0180  1351 LEU B CA    
4734 C  C     . LEU B 134 ? 0.6126 0.5244 0.6011 -0.0086 -0.0211 0.0229  1351 LEU B C     
4735 O  O     . LEU B 134 ? 0.7249 0.6397 0.7152 -0.0076 -0.0213 0.0261  1351 LEU B O     
4736 C  CB    . LEU B 134 ? 0.5377 0.4494 0.5166 -0.0105 -0.0275 0.0144  1351 LEU B CB    
4737 C  CG    . LEU B 134 ? 0.5836 0.4953 0.5629 -0.0122 -0.0317 0.0081  1351 LEU B CG    
4738 C  CD1   . LEU B 134 ? 0.5926 0.5059 0.5592 -0.0117 -0.0335 0.0052  1351 LEU B CD1   
4739 C  CD2   . LEU B 134 ? 0.3974 0.3047 0.3812 -0.0127 -0.0302 0.0048  1351 LEU B CD2   
4740 N  N     . ASN B 135 ? 0.3787 0.2876 0.3641 -0.0076 -0.0174 0.0231  1352 ASN B N     
4741 C  CA    . ASN B 135 ? 0.4540 0.3631 0.4365 -0.0055 -0.0135 0.0267  1352 ASN B CA    
4742 C  C     . ASN B 135 ? 0.5364 0.4434 0.5102 -0.0046 -0.0116 0.0247  1352 ASN B C     
4743 O  O     . ASN B 135 ? 0.4072 0.3125 0.3798 -0.0050 -0.0117 0.0215  1352 ASN B O     
4744 C  CB    . ASN B 135 ? 0.4846 0.3943 0.4746 -0.0048 -0.0104 0.0303  1352 ASN B CB    
4745 C  CG    . ASN B 135 ? 0.6500 0.5599 0.6354 -0.0023 -0.0065 0.0325  1352 ASN B CG    
4746 O  OD1   . ASN B 135 ? 0.7293 0.6410 0.7130 -0.0009 -0.0056 0.0342  1352 ASN B OD1   
4747 N  ND2   . ASN B 135 ? 0.6312 0.5389 0.6147 -0.0015 -0.0044 0.0321  1352 ASN B ND2   
4748 N  N     . GLN B 136 ? 0.5995 0.5069 0.5679 -0.0035 -0.0099 0.0264  1353 GLN B N     
4749 C  CA    . GLN B 136 ? 0.6910 0.5973 0.6524 -0.0031 -0.0077 0.0248  1353 GLN B CA    
4750 C  C     . GLN B 136 ? 0.6680 0.5748 0.6298 -0.0012 -0.0045 0.0270  1353 GLN B C     
4751 O  O     . GLN B 136 ? 0.7486 0.6559 0.7116 -0.0002 -0.0041 0.0295  1353 GLN B O     
4752 C  CB    . GLN B 136 ? 0.5988 0.5049 0.5526 -0.0042 -0.0088 0.0241  1353 GLN B CB    
4753 C  CG    . GLN B 136 ? 0.5992 0.5060 0.5494 -0.0058 -0.0115 0.0210  1353 GLN B CG    
4754 C  CD    . GLN B 136 ? 0.6547 0.5616 0.5958 -0.0070 -0.0112 0.0211  1353 GLN B CD    
4755 O  OE1   . GLN B 136 ? 0.6568 0.5642 0.5939 -0.0075 -0.0085 0.0197  1353 GLN B OE1   
4756 N  NE2   . GLN B 136 ? 0.3890 0.2957 0.3269 -0.0075 -0.0141 0.0230  1353 GLN B NE2   
4757 N  N     . TRP B 137 ? 0.5967 0.5035 0.5577 -0.0002 -0.0026 0.0258  1354 TRP B N     
4758 C  CA    . TRP B 137 ? 0.6222 0.5301 0.5810 0.0015  0.0000  0.0266  1354 TRP B CA    
4759 C  C     . TRP B 137 ? 0.6142 0.5223 0.5668 0.0003  0.0003  0.0239  1354 TRP B C     
4760 O  O     . TRP B 137 ? 0.6780 0.5871 0.6290 -0.0001 0.0004  0.0212  1354 TRP B O     
4761 C  CB    . TRP B 137 ? 0.5001 0.4089 0.4614 0.0035  0.0015  0.0272  1354 TRP B CB    
4762 C  CG    . TRP B 137 ? 0.4697 0.3782 0.4372 0.0041  0.0018  0.0306  1354 TRP B CG    
4763 C  CD1   . TRP B 137 ? 0.5935 0.5000 0.5660 0.0030  0.0005  0.0308  1354 TRP B CD1   
4764 C  CD2   . TRP B 137 ? 0.5934 0.5041 0.5632 0.0056  0.0038  0.0342  1354 TRP B CD2   
4765 N  NE1   . TRP B 137 ? 0.8053 0.7125 0.7839 0.0032  0.0017  0.0350  1354 TRP B NE1   
4766 C  CE2   . TRP B 137 ? 0.7351 0.6455 0.7119 0.0050  0.0040  0.0372  1354 TRP B CE2   
4767 C  CE3   . TRP B 137 ? 0.5844 0.4975 0.5515 0.0074  0.0056  0.0348  1354 TRP B CE3   
4768 C  CZ2   . TRP B 137 ? 0.7142 0.6276 0.6950 0.0060  0.0063  0.0414  1354 TRP B CZ2   
4769 C  CZ3   . TRP B 137 ? 0.7246 0.6405 0.6950 0.0091  0.0077  0.0382  1354 TRP B CZ3   
4770 C  CH2   . TRP B 137 ? 0.7863 0.7029 0.7635 0.0083  0.0083  0.0418  1354 TRP B CH2   
4771 N  N     . ASN B 138 ? 0.6448 0.5520 0.5946 -0.0003 0.0006  0.0247  1355 ASN B N     
4772 C  CA    . ASN B 138 ? 0.6769 0.5839 0.6216 -0.0023 0.0011  0.0229  1355 ASN B CA    
4773 C  C     . ASN B 138 ? 0.6825 0.5879 0.6259 -0.0021 0.0022  0.0235  1355 ASN B C     
4774 O  O     . ASN B 138 ? 0.7361 0.6414 0.6821 0.0002  0.0027  0.0247  1355 ASN B O     
4775 C  CB    . ASN B 138 ? 0.5553 0.4610 0.4963 -0.0048 -0.0005 0.0229  1355 ASN B CB    
4776 C  CG    . ASN B 138 ? 0.6150 0.5181 0.5566 -0.0046 -0.0026 0.0260  1355 ASN B CG    
4777 O  OD1   . ASN B 138 ? 0.7613 0.6631 0.7056 -0.0029 -0.0023 0.0278  1355 ASN B OD1   
4778 N  ND2   . ASN B 138 ? 0.5531 0.4560 0.4920 -0.0059 -0.0049 0.0262  1355 ASN B ND2   
4779 N  N     . ASN B 139 ? 0.6193 0.5239 0.5590 -0.0046 0.0028  0.0224  1356 ASN B N     
4780 C  CA    . ASN B 139 ? 0.6042 0.5061 0.5429 -0.0053 0.0035  0.0225  1356 ASN B CA    
4781 C  C     . ASN B 139 ? 0.6453 0.5423 0.5809 -0.0076 0.0024  0.0250  1356 ASN B C     
4782 O  O     . ASN B 139 ? 0.7896 0.6874 0.7219 -0.0099 0.0021  0.0256  1356 ASN B O     
4783 C  CB    . ASN B 139 ? 0.6033 0.5081 0.5413 -0.0070 0.0051  0.0192  1356 ASN B CB    
4784 C  CG    . ASN B 139 ? 0.6006 0.5078 0.5359 -0.0104 0.0059  0.0183  1356 ASN B CG    
4785 O  OD1   . ASN B 139 ? 0.5856 0.4941 0.5197 -0.0104 0.0053  0.0187  1356 ASN B OD1   
4786 N  ND2   . ASN B 139 ? 0.5815 0.4898 0.5162 -0.0134 0.0073  0.0166  1356 ASN B ND2   
4787 N  N     . VAL B 140 ? 0.6163 0.5084 0.5525 -0.0067 0.0019  0.0265  1357 VAL B N     
4788 C  CA    . VAL B 140 ? 0.6208 0.5072 0.5542 -0.0083 0.0005  0.0298  1357 VAL B CA    
4789 C  C     . VAL B 140 ? 0.6374 0.5181 0.5708 -0.0093 0.0012  0.0295  1357 VAL B C     
4790 O  O     . VAL B 140 ? 0.6990 0.5801 0.6353 -0.0076 0.0021  0.0265  1357 VAL B O     
4791 C  CB    . VAL B 140 ? 0.5703 0.4552 0.5056 -0.0053 -0.0021 0.0327  1357 VAL B CB    
4792 C  CG1   . VAL B 140 ? 0.3878 0.2783 0.3250 -0.0043 -0.0029 0.0322  1357 VAL B CG1   
4793 C  CG2   . VAL B 140 ? 0.6092 0.4921 0.5489 -0.0017 -0.0020 0.0323  1357 VAL B CG2   
4794 N  N     . VAL B 141 ? 0.5051 0.3803 0.4350 -0.0122 0.0008  0.0325  1358 VAL B N     
4795 C  CA    . VAL B 141 ? 0.5531 0.4215 0.4834 -0.0143 0.0014  0.0324  1358 VAL B CA    
4796 C  C     . VAL B 141 ? 0.4592 0.3189 0.3887 -0.0128 -0.0008 0.0368  1358 VAL B C     
4797 O  O     . VAL B 141 ? 0.5118 0.3697 0.4370 -0.0141 -0.0020 0.0415  1358 VAL B O     
4798 C  CB    . VAL B 141 ? 0.6826 0.5519 0.6104 -0.0201 0.0036  0.0322  1358 VAL B CB    
4799 C  CG1   . VAL B 141 ? 0.6396 0.5031 0.5700 -0.0224 0.0044  0.0303  1358 VAL B CG1   
4800 C  CG2   . VAL B 141 ? 0.5681 0.4473 0.4966 -0.0207 0.0053  0.0283  1358 VAL B CG2   
4801 N  N     . ARG B 142 ? 0.4542 0.3084 0.3874 -0.0101 -0.0014 0.0353  1359 ARG B N     
4802 C  CA    . ARG B 142 ? 0.5396 0.3843 0.4733 -0.0080 -0.0036 0.0389  1359 ARG B CA    
4803 C  C     . ARG B 142 ? 0.5863 0.4227 0.5218 -0.0102 -0.0028 0.0367  1359 ARG B C     
4804 O  O     . ARG B 142 ? 0.5748 0.4134 0.5137 -0.0092 -0.0017 0.0309  1359 ARG B O     
4805 C  CB    . ARG B 142 ? 0.5173 0.3640 0.4554 -0.0016 -0.0053 0.0381  1359 ARG B CB    
4806 C  CG    . ARG B 142 ? 0.4747 0.3292 0.4124 0.0001  -0.0065 0.0402  1359 ARG B CG    
4807 C  CD    . ARG B 142 ? 0.4686 0.3258 0.4122 0.0060  -0.0078 0.0395  1359 ARG B CD    
4808 N  NE    . ARG B 142 ? 0.4656 0.3303 0.4101 0.0068  -0.0092 0.0412  1359 ARG B NE    
4809 C  CZ    . ARG B 142 ? 0.5938 0.4641 0.5442 0.0108  -0.0098 0.0406  1359 ARG B CZ    
4810 N  NH1   . ARG B 142 ? 0.8127 0.6827 0.7681 0.0149  -0.0088 0.0385  1359 ARG B NH1   
4811 N  NH2   . ARG B 142 ? 0.7091 0.5856 0.6608 0.0105  -0.0113 0.0420  1359 ARG B NH2   
4812 N  N     . TRP B 143 ? 0.7032 0.5302 0.6363 -0.0135 -0.0033 0.0413  1360 TRP B N     
4813 C  CA    . TRP B 143 ? 0.8098 0.6278 0.7456 -0.0164 -0.0026 0.0392  1360 TRP B CA    
4814 C  C     . TRP B 143 ? 0.7955 0.6052 0.7356 -0.0106 -0.0049 0.0377  1360 TRP B C     
4815 O  O     . TRP B 143 ? 0.6719 0.4701 0.6120 -0.0099 -0.0067 0.0420  1360 TRP B O     
4816 C  CB    . TRP B 143 ? 0.8204 0.6307 0.7526 -0.0227 -0.0019 0.0451  1360 TRP B CB    
4817 C  CG    . TRP B 143 ? 0.8476 0.6542 0.7836 -0.0277 -0.0001 0.0411  1360 TRP B CG    
4818 C  CD1   . TRP B 143 ? 0.7950 0.5882 0.7339 -0.0298 -0.0008 0.0418  1360 TRP B CD1   
4819 C  CD2   . TRP B 143 ? 0.9629 0.7791 0.9010 -0.0311 0.0022  0.0348  1360 TRP B CD2   
4820 N  NE1   . TRP B 143 ? 0.7988 0.5930 0.7419 -0.0350 0.0010  0.0362  1360 TRP B NE1   
4821 C  CE2   . TRP B 143 ? 0.8956 0.7046 0.8383 -0.0357 0.0028  0.0319  1360 TRP B CE2   
4822 C  CE3   . TRP B 143 ? 0.9688 0.7990 0.9060 -0.0305 0.0036  0.0315  1360 TRP B CE3   
4823 C  CZ2   . TRP B 143 ? 0.9039 0.7204 0.8502 -0.0397 0.0045  0.0255  1360 TRP B CZ2   
4824 C  CZ3   . TRP B 143 ? 0.9015 0.7387 0.8420 -0.0340 0.0054  0.0257  1360 TRP B CZ3   
4825 C  CH2   . TRP B 143 ? 0.9109 0.7419 0.8559 -0.0386 0.0057  0.0226  1360 TRP B CH2   
4826 N  N     . GLU B 144 ? 0.8969 0.7128 0.8405 -0.0060 -0.0046 0.0314  1361 GLU B N     
4827 C  CA    . GLU B 144 ? 0.8980 0.7093 0.8458 0.0007  -0.0063 0.0293  1361 GLU B CA    
4828 C  C     . GLU B 144 ? 0.8527 0.6501 0.8030 -0.0004 -0.0072 0.0279  1361 GLU B C     
4829 O  O     . GLU B 144 ? 0.7577 0.5528 0.7087 -0.0054 -0.0060 0.0241  1361 GLU B O     
4830 C  CB    . GLU B 144 ? 0.8220 0.6433 0.7724 0.0048  -0.0049 0.0223  1361 GLU B CB    
4831 C  CG    . GLU B 144 ? 0.7962 0.6299 0.7457 0.0068  -0.0041 0.0238  1361 GLU B CG    
4832 C  CD    . GLU B 144 ? 1.0024 0.8372 0.9549 0.0129  -0.0057 0.0263  1361 GLU B CD    
4833 O  OE1   . GLU B 144 ? 1.1029 0.9474 1.0559 0.0145  -0.0054 0.0278  1361 GLU B OE1   
4834 O  OE2   . GLU B 144 ? 1.0910 0.9171 1.0462 0.0162  -0.0075 0.0266  1361 GLU B OE2   
4835 N  N     . PHE B 145 ? 1.0134 0.8012 0.9656 0.0041  -0.0097 0.0310  1362 PHE B N     
4836 C  CA    . PHE B 145 ? 1.0185 0.7915 0.9743 0.0043  -0.0110 0.0290  1362 PHE B CA    
4837 C  C     . PHE B 145 ? 0.8994 0.6734 0.8603 0.0104  -0.0110 0.0199  1362 PHE B C     
4838 O  O     . PHE B 145 ? 0.8807 0.6461 0.8445 0.0091  -0.0112 0.0143  1362 PHE B O     
4839 C  CB    . PHE B 145 ? 0.9318 0.6923 0.8874 0.0066  -0.0140 0.0369  1362 PHE B CB    
4840 C  CG    . PHE B 145 ? 0.9749 0.7413 0.9311 0.0140  -0.0161 0.0401  1362 PHE B CG    
4841 C  CD1   . PHE B 145 ? 0.9214 0.6835 0.8833 0.0220  -0.0181 0.0374  1362 PHE B CD1   
4842 C  CD2   . PHE B 145 ? 1.0121 0.7884 0.9637 0.0128  -0.0162 0.0456  1362 PHE B CD2   
4843 C  CE1   . PHE B 145 ? 0.9612 0.7299 0.9249 0.0286  -0.0200 0.0403  1362 PHE B CE1   
4844 C  CE2   . PHE B 145 ? 1.0097 0.7920 0.9630 0.0190  -0.0185 0.0482  1362 PHE B CE2   
4845 C  CZ    . PHE B 145 ? 0.9689 0.7477 0.9286 0.0268  -0.0204 0.0458  1362 PHE B CZ    
4846 N  N     . LYS B 146 ? 0.7178 0.5030 0.6797 0.0166  -0.0106 0.0180  1363 LYS B N     
4847 C  CA    . LYS B 146 ? 0.6302 0.4186 0.5959 0.0226  -0.0099 0.0095  1363 LYS B CA    
4848 C  C     . LYS B 146 ? 0.6971 0.4915 0.6612 0.0187  -0.0078 0.0023  1363 LYS B C     
4849 O  O     . LYS B 146 ? 0.6234 0.4248 0.5840 0.0130  -0.0065 0.0042  1363 LYS B O     
4850 C  CB    . LYS B 146 ? 0.5867 0.3875 0.5540 0.0292  -0.0092 0.0100  1363 LYS B CB    
4851 C  CG    . LYS B 146 ? 0.5360 0.3376 0.5030 0.0301  -0.0111 0.0189  1363 LYS B CG    
4852 C  CD    . LYS B 146 ? 0.6507 0.4623 0.6222 0.0376  -0.0111 0.0185  1363 LYS B CD    
4853 C  CE    . LYS B 146 ? 0.7419 0.5617 0.7122 0.0365  -0.0121 0.0256  1363 LYS B CE    
4854 N  NZ    . LYS B 146 ? 0.7900 0.6230 0.7654 0.0418  -0.0111 0.0248  1363 LYS B NZ    
4855 N  N     . HIS B 147 ? 0.6817 0.4738 0.6486 0.0221  -0.0079 -0.0065 1364 HIS B N     
4856 C  CA    . HIS B 147 ? 0.6010 0.3993 0.5663 0.0192  -0.0066 -0.0141 1364 HIS B CA    
4857 C  C     . HIS B 147 ? 0.5758 0.3906 0.5372 0.0186  -0.0043 -0.0126 1364 HIS B C     
4858 O  O     . HIS B 147 ? 0.5837 0.4074 0.5450 0.0241  -0.0031 -0.0114 1364 HIS B O     
4859 C  CB    . HIS B 147 ? 0.6322 0.4297 0.5999 0.0251  -0.0068 -0.0242 1364 HIS B CB    
4860 C  CG    . HIS B 147 ? 0.9377 0.7179 0.9096 0.0248  -0.0092 -0.0278 1364 HIS B CG    
4861 N  ND1   . HIS B 147 ? 1.0260 0.7922 0.9998 0.0206  -0.0110 -0.0207 1364 HIS B ND1   
4862 C  CD2   . HIS B 147 ? 0.9798 0.7541 0.9546 0.0281  -0.0103 -0.0378 1364 HIS B CD2   
4863 C  CE1   . HIS B 147 ? 0.9608 0.7120 0.9389 0.0212  -0.0130 -0.0256 1364 HIS B CE1   
4864 N  NE2   . HIS B 147 ? 0.9880 0.7438 0.9671 0.0258  -0.0128 -0.0365 1364 HIS B NE2   
4865 N  N     . PRO B 148 ? 0.6640 0.4831 0.6230 0.0121  -0.0036 -0.0123 1365 PRO B N     
4866 C  CA    . PRO B 148 ? 0.7288 0.5626 0.6844 0.0118  -0.0018 -0.0113 1365 PRO B CA    
4867 C  C     . PRO B 148 ? 0.8085 0.6515 0.7627 0.0153  -0.0009 -0.0192 1365 PRO B C     
4868 O  O     . PRO B 148 ? 0.8666 0.7064 0.8217 0.0143  -0.0019 -0.0266 1365 PRO B O     
4869 C  CB    . PRO B 148 ? 0.6076 0.4413 0.5618 0.0038  -0.0016 -0.0085 1365 PRO B CB    
4870 C  CG    . PRO B 148 ? 0.5034 0.3225 0.4598 -0.0002 -0.0030 -0.0052 1365 PRO B CG    
4871 C  CD    . PRO B 148 ? 0.5954 0.4054 0.5550 0.0043  -0.0045 -0.0102 1365 PRO B CD    
4872 N  N     . GLN B 149 ? 0.7882 0.6431 0.7402 0.0190  0.0010  -0.0175 1366 GLN B N     
4873 C  CA    . GLN B 149 ? 0.8230 0.6884 0.7723 0.0228  0.0022  -0.0233 1366 GLN B CA    
4874 C  C     . GLN B 149 ? 0.7530 0.6294 0.6991 0.0210  0.0035  -0.0196 1366 GLN B C     
4875 O  O     . GLN B 149 ? 0.7232 0.6014 0.6697 0.0201  0.0042  -0.0126 1366 GLN B O     
4876 C  CB    . GLN B 149 ? 1.0125 0.8817 0.9624 0.0306  0.0038  -0.0245 1366 GLN B CB    
4877 C  CG    . GLN B 149 ? 1.0795 0.9384 1.0330 0.0342  0.0025  -0.0293 1366 GLN B CG    
4878 C  CD    . GLN B 149 ? 1.1355 0.9966 1.0872 0.0378  0.0025  -0.0396 1366 GLN B CD    
4879 O  OE1   . GLN B 149 ? 1.2420 1.1136 1.1910 0.0433  0.0047  -0.0423 1366 GLN B OE1   
4880 N  NE2   . GLN B 149 ? 1.0481 0.8994 1.0012 0.0345  -0.0001 -0.0456 1366 GLN B NE2   
4881 N  N     . PRO B 150 ? 0.8351 0.7192 0.7781 0.0211  0.0035  -0.0244 1367 PRO B N     
4882 C  CA    . PRO B 150 ? 0.8362 0.7285 0.7770 0.0183  0.0038  -0.0214 1367 PRO B CA    
4883 C  C     . PRO B 150 ? 0.8926 0.7909 0.8326 0.0202  0.0058  -0.0142 1367 PRO B C     
4884 O  O     . PRO B 150 ? 1.2999 1.2002 1.2398 0.0167  0.0057  -0.0103 1367 PRO B O     
4885 C  CB    . PRO B 150 ? 0.8171 0.7173 0.7545 0.0202  0.0032  -0.0283 1367 PRO B CB    
4886 C  CG    . PRO B 150 ? 0.9485 0.8404 0.8881 0.0192  0.0012  -0.0359 1367 PRO B CG    
4887 C  CD    . PRO B 150 ? 0.9153 0.7966 0.8584 0.0206  0.0017  -0.0333 1367 PRO B CD    
4888 N  N     . PHE B 151 ? 0.5077 0.4094 0.4475 0.0253  0.0076  -0.0125 1368 PHE B N     
4889 C  CA    . PHE B 151 ? 0.4049 0.3104 0.3458 0.0253  0.0090  -0.0051 1368 PHE B CA    
4890 C  C     . PHE B 151 ? 0.8205 0.7212 0.7656 0.0265  0.0093  -0.0012 1368 PHE B C     
4891 O  O     . PHE B 151 ? 0.3995 0.3004 0.3464 0.0247  0.0093  0.0045  1368 PHE B O     
4892 C  CB    . PHE B 151 ? 0.4753 0.3912 0.4133 0.0292  0.0113  -0.0037 1368 PHE B CB    
4893 C  CG    . PHE B 151 ? 0.6309 0.5525 0.5651 0.0280  0.0107  -0.0050 1368 PHE B CG    
4894 C  CD1   . PHE B 151 ? 0.6989 0.6230 0.6333 0.0259  0.0108  0.0002  1368 PHE B CD1   
4895 C  CD2   . PHE B 151 ? 0.6723 0.5967 0.6029 0.0293  0.0096  -0.0117 1368 PHE B CD2   
4896 C  CE1   . PHE B 151 ? 0.7289 0.6584 0.6603 0.0255  0.0099  -0.0010 1368 PHE B CE1   
4897 C  CE2   . PHE B 151 ? 0.6998 0.6303 0.6271 0.0286  0.0085  -0.0129 1368 PHE B CE2   
4898 C  CZ    . PHE B 151 ? 0.7512 0.6844 0.6791 0.0269  0.0086  -0.0073 1368 PHE B CZ    
4899 N  N     . LEU B 152 ? 0.8880 0.7845 0.8347 0.0298  0.0092  -0.0048 1369 LEU B N     
4900 C  CA    . LEU B 152 ? 0.8365 0.7296 0.7879 0.0323  0.0091  -0.0018 1369 LEU B CA    
4901 C  C     . LEU B 152 ? 0.7567 0.6404 0.7101 0.0281  0.0066  0.0022  1369 LEU B C     
4902 O  O     . LEU B 152 ? 0.9389 0.8229 0.8952 0.0283  0.0062  0.0074  1369 LEU B O     
4903 C  CB    . LEU B 152 ? 0.7825 0.6733 0.7352 0.0375  0.0095  -0.0077 1369 LEU B CB    
4904 C  CG    . LEU B 152 ? 0.7205 0.6210 0.6696 0.0418  0.0120  -0.0127 1369 LEU B CG    
4905 C  CD1   . LEU B 152 ? 0.5380 0.4380 0.4889 0.0480  0.0129  -0.0184 1369 LEU B CD1   
4906 C  CD2   . LEU B 152 ? 0.8738 0.7856 0.8221 0.0429  0.0150  -0.0073 1369 LEU B CD2   
4907 N  N     . ARG B 153 ? 0.5604 0.4361 0.5122 0.0242  0.0048  -0.0002 1370 ARG B N     
4908 C  CA    . ARG B 153 ? 0.6206 0.4872 0.5733 0.0202  0.0028  0.0040  1370 ARG B CA    
4909 C  C     . ARG B 153 ? 0.5891 0.4529 0.5393 0.0140  0.0022  0.0026  1370 ARG B C     
4910 O  O     . ARG B 153 ? 0.7418 0.5988 0.6925 0.0124  0.0014  -0.0017 1370 ARG B O     
4911 C  CB    . ARG B 153 ? 0.6877 0.5441 0.6436 0.0229  0.0011  0.0034  1370 ARG B CB    
4912 C  CG    . ARG B 153 ? 0.7859 0.6328 0.7420 0.0195  -0.0011 0.0094  1370 ARG B CG    
4913 C  CD    . ARG B 153 ? 0.6559 0.4914 0.6154 0.0229  -0.0032 0.0096  1370 ARG B CD    
4914 N  NE    . ARG B 153 ? 0.6770 0.5174 0.6405 0.0303  -0.0027 0.0078  1370 ARG B NE    
4915 C  CZ    . ARG B 153 ? 0.6333 0.4791 0.5994 0.0331  -0.0031 0.0125  1370 ARG B CZ    
4916 N  NH1   . ARG B 153 ? 0.6517 0.5032 0.6225 0.0396  -0.0022 0.0106  1370 ARG B NH1   
4917 N  NH2   . ARG B 153 ? 0.5373 0.3834 0.5017 0.0295  -0.0045 0.0189  1370 ARG B NH2   
4918 N  N     . THR B 154 ? 0.4149 0.2838 0.3631 0.0105  0.0027  0.0059  1371 THR B N     
4919 C  CA    . THR B 154 ? 0.4148 0.2832 0.3613 0.0047  0.0026  0.0051  1371 THR B CA    
4920 C  C     . THR B 154 ? 0.5062 0.3700 0.4518 0.0006  0.0020  0.0110  1371 THR B C     
4921 O  O     . THR B 154 ? 0.5206 0.3850 0.4661 0.0024  0.0016  0.0156  1371 THR B O     
4922 C  CB    . THR B 154 ? 0.4565 0.3357 0.4013 0.0047  0.0038  0.0036  1371 THR B CB    
4923 O  OG1   . THR B 154 ? 0.5542 0.4388 0.4988 0.0070  0.0046  0.0080  1371 THR B OG1   
4924 C  CG2   . THR B 154 ? 0.4084 0.2921 0.3528 0.0083  0.0042  -0.0024 1371 THR B CG2   
4925 N  N     . ARG B 155 ? 0.5730 0.4327 0.5179 -0.0049 0.0020  0.0108  1372 ARG B N     
4926 C  CA    . ARG B 155 ? 0.4935 0.3483 0.4366 -0.0088 0.0017  0.0167  1372 ARG B CA    
4927 C  C     . ARG B 155 ? 0.5043 0.3674 0.4448 -0.0102 0.0025  0.0193  1372 ARG B C     
4928 O  O     . ARG B 155 ? 0.4461 0.3078 0.3843 -0.0105 0.0018  0.0242  1372 ARG B O     
4929 C  CB    . ARG B 155 ? 0.6513 0.4994 0.5948 -0.0149 0.0020  0.0161  1372 ARG B CB    
4930 C  CG    . ARG B 155 ? 0.7044 0.5398 0.6501 -0.0140 0.0005  0.0160  1372 ARG B CG    
4931 C  CD    . ARG B 155 ? 0.7823 0.6106 0.7297 -0.0205 0.0009  0.0151  1372 ARG B CD    
4932 N  NE    . ARG B 155 ? 0.8506 0.6689 0.8018 -0.0188 -0.0006 0.0107  1372 ARG B NE    
4933 C  CZ    . ARG B 155 ? 0.8525 0.6574 0.8047 -0.0183 -0.0020 0.0143  1372 ARG B CZ    
4934 N  NH1   . ARG B 155 ? 0.9420 0.7426 0.8910 -0.0195 -0.0023 0.0227  1372 ARG B NH1   
4935 N  NH2   . ARG B 155 ? 0.9206 0.7165 0.8768 -0.0162 -0.0035 0.0092  1372 ARG B NH2   
4936 N  N     . GLU B 156 ? 0.5354 0.4072 0.4762 -0.0104 0.0037  0.0157  1373 GLU B N     
4937 C  CA    . GLU B 156 ? 0.6039 0.4835 0.5434 -0.0097 0.0043  0.0172  1373 GLU B CA    
4938 C  C     . GLU B 156 ? 0.5944 0.4790 0.5355 -0.0044 0.0043  0.0156  1373 GLU B C     
4939 O  O     . GLU B 156 ? 0.6017 0.4882 0.5439 -0.0024 0.0046  0.0115  1373 GLU B O     
4940 C  CB    . GLU B 156 ? 0.7391 0.6251 0.6782 -0.0134 0.0056  0.0149  1373 GLU B CB    
4941 C  CG    . GLU B 156 ? 0.8513 0.7446 0.7895 -0.0121 0.0060  0.0158  1373 GLU B CG    
4942 C  CD    . GLU B 156 ? 0.8213 0.7227 0.7606 -0.0131 0.0070  0.0121  1373 GLU B CD    
4943 O  OE1   . GLU B 156 ? 0.8175 0.7206 0.7586 -0.0137 0.0071  0.0082  1373 GLU B OE1   
4944 O  OE2   . GLU B 156 ? 0.8083 0.7144 0.7469 -0.0132 0.0075  0.0126  1373 GLU B OE2   
4945 N  N     . PHE B 157 ? 0.5828 0.4699 0.5241 -0.0022 0.0040  0.0188  1374 PHE B N     
4946 C  CA    . PHE B 157 ? 0.5536 0.4462 0.4966 0.0021  0.0046  0.0182  1374 PHE B CA    
4947 C  C     . PHE B 157 ? 0.5537 0.4506 0.4970 0.0019  0.0045  0.0206  1374 PHE B C     
4948 O  O     . PHE B 157 ? 0.6657 0.5608 0.6080 -0.0004 0.0036  0.0229  1374 PHE B O     
4949 C  CB    . PHE B 157 ? 0.6641 0.5548 0.6096 0.0062  0.0043  0.0191  1374 PHE B CB    
4950 C  CG    . PHE B 157 ? 0.7271 0.6130 0.6738 0.0062  0.0027  0.0229  1374 PHE B CG    
4951 C  CD1   . PHE B 157 ? 0.6901 0.5795 0.6392 0.0077  0.0021  0.0260  1374 PHE B CD1   
4952 C  CD2   . PHE B 157 ? 0.7269 0.6047 0.6727 0.0049  0.0014  0.0236  1374 PHE B CD2   
4953 C  CE1   . PHE B 157 ? 0.7456 0.6315 0.6960 0.0082  -0.0001 0.0292  1374 PHE B CE1   
4954 C  CE2   . PHE B 157 ? 0.5413 0.4148 0.4877 0.0057  -0.0007 0.0276  1374 PHE B CE2   
4955 C  CZ    . PHE B 157 ? 0.4723 0.3504 0.4210 0.0075  -0.0016 0.0302  1374 PHE B CZ    
4956 N  N     . LEU B 158 ? 0.4856 0.3881 0.4301 0.0044  0.0055  0.0201  1375 LEU B N     
4957 C  CA    . LEU B 158 ? 0.5274 0.4329 0.4732 0.0046  0.0054  0.0222  1375 LEU B CA    
4958 C  C     . LEU B 158 ? 0.5672 0.4732 0.5167 0.0070  0.0053  0.0252  1375 LEU B C     
4959 O  O     . LEU B 158 ? 0.6568 0.5643 0.6077 0.0099  0.0064  0.0253  1375 LEU B O     
4960 C  CB    . LEU B 158 ? 0.5169 0.4275 0.4624 0.0059  0.0064  0.0207  1375 LEU B CB    
4961 C  CG    . LEU B 158 ? 0.4334 0.3463 0.3768 0.0050  0.0066  0.0169  1375 LEU B CG    
4962 C  CD1   . LEU B 158 ? 0.3684 0.2869 0.3119 0.0075  0.0070  0.0164  1375 LEU B CD1   
4963 C  CD2   . LEU B 158 ? 0.3824 0.2940 0.3247 0.0009  0.0062  0.0158  1375 LEU B CD2   
4964 N  N     . TRP B 159 ? 0.4307 0.3365 0.3820 0.0057  0.0041  0.0273  1376 TRP B N     
4965 C  CA    . TRP B 159 ? 0.4746 0.3820 0.4310 0.0073  0.0038  0.0301  1376 TRP B CA    
4966 C  C     . TRP B 159 ? 0.5831 0.4916 0.5421 0.0058  0.0027  0.0312  1376 TRP B C     
4967 O  O     . TRP B 159 ? 0.6844 0.5926 0.6412 0.0042  0.0023  0.0296  1376 TRP B O     
4968 C  CB    . TRP B 159 ? 0.4310 0.3355 0.3884 0.0077  0.0022  0.0312  1376 TRP B CB    
4969 C  CG    . TRP B 159 ? 0.4499 0.3514 0.4051 0.0051  -0.0004 0.0318  1376 TRP B CG    
4970 C  CD1   . TRP B 159 ? 0.4578 0.3588 0.4093 0.0023  -0.0010 0.0307  1376 TRP B CD1   
4971 C  CD2   . TRP B 159 ? 0.3772 0.2762 0.3332 0.0054  -0.0029 0.0337  1376 TRP B CD2   
4972 N  NE1   . TRP B 159 ? 0.5851 0.4838 0.5342 0.0006  -0.0035 0.0319  1376 TRP B NE1   
4973 C  CE2   . TRP B 159 ? 0.3797 0.2769 0.3313 0.0025  -0.0049 0.0340  1376 TRP B CE2   
4974 C  CE3   . TRP B 159 ? 0.3792 0.2779 0.3391 0.0083  -0.0037 0.0352  1376 TRP B CE3   
4975 C  CZ2   . TRP B 159 ? 0.4349 0.3297 0.3851 0.0024  -0.0079 0.0363  1376 TRP B CZ2   
4976 C  CZ3   . TRP B 159 ? 0.5163 0.4123 0.4758 0.0084  -0.0069 0.0373  1376 TRP B CZ3   
4977 C  CH2   . TRP B 159 ? 0.4698 0.3637 0.4240 0.0054  -0.0091 0.0381  1376 TRP B CH2   
4978 N  N     . GLN B 160 ? 0.5048 0.4151 0.4695 0.0065  0.0022  0.0336  1377 GLN B N     
4979 C  CA    . GLN B 160 ? 0.6364 0.5468 0.6046 0.0044  -0.0001 0.0341  1377 GLN B CA    
4980 C  C     . GLN B 160 ? 0.6760 0.5862 0.6463 0.0043  -0.0026 0.0351  1377 GLN B C     
4981 O  O     . GLN B 160 ? 0.7522 0.6639 0.7255 0.0066  -0.0020 0.0366  1377 GLN B O     
4982 C  CB    . GLN B 160 ? 0.7409 0.6538 0.7154 0.0046  0.0012  0.0361  1377 GLN B CB    
4983 C  CG    . GLN B 160 ? 0.7278 0.6447 0.7074 0.0068  0.0036  0.0389  1377 GLN B CG    
4984 C  CD    . GLN B 160 ? 0.7003 0.6197 0.6866 0.0063  0.0018  0.0402  1377 GLN B CD    
4985 O  OE1   . GLN B 160 ? 0.8327 0.7531 0.8249 0.0042  0.0003  0.0410  1377 GLN B OE1   
4986 N  NE2   . GLN B 160 ? 0.7151 0.6352 0.7009 0.0084  0.0015  0.0401  1377 GLN B NE2   
4987 N  N     . GLU B 161 ? 0.6020 0.5107 0.5702 0.0022  -0.0057 0.0341  1378 GLU B N     
4988 C  CA    . GLU B 161 ? 0.6538 0.5632 0.6242 0.0020  -0.0091 0.0351  1378 GLU B CA    
4989 C  C     . GLU B 161 ? 0.7400 0.6515 0.7147 -0.0001 -0.0117 0.0340  1378 GLU B C     
4990 O  O     . GLU B 161 ? 0.7916 0.7016 0.7625 -0.0019 -0.0124 0.0315  1378 GLU B O     
4991 C  CB    . GLU B 161 ? 0.5150 0.4209 0.4778 0.0015  -0.0111 0.0351  1378 GLU B CB    
4992 C  CG    . GLU B 161 ? 0.5286 0.4326 0.4840 -0.0011 -0.0112 0.0330  1378 GLU B CG    
4993 C  CD    . GLU B 161 ? 0.5250 0.4264 0.4732 -0.0020 -0.0133 0.0342  1378 GLU B CD    
4994 O  OE1   . GLU B 161 ? 0.4740 0.3757 0.4237 -0.0009 -0.0166 0.0363  1378 GLU B OE1   
4995 O  OE2   . GLU B 161 ? 0.4776 0.3772 0.4190 -0.0038 -0.0119 0.0332  1378 GLU B OE2   
4996 N  N     . GLY B 162 ? 0.6654 0.5808 0.6487 0.0002  -0.0130 0.0354  1379 GLY B N     
4997 C  CA    . GLY B 162 ? 0.5656 0.4831 0.5549 -0.0021 -0.0160 0.0341  1379 GLY B CA    
4998 C  C     . GLY B 162 ? 0.6397 0.5599 0.6304 -0.0020 -0.0208 0.0341  1379 GLY B C     
4999 O  O     . GLY B 162 ? 0.5703 0.4925 0.5630 0.0004  -0.0210 0.0365  1379 GLY B O     
5000 N  N     . HIS B 163 ? 0.6452 0.5656 0.6345 -0.0042 -0.0247 0.0312  1380 HIS B N     
5001 C  CA    . HIS B 163 ? 0.4592 0.3828 0.4486 -0.0041 -0.0301 0.0308  1380 HIS B CA    
5002 C  C     . HIS B 163 ? 0.5517 0.4786 0.5489 -0.0069 -0.0336 0.0274  1380 HIS B C     
5003 O  O     . HIS B 163 ? 0.5540 0.4782 0.5506 -0.0090 -0.0330 0.0242  1380 HIS B O     
5004 C  CB    . HIS B 163 ? 0.4858 0.4064 0.4623 -0.0038 -0.0321 0.0301  1380 HIS B CB    
5005 C  CG    . HIS B 163 ? 0.6334 0.5495 0.6026 -0.0020 -0.0285 0.0329  1380 HIS B CG    
5006 N  ND1   . HIS B 163 ? 0.5734 0.4882 0.5388 0.0002  -0.0301 0.0362  1380 HIS B ND1   
5007 C  CD2   . HIS B 163 ? 0.5762 0.4887 0.5419 -0.0022 -0.0238 0.0328  1380 HIS B CD2   
5008 C  CE1   . HIS B 163 ? 0.4791 0.3891 0.4393 0.0009  -0.0263 0.0377  1380 HIS B CE1   
5009 N  NE2   . HIS B 163 ? 0.5358 0.4450 0.4961 -0.0006 -0.0225 0.0355  1380 HIS B NE2   
5010 N  N     . THR B 164 ? 0.5619 0.4947 0.5674 -0.0067 -0.0374 0.0280  1381 THR B N     
5011 C  CA    . THR B 164 ? 0.3888 0.3255 0.4049 -0.0098 -0.0405 0.0251  1381 THR B CA    
5012 C  C     . THR B 164 ? 0.6456 0.5884 0.6635 -0.0094 -0.0474 0.0237  1381 THR B C     
5013 O  O     . THR B 164 ? 0.7476 0.6933 0.7643 -0.0062 -0.0489 0.0269  1381 THR B O     
5014 C  CB    . THR B 164 ? 0.5369 0.4770 0.5668 -0.0107 -0.0370 0.0279  1381 THR B CB    
5015 O  OG1   . THR B 164 ? 0.5327 0.4784 0.5672 -0.0077 -0.0365 0.0316  1381 THR B OG1   
5016 C  CG2   . THR B 164 ? 0.4174 0.3518 0.4449 -0.0108 -0.0306 0.0296  1381 THR B CG2   
5017 N  N     . ALA B 165 ? 0.6131 0.5577 0.6344 -0.0125 -0.0519 0.0187  1382 ALA B N     
5018 C  CA    . ALA B 165 ? 0.5920 0.5430 0.6148 -0.0126 -0.0595 0.0160  1382 ALA B CA    
5019 C  C     . ALA B 165 ? 0.5812 0.5366 0.6193 -0.0167 -0.0621 0.0123  1382 ALA B C     
5020 O  O     . ALA B 165 ? 0.6394 0.5901 0.6806 -0.0199 -0.0601 0.0094  1382 ALA B O     
5021 C  CB    . ALA B 165 ? 0.7515 0.6999 0.7595 -0.0123 -0.0631 0.0121  1382 ALA B CB    
5022 N  N     . PHE B 166 ? 0.6487 0.6134 0.6971 -0.0166 -0.0669 0.0126  1383 PHE B N     
5023 C  CA    . PHE B 166 ? 0.6715 0.6426 0.7381 -0.0205 -0.0687 0.0108  1383 PHE B CA    
5024 C  C     . PHE B 166 ? 0.6938 0.6739 0.7645 -0.0209 -0.0778 0.0066  1383 PHE B C     
5025 O  O     . PHE B 166 ? 0.6320 0.6156 0.6945 -0.0168 -0.0818 0.0080  1383 PHE B O     
5026 C  CB    . PHE B 166 ? 0.6267 0.6029 0.7057 -0.0197 -0.0637 0.0167  1383 PHE B CB    
5027 C  CG    . PHE B 166 ? 0.6867 0.6558 0.7644 -0.0200 -0.0552 0.0204  1383 PHE B CG    
5028 C  CD1   . PHE B 166 ? 0.8669 0.8346 0.9389 -0.0157 -0.0499 0.0256  1383 PHE B CD1   
5029 C  CD2   . PHE B 166 ? 0.3938 0.3574 0.4760 -0.0243 -0.0527 0.0186  1383 PHE B CD2   
5030 C  CE1   . PHE B 166 ? 0.7413 0.7034 0.8116 -0.0158 -0.0426 0.0287  1383 PHE B CE1   
5031 C  CE2   . PHE B 166 ? 0.5486 0.5062 0.6292 -0.0242 -0.0454 0.0225  1383 PHE B CE2   
5032 C  CZ    . PHE B 166 ? 0.6066 0.5640 0.6809 -0.0199 -0.0404 0.0274  1383 PHE B CZ    
5033 N  N     . ALA B 167 ? 0.7678 0.7515 0.8516 -0.0260 -0.0814 0.0015  1384 ALA B N     
5034 C  CA    . ALA B 167 ? 0.8535 0.8474 0.9438 -0.0269 -0.0906 -0.0032 1384 ALA B CA    
5035 C  C     . ALA B 167 ? 0.9241 0.9296 1.0261 -0.0244 -0.0919 0.0013  1384 ALA B C     
5036 O  O     . ALA B 167 ? 1.0006 1.0118 1.0965 -0.0199 -0.0972 0.0022  1384 ALA B O     
5037 C  CB    . ALA B 167 ? 0.9618 0.9562 1.0654 -0.0335 -0.0937 -0.0101 1384 ALA B CB    
5038 N  N     . THR B 168 ? 0.8524 0.8619 0.9712 -0.0269 -0.0869 0.0047  1385 THR B N     
5039 C  CA    . THR B 168 ? 0.9106 0.9324 1.0421 -0.0243 -0.0875 0.0086  1385 THR B CA    
5040 C  C     . THR B 168 ? 0.9736 0.9930 1.1032 -0.0203 -0.0787 0.0159  1385 THR B C     
5041 O  O     . THR B 168 ? 1.0153 1.0258 1.1411 -0.0217 -0.0713 0.0183  1385 THR B O     
5042 C  CB    . THR B 168 ? 0.8537 0.8861 1.0086 -0.0301 -0.0888 0.0065  1385 THR B CB    
5043 O  OG1   . THR B 168 ? 0.9613 1.0058 1.1286 -0.0270 -0.0871 0.0112  1385 THR B OG1   
5044 C  CG2   . THR B 168 ? 0.7342 0.7589 0.8952 -0.0355 -0.0814 0.0078  1385 THR B CG2   
5045 N  N     . GLN B 169 ? 0.8569 0.8857 0.9915 -0.0152 -0.0801 0.0191  1386 GLN B N     
5046 C  CA    . GLN B 169 ? 0.6800 0.7072 0.8119 -0.0101 -0.0729 0.0251  1386 GLN B CA    
5047 C  C     . GLN B 169 ? 0.6606 0.6897 0.8048 -0.0134 -0.0642 0.0281  1386 GLN B C     
5048 O  O     . GLN B 169 ? 0.5470 0.5713 0.6854 -0.0103 -0.0569 0.0322  1386 GLN B O     
5049 C  CB    . GLN B 169 ? 0.6360 0.6736 0.7730 -0.0039 -0.0772 0.0270  1386 GLN B CB    
5050 C  CG    . GLN B 169 ? 0.7634 0.8012 0.9008 0.0018  -0.0703 0.0322  1386 GLN B CG    
5051 C  CD    . GLN B 169 ? 0.8244 0.8688 0.9629 0.0093  -0.0753 0.0338  1386 GLN B CD    
5052 O  OE1   . GLN B 169 ? 0.7391 0.7946 0.8870 0.0098  -0.0830 0.0317  1386 GLN B OE1   
5053 N  NE2   . GLN B 169 ? 0.8062 0.8436 0.9350 0.0153  -0.0713 0.0374  1386 GLN B NE2   
5054 N  N     . LYS B 170 ? 0.7322 0.7686 0.8934 -0.0196 -0.0648 0.0262  1387 LYS B N     
5055 C  CA    . LYS B 170 ? 0.7282 0.7663 0.9006 -0.0232 -0.0561 0.0299  1387 LYS B CA    
5056 C  C     . LYS B 170 ? 0.5919 0.6151 0.7507 -0.0242 -0.0497 0.0319  1387 LYS B C     
5057 O  O     . LYS B 170 ? 0.6959 0.7177 0.8532 -0.0222 -0.0416 0.0367  1387 LYS B O     
5058 C  CB    . LYS B 170 ? 0.8001 0.8466 0.9925 -0.0308 -0.0583 0.0276  1387 LYS B CB    
5059 C  CG    . LYS B 170 ? 0.8136 0.8725 1.0247 -0.0325 -0.0518 0.0321  1387 LYS B CG    
5060 C  CD    . LYS B 170 ? 0.8692 0.9324 1.0986 -0.0417 -0.0525 0.0305  1387 LYS B CD    
5061 C  CE    . LYS B 170 ? 0.8797 0.9601 1.1312 -0.0438 -0.0485 0.0338  1387 LYS B CE    
5062 N  NZ    . LYS B 170 ? 0.8388 0.9230 1.1090 -0.0536 -0.0503 0.0317  1387 LYS B NZ    
5063 N  N     . GLU B 171 ? 0.4839 0.4968 0.6333 -0.0270 -0.0531 0.0279  1388 GLU B N     
5064 C  CA    . GLU B 171 ? 0.5920 0.5912 0.7284 -0.0272 -0.0477 0.0293  1388 GLU B CA    
5065 C  C     . GLU B 171 ? 0.5684 0.5632 0.6902 -0.0206 -0.0434 0.0328  1388 GLU B C     
5066 O  O     . GLU B 171 ? 0.6712 0.6612 0.7892 -0.0199 -0.0361 0.0366  1388 GLU B O     
5067 C  CB    . GLU B 171 ? 0.7210 0.7108 0.8477 -0.0296 -0.0529 0.0234  1388 GLU B CB    
5068 C  CG    . GLU B 171 ? 0.7361 0.7290 0.8763 -0.0361 -0.0584 0.0182  1388 GLU B CG    
5069 C  CD    . GLU B 171 ? 0.7720 0.7566 0.9014 -0.0373 -0.0642 0.0112  1388 GLU B CD    
5070 O  OE1   . GLU B 171 ? 0.8402 0.8133 0.9614 -0.0381 -0.0606 0.0108  1388 GLU B OE1   
5071 O  OE2   . GLU B 171 ? 0.7513 0.7415 0.8803 -0.0371 -0.0723 0.0060  1388 GLU B OE2   
5072 N  N     . ALA B 172 ? 0.4949 0.4914 0.6087 -0.0158 -0.0481 0.0318  1389 ALA B N     
5073 C  CA    . ALA B 172 ? 0.4388 0.4298 0.5389 -0.0100 -0.0450 0.0346  1389 ALA B CA    
5074 C  C     . ALA B 172 ? 0.4120 0.4090 0.5192 -0.0067 -0.0386 0.0390  1389 ALA B C     
5075 O  O     . ALA B 172 ? 0.4724 0.4634 0.5715 -0.0045 -0.0325 0.0415  1389 ALA B O     
5076 C  CB    . ALA B 172 ? 0.3847 0.3759 0.4760 -0.0061 -0.0520 0.0330  1389 ALA B CB    
5077 N  N     . ASP B 173 ? 0.3757 0.3855 0.4982 -0.0061 -0.0400 0.0396  1390 ASP B N     
5078 C  CA    . ASP B 173 ? 0.4272 0.4443 0.5571 -0.0027 -0.0335 0.0433  1390 ASP B CA    
5079 C  C     . ASP B 173 ? 0.5127 0.5275 0.6447 -0.0062 -0.0252 0.0461  1390 ASP B C     
5080 O  O     . ASP B 173 ? 0.5366 0.5492 0.6626 -0.0027 -0.0188 0.0488  1390 ASP B O     
5081 C  CB    . ASP B 173 ? 0.5049 0.5380 0.6533 -0.0021 -0.0364 0.0430  1390 ASP B CB    
5082 C  CG    . ASP B 173 ? 0.5975 0.6336 0.7433 0.0034  -0.0442 0.0413  1390 ASP B CG    
5083 O  OD1   . ASP B 173 ? 0.6388 0.6645 0.7684 0.0069  -0.0466 0.0411  1390 ASP B OD1   
5084 O  OD2   . ASP B 173 ? 0.5675 0.6169 0.7279 0.0044  -0.0480 0.0405  1390 ASP B OD2   
5085 N  N     . GLU B 174 ? 0.7138 0.7282 0.8534 -0.0130 -0.0256 0.0455  1391 GLU B N     
5086 C  CA    . GLU B 174 ? 0.6663 0.6782 0.8086 -0.0165 -0.0181 0.0492  1391 GLU B CA    
5087 C  C     . GLU B 174 ? 0.5718 0.5704 0.6965 -0.0147 -0.0147 0.0500  1391 GLU B C     
5088 O  O     . GLU B 174 ? 0.6166 0.6145 0.7386 -0.0134 -0.0076 0.0539  1391 GLU B O     
5089 C  CB    . GLU B 174 ? 0.5568 0.5692 0.7112 -0.0243 -0.0200 0.0483  1391 GLU B CB    
5090 C  CG    . GLU B 174 ? 0.6459 0.6732 0.8203 -0.0271 -0.0219 0.0481  1391 GLU B CG    
5091 C  CD    . GLU B 174 ? 0.8031 0.8303 0.9906 -0.0355 -0.0244 0.0467  1391 GLU B CD    
5092 O  OE1   . GLU B 174 ? 0.6867 0.7015 0.8681 -0.0390 -0.0233 0.0466  1391 GLU B OE1   
5093 O  OE2   . GLU B 174 ? 0.9718 1.0114 1.1767 -0.0387 -0.0273 0.0454  1391 GLU B OE2   
5094 N  N     . GLU B 175 ? 0.4641 0.4528 0.5766 -0.0144 -0.0198 0.0463  1392 GLU B N     
5095 C  CA    . GLU B 175 ? 0.5639 0.5412 0.6610 -0.0128 -0.0167 0.0467  1392 GLU B CA    
5096 C  C     . GLU B 175 ? 0.6083 0.5854 0.6962 -0.0066 -0.0134 0.0483  1392 GLU B C     
5097 O  O     . GLU B 175 ? 0.6821 0.6547 0.7626 -0.0052 -0.0080 0.0504  1392 GLU B O     
