data_9H9C
# 
_entry.id   9H9C 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9H9C         pdb_00009h9c 10.2210/pdb9h9c/pdb 
WWPDB D_1292142878 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-07 ? 
2 'Structure model' 1 1 2025-05-14 ? 
3 'Structure model' 1 2 2025-05-28 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 3 'Structure model' citation        
3 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
3 3 'Structure model' '_citation.journal_volume'          
4 3 'Structure model' '_citation.page_first'              
5 3 'Structure model' '_citation.page_last'               
6 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H9C 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              francesco.angelucci@univaq.it 
_pdbx_contact_author.name_first         Francesco 
_pdbx_contact_author.name_last          Angelucci 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7305-7903 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gabriele, F.'   1 0000-0002-1330-3452 
'Palerma, M.'    2 ?                   
'Ardini, M.'     3 ?                   
'Bogard, J.'     4 ?                   
'Chen, X.M.'     5 ?                   
'Williams, D.L.' 6 ?                   
'Angelucci, F.'  7 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biochemistry 
_citation.journal_id_ASTM           BICHAW 
_citation.journal_id_CSD            0033 
_citation.journal_id_ISSN           0006-2960 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            64 
_citation.language                  ? 
_citation.page_first                2212 
_citation.page_last                 2225 
_citation.title                     
;Targeting Apicomplexan Parasites: Structural and Functional Characterization of Cryptosporidium Thioredoxin Reductase as a Novel Drug Target.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.biochem.5c00059 
_citation.pdbx_database_id_PubMed   40304242 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gabriele, F.'   1  ?                   
primary 'Bogard, J.A.'   2  0009-0007-7920-1292 
primary 'Palerma, M.'    3  0009-0001-8404-6828 
primary 'Ardini, M.'     4  0000-0002-9044-3352 
primary 'Byrne, M.E.'    5  ?                   
primary 'Chen, X.M.'     6  0000-0001-9848-2244 
primary 'Petukhov, P.A.' 7  0000-0003-1554-242X 
primary 'Ippoliti, R.'   8  ?                   
primary 'Angelucci, F.'  9  0000-0001-7305-7903 
primary 'Williams, D.L.' 10 0000-0002-6815-4909 
# 
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 'Putative thioredoxin reductase' 56360.504 4   ? ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'    785.550   4   ? ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'          106.120   5   ? ? ? ? 
4 water       nat water                            18.015    284 ? ? ? ? 
# 
_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       
;MKFTLVTILFLIFMKKAKIVMADLTFMYDLVVIGGGSGGMAAAKEAAKYGKKVALFDFVKPSTQGTKWGLGGTCVNVGCV
PKKLMHYSALIASSIHHDAQMFGHKTSSSFEWGKLVETLRNHIRMLNFSYRTGLRVGNVEYINALAKLIDPHSVEYEDNG
QKKTITSRYILLATGGRPSIPETVPGAIQYSITSDDIFFLSKSPGKTLVIGASYIGLETAGFLNELGFDTTVAMRSIPLR
GFDRQCSEKIVEYMKATGTKFLVGVVPINIEKVNENIKVSFSDGSVEEFETVLYATGRNPDVKGLNLNAIGVEVSDSGKI
IAPKDATSVPSIFAVGDIVEGRPELTPVAVKAGILLARRLFAGSNEFIDYDFVPTTVFTPIEYGHVGLSSEAAIAKYGED
DIEEYLSEFSTLEIAAAHREKPEHLRENEMDFALPLNCLAKLVVVKSQGEKVVGFHFVGPNAGEITQGFSLAVKLGATKK
DFDDMIGIHPTDAEVFGILEVTKRSGESFVSSGGCGGGKCG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKFTLVTILFLIFMKKAKIVMADLTFMYDLVVIGGGSGGMAAAKEAAKYGKKVALFDFVKPSTQGTKWGLGGTCVNVGCV
PKKLMHYSALIASSIHHDAQMFGHKTSSSFEWGKLVETLRNHIRMLNFSYRTGLRVGNVEYINALAKLIDPHSVEYEDNG
QKKTITSRYILLATGGRPSIPETVPGAIQYSITSDDIFFLSKSPGKTLVIGASYIGLETAGFLNELGFDTTVAMRSIPLR
GFDRQCSEKIVEYMKATGTKFLVGVVPINIEKVNENIKVSFSDGSVEEFETVLYATGRNPDVKGLNLNAIGVEVSDSGKI
IAPKDATSVPSIFAVGDIVEGRPELTPVAVKAGILLARRLFAGSNEFIDYDFVPTTVFTPIEYGHVGLSSEAAIAKYGED
DIEEYLSEFSTLEIAAAHREKPEHLRENEMDFALPLNCLAKLVVVKSQGEKVVGFHFVGPNAGEITQGFSLAVKLGATKK
DFDDMIGIHPTDAEVFGILEVTKRSGESFVSSGGCGGGKCG
;
_entity_poly.pdbx_strand_id                 AAA,BBB,CCC,DDD 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 'DI(HYDROXYETHYL)ETHER'       PEG 
4 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   PHE n 
1 4   THR n 
1 5   LEU n 
1 6   VAL n 
1 7   THR n 
1 8   ILE n 
1 9   LEU n 
1 10  PHE n 
1 11  LEU n 
1 12  ILE n 
1 13  PHE n 
1 14  MET n 
1 15  LYS n 
1 16  LYS n 
1 17  ALA n 
1 18  LYS n 
1 19  ILE n 
1 20  VAL n 
1 21  MET n 
1 22  ALA n 
1 23  ASP n 
1 24  LEU n 
1 25  THR n 
1 26  PHE n 
1 27  MET n 
1 28  TYR n 
1 29  ASP n 
1 30  LEU n 
1 31  VAL n 
1 32  VAL n 
1 33  ILE n 
1 34  GLY n 
1 35  GLY n 
1 36  GLY n 
1 37  SER n 
1 38  GLY n 
1 39  GLY n 
1 40  MET n 
1 41  ALA n 
1 42  ALA n 
1 43  ALA n 
1 44  LYS n 
1 45  GLU n 
1 46  ALA n 
1 47  ALA n 
1 48  LYS n 
1 49  TYR n 
1 50  GLY n 
1 51  LYS n 
1 52  LYS n 
1 53  VAL n 
1 54  ALA n 
1 55  LEU n 
1 56  PHE n 
1 57  ASP n 
1 58  PHE n 
1 59  VAL n 
1 60  LYS n 
1 61  PRO n 
1 62  SER n 
1 63  THR n 
1 64  GLN n 
1 65  GLY n 
1 66  THR n 
1 67  LYS n 
1 68  TRP n 
1 69  GLY n 
1 70  LEU n 
1 71  GLY n 
1 72  GLY n 
1 73  THR n 
1 74  CYS n 
1 75  VAL n 
1 76  ASN n 
1 77  VAL n 
1 78  GLY n 
1 79  CYS n 
1 80  VAL n 
1 81  PRO n 
1 82  LYS n 
1 83  LYS n 
1 84  LEU n 
1 85  MET n 
1 86  HIS n 
1 87  TYR n 
1 88  SER n 
1 89  ALA n 
1 90  LEU n 
1 91  ILE n 
1 92  ALA n 
1 93  SER n 
1 94  SER n 
1 95  ILE n 
1 96  HIS n 
1 97  HIS n 
1 98  ASP n 
1 99  ALA n 
1 100 GLN n 
1 101 MET n 
1 102 PHE n 
1 103 GLY n 
1 104 HIS n 
1 105 LYS n 
1 106 THR n 
1 107 SER n 
1 108 SER n 
1 109 SER n 
1 110 PHE n 
1 111 GLU n 
1 112 TRP n 
1 113 GLY n 
1 114 LYS n 
1 115 LEU n 
1 116 VAL n 
1 117 GLU n 
1 118 THR n 
1 119 LEU n 
1 120 ARG n 
1 121 ASN n 
1 122 HIS n 
1 123 ILE n 
1 124 ARG n 
1 125 MET n 
1 126 LEU n 
1 127 ASN n 
1 128 PHE n 
1 129 SER n 
1 130 TYR n 
1 131 ARG n 
1 132 THR n 
1 133 GLY n 
1 134 LEU n 
1 135 ARG n 
1 136 VAL n 
1 137 GLY n 
1 138 ASN n 
1 139 VAL n 
1 140 GLU n 
1 141 TYR n 
1 142 ILE n 
1 143 ASN n 
1 144 ALA n 
1 145 LEU n 
1 146 ALA n 
1 147 LYS n 
1 148 LEU n 
1 149 ILE n 
1 150 ASP n 
1 151 PRO n 
1 152 HIS n 
1 153 SER n 
1 154 VAL n 
1 155 GLU n 
1 156 TYR n 
1 157 GLU n 
1 158 ASP n 
1 159 ASN n 
1 160 GLY n 
1 161 GLN n 
1 162 LYS n 
1 163 LYS n 
1 164 THR n 
1 165 ILE n 
1 166 THR n 
1 167 SER n 
1 168 ARG n 
1 169 TYR n 
1 170 ILE n 
1 171 LEU n 
1 172 LEU n 
1 173 ALA n 
1 174 THR n 
1 175 GLY n 
1 176 GLY n 
1 177 ARG n 
1 178 PRO n 
1 179 SER n 
1 180 ILE n 
1 181 PRO n 
1 182 GLU n 
1 183 THR n 
1 184 VAL n 
1 185 PRO n 
1 186 GLY n 
1 187 ALA n 
1 188 ILE n 
1 189 GLN n 
1 190 TYR n 
1 191 SER n 
1 192 ILE n 
1 193 THR n 
1 194 SER n 
1 195 ASP n 
1 196 ASP n 
1 197 ILE n 
1 198 PHE n 
1 199 PHE n 
1 200 LEU n 
1 201 SER n 
1 202 LYS n 
1 203 SER n 
1 204 PRO n 
1 205 GLY n 
1 206 LYS n 
1 207 THR n 
1 208 LEU n 
1 209 VAL n 
1 210 ILE n 
1 211 GLY n 
1 212 ALA n 
1 213 SER n 
1 214 TYR n 
1 215 ILE n 
1 216 GLY n 
1 217 LEU n 
1 218 GLU n 
1 219 THR n 
1 220 ALA n 
1 221 GLY n 
1 222 PHE n 
1 223 LEU n 
1 224 ASN n 
1 225 GLU n 
1 226 LEU n 
1 227 GLY n 
1 228 PHE n 
1 229 ASP n 
1 230 THR n 
1 231 THR n 
1 232 VAL n 
1 233 ALA n 
1 234 MET n 
1 235 ARG n 
1 236 SER n 
1 237 ILE n 
1 238 PRO n 
1 239 LEU n 
1 240 ARG n 
1 241 GLY n 
1 242 PHE n 
1 243 ASP n 
1 244 ARG n 
1 245 GLN n 
1 246 CYS n 
1 247 SER n 
1 248 GLU n 
1 249 LYS n 
1 250 ILE n 
1 251 VAL n 
1 252 GLU n 
1 253 TYR n 
1 254 MET n 
1 255 LYS n 
1 256 ALA n 
1 257 THR n 
1 258 GLY n 
1 259 THR n 
1 260 LYS n 
1 261 PHE n 
1 262 LEU n 
1 263 VAL n 
1 264 GLY n 
1 265 VAL n 
1 266 VAL n 
1 267 PRO n 
1 268 ILE n 
1 269 ASN n 
1 270 ILE n 
1 271 GLU n 
1 272 LYS n 
1 273 VAL n 
1 274 ASN n 
1 275 GLU n 
1 276 ASN n 
1 277 ILE n 
1 278 LYS n 
1 279 VAL n 
1 280 SER n 
1 281 PHE n 
1 282 SER n 
1 283 ASP n 
1 284 GLY n 
1 285 SER n 
1 286 VAL n 
1 287 GLU n 
1 288 GLU n 
1 289 PHE n 
1 290 GLU n 
1 291 THR n 
1 292 VAL n 
1 293 LEU n 
1 294 TYR n 
1 295 ALA n 
1 296 THR n 
1 297 GLY n 
1 298 ARG n 
1 299 ASN n 
1 300 PRO n 
1 301 ASP n 
1 302 VAL n 
1 303 LYS n 
1 304 GLY n 
1 305 LEU n 
1 306 ASN n 
1 307 LEU n 
1 308 ASN n 
1 309 ALA n 
1 310 ILE n 
1 311 GLY n 
1 312 VAL n 
1 313 GLU n 
1 314 VAL n 
1 315 SER n 
1 316 ASP n 
1 317 SER n 
1 318 GLY n 
1 319 LYS n 
1 320 ILE n 
1 321 ILE n 
1 322 ALA n 
1 323 PRO n 
1 324 LYS n 
1 325 ASP n 
1 326 ALA n 
1 327 THR n 
1 328 SER n 
1 329 VAL n 
1 330 PRO n 
1 331 SER n 
1 332 ILE n 
1 333 PHE n 
1 334 ALA n 
1 335 VAL n 
1 336 GLY n 
1 337 ASP n 
1 338 ILE n 
1 339 VAL n 
1 340 GLU n 
1 341 GLY n 
1 342 ARG n 
1 343 PRO n 
1 344 GLU n 
1 345 LEU n 
1 346 THR n 
1 347 PRO n 
1 348 VAL n 
1 349 ALA n 
1 350 VAL n 
1 351 LYS n 
1 352 ALA n 
1 353 GLY n 
1 354 ILE n 
1 355 LEU n 
1 356 LEU n 
1 357 ALA n 
1 358 ARG n 
1 359 ARG n 
1 360 LEU n 
1 361 PHE n 
1 362 ALA n 
1 363 GLY n 
1 364 SER n 
1 365 ASN n 
1 366 GLU n 
1 367 PHE n 
1 368 ILE n 
1 369 ASP n 
1 370 TYR n 
1 371 ASP n 
1 372 PHE n 
1 373 VAL n 
1 374 PRO n 
1 375 THR n 
1 376 THR n 
1 377 VAL n 
1 378 PHE n 
1 379 THR n 
1 380 PRO n 
1 381 ILE n 
1 382 GLU n 
1 383 TYR n 
1 384 GLY n 
1 385 HIS n 
1 386 VAL n 
1 387 GLY n 
1 388 LEU n 
1 389 SER n 
1 390 SER n 
1 391 GLU n 
1 392 ALA n 
1 393 ALA n 
1 394 ILE n 
1 395 ALA n 
1 396 LYS n 
1 397 TYR n 
1 398 GLY n 
1 399 GLU n 
1 400 ASP n 
1 401 ASP n 
1 402 ILE n 
1 403 GLU n 
1 404 GLU n 
1 405 TYR n 
1 406 LEU n 
1 407 SER n 
1 408 GLU n 
1 409 PHE n 
1 410 SER n 
1 411 THR n 
1 412 LEU n 
1 413 GLU n 
1 414 ILE n 
1 415 ALA n 
1 416 ALA n 
1 417 ALA n 
1 418 HIS n 
1 419 ARG n 
1 420 GLU n 
1 421 LYS n 
1 422 PRO n 
1 423 GLU n 
1 424 HIS n 
1 425 LEU n 
1 426 ARG n 
1 427 GLU n 
1 428 ASN n 
1 429 GLU n 
1 430 MET n 
1 431 ASP n 
1 432 PHE n 
1 433 ALA n 
1 434 LEU n 
1 435 PRO n 
1 436 LEU n 
1 437 ASN n 
1 438 CYS n 
1 439 LEU n 
1 440 ALA n 
1 441 LYS n 
1 442 LEU n 
1 443 VAL n 
1 444 VAL n 
1 445 VAL n 
1 446 LYS n 
1 447 SER n 
1 448 GLN n 
1 449 GLY n 
1 450 GLU n 
1 451 LYS n 
1 452 VAL n 
1 453 VAL n 
1 454 GLY n 
1 455 PHE n 
1 456 HIS n 
1 457 PHE n 
1 458 VAL n 
1 459 GLY n 
1 460 PRO n 
1 461 ASN n 
1 462 ALA n 
1 463 GLY n 
1 464 GLU n 
1 465 ILE n 
1 466 THR n 
1 467 GLN n 
1 468 GLY n 
1 469 PHE n 
1 470 SER n 
1 471 LEU n 
1 472 ALA n 
1 473 VAL n 
1 474 LYS n 
1 475 LEU n 
1 476 GLY n 
1 477 ALA n 
1 478 THR n 
1 479 LYS n 
1 480 LYS n 
1 481 ASP n 
1 482 PHE n 
1 483 ASP n 
1 484 ASP n 
1 485 MET n 
1 486 ILE n 
1 487 GLY n 
1 488 ILE n 
1 489 HIS n 
1 490 PRO n 
1 491 THR n 
1 492 ASP n 
1 493 ALA n 
1 494 GLU n 
1 495 VAL n 
1 496 PHE n 
1 497 GLY n 
1 498 ILE n 
1 499 LEU n 
1 500 GLU n 
1 501 VAL n 
1 502 THR n 
1 503 LYS n 
1 504 ARG n 
1 505 SER n 
1 506 GLY n 
1 507 GLU n 
1 508 SER n 
1 509 PHE n 
1 510 VAL n 
1 511 SER n 
1 512 SER n 
1 513 GLY n 
1 514 GLY n 
1 515 CYS n 
1 516 GLY n 
1 517 GLY n 
1 518 GLY n 
1 519 LYS n 
1 520 CYS n 
1 521 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   521 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CPATCC_000467 
_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      'Cryptosporidium parvum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5807 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                       ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                      ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                    ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'               ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                      ? 'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                     ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ? 'C5 H11 N O2 S'     149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'       ? 'C4 H10 O3'         106.120 
PHE 'L-peptide linking' y PHENYLALANINE                 ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                     ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   AAA . n 
A 1 2   LYS 2   2   ?   ?   ?   AAA . n 
A 1 3   PHE 3   3   ?   ?   ?   AAA . n 
A 1 4   THR 4   4   ?   ?   ?   AAA . n 
A 1 5   LEU 5   5   ?   ?   ?   AAA . n 
A 1 6   VAL 6   6   ?   ?   ?   AAA . n 
A 1 7   THR 7   7   ?   ?   ?   AAA . n 
A 1 8   ILE 8   8   ?   ?   ?   AAA . n 
A 1 9   LEU 9   9   ?   ?   ?   AAA . n 
A 1 10  PHE 10  10  ?   ?   ?   AAA . n 
A 1 11  LEU 11  11  ?   ?   ?   AAA . n 
A 1 12  ILE 12  12  ?   ?   ?   AAA . n 
A 1 13  PHE 13  13  ?   ?   ?   AAA . n 
A 1 14  MET 14  14  ?   ?   ?   AAA . n 
A 1 15  LYS 15  15  ?   ?   ?   AAA . n 
A 1 16  LYS 16  16  ?   ?   ?   AAA . n 
A 1 17  ALA 17  17  ?   ?   ?   AAA . n 
A 1 18  LYS 18  18  ?   ?   ?   AAA . n 
A 1 19  ILE 19  19  ?   ?   ?   AAA . n 
A 1 20  VAL 20  20  ?   ?   ?   AAA . n 
A 1 21  MET 21  21  ?   ?   ?   AAA . n 
A 1 22  ALA 22  22  ?   ?   ?   AAA . n 
A 1 23  ASP 23  23  ?   ?   ?   AAA . n 
A 1 24  LEU 24  24  24  LEU LEU AAA . n 
A 1 25  THR 25  25  25  THR THR AAA . n 
A 1 26  PHE 26  26  26  PHE PHE AAA . n 
A 1 27  MET 27  27  27  MET MET AAA . n 
A 1 28  TYR 28  28  28  TYR TYR AAA . n 
A 1 29  ASP 29  29  29  ASP ASP AAA . n 
A 1 30  LEU 30  30  30  LEU LEU AAA . n 
A 1 31  VAL 31  31  31  VAL VAL AAA . n 
A 1 32  VAL 32  32  32  VAL VAL AAA . n 
A 1 33  ILE 33  33  33  ILE ILE AAA . n 
A 1 34  GLY 34  34  34  GLY GLY AAA . n 
A 1 35  GLY 35  35  35  GLY GLY AAA . n 
A 1 36  GLY 36  36  36  GLY GLY AAA . n 
A 1 37  SER 37  37  37  SER SER AAA . n 
A 1 38  GLY 38  38  38  GLY GLY AAA . n 
A 1 39  GLY 39  39  39  GLY GLY AAA . n 
A 1 40  MET 40  40  40  MET MET AAA . n 
A 1 41  ALA 41  41  41  ALA ALA AAA . n 
A 1 42  ALA 42  42  42  ALA ALA AAA . n 
A 1 43  ALA 43  43  43  ALA ALA AAA . n 
A 1 44  LYS 44  44  44  LYS LYS AAA . n 
A 1 45  GLU 45  45  45  GLU GLU AAA . n 
A 1 46  ALA 46  46  46  ALA ALA AAA . n 
A 1 47  ALA 47  47  47  ALA ALA AAA . n 
A 1 48  LYS 48  48  48  LYS LYS AAA . n 
A 1 49  TYR 49  49  49  TYR TYR AAA . n 
A 1 50  GLY 50  50  50  GLY GLY AAA . n 
A 1 51  LYS 51  51  51  LYS LYS AAA . n 
A 1 52  LYS 52  52  52  LYS LYS AAA . n 
A 1 53  VAL 53  53  53  VAL VAL AAA . n 
A 1 54  ALA 54  54  54  ALA ALA AAA . n 
A 1 55  LEU 55  55  55  LEU LEU AAA . n 
A 1 56  PHE 56  56  56  PHE PHE AAA . n 
A 1 57  ASP 57  57  57  ASP ASP AAA . n 
A 1 58  PHE 58  58  58  PHE PHE AAA . n 
A 1 59  VAL 59  59  59  VAL VAL AAA . n 
A 1 60  LYS 60  60  60  LYS LYS AAA . n 
A 1 61  PRO 61  61  61  PRO PRO AAA . n 
A 1 62  SER 62  62  62  SER SER AAA . n 
A 1 63  THR 63  63  63  THR THR AAA . n 
A 1 64  GLN 64  64  64  GLN GLN AAA . n 
A 1 65  GLY 65  65  65  GLY GLY AAA . n 
A 1 66  THR 66  66  66  THR THR AAA . n 
A 1 67  LYS 67  67  67  LYS LYS AAA . n 
A 1 68  TRP 68  68  68  TRP TRP AAA . n 
A 1 69  GLY 69  69  69  GLY GLY AAA . n 
A 1 70  LEU 70  70  70  LEU LEU AAA . n 
A 1 71  GLY 71  71  71  GLY GLY AAA . n 
A 1 72  GLY 72  72  72  GLY GLY AAA . n 
A 1 73  THR 73  73  73  THR THR AAA . n 
A 1 74  CYS 74  74  74  CYS CYS AAA . n 
A 1 75  VAL 75  75  75  VAL VAL AAA . n 
A 1 76  ASN 76  76  76  ASN ASN AAA . n 
A 1 77  VAL 77  77  77  VAL VAL AAA . n 
A 1 78  GLY 78  78  78  GLY GLY AAA . n 
A 1 79  CYS 79  79  79  CYS CYS AAA . n 
A 1 80  VAL 80  80  80  VAL VAL AAA . n 
A 1 81  PRO 81  81  81  PRO PRO AAA . n 
A 1 82  LYS 82  82  82  LYS LYS AAA . n 
A 1 83  LYS 83  83  83  LYS LYS AAA . n 
A 1 84  LEU 84  84  84  LEU LEU AAA . n 
A 1 85  MET 85  85  85  MET MET AAA . n 
A 1 86  HIS 86  86  86  HIS HIS AAA . n 
A 1 87  TYR 87  87  87  TYR TYR AAA . n 
A 1 88  SER 88  88  88  SER SER AAA . n 
A 1 89  ALA 89  89  89  ALA ALA AAA . n 
A 1 90  LEU 90  90  90  LEU LEU AAA . n 
A 1 91  ILE 91  91  91  ILE ILE AAA . n 
A 1 92  ALA 92  92  92  ALA ALA AAA . n 
A 1 93  SER 93  93  93  SER SER AAA . n 
A 1 94  SER 94  94  94  SER SER AAA . n 
A 1 95  ILE 95  95  95  ILE ILE AAA . n 
A 1 96  HIS 96  96  96  HIS HIS AAA . n 
A 1 97  HIS 97  97  97  HIS HIS AAA . n 
A 1 98  ASP 98  98  98  ASP ASP AAA . n 
A 1 99  ALA 99  99  99  ALA ALA AAA . n 
A 1 100 GLN 100 100 100 GLN GLN AAA . n 
A 1 101 MET 101 101 101 MET MET AAA . n 
A 1 102 PHE 102 102 102 PHE PHE AAA . n 
A 1 103 GLY 103 103 103 GLY GLY AAA . n 
A 1 104 HIS 104 104 104 HIS HIS AAA . n 
A 1 105 LYS 105 105 105 LYS LYS AAA . n 
A 1 106 THR 106 106 106 THR THR AAA . n 
A 1 107 SER 107 107 107 SER SER AAA . n 
A 1 108 SER 108 108 108 SER SER AAA . n 
A 1 109 SER 109 109 109 SER SER AAA . n 
A 1 110 PHE 110 110 110 PHE PHE AAA . n 
A 1 111 GLU 111 111 111 GLU GLU AAA . n 
A 1 112 TRP 112 112 112 TRP TRP AAA . n 
A 1 113 GLY 113 113 113 GLY GLY AAA . n 
A 1 114 LYS 114 114 114 LYS LYS AAA . n 
A 1 115 LEU 115 115 115 LEU LEU AAA . n 
A 1 116 VAL 116 116 116 VAL VAL AAA . n 
A 1 117 GLU 117 117 117 GLU GLU AAA . n 