5098 C  CB    . GLU B 175 ? 0.5758 0.5439 0.6623 -0.0139 -0.0223 0.0422  1392 GLU B CB    
5099 C  CG    . GLU B 175 ? 0.5929 0.5504 0.6649 -0.0125 -0.0190 0.0425  1392 GLU B CG    
5100 C  CD    . GLU B 175 ? 0.6221 0.5722 0.6816 -0.0121 -0.0237 0.0381  1392 GLU B CD    
5101 O  OE1   . GLU B 175 ? 0.7240 0.6679 0.7808 -0.0148 -0.0246 0.0357  1392 GLU B OE1   
5102 O  OE2   . GLU B 175 ? 0.6284 0.5790 0.6810 -0.0090 -0.0265 0.0373  1392 GLU B OE2   
5103 N  N     . VAL B 176 ? 0.5534 0.5350 0.6415 -0.0026 -0.0168 0.0472  1393 VAL B N     
5104 C  CA    . VAL B 176 ? 0.5807 0.5615 0.6617 0.0033  -0.0137 0.0483  1393 VAL B CA    
5105 C  C     . VAL B 176 ? 0.5816 0.5682 0.6680 0.0043  -0.0060 0.0515  1393 VAL B C     
5106 O  O     . VAL B 176 ? 0.6197 0.6014 0.6966 0.0066  -0.0014 0.0524  1393 VAL B O     
5107 C  CB    . VAL B 176 ? 0.5654 0.5515 0.6495 0.0077  -0.0183 0.0474  1393 VAL B CB    
5108 C  CG1   . VAL B 176 ? 0.4225 0.4085 0.5024 0.0140  -0.0143 0.0483  1393 VAL B CG1   
5109 C  CG2   . VAL B 176 ? 0.5446 0.5238 0.6193 0.0077  -0.0253 0.0451  1393 VAL B CG2   
5110 N  N     . LEU B 177 ? 0.4037 0.4014 0.5054 0.0022  -0.0044 0.0533  1394 LEU B N     
5111 C  CA    . LEU B 177 ? 0.3751 0.3800 0.4815 0.0035  0.0034  0.0567  1394 LEU B CA    
5112 C  C     . LEU B 177 ? 0.4149 0.4137 0.5160 0.0002  0.0084  0.0596  1394 LEU B C     
5113 O  O     . LEU B 177 ? 0.4696 0.4695 0.5657 0.0029  0.0146  0.0619  1394 LEU B O     
5114 C  CB    . LEU B 177 ? 0.4127 0.4323 0.5375 0.0021  0.0043  0.0581  1394 LEU B CB    
5115 C  CG    . LEU B 177 ? 0.4980 0.5230 0.6244 0.0085  0.0013  0.0557  1394 LEU B CG    
5116 C  CD1   . LEU B 177 ? 0.5050 0.5420 0.6480 0.0073  -0.0035 0.0547  1394 LEU B CD1   
5117 C  CD2   . LEU B 177 ? 0.4290 0.4589 0.5533 0.0142  0.0082  0.0568  1394 LEU B CD2   
5118 N  N     . THR B 178 ? 0.3660 0.3585 0.4680 -0.0053 0.0055  0.0593  1395 THR B N     
5119 C  CA    . THR B 178 ? 0.4556 0.4407 0.5524 -0.0081 0.0093  0.0621  1395 THR B CA    
5120 C  C     . THR B 178 ? 0.4661 0.4428 0.5462 -0.0038 0.0108  0.0612  1395 THR B C     
5121 O  O     . THR B 178 ? 0.5944 0.5712 0.6696 -0.0022 0.0165  0.0644  1395 THR B O     
5122 C  CB    . THR B 178 ? 0.5469 0.5251 0.6471 -0.0138 0.0046  0.0604  1395 THR B CB    
5123 O  OG1   . THR B 178 ? 0.7008 0.6871 0.8180 -0.0186 0.0036  0.0615  1395 THR B OG1   
5124 C  CG2   . THR B 178 ? 0.3726 0.3420 0.4673 -0.0159 0.0077  0.0631  1395 THR B CG2   
5125 N  N     . ILE B 179 ? 0.5242 0.4942 0.5954 -0.0021 0.0057  0.0569  1396 ILE B N     
5126 C  CA    . ILE B 179 ? 0.6063 0.5686 0.6626 0.0013  0.0065  0.0554  1396 ILE B CA    
5127 C  C     . ILE B 179 ? 0.5985 0.5658 0.6520 0.0065  0.0111  0.0563  1396 ILE B C     
5128 O  O     . ILE B 179 ? 0.5551 0.5190 0.5992 0.0087  0.0145  0.0566  1396 ILE B O     
5129 C  CB    . ILE B 179 ? 0.6288 0.5847 0.6778 0.0017  0.0004  0.0512  1396 ILE B CB    
5130 C  CG1   . ILE B 179 ? 0.4812 0.4333 0.5331 -0.0031 -0.0041 0.0493  1396 ILE B CG1   
5131 C  CG2   . ILE B 179 ? 0.7707 0.7194 0.8057 0.0048  0.0014  0.0496  1396 ILE B CG2   
5132 C  CD1   . ILE B 179 ? 0.3672 0.3113 0.4130 -0.0052 -0.0031 0.0490  1396 ILE B CD1   
5133 N  N     . LEU B 180 ? 0.6251 0.6008 0.6867 0.0088  0.0110  0.0561  1397 LEU B N     
5134 C  CA    . LEU B 180 ? 0.6916 0.6720 0.7507 0.0143  0.0153  0.0560  1397 LEU B CA    
5135 C  C     . LEU B 180 ? 0.5878 0.5741 0.6482 0.0142  0.0225  0.0598  1397 LEU B C     
5136 O  O     . LEU B 180 ? 0.6504 0.6365 0.7025 0.0181  0.0263  0.0593  1397 LEU B O     
5137 C  CB    . LEU B 180 ? 0.6796 0.6687 0.7485 0.0174  0.0138  0.0549  1397 LEU B CB    
5138 C  CG    . LEU B 180 ? 0.5239 0.5149 0.5877 0.0239  0.0174  0.0532  1397 LEU B CG    
5139 C  CD1   . LEU B 180 ? 0.3682 0.3475 0.4200 0.0261  0.0134  0.0498  1397 LEU B CD1   
5140 C  CD2   . LEU B 180 ? 0.4050 0.4082 0.4809 0.0278  0.0187  0.0529  1397 LEU B CD2   
5141 N  N     . ASP B 181 ? 0.6043 0.5961 0.6752 0.0098  0.0244  0.0637  1398 ASP B N     
5142 C  CA    . ASP B 181 ? 0.6792 0.6759 0.7508 0.0091  0.0314  0.0687  1398 ASP B CA    
5143 C  C     . ASP B 181 ? 0.6265 0.6135 0.6849 0.0090  0.0323  0.0695  1398 ASP B C     
5144 O  O     . ASP B 181 ? 0.5637 0.5533 0.6156 0.0117  0.0375  0.0718  1398 ASP B O     
5145 C  CB    . ASP B 181 ? 0.7405 0.7431 0.8266 0.0032  0.0327  0.0731  1398 ASP B CB    
5146 C  CG    . ASP B 181 ? 0.8430 0.8523 0.9309 0.0025  0.0406  0.0794  1398 ASP B CG    
5147 O  OD1   . ASP B 181 ? 0.7870 0.7915 0.8761 -0.0022 0.0419  0.0840  1398 ASP B OD1   
5148 O  OD2   . ASP B 181 ? 0.9813 1.0004 1.0690 0.0069  0.0456  0.0798  1398 ASP B OD2   
5149 N  N     . LEU B 182 ? 0.5928 0.5693 0.6469 0.0064  0.0271  0.0674  1399 LEU B N     
5150 C  CA    . LEU B 182 ? 0.6177 0.5853 0.6598 0.0069  0.0273  0.0674  1399 LEU B CA    
5151 C  C     . LEU B 182 ? 0.7187 0.6853 0.7490 0.0122  0.0282  0.0641  1399 LEU B C     
5152 O  O     . LEU B 182 ? 0.6922 0.6584 0.7145 0.0143  0.0316  0.0656  1399 LEU B O     
5153 C  CB    . LEU B 182 ? 0.6534 0.6113 0.6937 0.0036  0.0215  0.0646  1399 LEU B CB    
5154 C  CG    . LEU B 182 ? 0.6467 0.6030 0.6967 -0.0018 0.0207  0.0675  1399 LEU B CG    
5155 C  CD1   . LEU B 182 ? 0.3719 0.3181 0.4184 -0.0042 0.0151  0.0636  1399 LEU B CD1   
5156 C  CD2   . LEU B 182 ? 0.3767 0.3343 0.4264 -0.0020 0.0264  0.0737  1399 LEU B CD2   
5157 N  N     . TYR B 183 ? 0.7648 0.7304 0.7939 0.0145  0.0249  0.0595  1400 TYR B N     
5158 C  CA    . TYR B 183 ? 0.5689 0.5327 0.5883 0.0192  0.0254  0.0557  1400 TYR B CA    
5159 C  C     . TYR B 183 ? 0.5242 0.4968 0.5431 0.0232  0.0313  0.0570  1400 TYR B C     
5160 O  O     . TYR B 183 ? 0.6599 0.6314 0.6692 0.0259  0.0336  0.0560  1400 TYR B O     
5161 C  CB    . TYR B 183 ? 0.6147 0.5762 0.6355 0.0207  0.0210  0.0519  1400 TYR B CB    
5162 C  CG    . TYR B 183 ? 0.5542 0.5066 0.5712 0.0177  0.0154  0.0499  1400 TYR B CG    
5163 C  CD1   . TYR B 183 ? 0.5260 0.4719 0.5357 0.0155  0.0148  0.0496  1400 TYR B CD1   
5164 C  CD2   . TYR B 183 ? 0.4745 0.4255 0.4949 0.0175  0.0107  0.0483  1400 TYR B CD2   
5165 C  CE1   . TYR B 183 ? 0.4789 0.4176 0.4848 0.0130  0.0103  0.0474  1400 TYR B CE1   
5166 C  CE2   . TYR B 183 ? 0.4282 0.3716 0.4437 0.0149  0.0060  0.0466  1400 TYR B CE2   
5167 C  CZ    . TYR B 183 ? 0.4051 0.3427 0.4133 0.0125  0.0061  0.0460  1400 TYR B CZ    
5168 O  OH    . TYR B 183 ? 0.3651 0.2965 0.3682 0.0102  0.0022  0.0441  1400 TYR B OH    
5169 N  N     . ALA B 184 ? 0.3731 0.3553 0.4023 0.0239  0.0340  0.0589  1401 ALA B N     
5170 C  CA    . ALA B 184 ? 0.3770 0.3692 0.4060 0.0277  0.0403  0.0602  1401 ALA B CA    
5171 C  C     . ALA B 184 ? 0.5654 0.5587 0.5887 0.0265  0.0447  0.0651  1401 ALA B C     
5172 O  O     . ALA B 184 ? 0.5753 0.5730 0.5908 0.0305  0.0488  0.0646  1401 ALA B O     
5173 C  CB    . ALA B 184 ? 0.3769 0.3806 0.4200 0.0276  0.0426  0.0622  1401 ALA B CB    
5174 N  N     . LYS B 185 ? 0.3964 0.3857 0.4230 0.0213  0.0438  0.0696  1402 LYS B N     
5175 C  CA    . LYS B 185 ? 0.5350 0.5242 0.5561 0.0205  0.0476  0.0751  1402 LYS B CA    
5176 C  C     . LYS B 185 ? 0.6416 0.6233 0.6486 0.0230  0.0455  0.0721  1402 LYS B C     
5177 O  O     . LYS B 185 ? 0.5708 0.5551 0.5699 0.0253  0.0490  0.0749  1402 LYS B O     
5178 C  CB    . LYS B 185 ? 0.5053 0.4911 0.5348 0.0144  0.0470  0.0807  1402 LYS B CB    
5179 C  CG    . LYS B 185 ? 0.5159 0.5119 0.5584 0.0115  0.0518  0.0865  1402 LYS B CG    
5180 C  CD    . LYS B 185 ? 0.6695 0.6600 0.7211 0.0049  0.0501  0.0910  1402 LYS B CD    
5181 C  CE    . LYS B 185 ? 0.8207 0.8208 0.8842 0.0013  0.0561  0.0985  1402 LYS B CE    
5182 N  NZ    . LYS B 185 ? 0.8581 0.8508 0.9302 -0.0055 0.0546  0.1033  1402 LYS B NZ    
5183 N  N     . VAL B 186 ? 0.6054 0.5783 0.6094 0.0224  0.0399  0.0669  1403 VAL B N     
5184 C  CA    . VAL B 186 ? 0.5731 0.5403 0.5650 0.0248  0.0379  0.0631  1403 VAL B CA    
5185 C  C     . VAL B 186 ? 0.6113 0.5847 0.5965 0.0302  0.0409  0.0600  1403 VAL B C     
5186 O  O     . VAL B 186 ? 0.5296 0.5037 0.5052 0.0327  0.0421  0.0595  1403 VAL B O     
5187 C  CB    . VAL B 186 ? 0.5718 0.5303 0.5624 0.0234  0.0321  0.0577  1403 VAL B CB    
5188 C  CG1   . VAL B 186 ? 0.3776 0.3324 0.3573 0.0261  0.0306  0.0528  1403 VAL B CG1   
5189 C  CG2   . VAL B 186 ? 0.6363 0.5884 0.6308 0.0188  0.0289  0.0597  1403 VAL B CG2   
5190 N  N     . TYR B 187 ? 0.7194 0.6979 0.7098 0.0323  0.0420  0.0574  1404 TYR B N     
5191 C  CA    . TYR B 187 ? 0.7879 0.7712 0.7719 0.0378  0.0443  0.0528  1404 TYR B CA    
5192 C  C     . TYR B 187 ? 0.8161 0.8099 0.7973 0.0403  0.0507  0.0569  1404 TYR B C     
5193 O  O     . TYR B 187 ? 0.8213 0.8170 0.7920 0.0438  0.0520  0.0547  1404 TYR B O     
5194 C  CB    . TYR B 187 ? 0.7285 0.7132 0.7188 0.0401  0.0432  0.0482  1404 TYR B CB    
5195 C  CG    . TYR B 187 ? 0.5607 0.5348 0.5465 0.0403  0.0377  0.0423  1404 TYR B CG    
5196 C  CD1   . TYR B 187 ? 0.5116 0.4780 0.5014 0.0363  0.0329  0.0427  1404 TYR B CD1   
5197 C  CD2   . TYR B 187 ? 0.4765 0.4484 0.4536 0.0439  0.0374  0.0364  1404 TYR B CD2   
5198 C  CE1   . TYR B 187 ? 0.5382 0.4953 0.5235 0.0359  0.0285  0.0383  1404 TYR B CE1   
5199 C  CE2   . TYR B 187 ? 0.4985 0.4604 0.4722 0.0431  0.0327  0.0316  1404 TYR B CE2   
5200 C  CZ    . TYR B 187 ? 0.5621 0.5167 0.5397 0.0391  0.0285  0.0330  1404 TYR B CZ    
5201 O  OH    . TYR B 187 ? 0.5704 0.5155 0.5445 0.0380  0.0244  0.0292  1404 TYR B OH    
5202 N  N     . THR B 188 ? 0.7699 0.7709 0.7602 0.0382  0.0546  0.0631  1405 THR B N     
5203 C  CA    . THR B 188 ? 0.6895 0.7021 0.6775 0.0408  0.0615  0.0672  1405 THR B CA    
5204 C  C     . THR B 188 ? 0.6630 0.6749 0.6453 0.0388  0.0636  0.0746  1405 THR B C     
5205 O  O     . THR B 188 ? 0.6730 0.6919 0.6465 0.0423  0.0680  0.0766  1405 THR B O     
5206 C  CB    . THR B 188 ? 0.5815 0.6046 0.5829 0.0396  0.0659  0.0709  1405 THR B CB    
5207 O  OG1   . THR B 188 ? 0.6284 0.6494 0.6378 0.0334  0.0660  0.0785  1405 THR B OG1   
5208 C  CG2   . THR B 188 ? 0.4992 0.5219 0.5093 0.0408  0.0626  0.0650  1405 THR B CG2   
5209 N  N     . ASP B 189 ? 0.7934 0.7968 0.7802 0.0336  0.0604  0.0786  1406 ASP B N     
5210 C  CA    . ASP B 189 ? 0.8028 0.8037 0.7859 0.0316  0.0619  0.0863  1406 ASP B CA    
5211 C  C     . ASP B 189 ? 0.7432 0.7359 0.7147 0.0333  0.0577  0.0838  1406 ASP B C     
5212 O  O     . ASP B 189 ? 0.6674 0.6608 0.6315 0.0345  0.0596  0.0890  1406 ASP B O     
5213 C  CB    . ASP B 189 ? 0.6391 0.6353 0.6347 0.0252  0.0609  0.0917  1406 ASP B CB    
5214 C  CG    . ASP B 189 ? 0.5980 0.6039 0.6065 0.0231  0.0650  0.0943  1406 ASP B CG    
5215 O  OD1   . ASP B 189 ? 0.5490 0.5663 0.5556 0.0269  0.0703  0.0943  1406 ASP B OD1   
5216 O  OD2   . ASP B 189 ? 0.6298 0.6327 0.6505 0.0180  0.0628  0.0956  1406 ASP B OD2   
5217 N  N     . LEU B 190 ? 0.7935 0.7789 0.7632 0.0335  0.0521  0.0761  1407 LEU B N     
5218 C  CA    . LEU B 190 ? 0.7328 0.7123 0.6922 0.0352  0.0484  0.0731  1407 LEU B CA    
5219 C  C     . LEU B 190 ? 0.7709 0.7553 0.7203 0.0404  0.0487  0.0665  1407 LEU B C     
5220 O  O     . LEU B 190 ? 0.9619 0.9493 0.9014 0.0435  0.0495  0.0675  1407 LEU B O     
5221 C  CB    . LEU B 190 ? 0.5794 0.5485 0.5421 0.0320  0.0424  0.0687  1407 LEU B CB    
5222 C  CG    . LEU B 190 ? 0.5106 0.4733 0.4825 0.0269  0.0406  0.0731  1407 LEU B CG    
5223 C  CD1   . LEU B 190 ? 0.3882 0.3419 0.3602 0.0248  0.0349  0.0679  1407 LEU B CD1   
5224 C  CD2   . LEU B 190 ? 0.4012 0.3630 0.3721 0.0262  0.0427  0.0809  1407 LEU B CD2   
5225 N  N     . LEU B 191 ? 0.6132 0.5988 0.5652 0.0418  0.0482  0.0599  1408 LEU B N     
5226 C  CA    . LEU B 191 ? 0.5541 0.5420 0.4979 0.0463  0.0475  0.0521  1408 LEU B CA    
5227 C  C     . LEU B 191 ? 0.5591 0.5583 0.5008 0.0508  0.0529  0.0515  1408 LEU B C     
5228 O  O     . LEU B 191 ? 0.5795 0.5811 0.5144 0.0550  0.0526  0.0443  1408 LEU B O     
5229 C  CB    . LEU B 191 ? 0.4770 0.4574 0.4244 0.0452  0.0430  0.0448  1408 LEU B CB    
5230 C  CG    . LEU B 191 ? 0.4735 0.4441 0.4215 0.0410  0.0380  0.0448  1408 LEU B CG    
5231 C  CD1   . LEU B 191 ? 0.3906 0.3535 0.3428 0.0390  0.0339  0.0395  1408 LEU B CD1   
5232 C  CD2   . LEU B 191 ? 0.3990 0.3692 0.3372 0.0426  0.0363  0.0430  1408 LEU B CD2   
5233 N  N     . ALA B 192 ? 0.5977 0.6041 0.5455 0.0500  0.0581  0.0584  1409 ALA B N     
5234 C  CA    . ALA B 192 ? 0.6448 0.6639 0.5911 0.0543  0.0643  0.0587  1409 ALA B CA    
5235 C  C     . ALA B 192 ? 0.6534 0.6741 0.6024 0.0579  0.0637  0.0496  1409 ALA B C     
5236 O  O     . ALA B 192 ? 0.5479 0.5758 0.4900 0.0633  0.0663  0.0444  1409 ALA B O     
5237 C  CB    . ALA B 192 ? 0.4325 0.4582 0.3650 0.0583  0.0670  0.0600  1409 ALA B CB    
5238 N  N     . ILE B 193 ? 0.5661 0.5800 0.5252 0.0552  0.0602  0.0477  1410 ILE B N     
5239 C  CA    . ILE B 193 ? 0.6578 0.6712 0.6212 0.0584  0.0589  0.0400  1410 ILE B CA    
5240 C  C     . ILE B 193 ? 0.7222 0.7417 0.6993 0.0575  0.0614  0.0432  1410 ILE B C     
5241 O  O     . ILE B 193 ? 0.8006 0.8179 0.7859 0.0523  0.0603  0.0492  1410 ILE B O     
5242 C  CB    . ILE B 193 ? 0.7110 0.7108 0.6737 0.0565  0.0519  0.0346  1410 ILE B CB    
5243 C  CG1   . ILE B 193 ? 0.7298 0.7253 0.6802 0.0575  0.0495  0.0305  1410 ILE B CG1   
5244 C  CG2   . ILE B 193 ? 0.6541 0.6518 0.6221 0.0597  0.0503  0.0279  1410 ILE B CG2   
5245 C  CD1   . ILE B 193 ? 0.7494 0.7326 0.6994 0.0549  0.0433  0.0259  1410 ILE B CD1   
5246 N  N     . PRO B 194 ? 0.6773 0.7054 0.6578 0.0626  0.0647  0.0391  1411 PRO B N     
5247 C  CA    . PRO B 194 ? 0.5519 0.5863 0.5468 0.0623  0.0663  0.0411  1411 PRO B CA    
5248 C  C     . PRO B 194 ? 0.6503 0.6748 0.6515 0.0622  0.0599  0.0364  1411 PRO B C     
5249 O  O     . PRO B 194 ? 0.7868 0.8031 0.7821 0.0651  0.0563  0.0293  1411 PRO B O     
5250 C  CB    . PRO B 194 ? 0.5756 0.6241 0.5704 0.0689  0.0728  0.0378  1411 PRO B CB    
5251 C  CG    . PRO B 194 ? 0.7039 0.7482 0.6851 0.0736  0.0715  0.0300  1411 PRO B CG    
5252 C  CD    . PRO B 194 ? 0.7828 0.8176 0.7542 0.0692  0.0680  0.0329  1411 PRO B CD    
5253 N  N     . VAL B 195 ? 0.6905 0.7157 0.7039 0.0584  0.0582  0.0406  1412 VAL B N     
5254 C  CA    . VAL B 195 ? 0.6023 0.6188 0.6219 0.0577  0.0519  0.0379  1412 VAL B CA    
5255 C  C     . VAL B 195 ? 0.6127 0.6389 0.6477 0.0581  0.0528  0.0401  1412 VAL B C     
5256 O  O     . VAL B 195 ? 0.5810 0.6182 0.6234 0.0556  0.0573  0.0455  1412 VAL B O     
5257 C  CB    . VAL B 195 ? 0.5634 0.5677 0.5806 0.0514  0.0462  0.0406  1412 VAL B CB    
5258 C  CG1   . VAL B 195 ? 0.5148 0.5102 0.5183 0.0511  0.0447  0.0380  1412 VAL B CG1   
5259 C  CG2   . VAL B 195 ? 0.4991 0.5078 0.5237 0.0455  0.0475  0.0481  1412 VAL B CG2   
5260 N  N     . VAL B 196 ? 0.7096 0.7316 0.7498 0.0611  0.0483  0.0359  1413 VAL B N     
5261 C  CA    . VAL B 196 ? 0.6003 0.6305 0.6554 0.0623  0.0474  0.0369  1413 VAL B CA    
5262 C  C     . VAL B 196 ? 0.6224 0.6442 0.6817 0.0569  0.0405  0.0396  1413 VAL B C     
5263 O  O     . VAL B 196 ? 0.7179 0.7266 0.7710 0.0571  0.0347  0.0370  1413 VAL B O     
5264 C  CB    . VAL B 196 ? 0.5646 0.5960 0.6223 0.0706  0.0469  0.0303  1413 VAL B CB    
5265 C  CG1   . VAL B 196 ? 0.4820 0.5178 0.5539 0.0721  0.0433  0.0307  1413 VAL B CG1   
5266 C  CG2   . VAL B 196 ? 0.5190 0.5637 0.5762 0.0760  0.0547  0.0278  1413 VAL B CG2   
5267 N  N     . LYS B 197 ? 0.5608 0.5903 0.6306 0.0520  0.0410  0.0448  1414 LYS B N     
5268 C  CA    . LYS B 197 ? 0.5534 0.5776 0.6289 0.0475  0.0342  0.0465  1414 LYS B CA    
5269 C  C     . LYS B 197 ? 0.5345 0.5631 0.6205 0.0520  0.0304  0.0441  1414 LYS B C     
5270 O  O     . LYS B 197 ? 0.4898 0.5318 0.5862 0.0560  0.0341  0.0435  1414 LYS B O     
5271 C  CB    . LYS B 197 ? 0.5922 0.6234 0.6766 0.0406  0.0358  0.0521  1414 LYS B CB    
5272 C  CG    . LYS B 197 ? 0.5692 0.5937 0.6455 0.0349  0.0373  0.0556  1414 LYS B CG    
5273 C  CD    . LYS B 197 ? 0.4460 0.4789 0.5346 0.0288  0.0394  0.0610  1414 LYS B CD    
5274 C  CE    . LYS B 197 ? 0.6818 0.7050 0.7650 0.0224  0.0379  0.0642  1414 LYS B CE    
5275 N  NZ    . LYS B 197 ? 0.7523 0.7788 0.8488 0.0157  0.0359  0.0674  1414 LYS B NZ    
5276 N  N     . GLY B 198 ? 0.5617 0.5797 0.6451 0.0516  0.0229  0.0430  1415 GLY B N     
5277 C  CA    . GLY B 198 ? 0.5184 0.5405 0.6120 0.0559  0.0184  0.0416  1415 GLY B CA    
5278 C  C     . GLY B 198 ? 0.5854 0.5976 0.6767 0.0536  0.0100  0.0423  1415 GLY B C     
5279 O  O     . GLY B 198 ? 0.5851 0.5873 0.6671 0.0483  0.0077  0.0435  1415 GLY B O     
5280 N  N     . ARG B 199 ? 0.6686 0.6848 0.7687 0.0579  0.0053  0.0415  1416 ARG B N     
5281 C  CA    . ARG B 199 ? 0.7233 0.7301 0.8201 0.0578  -0.0031 0.0421  1416 ARG B CA    
5282 C  C     . ARG B 199 ? 0.7850 0.7801 0.8737 0.0642  -0.0050 0.0397  1416 ARG B C     
5283 O  O     . ARG B 199 ? 0.8189 0.8180 0.9119 0.0709  -0.0020 0.0369  1416 ARG B O     
5284 C  CB    . ARG B 199 ? 0.7705 0.7887 0.8819 0.0591  -0.0079 0.0431  1416 ARG B CB    
5285 C  CG    . ARG B 199 ? 0.9135 0.9347 1.0285 0.0517  -0.0121 0.0453  1416 ARG B CG    
5286 C  CD    . ARG B 199 ? 0.9115 0.9441 1.0408 0.0538  -0.0180 0.0456  1416 ARG B CD    
5287 N  NE    . ARG B 199 ? 0.7935 0.8169 0.9164 0.0576  -0.0260 0.0458  1416 ARG B NE    
5288 C  CZ    . ARG B 199 ? 0.7625 0.7905 0.8910 0.0573  -0.0337 0.0466  1416 ARG B CZ    
5289 N  NH1   . ARG B 199 ? 0.7901 0.8319 0.9320 0.0529  -0.0347 0.0465  1416 ARG B NH1   
5290 N  NH2   . ARG B 199 ? 0.7686 0.7875 0.8894 0.0611  -0.0406 0.0476  1416 ARG B NH2   
5291 N  N     . LYS B 200 ? 0.7929 0.7736 0.8703 0.0621  -0.0098 0.0406  1417 LYS B N     
5292 C  CA    . LYS B 200 ? 0.8047 0.7733 0.8756 0.0675  -0.0123 0.0391  1417 LYS B CA    
5293 C  C     . LYS B 200 ? 0.8323 0.8030 0.9112 0.0729  -0.0187 0.0404  1417 LYS B C     
5294 O  O     . LYS B 200 ? 0.8120 0.7893 0.8966 0.0705  -0.0233 0.0430  1417 LYS B O     
5295 C  CB    . LYS B 200 ? 0.6766 0.6291 0.7324 0.0631  -0.0143 0.0401  1417 LYS B CB    
5296 C  CG    . LYS B 200 ? 0.7225 0.6712 0.7696 0.0596  -0.0085 0.0380  1417 LYS B CG    
5297 C  CD    . LYS B 200 ? 0.7686 0.7071 0.8092 0.0637  -0.0069 0.0345  1417 LYS B CD    
5298 C  CE    . LYS B 200 ? 0.8290 0.7627 0.8595 0.0593  -0.0029 0.0328  1417 LYS B CE    
5299 N  NZ    . LYS B 200 ? 0.9928 0.9156 1.0166 0.0622  -0.0021 0.0288  1417 LYS B NZ    
5300 N  N     . THR B 201 ? 0.7303 0.6955 0.8100 0.0804  -0.0193 0.0384  1418 THR B N     
5301 C  CA    . THR B 201 ? 0.6310 0.5972 0.7182 0.0867  -0.0256 0.0398  1418 THR B CA    
5302 C  C     . THR B 201 ? 0.6283 0.5839 0.7068 0.0835  -0.0330 0.0443  1418 THR B C     
5303 O  O     . THR B 201 ? 0.5087 0.4545 0.5749 0.0771  -0.0327 0.0457  1418 THR B O     
5304 C  CB    . THR B 201 ? 0.6620 0.6212 0.7503 0.0955  -0.0249 0.0366  1418 THR B CB    
5305 O  OG1   . THR B 201 ? 0.7734 0.7137 0.8478 0.0938  -0.0252 0.0365  1418 THR B OG1   
5306 C  CG2   . THR B 201 ? 0.5676 0.5383 0.6633 0.0990  -0.0173 0.0315  1418 THR B CG2   
5307 N  N     . GLU B 202 ? 0.7605 0.7190 0.8457 0.0884  -0.0396 0.0467  1419 GLU B N     
5308 C  CA    . GLU B 202 ? 0.7749 0.7235 0.8512 0.0868  -0.0470 0.0514  1419 GLU B CA    
5309 C  C     . GLU B 202 ? 0.8248 0.7532 0.8873 0.0870  -0.0470 0.0527  1419 GLU B C     
5310 O  O     . GLU B 202 ? 0.8636 0.7824 0.9147 0.0826  -0.0504 0.0566  1419 GLU B O     
5311 C  CB    . GLU B 202 ? 0.7359 0.6916 0.8221 0.0936  -0.0543 0.0536  1419 GLU B CB    
5312 C  CG    . GLU B 202 ? 0.8997 0.8749 0.9980 0.0908  -0.0562 0.0532  1419 GLU B CG    
5313 C  CD    . GLU B 202 ? 0.8852 0.8604 0.9753 0.0809  -0.0570 0.0545  1419 GLU B CD    
5314 O  OE1   . GLU B 202 ? 0.9252 0.9037 1.0150 0.0750  -0.0507 0.0521  1419 GLU B OE1   
5315 O  OE2   . GLU B 202 ? 0.8746 0.8467 0.9583 0.0794  -0.0639 0.0577  1419 GLU B OE2   
5316 N  N     . LYS B 203 ? 0.7405 0.6626 0.8042 0.0919  -0.0431 0.0493  1420 LYS B N     
5317 C  CA    . LYS B 203 ? 0.7859 0.6887 0.8376 0.0911  -0.0427 0.0498  1420 LYS B CA    
5318 C  C     . LYS B 203 ? 0.8100 0.7088 0.8514 0.0825  -0.0375 0.0483  1420 LYS B C     
5319 O  O     . LYS B 203 ? 0.8154 0.7007 0.8453 0.0783  -0.0386 0.0509  1420 LYS B O     
5320 C  CB    . LYS B 203 ? 0.8526 0.7496 0.9095 0.0992  -0.0406 0.0456  1420 LYS B CB    
5321 C  CG    . LYS B 203 ? 0.9068 0.7841 0.9530 0.0978  -0.0397 0.0451  1420 LYS B CG    
5322 C  CD    . LYS B 203 ? 0.9086 0.7777 0.9602 0.1064  -0.0393 0.0410  1420 LYS B CD    
5323 C  CE    . LYS B 203 ? 0.9033 0.7547 0.9449 0.1031  -0.0369 0.0386  1420 LYS B CE    
5324 N  NZ    . LYS B 203 ? 0.9495 0.7983 0.9964 0.1095  -0.0333 0.0305  1420 LYS B NZ    
5325 N  N     . GLU B 204 ? 0.7306 0.6412 0.7759 0.0799  -0.0320 0.0447  1421 GLU B N     
5326 C  CA    . GLU B 204 ? 0.6564 0.5636 0.6928 0.0731  -0.0271 0.0429  1421 GLU B CA    
5327 C  C     . GLU B 204 ? 0.5641 0.4773 0.5971 0.0654  -0.0275 0.0453  1421 GLU B C     
5328 O  O     . GLU B 204 ? 0.5335 0.4439 0.5590 0.0598  -0.0239 0.0442  1421 GLU B O     
5329 C  CB    . GLU B 204 ? 0.8279 0.7425 0.8689 0.0753  -0.0203 0.0373  1421 GLU B CB    
5330 C  CG    . GLU B 204 ? 0.9852 0.8942 1.0295 0.0832  -0.0194 0.0333  1421 GLU B CG    
5331 C  CD    . GLU B 204 ? 1.0780 0.9679 1.1122 0.0824  -0.0208 0.0327  1421 GLU B CD    
5332 O  OE1   . GLU B 204 ? 1.1307 1.0140 1.1550 0.0752  -0.0204 0.0344  1421 GLU B OE1   
5333 O  OE2   . GLU B 204 ? 1.0625 0.9444 1.0996 0.0889  -0.0221 0.0304  1421 GLU B OE2   
5334 N  N     . LYS B 205 ? 0.4857 0.4070 0.5241 0.0652  -0.0321 0.0482  1422 LYS B N     
5335 C  CA    . LYS B 205 ? 0.5109 0.4375 0.5466 0.0581  -0.0328 0.0496  1422 LYS B CA    
5336 C  C     . LYS B 205 ? 0.5839 0.4980 0.6053 0.0530  -0.0347 0.0520  1422 LYS B C     
5337 O  O     . LYS B 205 ? 0.6537 0.5553 0.6680 0.0547  -0.0359 0.0534  1422 LYS B O     
5338 C  CB    . LYS B 205 ? 0.4192 0.3578 0.4648 0.0592  -0.0379 0.0513  1422 LYS B CB    
5339 C  CG    . LYS B 205 ? 0.4282 0.3618 0.4692 0.0607  -0.0458 0.0553  1422 LYS B CG    
5340 C  CD    . LYS B 205 ? 0.4272 0.3745 0.4789 0.0619  -0.0513 0.0561  1422 LYS B CD    
5341 C  CE    . LYS B 205 ? 0.5073 0.4493 0.5514 0.0628  -0.0593 0.0603  1422 LYS B CE    
5342 N  NZ    . LYS B 205 ? 0.4356 0.3863 0.4800 0.0587  -0.0648 0.0607  1422 LYS B NZ    
5343 N  N     . PHE B 206 ? 0.5569 0.4741 0.5742 0.0466  -0.0343 0.0521  1423 PHE B N     
5344 C  CA    . PHE B 206 ? 0.5257 0.4337 0.5303 0.0419  -0.0362 0.0542  1423 PHE B CA    
5345 C  C     . PHE B 206 ? 0.6079 0.5154 0.6107 0.0437  -0.0433 0.0581  1423 PHE B C     
5346 O  O     . PHE B 206 ? 0.8247 0.7427 0.8354 0.0448  -0.0470 0.0582  1423 PHE B O     
5347 C  CB    . PHE B 206 ? 0.5785 0.4908 0.5803 0.0354  -0.0337 0.0524  1423 PHE B CB    
5348 C  CG    . PHE B 206 ? 0.7163 0.6220 0.7060 0.0307  -0.0354 0.0539  1423 PHE B CG    
5349 C  CD1   . PHE B 206 ? 0.8803 0.7747 0.8603 0.0306  -0.0356 0.0561  1423 PHE B CD1   
5350 C  CD2   . PHE B 206 ? 0.8045 0.7156 0.7929 0.0261  -0.0365 0.0528  1423 PHE B CD2   
5351 C  CE1   . PHE B 206 ? 0.8559 0.7456 0.8249 0.0260  -0.0365 0.0576  1423 PHE B CE1   
5352 C  CE2   . PHE B 206 ? 0.7349 0.6410 0.7121 0.0222  -0.0377 0.0535  1423 PHE B CE2   
5353 C  CZ    . PHE B 206 ? 0.7303 0.6264 0.6977 0.0221  -0.0374 0.0561  1423 PHE B CZ    
5354 N  N     . ALA B 207 ? 0.5908 0.4867 0.5837 0.0440  -0.0455 0.0616  1424 ALA B N     
5355 C  CA    . ALA B 207 ? 0.6667 0.5613 0.6579 0.0475  -0.0525 0.0663  1424 ALA B CA    
5356 C  C     . ALA B 207 ? 0.5542 0.4578 0.5437 0.0444  -0.0570 0.0668  1424 ALA B C     
5357 O  O     . ALA B 207 ? 0.5392 0.4507 0.5352 0.0479  -0.0626 0.0679  1424 ALA B O     
5358 C  CB    . ALA B 207 ? 0.8023 0.6818 0.7820 0.0476  -0.0535 0.0709  1424 ALA B CB    
5359 N  N     . GLY B 208 ? 0.5684 0.4710 0.5494 0.0380  -0.0549 0.0656  1425 GLY B N     
5360 C  CA    . GLY B 208 ? 0.7694 0.6801 0.7485 0.0352  -0.0594 0.0650  1425 GLY B CA    
5361 C  C     . GLY B 208 ? 0.6505 0.5741 0.6423 0.0341  -0.0595 0.0606  1425 GLY B C     
5362 O  O     . GLY B 208 ? 0.5873 0.5180 0.5792 0.0318  -0.0637 0.0592  1425 GLY B O     
5363 N  N     . GLY B 209 ? 0.5538 0.4808 0.5564 0.0358  -0.0549 0.0584  1426 GLY B N     
5364 C  CA    . GLY B 209 ? 0.4175 0.3563 0.4328 0.0341  -0.0537 0.0549  1426 GLY B CA    
5365 C  C     . GLY B 209 ? 0.5324 0.4818 0.5605 0.0388  -0.0585 0.0554  1426 GLY B C     
5366 O  O     . GLY B 209 ? 0.7239 0.6719 0.7503 0.0434  -0.0640 0.0584  1426 GLY B O     
5367 N  N     . ASP B 210 ? 0.5649 0.5257 0.6065 0.0372  -0.0567 0.0527  1427 ASP B N     
5368 C  CA    . ASP B 210 ? 0.5970 0.5706 0.6541 0.0410  -0.0600 0.0524  1427 ASP B CA    
5369 C  C     . ASP B 210 ? 0.5596 0.5357 0.6256 0.0452  -0.0539 0.0520  1427 ASP B C     
5370 O  O     . ASP B 210 ? 0.5107 0.4853 0.5789 0.0520  -0.0551 0.0534  1427 ASP B O     
5371 C  CB    . ASP B 210 ? 0.6746 0.6599 0.7419 0.0357  -0.0616 0.0495  1427 ASP B CB    
5372 C  CG    . ASP B 210 ? 0.8020 0.7984 0.8785 0.0379  -0.0697 0.0493  1427 ASP B CG    
5373 O  OD1   . ASP B 210 ? 0.9036 0.8964 0.9724 0.0417  -0.0760 0.0517  1427 ASP B OD1   
5374 O  OD2   . ASP B 210 ? 0.8283 0.8374 0.9200 0.0356  -0.0699 0.0471  1427 ASP B OD2   
5375 N  N     . TYR B 211 ? 0.6408 0.6209 0.7118 0.0415  -0.0473 0.0500  1428 TYR B N     
5376 C  CA    . TYR B 211 ? 0.7076 0.6892 0.7835 0.0447  -0.0403 0.0493  1428 TYR B CA    
5377 C  C     . TYR B 211 ? 0.4964 0.4692 0.5619 0.0404  -0.0342 0.0486  1428 TYR B C     
5378 O  O     . TYR B 211 ? 0.6188 0.5867 0.6765 0.0349  -0.0352 0.0484  1428 TYR B O     
5379 C  CB    . TYR B 211 ? 0.7715 0.7693 0.8651 0.0449  -0.0378 0.0482  1428 TYR B CB    
5380 C  CG    . TYR B 211 ? 0.6604 0.6644 0.7592 0.0372  -0.0364 0.0475  1428 TYR B CG    
5381 C  CD1   . TYR B 211 ? 0.6672 0.6699 0.7644 0.0334  -0.0291 0.0474  1428 TYR B CD1   
5382 C  CD2   . TYR B 211 ? 0.5269 0.5375 0.6319 0.0339  -0.0428 0.0470  1428 TYR B CD2   
5383 C  CE1   . TYR B 211 ? 0.4486 0.4553 0.5507 0.0265  -0.0280 0.0472  1428 TYR B CE1   
5384 C  CE2   . TYR B 211 ? 0.4231 0.4380 0.5335 0.0267  -0.0418 0.0459  1428 TYR B CE2   
5385 C  CZ    . TYR B 211 ? 0.4433 0.4556 0.5524 0.0231  -0.0343 0.0463  1428 TYR B CZ    
5386 O  OH    . TYR B 211 ? 0.6877 0.7028 0.8024 0.0161  -0.0333 0.0457  1428 TYR B OH    
5387 N  N     . THR B 212 ? 0.3913 0.3626 0.4567 0.0434  -0.0281 0.0477  1429 THR B N     
5388 C  CA    . THR B 212 ? 0.3880 0.3520 0.4440 0.0401  -0.0225 0.0468  1429 THR B CA    
5389 C  C     . THR B 212 ? 0.5979 0.5701 0.6610 0.0413  -0.0153 0.0457  1429 THR B C     
5390 O  O     . THR B 212 ? 0.6716 0.6486 0.7410 0.0472  -0.0135 0.0447  1429 THR B O     
5391 C  CB    . THR B 212 ? 0.5225 0.4727 0.5659 0.0424  -0.0226 0.0466  1429 THR B CB    
5392 O  OG1   . THR B 212 ? 0.6456 0.5877 0.6795 0.0393  -0.0277 0.0482  1429 THR B OG1   
5393 C  CG2   . THR B 212 ? 0.4381 0.3839 0.4749 0.0406  -0.0165 0.0449  1429 THR B CG2   
5394 N  N     . THR B 213 ? 0.5187 0.4928 0.5810 0.0361  -0.0113 0.0460  1430 THR B N     
5395 C  CA    . THR B 213 ? 0.6324 0.6129 0.6982 0.0367  -0.0039 0.0458  1430 THR B CA    
5396 C  C     . THR B 213 ? 0.6291 0.6001 0.6821 0.0376  -0.0003 0.0443  1430 THR B C     
5397 O  O     . THR B 213 ? 0.6738 0.6343 0.7162 0.0348  -0.0023 0.0441  1430 THR B O     
5398 C  CB    . THR B 213 ? 0.5951 0.5824 0.6672 0.0307  -0.0014 0.0478  1430 THR B CB    
5399 O  OG1   . THR B 213 ? 0.6356 0.6137 0.6987 0.0254  -0.0037 0.0480  1430 THR B OG1   
5400 C  CG2   . THR B 213 ? 0.5296 0.5284 0.6166 0.0296  -0.0042 0.0487  1430 THR B CG2   
5401 N  N     . THR B 214 ? 0.5612 0.5373 0.6157 0.0411  0.0055  0.0432  1431 THR B N     
5402 C  CA    . THR B 214 ? 0.5426 0.5112 0.5856 0.0422  0.0088  0.0411  1431 THR B CA    
5403 C  C     . THR B 214 ? 0.5051 0.4827 0.5499 0.0432  0.0159  0.0412  1431 THR B C     
5404 O  O     . THR B 214 ? 0.6228 0.6126 0.6781 0.0444  0.0189  0.0426  1431 THR B O     
5405 C  CB    . THR B 214 ? 0.5390 0.4999 0.5776 0.0478  0.0068  0.0378  1431 THR B CB    
5406 O  OG1   . THR B 214 ? 0.5917 0.5440 0.6189 0.0473  0.0087  0.0354  1431 THR B OG1   
5407 C  CG2   . THR B 214 ? 0.4014 0.3711 0.4483 0.0546  0.0098  0.0356  1431 THR B CG2   
5408 N  N     . VAL B 215 ? 0.4567 0.4286 0.4907 0.0430  0.0184  0.0397  1432 VAL B N     
5409 C  CA    . VAL B 215 ? 0.5011 0.4799 0.5328 0.0442  0.0249  0.0398  1432 VAL B CA    
5410 C  C     . VAL B 215 ? 0.5869 0.5602 0.6099 0.0491  0.0257  0.0346  1432 VAL B C     
5411 O  O     . VAL B 215 ? 0.6259 0.5891 0.6393 0.0474  0.0236  0.0328  1432 VAL B O     
5412 C  CB    . VAL B 215 ? 0.4970 0.4740 0.5236 0.0387  0.0264  0.0431  1432 VAL B CB    
5413 C  CG1   . VAL B 215 ? 0.5845 0.5632 0.6026 0.0407  0.0313  0.0422  1432 VAL B CG1   
5414 C  CG2   . VAL B 215 ? 0.5214 0.5070 0.5585 0.0351  0.0280  0.0480  1432 VAL B CG2   
5415 N  N     . GLU B 216 ? 0.6542 0.6342 0.6816 0.0551  0.0284  0.0316  1433 GLU B N     
5416 C  CA    . GLU B 216 ? 0.7708 0.7451 0.7915 0.0602  0.0286  0.0255  1433 GLU B CA    
5417 C  C     . GLU B 216 ? 0.8255 0.8066 0.8400 0.0624  0.0345  0.0235  1433 GLU B C     
5418 O  O     . GLU B 216 ? 0.8879 0.8813 0.9063 0.0624  0.0395  0.0266  1433 GLU B O     
5419 C  CB    . GLU B 216 ? 0.6964 0.6726 0.7251 0.0667  0.0274  0.0223  1433 GLU B CB    
5420 C  CG    . GLU B 216 ? 0.7328 0.7040 0.7683 0.0660  0.0213  0.0246  1433 GLU B CG    
5421 C  CD    . GLU B 216 ? 0.8055 0.7603 0.8336 0.0656  0.0160  0.0227  1433 GLU B CD    
5422 O  OE1   . GLU B 216 ? 0.8409 0.7888 0.8663 0.0604  0.0118  0.0261  1433 GLU B OE1   
5423 O  OE2   . GLU B 216 ? 0.8470 0.7959 0.8720 0.0703  0.0161  0.0176  1433 GLU B OE2   
5424 N  N     . ALA B 217 ? 0.7289 0.7023 0.7335 0.0642  0.0337  0.0182  1434 ALA B N     
5425 C  CA    . ALA B 217 ? 0.6945 0.6739 0.6915 0.0669  0.0384  0.0150  1434 ALA B CA    
5426 C  C     . ALA B 217 ? 0.7112 0.6855 0.7050 0.0728  0.0375  0.0066  1434 ALA B C     
5427 O  O     . ALA B 217 ? 0.6090 0.5720 0.6044 0.0731  0.0327  0.0041  1434 ALA B O     
5428 C  CB    . ALA B 217 ? 0.6420 0.6175 0.6292 0.0621  0.0380  0.0170  1434 ALA B CB    
5429 N  N     . TYR B 218 ? 0.7325 0.7150 0.7217 0.0775  0.0421  0.0021  1435 TYR B N     
5430 C  CA    . TYR B 218 ? 0.6531 0.6329 0.6403 0.0841  0.0420  -0.0070 1435 TYR B CA    
5431 C  C     . TYR B 218 ? 0.6662 0.6445 0.6410 0.0846  0.0426  -0.0126 1435 TYR B C     
5432 O  O     . TYR B 218 ? 0.8106 0.7991 0.7795 0.0842  0.0467  -0.0103 1435 TYR B O     
5433 C  CB    . TYR B 218 ? 0.7006 0.6945 0.6948 0.0908  0.0472  -0.0088 1435 TYR B CB    
5434 C  CG    . TYR B 218 ? 0.7230 0.7146 0.7169 0.0986  0.0472  -0.0188 1435 TYR B CG    
5435 C  CD1   . TYR B 218 ? 0.6442 0.6242 0.6445 0.1011  0.0423  -0.0221 1435 TYR B CD1   
5436 C  CD2   . TYR B 218 ? 0.7106 0.7113 0.6974 0.1037  0.0519  -0.0251 1435 TYR B CD2   
5437 C  CE1   . TYR B 218 ? 0.7548 0.7314 0.7556 0.1085  0.0421  -0.0316 1435 TYR B CE1   
5438 C  CE2   . TYR B 218 ? 0.7461 0.7444 0.7328 0.1111  0.0517  -0.0355 1435 TYR B CE2   
5439 C  CZ    . TYR B 218 ? 0.8205 0.8063 0.8148 0.1135  0.0468  -0.0388 1435 TYR B CZ    
5440 O  OH    . TYR B 218 ? 0.8305 0.8125 0.8254 0.1212  0.0463  -0.0493 1435 TYR B OH    
5441 N  N     . ILE B 219 ? 0.6307 0.5971 0.6019 0.0856  0.0385  -0.0199 1436 ILE B N     
5442 C  CA    . ILE B 219 ? 0.6904 0.6556 0.6510 0.0866  0.0383  -0.0271 1436 ILE B CA    
5443 C  C     . ILE B 219 ? 0.8221 0.7909 0.7829 0.0948  0.0404  -0.0367 1436 ILE B C     
5444 O  O     . ILE B 219 ? 0.9135 0.8725 0.8798 0.0977  0.0374  -0.0417 1436 ILE B O     
5445 C  CB    . ILE B 219 ? 0.6505 0.6002 0.6077 0.0816  0.0324  -0.0295 1436 ILE B CB    
5446 C  CG1   . ILE B 219 ? 0.7453 0.6924 0.7015 0.0740  0.0306  -0.0211 1436 ILE B CG1   
5447 C  CG2   . ILE B 219 ? 0.5420 0.4916 0.4898 0.0829  0.0318  -0.0380 1436 ILE B CG2   
5448 C  CD1   . ILE B 219 ? 0.7088 0.6488 0.6730 0.0709  0.0280  -0.0152 1436 ILE B CD1   
5449 N  N     . SER B 220 ? 0.8508 0.8335 0.8052 0.0989  0.0455  -0.0392 1437 SER B N     
5450 C  CA    . SER B 220 ? 0.9907 0.9782 0.9444 0.1072  0.0479  -0.0493 1437 SER B CA    
5451 C  C     . SER B 220 ? 1.1569 1.1323 1.1049 0.1081  0.0432  -0.0601 1437 SER B C     
5452 O  O     . SER B 220 ? 1.3050 1.2746 1.2570 0.1135  0.0419  -0.0687 1437 SER B O     
5453 C  CB    . SER B 220 ? 0.9357 0.9419 0.8823 0.1113  0.0548  -0.0495 1437 SER B CB    
5454 O  OG    . SER B 220 ? 0.9500 0.9671 0.9004 0.1085  0.0592  -0.0383 1437 SER B OG    
5455 N  N     . ALA B 221 ? 1.0811 1.0527 1.0207 0.1028  0.0404  -0.0599 1438 ALA B N     
5456 C  CA    . ALA B 221 ? 0.9090 0.8688 0.8444 0.1019  0.0353  -0.0695 1438 ALA B CA    
5457 C  C     . ALA B 221 ? 0.9201 0.8625 0.8648 0.1008  0.0307  -0.0716 1438 ALA B C     
5458 O  O     . ALA B 221 ? 0.9334 0.8687 0.8799 0.1055  0.0290  -0.0815 1438 ALA B O     
5459 C  CB    . ALA B 221 ? 0.8467 0.8048 0.7748 0.0948  0.0325  -0.0662 1438 ALA B CB    
5460 N  N     . SER B 222 ? 0.8760 0.8114 0.8265 0.0950  0.0286  -0.0620 1439 SER B N     
5461 C  CA    . SER B 222 ? 0.7222 0.6413 0.6807 0.0938  0.0243  -0.0619 1439 SER B CA    
5462 C  C     . SER B 222 ? 0.7053 0.6257 0.6728 0.1006  0.0259  -0.0621 1439 SER B C     