A 1 118 THR 118 118 118 THR THR AAA . n 
A 1 119 LEU 119 119 119 LEU LEU AAA . n 
A 1 120 ARG 120 120 120 ARG ARG AAA . n 
A 1 121 ASN 121 121 121 ASN ASN AAA . n 
A 1 122 HIS 122 122 122 HIS HIS AAA . n 
A 1 123 ILE 123 123 123 ILE ILE AAA . n 
A 1 124 ARG 124 124 124 ARG ARG AAA . n 
A 1 125 MET 125 125 125 MET MET AAA . n 
A 1 126 LEU 126 126 126 LEU LEU AAA . n 
A 1 127 ASN 127 127 127 ASN ASN AAA . n 
A 1 128 PHE 128 128 128 PHE PHE AAA . n 
A 1 129 SER 129 129 129 SER SER AAA . n 
A 1 130 TYR 130 130 130 TYR TYR AAA . n 
A 1 131 ARG 131 131 131 ARG ARG AAA . n 
A 1 132 THR 132 132 132 THR THR AAA . n 
A 1 133 GLY 133 133 133 GLY GLY AAA . n 
A 1 134 LEU 134 134 134 LEU LEU AAA . n 
A 1 135 ARG 135 135 135 ARG ARG AAA . n 
A 1 136 VAL 136 136 136 VAL VAL AAA . n 
A 1 137 GLY 137 137 137 GLY GLY AAA . n 
A 1 138 ASN 138 138 138 ASN ASN AAA . n 
A 1 139 VAL 139 139 139 VAL VAL AAA . n 
A 1 140 GLU 140 140 140 GLU GLU AAA . n 
A 1 141 TYR 141 141 141 TYR TYR AAA . n 
A 1 142 ILE 142 142 142 ILE ILE AAA . n 
A 1 143 ASN 143 143 143 ASN ASN AAA . n 
A 1 144 ALA 144 144 144 ALA ALA AAA . n 
A 1 145 LEU 145 145 145 LEU LEU AAA . n 
A 1 146 ALA 146 146 146 ALA ALA AAA . n 
A 1 147 LYS 147 147 147 LYS LYS AAA . n 
A 1 148 LEU 148 148 148 LEU LEU AAA . n 
A 1 149 ILE 149 149 149 ILE ILE AAA . n 
A 1 150 ASP 150 150 150 ASP ASP AAA . n 
A 1 151 PRO 151 151 151 PRO PRO AAA . n 
A 1 152 HIS 152 152 152 HIS HIS AAA . n 
A 1 153 SER 153 153 153 SER SER AAA . n 
A 1 154 VAL 154 154 154 VAL VAL AAA . n 
A 1 155 GLU 155 155 155 GLU GLU AAA . n 
A 1 156 TYR 156 156 156 TYR TYR AAA . n 
A 1 157 GLU 157 157 157 GLU GLU AAA . n 
A 1 158 ASP 158 158 158 ASP ASP AAA . n 
A 1 159 ASN 159 159 159 ASN ASN AAA . n 
A 1 160 GLY 160 160 160 GLY GLY AAA . n 
A 1 161 GLN 161 161 161 GLN GLN AAA . n 
A 1 162 LYS 162 162 162 LYS LYS AAA . n 
A 1 163 LYS 163 163 163 LYS LYS AAA . n 
A 1 164 THR 164 164 164 THR THR AAA . n 
A 1 165 ILE 165 165 165 ILE ILE AAA . n 
A 1 166 THR 166 166 166 THR THR AAA . n 
A 1 167 SER 167 167 167 SER SER AAA . n 
A 1 168 ARG 168 168 168 ARG ARG AAA . n 
A 1 169 TYR 169 169 169 TYR TYR AAA . n 
A 1 170 ILE 170 170 170 ILE ILE AAA . n 
A 1 171 LEU 171 171 171 LEU LEU AAA . n 
A 1 172 LEU 172 172 172 LEU LEU AAA . n 
A 1 173 ALA 173 173 173 ALA ALA AAA . n 
A 1 174 THR 174 174 174 THR THR AAA . n 
A 1 175 GLY 175 175 175 GLY GLY AAA . n 
A 1 176 GLY 176 176 176 GLY GLY AAA . n 
A 1 177 ARG 177 177 177 ARG ARG AAA . n 
A 1 178 PRO 178 178 178 PRO PRO AAA . n 
A 1 179 SER 179 179 179 SER SER AAA . n 
A 1 180 ILE 180 180 180 ILE ILE AAA . n 
A 1 181 PRO 181 181 181 PRO PRO AAA . n 
A 1 182 GLU 182 182 182 GLU GLU AAA . n 
A 1 183 THR 183 183 183 THR THR AAA . n 
A 1 184 VAL 184 184 184 VAL VAL AAA . n 
A 1 185 PRO 185 185 185 PRO PRO AAA . n 
A 1 186 GLY 186 186 186 GLY GLY AAA . n 
A 1 187 ALA 187 187 187 ALA ALA AAA . n 
A 1 188 ILE 188 188 188 ILE ILE AAA . n 
A 1 189 GLN 189 189 189 GLN GLN AAA . n 
A 1 190 TYR 190 190 190 TYR TYR AAA . n 
A 1 191 SER 191 191 191 SER SER AAA . n 
A 1 192 ILE 192 192 192 ILE ILE AAA . n 
A 1 193 THR 193 193 193 THR THR AAA . n 
A 1 194 SER 194 194 194 SER SER AAA . n 
A 1 195 ASP 195 195 195 ASP ASP AAA . n 
A 1 196 ASP 196 196 196 ASP ASP AAA . n 
A 1 197 ILE 197 197 197 ILE ILE AAA . n 
A 1 198 PHE 198 198 198 PHE PHE AAA . n 
A 1 199 PHE 199 199 199 PHE PHE AAA . n 
A 1 200 LEU 200 200 200 LEU LEU AAA . n 
A 1 201 SER 201 201 201 SER SER AAA . n 
A 1 202 LYS 202 202 202 LYS LYS AAA . n 
A 1 203 SER 203 203 203 SER SER AAA . n 
A 1 204 PRO 204 204 204 PRO PRO AAA . n 
A 1 205 GLY 205 205 205 GLY GLY AAA . n 
A 1 206 LYS 206 206 206 LYS LYS AAA . n 
A 1 207 THR 207 207 207 THR THR AAA . n 
A 1 208 LEU 208 208 208 LEU LEU AAA . n 
A 1 209 VAL 209 209 209 VAL VAL AAA . n 
A 1 210 ILE 210 210 210 ILE ILE AAA . n 
A 1 211 GLY 211 211 211 GLY GLY AAA . n 
A 1 212 ALA 212 212 212 ALA ALA AAA . n 
A 1 213 SER 213 213 213 SER SER AAA . n 
A 1 214 TYR 214 214 214 TYR TYR AAA . n 
A 1 215 ILE 215 215 215 ILE ILE AAA . n 
A 1 216 GLY 216 216 216 GLY GLY AAA . n 
A 1 217 LEU 217 217 217 LEU LEU AAA . n 
A 1 218 GLU 218 218 218 GLU GLU AAA . n 
A 1 219 THR 219 219 219 THR THR AAA . n 
A 1 220 ALA 220 220 220 ALA ALA AAA . n 
A 1 221 GLY 221 221 221 GLY GLY AAA . n 
A 1 222 PHE 222 222 222 PHE PHE AAA . n 
A 1 223 LEU 223 223 223 LEU LEU AAA . n 
A 1 224 ASN 224 224 224 ASN ASN AAA . n 
A 1 225 GLU 225 225 225 GLU GLU AAA . n 
A 1 226 LEU 226 226 226 LEU LEU AAA . n 
A 1 227 GLY 227 227 227 GLY GLY AAA . n 
A 1 228 PHE 228 228 228 PHE PHE AAA . n 
A 1 229 ASP 229 229 229 ASP ASP AAA . n 
A 1 230 THR 230 230 230 THR THR AAA . n 
A 1 231 THR 231 231 231 THR THR AAA . n 
A 1 232 VAL 232 232 232 VAL VAL AAA . n 
A 1 233 ALA 233 233 233 ALA ALA AAA . n 
A 1 234 MET 234 234 234 MET MET AAA . n 
A 1 235 ARG 235 235 235 ARG ARG AAA . n 
A 1 236 SER 236 236 236 SER SER AAA . n 
A 1 237 ILE 237 237 237 ILE ILE AAA . n 
A 1 238 PRO 238 238 238 PRO PRO AAA . n 
A 1 239 LEU 239 239 239 LEU LEU AAA . n 
A 1 240 ARG 240 240 240 ARG ARG AAA . n 
A 1 241 GLY 241 241 241 GLY GLY AAA . n 
A 1 242 PHE 242 242 242 PHE PHE AAA . n 
A 1 243 ASP 243 243 243 ASP ASP AAA . n 
A 1 244 ARG 244 244 244 ARG ARG AAA . n 
A 1 245 GLN 245 245 245 GLN GLN AAA . n 
A 1 246 CYS 246 246 246 CYS CYS AAA . n 
A 1 247 SER 247 247 247 SER SER AAA . n 
A 1 248 GLU 248 248 248 GLU GLU AAA . n 
A 1 249 LYS 249 249 249 LYS LYS AAA . n 
A 1 250 ILE 250 250 250 ILE ILE AAA . n 
A 1 251 VAL 251 251 251 VAL VAL AAA . n 
A 1 252 GLU 252 252 252 GLU GLU AAA . n 
A 1 253 TYR 253 253 253 TYR TYR AAA . n 
A 1 254 MET 254 254 254 MET MET AAA . n 
A 1 255 LYS 255 255 255 LYS LYS AAA . n 
A 1 256 ALA 256 256 256 ALA ALA AAA . n 
A 1 257 THR 257 257 257 THR THR AAA . n 
A 1 258 GLY 258 258 258 GLY GLY AAA . n 
A 1 259 THR 259 259 259 THR THR AAA . n 
A 1 260 LYS 260 260 260 LYS LYS AAA . n 
A 1 261 PHE 261 261 261 PHE PHE AAA . n 
A 1 262 LEU 262 262 262 LEU LEU AAA . n 
A 1 263 VAL 263 263 263 VAL VAL AAA . n 
A 1 264 GLY 264 264 264 GLY GLY AAA . n 
A 1 265 VAL 265 265 265 VAL VAL AAA . n 
A 1 266 VAL 266 266 266 VAL VAL AAA . n 
A 1 267 PRO 267 267 267 PRO PRO AAA . n 
A 1 268 ILE 268 268 268 ILE ILE AAA . n 
A 1 269 ASN 269 269 269 ASN ASN AAA . n 
A 1 270 ILE 270 270 270 ILE ILE AAA . n 
A 1 271 GLU 271 271 271 GLU GLU AAA . n 
A 1 272 LYS 272 272 272 LYS LYS AAA . n 
A 1 273 VAL 273 273 273 VAL VAL AAA . n 
A 1 274 ASN 274 274 274 ASN ASN AAA . n 
A 1 275 GLU 275 275 275 GLU GLU AAA . n 
A 1 276 ASN 276 276 276 ASN ASN AAA . n 
A 1 277 ILE 277 277 277 ILE ILE AAA . n 
A 1 278 LYS 278 278 278 LYS LYS AAA . n 
A 1 279 VAL 279 279 279 VAL VAL AAA . n 
A 1 280 SER 280 280 280 SER SER AAA . n 
A 1 281 PHE 281 281 281 PHE PHE AAA . n 
A 1 282 SER 282 282 282 SER SER AAA . n 
A 1 283 ASP 283 283 283 ASP ASP AAA . n 
A 1 284 GLY 284 284 284 GLY GLY AAA . n 
A 1 285 SER 285 285 285 SER SER AAA . n 
A 1 286 VAL 286 286 286 VAL VAL AAA . n 
A 1 287 GLU 287 287 287 GLU GLU AAA . n 
A 1 288 GLU 288 288 288 GLU GLU AAA . n 
A 1 289 PHE 289 289 289 PHE PHE AAA . n 
A 1 290 GLU 290 290 290 GLU GLU AAA . n 
A 1 291 THR 291 291 291 THR THR AAA . n 
A 1 292 VAL 292 292 292 VAL VAL AAA . n 
A 1 293 LEU 293 293 293 LEU LEU AAA . n 
A 1 294 TYR 294 294 294 TYR TYR AAA . n 
A 1 295 ALA 295 295 295 ALA ALA AAA . n 
A 1 296 THR 296 296 296 THR THR AAA . n 
A 1 297 GLY 297 297 297 GLY GLY AAA . n 
A 1 298 ARG 298 298 298 ARG ARG AAA . n 
A 1 299 ASN 299 299 299 ASN ASN AAA . n 
A 1 300 PRO 300 300 300 PRO PRO AAA . n 
A 1 301 ASP 301 301 301 ASP ASP AAA . n 
A 1 302 VAL 302 302 302 VAL VAL AAA . n 
A 1 303 LYS 303 303 303 LYS LYS AAA . n 
A 1 304 GLY 304 304 304 GLY GLY AAA . n 
A 1 305 LEU 305 305 305 LEU LEU AAA . n 
A 1 306 ASN 306 306 306 ASN ASN AAA . n 
A 1 307 LEU 307 307 307 LEU LEU AAA . n 
A 1 308 ASN 308 308 308 ASN ASN AAA . n 
A 1 309 ALA 309 309 309 ALA ALA AAA . n 
A 1 310 ILE 310 310 310 ILE ILE AAA . n 
A 1 311 GLY 311 311 311 GLY GLY AAA . n 
A 1 312 VAL 312 312 312 VAL VAL AAA . n 
A 1 313 GLU 313 313 313 GLU GLU AAA . n 
A 1 314 VAL 314 314 314 VAL VAL AAA . n 
A 1 315 SER 315 315 315 SER SER AAA . n 
A 1 316 ASP 316 316 316 ASP ASP AAA . n 
A 1 317 SER 317 317 317 SER SER AAA . n 
A 1 318 GLY 318 318 318 GLY GLY AAA . n 
A 1 319 LYS 319 319 319 LYS LYS AAA . n 
A 1 320 ILE 320 320 320 ILE ILE AAA . n 
A 1 321 ILE 321 321 321 ILE ILE AAA . n 
A 1 322 ALA 322 322 322 ALA ALA AAA . n 
A 1 323 PRO 323 323 323 PRO PRO AAA . n 
A 1 324 LYS 324 324 324 LYS LYS AAA . n 
A 1 325 ASP 325 325 325 ASP ASP AAA . n 
A 1 326 ALA 326 326 326 ALA ALA AAA . n 
A 1 327 THR 327 327 327 THR THR AAA . n 
A 1 328 SER 328 328 328 SER SER AAA . n 
A 1 329 VAL 329 329 329 VAL VAL AAA . n 
A 1 330 PRO 330 330 330 PRO PRO AAA . n 
A 1 331 SER 331 331 331 SER SER AAA . n 
A 1 332 ILE 332 332 332 ILE ILE AAA . n 
A 1 333 PHE 333 333 333 PHE PHE AAA . n 
A 1 334 ALA 334 334 334 ALA ALA AAA . n 
A 1 335 VAL 335 335 335 VAL VAL AAA . n 
A 1 336 GLY 336 336 336 GLY GLY AAA . n 
A 1 337 ASP 337 337 337 ASP ASP AAA . n 
A 1 338 ILE 338 338 338 ILE ILE AAA . n 
A 1 339 VAL 339 339 339 VAL VAL AAA . n 
A 1 340 GLU 340 340 340 GLU GLU AAA . n 
A 1 341 GLY 341 341 341 GLY GLY AAA . n 
A 1 342 ARG 342 342 342 ARG ARG AAA . n 
A 1 343 PRO 343 343 343 PRO PRO AAA . n 
A 1 344 GLU 344 344 344 GLU GLU AAA . n 
A 1 345 LEU 345 345 345 LEU LEU AAA . n 
A 1 346 THR 346 346 346 THR THR AAA . n 
A 1 347 PRO 347 347 347 PRO PRO AAA . n 
A 1 348 VAL 348 348 348 VAL VAL AAA . n 
A 1 349 ALA 349 349 349 ALA ALA AAA . n 
A 1 350 VAL 350 350 350 VAL VAL AAA . n 
A 1 351 LYS 351 351 351 LYS LYS AAA . n 
A 1 352 ALA 352 352 352 ALA ALA AAA . n 
A 1 353 GLY 353 353 353 GLY GLY AAA . n 
A 1 354 ILE 354 354 354 ILE ILE AAA . n 
A 1 355 LEU 355 355 355 LEU LEU AAA . n 
A 1 356 LEU 356 356 356 LEU LEU AAA . n 
A 1 357 ALA 357 357 357 ALA ALA AAA . n 
A 1 358 ARG 358 358 358 ARG ARG AAA . n 
A 1 359 ARG 359 359 359 ARG ARG AAA . n 
A 1 360 LEU 360 360 360 LEU LEU AAA . n 
A 1 361 PHE 361 361 361 PHE PHE AAA . n 
A 1 362 ALA 362 362 362 ALA ALA AAA . n 
A 1 363 GLY 363 363 363 GLY GLY AAA . n 
A 1 364 SER 364 364 364 SER SER AAA . n 
A 1 365 ASN 365 365 365 ASN ASN AAA . n 
A 1 366 GLU 366 366 366 GLU GLU AAA . n 
A 1 367 PHE 367 367 367 PHE PHE AAA . n 
A 1 368 ILE 368 368 368 ILE ILE AAA . n 
A 1 369 ASP 369 369 369 ASP ASP AAA . n 
A 1 370 TYR 370 370 370 TYR TYR AAA . n 
A 1 371 ASP 371 371 371 ASP ASP AAA . n 
A 1 372 PHE 372 372 372 PHE PHE AAA . n 
A 1 373 VAL 373 373 373 VAL VAL AAA . n 
A 1 374 PRO 374 374 374 PRO PRO AAA . n 
A 1 375 THR 375 375 375 THR THR AAA . n 
A 1 376 THR 376 376 376 THR THR AAA . n 
A 1 377 VAL 377 377 377 VAL VAL AAA . n 
A 1 378 PHE 378 378 378 PHE PHE AAA . n 
A 1 379 THR 379 379 379 THR THR AAA . n 
A 1 380 PRO 380 380 380 PRO PRO AAA . n 
A 1 381 ILE 381 381 381 ILE ILE AAA . n 
A 1 382 GLU 382 382 382 GLU GLU AAA . n 
A 1 383 TYR 383 383 383 TYR TYR AAA . n 
A 1 384 GLY 384 384 384 GLY GLY AAA . n 
A 1 385 HIS 385 385 385 HIS HIS AAA . n 
A 1 386 VAL 386 386 386 VAL VAL AAA . n 
A 1 387 GLY 387 387 387 GLY GLY AAA . n 
A 1 388 LEU 388 388 388 LEU LEU AAA . n 
A 1 389 SER 389 389 389 SER SER AAA . n 
A 1 390 SER 390 390 390 SER SER AAA . n 
A 1 391 GLU 391 391 391 GLU GLU AAA . n 
A 1 392 ALA 392 392 392 ALA ALA AAA . n 
A 1 393 ALA 393 393 393 ALA ALA AAA . n 
A 1 394 ILE 394 394 394 ILE ILE AAA . n 
A 1 395 ALA 395 395 395 ALA ALA AAA . n 
A 1 396 LYS 396 396 396 LYS LYS AAA . n 
A 1 397 TYR 397 397 397 TYR TYR AAA . n 
A 1 398 GLY 398 398 398 GLY GLY AAA . n 
A 1 399 GLU 399 399 399 GLU GLU AAA . n 
A 1 400 ASP 400 400 400 ASP ASP AAA . n 
A 1 401 ASP 401 401 401 ASP ASP AAA . n 
A 1 402 ILE 402 402 402 ILE ILE AAA . n 
A 1 403 GLU 403 403 403 GLU GLU AAA . n 
A 1 404 GLU 404 404 404 GLU GLU AAA . n 
A 1 405 TYR 405 405 405 TYR TYR AAA . n 
A 1 406 LEU 406 406 406 LEU LEU AAA . n 
A 1 407 SER 407 407 407 SER SER AAA . n 
A 1 408 GLU 408 408 408 GLU GLU AAA . n 
A 1 409 PHE 409 409 409 PHE PHE AAA . n 
A 1 410 SER 410 410 410 SER SER AAA . n 
A 1 411 THR 411 411 411 THR THR AAA . n 
A 1 412 LEU 412 412 412 LEU LEU AAA . n 
A 1 413 GLU 413 413 413 GLU GLU AAA . n 
A 1 414 ILE 414 414 414 ILE ILE AAA . n 
A 1 415 ALA 415 415 415 ALA ALA AAA . n 
A 1 416 ALA 416 416 416 ALA ALA AAA . n 
A 1 417 ALA 417 417 417 ALA ALA AAA . n 
A 1 418 HIS 418 418 418 HIS HIS AAA . n 
A 1 419 ARG 419 419 419 ARG ARG AAA . n 
A 1 420 GLU 420 420 420 GLU GLU AAA . n 
A 1 421 LYS 421 421 421 LYS LYS AAA . n 
A 1 422 PRO 422 422 422 PRO PRO AAA . n 
A 1 423 GLU 423 423 423 GLU GLU AAA . n 
A 1 424 HIS 424 424 424 HIS HIS AAA . n 
A 1 425 LEU 425 425 425 LEU LEU AAA . n 
A 1 426 ARG 426 426 426 ARG ARG AAA . n 
A 1 427 GLU 427 427 427 GLU GLU AAA . n 
A 1 428 ASN 428 428 428 ASN ASN AAA . n 
A 1 429 GLU 429 429 429 GLU GLU AAA . n 
A 1 430 MET 430 430 430 MET MET AAA . n 
A 1 431 ASP 431 431 431 ASP ASP AAA . n 
A 1 432 PHE 432 432 432 PHE PHE AAA . n 
A 1 433 ALA 433 433 433 ALA ALA AAA . n 
A 1 434 LEU 434 434 434 LEU LEU AAA . n 
A 1 435 PRO 435 435 435 PRO PRO AAA . n 
A 1 436 LEU 436 436 436 LEU LEU AAA . n 
A 1 437 ASN 437 437 437 ASN ASN AAA . n 
A 1 438 CYS 438 438 438 CYS CYS AAA . n 
A 1 439 LEU 439 439 439 LEU LEU AAA . n 
A 1 440 ALA 440 440 440 ALA ALA AAA . n 
A 1 441 LYS 441 441 441 LYS LYS AAA . n 
A 1 442 LEU 442 442 442 LEU LEU AAA . n 
A 1 443 VAL 443 443 443 VAL VAL AAA . n 
A 1 444 VAL 444 444 444 VAL VAL AAA . n 
A 1 445 VAL 445 445 445 VAL VAL AAA . n 
A 1 446 LYS 446 446 446 LYS LYS AAA . n 
A 1 447 SER 447 447 447 SER SER AAA . n 
A 1 448 GLN 448 448 448 GLN GLN AAA . n 
A 1 449 GLY 449 449 449 GLY GLY AAA . n 
A 1 450 GLU 450 450 450 GLU GLU AAA . n 
A 1 451 LYS 451 451 451 LYS LYS AAA . n 
A 1 452 VAL 452 452 452 VAL VAL AAA . n 
A 1 453 VAL 453 453 453 VAL VAL AAA . n 
A 1 454 GLY 454 454 454 GLY GLY AAA . n 
A 1 455 PHE 455 455 455 PHE PHE AAA . n 
A 1 456 HIS 456 456 456 HIS HIS AAA . n 
A 1 457 PHE 457 457 457 PHE PHE AAA . n 
A 1 458 VAL 458 458 458 VAL VAL AAA . n 
A 1 459 GLY 459 459 459 GLY GLY AAA . n 
A 1 460 PRO 460 460 460 PRO PRO AAA . n 
A 1 461 ASN 461 461 461 ASN ASN AAA . n 
A 1 462 ALA 462 462 462 ALA ALA AAA . n 
A 1 463 GLY 463 463 463 GLY GLY AAA . n 
A 1 464 GLU 464 464 464 GLU GLU AAA . n 
A 1 465 ILE 465 465 465 ILE ILE AAA . n 
A 1 466 THR 466 466 466 THR THR AAA . n 
A 1 467 GLN 467 467 467 GLN GLN AAA . n 
A 1 468 GLY 468 468 468 GLY GLY AAA . n 
A 1 469 PHE 469 469 469 PHE PHE AAA . n 
A 1 470 SER 470 470 470 SER SER AAA . n 
A 1 471 LEU 471 471 471 LEU LEU AAA . n 
A 1 472 ALA 472 472 472 ALA ALA AAA . n 
A 1 473 VAL 473 473 473 VAL VAL AAA . n 
A 1 474 LYS 474 474 474 LYS LYS AAA . n 
A 1 475 LEU 475 475 475 LEU LEU AAA . n 
A 1 476 GLY 476 476 476 GLY GLY AAA . n 
A 1 477 ALA 477 477 477 ALA ALA AAA . n 
A 1 478 THR 478 478 478 THR THR AAA . n 
A 1 479 LYS 479 479 479 LYS LYS AAA . n 
A 1 480 LYS 480 480 480 LYS LYS AAA . n 
A 1 481 ASP 481 481 481 ASP ASP AAA . n 
A 1 482 PHE 482 482 482 PHE PHE AAA . n 
A 1 483 ASP 483 483 483 ASP ASP AAA . n 
A 1 484 ASP 484 484 484 ASP ASP AAA . n 
A 1 485 MET 485 485 485 MET MET AAA . n 
A 1 486 ILE 486 486 486 ILE ILE AAA . n 
A 1 487 GLY 487 487 487 GLY GLY AAA . n 
A 1 488 ILE 488 488 488 ILE ILE AAA . n 
A 1 489 HIS 489 489 489 HIS HIS AAA . n 
A 1 490 PRO 490 490 490 PRO PRO AAA . n 
A 1 491 THR 491 491 491 THR THR AAA . n 
A 1 492 ASP 492 492 492 ASP ASP AAA . n 
A 1 493 ALA 493 493 493 ALA ALA AAA . n 
A 1 494 GLU 494 494 494 GLU GLU AAA . n 
A 1 495 VAL 495 495 495 VAL VAL AAA . n 
A 1 496 PHE 496 496 496 PHE PHE AAA . n 
A 1 497 GLY 497 497 497 GLY GLY AAA . n 
A 1 498 ILE 498 498 498 ILE ILE AAA . n 
A 1 499 LEU 499 499 499 LEU LEU AAA . n 
A 1 500 GLU 500 500 500 GLU GLU AAA . n 
A 1 501 VAL 501 501 501 VAL VAL AAA . n 
A 1 502 THR 502 502 502 THR THR AAA . n 
A 1 503 LYS 503 503 503 LYS LYS AAA . n 
A 1 504 ARG 504 504 504 ARG ARG AAA . n 
A 1 505 SER 505 505 505 SER SER AAA . n 
A 1 506 GLY 506 506 506 GLY GLY AAA . n 
A 1 507 GLU 507 507 507 GLU GLU AAA . n 
A 1 508 SER 508 508 508 SER SER AAA . n 
A 1 509 PHE 509 509 509 PHE PHE AAA . n 
A 1 510 VAL 510 510 510 VAL VAL AAA . n 
A 1 511 SER 511 511 511 SER SER AAA . n 
A 1 512 SER 512 512 512 SER SER AAA . n 
A 1 513 GLY 513 513 513 GLY GLY AAA . n 
A 1 514 GLY 514 514 514 GLY GLY AAA . n 
A 1 515 CYS 515 515 515 CYS CYS AAA . n 
A 1 516 GLY 516 516 516 GLY GLY AAA . n 
A 1 517 GLY 517 517 517 GLY GLY AAA . n 
A 1 518 GLY 518 518 518 GLY GLY AAA . n 
A 1 519 LYS 519 519 519 LYS LYS AAA . n 
A 1 520 CYS 520 520 520 CYS CYS AAA . n 
A 1 521 GLY 521 521 521 GLY GLY AAA . n 
B 1 1   MET 1   1   ?   ?   ?   BBB . n 
B 1 2   LYS 2   2   ?   ?   ?   BBB . n 
B 1 3   PHE 3   3   ?   ?   ?   BBB . n 
B 1 4   THR 4   4   ?   ?   ?   BBB . n 
B 1 5   LEU 5   5   ?   ?   ?   BBB . n 