5463 O  O     . SER B 222 ? 0.8091 0.7157 0.7829 0.1015  0.0222  -0.0635 1439 SER B O     
5464 C  CB    . SER B 222 ? 0.7988 0.7118 0.7594 0.0857  0.0218  -0.0513 1439 SER B CB    
5465 O  OG    . SER B 222 ? 0.9226 0.8287 0.8777 0.0792  0.0187  -0.0523 1439 SER B OG    
5466 N  N     . GLY B 223 ? 0.7445 0.6813 0.7131 0.1055  0.0313  -0.0606 1440 GLY B N     
5467 C  CA    . GLY B 223 ? 0.8076 0.7476 0.7865 0.1117  0.0328  -0.0598 1440 GLY B CA    
5468 C  C     . GLY B 223 ? 0.8450 0.7782 0.8322 0.1076  0.0297  -0.0501 1440 GLY B C     
5469 O  O     . GLY B 223 ? 0.9477 0.8779 0.9442 0.1123  0.0285  -0.0500 1440 GLY B O     
5470 N  N     . ARG B 224 ? 0.8380 0.7687 0.8219 0.0994  0.0281  -0.0422 1441 ARG B N     
5471 C  CA    . ARG B 224 ? 0.8620 0.7843 0.8517 0.0948  0.0241  -0.0340 1441 ARG B CA    
5472 C  C     . ARG B 224 ? 0.9527 0.8853 0.9423 0.0895  0.0263  -0.0246 1441 ARG B C     
5473 O  O     . ARG B 224 ? 1.0776 1.0184 1.0605 0.0871  0.0293  -0.0238 1441 ARG B O     
5474 C  CB    . ARG B 224 ? 0.8393 0.7437 0.8251 0.0893  0.0188  -0.0347 1441 ARG B CB    
5475 C  CG    . ARG B 224 ? 0.8928 0.7844 0.8797 0.0937  0.0161  -0.0436 1441 ARG B CG    
5476 C  CD    . ARG B 224 ? 1.0140 0.8883 0.9979 0.0872  0.0113  -0.0434 1441 ARG B CD    
5477 N  NE    . ARG B 224 ? 1.1437 1.0056 1.1339 0.0866  0.0073  -0.0379 1441 ARG B NE    
5478 C  CZ    . ARG B 224 ? 1.2905 1.1387 1.2850 0.0907  0.0044  -0.0421 1441 ARG B CZ    
5479 N  NH1   . ARG B 224 ? 1.2486 1.0939 1.2425 0.0955  0.0049  -0.0528 1441 ARG B NH1   
5480 N  NH2   . ARG B 224 ? 1.4089 1.2462 1.4083 0.0903  0.0006  -0.0356 1441 ARG B NH2   
5481 N  N     . ALA B 225 ? 0.8915 0.8236 0.8887 0.0880  0.0243  -0.0176 1442 ALA B N     
5482 C  CA    . ALA B 225 ? 0.7978 0.7381 0.7961 0.0825  0.0256  -0.0092 1442 ALA B CA    
5483 C  C     . ALA B 225 ? 0.7395 0.6681 0.7342 0.0751  0.0209  -0.0045 1442 ALA B C     
5484 O  O     . ALA B 225 ? 0.7789 0.6938 0.7720 0.0742  0.0168  -0.0064 1442 ALA B O     
5485 C  CB    . ALA B 225 ? 0.8073 0.7573 0.8170 0.0854  0.0266  -0.0049 1442 ALA B CB    
5486 N  N     . ILE B 226 ? 0.7426 0.6767 0.7361 0.0697  0.0218  0.0017  1443 ILE B N     
5487 C  CA    . ILE B 226 ? 0.7785 0.7038 0.7681 0.0627  0.0181  0.0058  1443 ILE B CA    
5488 C  C     . ILE B 226 ? 0.7143 0.6468 0.7083 0.0589  0.0185  0.0130  1443 ILE B C     
5489 O  O     . ILE B 226 ? 0.4559 0.4002 0.4525 0.0594  0.0225  0.0152  1443 ILE B O     
5490 C  CB    . ILE B 226 ? 0.5874 0.5094 0.5672 0.0594  0.0187  0.0027  1443 ILE B CB    
5491 C  CG1   . ILE B 226 ? 0.5077 0.4215 0.4838 0.0524  0.0153  0.0064  1443 ILE B CG1   
5492 C  CG2   . ILE B 226 ? 0.5291 0.4636 0.5057 0.0602  0.0235  0.0030  1443 ILE B CG2   
5493 C  CD1   . ILE B 226 ? 0.5123 0.4239 0.4802 0.0494  0.0155  0.0031  1443 ILE B CD1   
5494 N  N     . GLN B 227 ? 0.7647 0.6897 0.7594 0.0549  0.0141  0.0168  1444 GLN B N     
5495 C  CA    . GLN B 227 ? 0.7068 0.6368 0.7052 0.0507  0.0133  0.0227  1444 GLN B CA    
5496 C  C     . GLN B 227 ? 0.6421 0.5729 0.6339 0.0457  0.0149  0.0241  1444 GLN B C     
5497 O  O     . GLN B 227 ? 0.5245 0.4474 0.5089 0.0431  0.0135  0.0222  1444 GLN B O     
5498 C  CB    . GLN B 227 ? 0.7077 0.6293 0.7074 0.0486  0.0079  0.0254  1444 GLN B CB    
5499 C  CG    . GLN B 227 ? 0.6594 0.5822 0.6588 0.0430  0.0061  0.0299  1444 GLN B CG    
5500 C  CD    . GLN B 227 ? 0.7798 0.7018 0.7848 0.0432  0.0016  0.0330  1444 GLN B CD    
5501 O  OE1   . GLN B 227 ? 0.7701 0.7014 0.7834 0.0435  0.0017  0.0352  1444 GLN B OE1   
5502 N  NE2   . GLN B 227 ? 0.9278 0.8392 0.9286 0.0429  -0.0024 0.0334  1444 GLN B NE2   
5503 N  N     . GLY B 228 ? 0.5817 0.5223 0.5769 0.0444  0.0180  0.0275  1445 GLY B N     
5504 C  CA    . GLY B 228 ? 0.4749 0.4168 0.4649 0.0405  0.0196  0.0294  1445 GLY B CA    
5505 C  C     . GLY B 228 ? 0.4825 0.4207 0.4732 0.0350  0.0165  0.0331  1445 GLY B C     
5506 O  O     . GLY B 228 ? 0.4889 0.4239 0.4735 0.0318  0.0163  0.0333  1445 GLY B O     
5507 N  N     . ALA B 229 ? 0.3788 0.3177 0.3766 0.0341  0.0138  0.0354  1446 ALA B N     
5508 C  CA    . ALA B 229 ? 0.3754 0.3112 0.3739 0.0292  0.0103  0.0380  1446 ALA B CA    
5509 C  C     . ALA B 229 ? 0.4516 0.3895 0.4581 0.0301  0.0069  0.0394  1446 ALA B C     
5510 O  O     . ALA B 229 ? 0.5581 0.5010 0.5707 0.0343  0.0079  0.0389  1446 ALA B O     
5511 C  CB    . ALA B 229 ? 0.4416 0.3820 0.4420 0.0258  0.0123  0.0409  1446 ALA B CB    
5512 N  N     . THR B 230 ? 0.5052 0.4401 0.5117 0.0263  0.0029  0.0409  1447 THR B N     
5513 C  CA    . THR B 230 ? 0.6796 0.6176 0.6937 0.0269  -0.0011 0.0423  1447 THR B CA    
5514 C  C     . THR B 230 ? 0.7323 0.6731 0.7501 0.0221  -0.0033 0.0440  1447 THR B C     
5515 O  O     . THR B 230 ? 0.8573 0.7933 0.8690 0.0184  -0.0039 0.0437  1447 THR B O     
5516 C  CB    . THR B 230 ? 0.6254 0.5557 0.6350 0.0279  -0.0061 0.0421  1447 THR B CB    
5517 O  OG1   . THR B 230 ? 0.5364 0.4576 0.5353 0.0248  -0.0069 0.0414  1447 THR B OG1   
5518 C  CG2   . THR B 230 ? 0.7081 0.6373 0.7199 0.0336  -0.0060 0.0410  1447 THR B CG2   
5519 N  N     . SER B 231 ? 0.5680 0.5165 0.5963 0.0226  -0.0051 0.0451  1448 SER B N     
5520 C  CA    . SER B 231 ? 0.5498 0.5013 0.5834 0.0184  -0.0087 0.0459  1448 SER B CA    
5521 C  C     . SER B 231 ? 0.6054 0.5603 0.6446 0.0208  -0.0140 0.0460  1448 SER B C     
5522 O  O     . SER B 231 ? 0.5715 0.5341 0.6199 0.0243  -0.0130 0.0465  1448 SER B O     
5523 C  CB    . SER B 231 ? 0.6720 0.6315 0.7153 0.0158  -0.0051 0.0474  1448 SER B CB    
5524 O  OG    . SER B 231 ? 0.7606 0.7184 0.8050 0.0106  -0.0075 0.0473  1448 SER B OG    
5525 N  N     . HIS B 232 ? 0.7010 0.6505 0.7339 0.0195  -0.0194 0.0456  1449 HIS B N     
5526 C  CA    . HIS B 232 ? 0.6335 0.5859 0.6702 0.0219  -0.0253 0.0462  1449 HIS B CA    
5527 C  C     . HIS B 232 ? 0.5469 0.5057 0.5905 0.0180  -0.0295 0.0455  1449 HIS B C     
5528 O  O     . HIS B 232 ? 0.4503 0.4072 0.4917 0.0132  -0.0289 0.0443  1449 HIS B O     
5529 C  CB    . HIS B 232 ? 0.5573 0.5001 0.5822 0.0234  -0.0292 0.0469  1449 HIS B CB    
5530 C  CG    . HIS B 232 ? 0.5602 0.4937 0.5757 0.0248  -0.0253 0.0468  1449 HIS B CG    
5531 N  ND1   . HIS B 232 ? 0.5533 0.4859 0.5712 0.0297  -0.0229 0.0468  1449 HIS B ND1   
5532 C  CD2   . HIS B 232 ? 0.6526 0.5780 0.6572 0.0218  -0.0235 0.0462  1449 HIS B CD2   
5533 C  CE1   . HIS B 232 ? 0.6567 0.5804 0.6654 0.0295  -0.0201 0.0460  1449 HIS B CE1   
5534 N  NE2   . HIS B 232 ? 0.6589 0.5786 0.6598 0.0246  -0.0203 0.0458  1449 HIS B NE2   
5535 N  N     . HIS B 233 ? 0.5199 0.4866 0.5727 0.0204  -0.0341 0.0459  1450 HIS B N     
5536 C  CA    . HIS B 233 ? 0.5793 0.5515 0.6370 0.0174  -0.0403 0.0447  1450 HIS B CA    
5537 C  C     . HIS B 233 ? 0.4900 0.4575 0.5382 0.0201  -0.0467 0.0454  1450 HIS B C     
5538 O  O     . HIS B 233 ? 0.4840 0.4528 0.5341 0.0255  -0.0488 0.0473  1450 HIS B O     
5539 C  CB    . HIS B 233 ? 0.6772 0.6631 0.7526 0.0179  -0.0415 0.0446  1450 HIS B CB    
5540 C  CG    . HIS B 233 ? 0.8400 0.8321 0.9206 0.0157  -0.0492 0.0428  1450 HIS B CG    
5541 N  ND1   . HIS B 233 ? 0.9120 0.9011 0.9884 0.0101  -0.0519 0.0401  1450 HIS B ND1   
5542 C  CD2   . HIS B 233 ? 0.9235 0.9253 1.0134 0.0185  -0.0552 0.0426  1450 HIS B CD2   
5543 C  CE1   . HIS B 233 ? 0.9494 0.9460 1.0319 0.0094  -0.0593 0.0382  1450 HIS B CE1   
5544 N  NE2   . HIS B 233 ? 0.9291 0.9338 1.0199 0.0143  -0.0616 0.0399  1450 HIS B NE2   
5545 N  N     . LEU B 234 ? 0.4836 0.4455 0.5212 0.0167  -0.0496 0.0442  1451 LEU B N     
5546 C  CA    . LEU B 234 ? 0.4706 0.4275 0.4969 0.0188  -0.0549 0.0456  1451 LEU B CA    
5547 C  C     . LEU B 234 ? 0.5969 0.5627 0.6292 0.0201  -0.0629 0.0452  1451 LEU B C     
5548 O  O     . LEU B 234 ? 0.6279 0.5918 0.6539 0.0239  -0.0678 0.0478  1451 LEU B O     
5549 C  CB    . LEU B 234 ? 0.4048 0.3540 0.4172 0.0148  -0.0544 0.0442  1451 LEU B CB    
5550 C  CG    . LEU B 234 ? 0.5540 0.4955 0.5612 0.0134  -0.0471 0.0442  1451 LEU B CG    
5551 C  CD1   . LEU B 234 ? 0.7053 0.6399 0.6986 0.0104  -0.0471 0.0432  1451 LEU B CD1   
5552 C  CD2   . LEU B 234 ? 0.6032 0.5402 0.6092 0.0181  -0.0443 0.0473  1451 LEU B CD2   
5553 N  N     . GLY B 235 ? 0.5723 0.5479 0.6175 0.0169  -0.0643 0.0422  1452 GLY B N     
5554 C  CA    . GLY B 235 ? 0.4093 0.3946 0.4611 0.0175  -0.0725 0.0408  1452 GLY B CA    
5555 C  C     . GLY B 235 ? 0.6020 0.5833 0.6399 0.0155  -0.0780 0.0391  1452 GLY B C     
5556 O  O     . GLY B 235 ? 0.7327 0.7076 0.7620 0.0113  -0.0753 0.0367  1452 GLY B O     
5557 N  N     . GLN B 236 ? 0.5880 0.5730 0.6225 0.0191  -0.0855 0.0404  1453 GLN B N     
5558 C  CA    . GLN B 236 ? 0.6765 0.6594 0.6970 0.0176  -0.0911 0.0389  1453 GLN B CA    
5559 C  C     . GLN B 236 ? 0.6982 0.6717 0.7016 0.0214  -0.0914 0.0442  1453 GLN B C     
5560 O  O     . GLN B 236 ? 0.6064 0.5794 0.5973 0.0215  -0.0966 0.0444  1453 GLN B O     
5561 C  CB    . GLN B 236 ? 0.7226 0.7177 0.7505 0.0180  -0.1004 0.0359  1453 GLN B CB    
5562 C  CG    . GLN B 236 ? 0.6960 0.6980 0.7354 0.0118  -0.1012 0.0290  1453 GLN B CG    
5563 C  CD    . GLN B 236 ? 0.7343 0.7498 0.7836 0.0120  -0.1108 0.0255  1453 GLN B CD    
5564 O  OE1   . GLN B 236 ? 0.5671 0.5907 0.6256 0.0165  -0.1146 0.0282  1453 GLN B OE1   
5565 N  NE2   . GLN B 236 ? 0.9013 0.9193 0.9489 0.0073  -0.1151 0.0190  1453 GLN B NE2   
5566 N  N     . ASN B 237 ? 0.8425 0.8084 0.8450 0.0243  -0.0858 0.0486  1454 ASN B N     
5567 C  CA    . ASN B 237 ? 0.9198 0.8757 0.9081 0.0277  -0.0859 0.0543  1454 ASN B CA    
5568 C  C     . ASN B 237 ? 0.8712 0.8195 0.8426 0.0236  -0.0837 0.0539  1454 ASN B C     
5569 O  O     . ASN B 237 ? 1.0535 0.9997 1.0117 0.0246  -0.0879 0.0567  1454 ASN B O     
5570 C  CB    . ASN B 237 ? 1.0127 0.9619 1.0054 0.0308  -0.0798 0.0573  1454 ASN B CB    
5571 C  CG    . ASN B 237 ? 1.1130 1.0705 1.1220 0.0359  -0.0819 0.0578  1454 ASN B CG    
5572 O  OD1   . ASN B 237 ? 1.1908 1.1587 1.2138 0.0343  -0.0816 0.0540  1454 ASN B OD1   
5573 N  ND2   . ASN B 237 ? 1.1575 1.1103 1.1652 0.0422  -0.0838 0.0625  1454 ASN B ND2   
5574 N  N     . PHE B 238 ? 0.6955 0.6401 0.6669 0.0193  -0.0769 0.0507  1455 PHE B N     
5575 C  CA    . PHE B 238 ? 0.5929 0.5309 0.5494 0.0158  -0.0740 0.0501  1455 PHE B CA    
5576 C  C     . PHE B 238 ? 0.5792 0.5233 0.5305 0.0130  -0.0789 0.0455  1455 PHE B C     
5577 O  O     . PHE B 238 ? 0.6114 0.5531 0.5478 0.0124  -0.0803 0.0467  1455 PHE B O     
5578 C  CB    . PHE B 238 ? 0.5371 0.4702 0.4958 0.0125  -0.0659 0.0477  1455 PHE B CB    
5579 C  CG    . PHE B 238 ? 0.6233 0.5481 0.5812 0.0146  -0.0607 0.0518  1455 PHE B CG    
5580 C  CD1   . PHE B 238 ? 0.7000 0.6265 0.6702 0.0175  -0.0589 0.0525  1455 PHE B CD1   
5581 C  CD2   . PHE B 238 ? 0.6103 0.5264 0.5555 0.0135  -0.0575 0.0546  1455 PHE B CD2   
5582 C  CE1   . PHE B 238 ? 0.6398 0.5586 0.6091 0.0197  -0.0544 0.0552  1455 PHE B CE1   
5583 C  CE2   . PHE B 238 ? 0.5019 0.4101 0.4472 0.0150  -0.0531 0.0575  1455 PHE B CE2   
5584 C  CZ    . PHE B 238 ? 0.5249 0.4343 0.4820 0.0183  -0.0518 0.0574  1455 PHE B CZ    
5585 N  N     . SER B 239 ? 0.5354 0.4880 0.4990 0.0114  -0.0818 0.0402  1456 SER B N     
5586 C  CA    . SER B 239 ? 0.5797 0.5382 0.5394 0.0088  -0.0871 0.0345  1456 SER B CA    
5587 C  C     . SER B 239 ? 0.6284 0.5906 0.5778 0.0120  -0.0947 0.0372  1456 SER B C     
5588 O  O     . SER B 239 ? 0.7101 0.6748 0.6488 0.0105  -0.0982 0.0338  1456 SER B O     
5589 C  CB    . SER B 239 ? 0.6647 0.6315 0.6414 0.0062  -0.0895 0.0285  1456 SER B CB    
5590 O  OG    . SER B 239 ? 0.6984 0.6719 0.6903 0.0087  -0.0918 0.0306  1456 SER B OG    
5591 N  N     . ARG B 240 ? 0.6210 0.5834 0.5729 0.0169  -0.0973 0.0435  1457 ARG B N     
5592 C  CA    . ARG B 240 ? 0.7026 0.6663 0.6426 0.0206  -0.1040 0.0480  1457 ARG B CA    
5593 C  C     . ARG B 240 ? 0.6819 0.6351 0.6038 0.0206  -0.0997 0.0536  1457 ARG B C     
5594 O  O     . ARG B 240 ? 0.7630 0.7170 0.6695 0.0206  -0.1030 0.0549  1457 ARG B O     
5595 C  CB    . ARG B 240 ? 0.8093 0.7766 0.7593 0.0264  -0.1086 0.0528  1457 ARG B CB    
5596 C  CG    . ARG B 240 ? 0.9829 0.9638 0.9433 0.0275  -0.1173 0.0485  1457 ARG B CG    
5597 C  CD    . ARG B 240 ? 1.0556 1.0427 1.0365 0.0303  -0.1176 0.0487  1457 ARG B CD    
5598 N  NE    . ARG B 240 ? 1.1122 1.1134 1.1056 0.0292  -0.1249 0.0429  1457 ARG B NE    
5599 C  CZ    . ARG B 240 ? 1.0909 1.1011 1.1046 0.0298  -0.1254 0.0409  1457 ARG B CZ    
5600 N  NH1   . ARG B 240 ? 1.1450 1.1516 1.1678 0.0319  -0.1189 0.0442  1457 ARG B NH1   
5601 N  NH2   . ARG B 240 ? 0.9725 0.9959 0.9977 0.0280  -0.1322 0.0353  1457 ARG B NH2   
5602 N  N     . MET B 241 ? 0.5509 0.4946 0.4742 0.0203  -0.0922 0.0570  1458 MET B N     
5603 C  CA    . MET B 241 ? 0.6375 0.5713 0.5454 0.0193  -0.0877 0.0622  1458 MET B CA    
5604 C  C     . MET B 241 ? 0.6854 0.6206 0.5815 0.0147  -0.0855 0.0577  1458 MET B C     
5605 O  O     . MET B 241 ? 0.6345 0.5693 0.5151 0.0147  -0.0872 0.0607  1458 MET B O     
5606 C  CB    . MET B 241 ? 0.8537 0.7782 0.7671 0.0189  -0.0800 0.0644  1458 MET B CB    
5607 C  CG    . MET B 241 ? 1.0661 0.9842 0.9825 0.0239  -0.0809 0.0715  1458 MET B CG    
5608 S  SD    . MET B 241 ? 1.1840 1.0883 1.0978 0.0224  -0.0719 0.0748  1458 MET B SD    
5609 C  CE    . MET B 241 ? 1.0984 0.9955 0.9917 0.0193  -0.0704 0.0804  1458 MET B CE    
5610 N  N     . PHE B 242 ? 0.8276 0.7650 0.7311 0.0110  -0.0819 0.0503  1459 PHE B N     
5611 C  CA    . PHE B 242 ? 0.7822 0.7197 0.6763 0.0070  -0.0784 0.0453  1459 PHE B CA    
5612 C  C     . PHE B 242 ? 0.8331 0.7798 0.7273 0.0057  -0.0839 0.0375  1459 PHE B C     
5613 O  O     . PHE B 242 ? 0.8152 0.7626 0.7021 0.0030  -0.0816 0.0322  1459 PHE B O     
5614 C  CB    . PHE B 242 ? 0.6641 0.5968 0.5653 0.0042  -0.0707 0.0425  1459 PHE B CB    
5615 C  CG    . PHE B 242 ? 0.6754 0.5992 0.5737 0.0046  -0.0650 0.0489  1459 PHE B CG    
5616 C  CD1   . PHE B 242 ? 0.5737 0.4932 0.4588 0.0026  -0.0608 0.0513  1459 PHE B CD1   
5617 C  CD2   . PHE B 242 ? 0.6656 0.5858 0.5746 0.0071  -0.0639 0.0522  1459 PHE B CD2   
5618 C  CE1   . PHE B 242 ? 0.5119 0.4231 0.3952 0.0024  -0.0560 0.0567  1459 PHE B CE1   
5619 C  CE2   . PHE B 242 ? 0.4630 0.3745 0.3693 0.0074  -0.0590 0.0572  1459 PHE B CE2   
5620 C  CZ    . PHE B 242 ? 0.4689 0.3757 0.3627 0.0048  -0.0553 0.0594  1459 PHE B CZ    
5621 N  N     . ASP B 243 ? 0.8139 0.7676 0.7158 0.0080  -0.0914 0.0364  1460 ASP B N     
5622 C  CA    . ASP B 243 ? 0.8335 0.7963 0.7334 0.0075  -0.0987 0.0299  1460 ASP B CA    
5623 C  C     . ASP B 243 ? 0.8729 0.8375 0.7819 0.0033  -0.0967 0.0202  1460 ASP B C     
5624 O  O     . ASP B 243 ? 0.5601 0.5287 0.4625 0.0016  -0.0992 0.0130  1460 ASP B O     
5625 C  CB    . ASP B 243 ? 1.0142 0.9780 0.8932 0.0081  -0.1004 0.0315  1460 ASP B CB    
5626 C  CG    . ASP B 243 ? 1.2962 1.2582 1.1665 0.0124  -0.1037 0.0417  1460 ASP B CG    
5627 O  OD1   . ASP B 243 ? 1.4223 1.3888 1.3006 0.0159  -0.1103 0.0440  1460 ASP B OD1   
5628 O  OD2   . ASP B 243 ? 1.4344 1.3904 1.2899 0.0121  -0.0991 0.0474  1460 ASP B OD2   
5629 N  N     . ILE B 244 ? 1.0293 0.9911 0.9540 0.0021  -0.0925 0.0199  1461 ILE B N     
5630 C  CA    . ILE B 244 ? 1.0031 0.9654 0.9395 -0.0016 -0.0906 0.0125  1461 ILE B CA    
5631 C  C     . ILE B 244 ? 0.8588 0.8300 0.8078 -0.0020 -0.0983 0.0080  1461 ILE B C     
5632 O  O     . ILE B 244 ? 0.7837 0.7579 0.7472 -0.0012 -0.0991 0.0107  1461 ILE B O     
5633 C  CB    . ILE B 244 ? 0.9578 0.9137 0.9045 -0.0025 -0.0828 0.0155  1461 ILE B CB    
5634 C  CG1   . ILE B 244 ? 0.8550 0.8032 0.7901 -0.0011 -0.0766 0.0218  1461 ILE B CG1   
5635 C  CG2   . ILE B 244 ? 0.9284 0.8826 0.8841 -0.0064 -0.0796 0.0086  1461 ILE B CG2   
5636 C  CD1   . ILE B 244 ? 0.8006 0.7430 0.7439 -0.0014 -0.0695 0.0247  1461 ILE B CD1   
5637 N  N     . VAL B 245 ? 0.9113 0.8878 0.8550 -0.0032 -0.1042 0.0009  1462 VAL B N     
5638 C  CA    . VAL B 245 ? 0.8794 0.8657 0.8336 -0.0036 -0.1129 -0.0039 1462 VAL B CA    
5639 C  C     . VAL B 245 ? 0.8439 0.8311 0.8018 -0.0078 -0.1147 -0.0147 1462 VAL B C     
5640 O  O     . VAL B 245 ? 0.8223 0.8035 0.7719 -0.0093 -0.1101 -0.0183 1462 VAL B O     
5641 C  CB    . VAL B 245 ? 0.7651 0.7584 0.7075 0.0002  -0.1210 -0.0016 1462 VAL B CB    
5642 C  CG1   . VAL B 245 ? 0.7957 0.7884 0.7396 0.0046  -0.1207 0.0085  1462 VAL B CG1   
5643 C  CG2   . VAL B 245 ? 0.6866 0.6772 0.6069 0.0010  -0.1199 -0.0022 1462 VAL B CG2   
5644 N  N     . TYR B 246 ? 0.9333 0.9284 0.9052 -0.0097 -0.1216 -0.0202 1463 TYR B N     
5645 C  CA    . TYR B 246 ? 0.8853 0.8820 0.8617 -0.0137 -0.1253 -0.0314 1463 TYR B CA    
5646 C  C     . TYR B 246 ? 0.8041 0.8128 0.7890 -0.0139 -0.1360 -0.0358 1463 TYR B C     
5647 O  O     . TYR B 246 ? 0.5556 0.5708 0.5487 -0.0117 -0.1389 -0.0301 1463 TYR B O     
5648 C  CB    . TYR B 246 ? 0.7881 0.7781 0.7806 -0.0181 -0.1195 -0.0338 1463 TYR B CB    
5649 C  CG    . TYR B 246 ? 0.7389 0.7334 0.7518 -0.0195 -0.1199 -0.0298 1463 TYR B CG    
5650 C  CD1   . TYR B 246 ? 0.6785 0.6788 0.7091 -0.0238 -0.1251 -0.0362 1463 TYR B CD1   
5651 C  CD2   . TYR B 246 ? 0.8164 0.8103 0.8312 -0.0165 -0.1152 -0.0199 1463 TYR B CD2   
5652 C  CE1   . TYR B 246 ? 0.7212 0.7273 0.7710 -0.0252 -0.1250 -0.0323 1463 TYR B CE1   
5653 C  CE2   . TYR B 246 ? 0.8022 0.8017 0.8353 -0.0173 -0.1152 -0.0165 1463 TYR B CE2   
5654 C  CZ    . TYR B 246 ? 0.7390 0.7451 0.7897 -0.0217 -0.1199 -0.0224 1463 TYR B CZ    
5655 O  OH    . TYR B 246 ? 0.7771 0.7901 0.8468 -0.0227 -0.1192 -0.0186 1463 TYR B OH    
5656 N  N     . GLU B 247 ? 0.8510 0.8632 0.8345 -0.0162 -0.1420 -0.0467 1464 GLU B N     
5657 C  CA    . GLU B 247 ? 0.7341 0.7583 0.7259 -0.0169 -0.1529 -0.0525 1464 GLU B CA    
5658 C  C     . GLU B 247 ? 0.7832 0.8089 0.8010 -0.0225 -0.1535 -0.0564 1464 GLU B C     
5659 O  O     . GLU B 247 ? 0.7773 0.7942 0.8027 -0.0266 -0.1479 -0.0598 1464 GLU B O     
5660 C  CB    . GLU B 247 ? 0.7403 0.7683 0.7181 -0.0168 -0.1597 -0.0631 1464 GLU B CB    
5661 N  N     . HIS B 248 ? 0.7876 0.8247 0.8194 -0.0224 -0.1599 -0.0552 1465 HIS B N     
5662 C  CA    . HIS B 248 ? 0.9019 0.9417 0.9594 -0.0282 -0.1601 -0.0582 1465 HIS B CA    
5663 C  C     . HIS B 248 ? 1.0504 1.0887 1.1131 -0.0337 -0.1647 -0.0713 1465 HIS B C     
5664 O  O     . HIS B 248 ? 1.1231 1.1671 1.1754 -0.0326 -0.1732 -0.0795 1465 HIS B O     
5665 C  CB    . HIS B 248 ? 0.9415 0.9960 1.0134 -0.0270 -0.1671 -0.0558 1465 HIS B CB    
5666 C  CG    . HIS B 248 ? 1.0014 1.0581 1.0984 -0.0312 -0.1627 -0.0525 1465 HIS B CG    
5667 N  ND1   . HIS B 248 ? 1.0382 1.0992 1.1562 -0.0383 -0.1660 -0.0600 1465 HIS B ND1   
5668 C  CD2   . HIS B 248 ? 1.0214 1.0768 1.1259 -0.0294 -0.1550 -0.0425 1465 HIS B CD2   
5669 C  CE1   . HIS B 248 ? 1.0291 1.0918 1.1663 -0.0409 -0.1601 -0.0540 1465 HIS B CE1   
5670 N  NE2   . HIS B 248 ? 1.0081 1.0679 1.1372 -0.0353 -0.1534 -0.0437 1465 HIS B NE2   
5671 N  N     . PRO B 249 ? 0.9594 0.9901 1.0378 -0.0395 -0.1596 -0.0736 1466 PRO B N     
5672 C  CA    . PRO B 249 ? 0.9719 0.9993 1.0562 -0.0448 -0.1640 -0.0863 1466 PRO B CA    
5673 C  C     . PRO B 249 ? 1.1497 1.1907 1.2450 -0.0473 -0.1761 -0.0951 1466 PRO B C     
5674 O  O     . PRO B 249 ? 1.2374 1.2807 1.3232 -0.0472 -0.1836 -0.1060 1466 PRO B O     
5675 C  CB    . PRO B 249 ? 0.9737 0.9914 1.0767 -0.0505 -0.1561 -0.0838 1466 PRO B CB    
5676 C  CG    . PRO B 249 ? 0.8863 0.9002 0.9859 -0.0470 -0.1464 -0.0704 1466 PRO B CG    
5677 C  CD    . PRO B 249 ? 0.8668 0.8918 0.9586 -0.0413 -0.1500 -0.0646 1466 PRO B CD    
5678 N  N     . GLU B 250 ? 1.1907 1.2420 1.3058 -0.0494 -0.1782 -0.0909 1467 GLU B N     
5679 C  CA    . GLU B 250 ? 1.1372 1.2041 1.2642 -0.0513 -0.1900 -0.0978 1467 GLU B CA    
5680 C  C     . GLU B 250 ? 1.1601 1.2389 1.2779 -0.0439 -0.1937 -0.0901 1467 GLU B C     
5681 O  O     . GLU B 250 ? 1.1484 1.2241 1.2620 -0.0398 -0.1861 -0.0783 1467 GLU B O     
5682 C  CB    . GLU B 250 ? 1.0605 1.1320 1.2184 -0.0591 -0.1899 -0.0988 1467 GLU B CB    
5683 N  N     . THR B 251 ? 1.1717 1.2633 1.2853 -0.0420 -0.2056 -0.0968 1468 THR B N     
5684 C  CA    . THR B 251 ? 1.1757 1.2786 1.2791 -0.0344 -0.2107 -0.0899 1468 THR B CA    
5685 C  C     . THR B 251 ? 1.1188 1.2114 1.1959 -0.0276 -0.2036 -0.0808 1468 THR B C     
5686 O  O     . THR B 251 ? 0.9235 1.0164 0.9983 -0.0226 -0.1993 -0.0693 1468 THR B O     
5687 C  CB    . THR B 251 ? 1.2211 1.3346 1.3467 -0.0342 -0.2101 -0.0822 1468 THR B CB    
5688 N  N     . LYS B 252 ? 1.2799 1.3641 1.3376 -0.0274 -0.2029 -0.0869 1469 LYS B N     
5689 C  CA    . LYS B 252 ? 1.2883 1.3613 1.3222 -0.0227 -0.1948 -0.0798 1469 LYS B CA    
5690 C  C     . LYS B 252 ? 1.2387 1.3172 1.2591 -0.0151 -0.1967 -0.0691 1469 LYS B C     
5691 O  O     . LYS B 252 ? 1.2301 1.3198 1.2422 -0.0116 -0.2068 -0.0714 1469 LYS B O     
5692 C  CB    . LYS B 252 ? 1.2828 1.3509 1.2977 -0.0229 -0.1965 -0.0897 1469 LYS B CB    
5693 C  CG    . LYS B 252 ? 1.2616 1.3156 1.2594 -0.0211 -0.1854 -0.0846 1469 LYS B CG    
5694 C  CD    . LYS B 252 ? 1.2554 1.3049 1.2385 -0.0220 -0.1862 -0.0960 1469 LYS B CD    
5695 C  CE    . LYS B 252 ? 1.0942 1.1285 1.0765 -0.0242 -0.1750 -0.0960 1469 LYS B CE    
5696 N  NZ    . LYS B 252 ? 0.9558 0.9831 0.9626 -0.0298 -0.1704 -0.0961 1469 LYS B NZ    
5697 N  N     . GLU B 253 ? 1.1064 1.1766 1.1251 -0.0127 -0.1871 -0.0576 1470 GLU B N     
5698 C  CA    . GLU B 253 ? 1.0026 1.0747 1.0113 -0.0058 -0.1869 -0.0460 1470 GLU B CA    
5699 C  C     . GLU B 253 ? 0.9990 1.0567 1.0017 -0.0051 -0.1742 -0.0372 1470 GLU B C     
5700 O  O     . GLU B 253 ? 0.9437 0.9939 0.9579 -0.0097 -0.1667 -0.0386 1470 GLU B O     
5701 C  CB    . GLU B 253 ? 0.9288 1.0132 0.9570 -0.0040 -0.1924 -0.0423 1470 GLU B CB    
5702 N  N     . LYS B 254 ? 0.9724 1.0260 0.9565 0.0005  -0.1720 -0.0282 1471 LYS B N     
5703 C  CA    . LYS B 254 ? 0.9167 0.9567 0.8920 0.0012  -0.1607 -0.0207 1471 LYS B CA    
5704 C  C     . LYS B 254 ? 0.8960 0.9335 0.8892 0.0012  -0.1546 -0.0140 1471 LYS B C     
5705 O  O     . LYS B 254 ? 0.8518 0.8943 0.8498 0.0057  -0.1572 -0.0072 1471 LYS B O     
5706 C  CB    . LYS B 254 ? 0.9755 1.0125 0.9273 0.0069  -0.1609 -0.0127 1471 LYS B CB    
5707 C  CG    . LYS B 254 ? 0.9126 0.9361 0.8547 0.0077  -0.1497 -0.0044 1471 LYS B CG    
5708 C  CD    . LYS B 254 ? 0.7995 0.8205 0.7249 0.0135  -0.1503 0.0063  1471 LYS B CD    
5709 C  CE    . LYS B 254 ? 0.8151 0.8371 0.7167 0.0144  -0.1531 0.0048  1471 LYS B CE    
5710 N  NZ    . LYS B 254 ? 0.9541 0.9652 0.8391 0.0156  -0.1448 0.0133  1471 LYS B NZ    
5711 N  N     . GLU B 255 ? 0.8891 0.9188 0.8914 -0.0033 -0.1463 -0.0157 1472 GLU B N     
5712 C  CA    . GLU B 255 ? 0.9147 0.9419 0.9328 -0.0036 -0.1394 -0.0099 1472 GLU B CA    
5713 C  C     . GLU B 255 ? 0.9511 0.9650 0.9583 -0.0026 -0.1290 -0.0035 1472 GLU B C     
5714 O  O     . GLU B 255 ? 1.0006 1.0066 0.9970 -0.0049 -0.1249 -0.0067 1472 GLU B O     
5715 C  CB    . GLU B 255 ? 0.8400 0.8697 0.8789 -0.0099 -0.1384 -0.0162 1472 GLU B CB    
5716 C  CG    . GLU B 255 ? 0.9273 0.9708 0.9798 -0.0116 -0.1486 -0.0226 1472 GLU B CG    
5717 C  CD    . GLU B 255 ? 1.0745 1.1280 1.1467 -0.0102 -0.1495 -0.0179 1472 GLU B CD    
5718 O  OE1   . GLU B 255 ? 1.1520 1.2053 1.2419 -0.0145 -0.1441 -0.0179 1472 GLU B OE1   
5719 O  OE2   . GLU B 255 ? 1.1237 1.1855 1.1936 -0.0046 -0.1557 -0.0142 1472 GLU B OE2   
5720 N  N     . TYR B 256 ? 0.8681 0.8803 0.8792 0.0010  -0.1249 0.0048  1473 TYR B N     
5721 C  CA    . TYR B 256 ? 0.8051 0.8055 0.8081 0.0020  -0.1154 0.0106  1473 TYR B CA    
5722 C  C     . TYR B 256 ? 0.7943 0.7919 0.8130 -0.0014 -0.1080 0.0103  1473 TYR B C     
5723 O  O     . TYR B 256 ? 0.8364 0.8416 0.8731 -0.0020 -0.1090 0.0103  1473 TYR B O     
5724 C  CB    . TYR B 256 ? 0.8634 0.8620 0.8605 0.0082  -0.1152 0.0195  1473 TYR B CB    
5725 C  CG    . TYR B 256 ? 0.9110 0.9109 0.8908 0.0120  -0.1218 0.0221  1473 TYR B CG    
5726 C  CD1   . TYR B 256 ? 0.9181 0.9082 0.8787 0.0135  -0.1180 0.0271  1473 TYR B CD1   
5727 C  CD2   . TYR B 256 ? 0.9019 0.9131 0.8846 0.0140  -0.1320 0.0199  1473 TYR B CD2   
5728 C  CE1   . TYR B 256 ? 0.9781 0.9695 0.9223 0.0169  -0.1237 0.0304  1473 TYR B CE1   
5729 C  CE2   . TYR B 256 ? 0.8515 0.8643 0.8175 0.0179  -0.1383 0.0228  1473 TYR B CE2   
5730 C  CZ    . TYR B 256 ? 0.9689 0.9716 0.9154 0.0193  -0.1339 0.0284  1473 TYR B CZ    
5731 O  OH    . TYR B 256 ? 1.0511 1.0558 0.9807 0.0230  -0.1401 0.0321  1473 TYR B OH    
5732 N  N     . VAL B 257 ? 0.6705 0.6581 0.6822 -0.0034 -0.1004 0.0104  1474 VAL B N     
5733 C  CA    . VAL B 257 ? 0.5225 0.5068 0.5468 -0.0065 -0.0934 0.0104  1474 VAL B CA    
5734 C  C     . VAL B 257 ? 0.6500 0.6332 0.6793 -0.0031 -0.0881 0.0177  1474 VAL B C     
5735 O  O     . VAL B 257 ? 0.6949 0.6769 0.7161 0.0017  -0.0889 0.0227  1474 VAL B O     
5736 C  CB    . VAL B 257 ? 0.5322 0.5066 0.5470 -0.0092 -0.0878 0.0078  1474 VAL B CB    
5737 C  CG1   . VAL B 257 ? 0.6044 0.5800 0.6133 -0.0118 -0.0933 -0.0001 1474 VAL B CG1   
5738 C  CG2   . VAL B 257 ? 0.5185 0.4852 0.5172 -0.0060 -0.0832 0.0130  1474 VAL B CG2   
5739 N  N     . PHE B 258 ? 0.4172 0.4009 0.4602 -0.0054 -0.0826 0.0183  1475 PHE B N     
5740 C  CA    . PHE B 258 ? 0.4764 0.4600 0.5252 -0.0023 -0.0769 0.0240  1475 PHE B CA    
5741 C  C     . PHE B 258 ? 0.5679 0.5411 0.6091 -0.0030 -0.0686 0.0258  1475 PHE B C     
5742 O  O     . PHE B 258 ? 0.5799 0.5494 0.6225 -0.0072 -0.0658 0.0228  1475 PHE B O     
5743 C  CB    . PHE B 258 ? 0.6291 0.6225 0.6987 -0.0040 -0.0762 0.0240  1475 PHE B CB    
5744 C  CG    . PHE B 258 ? 0.6792 0.6845 0.7583 -0.0020 -0.0838 0.0233  1475 PHE B CG    
5745 C  CD1   . PHE B 258 ? 0.6988 0.7089 0.7815 0.0038  -0.0841 0.0278  1475 PHE B CD1   
5746 C  CD2   . PHE B 258 ? 0.5538 0.5656 0.6384 -0.0056 -0.0911 0.0177  1475 PHE B CD2   
5747 C  CE1   . PHE B 258 ? 0.7052 0.7270 0.7971 0.0063  -0.0915 0.0271  1475 PHE B CE1   
5748 C  CE2   . PHE B 258 ? 0.5777 0.6015 0.6711 -0.0036 -0.0987 0.0167  1475 PHE B CE2   
5749 C  CZ    . PHE B 258 ? 0.7134 0.7426 0.8108 0.0025  -0.0990 0.0217  1475 PHE B CZ    
5750 N  N     . GLN B 259 ? 0.5588 0.5274 0.5930 0.0011  -0.0649 0.0305  1476 GLN B N     
5751 C  CA    . GLN B 259 ? 0.4602 0.4191 0.4851 0.0006  -0.0581 0.0317  1476 GLN B CA    
5752 C  C     . GLN B 259 ? 0.3938 0.3526 0.4251 0.0030  -0.0519 0.0354  1476 GLN B C     
5753 O  O     . GLN B 259 ? 0.4604 0.4250 0.4993 0.0065  -0.0531 0.0377  1476 GLN B O     
5754 C  CB    . GLN B 259 ? 0.5486 0.5003 0.5563 0.0025  -0.0589 0.0331  1476 GLN B CB    
5755 C  CG    . GLN B 259 ? 0.6149 0.5654 0.6132 -0.0002 -0.0626 0.0290  1476 GLN B CG    
5756 C  CD    . GLN B 259 ? 0.7047 0.6495 0.6864 0.0016  -0.0629 0.0313  1476 GLN B CD    
5757 O  OE1   . GLN B 259 ? 0.5627 0.5097 0.5390 0.0041  -0.0682 0.0333  1476 GLN B OE1   
5758 N  NE2   . GLN B 259 ? 0.8951 0.8326 0.8685 0.0004  -0.0572 0.0315  1476 GLN B NE2   
5759 N  N     . ASN B 260 ? 0.3892 0.3422 0.4176 0.0012  -0.0456 0.0355  1477 ASN B N     
5760 C  CA    . ASN B 260 ? 0.3845 0.3350 0.4132 0.0037  -0.0391 0.0384  1477 ASN B CA    
5761 C  C     . ASN B 260 ? 0.4999 0.4408 0.5149 0.0035  -0.0357 0.0384  1477 ASN B C     
5762 O  O     . ASN B 260 ? 0.6242 0.5611 0.6317 0.0008  -0.0369 0.0359  1477 ASN B O     
5763 C  CB    . ASN B 260 ? 0.4249 0.3796 0.4653 0.0015  -0.0343 0.0388  1477 ASN B CB    
5764 C  CG    . ASN B 260 ? 0.6077 0.5731 0.6639 0.0006  -0.0369 0.0388  1477 ASN B CG    
5765 O  OD1   . ASN B 260 ? 0.6858 0.6548 0.7522 -0.0030 -0.0346 0.0387  1477 ASN B OD1   
5766 N  ND2   . ASN B 260 ? 0.6165 0.5873 0.6756 0.0039  -0.0416 0.0393  1477 ASN B ND2   
5767 N  N     . SER B 261 ? 0.4735 0.4114 0.4862 0.0064  -0.0311 0.0407  1478 SER B N     
5768 C  CA    . SER B 261 ? 0.6235 0.5539 0.6265 0.0059  -0.0267 0.0404  1478 SER B CA    
5769 C  C     . SER B 261 ? 0.6864 0.6178 0.6935 0.0082  -0.0212 0.0419  1478 SER B C     
5770 O  O     . SER B 261 ? 0.8297 0.7662 0.8445 0.0112  -0.0209 0.0433  1478 SER B O     
5771 C  CB    . SER B 261 ? 0.6376 0.5612 0.6281 0.0070  -0.0283 0.0411  1478 SER B CB    
5772 O  OG    . SER B 261 ? 0.6153 0.5385 0.6062 0.0108  -0.0305 0.0437  1478 SER B OG    
5773 N  N     . TRP B 262 ? 0.7366 0.6644 0.7392 0.0071  -0.0169 0.0413  1479 TRP B N     
5774 C  CA    . TRP B 262 ? 0.7316 0.6609 0.7367 0.0094  -0.0117 0.0423  1479 TRP B CA    
5775 C  C     . TRP B 262 ? 0.6917 0.6149 0.6871 0.0091  -0.0087 0.0412  1479 TRP B C     
5776 O  O     . TRP B 262 ? 0.5113 0.4307 0.5008 0.0065  -0.0097 0.0398  1479 TRP B O     
5777 C  CB    . TRP B 262 ? 0.6219 0.5578 0.6371 0.0081  -0.0090 0.0435  1479 TRP B CB    
5778 C  CG    . TRP B 262 ? 0.6347 0.5709 0.6535 0.0037  -0.0112 0.0427  1479 TRP B CG    
5779 C  CD1   . TRP B 262 ? 0.3694 0.3097 0.3959 0.0018  -0.0154 0.0421  1479 TRP B CD1   
5780 C  CD2   . TRP B 262 ? 0.6373 0.5692 0.6528 0.0011  -0.0096 0.0419  1479 TRP B CD2   
5781 N  NE1   . TRP B 262 ? 0.3700 0.3084 0.3981 -0.0021 -0.0165 0.0406  1479 TRP B NE1   
5782 C  CE2   . TRP B 262 ? 0.5299 0.4628 0.5514 -0.0024 -0.0129 0.0406  1479 TRP B CE2   
5783 C  CE3   . TRP B 262 ? 0.6584 0.5860 0.6668 0.0017  -0.0061 0.0419  1479 TRP B CE3   
5784 C  CZ2   . TRP B 262 ? 0.3697 0.2984 0.3905 -0.0051 -0.0126 0.0392  1479 TRP B CZ2   
5785 C  CZ3   . TRP B 262 ? 0.5179 0.4422 0.5256 -0.0008 -0.0058 0.0410  1479 TRP B CZ3   
5786 C  CH2   . TRP B 262 ? 0.5192 0.4435 0.5330 -0.0040 -0.0090 0.0397  1479 TRP B CH2   
5787 N  N     . GLY B 263 ? 0.7259 0.6493 0.7205 0.0119  -0.0050 0.0414  1480 GLY B N     
5788 C  CA    . GLY B 263 ? 0.6839 0.6024 0.6700 0.0119  -0.0027 0.0399  1480 GLY B CA    
5789 C  C     . GLY B 263 ? 0.5815 0.5022 0.5676 0.0148  0.0017  0.0396  1480 GLY B C     
5790 O  O     . GLY B 263 ? 0.4740 0.3988 0.4649 0.0180  0.0032  0.0401  1480 GLY B O     
5791 N  N     . ILE B 264 ? 0.5603 0.4791 0.5407 0.0139  0.0037  0.0384  1481 ILE B N     
5792 C  CA    . ILE B 264 ? 0.4978 0.4186 0.4760 0.0167  0.0073  0.0374  1481 ILE B CA    
5793 C  C     . ILE B 264 ? 0.5000 0.4165 0.4702 0.0156  0.0074  0.0348  1481 ILE B C     
5794 O  O     . ILE B 264 ? 0.4360 0.3501 0.4038 0.0127  0.0060  0.0346  1481 ILE B O     
5795 C  CB    . ILE B 264 ? 0.4883 0.4158 0.4711 0.0176  0.0107  0.0400  1481 ILE B CB    
5796 C  CG1   . ILE B 264 ? 0.5141 0.4459 0.4961 0.0218  0.0142  0.0391  1481 ILE B CG1   
5797 C  CG2   . ILE B 264 ? 0.5117 0.4384 0.4909 0.0159  0.0117  0.0406  1481 ILE B CG2   
5798 C  CD1   . ILE B 264 ? 0.4516 0.3909 0.4366 0.0228  0.0185  0.0423  1481 ILE B CD1   
5799 N  N     . THR B 265 ? 0.5865 0.5026 0.5533 0.0180  0.0089  0.0323  1482 THR B N     
5800 C  CA    . THR B 265 ? 0.5724 0.4848 0.5327 0.0168  0.0086  0.0292  1482 THR B CA    
5801 C  C     . THR B 265 ? 0.6464 0.5626 0.6035 0.0191  0.0110  0.0272  1482 THR B C     
5802 O  O     . THR B 265 ? 0.8360 0.7577 0.7948 0.0219  0.0135  0.0286  1482 THR B O     
5803 C  CB    . THR B 265 ? 0.5388 0.4451 0.4975 0.0168  0.0068  0.0272  1482 THR B CB    
5804 O  OG1   . THR B 265 ? 0.4910 0.3986 0.4513 0.0208  0.0083  0.0255  1482 THR B OG1   
5805 C  CG2   . THR B 265 ? 0.5793 0.4823 0.5403 0.0153  0.0041  0.0298  1482 THR B CG2   
5806 N  N     . THR B 266 ? 0.5190 0.4329 0.4714 0.0180  0.0103  0.0237  1483 THR B N     
5807 C  CA    . THR B 266 ? 0.5007 0.4183 0.4495 0.0205  0.0118  0.0208  1483 THR B CA    
5808 C  C     . THR B 266 ? 0.6513 0.5695 0.6001 0.0241  0.0130  0.0180  1483 THR B C     
5809 O  O     . THR B 266 ? 0.7386 0.6610 0.6839 0.0267  0.0142  0.0151  1483 THR B O     
5810 C  CB    . THR B 266 ? 0.4705 0.3859 0.4157 0.0180  0.0103  0.0170  1483 THR B CB    
5811 O  OG1   . THR B 266 ? 0.5200 0.4290 0.4655 0.0166  0.0090  0.0146  1483 THR B OG1   
5812 C  CG2   . THR B 266 ? 0.4773 0.3921 0.4226 0.0146  0.0093  0.0188  1483 THR B CG2   
5813 N  N     . ARG B 267 ? 0.6381 0.5528 0.5906 0.0248  0.0124  0.0185  1484 ARG B N     
5814 C  CA    . ARG B 267 ? 0.6330 0.5484 0.5862 0.0291  0.0135  0.0154  1484 ARG B CA    
5815 C  C     . ARG B 267 ? 0.6470 0.5716 0.5997 0.0329  0.0169  0.0161  1484 ARG B C     
5816 O  O     . ARG B 267 ? 0.6181 0.5455 0.5683 0.0366  0.0183  0.0118  1484 ARG B O     
5817 C  CB    . ARG B 267 ? 0.6024 0.5139 0.5610 0.0300  0.0123  0.0170  1484 ARG B CB    
5818 C  CG    . ARG B 267 ? 0.3961 0.3088 0.3571 0.0353  0.0136  0.0138  1484 ARG B CG    
5819 C  CD    . ARG B 267 ? 0.4370 0.3456 0.4038 0.0365  0.0117  0.0159  1484 ARG B CD    
5820 N  NE    . ARG B 267 ? 0.7077 0.6052 0.6730 0.0347  0.0085  0.0144  1484 ARG B NE    
5821 C  CZ    . ARG B 267 ? 0.8409 0.7325 0.8099 0.0360  0.0061  0.0159  1484 ARG B CZ    
5822 N  NH1   . ARG B 267 ? 0.8738 0.7706 0.8491 0.0394  0.0062  0.0184  1484 ARG B NH1   
5823 N  NH2   . ARG B 267 ? 0.9179 0.7986 0.8847 0.0339  0.0035  0.0153  1484 ARG B NH2   
5824 N  N     . THR B 268 ? 0.7462 0.6757 0.7010 0.0318  0.0183  0.0213  1485 THR B N     
5825 C  CA    . THR B 268 ? 0.7193 0.6575 0.6732 0.0346  0.0219  0.0236  1485 THR B CA    
5826 C  C     . THR B 268 ? 0.6762 0.6177 0.6225 0.0372  0.0228  0.0195  1485 THR B C     
5827 O  O     . THR B 268 ? 0.7157 0.6632 0.6600 0.0415  0.0256  0.0178  1485 THR B O     