B 1 6   VAL 6   6   ?   ?   ?   BBB . n 
B 1 7   THR 7   7   ?   ?   ?   BBB . n 
B 1 8   ILE 8   8   ?   ?   ?   BBB . n 
B 1 9   LEU 9   9   ?   ?   ?   BBB . n 
B 1 10  PHE 10  10  ?   ?   ?   BBB . n 
B 1 11  LEU 11  11  ?   ?   ?   BBB . n 
B 1 12  ILE 12  12  ?   ?   ?   BBB . n 
B 1 13  PHE 13  13  ?   ?   ?   BBB . n 
B 1 14  MET 14  14  ?   ?   ?   BBB . n 
B 1 15  LYS 15  15  ?   ?   ?   BBB . n 
B 1 16  LYS 16  16  ?   ?   ?   BBB . n 
B 1 17  ALA 17  17  ?   ?   ?   BBB . n 
B 1 18  LYS 18  18  ?   ?   ?   BBB . n 
B 1 19  ILE 19  19  ?   ?   ?   BBB . n 
B 1 20  VAL 20  20  ?   ?   ?   BBB . n 
B 1 21  MET 21  21  ?   ?   ?   BBB . n 
B 1 22  ALA 22  22  ?   ?   ?   BBB . n 
B 1 23  ASP 23  23  ?   ?   ?   BBB . n 
B 1 24  LEU 24  24  24  LEU LEU BBB . n 
B 1 25  THR 25  25  25  THR THR BBB . n 
B 1 26  PHE 26  26  26  PHE PHE BBB . n 
B 1 27  MET 27  27  27  MET MET BBB . n 
B 1 28  TYR 28  28  28  TYR TYR BBB . n 
B 1 29  ASP 29  29  29  ASP ASP BBB . n 
B 1 30  LEU 30  30  30  LEU LEU BBB . n 
B 1 31  VAL 31  31  31  VAL VAL BBB . n 
B 1 32  VAL 32  32  32  VAL VAL BBB . n 
B 1 33  ILE 33  33  33  ILE ILE BBB . n 
B 1 34  GLY 34  34  34  GLY GLY BBB . n 
B 1 35  GLY 35  35  35  GLY GLY BBB . n 
B 1 36  GLY 36  36  36  GLY GLY BBB . n 
B 1 37  SER 37  37  37  SER SER BBB . n 
B 1 38  GLY 38  38  38  GLY GLY BBB . n 
B 1 39  GLY 39  39  39  GLY GLY BBB . n 
B 1 40  MET 40  40  40  MET MET BBB . n 
B 1 41  ALA 41  41  41  ALA ALA BBB . n 
B 1 42  ALA 42  42  42  ALA ALA BBB . n 
B 1 43  ALA 43  43  43  ALA ALA BBB . n 
B 1 44  LYS 44  44  44  LYS LYS BBB . n 
B 1 45  GLU 45  45  45  GLU GLU BBB . n 
B 1 46  ALA 46  46  46  ALA ALA BBB . n 
B 1 47  ALA 47  47  47  ALA ALA BBB . n 
B 1 48  LYS 48  48  48  LYS LYS BBB . n 
B 1 49  TYR 49  49  49  TYR TYR BBB . n 
B 1 50  GLY 50  50  50  GLY GLY BBB . n 
B 1 51  LYS 51  51  51  LYS LYS BBB . n 
B 1 52  LYS 52  52  52  LYS LYS BBB . n 
B 1 53  VAL 53  53  53  VAL VAL BBB . n 
B 1 54  ALA 54  54  54  ALA ALA BBB . n 
B 1 55  LEU 55  55  55  LEU LEU BBB . n 
B 1 56  PHE 56  56  56  PHE PHE BBB . n 
B 1 57  ASP 57  57  57  ASP ASP BBB . n 
B 1 58  PHE 58  58  58  PHE PHE BBB . n 
B 1 59  VAL 59  59  59  VAL VAL BBB . n 
B 1 60  LYS 60  60  60  LYS LYS BBB . n 
B 1 61  PRO 61  61  61  PRO PRO BBB . n 
B 1 62  SER 62  62  62  SER SER BBB . n 
B 1 63  THR 63  63  63  THR THR BBB . n 
B 1 64  GLN 64  64  64  GLN GLN BBB . n 
B 1 65  GLY 65  65  65  GLY GLY BBB . n 
B 1 66  THR 66  66  66  THR THR BBB . n 
B 1 67  LYS 67  67  67  LYS LYS BBB . n 
B 1 68  TRP 68  68  68  TRP TRP BBB . n 
B 1 69  GLY 69  69  69  GLY GLY BBB . n 
B 1 70  LEU 70  70  70  LEU LEU BBB . n 
B 1 71  GLY 71  71  71  GLY GLY BBB . n 
B 1 72  GLY 72  72  72  GLY GLY BBB . n 
B 1 73  THR 73  73  73  THR THR BBB . n 
B 1 74  CYS 74  74  74  CYS CYS BBB . n 
B 1 75  VAL 75  75  75  VAL VAL BBB . n 
B 1 76  ASN 76  76  76  ASN ASN BBB . n 
B 1 77  VAL 77  77  77  VAL VAL BBB . n 
B 1 78  GLY 78  78  78  GLY GLY BBB . n 
B 1 79  CYS 79  79  79  CYS CYS BBB . n 
B 1 80  VAL 80  80  80  VAL VAL BBB . n 
B 1 81  PRO 81  81  81  PRO PRO BBB . n 
B 1 82  LYS 82  82  82  LYS LYS BBB . n 
B 1 83  LYS 83  83  83  LYS LYS BBB . n 
B 1 84  LEU 84  84  84  LEU LEU BBB . n 
B 1 85  MET 85  85  85  MET MET BBB . n 
B 1 86  HIS 86  86  86  HIS HIS BBB . n 
B 1 87  TYR 87  87  87  TYR TYR BBB . n 
B 1 88  SER 88  88  88  SER SER BBB . n 
B 1 89  ALA 89  89  89  ALA ALA BBB . n 
B 1 90  LEU 90  90  90  LEU LEU BBB . n 
B 1 91  ILE 91  91  91  ILE ILE BBB . n 
B 1 92  ALA 92  92  92  ALA ALA BBB . n 
B 1 93  SER 93  93  93  SER SER BBB . n 
B 1 94  SER 94  94  94  SER SER BBB . n 
B 1 95  ILE 95  95  95  ILE ILE BBB . n 
B 1 96  HIS 96  96  96  HIS HIS BBB . n 
B 1 97  HIS 97  97  97  HIS HIS BBB . n 
B 1 98  ASP 98  98  98  ASP ASP BBB . n 
B 1 99  ALA 99  99  99  ALA ALA BBB . n 
B 1 100 GLN 100 100 100 GLN GLN BBB . n 
B 1 101 MET 101 101 101 MET MET BBB . n 
B 1 102 PHE 102 102 102 PHE PHE BBB . n 
B 1 103 GLY 103 103 103 GLY GLY BBB . n 
B 1 104 HIS 104 104 104 HIS HIS BBB . n 
B 1 105 LYS 105 105 105 LYS LYS BBB . n 
B 1 106 THR 106 106 106 THR THR BBB . n 
B 1 107 SER 107 107 107 SER SER BBB . n 
B 1 108 SER 108 108 108 SER SER BBB . n 
B 1 109 SER 109 109 109 SER SER BBB . n 
B 1 110 PHE 110 110 110 PHE PHE BBB . n 
B 1 111 GLU 111 111 111 GLU GLU BBB . n 
B 1 112 TRP 112 112 112 TRP TRP BBB . n 
B 1 113 GLY 113 113 113 GLY GLY BBB . n 
B 1 114 LYS 114 114 114 LYS LYS BBB . n 
B 1 115 LEU 115 115 115 LEU LEU BBB . n 
B 1 116 VAL 116 116 116 VAL VAL BBB . n 
B 1 117 GLU 117 117 117 GLU GLU BBB . n 
B 1 118 THR 118 118 118 THR THR BBB . n 
B 1 119 LEU 119 119 119 LEU LEU BBB . n 
B 1 120 ARG 120 120 120 ARG ARG BBB . n 
B 1 121 ASN 121 121 121 ASN ASN BBB . n 
B 1 122 HIS 122 122 122 HIS HIS BBB . n 
B 1 123 ILE 123 123 123 ILE ILE BBB . n 
B 1 124 ARG 124 124 124 ARG ARG BBB . n 
B 1 125 MET 125 125 125 MET MET BBB . n 
B 1 126 LEU 126 126 126 LEU LEU BBB . n 
B 1 127 ASN 127 127 127 ASN ASN BBB . n 
B 1 128 PHE 128 128 128 PHE PHE BBB . n 
B 1 129 SER 129 129 129 SER SER BBB . n 
B 1 130 TYR 130 130 130 TYR TYR BBB . n 
B 1 131 ARG 131 131 131 ARG ARG BBB . n 
B 1 132 THR 132 132 132 THR THR BBB . n 
B 1 133 GLY 133 133 133 GLY GLY BBB . n 
B 1 134 LEU 134 134 134 LEU LEU BBB . n 
B 1 135 ARG 135 135 135 ARG ARG BBB . n 
B 1 136 VAL 136 136 136 VAL VAL BBB . n 
B 1 137 GLY 137 137 137 GLY GLY BBB . n 
B 1 138 ASN 138 138 138 ASN ASN BBB . n 
B 1 139 VAL 139 139 139 VAL VAL BBB . n 
B 1 140 GLU 140 140 140 GLU GLU BBB . n 
B 1 141 TYR 141 141 141 TYR TYR BBB . n 
B 1 142 ILE 142 142 142 ILE ILE BBB . n 
B 1 143 ASN 143 143 143 ASN ASN BBB . n 
B 1 144 ALA 144 144 144 ALA ALA BBB . n 
B 1 145 LEU 145 145 145 LEU LEU BBB . n 
B 1 146 ALA 146 146 146 ALA ALA BBB . n 
B 1 147 LYS 147 147 147 LYS LYS BBB . n 
B 1 148 LEU 148 148 148 LEU LEU BBB . n 
B 1 149 ILE 149 149 149 ILE ILE BBB . n 
B 1 150 ASP 150 150 150 ASP ASP BBB . n 
B 1 151 PRO 151 151 151 PRO PRO BBB . n 
B 1 152 HIS 152 152 152 HIS HIS BBB . n 
B 1 153 SER 153 153 153 SER SER BBB . n 
B 1 154 VAL 154 154 154 VAL VAL BBB . n 
B 1 155 GLU 155 155 155 GLU GLU BBB . n 
B 1 156 TYR 156 156 156 TYR TYR BBB . n 
B 1 157 GLU 157 157 157 GLU GLU BBB . n 
B 1 158 ASP 158 158 158 ASP ASP BBB . n 
B 1 159 ASN 159 159 159 ASN ASN BBB . n 
B 1 160 GLY 160 160 160 GLY GLY BBB . n 
B 1 161 GLN 161 161 161 GLN GLN BBB . n 
B 1 162 LYS 162 162 162 LYS LYS BBB . n 
B 1 163 LYS 163 163 163 LYS LYS BBB . n 
B 1 164 THR 164 164 164 THR THR BBB . n 
B 1 165 ILE 165 165 165 ILE ILE BBB . n 
B 1 166 THR 166 166 166 THR THR BBB . n 
B 1 167 SER 167 167 167 SER SER BBB . n 
B 1 168 ARG 168 168 168 ARG ARG BBB . n 
B 1 169 TYR 169 169 169 TYR TYR BBB . n 
B 1 170 ILE 170 170 170 ILE ILE BBB . n 
B 1 171 LEU 171 171 171 LEU LEU BBB . n 
B 1 172 LEU 172 172 172 LEU LEU BBB . n 
B 1 173 ALA 173 173 173 ALA ALA BBB . n 
B 1 174 THR 174 174 174 THR THR BBB . n 
B 1 175 GLY 175 175 175 GLY GLY BBB . n 
B 1 176 GLY 176 176 176 GLY GLY BBB . n 
B 1 177 ARG 177 177 177 ARG ARG BBB . n 
B 1 178 PRO 178 178 178 PRO PRO BBB . n 
B 1 179 SER 179 179 179 SER SER BBB . n 
B 1 180 ILE 180 180 180 ILE ILE BBB . n 
B 1 181 PRO 181 181 181 PRO PRO BBB . n 
B 1 182 GLU 182 182 182 GLU GLU BBB . n 
B 1 183 THR 183 183 183 THR THR BBB . n 
B 1 184 VAL 184 184 184 VAL VAL BBB . n 
B 1 185 PRO 185 185 185 PRO PRO BBB . n 
B 1 186 GLY 186 186 186 GLY GLY BBB . n 
B 1 187 ALA 187 187 187 ALA ALA BBB . n 
B 1 188 ILE 188 188 188 ILE ILE BBB . n 
B 1 189 GLN 189 189 189 GLN GLN BBB . n 
B 1 190 TYR 190 190 190 TYR TYR BBB . n 
B 1 191 SER 191 191 191 SER SER BBB . n 
B 1 192 ILE 192 192 192 ILE ILE BBB . n 
B 1 193 THR 193 193 193 THR THR BBB . n 
B 1 194 SER 194 194 194 SER SER BBB . n 
B 1 195 ASP 195 195 195 ASP ASP BBB . n 
B 1 196 ASP 196 196 196 ASP ASP BBB . n 
B 1 197 ILE 197 197 197 ILE ILE BBB . n 
B 1 198 PHE 198 198 198 PHE PHE BBB . n 
B 1 199 PHE 199 199 199 PHE PHE BBB . n 
B 1 200 LEU 200 200 200 LEU LEU BBB . n 
B 1 201 SER 201 201 201 SER SER BBB . n 
B 1 202 LYS 202 202 202 LYS LYS BBB . n 
B 1 203 SER 203 203 203 SER SER BBB . n 
B 1 204 PRO 204 204 204 PRO PRO BBB . n 
B 1 205 GLY 205 205 205 GLY GLY BBB . n 
B 1 206 LYS 206 206 206 LYS LYS BBB . n 
B 1 207 THR 207 207 207 THR THR BBB . n 
B 1 208 LEU 208 208 208 LEU LEU BBB . n 
B 1 209 VAL 209 209 209 VAL VAL BBB . n 
B 1 210 ILE 210 210 210 ILE ILE BBB . n 
B 1 211 GLY 211 211 211 GLY GLY BBB . n 
B 1 212 ALA 212 212 212 ALA ALA BBB . n 
B 1 213 SER 213 213 213 SER SER BBB . n 
B 1 214 TYR 214 214 214 TYR TYR BBB . n 
B 1 215 ILE 215 215 215 ILE ILE BBB . n 
B 1 216 GLY 216 216 216 GLY GLY BBB . n 
B 1 217 LEU 217 217 217 LEU LEU BBB . n 
B 1 218 GLU 218 218 218 GLU GLU BBB . n 
B 1 219 THR 219 219 219 THR THR BBB . n 
B 1 220 ALA 220 220 220 ALA ALA BBB . n 
B 1 221 GLY 221 221 221 GLY GLY BBB . n 
B 1 222 PHE 222 222 222 PHE PHE BBB . n 
B 1 223 LEU 223 223 223 LEU LEU BBB . n 
B 1 224 ASN 224 224 224 ASN ASN BBB . n 
B 1 225 GLU 225 225 225 GLU GLU BBB . n 
B 1 226 LEU 226 226 226 LEU LEU BBB . n 
B 1 227 GLY 227 227 227 GLY GLY BBB . n 
B 1 228 PHE 228 228 228 PHE PHE BBB . n 
B 1 229 ASP 229 229 229 ASP ASP BBB . n 
B 1 230 THR 230 230 230 THR THR BBB . n 
B 1 231 THR 231 231 231 THR THR BBB . n 
B 1 232 VAL 232 232 232 VAL VAL BBB . n 
B 1 233 ALA 233 233 233 ALA ALA BBB . n 
B 1 234 MET 234 234 234 MET MET BBB . n 
B 1 235 ARG 235 235 235 ARG ARG BBB . n 
B 1 236 SER 236 236 236 SER SER BBB . n 
B 1 237 ILE 237 237 237 ILE ILE BBB . n 
B 1 238 PRO 238 238 238 PRO PRO BBB . n 
B 1 239 LEU 239 239 239 LEU LEU BBB . n 
B 1 240 ARG 240 240 240 ARG ARG BBB . n 
B 1 241 GLY 241 241 241 GLY GLY BBB . n 
B 1 242 PHE 242 242 242 PHE PHE BBB . n 
B 1 243 ASP 243 243 243 ASP ASP BBB . n 
B 1 244 ARG 244 244 244 ARG ARG BBB . n 
B 1 245 GLN 245 245 245 GLN GLN BBB . n 
B 1 246 CYS 246 246 246 CYS CYS BBB . n 
B 1 247 SER 247 247 247 SER SER BBB . n 
B 1 248 GLU 248 248 248 GLU GLU BBB . n 
B 1 249 LYS 249 249 249 LYS LYS BBB . n 
B 1 250 ILE 250 250 250 ILE ILE BBB . n 
B 1 251 VAL 251 251 251 VAL VAL BBB . n 
B 1 252 GLU 252 252 252 GLU GLU BBB . n 
B 1 253 TYR 253 253 253 TYR TYR BBB . n 
B 1 254 MET 254 254 254 MET MET BBB . n 
B 1 255 LYS 255 255 255 LYS LYS BBB . n 
B 1 256 ALA 256 256 256 ALA ALA BBB . n 
B 1 257 THR 257 257 257 THR THR BBB . n 
B 1 258 GLY 258 258 258 GLY GLY BBB . n 
B 1 259 THR 259 259 259 THR THR BBB . n 
B 1 260 LYS 260 260 260 LYS LYS BBB . n 
B 1 261 PHE 261 261 261 PHE PHE BBB . n 
B 1 262 LEU 262 262 262 LEU LEU BBB . n 
B 1 263 VAL 263 263 263 VAL VAL BBB . n 
B 1 264 GLY 264 264 264 GLY GLY BBB . n 
B 1 265 VAL 265 265 265 VAL VAL BBB . n 
B 1 266 VAL 266 266 266 VAL VAL BBB . n 
B 1 267 PRO 267 267 267 PRO PRO BBB . n 
B 1 268 ILE 268 268 268 ILE ILE BBB . n 
B 1 269 ASN 269 269 269 ASN ASN BBB . n 
B 1 270 ILE 270 270 270 ILE ILE BBB . n 
B 1 271 GLU 271 271 271 GLU GLU BBB . n 
B 1 272 LYS 272 272 272 LYS LYS BBB . n 
B 1 273 VAL 273 273 273 VAL VAL BBB . n 
B 1 274 ASN 274 274 274 ASN ASN BBB . n 
B 1 275 GLU 275 275 275 GLU GLU BBB . n 
B 1 276 ASN 276 276 276 ASN ASN BBB . n 
B 1 277 ILE 277 277 277 ILE ILE BBB . n 
B 1 278 LYS 278 278 278 LYS LYS BBB . n 
B 1 279 VAL 279 279 279 VAL VAL BBB . n 
B 1 280 SER 280 280 280 SER SER BBB . n 
B 1 281 PHE 281 281 281 PHE PHE BBB . n 
B 1 282 SER 282 282 282 SER SER BBB . n 
B 1 283 ASP 283 283 283 ASP ASP BBB . n 
B 1 284 GLY 284 284 284 GLY GLY BBB . n 
B 1 285 SER 285 285 285 SER SER BBB . n 
B 1 286 VAL 286 286 286 VAL VAL BBB . n 
B 1 287 GLU 287 287 287 GLU GLU BBB . n 
B 1 288 GLU 288 288 288 GLU GLU BBB . n 
B 1 289 PHE 289 289 289 PHE PHE BBB . n 
B 1 290 GLU 290 290 290 GLU GLU BBB . n 
B 1 291 THR 291 291 291 THR THR BBB . n 
B 1 292 VAL 292 292 292 VAL VAL BBB . n 
B 1 293 LEU 293 293 293 LEU LEU BBB . n 
B 1 294 TYR 294 294 294 TYR TYR BBB . n 
B 1 295 ALA 295 295 295 ALA ALA BBB . n 
B 1 296 THR 296 296 296 THR THR BBB . n 
B 1 297 GLY 297 297 297 GLY GLY BBB . n 
B 1 298 ARG 298 298 298 ARG ARG BBB . n 
B 1 299 ASN 299 299 299 ASN ASN BBB . n 
B 1 300 PRO 300 300 300 PRO PRO BBB . n 
B 1 301 ASP 301 301 301 ASP ASP BBB . n 
B 1 302 VAL 302 302 302 VAL VAL BBB . n 
B 1 303 LYS 303 303 303 LYS LYS BBB . n 
B 1 304 GLY 304 304 304 GLY GLY BBB . n 
B 1 305 LEU 305 305 305 LEU LEU BBB . n 
B 1 306 ASN 306 306 306 ASN ASN BBB . n 
B 1 307 LEU 307 307 307 LEU LEU BBB . n 
B 1 308 ASN 308 308 308 ASN ASN BBB . n 
B 1 309 ALA 309 309 309 ALA ALA BBB . n 
B 1 310 ILE 310 310 310 ILE ILE BBB . n 
B 1 311 GLY 311 311 311 GLY GLY BBB . n 
B 1 312 VAL 312 312 312 VAL VAL BBB . n 
B 1 313 GLU 313 313 313 GLU GLU BBB . n 
B 1 314 VAL 314 314 314 VAL VAL BBB . n 
B 1 315 SER 315 315 315 SER SER BBB . n 
B 1 316 ASP 316 316 316 ASP ASP BBB . n 
B 1 317 SER 317 317 317 SER SER BBB . n 
B 1 318 GLY 318 318 318 GLY GLY BBB . n 
B 1 319 LYS 319 319 319 LYS LYS BBB . n 
B 1 320 ILE 320 320 320 ILE ILE BBB . n 
B 1 321 ILE 321 321 321 ILE ILE BBB . n 
B 1 322 ALA 322 322 322 ALA ALA BBB . n 
B 1 323 PRO 323 323 323 PRO PRO BBB . n 
B 1 324 LYS 324 324 324 LYS LYS BBB . n 
B 1 325 ASP 325 325 325 ASP ASP BBB . n 
B 1 326 ALA 326 326 326 ALA ALA BBB . n 
B 1 327 THR 327 327 327 THR THR BBB . n 
B 1 328 SER 328 328 328 SER SER BBB . n 
B 1 329 VAL 329 329 329 VAL VAL BBB . n 
B 1 330 PRO 330 330 330 PRO PRO BBB . n 
B 1 331 SER 331 331 331 SER SER BBB . n 
B 1 332 ILE 332 332 332 ILE ILE BBB . n 
B 1 333 PHE 333 333 333 PHE PHE BBB . n 
B 1 334 ALA 334 334 334 ALA ALA BBB . n 
B 1 335 VAL 335 335 335 VAL VAL BBB . n 
B 1 336 GLY 336 336 336 GLY GLY BBB . n 
B 1 337 ASP 337 337 337 ASP ASP BBB . n 
B 1 338 ILE 338 338 338 ILE ILE BBB . n 
B 1 339 VAL 339 339 339 VAL VAL BBB . n 
B 1 340 GLU 340 340 340 GLU GLU BBB . n 
B 1 341 GLY 341 341 341 GLY GLY BBB . n 
B 1 342 ARG 342 342 342 ARG ARG BBB . n 
B 1 343 PRO 343 343 343 PRO PRO BBB . n 
B 1 344 GLU 344 344 344 GLU GLU BBB . n 
B 1 345 LEU 345 345 345 LEU LEU BBB . n 
B 1 346 THR 346 346 346 THR THR BBB . n 
B 1 347 PRO 347 347 347 PRO PRO BBB . n 
B 1 348 VAL 348 348 348 VAL VAL BBB . n 
B 1 349 ALA 349 349 349 ALA ALA BBB . n 
B 1 350 VAL 350 350 350 VAL VAL BBB . n 
B 1 351 LYS 351 351 351 LYS LYS BBB . n 
B 1 352 ALA 352 352 352 ALA ALA BBB . n 
B 1 353 GLY 353 353 353 GLY GLY BBB . n 
B 1 354 ILE 354 354 354 ILE ILE BBB . n 
B 1 355 LEU 355 355 355 LEU LEU BBB . n 
B 1 356 LEU 356 356 356 LEU LEU BBB . n 
B 1 357 ALA 357 357 357 ALA ALA BBB . n 
B 1 358 ARG 358 358 358 ARG ARG BBB . n 
B 1 359 ARG 359 359 359 ARG ARG BBB . n 
B 1 360 LEU 360 360 360 LEU LEU BBB . n 
B 1 361 PHE 361 361 361 PHE PHE BBB . n 
B 1 362 ALA 362 362 362 ALA ALA BBB . n 
B 1 363 GLY 363 363 363 GLY GLY BBB . n 
B 1 364 SER 364 364 364 SER SER BBB . n 
B 1 365 ASN 365 365 365 ASN ASN BBB . n 
B 1 366 GLU 366 366 366 GLU GLU BBB . n 
B 1 367 PHE 367 367 367 PHE PHE BBB . n 
B 1 368 ILE 368 368 368 ILE ILE BBB . n 
B 1 369 ASP 369 369 369 ASP ASP BBB . n 
B 1 370 TYR 370 370 370 TYR TYR BBB . n 
B 1 371 ASP 371 371 371 ASP ASP BBB . n 
B 1 372 PHE 372 372 372 PHE PHE BBB . n 
B 1 373 VAL 373 373 373 VAL VAL BBB . n 
B 1 374 PRO 374 374 374 PRO PRO BBB . n 
B 1 375 THR 375 375 375 THR THR BBB . n 
B 1 376 THR 376 376 376 THR THR BBB . n 
B 1 377 VAL 377 377 377 VAL VAL BBB . n 
B 1 378 PHE 378 378 378 PHE PHE BBB . n 
B 1 379 THR 379 379 379 THR THR BBB . n 
B 1 380 PRO 380 380 380 PRO PRO BBB . n 
B 1 381 ILE 381 381 381 ILE ILE BBB . n 
B 1 382 GLU 382 382 382 GLU GLU BBB . n 
B 1 383 TYR 383 383 383 TYR TYR BBB . n 
B 1 384 GLY 384 384 384 GLY GLY BBB . n 
B 1 385 HIS 385 385 385 HIS HIS BBB . n 
B 1 386 VAL 386 386 386 VAL VAL BBB . n 
B 1 387 GLY 387 387 387 GLY GLY BBB . n 
B 1 388 LEU 388 388 388 LEU LEU BBB . n 
B 1 389 SER 389 389 389 SER SER BBB . n 
B 1 390 SER 390 390 390 SER SER BBB . n 
B 1 391 GLU 391 391 391 GLU GLU BBB . n 
B 1 392 ALA 392 392 392 ALA ALA BBB . n 
B 1 393 ALA 393 393 393 ALA ALA BBB . n 
B 1 394 ILE 394 394 394 ILE ILE BBB . n 
B 1 395 ALA 395 395 395 ALA ALA BBB . n 
B 1 396 LYS 396 396 396 LYS LYS BBB . n 
B 1 397 TYR 397 397 397 TYR TYR BBB . n 
B 1 398 GLY 398 398 398 GLY GLY BBB . n 
B 1 399 GLU 399 399 399 GLU GLU BBB . n 
B 1 400 ASP 400 400 400 ASP ASP BBB . n 
B 1 401 ASP 401 401 401 ASP ASP BBB . n 
B 1 402 ILE 402 402 402 ILE ILE BBB . n 
B 1 403 GLU 403 403 403 GLU GLU BBB . n 
B 1 404 GLU 404 404 404 GLU GLU BBB . n 
B 1 405 TYR 405 405 405 TYR TYR BBB . n 
B 1 406 LEU 406 406 406 LEU LEU BBB . n 
B 1 407 SER 407 407 407 SER SER BBB . n 
B 1 408 GLU 408 408 408 GLU GLU BBB . n 
B 1 409 PHE 409 409 409 PHE PHE BBB . n 
B 1 410 SER 410 410 410 SER SER BBB . n 
B 1 411 THR 411 411 411 THR THR BBB . n 
B 1 412 LEU 412 412 412 LEU LEU BBB . n 
B 1 413 GLU 413 413 413 GLU GLU BBB . n 
B 1 414 ILE 414 414 414 ILE ILE BBB . n 