5828 C  CB    . THR B 268 ? 0.6955 0.6351 0.6512 0.0317  0.0222  0.0294  1485 THR B CB    
5829 O  OG1   . THR B 268 ? 0.7037 0.6394 0.6550 0.0292  0.0198  0.0280  1485 THR B OG1   
5830 C  CG2   . THR B 268 ? 0.7863 0.7232 0.7493 0.0290  0.0208  0.0325  1485 THR B CG2   
5831 N  N     . ILE B 269 ? 0.4683 0.4066 0.4103 0.0349  0.0204  0.0173  1486 ILE B N     
5832 C  CA    . ILE B 269 ? 0.6859 0.6285 0.6210 0.0373  0.0205  0.0133  1486 ILE B CA    
5833 C  C     . ILE B 269 ? 0.7090 0.6515 0.6424 0.0406  0.0207  0.0066  1486 ILE B C     
5834 O  O     . ILE B 269 ? 0.6361 0.5857 0.5653 0.0449  0.0231  0.0047  1486 ILE B O     
5835 C  CB    . ILE B 269 ? 0.5999 0.5395 0.5325 0.0340  0.0174  0.0114  1486 ILE B CB    
5836 C  CG1   . ILE B 269 ? 0.4854 0.4253 0.4201 0.0318  0.0174  0.0177  1486 ILE B CG1   
5837 C  CG2   . ILE B 269 ? 0.3971 0.3421 0.3231 0.0366  0.0168  0.0067  1486 ILE B CG2   
5838 C  CD1   . ILE B 269 ? 0.4887 0.4265 0.4224 0.0289  0.0147  0.0164  1486 ILE B CD1   
5839 N  N     . GLY B 270 ? 0.6223 0.5566 0.5591 0.0388  0.0185  0.0034  1487 GLY B N     
5840 C  CA    . GLY B 270 ? 0.5634 0.4956 0.4997 0.0419  0.0183  -0.0033 1487 GLY B CA    
5841 C  C     . GLY B 270 ? 0.5204 0.4592 0.4581 0.0472  0.0219  -0.0028 1487 GLY B C     
5842 O  O     . GLY B 270 ? 0.4925 0.4361 0.4260 0.0515  0.0234  -0.0081 1487 GLY B O     
5843 N  N     . VAL B 271 ? 0.4942 0.4346 0.4376 0.0469  0.0236  0.0035  1488 VAL B N     
5844 C  CA    . VAL B 271 ? 0.5370 0.4851 0.4834 0.0517  0.0275  0.0042  1488 VAL B CA    
5845 C  C     . VAL B 271 ? 0.5473 0.5063 0.4873 0.0546  0.0311  0.0050  1488 VAL B C     
5846 O  O     . VAL B 271 ? 0.5855 0.5507 0.5226 0.0597  0.0337  0.0006  1488 VAL B O     
5847 C  CB    . VAL B 271 ? 0.4036 0.3527 0.3585 0.0501  0.0283  0.0110  1488 VAL B CB    
5848 C  CG1   . VAL B 271 ? 0.4065 0.3653 0.3657 0.0549  0.0327  0.0117  1488 VAL B CG1   
5849 C  CG2   . VAL B 271 ? 0.4018 0.3405 0.3616 0.0476  0.0242  0.0106  1488 VAL B CG2   
5850 N  N     . MET B 272 ? 0.4971 0.4580 0.4338 0.0517  0.0311  0.0099  1489 MET B N     
5851 C  CA    . MET B 272 ? 0.5076 0.4781 0.4370 0.0545  0.0340  0.0115  1489 MET B CA    
5852 C  C     . MET B 272 ? 0.5370 0.5096 0.4586 0.0584  0.0332  0.0028  1489 MET B C     
5853 O  O     . MET B 272 ? 0.5352 0.5162 0.4532 0.0634  0.0367  0.0005  1489 MET B O     
5854 C  CB    . MET B 272 ? 0.5587 0.5283 0.4855 0.0511  0.0326  0.0170  1489 MET B CB    
5855 C  CG    . MET B 272 ? 0.5319 0.5102 0.4500 0.0541  0.0347  0.0190  1489 MET B CG    
5856 S  SD    . MET B 272 ? 0.6534 0.6282 0.5684 0.0509  0.0312  0.0226  1489 MET B SD    
5857 C  CE    . MET B 272 ? 0.5865 0.5552 0.4996 0.0493  0.0257  0.0129  1489 MET B CE    
5858 N  N     . ILE B 273 ? 0.4914 0.4566 0.4114 0.0561  0.0287  -0.0029 1490 ILE B N     
5859 C  CA    . ILE B 273 ? 0.5020 0.4688 0.4153 0.0591  0.0271  -0.0121 1490 ILE B CA    
5860 C  C     . ILE B 273 ? 0.5623 0.5313 0.4767 0.0642  0.0295  -0.0176 1490 ILE B C     
5861 O  O     . ILE B 273 ? 0.7355 0.7140 0.6435 0.0692  0.0323  -0.0206 1490 ILE B O     
5862 C  CB    . ILE B 273 ? 0.4852 0.4422 0.3999 0.0549  0.0220  -0.0176 1490 ILE B CB    
5863 C  CG1   . ILE B 273 ? 0.4230 0.3800 0.3362 0.0508  0.0197  -0.0135 1490 ILE B CG1   
5864 C  CG2   . ILE B 273 ? 0.4941 0.4519 0.4040 0.0576  0.0201  -0.0282 1490 ILE B CG2   
5865 C  CD1   . ILE B 273 ? 0.5284 0.4768 0.4446 0.0459  0.0156  -0.0175 1490 ILE B CD1   
5866 N  N     . MET B 274 ? 0.4347 0.3960 0.3574 0.0633  0.0289  -0.0180 1491 MET B N     
5867 C  CA    . MET B 274 ? 0.5110 0.4722 0.4358 0.0684  0.0302  -0.0247 1491 MET B CA    
5868 C  C     . MET B 274 ? 0.5735 0.5478 0.4970 0.0738  0.0360  -0.0225 1491 MET B C     
5869 O  O     . MET B 274 ? 0.6621 0.6411 0.5827 0.0795  0.0378  -0.0297 1491 MET B O     
5870 C  CB    . MET B 274 ? 0.6142 0.5649 0.5486 0.0666  0.0283  -0.0236 1491 MET B CB    
5871 C  CG    . MET B 274 ? 0.8194 0.7570 0.7545 0.0622  0.0232  -0.0273 1491 MET B CG    
5872 S  SD    . MET B 274 ? 1.0642 0.9956 0.9995 0.0668  0.0216  -0.0392 1491 MET B SD    
5873 C  CE    . MET B 274 ? 1.0049 0.9276 0.9365 0.0613  0.0166  -0.0451 1491 MET B CE    
5874 N  N     . VAL B 275 ? 0.5596 0.5401 0.4847 0.0719  0.0390  -0.0128 1492 VAL B N     
5875 C  CA    . VAL B 275 ? 0.5830 0.5763 0.5085 0.0761  0.0451  -0.0094 1492 VAL B CA    
5876 C  C     . VAL B 275 ? 0.6048 0.6089 0.5187 0.0791  0.0479  -0.0096 1492 VAL B C     
5877 O  O     . VAL B 275 ? 0.6864 0.7012 0.5971 0.0845  0.0526  -0.0119 1492 VAL B O     
5878 C  CB    . VAL B 275 ? 0.7260 0.7207 0.6597 0.0721  0.0470  0.0013  1492 VAL B CB    
5879 C  CG1   . VAL B 275 ? 0.4361 0.4452 0.3695 0.0747  0.0539  0.0073  1492 VAL B CG1   
5880 C  CG2   . VAL B 275 ? 0.7836 0.7705 0.7285 0.0708  0.0447  0.0010  1492 VAL B CG2   
5881 N  N     . HIS B 276 ? 0.6002 0.6023 0.5075 0.0761  0.0449  -0.0078 1493 HIS B N     
5882 C  CA    . HIS B 276 ? 0.5300 0.5426 0.4263 0.0786  0.0474  -0.0052 1493 HIS B CA    
5883 C  C     . HIS B 276 ? 0.5220 0.5357 0.4078 0.0811  0.0438  -0.0142 1493 HIS B C     
5884 O  O     . HIS B 276 ? 0.6803 0.7050 0.5559 0.0856  0.0464  -0.0150 1493 HIS B O     
5885 C  CB    . HIS B 276 ? 0.5190 0.5309 0.4157 0.0741  0.0473  0.0058  1493 HIS B CB    
5886 C  CG    . HIS B 276 ? 0.4893 0.5030 0.3951 0.0718  0.0515  0.0152  1493 HIS B CG    
5887 N  ND1   . HIS B 276 ? 0.5586 0.5827 0.4664 0.0752  0.0577  0.0174  1493 HIS B ND1   
5888 C  CD2   . HIS B 276 ? 0.4330 0.4402 0.3470 0.0664  0.0502  0.0225  1493 HIS B CD2   
5889 C  CE1   . HIS B 276 ? 0.6319 0.6557 0.5494 0.0715  0.0599  0.0258  1493 HIS B CE1   
5890 N  NE2   . HIS B 276 ? 0.4972 0.5105 0.4185 0.0662  0.0553  0.0288  1493 HIS B NE2   
5891 N  N     . ALA B 277 ? 0.5036 0.5069 0.3911 0.0780  0.0378  -0.0205 1494 ALA B N     
5892 C  CA    . ALA B 277 ? 0.6058 0.6112 0.4842 0.0795  0.0339  -0.0286 1494 ALA B CA    
5893 C  C     . ALA B 277 ? 0.6547 0.6658 0.5278 0.0857  0.0353  -0.0390 1494 ALA B C     
5894 O  O     . ALA B 277 ? 0.6275 0.6346 0.5070 0.0875  0.0367  -0.0435 1494 ALA B O     
5895 C  CB    . ALA B 277 ? 0.4620 0.4557 0.3451 0.0742  0.0277  -0.0332 1494 ALA B CB    
5896 N  N     . ASP B 278 ? 0.6171 0.6382 0.4783 0.0896  0.0349  -0.0429 1495 ASP B N     
5897 C  CA    . ASP B 278 ? 0.5328 0.5609 0.3868 0.0960  0.0359  -0.0539 1495 ASP B CA    
5898 C  C     . ASP B 278 ? 0.5900 0.6127 0.4414 0.0951  0.0290  -0.0662 1495 ASP B C     
5899 O  O     . ASP B 278 ? 0.5928 0.6052 0.4506 0.0891  0.0242  -0.0663 1495 ASP B O     
5900 C  CB    . ASP B 278 ? 0.5837 0.6281 0.4253 0.1013  0.0406  -0.0495 1495 ASP B CB    
5901 C  CG    . ASP B 278 ? 0.7935 0.8421 0.6271 0.0996  0.0378  -0.0431 1495 ASP B CG    
5902 O  OD1   . ASP B 278 ? 0.8376 0.8786 0.6735 0.0955  0.0315  -0.0460 1495 ASP B OD1   
5903 O  OD2   . ASP B 278 ? 0.7660 0.8261 0.5909 0.1028  0.0421  -0.0352 1495 ASP B OD2   
5904 N  N     . ASN B 279 ? 0.8101 0.8407 0.6524 0.1007  0.0286  -0.0768 1496 ASN B N     
5905 C  CA    . ASN B 279 ? 0.8936 0.9195 0.7346 0.0998  0.0219  -0.0900 1496 ASN B CA    
5906 C  C     . ASN B 279 ? 0.8826 0.9152 0.7152 0.0985  0.0173  -0.0894 1496 ASN B C     
5907 O  O     . ASN B 279 ? 1.0153 1.0477 0.8450 0.0984  0.0118  -0.1009 1496 ASN B O     
5908 C  CB    . ASN B 279 ? 0.9497 0.9803 0.7850 0.1066  0.0225  -0.1038 1496 ASN B CB    
5909 C  CG    . ASN B 279 ? 0.9986 1.0222 0.8431 0.1089  0.0262  -0.1063 1496 ASN B CG    
5910 O  OD1   . ASN B 279 ? 0.9462 0.9555 0.8005 0.1059  0.0228  -0.1124 1496 ASN B OD1   
5911 N  ND2   . ASN B 279 ? 1.0062 1.0404 0.8475 0.1144  0.0333  -0.1018 1496 ASN B ND2   
5912 N  N     . GLN B 280 ? 0.7015 0.7400 0.5308 0.0975  0.0193  -0.0766 1497 GLN B N     
5913 C  CA    . GLN B 280 ? 0.7943 0.8388 0.6167 0.0966  0.0147  -0.0750 1497 GLN B CA    
5914 C  C     . GLN B 280 ? 0.8658 0.9028 0.6964 0.0901  0.0130  -0.0648 1497 GLN B C     
5915 O  O     . GLN B 280 ? 0.8870 0.9288 0.7134 0.0895  0.0093  -0.0620 1497 GLN B O     
5916 C  CB    . GLN B 280 ? 0.7830 0.8435 0.5905 0.1031  0.0177  -0.0701 1497 GLN B CB    
5917 C  CG    . GLN B 280 ? 0.9192 0.9894 0.7153 0.1092  0.0160  -0.0834 1497 GLN B CG    
5918 C  CD    . GLN B 280 ? 0.9904 1.0726 0.7763 0.1162  0.0232  -0.0806 1497 GLN B CD    
5919 O  OE1   . GLN B 280 ? 1.1443 1.2339 0.9246 0.1176  0.0277  -0.0676 1497 GLN B OE1   
5920 N  NE2   . GLN B 280 ? 0.8653 0.9493 0.6495 0.1205  0.0247  -0.0926 1497 GLN B NE2   
5921 N  N     . GLY B 281 ? 0.7837 0.8096 0.6259 0.0858  0.0153  -0.0597 1498 GLY B N     
5922 C  CA    . GLY B 281 ? 0.6512 0.6693 0.5017 0.0795  0.0135  -0.0519 1498 GLY B CA    
5923 C  C     . GLY B 281 ? 0.6261 0.6405 0.4824 0.0782  0.0188  -0.0403 1498 GLY B C     
5924 O  O     . GLY B 281 ? 0.6535 0.6694 0.5104 0.0811  0.0236  -0.0395 1498 GLY B O     
5925 N  N     . LEU B 282 ? 0.5896 0.5995 0.4510 0.0737  0.0177  -0.0319 1499 LEU B N     
5926 C  CA    . LEU B 282 ? 0.5552 0.5616 0.4228 0.0717  0.0220  -0.0208 1499 LEU B CA    
5927 C  C     . LEU B 282 ? 0.7489 0.7655 0.6094 0.0762  0.0273  -0.0128 1499 LEU B C     
5928 O  O     . LEU B 282 ? 0.7600 0.7866 0.6096 0.0808  0.0273  -0.0137 1499 LEU B O     
5929 C  CB    . LEU B 282 ? 0.4497 0.4504 0.3225 0.0667  0.0194  -0.0144 1499 LEU B CB    
5930 C  CG    . LEU B 282 ? 0.4834 0.4738 0.3646 0.0610  0.0153  -0.0191 1499 LEU B CG    
5931 C  CD1   . LEU B 282 ? 0.4848 0.4754 0.3667 0.0582  0.0114  -0.0168 1499 LEU B CD1   
5932 C  CD2   . LEU B 282 ? 0.4347 0.4162 0.3252 0.0576  0.0177  -0.0145 1499 LEU B CD2   
5933 N  N     . VAL B 283 ? 0.7677 0.7820 0.6348 0.0747  0.0319  -0.0046 1500 VAL B N     
5934 C  CA    . VAL B 283 ? 0.6910 0.7133 0.5544 0.0771  0.0373  0.0057  1500 VAL B CA    
5935 C  C     . VAL B 283 ? 0.6137 0.6288 0.4871 0.0720  0.0386  0.0155  1500 VAL B C     
5936 O  O     . VAL B 283 ? 0.6452 0.6565 0.5276 0.0701  0.0410  0.0167  1500 VAL B O     
5937 C  CB    . VAL B 283 ? 0.6234 0.6538 0.4841 0.0817  0.0430  0.0034  1500 VAL B CB    
5938 C  CG1   . VAL B 283 ? 0.5736 0.6128 0.4313 0.0832  0.0493  0.0151  1500 VAL B CG1   
5939 C  CG2   . VAL B 283 ? 0.6127 0.6502 0.4628 0.0869  0.0414  -0.0074 1500 VAL B CG2   
5940 N  N     . LEU B 284 ? 0.6157 0.6291 0.4880 0.0702  0.0366  0.0221  1501 LEU B N     
5941 C  CA    . LEU B 284 ? 0.6223 0.6277 0.5041 0.0653  0.0367  0.0299  1501 LEU B CA    
5942 C  C     . LEU B 284 ? 0.6374 0.6470 0.5215 0.0654  0.0428  0.0403  1501 LEU B C     
5943 O  O     . LEU B 284 ? 0.5417 0.5603 0.4175 0.0692  0.0462  0.0448  1501 LEU B O     
5944 C  CB    . LEU B 284 ? 0.5103 0.5123 0.3905 0.0638  0.0322  0.0323  1501 LEU B CB    
5945 C  CG    . LEU B 284 ? 0.5737 0.5718 0.4544 0.0625  0.0265  0.0221  1501 LEU B CG    
5946 C  CD1   . LEU B 284 ? 0.5073 0.5036 0.3873 0.0614  0.0219  0.0232  1501 LEU B CD1   
5947 C  CD2   . LEU B 284 ? 0.6377 0.6268 0.5282 0.0580  0.0259  0.0183  1501 LEU B CD2   
5948 N  N     . PRO B 285 ? 0.6416 0.6456 0.5369 0.0613  0.0443  0.0439  1502 PRO B N     
5949 C  CA    . PRO B 285 ? 0.7225 0.7295 0.6221 0.0600  0.0495  0.0542  1502 PRO B CA    
5950 C  C     . PRO B 285 ? 0.7619 0.7657 0.6598 0.0586  0.0483  0.0627  1502 PRO B C     
5951 O  O     . PRO B 285 ? 0.7925 0.7881 0.6929 0.0562  0.0433  0.0612  1502 PRO B O     
5952 C  CB    . PRO B 285 ? 0.7503 0.7510 0.6632 0.0556  0.0494  0.0539  1502 PRO B CB    
5953 C  CG    . PRO B 285 ? 0.6113 0.6069 0.5252 0.0556  0.0452  0.0436  1502 PRO B CG    
5954 C  CD    . PRO B 285 ? 0.6355 0.6301 0.5402 0.0573  0.0411  0.0390  1502 PRO B CD    
5955 N  N     . PRO B 286 ? 0.7074 0.7173 0.6014 0.0601  0.0528  0.0720  1503 PRO B N     
5956 C  CA    . PRO B 286 ? 0.5975 0.6041 0.4878 0.0602  0.0511  0.0798  1503 PRO B CA    
5957 C  C     . PRO B 286 ? 0.7045 0.6995 0.6054 0.0550  0.0481  0.0827  1503 PRO B C     
5958 O  O     . PRO B 286 ? 0.7774 0.7673 0.6761 0.0554  0.0440  0.0839  1503 PRO B O     
5959 C  CB    . PRO B 286 ? 0.7116 0.7261 0.5978 0.0617  0.0577  0.0905  1503 PRO B CB    
5960 C  CG    . PRO B 286 ? 0.7255 0.7503 0.6103 0.0640  0.0627  0.0862  1503 PRO B CG    
5961 C  CD    . PRO B 286 ? 0.7140 0.7330 0.6090 0.0611  0.0600  0.0770  1503 PRO B CD    
5962 N  N     . ARG B 287 ? 0.7206 0.7118 0.6332 0.0505  0.0497  0.0832  1504 ARG B N     
5963 C  CA    . ARG B 287 ? 0.5669 0.5480 0.4896 0.0456  0.0473  0.0866  1504 ARG B CA    
5964 C  C     . ARG B 287 ? 0.5265 0.4999 0.4515 0.0440  0.0413  0.0783  1504 ARG B C     
5965 O  O     . ARG B 287 ? 0.6009 0.5661 0.5332 0.0404  0.0388  0.0798  1504 ARG B O     
5966 C  CB    . ARG B 287 ? 0.5613 0.5424 0.4959 0.0413  0.0509  0.0898  1504 ARG B CB    
5967 C  CG    . ARG B 287 ? 0.6680 0.6594 0.6017 0.0426  0.0578  0.0961  1504 ARG B CG    
5968 C  CD    . ARG B 287 ? 0.6600 0.6502 0.6065 0.0374  0.0612  0.1035  1504 ARG B CD    
5969 N  NE    . ARG B 287 ? 0.7527 0.7532 0.6973 0.0385  0.0684  0.1115  1504 ARG B NE    
5970 C  CZ    . ARG B 287 ? 0.7047 0.7142 0.6562 0.0375  0.0736  0.1122  1504 ARG B CZ    
5971 N  NH1   . ARG B 287 ? 0.6473 0.6566 0.6085 0.0356  0.0719  0.1056  1504 ARG B NH1   
5972 N  NH2   . ARG B 287 ? 0.8423 0.8618 0.7911 0.0385  0.0806  0.1202  1504 ARG B NH2   
5973 N  N     . VAL B 288 ? 0.4824 0.4583 0.4022 0.0462  0.0391  0.0694  1505 VAL B N     
5974 C  CA    . VAL B 288 ? 0.4650 0.4346 0.3859 0.0447  0.0337  0.0620  1505 VAL B CA    
5975 C  C     . VAL B 288 ? 0.5865 0.5595 0.4980 0.0484  0.0306  0.0571  1505 VAL B C     
5976 O  O     . VAL B 288 ? 0.6832 0.6519 0.5957 0.0470  0.0263  0.0520  1505 VAL B O     
5977 C  CB    . VAL B 288 ? 0.5745 0.5421 0.5006 0.0426  0.0330  0.0551  1505 VAL B CB    
5978 C  CG1   . VAL B 288 ? 0.7155 0.6808 0.6517 0.0390  0.0353  0.0593  1505 VAL B CG1   
5979 C  CG2   . VAL B 288 ? 0.6732 0.6480 0.5932 0.0464  0.0348  0.0498  1505 VAL B CG2   
5980 N  N     . ALA B 289 ? 0.5663 0.5476 0.4686 0.0529  0.0326  0.0585  1506 ALA B N     
5981 C  CA    . ALA B 289 ? 0.4902 0.4758 0.3836 0.0566  0.0290  0.0536  1506 ALA B CA    
5982 C  C     . ALA B 289 ? 0.5815 0.5628 0.4758 0.0564  0.0253  0.0568  1506 ALA B C     
5983 O  O     . ALA B 289 ? 0.7043 0.6830 0.6002 0.0564  0.0268  0.0657  1506 ALA B O     
5984 C  CB    . ALA B 289 ? 0.5114 0.5072 0.3940 0.0618  0.0320  0.0562  1506 ALA B CB    
5985 N  N     . CYS B 290 ? 0.5776 0.5580 0.4716 0.0561  0.0205  0.0495  1507 CYS B N     
5986 C  CA    . CYS B 290 ? 0.5935 0.5699 0.4902 0.0560  0.0172  0.0521  1507 CYS B CA    
5987 C  C     . CYS B 290 ? 0.6977 0.6799 0.5860 0.0615  0.0160  0.0573  1507 CYS B C     
5988 O  O     . CYS B 290 ? 0.8966 0.8749 0.7866 0.0625  0.0154  0.0643  1507 CYS B O     
5989 C  CB    . CYS B 290 ? 0.5926 0.5664 0.4936 0.0534  0.0130  0.0434  1507 CYS B CB    
5990 S  SG    . CYS B 290 ? 0.7362 0.7177 0.6320 0.0562  0.0078  0.0353  1507 CYS B SG    
5991 N  N     . ILE B 291 ? 0.7761 0.7673 0.6551 0.0654  0.0155  0.0538  1508 ILE B N     
5992 C  CA    . ILE B 291 ? 0.9231 0.9211 0.7920 0.0711  0.0158  0.0604  1508 ILE B CA    
5993 C  C     . ILE B 291 ? 0.9681 0.9709 0.8317 0.0722  0.0216  0.0646  1508 ILE B C     
5994 O  O     . ILE B 291 ? 1.1628 1.1698 1.0244 0.0720  0.0230  0.0574  1508 ILE B O     
5995 C  CB    . ILE B 291 ? 0.9988 1.0057 0.8596 0.0755  0.0107  0.0538  1508 ILE B CB    
5996 C  CG1   . ILE B 291 ? 1.0104 1.0142 0.8784 0.0737  0.0052  0.0480  1508 ILE B CG1   
5997 C  CG2   . ILE B 291 ? 0.9790 0.9920 0.8297 0.0816  0.0103  0.0622  1508 ILE B CG2   
5998 C  CD1   . ILE B 291 ? 1.0271 1.0405 0.8889 0.0780  -0.0004 0.0420  1508 ILE B CD1   
5999 N  N     . GLN B 292 ? 0.8352 0.8369 0.6974 0.0732  0.0253  0.0762  1509 GLN B N     
6000 C  CA    . GLN B 292 ? 0.6782 0.6855 0.5360 0.0740  0.0317  0.0816  1509 GLN B CA    
6001 C  C     . GLN B 292 ? 0.7088 0.7273 0.5518 0.0804  0.0322  0.0842  1509 GLN B C     
6002 O  O     . GLN B 292 ? 0.7325 0.7593 0.5692 0.0822  0.0365  0.0830  1509 GLN B O     
6003 C  CB    . GLN B 292 ? 0.7296 0.7300 0.5948 0.0707  0.0359  0.0932  1509 GLN B CB    
6004 C  CG    . GLN B 292 ? 0.7506 0.7417 0.6297 0.0645  0.0359  0.0900  1509 GLN B CG    
6005 C  CD    . GLN B 292 ? 0.7283 0.7122 0.6156 0.0609  0.0390  0.1006  1509 GLN B CD    
6006 O  OE1   . GLN B 292 ? 0.7532 0.7330 0.6394 0.0623  0.0380  0.1086  1509 GLN B OE1   
6007 N  NE2   . GLN B 292 ? 0.8055 0.7878 0.7019 0.0564  0.0427  0.1007  1509 GLN B NE2   
6008 N  N     . VAL B 293 ? 0.7547 0.7738 0.5919 0.0841  0.0282  0.0885  1510 VAL B N     
6009 C  CA    . VAL B 293 ? 0.7229 0.7527 0.5450 0.0908  0.0275  0.0914  1510 VAL B CA    
6010 C  C     . VAL B 293 ? 0.8688 0.9014 0.6879 0.0939  0.0194  0.0836  1510 VAL B C     
6011 O  O     . VAL B 293 ? 0.9241 0.9490 0.7511 0.0926  0.0153  0.0843  1510 VAL B O     
6012 C  CB    . VAL B 293 ? 0.5803 0.6085 0.3982 0.0928  0.0306  0.1074  1510 VAL B CB    
6013 C  CG1   . VAL B 293 ? 0.5387 0.5783 0.3396 0.1003  0.0291  0.1107  1510 VAL B CG1   
6014 C  CG2   . VAL B 293 ? 0.5231 0.5498 0.3453 0.0890  0.0388  0.1151  1510 VAL B CG2   
6015 N  N     . VAL B 294 ? 0.8283 0.8721 0.6366 0.0982  0.0169  0.0757  1511 VAL B N     
6016 C  CA    . VAL B 294 ? 0.8576 0.9066 0.6619 0.1020  0.0091  0.0697  1511 VAL B CA    
6017 C  C     . VAL B 294 ? 0.9276 0.9888 0.7151 0.1095  0.0079  0.0739  1511 VAL B C     
6018 O  O     . VAL B 294 ? 0.9690 1.0392 0.7463 0.1118  0.0110  0.0711  1511 VAL B O     
6019 C  CB    . VAL B 294 ? 0.6737 0.7248 0.4824 0.0995  0.0050  0.0538  1511 VAL B CB    
6020 C  CG1   . VAL B 294 ? 0.5228 0.5815 0.3240 0.1005  0.0079  0.0463  1511 VAL B CG1   
6021 C  CG2   . VAL B 294 ? 0.7132 0.7705 0.5195 0.1030  -0.0032 0.0482  1511 VAL B CG2   
6022 N  N     . ILE B 295 ? 0.8000 0.8618 0.5843 0.1137  0.0030  0.0799  1512 ILE B N     
6023 C  CA    . ILE B 295 ? 0.7751 0.8485 0.5432 0.1215  0.0005  0.0844  1512 ILE B CA    
6024 C  C     . ILE B 295 ? 0.7889 0.8728 0.5531 0.1243  -0.0073 0.0704  1512 ILE B C     
6025 O  O     . ILE B 295 ? 0.9328 1.0136 0.7073 0.1224  -0.0129 0.0636  1512 ILE B O     
6026 C  CB    . ILE B 295 ? 0.7608 0.8294 0.5279 0.1252  -0.0016 0.0984  1512 ILE B CB    
6027 C  CG1   . ILE B 295 ? 0.9460 1.0030 0.7187 0.1215  0.0059  0.1121  1512 ILE B CG1   
6028 C  CG2   . ILE B 295 ? 0.6044 0.6857 0.3532 0.1337  -0.0045 0.1034  1512 ILE B CG2   
6029 C  CD1   . ILE B 295 ? 0.9788 1.0278 0.7533 0.1243  0.0038  0.1254  1512 ILE B CD1   
6030 N  N     . VAL B 296 ? 0.6109 0.7078 0.3605 0.1289  -0.0076 0.0659  1513 VAL B N     
6031 C  CA    . VAL B 296 ? 0.7256 0.8333 0.4714 0.1314  -0.0152 0.0516  1513 VAL B CA    
6032 C  C     . VAL B 296 ? 0.8621 0.9832 0.5900 0.1402  -0.0191 0.0563  1513 VAL B C     
6033 O  O     . VAL B 296 ? 0.9446 1.0743 0.6579 0.1438  -0.0152 0.0581  1513 VAL B O     
6034 C  CB    . VAL B 296 ? 0.7052 0.8160 0.4512 0.1282  -0.0131 0.0374  1513 VAL B CB    
6035 C  CG1   . VAL B 296 ? 0.5747 0.6971 0.3156 0.1311  -0.0212 0.0231  1513 VAL B CG1   
6036 C  CG2   . VAL B 296 ? 0.7628 0.8607 0.5265 0.1199  -0.0109 0.0320  1513 VAL B CG2   
6037 N  N     . PRO B 297 ? 0.8543 0.9784 0.5825 0.1442  -0.0267 0.0584  1514 PRO B N     
6038 C  CA    . PRO B 297 ? 0.7818 0.9187 0.4925 0.1532  -0.0309 0.0641  1514 PRO B CA    
6039 C  C     . PRO B 297 ? 0.7265 0.8791 0.4260 0.1565  -0.0356 0.0496  1514 PRO B C     
6040 O  O     . PRO B 297 ? 0.7022 0.8568 0.4106 0.1530  -0.0404 0.0342  1514 PRO B O     
6041 C  CB    . PRO B 297 ? 0.7728 0.9076 0.4906 0.1561  -0.0385 0.0681  1514 PRO B CB    
6042 C  CG    . PRO B 297 ? 0.7378 0.8655 0.4752 0.1488  -0.0407 0.0560  1514 PRO B CG    
6043 C  CD    . PRO B 297 ? 0.8167 0.9332 0.5612 0.1412  -0.0317 0.0559  1514 PRO B CD    
6044 N  N     . CYS B 298 ? 0.7928 0.9568 0.4726 0.1633  -0.0345 0.0550  1515 CYS B N     
6045 C  CA    . CYS B 298 ? 0.9469 1.1267 0.6131 0.1673  -0.0382 0.0420  1515 CYS B CA    
6046 C  C     . CYS B 298 ? 0.9368 1.1302 0.5831 0.1772  -0.0426 0.0506  1515 CYS B C     
6047 O  O     . CYS B 298 ? 0.9490 1.1383 0.5910 0.1806  -0.0408 0.0678  1515 CYS B O     
6048 C  CB    . CYS B 298 ? 1.1309 1.3116 0.7918 0.1648  -0.0298 0.0369  1515 CYS B CB    
6049 S  SG    . CYS B 298 ? 1.1910 1.3623 0.8502 0.1628  -0.0164 0.0553  1515 CYS B SG    
6050 N  N     . GLY B 299 ? 0.9779 1.1872 0.6114 0.1818  -0.0481 0.0384  1516 GLY B N     
6051 C  CA    . GLY B 299 ? 0.9955 1.2198 0.6082 0.1916  -0.0530 0.0444  1516 GLY B CA    
6052 C  C     . GLY B 299 ? 1.0620 1.2940 0.6779 0.1956  -0.0655 0.0393  1516 GLY B C     
6053 O  O     . GLY B 299 ? 1.1253 1.3709 0.7242 0.2044  -0.0713 0.0435  1516 GLY B O     
6054 N  N     . ILE B 300 ? 1.0113 1.2359 0.6483 0.1895  -0.0696 0.0302  1517 ILE B N     
6055 C  CA    . ILE B 300 ? 0.9652 1.1961 0.6093 0.1925  -0.0808 0.0263  1517 ILE B CA    
6056 C  C     . ILE B 300 ? 1.1245 1.3716 0.7645 0.1935  -0.0891 0.0062  1517 ILE B C     
6057 O  O     . ILE B 300 ? 1.1591 1.4040 0.8146 0.1866  -0.0914 -0.0091 1517 ILE B O     
6058 C  CB    . ILE B 300 ? 0.6737 0.8901 0.3423 0.1854  -0.0807 0.0263  1517 ILE B CB    
6059 N  N     . THR B 301 ? 1.1888 1.4525 0.8073 0.2023  -0.0936 0.0064  1518 THR B N     
6060 C  CA    . THR B 301 ? 1.0992 1.3798 0.7110 0.2044  -0.1019 -0.0126 1518 THR B CA    
6061 C  C     . THR B 301 ? 1.2777 1.5674 0.9008 0.2057  -0.1144 -0.0209 1518 THR B C     
6062 O  O     . THR B 301 ? 1.3230 1.6045 0.9621 0.2037  -0.1160 -0.0145 1518 THR B O     
6063 C  CB    . THR B 301 ? 0.8266 1.1229 0.4104 0.2139  -0.1026 -0.0091 1518 THR B CB    
6064 N  N     . ALA B 302 ? 1.3843 1.6919 0.9992 0.2092  -0.1237 -0.0361 1519 ALA B N     
6065 C  CA    . ALA B 302 ? 1.4017 1.7211 1.0262 0.2113  -0.1363 -0.0441 1519 ALA B CA    
6066 C  C     . ALA B 302 ? 1.3522 1.6792 0.9660 0.2218  -0.1417 -0.0280 1519 ALA B C     
6067 O  O     . ALA B 302 ? 1.4015 1.7294 1.0293 0.2228  -0.1482 -0.0258 1519 ALA B O     
6068 C  CB    . ALA B 302 ? 1.4562 1.7931 1.0752 0.2119  -0.1450 -0.0654 1519 ALA B CB    
6069 N  N     . THR B 303 ? 1.2196 1.5526 0.8085 0.2301  -0.1393 -0.0167 1520 THR B N     
6070 C  CA    . THR B 303 ? 1.1192 1.4558 0.7003 0.2385  -0.1424 -0.0004 1520 THR B CA    
6071 C  C     . THR B 303 ? 1.1544 1.4746 0.7363 0.2400  -0.1354 0.0220  1520 THR B C     
6072 O  O     . THR B 303 ? 1.1241 1.4424 0.6954 0.2457  -0.1331 0.0389  1520 THR B O     
6073 C  CB    . THR B 303 ? 0.8196 1.1655 0.3804 0.2431  -0.1403 0.0016  1520 THR B CB    
6074 N  N     . THR B 304 ? 1.1060 1.4097 0.7084 0.2316  -0.1299 0.0219  1521 THR B N     
6075 C  CA    . THR B 304 ? 0.9866 1.2711 0.5947 0.2304  -0.1216 0.0414  1521 THR B CA    
6076 C  C     . THR B 304 ? 1.0286 1.3125 0.6470 0.2356  -0.1295 0.0495  1521 THR B C     
6077 O  O     . THR B 304 ? 1.0179 1.3005 0.6574 0.2313  -0.1340 0.0397  1521 THR B O     
6078 C  CB    . THR B 304 ? 0.7381 1.0046 0.3647 0.2185  -0.1119 0.0370  1521 THR B CB    
6079 N  N     . THR B 305 ? 1.0240 1.3088 0.6278 0.2451  -0.1308 0.0678  1522 THR B N     
6080 C  CA    . THR B 305 ? 1.0426 1.3252 0.6556 0.2512  -0.1380 0.0770  1522 THR B CA    
6081 C  C     . THR B 305 ? 1.0338 1.2950 0.6689 0.2440  -0.1313 0.0825  1522 THR B C     
6082 O  O     . THR B 305 ? 1.1957 1.4406 0.8296 0.2394  -0.1203 0.0932  1522 THR B O     
6083 C  CB    . THR B 305 ? 1.1859 1.4679 0.7838 0.2598  -0.1381 0.0959  1522 THR B CB    
6084 O  OG1   . THR B 305 ? 1.2398 1.5191 0.8490 0.2656  -0.1455 0.1033  1522 THR B OG1   
6085 C  CG2   . THR B 305 ? 1.1828 1.4478 0.7713 0.2577  -0.1253 0.1148  1522 THR B CG2   
6086 N  N     . ASP B 306 ? 1.0132 1.2754 0.6688 0.2432  -0.1381 0.0749  1523 ASP B N     
6087 C  CA    . ASP B 306 ? 1.0471 1.2913 0.7258 0.2352  -0.1326 0.0750  1523 ASP B CA    
6088 C  C     . ASP B 306 ? 1.0525 1.2766 0.7298 0.2365  -0.1248 0.0957  1523 ASP B C     
6089 O  O     . ASP B 306 ? 0.8549 1.0619 0.5449 0.2279  -0.1161 0.0971  1523 ASP B O     
6090 C  CB    . ASP B 306 ? 0.9676 1.2199 0.6648 0.2374  -0.1424 0.0661  1523 ASP B CB    
6091 C  CG    . ASP B 306 ? 0.8765 1.1122 0.5970 0.2309  -0.1377 0.0667  1523 ASP B CG    
6092 O  OD1   . ASP B 306 ? 0.7476 0.9749 0.4785 0.2199  -0.1306 0.0579  1523 ASP B OD1   
6093 O  OD2   . ASP B 306 ? 0.8169 1.0485 0.5447 0.2373  -0.1417 0.0757  1523 ASP B OD2   
6094 N  N     . ASP B 307 ? 1.1170 1.3431 0.7783 0.2467  -0.1276 0.1119  1524 ASP B N     
6095 C  CA    . ASP B 307 ? 1.1373 1.3444 0.7950 0.2477  -0.1199 0.1325  1524 ASP B CA    
6096 C  C     . ASP B 307 ? 1.1384 1.3363 0.7887 0.2396  -0.1075 0.1358  1524 ASP B C     
6097 O  O     . ASP B 307 ? 1.1633 1.3422 0.8232 0.2336  -0.0989 0.1441  1524 ASP B O     
6098 C  CB    . ASP B 307 ? 1.2015 1.4138 0.8407 0.2603  -0.1253 0.1494  1524 ASP B CB    
6099 C  CG    . ASP B 307 ? 1.2012 1.4196 0.8496 0.2691  -0.1371 0.1492  1524 ASP B CG    
6100 O  OD1   . ASP B 307 ? 1.1149 1.3278 0.7861 0.2652  -0.1389 0.1404  1524 ASP B OD1   
6101 O  OD2   . ASP B 307 ? 1.1887 1.4146 0.8262 0.2764  -0.1424 0.1558  1524 ASP B OD2   
6102 N  N     . GLU B 308 ? 1.0709 1.2829 0.7046 0.2396  -0.1065 0.1288  1525 GLU B N     
6103 C  CA    . GLU B 308 ? 0.8407 1.0461 0.4676 0.2325  -0.0948 0.1306  1525 GLU B CA    
6104 C  C     . GLU B 308 ? 0.7663 0.9613 0.4137 0.2206  -0.0891 0.1177  1525 GLU B C     
6105 O  O     . GLU B 308 ? 0.8711 1.0522 0.5219 0.2139  -0.0787 0.1240  1525 GLU B O     
6106 C  CB    . GLU B 308 ? 0.7761 1.0002 0.3809 0.2360  -0.0957 0.1242  1525 GLU B CB    
6107 N  N     . ARG B 309 ? 0.7851 0.9867 0.4468 0.2177  -0.0958 0.1001  1526 ARG B N     
6108 C  CA    . ARG B 309 ? 0.7512 0.9426 0.4322 0.2065  -0.0906 0.0887  1526 ARG B CA    
6109 C  C     . ARG B 309 ? 0.7751 0.9469 0.4724 0.2030  -0.0863 0.0987  1526 ARG B C     
6110 O  O     . ARG B 309 ? 0.7460 0.9041 0.4529 0.1944  -0.0778 0.0984  1526 ARG B O     
6111 C  CB    . ARG B 309 ? 0.8072 1.0104 0.4999 0.2041  -0.0988 0.0686  1526 ARG B CB    
6112 N  N     . ARG B 310 ? 0.8139 0.9841 0.5142 0.2103  -0.0923 0.1079  1527 ARG B N     
6113 C  CA    . ARG B 310 ? 0.8327 0.9839 0.5477 0.2081  -0.0888 0.1178  1527 ARG B CA    
6114 C  C     . ARG B 310 ? 0.8343 0.9709 0.5411 0.2069  -0.0793 0.1354  1527 ARG B C     
6115 O  O     . ARG B 310 ? 0.8237 0.9434 0.5430 0.2000  -0.0724 0.1391  1527 ARG B O     
6116 C  CB    . ARG B 310 ? 0.8149 0.9686 0.5344 0.2173  -0.0980 0.1231  1527 ARG B CB    
6117 C  CG    . ARG B 310 ? 0.7661 0.9307 0.5000 0.2172  -0.1061 0.1072  1527 ARG B CG    
6118 C  CD    . ARG B 310 ? 0.8047 0.9670 0.5457 0.2258  -0.1129 0.1151  1527 ARG B CD    
6119 N  NE    . ARG B 310 ? 0.8708 1.0513 0.6195 0.2296  -0.1233 0.1015  1527 ARG B NE    
6120 C  CZ    . ARG B 310 ? 0.8516 1.0350 0.6188 0.2226  -0.1240 0.0860  1527 ARG B CZ    
6121 N  NH1   . ARG B 310 ? 0.7319 0.9012 0.5101 0.2123  -0.1154 0.0826  1527 ARG B NH1   
6122 N  NH2   . ARG B 310 ? 0.8340 1.0350 0.6093 0.2256  -0.1333 0.0737  1527 ARG B NH2   
6123 N  N     . ARG B 311 ? 0.7859 0.9293 0.4717 0.2134  -0.0788 0.1465  1528 ARG B N     
6124 C  CA    . ARG B 311 ? 0.8319 0.9636 0.5088 0.2121  -0.0695 0.1639  1528 ARG B CA    
6125 C  C     . ARG B 311 ? 0.9756 1.1024 0.6558 0.2018  -0.0593 0.1581  1528 ARG B C     
6126 O  O     . ARG B 311 ? 1.1601 1.2707 0.8480 0.1959  -0.0511 0.1671  1528 ARG B O     
6127 C  CB    . ARG B 311 ? 0.7530 0.8969 0.4051 0.2213  -0.0713 0.1750  1528 ARG B CB    
6128 C  CG    . ARG B 311 ? 0.8619 0.9936 0.5055 0.2243  -0.0659 0.1981  1528 ARG B CG    
6129 C  CD    . ARG B 311 ? 0.8852 1.0308 0.5041 0.2350  -0.0700 0.2089  1528 ARG B CD    
6130 N  NE    . ARG B 311 ? 0.8282 0.9917 0.4292 0.2351  -0.0678 0.2008  1528 ARG B NE    
6131 C  CZ    . ARG B 311 ? 0.8569 1.0197 0.4478 0.2307  -0.0571 0.2068  1528 ARG B CZ    
6132 N  NH1   . ARG B 311 ? 0.8108 0.9559 0.4085 0.2251  -0.0475 0.2210  1528 ARG B NH1   
6133 N  NH2   . ARG B 311 ? 0.8646 1.0440 0.4408 0.2310  -0.0556 0.1973  1528 ARG B NH2   
6134 N  N     . LEU B 312 ? 0.9213 1.0616 0.5970 0.1994  -0.0601 0.1424  1529 LEU B N     
6135 C  CA    . LEU B 312 ? 0.8728 1.0089 0.5529 0.1901  -0.0513 0.1350  1529 LEU B CA    
6136 C  C     . LEU B 312 ? 0.8347 0.9554 0.5379 0.1816  -0.0487 0.1300  1529 LEU B C     
6137 O  O     . LEU B 312 ? 0.7526 0.8610 0.4618 0.1748  -0.0399 0.1350  1529 LEU B O     
6138 C  CB    . LEU B 312 ? 0.9302 1.0831 0.6031 0.1897  -0.0542 0.1174  1529 LEU B CB    
6139 C  CG    . LEU B 312 ? 0.9580 1.1082 0.6343 0.1812  -0.0459 0.1082  1529 LEU B CG    
6140 C  CD1   . LEU B 312 ? 1.0471 1.1987 0.7076 0.1824  -0.0370 0.1198  1529 LEU B CD1   
6141 C  CD2   . LEU B 312 ? 0.9089 1.0722 0.5848 0.1800  -0.0508 0.0878  1529 LEU B CD2   
6142 N  N     . TYR B 313 ? 0.8298 0.9519 0.5463 0.1818  -0.0564 0.1198  1530 TYR B N     
6143 C  CA    . TYR B 313 ? 0.7575 0.8664 0.4950 0.1738  -0.0541 0.1139  1530 TYR B CA    
6144 C  C     . TYR B 313 ? 0.8900 0.9807 0.6345 0.1730  -0.0495 0.1294  1530 TYR B C     
6145 O  O     . TYR B 313 ? 0.9099 0.9879 0.6652 0.1650  -0.0427 0.1295  1530 TYR B O     
6146 C  CB    . TYR B 313 ? 0.6251 0.7411 0.3745 0.1748  -0.0630 0.1007  1530 TYR B CB    
6147 N  N     . GLU B 314 ? 1.0701 1.1594 0.8075 0.1811  -0.0529 0.1432  1531 GLU B N     
6148 C  CA    . GLU B 314 ? 1.0974 1.1687 0.8414 0.1810  -0.0493 0.1584  1531 GLU B CA    
6149 C  C     . GLU B 314 ? 0.9588 1.0213 0.6984 0.1751  -0.0387 0.1682  1531 GLU B C     
6150 O  O     . GLU B 314 ? 1.0808 1.1276 0.8331 0.1687  -0.0334 0.1719  1531 GLU B O     
6151 C  CB    . GLU B 314 ? 1.3568 1.4292 1.0895 0.1915  -0.0542 0.1734  1531 GLU B CB    
6152 C  CG    . GLU B 314 ? 1.5868 1.6401 1.3265 0.1931  -0.0525 0.1896  1531 GLU B CG    
6153 C  CD    . GLU B 314 ? 1.7711 1.8250 1.5126 0.2035  -0.0624 0.1940  1531 GLU B CD    
6154 O  OE1   . GLU B 314 ? 1.7969 1.8677 1.5295 0.2112  -0.0705 0.1889  1531 GLU B OE1   
6155 O  OE2   . GLU B 314 ? 1.8405 1.8776 1.5906 0.2050  -0.0620 0.2047  1531 GLU B OE2   
6156 N  N     . SER B 315 ? 0.8464 0.9200 0.5684 0.1769  -0.0356 0.1710  1532 SER B N     
6157 C  CA    . SER B 315 ? 0.8027 0.8706 0.5202 0.1717  -0.0251 0.1804  1532 SER B CA    
6158 C  C     . SER B 315 ? 0.9229 0.9875 0.6520 0.1618  -0.0194 0.1683  1532 SER B C     
6159 O  O     . SER B 315 ? 0.9440 0.9974 0.6800 0.1554  -0.0115 0.1749  1532 SER B O     
6160 C  CB    . SER B 315 ? 0.7416 0.8247 0.4368 0.1768  -0.0233 0.1850  1532 SER B CB    
6161 O  OG    . SER B 315 ? 0.7485 0.8288 0.4407 0.1710  -0.0126 0.1910  1532 SER B OG    
6162 N  N     . CYS B 316 ? 0.8769 0.9510 0.6091 0.1605  -0.0236 0.1507  1533 CYS B N     
6163 C  CA    . CYS B 316 ? 0.7952 0.8657 0.5386 0.1516  -0.0189 0.1393  1533 CYS B CA    
6164 C  C     . CYS B 316 ? 0.8127 0.8668 0.5757 0.1458  -0.0181 0.1394  1533 CYS B C     
6165 O  O     . CYS B 316 ? 0.8532 0.8982 0.6246 0.1384  -0.0113 0.1397  1533 CYS B O     
6166 C  CB    . CYS B 316 ? 0.7746 0.8580 0.5173 0.1516  -0.0243 0.1208  1533 CYS B CB    
6167 S  SG    . CYS B 316 ? 0.9434 1.0450 0.6654 0.1552  -0.0227 0.1157  1533 CYS B SG    
6168 N  N     . ARG B 317 ? 0.7270 0.7774 0.4971 0.1495  -0.0250 0.1396  1534 ARG B N     
6169 C  CA    . ARG B 317 ? 0.8059 0.8412 0.5940 0.1445  -0.0243 0.1390  1534 ARG B CA    
6170 C  C     . ARG B 317 ? 0.8682 0.8884 0.6589 0.1429  -0.0186 0.1550  1534 ARG B C     
6171 O  O     . ARG B 317 ? 0.8480 0.8559 0.6516 0.1357  -0.0142 0.1545  1534 ARG B O     
6172 C  CB    . ARG B 317 ? 0.7971 0.8342 0.5929 0.1492  -0.0331 0.1331  1534 ARG B CB    
6173 C  CG    . ARG B 317 ? 0.8189 0.8658 0.6212 0.1458  -0.0367 0.1148  1534 ARG B CG    
6174 C  CD    . ARG B 317 ? 0.9174 0.9646 0.7320 0.1481  -0.0436 0.1081  1534 ARG B CD    
6175 N  NE    . ARG B 317 ? 1.0267 1.0908 0.8382 0.1513  -0.0505 0.0963  1534 ARG B NE    
6176 C  CZ    . ARG B 317 ? 1.1238 1.1995 0.9248 0.1601  -0.0568 0.0993  1534 ARG B CZ    
6177 N  NH1   . ARG B 317 ? 1.1923 1.2635 0.9842 0.1666  -0.0568 0.1145  1534 ARG B NH1   
6178 N  NH2   . ARG B 317 ? 1.0898 1.1814 0.8894 0.1622  -0.0634 0.0875  1534 ARG B NH2   
6179 N  N     . GLU B 318 ? 0.8765 0.8977 0.6547 0.1489  -0.0182 0.1694  1535 GLU B N     
6180 C  CA    . GLU B 318 ? 1.0172 1.0242 0.7977 0.1465  -0.0120 0.1853  1535 GLU B CA    
6181 C  C     . GLU B 318 ? 1.0927 1.0988 0.8735 0.1384  -0.0026 0.1860  1535 GLU B C     
6182 O  O     . GLU B 318 ? 1.1957 1.1883 0.9880 0.1321  0.0025  0.1912  1535 GLU B O     
6183 C  CB    . GLU B 318 ? 1.1373 1.1459 0.9032 0.1546  -0.0133 0.2016  1535 GLU B CB    
6184 C  CG    . GLU B 318 ? 1.2927 1.2851 1.0624 0.1517  -0.0071 0.2190  1535 GLU B CG    
6185 C  CD    . GLU B 318 ? 1.4285 1.4249 1.1806 0.1574  -0.0048 0.2361  1535 GLU B CD    
6186 O  OE1   . GLU B 318 ? 1.4586 1.4424 1.2127 0.1549  0.0007  0.2517  1535 GLU B OE1   
6187 O  OE2   . GLU B 318 ? 1.4550 1.4674 1.1913 0.1643  -0.0087 0.2339  1535 GLU B OE2   
6188 N  N     . LEU B 319 ? 1.0348 1.0556 0.8038 0.1388  -0.0003 0.1801  1536 LEU B N     
6189 C  CA    . LEU B 319 ? 0.8846 0.9061 0.6548 0.1318  0.0085  0.1794  1536 LEU B CA    
6190 C  C     . LEU B 319 ? 0.8891 0.9030 0.6767 0.1237  0.0094  0.1676  1536 LEU B C     
6191 O  O     . LEU B 319 ? 0.9071 0.9122 0.7037 0.1170  0.0158  0.1716  1536 LEU B O     
6192 C  CB    . LEU B 319 ? 0.7692 0.8086 0.5238 0.1346  0.0099  0.1731  1536 LEU B CB    
6193 C  CG    . LEU B 319 ? 0.7848 0.8276 0.5396 0.1286  0.0188  0.1711  1536 LEU B CG    
6194 C  CD1   . LEU B 319 ? 0.8627 0.8981 0.6184 0.1256  0.0272  0.1882  1536 LEU B CD1   
6195 C  CD2   . LEU B 319 ? 0.6867 0.7474 0.4252 0.1328  0.0194  0.1639  1536 LEU B CD2   
6196 N  N     . GLU B 320 ? 0.8048 0.8222 0.5975 0.1242  0.0031  0.1532  1537 GLU B N     
6197 C  CA    . GLU B 320 ? 0.7744 0.7851 0.5821 0.1167  0.0041  0.1424  1537 GLU B CA    
6198 C  C     . GLU B 320 ? 0.7293 0.7232 0.5513 0.1128  0.0052  0.1489  1537 GLU B C     
6199 O  O     . GLU B 320 ? 0.5526 0.5391 0.3846 0.1057  0.0099  0.1475  1537 GLU B O     
6200 C  CB    . GLU B 320 ? 0.7953 0.8129 0.6058 0.1179  -0.0029 0.1269  1537 GLU B CB    
6201 C  CG    . GLU B 320 ? 0.8226 0.8327 0.6449 0.1187  -0.0088 0.1242  1537 GLU B CG    
6202 C  CD    . GLU B 320 ? 0.8818 0.9008 0.7069 0.1194  -0.0149 0.1092  1537 GLU B CD    
6203 O  OE1   . GLU B 320 ? 0.5239 0.5375 0.3617 0.1142  -0.0154 0.1007  1537 GLU B OE1   
6204 O  OE2   . GLU B 320 ? 1.0308 1.0628 0.8454 0.1248  -0.0192 0.1057  1537 GLU B OE2   
6205 N  N     . GLN B 321 ? 0.8887 0.8762 0.7116 0.1177  0.0009  0.1565  1538 GLN B N     
6206 C  CA    . GLN B 321 ? 1.1719 1.1429 1.0090 0.1141  0.0015  0.1611  1538 GLN B CA    
6207 C  C     . GLN B 321 ? 1.1373 1.0989 0.9754 0.1104  0.0087  0.1754  1538 GLN B C     
6208 O  O     . GLN B 321 ? 1.1892 1.1389 1.0403 0.1041  0.0114  0.1760  1538 GLN B O     
6209 C  CB    . GLN B 321 ? 1.3682 1.3346 1.2089 0.1204  -0.0059 0.1618  1538 GLN B CB    
6210 C  CG    . GLN B 321 ? 1.5183 1.4907 1.3660 0.1199  -0.0112 0.1451  1538 GLN B CG    
6211 C  CD    . GLN B 321 ? 1.6116 1.5726 1.4756 0.1130  -0.0100 0.1383  1538 GLN B CD    
6212 O  OE1   . GLN B 321 ? 1.7078 1.6549 1.5796 0.1107  -0.0077 0.1457  1538 GLN B OE1   
6213 N  NE2   . GLN B 321 ? 1.5744 1.5415 1.4428 0.1090  -0.0107 0.1245  1538 GLN B NE2   
6214 N  N     . THR B 322 ? 0.9106 0.8778 0.7355 0.1140  0.0117  0.1872  1539 THR B N     
6215 C  CA    . THR B 322 ? 0.9332 0.8935 0.7601 0.1089  0.0197  0.1997  1539 THR B CA    
6216 C  C     . THR B 322 ? 0.9708 0.9352 0.8030 0.1011  0.0258  0.1924  1539 THR B C     
6217 O  O     . THR B 322 ? 1.0969 1.0539 0.9372 0.0949  0.0318  0.1994  1539 THR B O     
6218 C  CB    . THR B 322 ? 1.0445 1.0112 0.8555 0.1138  0.0228  0.2144  1539 THR B CB    
6219 O  OG1   . THR B 322 ? 1.1966 1.1541 1.0128 0.1083  0.0302  0.2278  1539 THR B OG1   
6220 C  CG2   . THR B 322 ? 0.9986 0.9838 0.7953 0.1158  0.0252  0.2087  1539 THR B CG2   
6221 N  N     . PHE B 323 ? 0.8676 0.8437 0.6962 0.1014  0.0244  0.1785  1540 PHE B N     
6222 C  CA    . PHE B 323 ? 0.7675 0.7452 0.6038 0.0943  0.0290  0.1703  1540 PHE B CA    
6223 C  C     . PHE B 323 ? 0.8927 0.8578 0.7459 0.0886  0.0269  0.1639  1540 PHE B C     
6224 O  O     . PHE B 323 ? 0.9492 0.9091 0.8123 0.0818  0.0316  0.1646  1540 PHE B O     
6225 C  CB    . PHE B 323 ? 0.6535 0.6452 0.4821 0.0961  0.0274  0.1569  1540 PHE B CB    
6226 C  CG    . PHE B 323 ? 0.7630 0.7678 0.5769 0.0993  0.0319  0.1608  1540 PHE B CG    
6227 C  CD1   . PHE B 323 ? 0.8308 0.8364 0.6449 0.0958  0.0403  0.1699  1540 PHE B CD1   
6228 C  CD2   . PHE B 323 ? 0.8571 0.8745 0.6570 0.1060  0.0279  0.1554  1540 PHE B CD2   
6229 C  CE1   . PHE B 323 ? 0.8875 0.9065 0.6872 0.0992  0.0451  0.1736  1540 PHE B CE1   
6230 C  CE2   . PHE B 323 ? 0.9151 0.9454 0.7003 0.1094  0.0321  0.1586  1540 PHE B CE2   
6231 C  CZ    . PHE B 323 ? 0.8680 0.8993 0.6527 0.1062  0.0410  0.1678  1540 PHE B CZ    
6232 N  N     . VAL B 324 ? 0.9276 0.8889 0.7846 0.0913  0.0200  0.1575  1541 VAL B N     
6233 C  CA    . VAL B 324 ? 0.8362 0.7865 0.7082 0.0863  0.0180  0.1507  1541 VAL B CA    
6234 C  C     . VAL B 324 ? 0.9205 0.8565 0.8022 0.0826  0.0209  0.1614  1541 VAL B C     
6235 O  O     . VAL B 324 ? 0.8683 0.7975 0.7615 0.0759  0.0233  0.1586  1541 VAL B O     
6236 C  CB    . VAL B 324 ? 0.5757 0.5258 0.4497 0.0907  0.0104  0.1426  1541 VAL B CB    
6237 C  CG1   . VAL B 324 ? 0.5123 0.4528 0.4006 0.0856  0.0089  0.1346  1541 VAL B CG1   
6238 C  CG2   . VAL B 324 ? 0.5208 0.4853 0.3858 0.0939  0.0074  0.1324  1541 VAL B CG2   
6239 N  N     . LYS B 325 ? 0.9957 0.9270 0.8727 0.0869  0.0206  0.1742  1542 LYS B N     
6240 C  CA    . LYS B 325 ? 0.9924 0.9088 0.8789 0.0834  0.0230  0.1851  1542 LYS B CA    
6241 C  C     . LYS B 325 ? 1.0566 0.9735 0.9468 0.0762  0.0309  0.1908  1542 LYS B C     
6242 O  O     . LYS B 325 ? 1.1177 1.0230 1.0207 0.0701  0.0329  0.1938  1542 LYS B O     
6243 C  CB    . LYS B 325 ? 0.8229 0.7343 0.7024 0.0901  0.0211  0.1986  1542 LYS B CB    
6244 N  N     . ALA B 326 ? 0.9176 0.8484 0.7973 0.0767  0.0354  0.1916  1543 ALA B N     
6245 C  CA    . ALA B 326 ? 0.7424 0.6767 0.6264 0.0701  0.0429  0.1944  1543 ALA B CA    
6246 C  C     . ALA B 326 ? 0.8944 0.8324 0.7858 0.0655  0.0428  0.1803  1543 ALA B C     
6247 O  O     . ALA B 326 ? 0.9682 0.9146 0.8595 0.0623  0.0482  0.1793  1543 ALA B O     
6248 C  CB    . ALA B 326 ? 0.6520 0.6003 0.5213 0.0732  0.0484  0.2016  1543 ALA B CB    
6249 N  N     . GLY B 327 ? 0.9523 0.8848 0.8500 0.0656  0.0367  0.1694  1544 GLY B N     
6250 C  CA    . GLY B 327 ? 0.8865 0.8200 0.7925 0.0607  0.0363  0.1573  1544 GLY B CA    
6251 C  C     . GLY B 327 ? 0.8576 0.8046 0.7556 0.0622  0.0370  0.1478  1544 GLY B C     
6252 O  O     . GLY B 327 ? 0.9507 0.8997 0.8548 0.0578  0.0386  0.1407  1544 GLY B O     
6253 N  N     . ILE B 328 ? 0.8474 0.8037 0.7321 0.0686  0.0354  0.1474  1545 ILE B N     
6254 C  CA    . ILE B 328 ? 0.7505 0.7192 0.6274 0.0703  0.0356  0.1378  1545 ILE B CA    
6255 C  C     . ILE B 328 ? 0.8414 0.8109 0.7173 0.0729  0.0286  0.1261  1545 ILE B C     
6256 O  O     . ILE B 328 ? 0.8625 0.8300 0.7354 0.0773  0.0239  0.1278  1545 ILE B O     
6257 C  CB    . ILE B 328 ? 0.6509 0.6312 0.5129 0.0755  0.0388  0.1440  1545 ILE B CB    
6258 C  CG1   . ILE B 328 ? 0.6112 0.5940 0.4749 0.0719  0.0471  0.1532  1545 ILE B CG1   
6259 C  CG2   . ILE B 328 ? 0.5771 0.5692 0.4298 0.0791  0.0363  0.1320  1545 ILE B CG2   
6260 C  CD1   . ILE B 328 ? 0.5571 0.5511 0.4056 0.0770  0.0512  0.1618  1545 ILE B CD1   
6261 N  N     . ARG B 329 ? 0.8413 0.8137 0.7206 0.0701  0.0280  0.1146  1546 ARG B N     
6262 C  CA    . ARG B 329 ? 0.7847 0.7593 0.6632 0.0718  0.0220  0.1033  1546 ARG B CA    
6263 C  C     . ARG B 329 ? 0.8558 0.8426 0.7207 0.0776  0.0207  0.1009  1546 ARG B C     
6264 O  O     . ARG B 329 ? 0.9034 0.8981 0.7635 0.0776  0.0227  0.0952  1546 ARG B O     
6265 C  CB    . ARG B 329 ? 0.6480 0.6208 0.5344 0.0666  0.0220  0.0929  1546 ARG B CB    
6266 C  CG    . ARG B 329 ? 0.7455 0.7070 0.6446 0.0613  0.0222  0.0940  1546 ARG B CG    
6267 C  CD    . ARG B 329 ? 0.7998 0.7598 0.7052 0.0568  0.0214  0.0839  1546 ARG B CD    
6268 N  NE    . ARG B 329 ? 0.7637 0.7290 0.6678 0.0552  0.0255  0.0821  1546 ARG B NE    
6269 C  CZ    . ARG B 329 ? 0.7698 0.7330 0.6795 0.0519  0.0299  0.0872  1546 ARG B CZ    
6270 N  NH1   . ARG B 329 ? 0.8574 0.8128 0.7743 0.0493  0.0308  0.0944  1546 ARG B NH1   
6271 N  NH2   . ARG B 329 ? 0.7815 0.7506 0.6902 0.0513  0.0334  0.0848  1546 ARG B NH2   
6272 N  N     . CYS B 330 ? 0.7286 0.7173 0.5873 0.0831  0.0170  0.1054  1547 CYS B N     
6273 C  CA    . CYS B 330 ? 0.5655 0.5663 0.4104 0.0893  0.0149  0.1040  1547 CYS B CA    
6274 C  C     . CYS B 330 ? 0.6563 0.6596 0.5011 0.0928  0.0073  0.0972  1547 CYS B C     
6275 O  O     . CYS B 330 ? 0.6860 0.6820 0.5376 0.0933  0.0041  0.1000  1547 CYS B O     
6276 C  CB    . CYS B 330 ? 0.5193 0.5226 0.3543 0.0936  0.0178  0.1176  1547 CYS B CB    
6277 S  SG    . CYS B 330 ? 0.7261 0.7434 0.5444 0.1024  0.0128  0.1163  1547 CYS B SG    
6278 N  N     . GLU B 331 ? 0.6419 0.6562 0.4796 0.0952  0.0043  0.0877  1548 GLU B N     
6279 C  CA    . GLU B 331 ? 0.6566 0.6764 0.4933 0.0991  -0.0030 0.0814  1548 GLU B CA    
6280 C  C     . GLU B 331 ? 0.6792 0.7130 0.5015 0.1049  -0.0054 0.0788  1548 GLU B C     
6281 O  O     . GLU B 331 ? 0.6764 0.7157 0.4908 0.1049  -0.0015 0.0778  1548 GLU B O     
6282 C  CB    . GLU B 331 ? 0.7751 0.7933 0.6222 0.0942  -0.0057 0.0687  1548 GLU B CB    
6283 C  CG    . GLU B 331 ? 0.9777 0.9849 0.8375 0.0911  -0.0064 0.0705  1548 GLU B CG    
6284 C  CD    . GLU B 331 ? 1.0624 1.0665 0.9324 0.0847  -0.0067 0.0598  1548 GLU B CD    
6285 O  OE1   . GLU B 331 ? 1.1144 1.1083 0.9929 0.0799  -0.0036 0.0618  1548 GLU B OE1   
6286 O  OE2   . GLU B 331 ? 0.9865 0.9982 0.8558 0.0845  -0.0100 0.0496  1548 GLU B OE2   
6287 N  N     . GLY B 332 ? 0.6605 0.7005 0.4793 0.1104  -0.0120 0.0777  1549 GLY B N     
6288 C  CA    . GLY B 332 ? 0.7904 0.8449 0.5962 0.1161  -0.0159 0.0734  1549 GLY B CA    
6289 C  C     . GLY B 332 ? 0.8010 0.8622 0.6117 0.1143  -0.0213 0.0578  1549 GLY B C     
6290 O  O     . GLY B 332 ? 0.9650 1.0208 0.7885 0.1102  -0.0233 0.0526  1549 GLY B O     
6291 N  N     . ASP B 333 ? 0.6481 0.7214 0.4487 0.1169  -0.0235 0.0501  1550 ASP B N     
6292 C  CA    . ASP B 333 ? 0.6686 0.7493 0.4734 0.1152  -0.0293 0.0352  1550 ASP B CA    
6293 C  C     . ASP B 333 ? 0.8033 0.8980 0.5984 0.1229  -0.0367 0.0338  1550 ASP B C     
6294 O  O     . ASP B 333 ? 0.6648 0.7694 0.4459 0.1272  -0.0373 0.0324  1550 ASP B O     
6295 C  CB    . ASP B 333 ? 0.7591 0.8412 0.5619 0.1112  -0.0262 0.0252  1550 ASP B CB    
6296 C  CG    . ASP B 333 ? 0.8421 0.9316 0.6490 0.1092  -0.0321 0.0096  1550 ASP B CG    
6297 O  OD1   . ASP B 333 ? 0.9076 1.0096 0.7073 0.1141  -0.0384 0.0047  1550 ASP B OD1   
6298 O  OD2   . ASP B 333 ? 0.8335 0.9161 0.6509 0.1023  -0.0305 0.0021  1550 ASP B OD2   
6299 N  N     . TYR B 334 ? 0.8878 0.9840 0.6900 0.1251  -0.0425 0.0344  1551 TYR B N     
6300 C  CA    . TYR B 334 ? 0.8651 0.9751 0.6591 0.1328  -0.0503 0.0334  1551 TYR B CA    
6301 C  C     . TYR B 334 ? 0.9645 1.0833 0.7683 0.1308  -0.0574 0.0191  1551 TYR B C     
6302 O  O     . TYR B 334 ? 1.2111 1.3331 1.0223 0.1336  -0.0627 0.0197  1551 TYR B O     
6303 C  CB    . TYR B 334 ? 0.8507 0.9577 0.6437 0.1392  -0.0523 0.0470  1551 TYR B CB    
6304 C  CG    . TYR B 334 ? 0.9179 1.0109 0.7096 0.1385  -0.0449 0.0617  1551 TYR B CG    
6305 C  CD1   . TYR B 334 ? 1.0658 1.1603 0.8424 0.1423  -0.0410 0.0719  1551 TYR B CD1   
6306 C  CD2   . TYR B 334 ? 0.7967 0.8756 0.6024 0.1338  -0.0418 0.0653  1551 TYR B CD2   
6307 C  CE1   . TYR B 334 ? 1.0291 1.1112 0.8057 0.1409  -0.0340 0.0855  1551 TYR B CE1   
6308 C  CE2   . TYR B 334 ? 0.7317 0.7978 0.5372 0.1326  -0.0354 0.0782  1551 TYR B CE2   
6309 C  CZ    . TYR B 334 ? 0.8535 0.9212 0.6451 0.1359  -0.0315 0.0884  1551 TYR B CZ    
6310 O  OH    . TYR B 334 ? 0.8991 0.9546 0.6917 0.1340  -0.0250 0.1014  1551 TYR B OH    
6311 N  N     . ARG B 335 ? 0.8267 0.9492 0.6320 0.1258  -0.0575 0.0062  1552 ARG B N     
6312 C  CA    . ARG B 335 ? 0.7399 0.8709 0.5552 0.1229  -0.0639 -0.0076 1552 ARG B CA    
6313 C  C     . ARG B 335 ? 0.8670 1.0146 0.6706 0.1284  -0.0706 -0.0149 1552 ARG B C     
6314 O  O     . ARG B 335 ? 1.0154 1.1655 0.8067 0.1296  -0.0684 -0.0171 1552 ARG B O     
6315 C  CB    . ARG B 335 ? 0.6291 0.7525 0.4549 0.1132  -0.0601 -0.0174 1552 ARG B CB    
6316 C  CG    . ARG B 335 ? 0.5612 0.6693 0.3978 0.1078  -0.0538 -0.0111 1552 ARG B CG    
6317 C  CD    . ARG B 335 ? 0.6653 0.7653 0.5085 0.0993  -0.0495 -0.0189 1552 ARG B CD    
6318 N  NE    . ARG B 335 ? 0.8041 0.8998 0.6372 0.0996  -0.0442 -0.0165 1552 ARG B NE    
6319 C  CZ    . ARG B 335 ? 0.9106 0.9997 0.7470 0.0937  -0.0404 -0.0231 1552 ARG B CZ    
6320 N  NH1   . ARG B 335 ? 0.8450 0.9303 0.6941 0.0867  -0.0415 -0.0314 1552 ARG B NH1   
6321 N  NH2   . ARG B 335 ? 0.9875 1.0738 0.8149 0.0949  -0.0355 -0.0208 1552 ARG B NH2   
6322 N  N     . ASP B 336 ? 0.8973 1.0571 0.7048 0.1321  -0.0789 -0.0191 1553 ASP B N     
6323 C  CA    . ASP B 336 ? 0.9834 1.1597 0.7778 0.1385  -0.0859 -0.0247 1553 ASP B CA    
6324 C  C     . ASP B 336 ? 0.9080 1.0919 0.7058 0.1332  -0.0893 -0.0424 1553 ASP B C     
6325 O  O     . ASP B 336 ? 0.9022 1.0999 0.6888 0.1379  -0.0950 -0.0491 1553 ASP B O     
6326 C  CB    . ASP B 336 ? 1.1695 1.3574 0.9642 0.1464  -0.0942 -0.0208 1553 ASP B CB    
6327 C  CG    . ASP B 336 ? 1.3169 1.5054 1.1318 0.1427  -0.0975 -0.0257 1553 ASP B CG    
6328 O  OD1   . ASP B 336 ? 1.3929 1.5870 1.2186 0.1362  -0.1002 -0.0397 1553 ASP B OD1   
6329 O  OD2   . ASP B 336 ? 1.3347 1.5190 1.1548 0.1464  -0.0976 -0.0157 1553 ASP B OD2   
6330 N  N     . ASN B 337 ? 0.8879 1.0630 0.7006 0.1236  -0.0860 -0.0500 1554 ASN B N     
6331 C  CA    . ASN B 337 ? 0.9365 1.1155 0.7546 0.1173  -0.0884 -0.0663 1554 ASN B CA    
6332 C  C     . ASN B 337 ? 0.9845 1.1569 0.7929 0.1154  -0.0830 -0.0699 1554 ASN B C     
6333 O  O     . ASN B 337 ? 1.0622 1.2356 0.8752 0.1101  -0.0847 -0.0835 1554 ASN B O     
6334 C  CB    . ASN B 337 ? 0.9326 1.1055 0.7713 0.1078  -0.0876 -0.0725 1554 ASN B CB    
6335 C  CG    . ASN B 337 ? 1.0137 1.1705 0.8597 0.1043  -0.0799 -0.0617 1554 ASN B CG    
6336 O  OD1   . ASN B 337 ? 1.1117 1.2658 0.9546 0.1095  -0.0784 -0.0494 1554 ASN B OD1   
6337 N  ND2   . ASN B 337 ? 1.0139 1.1597 0.8702 0.0953  -0.0752 -0.0664 1554 ASN B ND2   
6338 N  N     . TYR B 338 ? 0.9219 1.0859 0.7197 0.1184  -0.0759 -0.0584 1555 TYR B N     
6339 C  CA    . TYR B 338 ? 0.8856 1.0442 0.6756 0.1168  -0.0704 -0.0621 1555 TYR B CA    
6340 C  C     . TYR B 338 ? 0.8053 0.9714 0.5746 0.1256  -0.0690 -0.0556 1555 TYR B C     
6341 O  O     . TYR B 338 ? 0.8432 1.0117 0.6049 0.1317  -0.0688 -0.0425 1555 TYR B O     
6342 C  CB    . TYR B 338 ? 0.9787 1.1197 0.7770 0.1107  -0.0616 -0.0559 1555 TYR B CB    
6343 C  CG    . TYR B 338 ? 1.0504 1.1838 0.8675 0.1017  -0.0620 -0.0627 1555 TYR B CG    
6344 C  CD1   . TYR B 338 ? 1.0247 1.1481 0.8529 0.0982  -0.0586 -0.0539 1555 TYR B CD1   
6345 C  CD2   . TYR B 338 ? 1.0814 1.2176 0.9048 0.0967  -0.0659 -0.0778 1555 TYR B CD2   
6346 C  CE1   . TYR B 338 ? 0.9955 1.1127 0.8397 0.0901  -0.0586 -0.0596 1555 TYR B CE1   
6347 C  CE2   . TYR B 338 ? 1.1122 1.2414 0.9525 0.0881  -0.0658 -0.0830 1555 TYR B CE2   
6348 C  CZ    . TYR B 338 ? 1.0665 1.1868 0.9167 0.0850  -0.0620 -0.0736 1555 TYR B CZ    
6349 O  OH    . TYR B 338 ? 1.0669 1.1811 0.9328 0.0765  -0.0615 -0.0783 1555 TYR B OH    
6350 N  N     . SER B 339 ? 0.6801 0.8491 0.4404 0.1261  -0.0677 -0.0645 1556 SER B N     
6351 C  CA    . SER B 339 ? 0.7628 0.9395 0.5030 0.1340  -0.0653 -0.0591 1556 SER B CA    
6352 C  C     . SER B 339 ? 1.0726 1.2375 0.8104 0.1335  -0.0548 -0.0453 1556 SER B C     
6353 O  O     . SER B 339 ? 1.1778 1.3287 0.9286 0.1266  -0.0497 -0.0444 1556 SER B O     
6354 C  CB    . SER B 339 ? 0.7120 0.8959 0.4441 0.1348  -0.0670 -0.0745 1556 SER B CB    
6355 O  OG    . SER B 339 ? 0.5955 0.7662 0.3369 0.1281  -0.0609 -0.0798 1556 SER B OG    
6356 N  N     . PRO B 340 ? 1.1879 1.3584 0.9092 0.1405  -0.0515 -0.0341 1557 PRO B N     
6357 C  CA    . PRO B 340 ? 1.1261 1.2866 0.8459 0.1394  -0.0412 -0.0216 1557 PRO B CA    
6358 C  C     . PRO B 340 ? 0.9666 1.1207 0.6899 0.1350  -0.0352 -0.0301 1557 PRO B C     
6359 O  O     . PRO B 340 ? 0.8299 0.9716 0.5620 0.1303  -0.0281 -0.0235 1557 PRO B O     
6360 C  CB    . PRO B 340 ? 1.1774 1.3487 0.8766 0.1482  -0.0397 -0.0108 1557 PRO B CB    
6361 C  CG    . PRO B 340 ? 1.2584 1.4396 0.9541 0.1531  -0.0493 -0.0103 1557 PRO B CG    
6362 C  CD    . PRO B 340 ? 1.3051 1.4901 1.0109 0.1493  -0.0571 -0.0290 1557 PRO B CD    
6363 N  N     . GLY B 341 ? 0.9512 1.1135 0.6685 0.1364  -0.0384 -0.0453 1558 GLY B N     
6364 C  CA    . GLY B 341 ? 0.8872 1.0428 0.6089 0.1327  -0.0332 -0.0543 1558 GLY B CA    
6365 C  C     . GLY B 341 ? 0.7411 0.8826 0.4830 0.1237  -0.0338 -0.0602 1558 GLY B C     
6366 O  O     . GLY B 341 ? 0.6736 0.8039 0.4231 0.1196  -0.0273 -0.0591 1558 GLY B O     
6367 N  N     . TRP B 342 ? 0.6107 0.7531 0.3618 0.1207  -0.0415 -0.0663 1559 TRP B N     
6368 C  CA    . TRP B 342 ? 0.6371 0.7665 0.4073 0.1120  -0.0417 -0.0695 1559 TRP B CA    
6369 C  C     . TRP B 342 ? 0.8237 0.9410 0.6010 0.1092  -0.0348 -0.0547 1559 TRP B C     
6370 O  O     . TRP B 342 ? 0.8781 0.9832 0.6658 0.1034  -0.0303 -0.0553 1559 TRP B O     
6371 C  CB    . TRP B 342 ? 0.6316 0.7661 0.4103 0.1097  -0.0503 -0.0756 1559 TRP B CB    
6372 C  CG    . TRP B 342 ? 0.8474 0.9701 0.6452 0.1004  -0.0505 -0.0804 1559 TRP B CG    
6373 C  CD1   . TRP B 342 ? 0.9584 1.0793 0.7650 0.0949  -0.0542 -0.0948 1559 TRP B CD1   
6374 C  CD2   . TRP B 342 ? 0.8663 0.9774 0.6763 0.0955  -0.0467 -0.0705 1559 TRP B CD2   
6375 N  NE1   . TRP B 342 ? 0.9491 1.0584 0.7720 0.0869  -0.0526 -0.0937 1559 TRP B NE1   
6376 C  CE2   . TRP B 342 ? 0.8198 0.9235 0.6446 0.0873  -0.0481 -0.0793 1559 TRP B CE2   
6377 C  CE3   . TRP B 342 ? 0.8730 0.9793 0.6826 0.0972  -0.0424 -0.0552 1559 TRP B CE3   
6378 C  CZ2   . TRP B 342 ? 0.7811 0.8739 0.6191 0.0813  -0.0453 -0.0734 1559 TRP B CZ2   
6379 C  CZ3   . TRP B 342 ? 0.8613 0.9564 0.6847 0.0911  -0.0400 -0.0504 1559 TRP B CZ3   
6380 C  CH2   . TRP B 342 ? 0.7869 0.8758 0.6238 0.0834  -0.0413 -0.0595 1559 TRP B CH2   
6381 N  N     . LYS B 343 ? 0.9138 1.0343 0.6861 0.1132  -0.0346 -0.0413 1560 LYS B N     
6382 C  CA    . LYS B 343 ? 0.8666 0.9760 0.6455 0.1108  -0.0287 -0.0271 1560 LYS B CA    
6383 C  C     . LYS B 343 ? 0.7875 0.8909 0.5636 0.1103  -0.0199 -0.0221 1560 LYS B C     
6384 O  O     . LYS B 343 ? 0.6505 0.7417 0.4376 0.1050  -0.0152 -0.0175 1560 LYS B O     
6385 C  CB    . LYS B 343 ? 0.8890 1.0037 0.6610 0.1164  -0.0304 -0.0143 1560 LYS B CB    
6386 N  N     . TYR B 344 ? 0.8897 1.0024 0.6509 0.1160  -0.0176 -0.0231 1561 TYR B N     
6387 C  CA    . TYR B 344 ? 0.9521 1.0621 0.7107 0.1160  -0.0094 -0.0213 1561 TYR B CA    
6388 C  C     . TYR B 344 ? 0.8844 0.9838 0.6560 0.1097  -0.0080 -0.0313 1561 TYR B C     
6389 O  O     . TYR B 344 ? 0.8766 0.9663 0.6562 0.1062  -0.0020 -0.0256 1561 TYR B O     
6390 C  CB    . TYR B 344 ? 1.1386 1.2624 0.8797 0.1231  -0.0085 -0.0259 1561 TYR B CB    
6391 C  CG    . TYR B 344 ? 1.2560 1.3911 0.9809 0.1302  -0.0081 -0.0146 1561 TYR B CG    
6392 C  CD1   . TYR B 344 ? 1.2874 1.4190 1.0142 0.1302  -0.0082 0.0000  1561 TYR B CD1   
6393 C  CD2   . TYR B 344 ? 1.2513 1.4007 0.9585 0.1371  -0.0076 -0.0187 1561 TYR B CD2   
6394 C  CE1   . TYR B 344 ? 1.2887 1.4296 1.0005 0.1369  -0.0081 0.0112  1561 TYR B CE1   
6395 C  CE2   . TYR B 344 ? 1.2142 1.3741 0.9054 0.1437  -0.0072 -0.0076 1561 TYR B CE2   
6396 C  CZ    . TYR B 344 ? 1.2468 1.4020 0.9406 0.1435  -0.0074 0.0078  1561 TYR B CZ    
6397 O  OH    . TYR B 344 ? 1.2934 1.4579 0.9715 0.1501  -0.0072 0.0198  1561 TYR B OH    
6398 N  N     . ASN B 345 ? 0.5455 0.6467 0.3193 0.1084  -0.0138 -0.0463 1562 ASN B N     
6399 C  CA    . ASN B 345 ? 0.5983 0.6888 0.3839 0.1028  -0.0125 -0.0555 1562 ASN B CA    
6400 C  C     . ASN B 345 ? 0.5845 0.6618 0.3858 0.0956  -0.0122 -0.0501 1562 ASN B C     
6401 O  O     . ASN B 345 ? 0.5123 0.5792 0.3220 0.0918  -0.0075 -0.0481 1562 ASN B O     
6402 C  CB    . ASN B 345 ? 0.6807 0.7745 0.4667 0.1021  -0.0191 -0.0726 1562 ASN B CB    
6403 C  CG    . ASN B 345 ? 0.8020 0.8830 0.6005 0.0962  -0.0179 -0.0812 1562 ASN B CG    
6404 O  OD1   . ASN B 345 ? 0.8266 0.8996 0.6376 0.0897  -0.0214 -0.0849 1562 ASN B OD1   
6405 N  ND2   . ASN B 345 ? 0.8329 0.9119 0.6282 0.0986  -0.0127 -0.0838 1562 ASN B ND2   
6406 N  N     . HIS B 346 ? 0.5161 0.5947 0.3216 0.0939  -0.0173 -0.0480 1563 HIS B N     
6407 C  CA    . HIS B 346 ? 0.7931 0.8607 0.6128 0.0874  -0.0172 -0.0435 1563 HIS B CA    
6408 C  C     . HIS B 346 ? 0.7217 0.7810 0.5443 0.0863  -0.0101 -0.0309 1563 HIS B C     
6409 O  O     . HIS B 346 ? 0.4844 0.5327 0.3171 0.0811  -0.0072 -0.0308 1563 HIS B O     
6410 C  CB    . HIS B 346 ? 0.8072 0.8800 0.6289 0.0878  -0.0228 -0.0409 1563 HIS B CB    
6411 C  CG    . HIS B 346 ? 0.6757 0.7387 0.5113 0.0817  -0.0225 -0.0369 1563 HIS B CG    
6412 N  ND1   . HIS B 346 ? 0.6973 0.7575 0.5348 0.0826  -0.0209 -0.0249 1563 HIS B ND1   
6413 C  CD2   . HIS B 346 ? 0.5999 0.6553 0.4477 0.0747  -0.0236 -0.0433 1563 HIS B CD2   
6414 C  CE1   . HIS B 346 ? 0.7269 0.7790 0.5770 0.0767  -0.0210 -0.0248 1563 HIS B CE1   
6415 N  NE2   . HIS B 346 ? 0.7439 0.7932 0.6000 0.0718  -0.0225 -0.0354 1563 HIS B NE2   
6416 N  N     . TRP B 347 ? 0.7106 0.7749 0.5248 0.0911  -0.0076 -0.0199 1564 TRP B N     
6417 C  CA    . TRP B 347 ? 0.7098 0.7665 0.5277 0.0896  -0.0011 -0.0080 1564 TRP B CA    
6418 C  C     . TRP B 347 ? 0.6482 0.7033 0.4649 0.0898  0.0050  -0.0095 1564 TRP B C     
6419 O  O     . TRP B 347 ? 0.7049 0.7520 0.5289 0.0866  0.0098  -0.0029 1564 TRP B O     
6420 C  CB    . TRP B 347 ? 0.7921 0.8538 0.6022 0.0941  0.0000  0.0049  1564 TRP B CB    
6421 C  CG    . TRP B 347 ? 0.7793 0.8418 0.5925 0.0943  -0.0061 0.0062  1564 TRP B CG    
6422 C  CD1   . TRP B 347 ? 0.7266 0.7996 0.5311 0.0995  -0.0117 0.0047  1564 TRP B CD1   
6423 C  CD2   . TRP B 347 ? 0.7181 0.7712 0.5442 0.0894  -0.0076 0.0083  1564 TRP B CD2   
6424 N  NE1   . TRP B 347 ? 0.6397 0.7107 0.4519 0.0983  -0.0164 0.0061  1564 TRP B NE1   
6425 C  CE2   . TRP B 347 ? 0.5652 0.6240 0.3905 0.0921  -0.0137 0.0082  1564 TRP B CE2   
6426 C  CE3   . TRP B 347 ? 0.8071 0.8483 0.6451 0.0833  -0.0044 0.0102  1564 TRP B CE3   
6427 C  CZ2   . TRP B 347 ? 0.5539 0.6071 0.3902 0.0890  -0.0162 0.0095  1564 TRP B CZ2   
6428 C  CZ3   . TRP B 347 ? 0.7893 0.8249 0.6371 0.0801  -0.0070 0.0116  1564 TRP B CZ3   
6429 C  CH2   . TRP B 347 ? 0.6794 0.7210 0.5265 0.0830  -0.0126 0.0111  1564 TRP B CH2   
6430 N  N     . GLU B 348 ? 0.6131 0.6758 0.4215 0.0934  0.0047  -0.0188 1565 GLU B N     
6431 C  CA    . GLU B 348 ? 0.6674 0.7281 0.4765 0.0937  0.0103  -0.0215 1565 GLU B CA    
6432 C  C     . GLU B 348 ? 0.6666 0.7150 0.4893 0.0877  0.0098  -0.0280 1565 GLU B C     
6433 O  O     . GLU B 348 ? 0.6142 0.6571 0.4424 0.0864  0.0148  -0.0253 1565 GLU B O     
6434 C  CB    . GLU B 348 ? 0.7828 0.8546 0.5796 0.0996  0.0099  -0.0312 1565 GLU B CB    
6435 C  CG    . GLU B 348 ? 0.9184 1.0028 0.7003 0.1062  0.0137  -0.0235 1565 GLU B CG    
6436 C  CD    . GLU B 348 ? 1.2471 1.3407 1.0191 0.1116  0.0166  -0.0323 1565 GLU B CD    
6437 O  OE1   . GLU B 348 ? 1.3335 1.4374 1.0936 0.1167  0.0215  -0.0255 1565 GLU B OE1   
6438 O  OE2   . GLU B 348 ? 1.3880 1.4783 1.1639 0.1107  0.0142  -0.0460 1565 GLU B OE2   
6439 N  N     . LEU B 349 ? 0.6807 0.7251 0.5092 0.0840  0.0037  -0.0362 1566 LEU B N     
6440 C  CA    . LEU B 349 ? 0.5755 0.6075 0.4167 0.0778  0.0031  -0.0407 1566 LEU B CA    
6441 C  C     . LEU B 349 ? 0.6746 0.6980 0.5249 0.0734  0.0055  -0.0300 1566 LEU B C     
6442 O  O     . LEU B 349 ? 0.7510 0.7648 0.6099 0.0696  0.0077  -0.0296 1566 LEU B O     
6443 C  CB    . LEU B 349 ? 0.5487 0.5792 0.3941 0.0744  -0.0035 -0.0517 1566 LEU B CB    
6444 C  CG    . LEU B 349 ? 0.6165 0.6516 0.4573 0.0765  -0.0071 -0.0660 1566 LEU B CG    
6445 C  CD1   . LEU B 349 ? 0.4955 0.5337 0.3389 0.0737  -0.0142 -0.0741 1566 LEU B CD1   
6446 C  CD2   . LEU B 349 ? 0.6894 0.7144 0.5366 0.0744  -0.0051 -0.0728 1566 LEU B CD2   
6447 N  N     . LYS B 350 ? 0.7755 0.8019 0.6241 0.0739  0.0045  -0.0216 1567 LYS B N     
6448 C  CA    . LYS B 350 ? 0.7198 0.7383 0.5767 0.0701  0.0065  -0.0119 1567 LYS B CA    
6449 C  C     . LYS B 350 ? 0.6722 0.6901 0.5280 0.0717  0.0129  -0.0023 1567 LYS B C     
6450 O  O     . LYS B 350 ? 0.6116 0.6225 0.4749 0.0683  0.0149  0.0052  1567 LYS B O     
6451 C  CB    . LYS B 350 ? 0.6241 0.6451 0.4809 0.0702  0.0028  -0.0075 1567 LYS B CB    
6452 C  CG    . LYS B 350 ? 0.6139 0.6350 0.4755 0.0671  -0.0031 -0.0169 1567 LYS B CG    
6453 C  CD    . LYS B 350 ? 0.6668 0.6902 0.5306 0.0672  -0.0066 -0.0126 1567 LYS B CD    
6454 C  CE    . LYS B 350 ? 0.6435 0.6580 0.5191 0.0609  -0.0069 -0.0125 1567 LYS B CE    
6455 N  NZ    . LYS B 350 ? 0.5517 0.5683 0.4303 0.0615  -0.0095 -0.0081 1567 LYS B NZ    
6456 N  N     . GLY B 351 ? 0.7429 0.7686 0.5900 0.0765  0.0161  -0.0028 1568 GLY B N     
6457 C  CA    . GLY B 351 ? 0.8003 0.8266 0.6480 0.0775  0.0228  0.0050  1568 GLY B CA    
6458 C  C     . GLY B 351 ? 0.7573 0.7839 0.6047 0.0775  0.0255  0.0185  1568 GLY B C     
6459 O  O     . GLY B 351 ? 0.7542 0.7774 0.6076 0.0755  0.0303  0.0254  1568 GLY B O     
6460 N  N     . VAL B 352 ? 0.7428 0.7731 0.5840 0.0797  0.0224  0.0222  1569 VAL B N     
6461 C  CA    . VAL B 352 ? 0.5984 0.6285 0.4386 0.0803  0.0247  0.0355  1569 VAL B CA    
6462 C  C     . VAL B 352 ? 0.5516 0.5891 0.3850 0.0836  0.0313  0.0423  1569 VAL B C     
6463 O  O     . VAL B 352 ? 0.4933 0.5409 0.3156 0.0885  0.0321  0.0379  1569 VAL B O     
6464 C  CB    . VAL B 352 ? 0.6285 0.6625 0.4622 0.0835  0.0195  0.0373  1569 VAL B CB    
6465 C  CG1   . VAL B 352 ? 0.6819 0.7147 0.5140 0.0848  0.0219  0.0514  1569 VAL B CG1   
6466 C  CG2   . VAL B 352 ? 0.6861 0.7137 0.5282 0.0799  0.0136  0.0308  1569 VAL B CG2   
6467 N  N     . PRO B 353 ? 0.5596 0.5931 0.3994 0.0809  0.0364  0.0522  1570 PRO B N     
6468 C  CA    . PRO B 353 ? 0.5758 0.6171 0.4114 0.0831  0.0437  0.0576  1570 PRO B CA    
6469 C  C     . PRO B 353 ? 0.6659 0.7189 0.4857 0.0893  0.0451  0.0618  1570 PRO B C     
6470 O  O     . PRO B 353 ? 0.7906 0.8536 0.6023 0.0932  0.0481  0.0569  1570 PRO B O     
6471 C  CB    . PRO B 353 ? 0.5671 0.6012 0.4134 0.0784  0.0475  0.0688  1570 PRO B CB    
6472 C  CG    . PRO B 353 ? 0.4683 0.4903 0.3269 0.0731  0.0428  0.0637  1570 PRO B CG    
6473 C  CD    . PRO B 353 ? 0.4688 0.4905 0.3216 0.0752  0.0359  0.0568  1570 PRO B CD    
6474 N  N     . VAL B 354 ? 0.6988 0.7511 0.5137 0.0908  0.0425  0.0699  1571 VAL B N     
6475 C  CA    . VAL B 354 ? 0.7123 0.7755 0.5114 0.0969  0.0437  0.0755  1571 VAL B CA    
6476 C  C     . VAL B 354 ? 0.7811 0.8459 0.5733 0.1004  0.0356  0.0716  1571 VAL B C     
6477 O  O     . VAL B 354 ? 0.9266 0.9826 0.7259 0.0981  0.0310  0.0739  1571 VAL B O     
6478 C  CB    . VAL B 354 ? 0.7197 0.7820 0.5182 0.0963  0.0492  0.0922  1571 VAL B CB    
6479 C  CG1   . VAL B 354 ? 0.7422 0.8115 0.5257 0.1023  0.0473  0.0996  1571 VAL B CG1   
6480 C  CG2   . VAL B 354 ? 0.8541 0.9230 0.6532 0.0956  0.0581  0.0956  1571 VAL B CG2   
6481 N  N     . ARG B 355 ? 0.5402 0.6167 0.3187 0.1060  0.0336  0.0649  1572 ARG B N     
6482 C  CA    . ARG B 355 ? 0.7243 0.8058 0.4939 0.1104  0.0262  0.0624  1572 ARG B CA    
6483 C  C     . ARG B 355 ? 0.8233 0.9122 0.5790 0.1159  0.0284  0.0757  1572 ARG B C     
6484 O  O     . ARG B 355 ? 0.8838 0.9802 0.6312 0.1180  0.0353  0.0811  1572 ARG B O     
6485 C  CB    . ARG B 355 ? 0.7022 0.7928 0.4645 0.1135  0.0220  0.0467  1572 ARG B CB    
6486 C  CG    . ARG B 355 ? 0.6292 0.7298 0.3785 0.1196  0.0152  0.0446  1572 ARG B CG    
6487 C  CD    . ARG B 355 ? 0.8041 0.9160 0.5433 0.1234  0.0130  0.0305  1572 ARG B CD    
6488 N  NE    . ARG B 355 ? 1.0258 1.1325 0.7744 0.1192  0.0153  0.0193  1572 ARG B NE    
6489 C  CZ    . ARG B 355 ? 1.1204 1.2349 0.8620 0.1220  0.0170  0.0089  1572 ARG B CZ    
6490 N  NH1   . ARG B 355 ? 0.8752 1.0037 0.5996 0.1289  0.0167  0.0080  1572 ARG B NH1   
6491 N  NH2   . ARG B 355 ? 1.3445 1.4527 1.0958 0.1184  0.0189  -0.0006 1572 ARG B NH2   
6492 N  N     . ILE B 356 ? 0.7673 0.8540 0.5211 0.1181  0.0230  0.0818  1573 ILE B N     
6493 C  CA    . ILE B 356 ? 0.8061 0.9000 0.5454 0.1242  0.0236  0.0940  1573 ILE B CA    
6494 C  C     . ILE B 356 ? 0.5966 0.7030 0.3224 0.1308  0.0163  0.0855  1573 ILE B C     
6495 O  O     . ILE B 356 ? 0.5888 0.6938 0.3203 0.1303  0.0085  0.0754  1573 ILE B O     
6496 C  CB    . ILE B 356 ? 0.8412 0.9242 0.5869 0.1232  0.0225  0.1079  1573 ILE B CB    
6497 C  CG1   . ILE B 356 ? 0.7552 0.8292 0.5100 0.1177  0.0309  0.1188  1573 ILE B CG1   
6498 C  CG2   . ILE B 356 ? 0.8687 0.9591 0.5988 0.1305  0.0203  0.1186  1573 ILE B CG2   
6499 C  CD1   . ILE B 356 ? 0.7207 0.7857 0.4777 0.1177  0.0316  0.1350  1573 ILE B CD1   
6500 N  N     . GLU B 357 ? 0.6146 0.7340 0.3226 0.1368  0.0188  0.0892  1574 GLU B N     
6501 C  CA    . GLU B 357 ? 0.9932 1.1262 0.6855 0.1442  0.0121  0.0835  1574 GLU B CA    
6502 C  C     . GLU B 357 ? 1.0915 1.2268 0.7724 0.1496  0.0116  0.1005  1574 GLU B C     
6503 O  O     . GLU B 357 ? 1.2516 1.3896 0.9237 0.1509  0.0193  0.1134  1574 GLU B O     
6504 C  CB    . GLU B 357 ? 0.9279 1.0749 0.6067 0.1476  0.0151  0.0739  1574 GLU B CB    
6505 C  CG    . GLU B 357 ? 0.9267 1.0715 0.6155 0.1432  0.0148  0.0561  1574 GLU B CG    
6506 C  CD    . GLU B 357 ? 0.8764 1.0340 0.5526 0.1470  0.0190  0.0472  1574 GLU B CD    
6507 O  OE1   . GLU B 357 ? 0.8976 1.0677 0.5558 0.1533  0.0217  0.0538  1574 GLU B OE1   
6508 O  OE2   . GLU B 357 ? 0.7565 0.9118 0.4406 0.1439  0.0196  0.0336  1574 GLU B OE2   
6509 N  N     . LEU B 358 ? 0.9022 1.0369 0.5836 0.1528  0.0027  0.1007  1575 LEU B N     
6510 C  CA    . LEU B 358 ? 0.8427 0.9779 0.5148 0.1584  0.0007  0.1167  1575 LEU B CA    
6511 C  C     . LEU B 358 ? 0.8017 0.9512 0.4604 0.1663  -0.0089 0.1095  1575 LEU B C     
6512 O  O     . LEU B 358 ? 0.6663 0.8146 0.3335 0.1666  -0.0175 0.1014  1575 LEU B O     
6513 C  CB    . LEU B 358 ? 0.8307 0.9494 0.5191 0.1549  -0.0011 0.1250  1575 LEU B CB    
6514 C  CG    . LEU B 358 ? 0.8499 0.9628 0.5336 0.1590  -0.0009 0.1445  1575 LEU B CG    
6515 C  CD1   . LEU B 358 ? 0.8916 1.0112 0.5681 0.1669  -0.0113 0.1443  1575 LEU B CD1   
6516 C  CD2   . LEU B 358 ? 0.6857 0.8037 0.3544 0.1611  0.0076  0.1589  1575 LEU B CD2   
6517 N  N     . GLY B 359 ? 0.8609 1.0249 0.4990 0.1726  -0.0073 0.1121  1576 GLY B N     
6518 C  CA    . GLY B 359 ? 0.9680 1.1471 0.5909 0.1808  -0.0162 0.1068  1576 GLY B CA    
6519 C  C     . GLY B 359 ? 1.0470 1.2288 0.6558 0.1882  -0.0176 0.1255  1576 GLY B C     
6520 O  O     . GLY B 359 ? 1.0228 1.1935 0.6346 0.1865  -0.0116 0.1427  1576 GLY B O     
6521 N  N     . PHE B 360 ? 1.0513 1.2484 0.6443 0.1965  -0.0259 0.1217  1577 PHE B N     
6522 C  CA    . PHE B 360 ? 1.0607 1.2613 0.6391 0.2046  -0.0286 0.1392  1577 PHE B CA    
6523 C  C     . PHE B 360 ? 1.1404 1.3453 0.7011 0.2067  -0.0184 0.1542  1577 PHE B C     
6524 O  O     . PHE B 360 ? 1.2926 1.4910 0.8483 0.2091  -0.0156 0.1742  1577 PHE B O     
6525 C  CB    . PHE B 360 ? 1.0174 1.2345 0.5834 0.2133  -0.0409 0.1307  1577 PHE B CB    
6526 C  CG    . PHE B 360 ? 1.0137 1.2268 0.5974 0.2122  -0.0512 0.1205  1577 PHE B CG    
6527 C  CD1   . PHE B 360 ? 1.0475 1.2483 0.6422 0.2131  -0.0542 0.1324  1577 PHE B CD1   
6528 C  CD2   . PHE B 360 ? 0.9643 1.1855 0.5547 0.2098  -0.0574 0.0988  1577 PHE B CD2   
6529 C  CE1   . PHE B 360 ? 0.9300 1.1282 0.5417 0.2121  -0.0630 0.1227  1577 PHE B CE1   
6530 C  CE2   . PHE B 360 ? 0.8752 1.0935 0.4829 0.2082  -0.0660 0.0898  1577 PHE B CE2   
6531 C  CZ    . PHE B 360 ? 0.8770 1.0844 0.4951 0.2095  -0.0687 0.1018  1577 PHE B CZ    
6532 N  N     . LYS B 361 ? 1.0064 1.2222 0.5577 0.2058  -0.0126 0.1450  1578 LYS B N     
6533 C  CA    . LYS B 361 ? 1.0018 1.2235 0.5365 0.2077  -0.0021 0.1587  1578 LYS B CA    
6534 C  C     . LYS B 361 ? 1.0636 1.2683 0.6128 0.1998  0.0086  0.1730  1578 LYS B C     
6535 O  O     . LYS B 361 ? 1.1340 1.3364 0.6766 0.2001  0.0155  0.1915  1578 LYS B O     
6536 C  CB    . LYS B 361 ? 0.9454 1.1822 0.4702 0.2080  0.0018  0.1433  1578 LYS B CB    
6537 N  N     . ASP B 362 ? 1.0194 1.2117 0.5909 0.1913  0.0104  0.1633  1579 ASP B N     
6538 C  CA    . ASP B 362 ? 1.0823 1.2579 0.6699 0.1835  0.0188  0.1755  1579 ASP B CA    
6539 C  C     . ASP B 362 ? 1.1103 1.2724 0.7032 0.1846  0.0153  0.1923  1579 ASP B C     
6540 O  O     . ASP B 362 ? 1.2228 1.3751 0.8187 0.1815  0.0229  0.2097  1579 ASP B O     
6541 C  CB    . ASP B 362 ? 1.2057 1.3713 0.8155 0.1750  0.0195  0.1605  1579 ASP B CB    
6542 C  CG    . ASP B 362 ? 1.4081 1.5860 1.0136 0.1748  0.0209  0.1417  1579 ASP B CG    
6543 O  OD1   . ASP B 362 ? 1.4320 1.6109 1.0443 0.1742  0.0131  0.1242  1579 ASP B OD1   
6544 O  OD2   . ASP B 362 ? 1.4850 1.6718 1.0805 0.1753  0.0298  0.1444  1579 ASP B OD2   
6545 N  N     . LEU B 363 ? 1.0214 1.1829 0.6162 0.1892  0.0038  0.1874  1580 LEU B N     
6546 C  CA    . LEU B 363 ? 0.8922 1.0416 0.4912 0.1918  -0.0005 0.2027  1580 LEU B CA    
6547 C  C     . LEU B 363 ? 0.9758 1.1302 0.5544 0.1985  0.0025  0.2231  1580 LEU B C     
6548 O  O     . LEU B 363 ? 1.0488 1.1896 0.6316 0.1971  0.0064  0.2415  1580 LEU B O     
6549 C  CB    . LEU B 363 ? 0.8448 0.9967 0.4482 0.1966  -0.0137 0.1920  1580 LEU B CB    
6550 C  CG    . LEU B 363 ? 0.9202 1.0569 0.5481 0.1912  -0.0180 0.1851  1580 LEU B CG    
6551 C  CD1   . LEU B 363 ? 1.0434 1.1885 0.6726 0.1967  -0.0306 0.1724  1580 LEU B CD1   
6552 C  CD2   . LEU B 363 ? 0.8690 0.9870 0.5069 0.1897  -0.0155 0.2028  1580 LEU B CD2   
6553 N  N     . GLN B 364 ? 0.9697 1.1422 0.5293 0.2044  0.0005  0.2185  1581 GLN B N     
6554 C  CA    . GLN B 364 ? 0.9926 1.1681 0.5406 0.2067  0.0033  0.2325  1581 GLN B CA    
6555 C  C     . GLN B 364 ? 1.0710 1.2396 0.6211 0.2000  0.0169  0.2466  1581 GLN B C     
6556 O  O     . GLN B 364 ? 1.1151 1.2800 0.6600 0.2003  0.0200  0.2626  1581 GLN B O     