B 1 415 ALA 415 415 415 ALA ALA BBB . n 
B 1 416 ALA 416 416 416 ALA ALA BBB . n 
B 1 417 ALA 417 417 417 ALA ALA BBB . n 
B 1 418 HIS 418 418 418 HIS HIS BBB . n 
B 1 419 ARG 419 419 419 ARG ARG BBB . n 
B 1 420 GLU 420 420 420 GLU GLU BBB . n 
B 1 421 LYS 421 421 421 LYS LYS BBB . n 
B 1 422 PRO 422 422 422 PRO PRO BBB . n 
B 1 423 GLU 423 423 423 GLU GLU BBB . n 
B 1 424 HIS 424 424 424 HIS HIS BBB . n 
B 1 425 LEU 425 425 425 LEU LEU BBB . n 
B 1 426 ARG 426 426 426 ARG ARG BBB . n 
B 1 427 GLU 427 427 427 GLU GLU BBB . n 
B 1 428 ASN 428 428 428 ASN ASN BBB . n 
B 1 429 GLU 429 429 429 GLU GLU BBB . n 
B 1 430 MET 430 430 430 MET MET BBB . n 
B 1 431 ASP 431 431 431 ASP ASP BBB . n 
B 1 432 PHE 432 432 432 PHE PHE BBB . n 
B 1 433 ALA 433 433 433 ALA ALA BBB . n 
B 1 434 LEU 434 434 434 LEU LEU BBB . n 
B 1 435 PRO 435 435 435 PRO PRO BBB . n 
B 1 436 LEU 436 436 436 LEU LEU BBB . n 
B 1 437 ASN 437 437 437 ASN ASN BBB . n 
B 1 438 CYS 438 438 438 CYS CYS BBB . n 
B 1 439 LEU 439 439 439 LEU LEU BBB . n 
B 1 440 ALA 440 440 440 ALA ALA BBB . n 
B 1 441 LYS 441 441 441 LYS LYS BBB . n 
B 1 442 LEU 442 442 442 LEU LEU BBB . n 
B 1 443 VAL 443 443 443 VAL VAL BBB . n 
B 1 444 VAL 444 444 444 VAL VAL BBB . n 
B 1 445 VAL 445 445 445 VAL VAL BBB . n 
B 1 446 LYS 446 446 446 LYS LYS BBB . n 
B 1 447 SER 447 447 447 SER SER BBB . n 
B 1 448 GLN 448 448 448 GLN GLN BBB . n 
B 1 449 GLY 449 449 449 GLY GLY BBB . n 
B 1 450 GLU 450 450 450 GLU GLU BBB . n 
B 1 451 LYS 451 451 451 LYS LYS BBB . n 
B 1 452 VAL 452 452 452 VAL VAL BBB . n 
B 1 453 VAL 453 453 453 VAL VAL BBB . n 
B 1 454 GLY 454 454 454 GLY GLY BBB . n 
B 1 455 PHE 455 455 455 PHE PHE BBB . n 
B 1 456 HIS 456 456 456 HIS HIS BBB . n 
B 1 457 PHE 457 457 457 PHE PHE BBB . n 
B 1 458 VAL 458 458 458 VAL VAL BBB . n 
B 1 459 GLY 459 459 459 GLY GLY BBB . n 
B 1 460 PRO 460 460 460 PRO PRO BBB . n 
B 1 461 ASN 461 461 461 ASN ASN BBB . n 
B 1 462 ALA 462 462 462 ALA ALA BBB . n 
B 1 463 GLY 463 463 463 GLY GLY BBB . n 
B 1 464 GLU 464 464 464 GLU GLU BBB . n 
B 1 465 ILE 465 465 465 ILE ILE BBB . n 
B 1 466 THR 466 466 466 THR THR BBB . n 
B 1 467 GLN 467 467 467 GLN GLN BBB . n 
B 1 468 GLY 468 468 468 GLY GLY BBB . n 
B 1 469 PHE 469 469 469 PHE PHE BBB . n 
B 1 470 SER 470 470 470 SER SER BBB . n 
B 1 471 LEU 471 471 471 LEU LEU BBB . n 
B 1 472 ALA 472 472 472 ALA ALA BBB . n 
B 1 473 VAL 473 473 473 VAL VAL BBB . n 
B 1 474 LYS 474 474 474 LYS LYS BBB . n 
B 1 475 LEU 475 475 475 LEU LEU BBB . n 
B 1 476 GLY 476 476 476 GLY GLY BBB . n 
B 1 477 ALA 477 477 477 ALA ALA BBB . n 
B 1 478 THR 478 478 478 THR THR BBB . n 
B 1 479 LYS 479 479 479 LYS LYS BBB . n 
B 1 480 LYS 480 480 480 LYS LYS BBB . n 
B 1 481 ASP 481 481 481 ASP ASP BBB . n 
B 1 482 PHE 482 482 482 PHE PHE BBB . n 
B 1 483 ASP 483 483 483 ASP ASP BBB . n 
B 1 484 ASP 484 484 484 ASP ASP BBB . n 
B 1 485 MET 485 485 485 MET MET BBB . n 
B 1 486 ILE 486 486 486 ILE ILE BBB . n 
B 1 487 GLY 487 487 487 GLY GLY BBB . n 
B 1 488 ILE 488 488 488 ILE ILE BBB . n 
B 1 489 HIS 489 489 489 HIS HIS BBB . n 
B 1 490 PRO 490 490 490 PRO PRO BBB . n 
B 1 491 THR 491 491 491 THR THR BBB . n 
B 1 492 ASP 492 492 492 ASP ASP BBB . n 
B 1 493 ALA 493 493 493 ALA ALA BBB . n 
B 1 494 GLU 494 494 494 GLU GLU BBB . n 
B 1 495 VAL 495 495 495 VAL VAL BBB . n 
B 1 496 PHE 496 496 496 PHE PHE BBB . n 
B 1 497 GLY 497 497 497 GLY GLY BBB . n 
B 1 498 ILE 498 498 498 ILE ILE BBB . n 
B 1 499 LEU 499 499 499 LEU LEU BBB . n 
B 1 500 GLU 500 500 500 GLU GLU BBB . n 
B 1 501 VAL 501 501 501 VAL VAL BBB . n 
B 1 502 THR 502 502 502 THR THR BBB . n 
B 1 503 LYS 503 503 503 LYS LYS BBB . n 
B 1 504 ARG 504 504 504 ARG ARG BBB . n 
B 1 505 SER 505 505 505 SER SER BBB . n 
B 1 506 GLY 506 506 506 GLY GLY BBB . n 
B 1 507 GLU 507 507 507 GLU GLU BBB . n 
B 1 508 SER 508 508 508 SER SER BBB . n 
B 1 509 PHE 509 509 509 PHE PHE BBB . n 
B 1 510 VAL 510 510 510 VAL VAL BBB . n 
B 1 511 SER 511 511 511 SER SER BBB . n 
B 1 512 SER 512 512 512 SER SER BBB . n 
B 1 513 GLY 513 513 513 GLY GLY BBB . n 
B 1 514 GLY 514 514 514 GLY GLY BBB . n 
B 1 515 CYS 515 515 515 CYS CYS BBB . n 
B 1 516 GLY 516 516 516 GLY GLY BBB . n 
B 1 517 GLY 517 517 517 GLY GLY BBB . n 
B 1 518 GLY 518 518 518 GLY GLY BBB . n 
B 1 519 LYS 519 519 ?   ?   ?   BBB . n 
B 1 520 CYS 520 520 ?   ?   ?   BBB . n 
B 1 521 GLY 521 521 ?   ?   ?   BBB . n 
C 1 1   MET 1   1   ?   ?   ?   CCC . n 
C 1 2   LYS 2   2   ?   ?   ?   CCC . n 
C 1 3   PHE 3   3   ?   ?   ?   CCC . n 
C 1 4   THR 4   4   ?   ?   ?   CCC . n 
C 1 5   LEU 5   5   ?   ?   ?   CCC . n 
C 1 6   VAL 6   6   ?   ?   ?   CCC . n 
C 1 7   THR 7   7   ?   ?   ?   CCC . n 
C 1 8   ILE 8   8   ?   ?   ?   CCC . n 
C 1 9   LEU 9   9   ?   ?   ?   CCC . n 
C 1 10  PHE 10  10  ?   ?   ?   CCC . n 
C 1 11  LEU 11  11  ?   ?   ?   CCC . n 
C 1 12  ILE 12  12  ?   ?   ?   CCC . n 
C 1 13  PHE 13  13  ?   ?   ?   CCC . n 
C 1 14  MET 14  14  ?   ?   ?   CCC . n 
C 1 15  LYS 15  15  ?   ?   ?   CCC . n 
C 1 16  LYS 16  16  ?   ?   ?   CCC . n 
C 1 17  ALA 17  17  ?   ?   ?   CCC . n 
C 1 18  LYS 18  18  ?   ?   ?   CCC . n 
C 1 19  ILE 19  19  ?   ?   ?   CCC . n 
C 1 20  VAL 20  20  ?   ?   ?   CCC . n 
C 1 21  MET 21  21  ?   ?   ?   CCC . n 
C 1 22  ALA 22  22  ?   ?   ?   CCC . n 
C 1 23  ASP 23  23  ?   ?   ?   CCC . n 
C 1 24  LEU 24  24  24  LEU LEU CCC . n 
C 1 25  THR 25  25  25  THR THR CCC . n 
C 1 26  PHE 26  26  26  PHE PHE CCC . n 
C 1 27  MET 27  27  27  MET MET CCC . n 
C 1 28  TYR 28  28  28  TYR TYR CCC . n 
C 1 29  ASP 29  29  29  ASP ASP CCC . n 
C 1 30  LEU 30  30  30  LEU LEU CCC . n 
C 1 31  VAL 31  31  31  VAL VAL CCC . n 
C 1 32  VAL 32  32  32  VAL VAL CCC . n 
C 1 33  ILE 33  33  33  ILE ILE CCC . n 
C 1 34  GLY 34  34  34  GLY GLY CCC . n 
C 1 35  GLY 35  35  35  GLY GLY CCC . n 
C 1 36  GLY 36  36  36  GLY GLY CCC . n 
C 1 37  SER 37  37  37  SER SER CCC . n 
C 1 38  GLY 38  38  38  GLY GLY CCC . n 
C 1 39  GLY 39  39  39  GLY GLY CCC . n 
C 1 40  MET 40  40  40  MET MET CCC . n 
C 1 41  ALA 41  41  41  ALA ALA CCC . n 
C 1 42  ALA 42  42  42  ALA ALA CCC . n 
C 1 43  ALA 43  43  43  ALA ALA CCC . n 
C 1 44  LYS 44  44  44  LYS LYS CCC . n 
C 1 45  GLU 45  45  45  GLU GLU CCC . n 
C 1 46  ALA 46  46  46  ALA ALA CCC . n 
C 1 47  ALA 47  47  47  ALA ALA CCC . n 
C 1 48  LYS 48  48  48  LYS LYS CCC . n 
C 1 49  TYR 49  49  49  TYR TYR CCC . n 
C 1 50  GLY 50  50  50  GLY GLY CCC . n 
C 1 51  LYS 51  51  51  LYS LYS CCC . n 
C 1 52  LYS 52  52  52  LYS LYS CCC . n 
C 1 53  VAL 53  53  53  VAL VAL CCC . n 
C 1 54  ALA 54  54  54  ALA ALA CCC . n 
C 1 55  LEU 55  55  55  LEU LEU CCC . n 
C 1 56  PHE 56  56  56  PHE PHE CCC . n 
C 1 57  ASP 57  57  57  ASP ASP CCC . n 
C 1 58  PHE 58  58  58  PHE PHE CCC . n 
C 1 59  VAL 59  59  59  VAL VAL CCC . n 
C 1 60  LYS 60  60  60  LYS LYS CCC . n 
C 1 61  PRO 61  61  61  PRO PRO CCC . n 
C 1 62  SER 62  62  62  SER SER CCC . n 
C 1 63  THR 63  63  63  THR THR CCC . n 
C 1 64  GLN 64  64  64  GLN GLN CCC . n 
C 1 65  GLY 65  65  65  GLY GLY CCC . n 
C 1 66  THR 66  66  66  THR THR CCC . n 
C 1 67  LYS 67  67  67  LYS LYS CCC . n 
C 1 68  TRP 68  68  68  TRP TRP CCC . n 
C 1 69  GLY 69  69  69  GLY GLY CCC . n 
C 1 70  LEU 70  70  70  LEU LEU CCC . n 
C 1 71  GLY 71  71  71  GLY GLY CCC . n 
C 1 72  GLY 72  72  72  GLY GLY CCC . n 
C 1 73  THR 73  73  73  THR THR CCC . n 
C 1 74  CYS 74  74  74  CYS CYS CCC . n 
C 1 75  VAL 75  75  75  VAL VAL CCC . n 
C 1 76  ASN 76  76  76  ASN ASN CCC . n 
C 1 77  VAL 77  77  77  VAL VAL CCC . n 
C 1 78  GLY 78  78  78  GLY GLY CCC . n 
C 1 79  CYS 79  79  79  CYS CYS CCC . n 
C 1 80  VAL 80  80  80  VAL VAL CCC . n 
C 1 81  PRO 81  81  81  PRO PRO CCC . n 
C 1 82  LYS 82  82  82  LYS LYS CCC . n 
C 1 83  LYS 83  83  83  LYS LYS CCC . n 
C 1 84  LEU 84  84  84  LEU LEU CCC . n 
C 1 85  MET 85  85  85  MET MET CCC . n 
C 1 86  HIS 86  86  86  HIS HIS CCC . n 
C 1 87  TYR 87  87  87  TYR TYR CCC . n 
C 1 88  SER 88  88  88  SER SER CCC . n 
C 1 89  ALA 89  89  89  ALA ALA CCC . n 
C 1 90  LEU 90  90  90  LEU LEU CCC . n 
C 1 91  ILE 91  91  91  ILE ILE CCC . n 
C 1 92  ALA 92  92  92  ALA ALA CCC . n 
C 1 93  SER 93  93  93  SER SER CCC . n 
C 1 94  SER 94  94  94  SER SER CCC . n 
C 1 95  ILE 95  95  95  ILE ILE CCC . n 
C 1 96  HIS 96  96  96  HIS HIS CCC . n 
C 1 97  HIS 97  97  97  HIS HIS CCC . n 