6557 C  CB    . GLN B 364 ? 0.9885 1.1849 0.5186 0.2124  -0.0003 0.2213  1581 GLN B CB    
6558 C  CG    . GLN B 364 ? 1.0272 1.2311 0.5550 0.2192  -0.0143 0.2101  1581 GLN B CG    
6559 C  CD    . GLN B 364 ? 1.1165 1.3396 0.6263 0.2249  -0.0177 0.2025  1581 GLN B CD    
6560 O  OE1   . GLN B 364 ? 1.0566 1.2897 0.5572 0.2233  -0.0104 0.1977  1581 GLN B OE1   
6561 N  NE2   . GLN B 364 ? 1.1970 1.4257 0.7018 0.2317  -0.0288 0.2015  1581 GLN B NE2   
6562 N  N     . ASN B 365 ? 1.0503 1.2182 0.6075 0.1939  0.0250  0.2408  1582 ASN B N     
6563 C  CA    . ASN B 365 ? 1.0725 1.2358 0.6333 0.1871  0.0381  0.2532  1582 ASN B CA    
6564 C  C     . ASN B 365 ? 1.0689 1.2132 0.6497 0.1796  0.0428  0.2606  1582 ASN B C     
6565 O  O     . ASN B 365 ? 1.2169 1.3592 0.8038 0.1729  0.0536  0.2658  1582 ASN B O     
6566 C  CB    . ASN B 365 ? 1.0263 1.2061 0.5785 0.1861  0.0457  0.2428  1582 ASN B CB    
6567 C  CG    . ASN B 365 ? 1.1788 1.3663 0.7197 0.1858  0.0538  0.2546  1582 ASN B CG    
6568 O  OD1   . ASN B 365 ? 1.2147 1.3911 0.7605 0.1820  0.0587  0.2726  1582 ASN B OD1   
6569 N  ND2   . ASN B 365 ? 1.2363 1.4425 0.7618 0.1899  0.0547  0.2446  1582 ASN B ND2   
6570 N  N     . ASP B 366 ? 0.9388 1.0698 0.5304 0.1806  0.0347  0.2606  1583 ASP B N     
6571 C  CA    . ASP B 366 ? 0.9130 1.0237 0.5273 0.1726  0.0376  0.2657  1583 ASP B CA    
6572 C  C     . ASP B 366 ? 0.9658 1.0759 0.5940 0.1634  0.0456  0.2550  1583 ASP B C     
6573 O  O     . ASP B 366 ? 0.8967 0.9968 0.5365 0.1560  0.0540  0.2644  1583 ASP B O     
6574 C  CB    . ASP B 366 ? 1.0252 1.1231 0.6412 0.1705  0.0426  0.2882  1583 ASP B CB    
6575 C  CG    . ASP B 366 ? 1.1822 1.2576 0.8197 0.1649  0.0420  0.2944  1583 ASP B CG    
6576 O  OD1   . ASP B 366 ? 1.1522 1.2205 0.8018 0.1654  0.0332  0.2823  1583 ASP B OD1   
6577 O  OD2   . ASP B 366 ? 1.2763 1.3405 0.9222 0.1584  0.0499  0.3084  1583 ASP B OD2   
6578 N  N     . GLN B 367 ? 1.0636 1.1835 0.6923 0.1638  0.0420  0.2345  1584 GLN B N     
6579 C  CA    . GLN B 367 ? 1.0745 1.1955 0.7145 0.1565  0.0485  0.2229  1584 GLN B CA    
6580 C  C     . GLN B 367 ? 1.0352 1.1572 0.6837 0.1561  0.0404  0.2008  1584 GLN B C     
6581 O  O     . GLN B 367 ? 0.9935 1.1145 0.6413 0.1604  0.0302  0.1955  1584 GLN B O     
6582 C  CB    . GLN B 367 ? 1.0568 1.1952 0.6808 0.1583  0.0576  0.2245  1584 GLN B CB    
6583 C  CG    . GLN B 367 ? 1.1224 1.2787 0.7227 0.1681  0.0526  0.2198  1584 GLN B CG    
6584 C  CD    . GLN B 367 ? 1.1644 1.3388 0.7481 0.1704  0.0617  0.2199  1584 GLN B CD    
6585 O  OE1   . GLN B 367 ? 1.1758 1.3513 0.7561 0.1681  0.0719  0.2356  1584 GLN B OE1   
6586 N  NE2   . GLN B 367 ? 1.1020 1.2912 0.6754 0.1750  0.0580  0.2020  1584 GLN B NE2   
6587 N  N     . PHE B 368 ? 0.9801 1.1040 0.6376 0.1506  0.0450  0.1885  1585 PHE B N     
6588 C  CA    . PHE B 368 ? 0.8619 0.9869 0.5278 0.1491  0.0390  0.1676  1585 PHE B CA    
6589 C  C     . PHE B 368 ? 0.7841 0.9155 0.4525 0.1454  0.0467  0.1585  1585 PHE B C     
6590 O  O     . PHE B 368 ? 0.8660 0.9973 0.5360 0.1421  0.0564  0.1685  1585 PHE B O     
6591 C  CB    . PHE B 368 ? 0.8869 0.9945 0.5740 0.1435  0.0342  0.1643  1585 PHE B CB    
6592 C  CG    . PHE B 368 ? 0.8892 0.9837 0.5925 0.1353  0.0417  0.1722  1585 PHE B CG    
6593 C  CD1   . PHE B 368 ? 0.9600 1.0449 0.6656 0.1341  0.0451  0.1907  1585 PHE B CD1   
6594 C  CD2   . PHE B 368 ? 0.8106 0.9020 0.5274 0.1288  0.0450  0.1611  1585 PHE B CD2   
6595 C  CE1   . PHE B 368 ? 1.0349 1.1080 0.7563 0.1261  0.0517  0.1973  1585 PHE B CE1   
6596 C  CE2   . PHE B 368 ? 0.7241 0.8045 0.4562 0.1214  0.0513  0.1677  1585 PHE B CE2   
6597 C  CZ    . PHE B 368 ? 0.9106 0.9821 0.6453 0.1198  0.0546  0.1854  1585 PHE B CZ    
6598 N  N     . VAL B 369 ? 0.7741 0.9106 0.4444 0.1456  0.0426  0.1394  1586 VAL B N     
6599 C  CA    . VAL B 369 ? 0.9058 1.0475 0.5794 0.1426  0.0494  0.1300  1586 VAL B CA    
6600 C  C     . VAL B 369 ? 0.9237 1.0524 0.6187 0.1353  0.0477  0.1197  1586 VAL B C     
6601 O  O     . VAL B 369 ? 0.8907 1.0135 0.5924 0.1346  0.0392  0.1103  1586 VAL B O     
6602 C  CB    . VAL B 369 ? 0.8777 1.0363 0.5351 0.1489  0.0474  0.1161  1586 VAL B CB    
6603 C  CG1   . VAL B 369 ? 0.7702 0.9363 0.4275 0.1476  0.0569  0.1113  1586 VAL B CG1   
6604 C  CG2   . VAL B 369 ? 0.9192 1.0903 0.5543 0.1573  0.0451  0.1243  1586 VAL B CG2   
6605 N  N     . ALA B 370 ? 0.8816 1.0063 0.5875 0.1298  0.0559  0.1220  1587 ALA B N     
6606 C  CA    . ALA B 370 ? 0.9080 1.0214 0.6334 0.1230  0.0552  0.1131  1587 ALA B CA    
6607 C  C     . ALA B 370 ? 0.8802 1.0016 0.6049 0.1236  0.0575  0.0981  1587 ALA B C     
6608 O  O     . ALA B 370 ? 1.0136 1.1470 0.7288 0.1267  0.0645  0.0995  1587 ALA B O     
6609 C  CB    . ALA B 370 ? 0.8820 0.9850 0.6215 0.1164  0.0617  0.1256  1587 ALA B CB    
6610 N  N     . VAL B 371 ? 0.6640 0.7790 0.3984 0.1212  0.0517  0.0835  1588 VAL B N     
6611 C  CA    . VAL B 371 ? 0.7879 0.9078 0.5234 0.1217  0.0527  0.0682  1588 VAL B CA    
6612 C  C     . VAL B 371 ? 0.8042 0.9112 0.5595 0.1146  0.0533  0.0639  1588 VAL B C     
6613 O  O     . VAL B 371 ? 0.8058 0.9011 0.5714 0.1106  0.0476  0.0625  1588 VAL B O     
6614 C  CB    . VAL B 371 ? 0.7645 0.8900 0.4912 0.1260  0.0442  0.0535  1588 VAL B CB    
6615 C  CG1   . VAL B 371 ? 0.5878 0.7160 0.3167 0.1263  0.0447  0.0371  1588 VAL B CG1   
6616 C  CG2   . VAL B 371 ? 0.7847 0.9240 0.4909 0.1334  0.0433  0.0581  1588 VAL B CG2   
6617 N  N     . ARG B 372 ? 0.7941 0.9039 0.5543 0.1136  0.0600  0.0609  1589 ARG B N     
6618 C  CA    . ARG B 372 ? 0.8753 0.9740 0.6538 0.1074  0.0610  0.0579  1589 ARG B CA    
6619 C  C     . ARG B 372 ? 0.8164 0.9111 0.5994 0.1071  0.0558  0.0409  1589 ARG B C     
6620 O  O     . ARG B 372 ? 0.7571 0.8606 0.5308 0.1120  0.0553  0.0303  1589 ARG B O     
6621 C  CB    . ARG B 372 ? 0.9474 1.0513 0.7307 0.1064  0.0706  0.0635  1589 ARG B CB    
6622 C  CG    . ARG B 372 ? 1.0010 1.1093 0.7804 0.1061  0.0768  0.0806  1589 ARG B CG    
6623 C  CD    . ARG B 372 ? 0.9766 1.0962 0.7562 0.1071  0.0867  0.0838  1589 ARG B CD    
6624 N  NE    . ARG B 372 ? 0.9019 1.0156 0.6988 0.1026  0.0887  0.0790  1589 ARG B NE    
6625 C  CZ    . ARG B 372 ? 0.8534 0.9744 0.6569 0.1017  0.0970  0.0826  1589 ARG B CZ    
6626 N  NH1   . ARG B 372 ? 0.8563 0.9908 0.6503 0.1045  0.1049  0.0915  1589 ARG B NH1   
6627 N  NH2   . ARG B 372 ? 0.8215 0.9367 0.6410 0.0980  0.0973  0.0776  1589 ARG B NH2   
6628 N  N     . ARG B 373 ? 0.6801 0.7615 0.4778 0.1013  0.0521  0.0384  1590 ARG B N     
6629 C  CA    . ARG B 373 ? 0.5577 0.6338 0.3605 0.1003  0.0471  0.0235  1590 ARG B CA    
6630 C  C     . ARG B 373 ? 0.7075 0.7863 0.5142 0.1015  0.0520  0.0166  1590 ARG B C     
6631 O  O     . ARG B 373 ? 0.6599 0.7394 0.4646 0.1038  0.0491  0.0033  1590 ARG B O     
6632 C  CB    . ARG B 373 ? 0.5932 0.6550 0.4096 0.0939  0.0424  0.0236  1590 ARG B CB    
6633 C  CG    . ARG B 373 ? 0.5267 0.5814 0.3493 0.0918  0.0372  0.0098  1590 ARG B CG    
6634 C  CD    . ARG B 373 ? 0.5063 0.5674 0.3187 0.0957  0.0318  -0.0016 1590 ARG B CD    
6635 N  NE    . ARG B 373 ? 0.5635 0.6171 0.3832 0.0931  0.0276  -0.0145 1590 ARG B NE    
6636 C  CZ    . ARG B 373 ? 0.6135 0.6657 0.4363 0.0940  0.0301  -0.0222 1590 ARG B CZ    
6637 N  NH1   . ARG B 373 ? 0.7688 0.8282 0.5883 0.0978  0.0368  -0.0189 1590 ARG B NH1   
6638 N  NH2   . ARG B 373 ? 0.5346 0.5782 0.3646 0.0913  0.0261  -0.0327 1590 ARG B NH2   
6639 N  N     . ASP B 374 ? 0.9575 1.0375 0.7708 0.1000  0.0590  0.0251  1591 ASP B N     
6640 C  CA    . ASP B 374 ? 0.8851 0.9706 0.7017 0.1023  0.0647  0.0200  1591 ASP B CA    
6641 C  C     . ASP B 374 ? 0.9746 1.0767 0.7767 0.1087  0.0705  0.0219  1591 ASP B C     
6642 O  O     . ASP B 374 ? 1.1883 1.2964 0.9842 0.1090  0.0743  0.0344  1591 ASP B O     
6643 C  CB    . ASP B 374 ? 0.7215 0.8020 0.5533 0.0974  0.0692  0.0281  1591 ASP B CB    
6644 C  CG    . ASP B 374 ? 0.7125 0.7994 0.5430 0.0963  0.0757  0.0435  1591 ASP B CG    
6645 O  OD1   . ASP B 374 ? 0.6989 0.7882 0.5196 0.0972  0.0748  0.0509  1591 ASP B OD1   
6646 O  OD2   . ASP B 374 ? 0.7628 0.8524 0.6027 0.0945  0.0817  0.0485  1591 ASP B OD2   
6647 N  N     . ASN B 375 ? 0.7615 0.8707 0.5577 0.1140  0.0712  0.0095  1592 ASN B N     
6648 C  CA    . ASN B 375 ? 0.8525 0.9787 0.6342 0.1209  0.0770  0.0088  1592 ASN B CA    
6649 C  C     . ASN B 375 ? 0.8356 0.9695 0.5994 0.1245  0.0740  0.0114  1592 ASN B C     
6650 O  O     . ASN B 375 ? 0.7355 0.8841 0.4849 0.1308  0.0780  0.0098  1592 ASN B O     
6651 C  CB    . ASN B 375 ? 0.8028 0.9377 0.5888 0.1206  0.0873  0.0200  1592 ASN B CB    
6652 C  CG    . ASN B 375 ? 0.7937 0.9311 0.5764 0.1179  0.0907  0.0378  1592 ASN B CG    
6653 O  OD1   . ASN B 375 ? 0.8473 0.9867 0.6174 0.1195  0.0878  0.0424  1592 ASN B OD1   
6654 N  ND2   . ASN B 375 ? 0.8804 1.0175 0.6750 0.1138  0.0970  0.0480  1592 ASN B ND2   
6655 N  N     . GLY B 376 ? 0.8699 0.9952 0.6343 0.1211  0.0674  0.0158  1593 GLY B N     
6656 C  CA    . GLY B 376 ? 0.7616 0.8935 0.5101 0.1252  0.0624  0.0151  1593 GLY B CA    
6657 C  C     . GLY B 376 ? 0.8180 0.9633 0.5514 0.1295  0.0680  0.0272  1593 GLY B C     
6658 O  O     . GLY B 376 ? 0.8816 1.0364 0.5988 0.1349  0.0648  0.0242  1593 GLY B O     
6659 N  N     . ALA B 377 ? 0.9093 1.0564 0.6476 0.1272  0.0764  0.0405  1594 ALA B N     
6660 C  CA    . ALA B 377 ? 0.8245 0.9846 0.5488 0.1309  0.0829  0.0531  1594 ALA B CA    
6661 C  C     . ALA B 377 ? 0.8546 1.0107 0.5722 0.1304  0.0782  0.0647  1594 ALA B C     
6662 O  O     . ALA B 377 ? 0.8648 1.0071 0.5946 0.1249  0.0746  0.0707  1594 ALA B O     
6663 C  CB    . ALA B 377 ? 0.7956 0.9581 0.5292 0.1276  0.0932  0.0646  1594 ALA B CB    
6664 N  N     . LYS B 378 ? 0.9419 1.1106 0.6400 0.1367  0.0782  0.0677  1595 LYS B N     
6665 C  CA    . LYS B 378 ? 0.9982 1.1655 0.6875 0.1379  0.0744  0.0799  1595 LYS B CA    
6666 C  C     . LYS B 378 ? 1.0806 1.2528 0.7657 0.1374  0.0836  0.0993  1595 LYS B C     
6667 O  O     . LYS B 378 ? 1.0474 1.2307 0.7286 0.1388  0.0928  0.1014  1595 LYS B O     
6668 C  CB    . LYS B 378 ? 0.9887 1.1673 0.6586 0.1455  0.0680  0.0718  1595 LYS B CB    
6669 C  CG    . LYS B 378 ? 0.9994 1.1753 0.6734 0.1459  0.0599  0.0513  1595 LYS B CG    
6670 C  CD    . LYS B 378 ? 1.0772 1.2628 0.7341 0.1524  0.0519  0.0438  1595 LYS B CD    
6671 C  CE    . LYS B 378 ? 1.0095 1.1857 0.6757 0.1498  0.0410  0.0310  1595 LYS B CE    
6672 N  NZ    . LYS B 378 ? 0.9856 1.1640 0.6433 0.1527  0.0331  0.0361  1595 LYS B NZ    
6673 N  N     . GLN B 379 ? 1.1588 1.3227 0.8446 0.1354  0.0812  0.1135  1596 GLN B N     
6674 C  CA    . GLN B 379 ? 1.2006 1.3667 0.8831 0.1342  0.0894  0.1333  1596 GLN B CA    
6675 C  C     . GLN B 379 ? 1.2159 1.3738 0.8942 0.1349  0.0836  0.1457  1596 GLN B C     
6676 O  O     . GLN B 379 ? 1.2219 1.3653 0.9128 0.1314  0.0765  0.1436  1596 GLN B O     
6677 C  CB    . GLN B 379 ? 1.1283 1.2863 0.8309 0.1263  0.0966  0.1393  1596 GLN B CB    
6678 C  CG    . GLN B 379 ? 1.0988 1.2541 0.8026 0.1230  0.1032  0.1604  1596 GLN B CG    
6679 C  CD    . GLN B 379 ? 1.0680 1.2071 0.7946 0.1142  0.1038  0.1659  1596 GLN B CD    
6680 O  OE1   . GLN B 379 ? 1.0352 1.1645 0.7754 0.1109  0.0986  0.1544  1596 GLN B OE1   
6681 N  NE2   . GLN B 379 ? 1.0831 1.2190 0.8136 0.1102  0.1102  0.1836  1596 GLN B NE2   
6682 N  N     . THR B 380 ? 1.1499 1.3172 0.8106 0.1399  0.0865  0.1585  1597 THR B N     
6683 C  CA    . THR B 380 ? 1.1138 1.2745 0.7683 0.1421  0.0806  0.1708  1597 THR B CA    
6684 C  C     . THR B 380 ? 1.0669 1.2150 0.7327 0.1360  0.0860  0.1898  1597 THR B C     
6685 O  O     . THR B 380 ? 1.0493 1.2005 0.7196 0.1320  0.0962  0.1980  1597 THR B O     
6686 C  CB    . THR B 380 ? 1.0651 1.2416 0.6937 0.1510  0.0801  0.1755  1597 THR B CB    
6687 O  OG1   . THR B 380 ? 1.1249 1.3088 0.7455 0.1508  0.0911  0.1924  1597 THR B OG1   
6688 C  CG2   . THR B 380 ? 1.0301 1.2216 0.6474 0.1565  0.0774  0.1561  1597 THR B CG2   
6689 N  N     . ILE B 381 ? 0.9825 1.1163 0.6547 0.1351  0.0788  0.1957  1598 ILE B N     
6690 C  CA    . ILE B 381 ? 0.9054 1.0234 0.5918 0.1288  0.0815  0.2110  1598 ILE B CA    
6691 C  C     . ILE B 381 ? 0.9333 1.0443 0.6117 0.1333  0.0752  0.2232  1598 ILE B C     
6692 O  O     . ILE B 381 ? 0.9020 1.0104 0.5787 0.1373  0.0651  0.2147  1598 ILE B O     
6693 C  CB    . ILE B 381 ? 0.8692 0.9722 0.5791 0.1214  0.0785  0.2015  1598 ILE B CB    
6694 C  CG1   . ILE B 381 ? 0.8758 0.9861 0.5927 0.1181  0.0836  0.1884  1598 ILE B CG1   
6695 C  CG2   . ILE B 381 ? 0.8406 0.9273 0.5656 0.1148  0.0812  0.2163  1598 ILE B CG2   
6696 C  CD1   . ILE B 381 ? 0.8520 0.9512 0.5875 0.1129  0.0788  0.1747  1598 ILE B CD1   
6697 N  N     . LYS B 382 ? 0.9643 1.0720 0.6390 0.1324  0.0811  0.2432  1599 LYS B N     
6698 C  CA    . LYS B 382 ? 0.8216 0.9208 0.4902 0.1366  0.0754  0.2566  1599 LYS B CA    
6699 C  C     . LYS B 382 ? 0.8314 0.9098 0.5206 0.1319  0.0694  0.2556  1599 LYS B C     
6700 O  O     . LYS B 382 ? 0.8525 0.9215 0.5605 0.1238  0.0727  0.2521  1599 LYS B O     
6701 C  CB    . LYS B 382 ? 0.7670 0.8674 0.4265 0.1364  0.0842  0.2791  1599 LYS B CB    
6702 N  N     . ARG B 383 ? 0.9032 0.9746 0.5886 0.1373  0.0604  0.2592  1600 ARG B N     
6703 C  CA    . ARG B 383 ? 1.0515 1.1053 0.7558 0.1340  0.0537  0.2546  1600 ARG B CA    
6704 C  C     . ARG B 383 ? 1.0280 1.0642 0.7478 0.1268  0.0589  0.2686  1600 ARG B C     
6705 O  O     . ARG B 383 ? 0.8684 0.8900 0.6062 0.1222  0.0552  0.2634  1600 ARG B O     
6706 C  CB    . ARG B 383 ? 1.1804 1.2318 0.8779 0.1422  0.0428  0.2549  1600 ARG B CB    
6707 C  CG    . ARG B 383 ? 1.3215 1.3909 1.0023 0.1502  0.0367  0.2430  1600 ARG B CG    
6708 C  CD    . ARG B 383 ? 1.3861 1.4565 1.0771 0.1492  0.0292  0.2217  1600 ARG B CD    
6709 N  NE    . ARG B 383 ? 1.3962 1.4512 1.1031 0.1479  0.0223  0.2200  1600 ARG B NE    
6710 C  CZ    . ARG B 383 ? 1.3633 1.4208 1.0724 0.1519  0.0126  0.2081  1600 ARG B CZ    
6711 N  NH1   . ARG B 383 ? 1.3967 1.4707 1.0933 0.1570  0.0081  0.1971  1600 ARG B NH1   
6712 N  NH2   . ARG B 383 ? 1.2682 1.3122 0.9924 0.1507  0.0073  0.2069  1600 ARG B NH2   
6713 N  N     . ALA B 384 ? 1.1467 1.1843 0.8602 0.1253  0.0674  0.2859  1601 ALA B N     
6714 C  CA    . ALA B 384 ? 1.1492 1.1703 0.8788 0.1173  0.0727  0.2986  1601 ALA B CA    
6715 C  C     . ALA B 384 ? 1.1184 1.1384 0.8657 0.1080  0.0781  0.2886  1601 ALA B C     
6716 O  O     . ALA B 384 ? 1.0715 1.0761 0.8379 0.1020  0.0760  0.2857  1601 ALA B O     
6717 C  CB    . ALA B 384 ? 1.0651 1.0890 0.7836 0.1176  0.0811  0.3202  1601 ALA B CB    
6718 N  N     . GLN B 385 ? 1.1806 1.2175 0.9214 0.1075  0.0841  0.2816  1602 GLN B N     
6719 C  CA    . GLN B 385 ? 1.0977 1.1362 0.8537 0.0995  0.0898  0.2729  1602 GLN B CA    
6720 C  C     . GLN B 385 ? 0.9160 0.9516 0.6821 0.0986  0.0826  0.2527  1602 GLN B C     
6721 O  O     . GLN B 385 ? 0.8250 0.8624 0.6031 0.0929  0.0860  0.2436  1602 GLN B O     
6722 C  CB    . GLN B 385 ? 1.0640 1.1225 0.8088 0.1003  0.0991  0.2731  1602 GLN B CB    
6723 N  N     . ALA B 386 ? 0.9097 0.9410 0.6718 0.1042  0.0726  0.2459  1603 ALA B N     
6724 C  CA    . ALA B 386 ? 0.6477 0.6768 0.4187 0.1033  0.0659  0.2273  1603 ALA B CA    
6725 C  C     . ALA B 386 ? 0.8817 0.8974 0.6749 0.0944  0.0670  0.2237  1603 ALA B C     
6726 O  O     . ALA B 386 ? 0.8963 0.9155 0.6971 0.0909  0.0678  0.2108  1603 ALA B O     
6727 C  CB    . ALA B 386 ? 0.6494 0.6747 0.4150 0.1099  0.0555  0.2236  1603 ALA B CB    
6728 N  N     . THR B 387 ? 0.9954 0.9955 0.7993 0.0908  0.0669  0.2347  1604 THR B N     
6729 C  CA    . THR B 387 ? 1.0226 1.0103 0.8472 0.0825  0.0674  0.2305  1604 THR B CA    
6730 C  C     . THR B 387 ? 1.1107 1.1032 0.9437 0.0752  0.0767  0.2335  1604 THR B C     
6731 O  O     . THR B 387 ? 1.1723 1.1567 1.0221 0.0684  0.0769  0.2285  1604 THR B O     
6732 C  CB    . THR B 387 ? 0.8997 0.8685 0.7348 0.0805  0.0640  0.2395  1604 THR B CB    
6733 O  OG1   . THR B 387 ? 1.0176 0.9832 0.8498 0.0794  0.0699  0.2580  1604 THR B OG1   
6734 C  CG2   . THR B 387 ? 0.7909 0.7549 0.6207 0.0877  0.0543  0.2350  1604 THR B CG2   
6735 N  N     . VAL B 388 ? 1.0948 1.1000 0.9172 0.0764  0.0845  0.2420  1605 VAL B N     
6736 C  CA    . VAL B 388 ? 1.0125 1.0245 0.8437 0.0698  0.0935  0.2437  1605 VAL B CA    
6737 C  C     . VAL B 388 ? 0.9796 1.0084 0.8045 0.0724  0.0956  0.2303  1605 VAL B C     
6738 O  O     . VAL B 388 ? 0.9794 1.0097 0.8169 0.0675  0.0976  0.2216  1605 VAL B O     
6739 C  CB    . VAL B 388 ? 1.0692 1.0840 0.8966 0.0679  0.1024  0.2630  1605 VAL B CB    
6740 C  CG1   . VAL B 388 ? 1.1703 1.1665 1.0131 0.0613  0.1021  0.2740  1605 VAL B CG1   
6741 C  CG2   . VAL B 388 ? 1.0743 1.0969 0.8795 0.0763  0.1021  0.2714  1605 VAL B CG2   
6742 N  N     . GLU B 389 ? 1.0211 1.0625 0.8266 0.0803  0.0949  0.2280  1606 GLU B N     
6743 C  CA    . GLU B 389 ? 1.0427 1.0997 0.8418 0.0831  0.0970  0.2150  1606 GLU B CA    
6744 C  C     . GLU B 389 ? 0.9618 1.0138 0.7699 0.0822  0.0898  0.1970  1606 GLU B C     
6745 O  O     . GLU B 389 ? 0.8958 0.9527 0.7117 0.0795  0.0926  0.1877  1606 GLU B O     
6746 C  CB    . GLU B 389 ? 1.1415 1.2122 0.9175 0.0921  0.0962  0.2150  1606 GLU B CB    
6747 C  CG    . GLU B 389 ? 1.2547 1.3366 1.0186 0.0937  0.1053  0.2300  1606 GLU B CG    
6748 C  CD    . GLU B 389 ? 1.3077 1.3946 1.0835 0.0870  0.1157  0.2347  1606 GLU B CD    
6749 O  OE1   . GLU B 389 ? 1.3453 1.4291 1.1242 0.0830  0.1219  0.2515  1606 GLU B OE1   
6750 O  OE2   . GLU B 389 ? 1.3104 1.4041 1.0932 0.0856  0.1175  0.2218  1606 GLU B OE2   
6751 N  N     . MET B 390 ? 0.8720 0.9140 0.6800 0.0844  0.0807  0.1926  1607 MET B N     
6752 C  CA    . MET B 390 ? 0.7279 0.7667 0.5419 0.0841  0.0740  0.1757  1607 MET B CA    
6753 C  C     . MET B 390 ? 0.7535 0.7850 0.5865 0.0765  0.0757  0.1708  1607 MET B C     
6754 O  O     . MET B 390 ? 0.9237 0.9603 0.7595 0.0760  0.0756  0.1584  1607 MET B O     
6755 C  CB    . MET B 390 ? 0.5782 0.6080 0.3903 0.0872  0.0646  0.1733  1607 MET B CB    
6756 C  CG    . MET B 390 ? 0.6011 0.6333 0.4124 0.0893  0.0578  0.1561  1607 MET B CG    
6757 S  SD    . MET B 390 ? 0.7299 0.7800 0.5283 0.0938  0.0600  0.1443  1607 MET B SD    
6758 C  CE    . MET B 390 ? 0.6102 0.6693 0.3888 0.1028  0.0539  0.1435  1607 MET B CE    
6759 N  N     . PRO B 391 ? 0.6270 0.6467 0.4735 0.0705  0.0769  0.1793  1608 PRO B N     
6760 C  CA    . PRO B 391 ? 0.6081 0.6231 0.4719 0.0636  0.0784  0.1738  1608 PRO B CA    
6761 C  C     . PRO B 391 ? 0.6879 0.7158 0.5530 0.0622  0.0863  0.1730  1608 PRO B C     
6762 O  O     . PRO B 391 ? 0.8711 0.9006 0.7446 0.0601  0.0859  0.1624  1608 PRO B O     
6763 C  CB    . PRO B 391 ? 0.6400 0.6410 0.5160 0.0580  0.0786  0.1847  1608 PRO B CB    
6764 C  CG    . PRO B 391 ? 0.5863 0.5804 0.4535 0.0628  0.0732  0.1898  1608 PRO B CG    
6765 C  CD    . PRO B 391 ? 0.5972 0.6054 0.4452 0.0698  0.0755  0.1923  1608 PRO B CD    
6766 N  N     . LYS B 392 ? 0.6169 0.6548 0.4735 0.0639  0.0936  0.1838  1609 LYS B N     
6767 C  CA    . LYS B 392 ? 0.7907 0.8430 0.6482 0.0634  0.1016  0.1821  1609 LYS B CA    
6768 C  C     . LYS B 392 ? 0.8894 0.9502 0.7401 0.0684  0.0988  0.1661  1609 LYS B C     
6769 O  O     . LYS B 392 ? 0.9883 1.0512 0.8492 0.0661  0.0997  0.1571  1609 LYS B O     
6770 C  CB    . LYS B 392 ? 0.7721 0.8357 0.6182 0.0656  0.1098  0.1958  1609 LYS B CB    
6771 N  N     . LEU B 393 ? 0.7770 0.8407 0.6117 0.0751  0.0941  0.1617  1610 LEU B N     
6772 C  CA    . LEU B 393 ? 0.6453 0.7157 0.4731 0.0798  0.0906  0.1460  1610 LEU B CA    
6773 C  C     . LEU B 393 ? 0.7488 0.8095 0.5907 0.0759  0.0854  0.1343  1610 LEU B C     
6774 O  O     . LEU B 393 ? 0.8581 0.9240 0.7038 0.0762  0.0867  0.1243  1610 LEU B O     
6775 C  CB    . LEU B 393 ? 0.5579 0.6297 0.3696 0.0862  0.0842  0.1430  1610 LEU B CB    
6776 C  CG    . LEU B 393 ? 0.7189 0.8068 0.5123 0.0935  0.0864  0.1390  1610 LEU B CG    
6777 C  CD1   . LEU B 393 ? 0.6881 0.7753 0.4701 0.0987  0.0777  0.1320  1610 LEU B CD1   
6778 C  CD2   . LEU B 393 ? 0.6546 0.7506 0.4514 0.0940  0.0896  0.1267  1610 LEU B CD2   
6779 N  N     . LEU B 394 ? 0.5235 0.5700 0.3738 0.0722  0.0797  0.1360  1611 LEU B N     
6780 C  CA    . LEU B 394 ? 0.6857 0.7236 0.5476 0.0689  0.0746  0.1249  1611 LEU B CA    
6781 C  C     . LEU B 394 ? 0.7386 0.7780 0.6141 0.0643  0.0795  0.1239  1611 LEU B C     
6782 O  O     . LEU B 394 ? 0.8339 0.8759 0.7128 0.0648  0.0786  0.1130  1611 LEU B O     
6783 C  CB    . LEU B 394 ? 0.5535 0.5769 0.4216 0.0660  0.0681  0.1268  1611 LEU B CB    
6784 C  CG    . LEU B 394 ? 0.5884 0.6106 0.4447 0.0711  0.0620  0.1256  1611 LEU B CG    
6785 C  CD1   . LEU B 394 ? 0.5673 0.5773 0.4317 0.0687  0.0545  0.1195  1611 LEU B CD1   
6786 C  CD2   . LEU B 394 ? 0.5116 0.5455 0.3538 0.0773  0.0608  0.1169  1611 LEU B CD2   
6787 N  N     . GLU B 395 ? 0.6988 0.7384 0.5819 0.0602  0.0852  0.1356  1612 GLU B N     
6788 C  CA    . GLU B 395 ? 0.8070 0.8503 0.7039 0.0559  0.0899  0.1348  1612 GLU B CA    
6789 C  C     . GLU B 395 ? 0.9144 0.9729 0.8051 0.0605  0.0951  0.1291  1612 GLU B C     
6790 O  O     . GLU B 395 ? 1.1000 1.1606 0.9979 0.0604  0.0946  0.1196  1612 GLU B O     
6791 C  CB    . GLU B 395 ? 0.7978 0.8393 0.7042 0.0503  0.0952  0.1487  1612 GLU B CB    
6792 C  CG    . GLU B 395 ? 0.8122 0.8378 0.7311 0.0443  0.0900  0.1510  1612 GLU B CG    
6793 C  CD    . GLU B 395 ? 0.8938 0.9184 0.8285 0.0372  0.0949  0.1598  1612 GLU B CD    
6794 N  N     . THR B 396 ? 0.7390 0.8083 0.6152 0.0653  0.0995  0.1342  1613 THR B N     
6795 C  CA    . THR B 396 ? 0.6933 0.7780 0.5617 0.0706  0.1047  0.1282  1613 THR B CA    
6796 C  C     . THR B 396 ? 0.6469 0.7303 0.5133 0.0742  0.0989  0.1118  1613 THR B C     
6797 O  O     . THR B 396 ? 0.6027 0.6942 0.4720 0.0764  0.1020  0.1040  1613 THR B O     
6798 C  CB    . THR B 396 ? 0.7003 0.7955 0.5503 0.0759  0.1085  0.1352  1613 THR B CB    
6799 O  OG1   . THR B 396 ? 0.7853 0.8855 0.6385 0.0725  0.1166  0.1504  1613 THR B OG1   
6800 C  CG2   . THR B 396 ? 0.5453 0.6554 0.3837 0.0830  0.1113  0.1250  1613 THR B CG2   
6801 N  N     . ILE B 397 ? 0.6976 0.7709 0.5592 0.0750  0.0906  0.1063  1614 ILE B N     
6802 C  CA    . ILE B 397 ? 0.8024 0.8736 0.6624 0.0778  0.0851  0.0913  1614 ILE B CA    
6803 C  C     . ILE B 397 ? 0.8187 0.8827 0.6952 0.0734  0.0838  0.0859  1614 ILE B C     
6804 O  O     . ILE B 397 ? 0.8320 0.9003 0.7111 0.0756  0.0847  0.0766  1614 ILE B O     
6805 C  CB    . ILE B 397 ? 0.8623 0.9253 0.7145 0.0790  0.0769  0.0875  1614 ILE B CB    
6806 C  CG1   . ILE B 397 ? 0.8293 0.9024 0.6633 0.0853  0.0776  0.0895  1614 ILE B CG1   
6807 C  CG2   . ILE B 397 ? 0.8786 0.9352 0.7348 0.0790  0.0707  0.0733  1614 ILE B CG2   
6808 C  CD1   . ILE B 397 ? 0.7812 0.8501 0.6066 0.0878  0.0693  0.0836  1614 ILE B CD1   
6809 N  N     . HIS B 398 ? 0.7315 0.7850 0.6194 0.0673  0.0818  0.0922  1615 HIS B N     
6810 C  CA    . HIS B 398 ? 0.6646 0.7115 0.5679 0.0628  0.0800  0.0882  1615 HIS B CA    
6811 C  C     . HIS B 398 ? 0.6007 0.6583 0.5106 0.0639  0.0863  0.0866  1615 HIS B C     
6812 O  O     . HIS B 398 ? 0.6130 0.6707 0.5267 0.0657  0.0846  0.0768  1615 HIS B O     
6813 C  CB    . HIS B 398 ? 0.6750 0.7123 0.5891 0.0563  0.0789  0.0971  1615 HIS B CB    
6814 C  CG    . HIS B 398 ? 0.5579 0.5886 0.4868 0.0518  0.0764  0.0930  1615 HIS B CG    
6815 N  ND1   . HIS B 398 ? 0.6648 0.6845 0.5960 0.0503  0.0692  0.0858  1615 HIS B ND1   
6816 C  CD2   . HIS B 398 ? 0.5713 0.6060 0.5132 0.0488  0.0800  0.0951  1615 HIS B CD2   
6817 C  CE1   . HIS B 398 ? 0.7062 0.7228 0.6502 0.0467  0.0684  0.0838  1615 HIS B CE1   
6818 N  NE2   . HIS B 398 ? 0.6728 0.6984 0.6239 0.0458  0.0745  0.0892  1615 HIS B NE2   
6819 N  N     . THR B 399 ? 0.6200 0.6874 0.5308 0.0633  0.0938  0.0964  1616 THR B N     
6820 C  CA    . THR B 399 ? 0.6260 0.7053 0.5450 0.0640  0.1005  0.0959  1616 THR B CA    
6821 C  C     . THR B 399 ? 0.6888 0.7770 0.5990 0.0713  0.1016  0.0848  1616 THR B C     
6822 O  O     . THR B 399 ? 0.7479 0.8374 0.6664 0.0726  0.1011  0.0766  1616 THR B O     
6823 C  CB    . THR B 399 ? 0.5987 0.6889 0.5173 0.0626  0.1091  0.1087  1616 THR B CB    
6824 O  OG1   . THR B 399 ? 0.6102 0.6905 0.5325 0.0568  0.1076  0.1196  1616 THR B OG1   
6825 C  CG2   . THR B 399 ? 0.4848 0.5860 0.4168 0.0613  0.1155  0.1093  1616 THR B CG2   
6826 N  N     . SER B 400 ? 0.6660 0.7583 0.5593 0.0762  0.1015  0.0833  1617 SER B N     
6827 C  CA    . SER B 400 ? 0.6217 0.7233 0.5058 0.0834  0.1028  0.0724  1617 SER B CA    
6828 C  C     . SER B 400 ? 0.5615 0.6529 0.4489 0.0845  0.0953  0.0591  1617 SER B C     
6829 O  O     . SER B 400 ? 0.5539 0.6504 0.4413 0.0891  0.0963  0.0491  1617 SER B O     
6830 C  CB    . SER B 400 ? 0.6955 0.8041 0.5604 0.0883  0.1036  0.0736  1617 SER B CB    
6831 O  OG    . SER B 400 ? 0.9329 1.0456 0.7890 0.0947  0.1016  0.0599  1617 SER B OG    
6832 N  N     . MET B 401 ? 0.4973 0.5741 0.3880 0.0802  0.0880  0.0589  1618 MET B N     
6833 C  CA    . MET B 401 ? 0.6108 0.6771 0.5065 0.0799  0.0815  0.0479  1618 MET B CA    
6834 C  C     . MET B 401 ? 0.7546 0.8198 0.6662 0.0777  0.0829  0.0471  1618 MET B C     
6835 O  O     . MET B 401 ? 0.8352 0.9022 0.7498 0.0814  0.0829  0.0380  1618 MET B O     
6836 C  CB    . MET B 401 ? 0.5755 0.6281 0.4707 0.0757  0.0741  0.0486  1618 MET B CB    
6837 C  CG    . MET B 401 ? 0.5974 0.6506 0.4778 0.0788  0.0707  0.0458  1618 MET B CG    
6838 S  SD    . MET B 401 ? 0.6496 0.6886 0.5310 0.0740  0.0629  0.0478  1618 MET B SD    
6839 C  CE    . MET B 401 ? 0.5266 0.5545 0.4161 0.0720  0.0568  0.0359  1618 MET B CE    
6840 N  N     . TYR B 402 ? 0.7255 0.7881 0.6479 0.0720  0.0841  0.0566  1619 TYR B N     
6841 C  CA    . TYR B 402 ? 0.7183 0.7797 0.6565 0.0694  0.0844  0.0560  1619 TYR B CA    
6842 C  C     . TYR B 402 ? 0.7612 0.8365 0.7029 0.0743  0.0907  0.0528  1619 TYR B C     
6843 O  O     . TYR B 402 ? 0.6637 0.7377 0.6117 0.0769  0.0889  0.0446  1619 TYR B O     
6844 C  CB    . TYR B 402 ? 0.6907 0.7498 0.6392 0.0626  0.0855  0.0670  1619 TYR B CB    
6845 C  CG    . TYR B 402 ? 0.7525 0.8129 0.7176 0.0602  0.0859  0.0666  1619 TYR B CG    
6846 C  CD1   . TYR B 402 ? 0.7892 0.8392 0.7605 0.0591  0.0793  0.0601  1619 TYR B CD1   
6847 C  CD2   . TYR B 402 ? 0.7152 0.7879 0.6897 0.0590  0.0927  0.0729  1619 TYR B CD2   
6848 C  CE1   . TYR B 402 ? 0.7508 0.8026 0.7367 0.0574  0.0790  0.0599  1619 TYR B CE1   
6849 C  CE2   . TYR B 402 ? 0.7498 0.8250 0.7402 0.0570  0.0925  0.0722  1619 TYR B CE2   
6850 C  CZ    . TYR B 402 ? 0.7410 0.8056 0.7367 0.0565  0.0854  0.0656  1619 TYR B CZ    
6851 O  OH    . TYR B 402 ? 0.8603 0.9279 0.8714 0.0550  0.0846  0.0649  1619 TYR B OH    
6852 N  N     . GLU B 403 ? 0.8661 0.9552 0.8036 0.0759  0.0984  0.0591  1620 GLU B N     
6853 C  CA    . GLU B 403 ? 0.8312 0.9355 0.7721 0.0809  0.1052  0.0560  1620 GLU B CA    
6854 C  C     . GLU B 403 ? 0.7596 0.8643 0.6922 0.0883  0.1031  0.0425  1620 GLU B C     
6855 O  O     . GLU B 403 ? 0.8266 0.9351 0.7674 0.0920  0.1040  0.0355  1620 GLU B O     
6856 C  CB    . GLU B 403 ? 0.8794 0.9986 0.8143 0.0815  0.1141  0.0654  1620 GLU B CB    
6857 C  CG    . GLU B 403 ? 0.9258 1.0424 0.8679 0.0737  0.1158  0.0791  1620 GLU B CG    
6858 C  CD    . GLU B 403 ? 1.0884 1.2209 1.0292 0.0734  0.1257  0.0893  1620 GLU B CD    
6859 O  OE1   . GLU B 403 ? 1.2170 1.3608 1.1442 0.0794  0.1305  0.0876  1620 GLU B OE1   
6860 O  OE2   . GLU B 403 ? 1.1510 1.2848 1.1043 0.0670  0.1288  0.0993  1620 GLU B OE2   
6861 N  N     . ARG B 404 ? 0.6583 0.7582 0.5757 0.0906  0.0995  0.0383  1621 ARG B N     
6862 C  CA    . ARG B 404 ? 0.5457 0.6453 0.4559 0.0973  0.0970  0.0246  1621 ARG B CA    
6863 C  C     . ARG B 404 ? 0.6124 0.6998 0.5339 0.0966  0.0911  0.0168  1621 ARG B C     
6864 O  O     . ARG B 404 ? 0.7974 0.8876 0.7214 0.1022  0.0918  0.0074  1621 ARG B O     
6865 C  CB    . ARG B 404 ? 0.4897 0.5848 0.3836 0.0986  0.0927  0.0211  1621 ARG B CB    
6866 C  CG    . ARG B 404 ? 0.6788 0.7744 0.5646 0.1052  0.0902  0.0066  1621 ARG B CG    
6867 C  CD    . ARG B 404 ? 0.7515 0.8431 0.6222 0.1061  0.0850  0.0024  1621 ARG B CD    
6868 N  NE    . ARG B 404 ? 0.9310 1.0109 0.8032 0.0995  0.0795  0.0093  1621 ARG B NE    
6869 C  CZ    . ARG B 404 ? 0.9565 1.0389 0.8220 0.0972  0.0805  0.0196  1621 ARG B CZ    
6870 N  NH1   . ARG B 404 ? 0.8289 0.9254 0.6848 0.1005  0.0869  0.0257  1621 ARG B NH1   
6871 N  NH2   . ARG B 404 ? 0.8636 0.9345 0.7320 0.0918  0.0750  0.0242  1621 ARG B NH2   
6872 N  N     . ALA B 405 ? 0.4966 0.5704 0.4248 0.0902  0.0854  0.0209  1622 ALA B N     
6873 C  CA    . ALA B 405 ? 0.5487 0.6109 0.4872 0.0892  0.0798  0.0151  1622 ALA B CA    
6874 C  C     . ALA B 405 ? 0.6185 0.6872 0.5723 0.0896  0.0832  0.0174  1622 ALA B C     
6875 O  O     . ALA B 405 ? 0.6375 0.7030 0.5980 0.0930  0.0811  0.0100  1622 ALA B O     
6876 C  CB    . ALA B 405 ? 0.4797 0.5269 0.4199 0.0824  0.0730  0.0187  1622 ALA B CB    
6877 N  N     . GLU B 406 ? 0.6954 0.7738 0.6551 0.0864  0.0886  0.0274  1623 GLU B N     
6878 C  CA    . GLU B 406 ? 0.6934 0.7789 0.6692 0.0861  0.0913  0.0298  1623 GLU B CA    
6879 C  C     . GLU B 406 ? 0.5877 0.6864 0.5650 0.0941  0.0967  0.0227  1623 GLU B C     
6880 O  O     . GLU B 406 ? 0.6259 0.7237 0.6138 0.0972  0.0948  0.0171  1623 GLU B O     
6881 C  CB    . GLU B 406 ? 0.7797 0.8725 0.7621 0.0800  0.0959  0.0422  1623 GLU B CB    
6882 C  CG    . GLU B 406 ? 0.8623 0.9634 0.8628 0.0783  0.0985  0.0455  1623 GLU B CG    
6883 C  CD    . GLU B 406 ? 1.1425 1.2570 1.1475 0.0744  0.1063  0.0563  1623 GLU B CD    
6884 O  OE1   . GLU B 406 ? 1.2344 1.3619 1.2317 0.0782  0.1136  0.0574  1623 GLU B OE1   
6885 O  OE2   . GLU B 406 ? 1.2225 1.3342 1.2383 0.0673  0.1050  0.0639  1623 GLU B OE2   
6886 N  N     . ARG B 407 ? 0.5098 0.6202 0.4756 0.0983  0.1027  0.0219  1624 ARG B N     
6887 C  CA    . ARG B 407 ? 0.6188 0.7415 0.5840 0.1068  0.1076  0.0132  1624 ARG B CA    
6888 C  C     . ARG B 407 ? 0.6704 0.7807 0.6343 0.1116  0.1009  0.0004  1624 ARG B C     
6889 O  O     . ARG B 407 ? 0.6848 0.7983 0.6579 0.1170  0.1014  -0.0063 1624 ARG B O     
6890 C  CB    . ARG B 407 ? 0.7251 0.8608 0.6748 0.1107  0.1141  0.0135  1624 ARG B CB    
6891 C  CG    . ARG B 407 ? 0.8936 1.0489 0.8469 0.1099  0.1244  0.0233  1624 ARG B CG    
6892 C  CD    . ARG B 407 ? 1.0378 1.1991 0.9743 0.1089  0.1284  0.0302  1624 ARG B CD    
6893 N  NE    . ARG B 407 ? 1.0694 1.2257 0.9884 0.1141  0.1244  0.0206  1624 ARG B NE    
6894 C  CZ    . ARG B 407 ? 0.9524 1.1026 0.8573 0.1118  0.1214  0.0243  1624 ARG B CZ    
6895 N  NH1   . ARG B 407 ? 0.8109 0.9581 0.7169 0.1048  0.1219  0.0375  1624 ARG B NH1   
6896 N  NH2   . ARG B 407 ? 0.9692 1.1162 0.8597 0.1167  0.1174  0.0143  1624 ARG B NH2   
6897 N  N     . ASP B 408 ? 0.6306 0.7256 0.5853 0.1090  0.0939  -0.0023 1625 ASP B N     
6898 C  CA    . ASP B 408 ? 0.6354 0.7169 0.5896 0.1123  0.0873  -0.0136 1625 ASP B CA    
6899 C  C     . ASP B 408 ? 0.6421 0.7166 0.6124 0.1116  0.0838  -0.0136 1625 ASP B C     
6900 O  O     . ASP B 408 ? 0.7573 0.8326 0.7335 0.1180  0.0838  -0.0216 1625 ASP B O     
6901 C  CB    . ASP B 408 ? 0.5821 0.6489 0.5263 0.1078  0.0805  -0.0143 1625 ASP B CB    
6902 C  CG    . ASP B 408 ? 0.7327 0.7890 0.6716 0.1118  0.0754  -0.0270 1625 ASP B CG    
6903 O  OD1   . ASP B 408 ? 0.7461 0.8094 0.6832 0.1193  0.0782  -0.0362 1625 ASP B OD1   
6904 O  OD2   . ASP B 408 ? 0.7732 0.8145 0.7105 0.1072  0.0686  -0.0278 1625 ASP B OD2   
6905 N  N     . LEU B 409 ? 0.4680 0.5373 0.4459 0.1042  0.0814  -0.0042 1626 LEU B N     
6906 C  CA    . LEU B 409 ? 0.5636 0.6275 0.5562 0.1034  0.0777  -0.0034 1626 LEU B CA    
6907 C  C     . LEU B 409 ? 0.7096 0.7890 0.7138 0.1092  0.0834  -0.0048 1626 LEU B C     
6908 O  O     . LEU B 409 ? 0.7279 0.8039 0.7407 0.1139  0.0806  -0.0106 1626 LEU B O     
6909 C  CB    . LEU B 409 ? 0.4909 0.5500 0.4892 0.0947  0.0752  0.0070  1626 LEU B CB    
6910 C  CG    . LEU B 409 ? 0.4867 0.5324 0.4938 0.0916  0.0678  0.0075  1626 LEU B CG    
6911 C  CD1   . LEU B 409 ? 0.5491 0.5916 0.5582 0.0831  0.0661  0.0169  1626 LEU B CD1   
6912 C  CD2   . LEU B 409 ? 0.5307 0.5831 0.5525 0.0958  0.0683  0.0060  1626 LEU B CD2   
6913 N  N     . GLN B 410 ? 0.7165 0.8134 0.7212 0.1091  0.0914  0.0007  1627 GLN B N     
6914 C  CA    . GLN B 410 ? 0.7576 0.8710 0.7750 0.1139  0.0972  0.0000  1627 GLN B CA    
6915 C  C     . GLN B 410 ? 0.7636 0.8804 0.7785 0.1241  0.0986  -0.0123 1627 GLN B C     
6916 O  O     . GLN B 410 ? 0.7592 0.8838 0.7866 0.1296  0.1002  -0.0159 1627 GLN B O     
6917 C  CB    . GLN B 410 ? 0.8464 0.9780 0.8647 0.1109  0.1061  0.0092  1627 GLN B CB    
6918 C  CG    . GLN B 410 ? 0.9448 1.0728 0.9725 0.1013  0.1039  0.0203  1627 GLN B CG    
6919 C  CD    . GLN B 410 ? 0.9682 1.1123 1.0002 0.0969  0.1121  0.0307  1627 GLN B CD    
6920 O  OE1   . GLN B 410 ? 1.0374 1.1927 1.0597 0.0992  0.1193  0.0321  1627 GLN B OE1   
6921 N  NE2   . GLN B 410 ? 0.8269 0.9723 0.8736 0.0904  0.1110  0.0381  1627 GLN B NE2   
6922 N  N     . SER B 411 ? 0.8243 0.9349 0.8236 0.1270  0.0975  -0.0194 1628 SER B N     
6923 C  CA    . SER B 411 ? 0.7550 0.8674 0.7516 0.1367  0.0983  -0.0322 1628 SER B CA    
6924 C  C     . SER B 411 ? 0.7181 0.8116 0.7193 0.1390  0.0898  -0.0398 1628 SER B C     
6925 O  O     . SER B 411 ? 0.8163 0.9103 0.8203 0.1474  0.0899  -0.0501 1628 SER B O     
6926 C  CB    . SER B 411 ? 0.6706 0.7857 0.6488 0.1393  0.1007  -0.0378 1628 SER B CB    
6927 O  OG    . SER B 411 ? 0.7273 0.8610 0.7007 0.1382  0.1092  -0.0304 1628 SER B OG    
6928 N  N     . HIS B 412 ? 0.6716 0.7488 0.6746 0.1319  0.0826  -0.0347 1629 HIS B N     
6929 C  CA    . HIS B 412 ? 0.7152 0.7744 0.7235 0.1333  0.0747  -0.0399 1629 HIS B CA    
6930 C  C     . HIS B 412 ? 0.7769 0.8354 0.8015 0.1323  0.0720  -0.0344 1629 HIS B C     
6931 O  O     . HIS B 412 ? 0.7827 0.8260 0.8118 0.1333  0.0652  -0.0370 1629 HIS B O     
6932 C  CB    . HIS B 412 ? 0.7063 0.7472 0.7043 0.1268  0.0681  -0.0393 1629 HIS B CB    
6933 C  CG    . HIS B 412 ? 0.8661 0.9047 0.8499 0.1295  0.0685  -0.0482 1629 HIS B CG    
6934 N  ND1   . HIS B 412 ? 0.8885 0.9429 0.8633 0.1323  0.0752  -0.0495 1629 HIS B ND1   
6935 C  CD2   . HIS B 412 ? 0.8957 0.9186 0.8730 0.1301  0.0628  -0.0566 1629 HIS B CD2   
6936 C  CE1   . HIS B 412 ? 0.9139 0.9628 0.8767 0.1346  0.0732  -0.0587 1629 HIS B CE1   
6937 N  NE2   . HIS B 412 ? 0.9146 0.9444 0.8794 0.1331  0.0658  -0.0634 1629 HIS B NE2   
6938 N  N     . THR B 413 ? 0.8063 0.8802 0.8398 0.1299  0.0767  -0.0263 1630 THR B N     
6939 C  CA    . THR B 413 ? 0.7676 0.8435 0.8176 0.1300  0.0742  -0.0223 1630 THR B CA    
6940 C  C     . THR B 413 ? 0.8312 0.9244 0.8924 0.1388  0.0798  -0.0269 1630 THR B C     
6941 O  O     . THR B 413 ? 0.8582 0.9707 0.9204 0.1398  0.0881  -0.0251 1630 THR B O     
6942 C  CB    . THR B 413 ? 0.6122 0.6920 0.6672 0.1207  0.0742  -0.0107 1630 THR B CB    
6943 O  OG1   . THR B 413 ? 0.6926 0.7569 0.7362 0.1135  0.0695  -0.0076 1630 THR B OG1   
6944 C  CG2   . THR B 413 ? 0.4664 0.5454 0.5374 0.1206  0.0694  -0.0077 1630 THR B CG2   
6945 N  N     . LYS B 414 ? 0.4715 0.5582 0.5417 0.1453  0.0752  -0.0325 1631 LYS B N     
6946 C  CA    . LYS B 414 ? 0.6253 0.7273 0.7080 0.1546  0.0793  -0.0376 1631 LYS B CA    
6947 C  C     . LYS B 414 ? 0.8150 0.9172 0.9145 0.1539  0.0743  -0.0324 1631 LYS B C     
6948 O  O     . LYS B 414 ? 0.8804 0.9658 0.9794 0.1492  0.0663  -0.0286 1631 LYS B O     
6949 C  CB    . LYS B 414 ? 0.5183 0.6120 0.5969 0.1646  0.0779  -0.0504 1631 LYS B CB    
6950 C  CG    . LYS B 414 ? 0.6170 0.7041 0.6773 0.1642  0.0795  -0.0563 1631 LYS B CG    
6951 C  CD    . LYS B 414 ? 0.7495 0.8588 0.8054 0.1678  0.0897  -0.0587 1631 LYS B CD    
6952 C  CE    . LYS B 414 ? 0.8216 0.9277 0.8586 0.1629  0.0914  -0.0586 1631 LYS B CE    
6953 N  NZ    . LYS B 414 ? 0.8034 0.9262 0.8383 0.1563  0.0983  -0.0478 1631 LYS B NZ    
6954 N  N     . LEU B 415 ? 0.7690 0.8916 0.8834 0.1584  0.0792  -0.0320 1632 LEU B N     
6955 C  CA    . LEU B 415 ? 0.6878 0.8143 0.8194 0.1584  0.0748  -0.0275 1632 LEU B CA    
6956 C  C     . LEU B 415 ? 0.6999 0.8308 0.8424 0.1708  0.0742  -0.0362 1632 LEU B C     
6957 O  O     . LEU B 415 ? 0.8142 0.9581 0.9567 0.1783  0.0815  -0.0433 1632 LEU B O     
6958 C  CB    . LEU B 415 ? 0.7105 0.8585 0.8530 0.1523  0.0806  -0.0191 1632 LEU B CB    
6959 C  CG    . LEU B 415 ? 0.6295 0.7893 0.7931 0.1535  0.0778  -0.0157 1632 LEU B CG    
6960 C  CD1   . LEU B 415 ? 0.5563 0.7027 0.7205 0.1445  0.0693  -0.0080 1632 LEU B CD1   
6961 C  CD2   . LEU B 415 ? 0.6240 0.8116 0.7997 0.1521  0.0875  -0.0121 1632 LEU B CD2   
6962 N  N     . THR B 416 ? 0.6105 0.7309 0.7621 0.1735  0.0657  -0.0356 1633 THR B N     
6963 C  CA    . THR B 416 ? 0.5523 0.6751 0.7149 0.1860  0.0643  -0.0437 1633 THR B CA    
6964 C  C     . THR B 416 ? 0.5471 0.6667 0.7240 0.1870  0.0559  -0.0389 1633 THR B C     
6965 O  O     . THR B 416 ? 0.4747 0.5822 0.6483 0.1787  0.0493  -0.0314 1633 THR B O     
6966 C  CB    . THR B 416 ? 0.5965 0.6990 0.7471 0.1925  0.0614  -0.0534 1633 THR B CB    
6967 O  OG1   . THR B 416 ? 0.7086 0.8157 0.8706 0.2056  0.0614  -0.0621 1633 THR B OG1   
6968 C  CG2   . THR B 416 ? 0.4978 0.5730 0.6407 0.1876  0.0514  -0.0499 1633 THR B CG2   
6969 N  N     . LYS B 417 ? 0.6137 0.7440 0.8059 0.1979  0.0558  -0.0440 1634 LYS B N     
6970 C  CA    . LYS B 417 ? 0.7085 0.8360 0.9146 0.2013  0.0472  -0.0407 1634 LYS B CA    
6971 C  C     . LYS B 417 ? 0.9426 1.0512 1.1486 0.2122  0.0406  -0.0477 1634 LYS B C     
6972 O  O     . LYS B 417 ? 0.9654 1.0677 1.1806 0.2157  0.0322  -0.0446 1634 LYS B O     
6973 C  CB    . LYS B 417 ? 0.5183 0.6752 0.7456 0.2047  0.0515  -0.0394 1634 LYS B CB    
6974 N  N     . GLN B 418 ? 1.0220 1.1209 1.2175 0.2177  0.0438  -0.0570 1635 GLN B N     
6975 C  CA    . GLN B 418 ? 1.0645 1.1424 1.2587 0.2274  0.0377  -0.0642 1635 GLN B CA    
6976 C  C     . GLN B 418 ? 0.9519 1.0010 1.1280 0.2225  0.0332  -0.0653 1635 GLN B C     
6977 O  O     . GLN B 418 ? 0.8548 0.9011 1.0167 0.2174  0.0380  -0.0683 1635 GLN B O     
6978 C  CB    . GLN B 418 ? 1.1648 1.2536 1.3671 0.2412  0.0430  -0.0763 1635 GLN B CB    
6979 C  CG    . GLN B 418 ? 1.4233 1.4875 1.6273 0.2502  0.0340  -0.0809 1635 GLN B CG    
6980 C  CD    . GLN B 418 ? 1.4893 1.5517 1.7076 0.2540  0.0255  -0.0743 1635 GLN B CD    
6981 O  OE1   . GLN B 418 ? 1.5785 1.6180 1.7898 0.2492  0.0171  -0.0682 1635 GLN B OE1   
6982 N  NE2   . GLN B 418 ? 1.4372 1.5201 1.6748 0.2640  0.0268  -0.0767 1635 GLN B NE2   
6983 N  N     . TRP B 419 ? 0.9202 0.9485 1.0979 0.2247  0.0236  -0.0626 1636 TRP B N     
6984 C  CA    . TRP B 419 ? 0.8997 0.8986 1.0638 0.2214  0.0178  -0.0631 1636 TRP B CA    
6985 C  C     . TRP B 419 ? 0.8824 0.8730 1.0373 0.2258  0.0219  -0.0751 1636 TRP B C     
6986 O  O     . TRP B 419 ? 0.8130 0.7896 0.9529 0.2181  0.0218  -0.0756 1636 TRP B O     
6987 C  CB    . TRP B 419 ? 0.9494 0.9327 1.1220 0.2285  0.0084  -0.0607 1636 TRP B CB    
6988 C  CG    . TRP B 419 ? 0.9322 0.8855 1.0934 0.2255  0.0021  -0.0601 1636 TRP B CG    
6989 C  CD1   . TRP B 419 ? 0.7437 0.6770 0.9042 0.2335  -0.0010 -0.0677 1636 TRP B CD1   
6990 C  CD2   . TRP B 419 ? 0.9799 0.9192 1.1287 0.2131  -0.0016 -0.0512 1636 TRP B CD2   
6991 N  NE1   . TRP B 419 ? 0.7763 0.6837 0.9249 0.2259  -0.0064 -0.0635 1636 TRP B NE1   
6992 C  CE2   . TRP B 419 ? 0.9017 0.8131 1.0428 0.2135  -0.0067 -0.0533 1636 TRP B CE2   
6993 C  CE3   . TRP B 419 ? 0.9637 0.9116 1.1077 0.2016  -0.0010 -0.0419 1636 TRP B CE3   
6994 C  CZ2   . TRP B 419 ? 0.9103 0.8037 1.0391 0.2028  -0.0108 -0.0461 1636 TRP B CZ2   
6995 C  CZ3   . TRP B 419 ? 0.9366 0.8667 1.0684 0.1918  -0.0052 -0.0355 1636 TRP B CZ3   
6996 C  CH2   . TRP B 419 ? 0.9350 0.8387 1.0593 0.1923  -0.0099 -0.0373 1636 TRP B CH2   
6997 N  N     . ALA B 420 ? 0.8184 0.8175 0.9825 0.2384  0.0251  -0.0853 1637 ALA B N     
6998 C  CA    . ALA B 420 ? 0.7311 0.7222 0.8870 0.2437  0.0284  -0.0981 1637 ALA B CA    
6999 C  C     . ALA B 420 ? 0.8141 0.8152 0.9559 0.2353  0.0359  -0.0995 1637 ALA B C     
7000 O  O     . ALA B 420 ? 0.7818 0.7665 0.9094 0.2302  0.0347  -0.1030 1637 ALA B O     
7001 C  CB    . ALA B 420 ? 0.6649 0.6694 0.8341 0.2588  0.0320  -0.1089 1637 ALA B CB    
7002 N  N     . GLU B 421 ? 0.8399 0.8681 0.9855 0.2332  0.0434  -0.0961 1638 GLU B N     
7003 C  CA    . GLU B 421 ? 0.8245 0.8626 0.9565 0.2256  0.0505  -0.0963 1638 GLU B CA    
7004 C  C     . GLU B 421 ? 0.6916 0.7202 0.8135 0.2114  0.0473  -0.0850 1638 GLU B C     
7005 O  O     . GLU B 421 ? 0.6699 0.6986 0.7778 0.2048  0.0508  -0.0855 1638 GLU B O     
7006 C  CB    . GLU B 421 ? 0.8913 0.9612 1.0303 0.2280  0.0604  -0.0961 1638 GLU B CB    
7007 C  CG    . GLU B 421 ? 1.0091 1.0951 1.1667 0.2300  0.0601  -0.0890 1638 GLU B CG    
7008 C  CD    . GLU B 421 ? 1.1312 1.2482 1.2940 0.2288  0.0705  -0.0868 1638 GLU B CD    
7009 O  OE1   . GLU B 421 ? 1.1784 1.3021 1.3282 0.2252  0.0774  -0.0889 1638 GLU B OE1   
7010 O  OE2   . GLU B 421 ? 1.1552 1.2902 1.3351 0.2313  0.0718  -0.0827 1638 GLU B OE2   
7011 N  N     . PHE B 422 ? 0.5384 0.5592 0.6669 0.2072  0.0405  -0.0753 1639 PHE B N     
7012 C  CA    . PHE B 422 ? 0.6667 0.6733 0.7848 0.1949  0.0360  -0.0662 1639 PHE B CA    
7013 C  C     . PHE B 422 ? 0.7099 0.6926 0.8143 0.1927  0.0324  -0.0718 1639 PHE B C     
7014 O  O     . PHE B 422 ? 0.6006 0.5795 0.6919 0.1840  0.0339  -0.0701 1639 PHE B O     
7015 C  CB    . PHE B 422 ? 0.7109 0.7116 0.8387 0.1932  0.0284  -0.0569 1639 PHE B CB    
7016 C  CG    . PHE B 422 ? 0.6755 0.6615 0.7938 0.1814  0.0231  -0.0475 1639 PHE B CG    
7017 C  CD1   . PHE B 422 ? 0.7654 0.7628 0.8865 0.1734  0.0233  -0.0378 1639 PHE B CD1   
7018 C  CD2   . PHE B 422 ? 0.5625 0.5234 0.6707 0.1787  0.0176  -0.0485 1639 PHE B CD2   
7019 C  CE1   . PHE B 422 ? 0.8140 0.7985 0.9267 0.1634  0.0184  -0.0299 1639 PHE B CE1   
7020 C  CE2   . PHE B 422 ? 0.6319 0.5807 0.7320 0.1684  0.0131  -0.0400 1639 PHE B CE2   
7021 C  CZ    . PHE B 422 ? 0.7651 0.7258 0.8671 0.1610  0.0135  -0.0310 1639 PHE B CZ    
7022 N  N     . LEU B 423 ? 0.7376 0.7039 0.8456 0.2009  0.0277  -0.0785 1640 LEU B N     
7023 C  CA    . LEU B 423 ? 0.6906 0.6333 0.7878 0.1992  0.0240  -0.0845 1640 LEU B CA    
7024 C  C     . LEU B 423 ? 0.6635 0.6133 0.7510 0.2007  0.0303  -0.0953 1640 LEU B C     
7025 O  O     . LEU B 423 ? 0.6131 0.5507 0.6881 0.1943  0.0292  -0.0977 1640 LEU B O     
7026 C  CB    . LEU B 423 ? 0.5809 0.5055 0.6863 0.2085  0.0178  -0.0895 1640 LEU B CB    
7027 C  CG    . LEU B 423 ? 0.5822 0.4878 0.6909 0.2055  0.0091  -0.0799 1640 LEU B CG    
7028 C  CD1   . LEU B 423 ? 0.7147 0.6335 0.8276 0.1997  0.0086  -0.0675 1640 LEU B CD1   
7029 C  CD2   . LEU B 423 ? 0.5993 0.4947 0.7199 0.2180  0.0047  -0.0847 1640 LEU B CD2   
7030 N  N     . GLN B 424 ? 0.5828 0.5528 0.6763 0.2096  0.0369  -0.1022 1641 GLN B N     
7031 C  CA    . GLN B 424 ? 0.6363 0.6168 0.7196 0.2113  0.0437  -0.1118 1641 GLN B CA    
7032 C  C     . GLN B 424 ? 0.6713 0.6583 0.7419 0.1994  0.0467  -0.1045 1641 GLN B C     
7033 O  O     . GLN B 424 ? 0.5821 0.5587 0.6397 0.1946  0.0455  -0.1084 1641 GLN B O     
7034 C  CB    . GLN B 424 ? 0.6039 0.6094 0.6963 0.2216  0.0513  -0.1175 1641 GLN B CB    
7035 N  N     . PHE B 425 ? 0.6838 0.6870 0.7590 0.1943  0.0498  -0.0935 1642 PHE B N     
7036 C  CA    . PHE B 425 ? 0.5986 0.6082 0.6632 0.1835  0.0525  -0.0856 1642 PHE B CA    
7037 C  C     . PHE B 425 ? 0.7131 0.7004 0.7681 0.1744  0.0458  -0.0821 1642 PHE B C     
7038 O  O     . PHE B 425 ? 0.7018 0.6872 0.7436 0.1688  0.0471  -0.0834 1642 PHE B O     
7039 C  CB    . PHE B 425 ? 0.5213 0.5476 0.5953 0.1793  0.0552  -0.0740 1642 PHE B CB    
7040 C  CG    . PHE B 425 ? 0.6778 0.7296 0.7606 0.1863  0.0634  -0.0763 1642 PHE B CG    
7041 C  CD1   . PHE B 425 ? 0.6427 0.7059 0.7186 0.1921  0.0703  -0.0856 1642 PHE B CD1   
7042 C  CD2   . PHE B 425 ? 0.7776 0.8430 0.8758 0.1871  0.0642  -0.0695 1642 PHE B CD2   
7043 C  CE1   . PHE B 425 ? 0.6891 0.7772 0.7730 0.1984  0.0786  -0.0874 1642 PHE B CE1   
7044 C  CE2   . PHE B 425 ? 0.7672 0.8575 0.8748 0.1931  0.0722  -0.0715 1642 PHE B CE2   
7045 C  CZ    . PHE B 425 ? 0.6875 0.7893 0.7878 0.1988  0.0797  -0.0802 1642 PHE B CZ    
7046 N  N     . LEU B 426 ? 0.7735 0.7442 0.8347 0.1728  0.0384  -0.0773 1643 LEU B N     
7047 C  CA    . LEU B 426 ? 0.6933 0.6437 0.7460 0.1638  0.0324  -0.0731 1643 LEU B CA    
7048 C  C     . LEU B 426 ? 0.6524 0.5899 0.6947 0.1643  0.0314  -0.0835 1643 LEU B C     
7049 O  O     . LEU B 426 ? 0.6654 0.5989 0.6966 0.1564  0.0312  -0.0823 1643 LEU B O     
7050 C  CB    . LEU B 426 ? 0.6823 0.6166 0.7430 0.1639  0.0249  -0.0674 1643 LEU B CB    
7051 C  CG    . LEU B 426 ? 0.6823 0.5943 0.7348 0.1555  0.0189  -0.0641 1643 LEU B CG    
7052 C  CD1   . LEU B 426 ? 0.5179 0.4359 0.5619 0.1448  0.0206  -0.0566 1643 LEU B CD1   
7053 C  CD2   . LEU B 426 ? 0.8050 0.7019 0.8645 0.1558  0.0118  -0.0575 1643 LEU B CD2   
7054 N  N     . GLU B 427 ? 0.6226 0.5541 0.6690 0.1739  0.0307  -0.0944 1644 GLU B N     
7055 C  CA    . GLU B 427 ? 0.7086 0.6285 0.7459 0.1745  0.0296  -0.1056 1644 GLU B CA    
7056 C  C     . GLU B 427 ? 0.7730 0.7100 0.7991 0.1732  0.0360  -0.1101 1644 GLU B C     
7057 O  O     . GLU B 427 ? 0.7145 0.6441 0.7297 0.1681  0.0345  -0.1141 1644 GLU B O     
7058 C  CB    . GLU B 427 ? 0.7393 0.6497 0.7839 0.1857  0.0276  -0.1173 1644 GLU B CB    
7059 N  N     . THR B 428 ? 0.8672 0.8277 0.8957 0.1767  0.0430  -0.1079 1645 THR B N     
7060 C  CA    . THR B 428 ? 0.8943 0.8712 0.9110 0.1752  0.0492  -0.1105 1645 THR B CA    
7061 C  C     . THR B 428 ? 0.9435 0.9235 0.9528 0.1638  0.0495  -0.0987 1645 THR B C     
7062 O  O     . THR B 428 ? 0.8995 0.8978 0.9035 0.1623  0.0557  -0.0951 1645 THR B O     
7063 C  CB    . THR B 428 ? 0.8013 0.8027 0.8232 0.1834  0.0574  -0.1126 1645 THR B CB    
7064 O  OG1   . THR B 428 ? 0.8081 0.8217 0.8385 0.1796  0.0599  -0.0997 1645 THR B OG1   
7065 C  CG2   . THR B 428 ? 0.6264 0.6258 0.6575 0.1955  0.0572  -0.1240 1645 THR B CG2   
7066 N  N     . LYS B 429 ? 0.9846 0.9469 0.9933 0.1558  0.0431  -0.0927 1646 LYS B N     
7067 C  CA    . LYS B 429 ? 0.9882 0.9496 0.9875 0.1455  0.0423  -0.0852 1646 LYS B CA    
7068 C  C     . LYS B 429 ? 1.0265 1.0049 1.0281 0.1416  0.0470  -0.0736 1646 LYS B C     
7069 O  O     . LYS B 429 ? 1.1682 1.1551 1.1610 0.1367  0.0500  -0.0697 1646 LYS B O     
7070 C  CB    . LYS B 429 ? 0.8687 0.8321 0.8544 0.1450  0.0436  -0.0936 1646 LYS B CB    
7071 C  CG    . LYS B 429 ? 0.7047 0.6611 0.6807 0.1351  0.0406  -0.0890 1646 LYS B CG    
7072 C  CD    . LYS B 429 ? 0.8076 0.7727 0.7711 0.1370  0.0431  -0.0976 1646 LYS B CD    
7073 C  CE    . LYS B 429 ? 0.9464 0.9090 0.8998 0.1284  0.0409  -0.0938 1646 LYS B CE    
7074 N  NZ    . LYS B 429 ? 1.0076 0.9860 0.9486 0.1304  0.0451  -0.0974 1646 LYS B NZ    
7075 N  N     . ASN B 430 ? 0.9784 0.9617 0.9924 0.1440  0.0474  -0.0682 1647 ASN B N     
7076 C  CA    . ASN B 430 ? 0.9524 0.9509 0.9704 0.1397  0.0513  -0.0574 1647 ASN B CA    
7077 C  C     . ASN B 430 ? 0.8949 0.8884 0.9254 0.1382  0.0471  -0.0501 1647 ASN B C     
7078 O  O     . ASN B 430 ? 0.9192 0.8993 0.9552 0.1418  0.0418  -0.0532 1647 ASN B O     
7079 C  CB    . ASN B 430 ? 1.0711 1.0927 1.0908 0.1457  0.0600  -0.0597 1647 ASN B CB    
7080 C  CG    . ASN B 430 ? 1.0781 1.1059 1.1097 0.1561  0.0616  -0.0662 1647 ASN B CG    
7081 O  OD1   . ASN B 430 ? 1.1178 1.1373 1.1603 0.1580  0.0568  -0.0647 1647 ASN B OD1   
7082 N  ND2   . ASN B 430 ? 0.9676 1.0115 0.9971 0.1632  0.0685  -0.0732 1647 ASN B ND2   
7083 N  N     . ILE B 431 ? 0.8102 0.8138 0.8449 0.1326  0.0489  -0.0400 1648 ILE B N     
7084 C  CA    . ILE B 431 ? 0.8408 0.8405 0.8862 0.1303  0.0442  -0.0329 1648 ILE B CA    
7085 C  C     . ILE B 431 ? 0.7691 0.7883 0.8281 0.1350  0.0487  -0.0309 1648 ILE B C     
7086 O  O     . ILE B 431 ? 0.6102 0.6469 0.6691 0.1372  0.0562  -0.0320 1648 ILE B O     
7087 C  CB    . ILE B 431 ? 0.9299 0.9231 0.9709 0.1197  0.0410  -0.0237 1648 ILE B CB    
7088 C  CG1   . ILE B 431 ? 0.8249 0.8317 0.8611 0.1144  0.0468  -0.0186 1648 ILE B CG1   
7089 C  CG2   . ILE B 431 ? 1.0511 1.0245 1.0814 0.1160  0.0359  -0.0263 1648 ILE B CG2   
7090 C  CD1   . ILE B 431 ? 0.7102 0.7148 0.7480 0.1056  0.0441  -0.0090 1648 ILE B CD1   
7091 N  N     . ILE B 432 ? 0.7873 0.8041 0.8582 0.1366  0.0440  -0.0275 1649 ILE B N     
7092 C  CA    . ILE B 432 ? 0.7707 0.8025 0.8567 0.1443  0.0463  -0.0290 1649 ILE B CA    
7093 C  C     . ILE B 432 ? 0.8280 0.8671 0.9253 0.1395  0.0439  -0.0197 1649 ILE B C     
7094 O  O     . ILE B 432 ? 0.9216 0.9474 1.0184 0.1350  0.0367  -0.0149 1649 ILE B O     
7095 C  CB    . ILE B 432 ? 0.8305 0.8515 0.9216 0.1541  0.0420  -0.0366 1649 ILE B CB    
7096 C  CG1   . ILE B 432 ? 0.8477 0.8544 0.9264 0.1568  0.0418  -0.0458 1649 ILE B CG1   
7097 C  CG2   . ILE B 432 ? 0.8854 0.9249 0.9906 0.1635  0.0463  -0.0405 1649 ILE B CG2   
7098 C  CD1   . ILE B 432 ? 0.8465 0.8290 0.9161 0.1506  0.0344  -0.0437 1649 ILE B CD1   
7099 N  N     . MET B 433 ? 0.8017 0.8625 0.9098 0.1407  0.0497  -0.0176 1650 MET B N     
7100 C  CA    . MET B 433 ? 0.6590 0.7295 0.7802 0.1367  0.0477  -0.0100 1650 MET B CA    
7101 C  C     . MET B 433 ? 0.6189 0.6979 0.7563 0.1460  0.0458  -0.0132 1650 MET B C     
7102 O  O     . MET B 433 ? 0.7985 0.8928 0.9427 0.1533  0.0520  -0.0184 1650 MET B O     
7103 C  CB    . MET B 433 ? 0.6962 0.7857 0.8200 0.1309  0.0555  -0.0049 1650 MET B CB    
7104 C  CG    . MET B 433 ? 0.8250 0.9218 0.9605 0.1244  0.0528  0.0030  1650 MET B CG    
7105 S  SD    . MET B 433 ? 0.8064 0.9040 0.9335 0.1120  0.0562  0.0110  1650 MET B SD    
7106 C  CE    . MET B 433 ? 0.7624 0.8593 0.9017 0.1056  0.0484  0.0176  1650 MET B CE    
7107 N  N     . ALA B 434 ? 0.4665 0.5360 0.6096 0.1462  0.0373  -0.0102 1651 ALA B N     
7108 C  CA    . ALA B 434 ? 0.5395 0.6159 0.6980 0.1558  0.0344  -0.0131 1651 ALA B CA    
7109 C  C     . ALA B 434 ? 0.5477 0.6281 0.7175 0.1523  0.0278  -0.0060 1651 ALA B C     
7110 O  O     . ALA B 434 ? 0.5749 0.6458 0.7379 0.1433  0.0235  0.0002  1651 ALA B O     
7111 C  CB    . ALA B 434 ? 0.4690 0.5261 0.6226 0.1642  0.0294  -0.0195 1651 ALA B CB    
7112 N  N     . PRO B 435 ? 0.4559 0.5512 0.6432 0.1594  0.0269  -0.0071 1652 PRO B N     
7113 C  CA    . PRO B 435 ? 0.4883 0.5867 0.6867 0.1575  0.0190  -0.0013 1652 PRO B CA    
7114 C  C     . PRO B 435 ? 0.6662 0.7411 0.8569 0.1594  0.0088  0.0002  1652 PRO B C     
7115 O  O     . PRO B 435 ? 0.8072 0.8668 0.9914 0.1663  0.0072  -0.0045 1652 PRO B O     
7116 C  CB    . PRO B 435 ? 0.5182 0.6385 0.7373 0.1668  0.0208  -0.0046 1652 PRO B CB    
7117 C  CG    . PRO B 435 ? 0.4998 0.6239 0.7172 0.1755  0.0285  -0.0130 1652 PRO B CG    
7118 C  CD    . PRO B 435 ? 0.4570 0.5712 0.6555 0.1686  0.0341  -0.0135 1652 PRO B CD    
7119 N  N     . PHE B 436 ? 0.6612 0.7331 0.8523 0.1529  0.0020  0.0069  1653 PHE B N     
7120 C  CA    . PHE B 436 ? 0.4623 0.5123 0.6439 0.1526  -0.0073 0.0101  1653 PHE B CA    
7121 C  C     . PHE B 436 ? 0.5196 0.5761 0.7098 0.1500  -0.0152 0.0161  1653 PHE B C     
7122 O  O     . PHE B 436 ? 0.7416 0.8146 0.9398 0.1435  -0.0135 0.0188  1653 PHE B O     
7123 C  CB    . PHE B 436 ? 0.4898 0.5221 0.6519 0.1438  -0.0060 0.0117  1653 PHE B CB    
7124 C  CG    . PHE B 436 ? 0.5499 0.5596 0.7010 0.1429  -0.0140 0.0149  1653 PHE B CG    
7125 C  CD1   . PHE B 436 ? 0.5354 0.5338 0.6885 0.1523  -0.0191 0.0132  1653 PHE B CD1   
7126 C  CD2   . PHE B 436 ? 0.5840 0.5834 0.7223 0.1326  -0.0161 0.0198  1653 PHE B CD2   
7127 C  CE1   . PHE B 436 ? 0.5320 0.5092 0.6746 0.1510  -0.0261 0.0171  1653 PHE B CE1   
7128 C  CE2   . PHE B 436 ? 0.5551 0.5346 0.6829 0.1315  -0.0228 0.0232  1653 PHE B CE2   
7129 C  CZ    . PHE B 436 ? 0.5602 0.5285 0.6900 0.1404  -0.0277 0.0223  1653 PHE B CZ    
7130 N  N     . CYS B 437 ? 0.5230 0.5663 0.7118 0.1554  -0.0240 0.0181  1654 CYS B N     
7131 C  CA    . CYS B 437 ? 0.4907 0.5369 0.6849 0.1544  -0.0332 0.0237  1654 CYS B CA    
7132 C  C     . CYS B 437 ? 0.5231 0.5575 0.7027 0.1433  -0.0367 0.0292  1654 CYS B C     
7133 O  O     . CYS B 437 ? 0.5683 0.6092 0.7518 0.1396  -0.0428 0.0334  1654 CYS B O     
7134 C  CB    . CYS B 437 ? 0.5228 0.5590 0.7201 0.1654  -0.0412 0.0241  1654 CYS B CB    
7135 S  SG    . CYS B 437 ? 0.5588 0.5611 0.7357 0.1665  -0.0444 0.0254  1654 CYS B SG    
7136 N  N     . GLY B 438 ? 0.4980 0.5140 0.6606 0.1389  -0.0340 0.0290  1655 GLY B N     
7137 C  CA    . GLY B 438 ? 0.5764 0.5808 0.7247 0.1290  -0.0366 0.0336  1655 GLY B CA    
7138 C  C     . GLY B 438 ? 0.6724 0.6570 0.8098 0.1306  -0.0446 0.0378  1655 GLY B C     
7139 O  O     . GLY B 438 ? 0.8305 0.8021 0.9533 0.1230  -0.0454 0.0408  1655 GLY B O     
7140 N  N     . GLU B 439 ? 0.4739 0.4554 0.6180 0.1406  -0.0499 0.0381  1656 GLU B N     
7141 C  CA    . GLU B 439 ? 0.5790 0.5434 0.7143 0.1426  -0.0582 0.0436  1656 GLU B CA    
7142 C  C     . GLU B 439 ? 0.7113 0.6523 0.8308 0.1404  -0.0561 0.0436  1656 GLU B C     
7143 O  O     . GLU B 439 ? 0.5991 0.5352 0.7187 0.1435  -0.0504 0.0379  1656 GLU B O     
7144 C  CB    . GLU B 439 ? 0.7754 0.7427 0.9229 0.1548  -0.0641 0.0438  1656 GLU B CB    
7145 C  CG    . GLU B 439 ? 0.9578 0.9478 1.1208 0.1567  -0.0682 0.0448  1656 GLU B CG    
7146 C  CD    . GLU B 439 ? 1.1094 1.0980 1.2650 0.1507  -0.0761 0.0515  1656 GLU B CD    
7147 O  OE1   . GLU B 439 ? 1.2578 1.2270 1.3990 0.1501  -0.0807 0.0564  1656 GLU B OE1   
7148 O  OE2   . GLU B 439 ? 1.0452 1.0521 1.2092 0.1463  -0.0776 0.0516  1656 GLU B OE2   
7149 N  N     . ILE B 440 ? 0.8415 0.7681 0.9477 0.1353  -0.0610 0.0497  1657 ILE B N     
7150 C  CA    . ILE B 440 ? 0.7715 0.6777 0.8625 0.1305  -0.0584 0.0501  1657 ILE B CA    
7151 C  C     . ILE B 440 ? 0.7688 0.6587 0.8603 0.1389  -0.0597 0.0487  1657 ILE B C     
7152 O  O     . ILE B 440 ? 0.8729 0.7515 0.9590 0.1377  -0.0548 0.0444  1657 ILE B O     
7153 C  CB    . ILE B 440 ? 0.6617 0.5583 0.7388 0.1228  -0.0630 0.0574  1657 ILE B CB    
7154 C  CG1   . ILE B 440 ? 0.6310 0.5415 0.7064 0.1137  -0.0610 0.0575  1657 ILE B CG1   
7155 C  CG2   . ILE B 440 ? 0.5117 0.3866 0.5749 0.1189  -0.0611 0.0586  1657 ILE B CG2   
7156 C  CD1   . ILE B 440 ? 0.4913 0.3980 0.5565 0.1085  -0.0670 0.0641  1657 ILE B CD1   
7157 N  N     . SER B 441 ? 0.7596 0.6480 0.8582 0.1477  -0.0665 0.0520  1658 SER B N     
7158 C  CA    . SER B 441 ? 0.7527 0.6251 0.8536 0.1569  -0.0683 0.0506  1658 SER B CA    
7159 C  C     . SER B 441 ? 0.8819 0.7593 0.9911 0.1618  -0.0612 0.0405  1658 SER B C     
7160 O  O     . SER B 441 ? 0.9774 0.8386 1.0819 0.1632  -0.0586 0.0366  1658 SER B O     
7161 C  CB    . SER B 441 ? 0.7198 0.5955 0.8303 0.1669  -0.0766 0.0550  1658 SER B CB    
7162 O  OG    . SER B 441 ? 0.7803 0.6813 0.9032 0.1681  -0.0771 0.0535  1658 SER B OG    
7163 N  N     . CYS B 442 ? 0.8835 0.7842 1.0049 0.1640  -0.0577 0.0361  1659 CYS B N     
7164 C  CA    . CYS B 442 ? 0.7466 0.6555 0.8759 0.1690  -0.0504 0.0267  1659 CYS B CA    
7165 C  C     . CYS B 442 ? 0.8006 0.7049 0.9188 0.1606  -0.0429 0.0224  1659 CYS B C     
7166 O  O     . CYS B 442 ? 0.8419 0.7402 0.9596 0.1644  -0.0385 0.0152  1659 CYS B O     
7167 C  CB    . CYS B 442 ? 0.7016 0.6380 0.8464 0.1720  -0.0481 0.0243  1659 CYS B CB    
7168 S  SG    . CYS B 442 ? 0.8459 0.7960 1.0000 0.1779  -0.0383 0.0133  1659 CYS B SG    
7169 N  N     . GLU B 443 ? 0.7672 0.6749 0.8767 0.1496  -0.0415 0.0264  1660 GLU B N     
7170 C  CA    . GLU B 443 ? 0.7537 0.6570 0.8524 0.1416  -0.0351 0.0231  1660 GLU B CA    
7171 C  C     . GLU B 443 ? 0.8530 0.7321 0.9411 0.1411  -0.0362 0.0220  1660 GLU B C     
7172 O  O     . GLU B 443 ? 0.8990 0.7736 0.9832 0.1407  -0.0310 0.0152  1660 GLU B O     
7173 C  CB    . GLU B 443 ? 0.7602 0.6697 0.8519 0.1306  -0.0349 0.0284  1660 GLU B CB    
7174 C  CG    . GLU B 443 ? 0.8497 0.7668 0.9365 0.1237  -0.0272 0.0246  1660 GLU B CG    
7175 C  CD    . GLU B 443 ? 1.0244 0.9472 1.1058 0.1136  -0.0276 0.0297  1660 GLU B CD    
7176 O  OE1   . GLU B 443 ? 1.1272 1.0619 1.2162 0.1134  -0.0309 0.0334  1660 GLU B OE1   
7177 O  OE2   . GLU B 443 ? 1.0422 0.9575 1.1120 0.1061  -0.0249 0.0298  1660 GLU B OE2   
7178 N  N     . ASP B 444 ? 0.8506 0.7141 0.9339 0.1410  -0.0430 0.0289  1661 ASP B N     
7179 C  CA    . ASP B 444 ? 0.8459 0.6854 0.9213 0.1410  -0.0446 0.0286  1661 ASP B CA    
7180 C  C     . ASP B 444 ? 0.8037 0.6376 0.8874 0.1515  -0.0435 0.0208  1661 ASP B C     
7181 O  O     . ASP B 444 ? 0.8095 0.6306 0.8883 0.1506  -0.0407 0.0150  1661 ASP B O     
7182 C  CB    . ASP B 444 ? 0.7440 0.5692 0.8143 0.1403  -0.0522 0.0384  1661 ASP B CB    
7183 C  CG    . ASP B 444 ? 0.7889 0.6166 0.8489 0.1298  -0.0531 0.0454  1661 ASP B CG    
7184 O  OD1   . ASP B 444 ? 0.7216 0.5478 0.7800 0.1304  -0.0594 0.0534  1661 ASP B OD1   
7185 O  OD2   . ASP B 444 ? 0.9083 0.7396 0.9616 0.1214  -0.0479 0.0428  1661 ASP B OD2   
7186 N  N     . ARG B 445 ? 0.5937 0.4376 0.6905 0.1618  -0.0460 0.0198  1662 ARG B N     
7187 C  CA    . ARG B 445 ? 0.8260 0.6648 0.9315 0.1730  -0.0453 0.0119  1662 ARG B CA    
7188 C  C     . ARG B 445 ? 0.9774 0.8258 1.0836 0.1731  -0.0370 0.0011  1662 ARG B C     
7189 O  O     . ARG B 445 ? 1.0881 0.9243 1.1936 0.1774  -0.0353 -0.0066 1662 ARG B O     
7190 C  CB    . ARG B 445 ? 0.8050 0.6562 0.9255 0.1840  -0.0493 0.0130  1662 ARG B CB    
7191 N  N     . ILE B 446 ? 0.8761 0.7461 0.9835 0.1684  -0.0318 0.0004  1663 ILE B N     
7192 C  CA    . ILE B 446 ? 0.8443 0.7248 0.9504 0.1677  -0.0236 -0.0086 1663 ILE B CA    
7193 C  C     . ILE B 446 ? 0.8085 0.6723 0.9007 0.1603  -0.0218 -0.0112 1663 ILE B C     
7194 O  O     . ILE B 446 ? 0.9435 0.8010 1.0344 0.1641  -0.0189 -0.0203 1663 ILE B O     
7195 C  CB    . ILE B 446 ? 0.8455 0.7506 0.9545 0.1626  -0.0188 -0.0065 1663 ILE B CB    
7196 C  CG1   . ILE B 446 ? 0.7926 0.7143 0.9162 0.1685  -0.0214 -0.0031 1663 ILE B CG1   
7197 C  CG2   . ILE B 446 ? 0.8630 0.7811 0.9719 0.1637  -0.0102 -0.0151 1663 ILE B CG2   
7198 C  CD1   . ILE B 446 ? 0.7340 0.6811 0.8637 0.1648  -0.0158 -0.0027 1663 ILE B CD1   
7199 N  N     . LYS B 447 ? 0.7431 0.6000 0.8252 0.1498  -0.0237 -0.0038 1664 LYS B N     
7200 C  CA    . LYS B 447 ? 0.9663 0.8087 1.0363 0.1424  -0.0221 -0.0062 1664 LYS B CA    
7201 C  C     . LYS B 447 ? 1.0715 0.8912 1.1410 0.1471  -0.0254 -0.0101 1664 LYS B C     
7202 O  O     . LYS B 447 ? 1.1550 0.9670 1.2199 0.1460  -0.0226 -0.0180 1664 LYS B O     
7203 C  CB    . LYS B 447 ? 0.9712 0.8089 1.0314 0.1312  -0.0242 0.0027  1664 LYS B CB    
7204 C  CG    . LYS B 447 ? 0.9671 0.7928 1.0159 0.1231  -0.0222 0.0002  1664 LYS B CG    
7205 C  CD    . LYS B 447 ? 0.9734 0.7749 1.0176 0.1211  -0.0272 0.0038  1664 LYS B CD    
7206 C  CE    . LYS B 447 ? 0.9769 0.7689 1.0107 0.1116  -0.0251 0.0021  1664 LYS B CE    
7207 N  NZ    . LYS B 447 ? 0.8788 0.6819 0.9055 0.1023  -0.0230 0.0070  1664 LYS B NZ    
7208 N  N     . ALA B 448 ? 0.8896 0.6984 0.9643 0.1525  -0.0316 -0.0048 1665 ALA B N     
7209 C  CA    . ALA B 448 ? 0.7744 0.5598 0.8495 0.1569  -0.0352 -0.0075 1665 ALA B CA    
7210 C  C     . ALA B 448 ? 0.7730 0.5602 0.8552 0.1664  -0.0320 -0.0202 1665 ALA B C     
7211 O  O     . ALA B 448 ? 0.8956 0.6700 0.9734 0.1651  -0.0305 -0.0277 1665 ALA B O     
7212 C  CB    . ALA B 448 ? 0.7877 0.5634 0.8680 0.1624  -0.0425 0.0013  1665 ALA B CB    
7213 N  N     . GLU B 449 ? 0.7309 0.5348 0.8242 0.1761  -0.0308 -0.0232 1666 GLU B N     
7214 C  CA    . GLU B 449 ? 0.7257 0.5316 0.8269 0.1870  -0.0282 -0.0352 1666 GLU B CA    
7215 C  C     . GLU B 449 ? 0.8590 0.6787 0.9558 0.1849  -0.0204 -0.0452 1666 GLU B C     
7216 O  O     . GLU B 449 ? 0.6072 0.4310 0.7096 0.1940  -0.0174 -0.0561 1666 GLU B O     
7217 C  CB    . GLU B 449 ? 0.8290 0.6491 0.9446 0.1986  -0.0296 -0.0349 1666 GLU B CB    
7218 C  CG    . GLU B 449 ? 0.9186 0.7205 1.0400 0.2053  -0.0379 -0.0290 1666 GLU B CG    
7219 C  CD    . GLU B 449 ? 0.8619 0.6794 0.9977 0.2159  -0.0403 -0.0269 1666 GLU B CD    
7220 O  OE1   . GLU B 449 ? 0.7598 0.5931 0.9056 0.2249  -0.0360 -0.0362 1666 GLU B OE1   
7221 O  OE2   . GLU B 449 ? 0.8770 0.6917 1.0142 0.2153  -0.0466 -0.0161 1666 GLU B OE2   
7222 N  N     . SER B 450 ? 1.0398 0.8666 1.1265 0.1735  -0.0171 -0.0417 1667 SER B N     
7223 C  CA    . SER B 450 ? 1.1165 0.9548 1.1967 0.1705  -0.0102 -0.0499 1667 SER B CA    
7224 C  C     . SER B 450 ? 1.1027 0.9238 1.1724 0.1645  -0.0103 -0.0555 1667 SER B C     
7225 O  O     . SER B 450 ? 1.0710 0.9000 1.1362 0.1647  -0.0054 -0.0647 1667 SER B O     
7226 C  CB    . SER B 450 ? 1.1990 1.0573 1.2754 0.1625  -0.0062 -0.0435 1667 SER B CB    
7227 O  OG    . SER B 450 ? 1.2579 1.1306 1.3443 0.1661  -0.0070 -0.0372 1667 SER B OG    
7228 N  N     . ALA B 451 ? 1.1463 0.9455 1.2119 0.1589  -0.0157 -0.0502 1668 ALA B N     
7229 C  CA    . ALA B 451 ? 1.1510 0.9339 1.2084 0.1527  -0.0161 -0.0556 1668 ALA B CA    
7230 C  C     . ALA B 451 ? 1.1753 0.9518 1.2356 0.1609  -0.0150 -0.0701 1668 ALA B C     
7231 O  O     . ALA B 451 ? 1.1519 0.9088 1.2096 0.1585  -0.0175 -0.0751 1668 ALA B O     
7232 C  CB    . ALA B 451 ? 1.1753 0.9351 1.2304 0.1469  -0.0221 -0.0469 1668 ALA B CB    
7233 N  N     . MET B 464 ? 1.1008 0.9054 1.1172 0.1036  -0.0088 -0.0340 1681 MET B N     
7234 C  CA    . MET B 464 ? 1.2689 1.0758 1.2892 0.1125  -0.0068 -0.0453 1681 MET B CA    
7235 C  C     . MET B 464 ? 1.1439 0.9602 1.1739 0.1229  -0.0062 -0.0453 1681 MET B C     
7236 O  O     . MET B 464 ? 1.1268 0.9525 1.1599 0.1306  -0.0029 -0.0541 1681 MET B O     
7237 C  CB    . MET B 464 ? 1.4349 1.2201 1.4558 0.1131  -0.0103 -0.0517 1681 MET B CB    
7238 C  CG    . MET B 464 ? 1.4740 1.2569 1.4876 0.1073  -0.0089 -0.0597 1681 MET B CG    
7239 S  SD    . MET B 464 ? 1.4023 1.2043 1.4140 0.1145  -0.0035 -0.0722 1681 MET B SD    
7240 C  CE    . MET B 464 ? 1.3706 1.1687 1.3931 0.1281  -0.0043 -0.0783 1681 MET B CE    
7241 N  N     . GLY B 465 ? 0.9559 0.7707 0.9905 0.1232  -0.0095 -0.0356 1682 GLY B N     
7242 C  CA    . GLY B 465 ? 0.9282 0.7554 0.9725 0.1317  -0.0090 -0.0342 1682 GLY B CA    
7243 C  C     . GLY B 465 ? 0.9092 0.7580 0.9531 0.1282  -0.0051 -0.0292 1682 GLY B C     
7244 O  O     . GLY B 465 ? 0.9728 0.8253 1.0087 0.1195  -0.0033 -0.0263 1682 GLY B O     
7245 N  N     . ALA B 466 ? 0.8343 0.6973 0.8879 0.1347  -0.0042 -0.0277 1683 ALA B N     
7246 C  CA    . ALA B 466 ? 0.7679 0.6525 0.8230 0.1319  0.0001  -0.0241 1683 ALA B CA    
7247 C  C     . ALA B 466 ? 0.7384 0.6239 0.7948 0.1264  -0.0038 -0.0132 1683 ALA B C     
7248 O  O     . ALA B 466 ? 0.8054 0.6872 0.8690 0.1307  -0.0086 -0.0092 1683 ALA B O     
7249 C  CB    . ALA B 466 ? 0.7097 0.6123 0.7752 0.1411  0.0043  -0.0288 1683 ALA B CB    
7250 N  N     . LYS B 467 ? 0.6838 0.5744 0.7331 0.1173  -0.0021 -0.0088 1684 LYS B N     
7251 C  CA    . LYS B 467 ? 0.6463 0.5392 0.6954 0.1111  -0.0052 0.0005  1684 LYS B CA    
7252 C  C     . LYS B 467 ? 0.6095 0.5239 0.6658 0.1109  -0.0016 0.0026  1684 LYS B C     
7253 O  O     . LYS B 467 ? 0.6198 0.5471 0.6792 0.1143  0.0041  -0.0022 1684 LYS B O     
7254 C  CB    . LYS B 467 ? 0.6308 0.5146 0.6679 0.1011  -0.0057 0.0035  1684 LYS B CB    
7255 N  N     . SER B 468 ? 0.6976 0.6160 0.7569 0.1072  -0.0051 0.0099  1685 SER B N     
7256 C  CA    . SER B 468 ? 0.8497 0.7869 0.9153 0.1045  -0.0021 0.0129  1685 SER B CA    
7257 C  C     . SER B 468 ? 0.8573 0.7963 0.9138 0.0954  0.0011  0.0147  1685 SER B C     
7258 O  O     . SER B 468 ? 0.9823 0.9093 1.0294 0.0893  -0.0017 0.0175  1685 SER B O     
7259 C  CB    . SER B 468 ? 0.8653 0.8061 0.9383 0.1041  -0.0079 0.0190  1685 SER B CB    
7260 O  OG    . SER B 468 ? 0.9256 0.8496 0.9906 0.1013  -0.0140 0.0229  1685 SER B OG    
7261 N  N     . LEU B 469 ? 0.7556 0.7094 0.8147 0.0946  0.0073  0.0134  1686 LEU B N     
7262 C  CA    . LEU B 469 ? 0.6781 0.6345 0.7298 0.0866  0.0103  0.0160  1686 LEU B CA    
7263 C  C     . LEU B 469 ? 0.6887 0.6543 0.7466 0.0814  0.0089  0.0222  1686 LEU B C     
7264 O  O     . LEU B 469 ? 0.6318 0.5903 0.6841 0.0750  0.0054  0.0259  1686 LEU B O     
7265 C  CB    . LEU B 469 ? 0.4603 0.4264 0.5098 0.0884  0.0177  0.0118  1686 LEU B CB    
7266 C  CG    . LEU B 469 ? 0.5798 0.5396 0.6270 0.0957  0.0185  0.0042  1686 LEU B CG    
7267 C  CD1   . LEU B 469 ? 0.6671 0.6392 0.7129 0.0990  0.0257  -0.0004 1686 LEU B CD1   
7268 C  CD2   . LEU B 469 ? 0.6471 0.5880 0.6830 0.0928  0.0149  0.0022  1686 LEU B CD2   
7269 N  N     . CYS B 470 ? 0.7194 0.7011 0.7893 0.0839  0.0116  0.0229  1687 CYS B N     
7270 C  CA    . CYS B 470 ? 0.5755 0.5662 0.6541 0.0796  0.0093  0.0280  1687 CYS B CA    
7271 C  C     . CYS B 470 ? 0.5909 0.5992 0.6853 0.0848  0.0118  0.0272  1687 CYS B C     
7272 O  O     . CYS B 470 ? 0.5131 0.5280 0.6105 0.0910  0.0167  0.0231  1687 CYS B O     
7273 C  CB    . CYS B 470 ? 0.5318 0.5249 0.6058 0.0711  0.0121  0.0313  1687 CYS B CB    
7274 S  SG    . CYS B 470 ? 0.4313 0.4411 0.5101 0.0716  0.0216  0.0309  1687 CYS B SG    
7275 N  N     . ILE B 471 ? 0.5654 0.5811 0.6699 0.0825  0.0079  0.0309  1688 ILE B N     
7276 C  CA    . ILE B 471 ? 0.6086 0.6438 0.7298 0.0847  0.0105  0.0313  1688 ILE B CA    
7277 C  C     . ILE B 471 ? 0.9262 0.9712 1.0488 0.0775  0.0167  0.0342  1688 ILE B C     
7278 O  O     . ILE B 471 ? 1.0751 1.1179 1.1968 0.0698  0.0140  0.0379  1688 ILE B O     
7279 C  CB    . ILE B 471 ? 0.5929 0.6323 0.7247 0.0846  0.0029  0.0338  1688 ILE B CB    
7280 C  CG1   . ILE B 471 ? 0.4062 0.4303 0.5315 0.0892  -0.0046 0.0332  1688 ILE B CG1   
7281 C  CG2   . ILE B 471 ? 0.5701 0.6292 0.7201 0.0893  0.0051  0.0328  1688 ILE B CG2   
7282 C  CD1   . ILE B 471 ? 0.4057 0.4293 0.5345 0.0867  -0.0130 0.0367  1688 ILE B CD1   
7283 N  N     . PRO B 472 ? 0.9144 0.9691 1.0380 0.0796  0.0249  0.0326  1689 PRO B N     
7284 C  CA    . PRO B 472 ? 0.8438 0.9047 0.9656 0.0727  0.0311  0.0362  1689 PRO B CA    
7285 C  C     . PRO B 472 ? 0.8659 0.9404 1.0029 0.0673  0.0311  0.0406  1689 PRO B C     
7286 O  O     . PRO B 472 ? 1.0299 1.1162 1.1817 0.0704  0.0294  0.0400  1689 PRO B O     
7287 C  CB    . PRO B 472 ? 0.8455 0.9156 0.9658 0.0781  0.0396  0.0332  1689 PRO B CB    
7288 C  CG    . PRO B 472 ? 0.8549 0.9187 0.9725 0.0872  0.0373  0.0270  1689 PRO B CG    
7289 C  CD    . PRO B 472 ? 0.8998 0.9609 1.0265 0.0887  0.0291  0.0275  1689 PRO B CD    
7290 N  N     . PHE B 473 ? 0.6846 0.7574 0.8183 0.0590  0.0329  0.0449  1690 PHE B N     
7291 C  CA    . PHE B 473 ? 0.4339 0.5192 0.5821 0.0528  0.0340  0.0491  1690 PHE B CA    
7292 C  C     . PHE B 473 ? 0.4784 0.5832 0.6382 0.0547  0.0428  0.0502  1690 PHE B C     
7293 O  O     . PHE B 473 ? 0.5727 0.6923 0.7498 0.0527  0.0432  0.0519  1690 PHE B O     
7294 C  CB    . PHE B 473 ? 0.3809 0.4583 0.5224 0.0439  0.0344  0.0533  1690 PHE B CB    
7295 C  CG    . PHE B 473 ? 0.4225 0.4828 0.5535 0.0410  0.0265  0.0524  1690 PHE B CG    
7296 C  CD1   . PHE B 473 ? 0.4864 0.5405 0.6164 0.0447  0.0190  0.0494  1690 PHE B CD1   
7297 C  CD2   . PHE B 473 ? 0.4509 0.5017 0.5731 0.0345  0.0269  0.0550  1690 PHE B CD2   
7298 C  CE1   . PHE B 473 ? 0.4729 0.5124 0.5928 0.0417  0.0124  0.0491  1690 PHE B CE1   
7299 C  CE2   . PHE B 473 ? 0.4976 0.5340 0.6104 0.0319  0.0202  0.0540  1690 PHE B CE2   
7300 C  CZ    . PHE B 473 ? 0.4794 0.5104 0.5907 0.0353  0.0132  0.0511  1690 PHE B CZ    
7301 N  N     . GLU B 474 ? 0.5256 0.6314 0.6761 0.0588  0.0498  0.0489  1691 GLU B N     
7302 C  CA    . GLU B 474 ? 0.6277 0.7519 0.7861 0.0612  0.0592  0.0498  1691 GLU B CA    
7303 C  C     . GLU B 474 ? 0.6909 0.8231 0.8554 0.0715  0.0593  0.0437  1691 GLU B C     
7304 O  O     . GLU B 474 ? 0.7280 0.8560 0.8818 0.0783  0.0619  0.0390  1691 GLU B O     
7305 C  CB    . GLU B 474 ? 0.8911 1.0117 1.0341 0.0604  0.0662  0.0516  1691 GLU B CB    
7306 C  CG    . GLU B 474 ? 1.0103 1.1136 1.1401 0.0531  0.0628  0.0551  1691 GLU B CG    
7307 C  CD    . GLU B 474 ? 1.0986 1.1832 1.2110 0.0565  0.0576  0.0502  1691 GLU B CD    
7308 O  OE1   . GLU B 474 ? 1.0276 1.1037 1.1406 0.0589  0.0503  0.0466  1691 GLU B OE1   
7309 O  OE2   . GLU B 474 ? 1.1389 1.2174 1.2370 0.0566  0.0607  0.0503  1691 GLU B OE2   
7310 N  N     . GLN B 475 ? 0.7110 0.8548 0.8933 0.0729  0.0563  0.0432  1692 GLN B N     
7311 C  CA    . GLN B 475 ? 0.6031 0.7549 0.7931 0.0832  0.0559  0.0374  1692 GLN B CA    
7312 C  C     . GLN B 475 ? 0.6123 0.7825 0.8071 0.0879  0.0666  0.0360  1692 GLN B C     
7313 O  O     . GLN B 475 ? 0.7103 0.8952 0.9132 0.0824  0.0735  0.0410  1692 GLN B O     
7314 C  CB    . GLN B 475 ? 0.5724 0.7338 0.7812 0.0836  0.0497  0.0376  1692 GLN B CB    
7315 C  CG    . GLN B 475 ? 0.6643 0.8093 0.8685 0.0815  0.0386  0.0379  1692 GLN B CG    
7316 C  CD    . GLN B 475 ? 0.7078 0.8398 0.9038 0.0907  0.0332  0.0327  1692 GLN B CD    
7317 O  OE1   . GLN B 475 ? 0.8189 0.9591 1.0261 0.0987  0.0311  0.0295  1692 GLN B OE1   
7318 N  NE2   . GLN B 475 ? 0.6800 0.7916 0.8571 0.0897  0.0310  0.0320  1692 GLN B NE2   
7319 N  N     . PRO B 476 ? 0.7395 0.9097 0.9301 0.0982  0.0683  0.0292  1693 PRO B N     
7320 C  CA    . PRO B 476 ? 0.8925 1.0826 1.0895 0.1041  0.0782  0.0267  1693 PRO B CA    
7321 C  C     . PRO B 476 ? 0.9645 1.1717 1.1833 0.1095  0.0768  0.0244  1693 PRO B C     
7322 O  O     . PRO B 476 ? 1.1724 1.3742 1.3934 0.1182  0.0711  0.0185  1693 PRO B O     
7323 C  CB    . PRO B 476 ? 0.8844 1.0632 1.0650 0.1125  0.0792  0.0193  1693 PRO B CB    
7324 C  CG    . PRO B 476 ? 0.8091 0.9657 0.9834 0.1141  0.0681  0.0167  1693 PRO B CG    
7325 C  CD    . PRO B 476 ? 0.7779 0.9296 0.9579 0.1049  0.0613  0.0233  1693 PRO B CD    
7326 N  N     . ALA B 477 ? 0.8464 1.0734 1.0818 0.1040  0.0813  0.0294  1694 ALA B N     
7327 C  CA    . ALA B 477 ? 0.9309 1.1766 1.1896 0.1078  0.0796  0.0279  1694 ALA B CA    
7328 C  C     . ALA B 477 ? 0.9036 1.1395 1.1689 0.1068  0.0670  0.0280  1694 ALA B C     
7329 O  O     . ALA B 477 ? 0.8711 1.0847 1.1224 0.1079  0.0591  0.0265  1694 ALA B O     
7330 C  CB    . ALA B 477 ? 1.0394 1.2956 1.3021 0.1211  0.0836  0.0199  1694 ALA B CB    
7331 N  N     . LYS B 478 ? 0.8485 1.1027 1.1359 0.1051  0.0653  0.0297  1695 LYS B N     
7332 C  CA    . LYS B 478 ? 0.7324 0.9826 1.0291 0.1047  0.0536  0.0297  1695 LYS B CA    
7333 C  C     . LYS B 478 ? 0.7434 0.9933 1.0446 0.1179  0.0483  0.0232  1695 LYS B C     
7334 O  O     . LYS B 478 ? 0.7800 1.0438 1.0884 0.1268  0.0546  0.0187  1695 LYS B O     
7335 C  CB    . LYS B 478 ? 0.6003 0.8717 0.9197 0.0970  0.0540  0.0337  1695 LYS B CB    
7336 N  N     . ILE B 479 ? 0.7111 0.9446 1.0074 0.1197  0.0367  0.0228  1696 ILE B N     
7337 C  CA    . ILE B 479 ? 0.6025 0.8319 0.9014 0.1323  0.0307  0.0176  1696 ILE B CA    
7338 C  C     . ILE B 479 ? 0.6603 0.9143 0.9852 0.1366  0.0285  0.0166  1696 ILE B C     
7339 O  O     . ILE B 479 ? 0.7502 1.0114 1.0861 0.1300  0.0227  0.0201  1696 ILE B O     
7340 C  CB    . ILE B 479 ? 0.4094 0.6132 0.6939 0.1324  0.0192  0.0186  1696 ILE B CB    
7341 N  N     . ASP B 480 ? 0.6100 0.8787 0.9455 0.1476  0.0338  0.0112  1697 ASP B N     
7342 C  CA    . ASP B 480 ? 0.5683 0.8619 0.9294 0.1537  0.0324  0.0092  1697 ASP B CA    
7343 C  C     . ASP B 480 ? 0.5935 0.8751 0.9554 0.1630  0.0197  0.0071  1697 ASP B C     
7344 O  O     . ASP B 480 ? 0.5823 0.8499 0.9345 0.1732  0.0186  0.0027  1697 ASP B O     
7345 C  CB    . ASP B 480 ? 0.4192 0.7329 0.7901 0.1622  0.0437  0.0038  1697 ASP B CB    
7346 C  CG    . ASP B 480 ? 0.5681 0.9118 0.9680 0.1675  0.0437  0.0019  1697 ASP B CG    
7347 O  OD1   . ASP B 480 ? 0.5365 0.9033 0.9483 0.1707  0.0546  -0.0007 1697 ASP B OD1   
7348 O  OD2   . ASP B 480 ? 0.5479 0.8929 0.9588 0.1688  0.0328  0.0030  1697 ASP B OD2   
7349 N  N     . PRO B 481 ? 0.6478 0.9342 1.0206 0.1598  0.0100  0.0102  1698 PRO B N     
7350 C  CA    . PRO B 481 ? 0.6630 0.9341 1.0320 0.1673  -0.0030 0.0100  1698 PRO B CA    
7351 C  C     . PRO B 481 ? 0.6622 0.9446 1.0466 0.1827  -0.0052 0.0048  1698 PRO B C     
7352 O  O     . PRO B 481 ? 0.7549 1.0195 1.1312 0.1920  -0.0126 0.0034  1698 PRO B O     
7353 C  CB    . PRO B 481 ? 0.6899 0.9665 1.0666 0.1581  -0.0118 0.0148  1698 PRO B CB    
7354 C  CG    . PRO B 481 ? 0.7364 1.0184 1.1111 0.1439  -0.0038 0.0180  1698 PRO B CG    
7355 C  CD    . PRO B 481 ? 0.7370 1.0364 1.1202 0.1469  0.0095  0.0150  1698 PRO B CD    
7356 N  N     . LYS B 482 ? 0.5195 0.8316 0.9268 0.1854  0.0010  0.0021  1699 LYS B N     
7357 C  CA    . LYS B 482 ? 0.5637 0.8889 0.9869 0.2008  0.0003  -0.0037 1699 LYS B CA    
7358 C  C     . LYS B 482 ? 0.7273 1.0366 1.1363 0.2109  0.0057  -0.0093 1699 LYS B C     
7359 O  O     . LYS B 482 ? 0.4591 0.7632 0.8720 0.2245  0.0006  -0.0135 1699 LYS B O     
7360 C  CB    . LYS B 482 ? 0.5109 0.8726 0.9609 0.2006  0.0083  -0.0057 1699 LYS B CB    
7361 C  CG    . LYS B 482 ? 0.5068 0.8879 0.9764 0.1928  0.0019  -0.0017 1699 LYS B CG    
7362 C  CD    . LYS B 482 ? 0.5824 0.9808 1.0589 0.1789  0.0123  0.0014  1699 LYS B CD    
7363 C  CE    . LYS B 482 ? 0.7327 1.1081 1.1877 0.1647  0.0105  0.0072  1699 LYS B CE    
7364 N  NZ    . LYS B 482 ? 0.7047 1.0916 1.1626 0.1507  0.0210  0.0111  1699 LYS B NZ    
7365 N  N     . VAL B 483 ? 0.7899 1.0912 1.1828 0.2045  0.0156  -0.0096 1700 VAL B N     
7366 C  CA    . VAL B 483 ? 0.6749 0.9661 1.0558 0.2129  0.0228  -0.0161 1700 VAL B CA    
7367 C  C     . VAL B 483 ? 0.7507 1.0070 1.1047 0.2107  0.0186  -0.0151 1700 VAL B C     
7368 O  O     . VAL B 483 ? 0.9253 1.1643 1.2730 0.2211  0.0139  -0.0193 1700 VAL B O     
7369 C  CB    . VAL B 483 ? 0.5640 0.8745 0.9469 0.2086  0.0377  -0.0179 1700 VAL B CB    
7370 C  CG1   . VAL B 483 ? 0.7204 1.0194 1.0884 0.2166  0.0445  -0.0251 1700 VAL B CG1   
7371 C  CG2   . VAL B 483 ? 0.5617 0.9079 0.9723 0.2117  0.0430  -0.0195 1700 VAL B CG2   
7372 N  N     . ASP B 484 ? 0.6048 0.8506 0.9436 0.1972  0.0202  -0.0097 1701 ASP B N     
7373 C  CA    . ASP B 484 ? 0.5341 0.7504 0.8476 0.1940  0.0190  -0.0093 1701 ASP B CA    
7374 C  C     . ASP B 484 ? 0.6571 0.8486 0.9622 0.1985  0.0068  -0.0080 1701 ASP B C     
7375 O  O     . ASP B 484 ? 0.7328 0.9252 1.0450 0.1971  -0.0025 -0.0033 1701 ASP B O     
7376 C  CB    . ASP B 484 ? 0.4969 0.7089 0.7986 0.1785  0.0218  -0.0030 1701 ASP B CB    
7377 C  CG    . ASP B 484 ? 0.7225 0.9545 1.0280 0.1735  0.0347  -0.0033 1701 ASP B CG    
7378 O  OD1   . ASP B 484 ? 0.7827 1.0223 1.0902 0.1617  0.0369  0.0026  1701 ASP B OD1   
7379 O  OD2   . ASP B 484 ? 0.7923 1.0325 1.0990 0.1815  0.0426  -0.0095 1701 ASP B OD2   
7380 N  N     . LYS B 485 ? 0.7936 0.9627 1.0832 0.2036  0.0067  -0.0119 1702 LYS B N     
7381 C  CA    . LYS B 485 ? 0.7796 0.9223 1.0590 0.2073  -0.0038 -0.0102 1702 LYS B CA    
7382 C  C     . LYS B 485 ? 0.7523 0.8697 1.0079 0.2008  -0.0022 -0.0099 1702 LYS B C     
7383 O  O     . LYS B 485 ? 0.7514 0.8718 0.9994 0.1970  0.0069  -0.0130 1702 LYS B O     
7384 C  CB    . LYS B 485 ? 0.4924 0.6333 0.7818 0.2233  -0.0072 -0.0161 1702 LYS B CB    
7385 N  N     . CYS B 486 ? 0.6428 0.7364 0.8867 0.1989  -0.0112 -0.0056 1703 CYS B N     
7386 C  CA    . CYS B 486 ? 0.5924 0.6618 0.8148 0.1926  -0.0105 -0.0050 1703 CYS B CA    
7387 C  C     . CYS B 486 ? 0.6830 0.7424 0.9000 0.2007  -0.0058 -0.0137 1703 CYS B C     
7388 O  O     . CYS B 486 ? 0.8412 0.9075 1.0701 0.2127  -0.0051 -0.0196 1703 CYS B O     
7389 C  CB    . CYS B 486 ? 0.5628 0.6102 0.7756 0.1900  -0.0210 0.0015  1703 CYS B CB    
7390 S  SG    . CYS B 486 ? 0.6354 0.6527 0.8242 0.1836  -0.0211 0.0019  1703 CYS B SG    
7391 N  N     . VAL B 487 ? 0.6238 0.6683 0.8234 0.1944  -0.0022 -0.0151 1704 VAL B N     
7392 C  CA    . VAL B 487 ? 0.7106 0.7468 0.9049 0.2015  0.0025  -0.0243 1704 VAL B CA    
7393 C  C     . VAL B 487 ? 0.8047 0.8164 0.9957 0.2093  -0.0048 -0.0266 1704 VAL B C     
7394 O  O     . VAL B 487 ? 0.7455 0.7505 0.9350 0.2169  -0.0019 -0.0354 1704 VAL B O     
7395 C  CB    . VAL B 487 ? 0.6047 0.6350 0.7824 0.1934  0.0092  -0.0267 1704 VAL B CB    
7396 C  CG1   . VAL B 487 ? 0.5444 0.6001 0.7271 0.1912  0.0190  -0.0285 1704 VAL B CG1   
7397 C  CG2   . VAL B 487 ? 0.6119 0.6272 0.7758 0.1812  0.0051  -0.0189 1704 VAL B CG2   
7398 N  N     . HIS B 488 ? 0.8946 0.8924 1.0840 0.2075  -0.0141 -0.0191 1705 HIS B N     
7399 C  CA    . HIS B 488 ? 0.9601 0.9339 1.1470 0.2147  -0.0213 -0.0196 1705 HIS B CA    
7400 C  C     . HIS B 488 ? 0.9305 0.9104 1.1343 0.2273  -0.0272 -0.0195 1705 HIS B C     
7401 O  O     . HIS B 488 ? 0.6639 0.6657 0.8809 0.2285  -0.0279 -0.0166 1705 HIS B O     
7402 C  CB    . HIS B 488 ? 0.9765 0.9286 1.1492 0.2055  -0.0278 -0.0110 1705 HIS B CB    
7403 C  CG    . HIS B 488 ? 1.0085 0.9324 1.1729 0.2092  -0.0317 -0.0130 1705 HIS B CG    
7404 N  ND1   . HIS B 488 ? 1.0022 0.9194 1.1669 0.2163  -0.0278 -0.0233 1705 HIS B ND1   
7405 C  CD2   . HIS B 488 ? 1.0660 0.9668 1.2219 0.2065  -0.0391 -0.0061 1705 HIS B CD2   
7406 C  CE1   . HIS B 488 ? 1.1024 0.9927 1.2600 0.2175  -0.0327 -0.0228 1705 HIS B CE1   
7407 N  NE2   . HIS B 488 ? 1.1099 0.9899 1.2621 0.2116  -0.0395 -0.0120 1705 HIS B NE2   
7408 N  N     . PRO B 489 ? 1.0348 0.9956 1.2393 0.2371  -0.0314 -0.0232 1706 PRO B N     
7409 C  CA    . PRO B 489 ? 0.8792 0.8432 1.0997 0.2506  -0.0376 -0.0235 1706 PRO B CA    
7410 C  C     . PRO B 489 ? 0.8445 0.8118 1.0705 0.2501  -0.0468 -0.0129 1706 PRO B C     
7411 O  O     . PRO B 489 ? 0.9771 0.9622 1.2203 0.2593  -0.0490 -0.0137 1706 PRO B O     
7412 C  CB    . PRO B 489 ? 0.7821 0.7173 0.9969 0.2577  -0.0411 -0.0274 1706 PRO B CB    
7413 C  CG    . PRO B 489 ? 0.9553 0.8842 1.1579 0.2520  -0.0330 -0.0353 1706 PRO B CG    
7414 C  CD    . PRO B 489 ? 1.0304 0.9770 1.2267 0.2394  -0.0266 -0.0326 1706 PRO B CD    
7415 N  N     . ALA B 490 ? 0.7179 0.6699 0.9309 0.2408  -0.0525 -0.0034 1707 ALA B N     
7416 C  CA    . ALA B 490 ? 0.7702 0.7284 0.9890 0.2413  -0.0613 0.0058  1707 ALA B CA    
7417 C  C     . ALA B 490 ? 0.8976 0.8764 1.1161 0.2296  -0.0592 0.0102  1707 ALA B C     
7418 O  O     . ALA B 490 ? 0.6219 0.6273 0.8554 0.2315  -0.0560 0.0074  1707 ALA B O     
7419 C  CB    . ALA B 490 ? 0.6882 0.6183 0.8946 0.2404  -0.0703 0.0143  1707 ALA B CB    
7420 N  N     . CYS B 491 ? 1.1792 1.1456 1.3811 0.2174  -0.0607 0.0168  1708 CYS B N     
7421 C  CA    . CYS B 491 ? 1.0808 1.0605 1.2785 0.2047  -0.0586 0.0207  1708 CYS B CA    
7422 C  C     . CYS B 491 ? 1.0796 1.0749 1.2860 0.2036  -0.0657 0.0269  1708 CYS B C     
7423 O  O     . CYS B 491 ? 1.1275 1.1181 1.3378 0.2108  -0.0747 0.0313  1708 CYS B O     
7424 C  CB    . CYS B 491 ? 1.0505 1.0496 1.2539 0.2014  -0.0479 0.0138  1708 CYS B CB    
7425 S  SG    . CYS B 491 ? 1.2412 1.2297 1.4407 0.2074  -0.0401 0.0039  1708 CYS B SG    
7426 N  N     . GLY B 492 ? 1.0825 1.0950 1.2906 0.1939  -0.0620 0.0276  1709 GLY B N     
7427 C  CA    . GLY B 492 ? 1.1060 1.1404 1.3273 0.1928  -0.0664 0.0304  1709 GLY B CA    
7428 C  C     . GLY B 492 ? 1.1078 1.1671 1.3505 0.2003  -0.0620 0.0243  1709 GLY B C     
7429 O  O     . GLY B 492 ? 1.1950 1.2765 1.4523 0.1993  -0.0642 0.0253  1709 GLY B O     
7430 N  N     . ARG B 493 ? 1.0085 1.0650 1.2539 0.2078  -0.0555 0.0175  1710 ARG B N     
7431 C  CA    . ARG B 493 ? 0.9711 1.0507 1.2345 0.2147  -0.0485 0.0104  1710 ARG B CA    
7432 C  C     . ARG B 493 ? 0.8969 0.9997 1.1667 0.2051  -0.0401 0.0093  1710 ARG B C     
7433 O  O     . ARG B 493 ? 0.8657 0.9725 1.1331 0.2037  -0.0300 0.0043  1710 ARG B O     
7434 C  CB    . ARG B 493 ? 0.9768 1.0699 1.2597 0.2268  -0.0558 0.0103  1710 ARG B CB    
7435 N  N     . VAL B 494 ? 0.8936 1.0117 1.1715 0.1986  -0.0441 0.0139  1711 VAL B N     
7436 C  CA    . VAL B 494 ? 0.7706 0.9109 1.0570 0.1897  -0.0363 0.0133  1711 VAL B CA    
7437 C  C     . VAL B 494 ? 0.7646 0.8922 1.0322 0.1779  -0.0300 0.0147  1711 VAL B C     
7438 O  O     . VAL B 494 ? 0.7534 0.8606 1.0042 0.1721  -0.0349 0.0189  1711 VAL B O     
7439 C  CB    . VAL B 494 ? 0.6628 0.8203 0.9622 0.1849  -0.0431 0.0176  1711 VAL B CB    
7440 N  N     . ALA B 495 ? 0.7178 0.8574 0.9878 0.1748  -0.0191 0.0113  1712 ALA B N     
7441 C  CA    . ALA B 495 ? 0.7602 0.8889 1.0130 0.1646  -0.0128 0.0123  1712 ALA B CA    
7442 C  C     . ALA B 495 ? 0.6935 0.8286 0.9465 0.1518  -0.0142 0.0180  1712 ALA B C     
7443 O  O     . ALA B 495 ? 0.6501 0.8077 0.9189 0.1484  -0.0110 0.0185  1712 ALA B O     
7444 C  CB    . ALA B 495 ? 0.7788 0.9182 1.0330 0.1663  -0.0008 0.0071  1712 ALA B CB    
7445 N  N     . LYS B 496 ? 0.5838 0.6993 0.8201 0.1447  -0.0191 0.0219  1713 LYS B N     
7446 C  CA    . LYS B 496 ? 0.5543 0.6744 0.7898 0.1327  -0.0203 0.0264  1713 LYS B CA    
7447 C  C     . LYS B 496 ? 0.6401 0.7646 0.8710 0.1245  -0.0099 0.0262  1713 LYS B C     
7448 O  O     . LYS B 496 ? 0.5208 0.6591 0.7603 0.1165  -0.0078 0.0286  1713 LYS B O     
7449 C  CB    . LYS B 496 ? 0.6052 0.7045 0.8247 0.1283  -0.0288 0.0304  1713 LYS B CB    
7450 C  CG    . LYS B 496 ? 0.6112 0.7076 0.8350 0.1352  -0.0399 0.0322  1713 LYS B CG    
7451 C  CD    . LYS B 496 ? 0.8681 0.9729 1.0972 0.1286  -0.0472 0.0358  1713 LYS B CD    
7452 C  CE    . LYS B 496 ? 1.0858 1.2176 1.3391 0.1307  -0.0475 0.0342  1713 LYS B CE    
7453 N  NZ    . LYS B 496 ? 1.1197 1.2620 1.3789 0.1207  -0.0513 0.0364  1713 LYS B NZ    
7454 N  N     . PHE B 497 ? 0.6833 0.7973 0.9016 0.1265  -0.0034 0.0234  1714 PHE B N     
7455 C  CA    . PHE B 497 ? 0.5696 0.6883 0.7827 0.1193  0.0062  0.0238  1714 PHE B CA    
7456 C  C     . PHE B 497 ? 0.6474 0.7576 0.8493 0.1250  0.0126  0.0189  1714 PHE B C     
7457 O  O     . PHE B 497 ? 0.5612 0.6647 0.7629 0.1347  0.0102  0.0147  1714 PHE B O     
7458 C  CB    . PHE B 497 ? 0.4845 0.5914 0.6855 0.1080  0.0037  0.0284  1714 PHE B CB    
7459 C  CG    . PHE B 497 ? 0.7054 0.7882 0.8888 0.1084  -0.0022 0.0287  1714 PHE B CG    
7460 C  CD1   . PHE B 497 ? 1.0225 1.0924 1.1944 0.1137  0.0007  0.0249  1714 PHE B CD1   
7461 C  CD2   . PHE B 497 ? 0.6046 0.6780 0.7830 0.1035  -0.0105 0.0324  1714 PHE B CD2   
7462 C  CE1   . PHE B 497 ? 1.0866 1.1346 1.2433 0.1137  -0.0042 0.0253  1714 PHE B CE1   
7463 C  CE2   . PHE B 497 ? 0.8339 0.8858 0.9961 0.1037  -0.0152 0.0331  1714 PHE B CE2   
7464 C  CZ    . PHE B 497 ? 1.0411 1.0802 1.1930 0.1086  -0.0119 0.0297  1714 PHE B CZ    
7465 N  N     . TYR B 498 ? 0.4135 0.5236 0.6061 0.1192  0.0204  0.0193  1715 TYR B N     
7466 C  CA    . TYR B 498 ? 0.4191 0.5182 0.5973 0.1229  0.0252  0.0148  1715 TYR B CA    
7467 C  C     . TYR B 498 ? 0.4568 0.5342 0.6162 0.1162  0.0219  0.0170  1715 TYR B C     
7468 O  O     . TYR B 498 ? 0.5294 0.6063 0.6851 0.1067  0.0220  0.0218  1715 TYR B O     
7469 C  CB    . TYR B 498 ? 0.4179 0.5322 0.5969 0.1222  0.0363  0.0133  1715 TYR B CB    
7470 C  CG    . TYR B 498 ? 0.4210 0.5573 0.6171 0.1298  0.0413  0.0101  1715 TYR B CG    
7471 C  CD1   . TYR B 498 ? 0.4770 0.6153 0.6721 0.1401  0.0454  0.0027  1715 TYR B CD1   
7472 C  CD2   . TYR B 498 ? 0.5131 0.6691 0.7270 0.1266  0.0422  0.0139  1715 TYR B CD2   
7473 C  CE1   . TYR B 498 ? 0.4333 0.5934 0.6446 0.1476  0.0505  -0.0007 1715 TYR B CE1   
7474 C  CE2   . TYR B 498 ? 0.6170 0.7951 0.8478 0.1333  0.0473  0.0110  1715 TYR B CE2   
7475 C  CZ    . TYR B 498 ? 0.5761 0.7566 0.8055 0.1440  0.0516  0.0037  1715 TYR B CZ    
7476 O  OH    . TYR B 498 ? 0.5935 0.7976 0.8407 0.1509  0.0569  0.0006  1715 TYR B OH    
7477 N  N     . THR B 499 ? 0.4251 0.4851 0.5733 0.1210  0.0194  0.0130  1716 THR B N     
7478 C  CA    . THR B 499 ? 0.4249 0.4648 0.5555 0.1155  0.0171  0.0140  1716 THR B CA    
7479 C  C     . THR B 499 ? 0.5379 0.5731 0.6576 0.1179  0.0232  0.0086  1716 THR B C     
7480 O  O     . THR B 499 ? 0.5477 0.5877 0.6713 0.1266  0.0264  0.0025  1716 THR B O     
7481 C  CB    . THR B 499 ? 0.5948 0.6160 0.7204 0.1176  0.0082  0.0146  1716 THR B CB    
7482 O  OG1   . THR B 499 ? 0.9109 0.9326 1.0447 0.1284  0.0065  0.0102  1716 THR B OG1   
7483 C  CG2   . THR B 499 ? 0.5381 0.5588 0.6669 0.1121  0.0015  0.0209  1716 THR B CG2   
7484 N  N     . LEU B 500 ? 0.5808 0.6072 0.6871 0.1104  0.0244  0.0104  1717 LEU B N     
7485 C  CA    . LEU B 500 ? 0.6992 0.7186 0.7929 0.1116  0.0285  0.0055  1717 LEU B CA    
7486 C  C     . LEU B 500 ? 0.7526 0.7502 0.8371 0.1130  0.0224  0.0027  1717 LEU B C     
7487 O  O     . LEU B 500 ? 0.8831 0.8690 0.9636 0.1078  0.0165  0.0073  1717 LEU B O     
7488 C  CB    . LEU B 500 ? 0.7592 0.7807 0.8437 0.1031  0.0327  0.0091  1717 LEU B CB    
7489 C  CG    . LEU B 500 ? 0.8571 0.8871 0.9358 0.1057  0.0407  0.0049  1717 LEU B CG    
7490 C  CD1   . LEU B 500 ? 0.8791 0.9241 0.9687 0.1145  0.0451  0.0004  1717 LEU B CD1   
7491 C  CD2   . LEU B 500 ? 0.9502 0.9896 1.0264 0.0984  0.0456  0.0107  1717 LEU B CD2   
7492 N  N     . PHE B 501 ? 0.6403 0.6329 0.7222 0.1203  0.0238  -0.0047 1718 PHE B N     
7493 C  CA    . PHE B 501 ? 0.6466 0.6183 0.7211 0.1220  0.0186  -0.0079 1718 PHE B CA    
7494 C  C     . PHE B 501 ? 0.7456 0.7113 0.8084 0.1220  0.0222  -0.0146 1718 PHE B C     
7495 O  O     . PHE B 501 ? 0.7651 0.7435 0.8275 0.1252  0.0287  -0.0191 1718 PHE B O     
7496 C  CB    . PHE B 501 ? 0.6674 0.6357 0.7512 0.1318  0.0154  -0.0119 1718 PHE B CB    
7497 C  CG    . PHE B 501 ? 0.6163 0.5877 0.7110 0.1330  0.0101  -0.0060 1718 PHE B CG    
7498 C  CD1   . PHE B 501 ? 0.4647 0.4533 0.5741 0.1399  0.0119  -0.0071 1718 PHE B CD1   
7499 C  CD2   . PHE B 501 ? 0.5026 0.4602 0.5929 0.1279  0.0032  0.0002  1718 PHE B CD2   
7500 C  CE1   . PHE B 501 ? 0.4636 0.4558 0.5835 0.1415  0.0064  -0.0022 1718 PHE B CE1   
7501 C  CE2   . PHE B 501 ? 0.6104 0.5712 0.7098 0.1295  -0.0023 0.0053  1718 PHE B CE2   
7502 C  CZ    . PHE B 501 ? 0.6085 0.5867 0.7231 0.1364  -0.0011 0.0041  1718 PHE B CZ    
7503 N  N     . GLY B 502 ? 0.8283 0.7748 0.8821 0.1193  0.0179  -0.0158 1719 GLY B N     
7504 C  CA    . GLY B 502 ? 0.7847 0.7243 0.8284 0.1196  0.0201  -0.0232 1719 GLY B CA    
7505 C  C     . GLY B 502 ? 0.7720 0.6916 0.8069 0.1138  0.0150  -0.0223 1719 GLY B C     
7506 O  O     . GLY B 502 ? 0.7577 0.6688 0.7932 0.1093  0.0102  -0.0155 1719 GLY B O     
7507 N  N     . ARG B 503 ? 0.7548 0.6674 0.7818 0.1141  0.0161  -0.0297 1720 ARG B N     
7508 C  CA    . ARG B 503 ? 0.8267 0.7224 0.8451 0.1074  0.0123  -0.0295 1720 ARG B CA    
7509 C  C     . ARG B 503 ? 0.6810 0.5813 0.6927 0.0982  0.0133  -0.0229 1720 ARG B C     
7510 O  O     . ARG B 503 ? 0.5571 0.4724 0.5675 0.0973  0.0179  -0.0217 1720 ARG B O     
7511 C  CB    . ARG B 503 ? 0.9452 0.8344 0.9578 0.1100  0.0133  -0.0401 1720 ARG B CB    
7512 C  CG    . ARG B 503 ? 0.9654 0.8508 0.9848 0.1200  0.0129  -0.0482 1720 ARG B CG    
7513 C  CD    . ARG B 503 ? 0.8830 0.7464 0.9012 0.1200  0.0079  -0.0529 1720 ARG B CD    
7514 N  NE    . ARG B 503 ? 0.8789 0.7384 0.9037 0.1302  0.0077  -0.0618 1720 ARG B NE    
7515 C  CZ    . ARG B 503 ? 0.9238 0.7905 0.9466 0.1361  0.0114  -0.0727 1720 ARG B CZ    
7516 N  NH1   . ARG B 503 ? 0.9482 0.8267 0.9623 0.1327  0.0155  -0.0754 1720 ARG B NH1   
7517 N  NH2   . ARG B 503 ? 0.9076 0.7700 0.9370 0.1458  0.0109  -0.0810 1720 ARG B NH2   
7518 N  N     . SER B 504 ? 0.7199 0.6075 0.7277 0.0915  0.0090  -0.0181 1721 SER B N     
7519 C  CA    . SER B 504 ? 0.7053 0.5970 0.7076 0.0832  0.0096  -0.0121 1721 SER B CA    
7520 C  C     . SER B 504 ? 0.7955 0.6735 0.7899 0.0767  0.0069  -0.0126 1721 SER B C     
7521 O  O     . SER B 504 ? 0.8672 0.7314 0.8612 0.0775  0.0041  -0.0162 1721 SER B O     
7522 C  CB    . SER B 504 ? 0.6278 0.5231 0.6351 0.0807  0.0075  -0.0033 1721 SER B CB    
7523 O  OG    . SER B 504 ? 0.5868 0.4677 0.5924 0.0771  0.0023  0.0007  1721 SER B OG    
7524 N  N     . TYR B 505 ? 0.8622 0.7448 0.8512 0.0700  0.0079  -0.0088 1722 TYR B N     
7525 C  CA    . TYR B 505 ? 0.9210 0.7941 0.9033 0.0629  0.0058  -0.0080 1722 TYR B CA    
7526 C  C     . TYR B 505 ? 1.0168 0.8821 0.9997 0.0583  0.0021  -0.0005 1722 TYR B C     
7527 O  O     . TYR B 505 ? 0.9549 0.8243 0.9427 0.0599  0.0011  0.0048  1722 TYR B O     
7528 C  CB    . TYR B 505 ? 0.8085 0.6911 0.7848 0.0588  0.0087  -0.0079 1722 TYR B CB    
7529 C  CG    . TYR B 505 ? 0.8285 0.7125 0.7999 0.0604  0.0104  -0.0161 1722 TYR B CG    
7530 C  CD1   . TYR B 505 ? 0.7852 0.6610 0.7517 0.0556  0.0084  -0.0194 1722 TYR B CD1   
7531 C  CD2   . TYR B 505 ? 0.9204 0.8148 0.8922 0.0667  0.0140  -0.0209 1722 TYR B CD2   
7532 C  CE1   . TYR B 505 ? 0.9261 0.8039 0.8882 0.0571  0.0094  -0.0278 1722 TYR B CE1   
7533 C  CE2   . TYR B 505 ? 0.9702 0.8666 0.9365 0.0686  0.0152  -0.0291 1722 TYR B CE2   
7534 C  CZ    . TYR B 505 ? 1.0377 0.9257 0.9992 0.0638  0.0126  -0.0327 1722 TYR B CZ    
7535 O  OH    . TYR B 505 ? 1.0926 0.9835 1.0489 0.0657  0.0132  -0.0415 1722 TYR B OH    
7536 O  OXT   . TYR B 505 ? 1.0590 0.9145 1.0376 0.0528  0.0002  0.0003  1722 TYR B OXT   
7537 P  PG    . ANP C .   ? 1.1454 1.2314 1.1161 -0.0133 0.0527  -0.0516 1801 ANP A PG    
7538 O  O1G   . ANP C .   ? 1.0740 1.1784 1.0478 -0.0129 0.0587  -0.0573 1801 ANP A O1G   
7539 O  O2G   . ANP C .   ? 1.0505 1.1321 1.0178 -0.0231 0.0545  -0.0436 1801 ANP A O2G   
7540 O  O3G   . ANP C .   ? 1.0592 1.1312 1.0195 -0.0094 0.0495  -0.0512 1801 ANP A O3G   
7541 P  PB    . ANP C .   ? 0.8937 0.9687 0.8774 -0.0105 0.0429  -0.0483 1801 ANP A PB    
7542 O  O1B   . ANP C .   ? 0.8115 0.9001 0.8062 -0.0132 0.0442  -0.0502 1801 ANP A O1B   
7543 O  O2B   . ANP C .   ? 1.0124 1.0779 0.9868 -0.0186 0.0447  -0.0412 1801 ANP A O2B   
7544 N  N3B   . ANP C .   ? 1.0576 1.1413 1.0390 -0.0066 0.0467  -0.0542 1801 ANP A N3B   
7545 P  PA    . ANP C .   ? 0.5396 0.5934 0.5245 -0.0050 0.0323  -0.0432 1801 ANP A PA    
7546 O  O1A   . ANP C .   ? 0.4602 0.5223 0.4548 -0.0014 0.0297  -0.0461 1801 ANP A O1A   
7547 O  O2A   . ANP C .   ? 0.7721 0.8254 0.7538 -0.0143 0.0355  -0.0389 1801 ANP A O2A   
7548 O  O3A   . ANP C .   ? 0.7383 0.8007 0.7221 -0.0034 0.0365  -0.0477 1801 ANP A O3A   
7549 O  "O5'" . ANP C .   ? 0.6270 0.6636 0.6049 -0.0014 0.0282  -0.0395 1801 ANP A "O5'" 
7550 C  "C5'" . ANP C .   ? 0.7994 0.8312 0.7806 0.0061  0.0236  -0.0404 1801 ANP A "C5'" 
7551 C  "C4'" . ANP C .   ? 0.7475 0.7742 0.7260 0.0111  0.0230  -0.0428 1801 ANP A "C4'" 
7552 O  "O4'" . ANP C .   ? 0.5464 0.5643 0.5160 0.0067  0.0241  -0.0396 1801 ANP A "O4'" 
7553 C  "C3'" . ANP C .   ? 0.6745 0.7140 0.6574 0.0139  0.0260  -0.0497 1801 ANP A "C3'" 
7554 O  "O3'" . ANP C .   ? 0.6566 0.6952 0.6454 0.0224  0.0227  -0.0530 1801 ANP A "O3'" 
7555 C  "C2'" . ANP C .   ? 0.5822 0.6179 0.5570 0.0120  0.0284  -0.0507 1801 ANP A "C2'" 
7556 O  "O2'" . ANP C .   ? 0.5647 0.5983 0.5406 0.0188  0.0270  -0.0560 1801 ANP A "O2'" 
7557 C  "C1'" . ANP C .   ? 0.5864 0.6075 0.5531 0.0080  0.0263  -0.0439 1801 ANP A "C1'" 
7558 N  N9    . ANP C .   ? 0.6981 0.7201 0.6574 0.0010  0.0298  -0.0412 1801 ANP A N9    
7559 C  C8    . ANP C .   ? 0.7334 0.7651 0.6930 -0.0050 0.0341  -0.0402 1801 ANP A C8    
7560 N  N7    . ANP C .   ? 0.7940 0.8223 0.7451 -0.0106 0.0362  -0.0361 1801 ANP A N7    
7561 C  C5    . ANP C .   ? 0.7178 0.7339 0.6629 -0.0080 0.0327  -0.0348 1801 ANP A C5    
7562 C  C6    . ANP C .   ? 0.6397 0.6478 0.5751 -0.0109 0.0322  -0.0310 1801 ANP A C6    
7563 N  N6    . ANP C .   ? 0.6796 0.6896 0.6085 -0.0170 0.0354  -0.0269 1801 ANP A N6    
7564 N  N1    . ANP C .   ? 0.6464 0.6440 0.5794 -0.0073 0.0279  -0.0311 1801 ANP A N1    
7565 C  C2    . ANP C .   ? 0.6691 0.6638 0.6088 -0.0015 0.0249  -0.0343 1801 ANP A C2    
7566 N  N3    . ANP C .   ? 0.5569 0.5577 0.5050 0.0021  0.0250  -0.0375 1801 ANP A N3    
7567 C  C4    . ANP C .   ? 0.6736 0.6855 0.6241 -0.0013 0.0288  -0.0378 1801 ANP A C4    
7568 O  "O4'" . HFG D .   ? 0.3734 0.4161 0.3622 -0.0184 0.0270  -0.0339 1802 HFG A "O4'" 
7569 C  C21   . HFG D .   ? 0.4859 0.5427 0.4828 -0.0173 0.0280  -0.0386 1802 HFG A C21   
7570 C  "C3'" . HFG D .   ? 0.4176 0.4813 0.4217 -0.0106 0.0237  -0.0424 1802 HFG A "C3'" 
7571 C  "C2'" . HFG D .   ? 0.4831 0.5348 0.4824 -0.0041 0.0187  -0.0398 1802 HFG A "C2'" 
7572 N  "N1'" . HFG D .   ? 0.3671 0.4067 0.3605 -0.0079 0.0172  -0.0354 1802 HFG A "N1'" 
7573 C  "C6'" . HFG D .   ? 0.3654 0.3967 0.3555 -0.0015 0.0128  -0.0332 1802 HFG A "C6'" 
7574 C  "C5'" . HFG D .   ? 0.3657 0.3891 0.3514 0.0037  0.0126  -0.0312 1802 HFG A "C5'" 
7575 C  "C4'" . HFG D .   ? 0.4096 0.4429 0.4007 0.0076  0.0138  -0.0357 1802 HFG A "C4'" 
7576 C  C39   . HFG D .   ? 0.5286 0.5724 0.5229 0.0016  0.0185  -0.0387 1802 HFG A C39   
7577 O  "O7'" . HFG D .   ? 0.5327 0.5874 0.5326 0.0058  0.0199  -0.0436 1802 HFG A "O7'" 
7578 C  "C1'" . HFG D .   ? 0.5043 0.5735 0.5045 -0.0223 0.0338  -0.0407 1802 HFG A "C1'" 
7579 N  N3    . HFG D .   ? 0.5640 0.6263 0.5576 -0.0303 0.0373  -0.0357 1802 HFG A N3    
7580 C  C4    . HFG D .   ? 0.6547 0.7131 0.6501 -0.0370 0.0369  -0.0331 1802 HFG A C4    
7581 O  O11   . HFG D .   ? 0.7613 0.8243 0.7640 -0.0368 0.0341  -0.0359 1802 HFG A O11   
7582 C  C10   . HFG D .   ? 0.4998 0.5488 0.4877 -0.0440 0.0400  -0.0272 1802 HFG A C10   
7583 C  C5    . HFG D .   ? 0.5108 0.5534 0.4999 -0.0508 0.0397  -0.0242 1802 HFG A C5    
7584 C  C2    . HFG D .   ? 0.6278 0.6869 0.6134 -0.0308 0.0405  -0.0337 1802 HFG A C2    
7585 N  N1    . HFG D .   ? 0.6983 0.7503 0.6765 -0.0369 0.0432  -0.0285 1802 HFG A N1    
7586 C  C9    . HFG D .   ? 0.6630 0.7093 0.6423 -0.0436 0.0429  -0.0247 1802 HFG A C9    
7587 C  C8    . HFG D .   ? 0.7884 0.8257 0.7598 -0.0497 0.0453  -0.0184 1802 HFG A C8    
7588 C  C7    . HFG D .   ? 0.8157 0.8458 0.7887 -0.0561 0.0449  -0.0147 1802 HFG A C7    
7589 BR BR1   . HFG D .   ? 0.9305 0.9457 0.8926 -0.0630 0.0471  -0.0053 1802 HFG A BR1   
7590 C  C6    . HFG D .   ? 0.6659 0.6988 0.6480 -0.0568 0.0423  -0.0180 1802 HFG A C6    
7591 CL CL1   . HFG D .   ? 0.5934 0.6176 0.5783 -0.0654 0.0421  -0.0146 1802 HFG A CL1   
7592 MG MG    . MG  E .   ? 0.7892 0.8515 0.7489 -0.0319 0.0520  -0.0321 1803 MG  A MG    
7593 ZN ZN    . ZN  F .   ? 0.4876 0.9607 0.6984 0.0674  0.1037  -0.1841 1804 ZN  A ZN    
7594 P  PG    . ANP G .   ? 0.8146 0.6772 0.7899 0.0371  -0.0079 0.0295  1801 ANP B PG    
7595 O  O1G   . ANP G .   ? 0.8376 0.7010 0.8194 0.0442  -0.0074 0.0260  1801 ANP B O1G   
7596 O  O2G   . ANP G .   ? 0.7459 0.5969 0.7176 0.0348  -0.0119 0.0343  1801 ANP B O2G   
7597 O  O3G   . ANP G .   ? 0.9244 0.7850 0.8943 0.0331  -0.0052 0.0253  1801 ANP B O3G   
7598 P  PB    . ANP G .   ? 0.7646 0.6377 0.7376 0.0301  -0.0108 0.0377  1801 ANP B PB    
7599 O  O1B   . ANP G .   ? 0.6544 0.5284 0.6312 0.0327  -0.0150 0.0417  1801 ANP B O1B   
7600 O  O2B   . ANP G .   ? 0.8243 0.6862 0.7898 0.0262  -0.0116 0.0386  1801 ANP B O2B   
7601 N  N3B   . ANP G .   ? 0.6393 0.5146 0.6171 0.0354  -0.0076 0.0326  1801 ANP B N3B   
7602 P  PA    . ANP G .   ? 0.7979 0.6870 0.7714 0.0237  -0.0100 0.0397  1801 ANP B PA    
7603 O  O1A   . ANP G .   ? 0.6137 0.5114 0.5963 0.0271  -0.0106 0.0405  1801 ANP B O1A   
7604 O  O2A   . ANP G .   ? 0.8198 0.7029 0.7865 0.0201  -0.0131 0.0425  1801 ANP B O2A   
7605 O  O3A   . ANP G .   ? 0.7585 0.6414 0.7316 0.0270  -0.0084 0.0369  1801 ANP B O3A   
7606 O  "O5'" . ANP G .   ? 0.6385 0.5314 0.6095 0.0206  -0.0065 0.0375  1801 ANP B "O5'" 
7607 C  "C5'" . ANP G .   ? 0.7047 0.6065 0.6811 0.0208  -0.0048 0.0375  1801 ANP B "C5'" 
7608 C  "C4'" . ANP G .   ? 0.6651 0.5695 0.6419 0.0232  -0.0006 0.0348  1801 ANP B "C4'" 
7609 O  "O4'" . ANP G .   ? 0.6551 0.5542 0.6247 0.0211  0.0004  0.0324  1801 ANP B "O4'" 
7610 C  "C3'" . ANP G .   ? 0.6665 0.5713 0.6475 0.0284  0.0002  0.0333  1801 ANP B "C3'" 
7611 O  "O3'" . ANP G .   ? 0.9168 0.8313 0.9056 0.0309  0.0021  0.0343  1801 ANP B "O3'" 
7612 C  "C2'" . ANP G .   ? 0.5648 0.4660 0.5406 0.0293  0.0026  0.0293  1801 ANP B "C2'" 
7613 O  "O2'" . ANP G .   ? 0.5644 0.4736 0.5425 0.0323  0.0065  0.0275  1801 ANP B "O2'" 
7614 C  "C1'" . ANP G .   ? 0.4915 0.3900 0.4607 0.0243  0.0026  0.0291  1801 ANP B "C1'" 
7615 N  N9    . ANP G .   ? 0.6349 0.5244 0.5990 0.0225  0.0014  0.0273  1801 ANP B N9    
7616 C  C8    . ANP G .   ? 0.7901 0.6717 0.7537 0.0223  -0.0015 0.0289  1801 ANP B C8    
7617 N  N7    . ANP G .   ? 0.9000 0.7739 0.8593 0.0199  -0.0018 0.0273  1801 ANP B N7    
7618 C  C5    . ANP G .   ? 0.7264 0.6043 0.6834 0.0188  0.0007  0.0236  1801 ANP B C5    
7619 C  C6    . ANP G .   ? 0.6605 0.5350 0.6139 0.0160  0.0015  0.0201  1801 ANP B C6    
7620 N  N6    . ANP G .   ? 0.6539 0.5193 0.6055 0.0133  0.0001  0.0199  1801 ANP B N6    
7621 N  N1    . ANP G .   ? 0.6280 0.5091 0.5799 0.0161  0.0035  0.0170  1801 ANP B N1    
7622 C  C2    . ANP G .   ? 0.6784 0.5679 0.6321 0.0186  0.0051  0.0181  1801 ANP B C2    
7623 N  N3    . ANP G .   ? 0.6634 0.5564 0.6211 0.0207  0.0050  0.0215  1801 ANP B N3    
7624 C  C4    . ANP G .   ? 0.6986 0.5858 0.6579 0.0207  0.0026  0.0238  1801 ANP B C4    
7625 O  "O4'" . HFG H .   ? 0.7865 0.6720 0.7428 0.0124  -0.0191 0.0469  1802 HFG B "O4'" 
7626 C  C21   . HFG H .   ? 0.6426 0.5298 0.6049 0.0162  -0.0211 0.0481  1802 HFG B C21   
7627 C  "C3'" . HFG H .   ? 0.5195 0.4162 0.4905 0.0175  -0.0226 0.0475  1802 HFG B "C3'" 
7628 C  "C2'" . HFG H .   ? 0.4426 0.3449 0.4153 0.0143  -0.0201 0.0449  1802 HFG B "C2'" 
7629 N  "N1'" . HFG H .   ? 0.3948 0.2947 0.3593 0.0101  -0.0205 0.0443  1802 HFG B "N1'" 
7630 C  "C6'" . HFG H .   ? 0.4377 0.3428 0.4056 0.0077  -0.0191 0.0419  1802 HFG B "C6'" 
7631 C  "C5'" . HFG H .   ? 0.4326 0.3386 0.4034 0.0083  -0.0142 0.0404  1802 HFG B "C5'" 
7632 C  "C4'" . HFG H .   ? 0.4049 0.3132 0.3825 0.0123  -0.0129 0.0413  1802 HFG B "C4'" 
7633 C  C39   . HFG H .   ? 0.4997 0.4027 0.4746 0.0149  -0.0149 0.0428  1802 HFG B C39   
7634 O  "O7'" . HFG H .   ? 0.4772 0.3831 0.4594 0.0193  -0.0139 0.0429  1802 HFG B "O7'" 
7635 C  "C1'" . HFG H .   ? 0.5051 0.3846 0.4674 0.0201  -0.0227 0.0505  1802 HFG B "C1'" 
7636 N  N3    . HFG H .   ? 0.4697 0.3394 0.4235 0.0175  -0.0219 0.0519  1802 HFG B N3    
7637 C  C4    . HFG H .   ? 0.4442 0.3115 0.3901 0.0143  -0.0243 0.0553  1802 HFG B C4    
7638 O  O11   . HFG H .   ? 0.4655 0.3376 0.4111 0.0148  -0.0279 0.0571  1802 HFG B O11   
7639 C  C10   . HFG H .   ? 0.4813 0.3403 0.4196 0.0106  -0.0221 0.0565  1802 HFG B C10   
7640 C  C5    . HFG H .   ? 0.5877 0.4445 0.5172 0.0072  -0.0235 0.0603  1802 HFG B C5    
7641 C  C2    . HFG H .   ? 0.5077 0.3719 0.4615 0.0176  -0.0187 0.0495  1802 HFG B C2    
7642 N  N1    . HFG H .   ? 0.5226 0.3791 0.4705 0.0143  -0.0173 0.0500  1802 HFG B N1    
7643 C  C9    . HFG H .   ? 0.4831 0.3369 0.4233 0.0105  -0.0188 0.0538  1802 HFG B C9    
7644 C  C8    . HFG H .   ? 0.5588 0.4052 0.4933 0.0063  -0.0170 0.0548  1802 HFG B C8    
7645 C  C7    . HFG H .   ? 0.6335 0.4778 0.5599 0.0025  -0.0178 0.0592  1802 HFG B C7    
7646 BR BR1   . HFG H .   ? 0.7928 0.6288 0.7128 -0.0042 -0.0143 0.0609  1802 HFG B BR1   
7647 C  C6    . HFG H .   ? 0.6257 0.4750 0.5490 0.0033  -0.0211 0.0620  1802 HFG B C6    
7648 CL CL1   . HFG H .   ? 0.7542 0.6010 0.6660 -0.0005 -0.0224 0.0680  1802 HFG B CL1   
7649 MG MG    . MG  I .   ? 0.5707 0.4173 0.5296 0.0224  -0.0110 0.0371  1803 MG  B MG    
7650 ZN ZN    . ZN  J .   ? 0.7608 0.7496 0.9408 0.1826  -0.0400 0.0151  1804 ZN  B ZN    
# 