C 1 98  ASP 98  98  98  ASP ASP CCC . n 
C 1 99  ALA 99  99  99  ALA ALA CCC . n 
C 1 100 GLN 100 100 100 GLN GLN CCC . n 
C 1 101 MET 101 101 101 MET MET CCC . n 
C 1 102 PHE 102 102 102 PHE PHE CCC . n 
C 1 103 GLY 103 103 103 GLY GLY CCC . n 
C 1 104 HIS 104 104 104 HIS HIS CCC . n 
C 1 105 LYS 105 105 105 LYS LYS CCC . n 
C 1 106 THR 106 106 106 THR THR CCC . n 
C 1 107 SER 107 107 107 SER SER CCC . n 
C 1 108 SER 108 108 108 SER SER CCC . n 
C 1 109 SER 109 109 109 SER SER CCC . n 
C 1 110 PHE 110 110 110 PHE PHE CCC . n 
C 1 111 GLU 111 111 111 GLU GLU CCC . n 
C 1 112 TRP 112 112 112 TRP TRP CCC . n 
C 1 113 GLY 113 113 113 GLY GLY CCC . n 
C 1 114 LYS 114 114 114 LYS LYS CCC . n 
C 1 115 LEU 115 115 115 LEU LEU CCC . n 
C 1 116 VAL 116 116 116 VAL VAL CCC . n 
C 1 117 GLU 117 117 117 GLU GLU CCC . n 
C 1 118 THR 118 118 118 THR THR CCC . n 
C 1 119 LEU 119 119 119 LEU LEU CCC . n 
C 1 120 ARG 120 120 120 ARG ARG CCC . n 
C 1 121 ASN 121 121 121 ASN ASN CCC . n 
C 1 122 HIS 122 122 122 HIS HIS CCC . n 
C 1 123 ILE 123 123 123 ILE ILE CCC . n 
C 1 124 ARG 124 124 124 ARG ARG CCC . n 
C 1 125 MET 125 125 125 MET MET CCC . n 
C 1 126 LEU 126 126 126 LEU LEU CCC . n 
C 1 127 ASN 127 127 127 ASN ASN CCC . n 
C 1 128 PHE 128 128 128 PHE PHE CCC . n 
C 1 129 SER 129 129 129 SER SER CCC . n 
C 1 130 TYR 130 130 130 TYR TYR CCC . n 
C 1 131 ARG 131 131 131 ARG ARG CCC . n 
C 1 132 THR 132 132 132 THR THR CCC . n 
C 1 133 GLY 133 133 133 GLY GLY CCC . n 
C 1 134 LEU 134 134 134 LEU LEU CCC . n 
C 1 135 ARG 135 135 135 ARG ARG CCC . n 
C 1 136 VAL 136 136 136 VAL VAL CCC . n 
C 1 137 GLY 137 137 137 GLY GLY CCC . n 
C 1 138 ASN 138 138 138 ASN ASN CCC . n 
C 1 139 VAL 139 139 139 VAL VAL CCC . n 
C 1 140 GLU 140 140 140 GLU GLU CCC . n 
C 1 141 TYR 141 141 141 TYR TYR CCC . n 
C 1 142 ILE 142 142 142 ILE ILE CCC . n 
C 1 143 ASN 143 143 143 ASN ASN CCC . n 
C 1 144 ALA 144 144 144 ALA ALA CCC . n 
C 1 145 LEU 145 145 145 LEU LEU CCC . n 
C 1 146 ALA 146 146 146 ALA ALA CCC . n 
C 1 147 LYS 147 147 147 LYS LYS CCC . n 
C 1 148 LEU 148 148 148 LEU LEU CCC . n 
C 1 149 ILE 149 149 149 ILE ILE CCC . n 
C 1 150 ASP 150 150 150 ASP ASP CCC . n 
C 1 151 PRO 151 151 151 PRO PRO CCC . n 
C 1 152 HIS 152 152 152 HIS HIS CCC . n 
C 1 153 SER 153 153 153 SER SER CCC . n 
C 1 154 VAL 154 154 154 VAL VAL CCC . n 
C 1 155 GLU 155 155 155 GLU GLU CCC . n 
C 1 156 TYR 156 156 156 TYR TYR CCC . n 
C 1 157 GLU 157 157 157 GLU GLU CCC . n 
C 1 158 ASP 158 158 158 ASP ASP CCC . n 
C 1 159 ASN 159 159 159 ASN ASN CCC . n 
C 1 160 GLY 160 160 160 GLY GLY CCC . n 
C 1 161 GLN 161 161 161 GLN GLN CCC . n 
C 1 162 LYS 162 162 162 LYS LYS CCC . n 
C 1 163 LYS 163 163 163 LYS LYS CCC . n 
C 1 164 THR 164 164 164 THR THR CCC . n 
C 1 165 ILE 165 165 165 ILE ILE CCC . n 
C 1 166 THR 166 166 166 THR THR CCC . n 
C 1 167 SER 167 167 167 SER SER CCC . n 
C 1 168 ARG 168 168 168 ARG ARG CCC . n 
C 1 169 TYR 169 169 169 TYR TYR CCC . n 
C 1 170 ILE 170 170 170 ILE ILE CCC . n 
C 1 171 LEU 171 171 171 LEU LEU CCC . n 
C 1 172 LEU 172 172 172 LEU LEU CCC . n 
C 1 173 ALA 173 173 173 ALA ALA CCC . n 
C 1 174 THR 174 174 174 THR THR CCC . n 
C 1 175 GLY 175 175 175 GLY GLY CCC . n 
C 1 176 GLY 176 176 176 GLY GLY CCC . n 
C 1 177 ARG 177 177 177 ARG ARG CCC . n 
C 1 178 PRO 178 178 178 PRO PRO CCC . n 
C 1 179 SER 179 179 179 SER SER CCC . n 
C 1 180 ILE 180 180 180 ILE ILE CCC . n 
C 1 181 PRO 181 181 181 PRO PRO CCC . n 
C 1 182 GLU 182 182 182 GLU GLU CCC . n 
C 1 183 THR 183 183 183 THR THR CCC . n 
C 1 184 VAL 184 184 184 VAL VAL CCC . n 
C 1 185 PRO 185 185 185 PRO PRO CCC . n 
C 1 186 GLY 186 186 186 GLY GLY CCC . n 
C 1 187 ALA 187 187 187 ALA ALA CCC . n 
C 1 188 ILE 188 188 188 ILE ILE CCC . n 
C 1 189 GLN 189 189 189 GLN GLN CCC . n 
C 1 190 TYR 190 190 190 TYR TYR CCC . n 
C 1 191 SER 191 191 191 SER SER CCC . n 
C 1 192 ILE 192 192 192 ILE ILE CCC . n 
C 1 193 THR 193 193 193 THR THR CCC . n 
C 1 194 SER 194 194 194 SER SER CCC . n 
C 1 195 ASP 195 195 195 ASP ASP CCC . n 
C 1 196 ASP 196 196 196 ASP ASP CCC . n 
C 1 197 ILE 197 197 197 ILE ILE CCC . n 
C 1 198 PHE 198 198 198 PHE PHE CCC . n 
C 1 199 PHE 199 199 199 PHE PHE CCC . n 
C 1 200 LEU 200 200 200 LEU LEU CCC . n 
C 1 201 SER 201 201 201 SER SER CCC . n 
C 1 202 LYS 202 202 202 LYS LYS CCC . n 
C 1 203 SER 203 203 203 SER SER CCC . n 
C 1 204 PRO 204 204 204 PRO PRO CCC . n 
C 1 205 GLY 205 205 205 GLY GLY CCC . n 
C 1 206 LYS 206 206 206 LYS LYS CCC . n 
C 1 207 THR 207 207 207 THR THR CCC . n 
C 1 208 LEU 208 208 208 LEU LEU CCC . n 
C 1 209 VAL 209 209 209 VAL VAL CCC . n 
C 1 210 ILE 210 210 210 ILE ILE CCC . n 
C 1 211 GLY 211 211 211 GLY GLY CCC . n 
C 1 212 ALA 212 212 212 ALA ALA CCC . n 
C 1 213 SER 213 213 213 SER SER CCC . n 
C 1 214 TYR 214 214 214 TYR TYR CCC . n 
C 1 215 ILE 215 215 215 ILE ILE CCC . n 
C 1 216 GLY 216 216 216 GLY GLY CCC . n 
C 1 217 LEU 217 217 217 LEU LEU CCC . n 
C 1 218 GLU 218 218 218 GLU GLU CCC . n 
C 1 219 THR 219 219 219 THR THR CCC . n 
C 1 220 ALA 220 220 220 ALA ALA CCC . n 
C 1 221 GLY 221 221 221 GLY GLY CCC . n 
C 1 222 PHE 222 222 222 PHE PHE CCC . n 
C 1 223 LEU 223 223 223 LEU LEU CCC . n 
C 1 224 ASN 224 224 224 ASN ASN CCC . n 
C 1 225 GLU 225 225 225 GLU GLU CCC . n 
C 1 226 LEU 226 226 226 LEU LEU CCC . n 
C 1 227 GLY 227 227 227 GLY GLY CCC . n 
C 1 228 PHE 228 228 228 PHE PHE CCC . n 
C 1 229 ASP 229 229 229 ASP ASP CCC . n 
C 1 230 THR 230 230 230 THR THR CCC . n 
C 1 231 THR 231 231 231 THR THR CCC . n 
C 1 232 VAL 232 232 232 VAL VAL CCC . n 
C 1 233 ALA 233 233 233 ALA ALA CCC . n 
C 1 234 MET 234 234 234 MET MET CCC . n 
C 1 235 ARG 235 235 235 ARG ARG CCC . n 
C 1 236 SER 236 236 236 SER SER CCC . n 
C 1 237 ILE 237 237 237 ILE ILE CCC . n 
C 1 238 PRO 238 238 238 PRO PRO CCC . n 
C 1 239 LEU 239 239 239 LEU LEU CCC . n 
C 1 240 ARG 240 240 240 ARG ARG CCC . n 
C 1 241 GLY 241 241 241 GLY GLY CCC . n 
C 1 242 PHE 242 242 242 PHE PHE CCC . n 
C 1 243 ASP 243 243 243 ASP ASP CCC . n 
C 1 244 ARG 244 244 244 ARG ARG CCC . n 
C 1 245 GLN 245 245 245 GLN GLN CCC . n 
C 1 246 CYS 246 246 246 CYS CYS CCC . n 
C 1 247 SER 247 247 247 SER SER CCC . n 
C 1 248 GLU 248 248 248 GLU GLU CCC . n 
C 1 249 LYS 249 249 249 LYS LYS CCC . n 
C 1 250 ILE 250 250 250 ILE ILE CCC . n 
C 1 251 VAL 251 251 251 VAL VAL CCC . n 
C 1 252 GLU 252 252 252 GLU GLU CCC . n 
C 1 253 TYR 253 253 253 TYR TYR CCC . n 
C 1 254 MET 254 254 254 MET MET CCC . n 
C 1 255 LYS 255 255 255 LYS LYS CCC . n 
C 1 256 ALA 256 256 256 ALA ALA CCC . n 
C 1 257 THR 257 257 257 THR THR CCC . n 
C 1 258 GLY 258 258 258 GLY GLY CCC . n 
C 1 259 THR 259 259 259 THR THR CCC . n 
C 1 260 LYS 260 260 260 LYS LYS CCC . n 
C 1 261 PHE 261 261 261 PHE PHE CCC . n 
C 1 262 LEU 262 262 262 LEU LEU CCC . n 
C 1 263 VAL 263 263 263 VAL VAL CCC . n 
C 1 264 GLY 264 264 264 GLY GLY CCC . n 
C 1 265 VAL 265 265 265 VAL VAL CCC . n 
C 1 266 VAL 266 266 266 VAL VAL CCC . n 
C 1 267 PRO 267 267 267 PRO PRO CCC . n 
C 1 268 ILE 268 268 268 ILE ILE CCC . n 
C 1 269 ASN 269 269 269 ASN ASN CCC . n 
C 1 270 ILE 270 270 270 ILE ILE CCC . n 
C 1 271 GLU 271 271 271 GLU GLU CCC . n 
C 1 272 LYS 272 272 272 LYS LYS CCC . n 
C 1 273 VAL 273 273 273 VAL VAL CCC . n 
C 1 274 ASN 274 274 274 ASN ASN CCC . n 
C 1 275 GLU 275 275 275 GLU GLU CCC . n 
C 1 276 ASN 276 276 276 ASN ASN CCC . n 
C 1 277 ILE 277 277 277 ILE ILE CCC . n 
C 1 278 LYS 278 278 278 LYS LYS CCC . n 
C 1 279 VAL 279 279 279 VAL VAL CCC . n 
C 1 280 SER 280 280 280 SER SER CCC . n 
C 1 281 PHE 281 281 281 PHE PHE CCC . n 
C 1 282 SER 282 282 282 SER SER CCC . n 
C 1 283 ASP 283 283 283 ASP ASP CCC . n 
C 1 284 GLY 284 284 284 GLY GLY CCC . n 
C 1 285 SER 285 285 285 SER SER CCC . n 
C 1 286 VAL 286 286 286 VAL VAL CCC . n 
C 1 287 GLU 287 287 287 GLU GLU CCC . n 
C 1 288 GLU 288 288 288 GLU GLU CCC . n 
C 1 289 PHE 289 289 289 PHE PHE CCC . n 
C 1 290 GLU 290 290 290 GLU GLU CCC . n 
C 1 291 THR 291 291 291 THR THR CCC . n 
C 1 292 VAL 292 292 292 VAL VAL CCC . n 
C 1 293 LEU 293 293 293 LEU LEU CCC . n 
C 1 294 TYR 294 294 294 TYR TYR CCC . n 
C 1 295 ALA 295 295 295 ALA ALA CCC . n 
C 1 296 THR 296 296 296 THR THR CCC . n 
C 1 297 GLY 297 297 297 GLY GLY CCC . n 
C 1 298 ARG 298 298 298 ARG ARG CCC . n 
C 1 299 ASN 299 299 299 ASN ASN CCC . n 
C 1 300 PRO 300 300 300 PRO PRO CCC . n 
C 1 301 ASP 301 301 301 ASP ASP CCC . n 
C 1 302 VAL 302 302 302 VAL VAL CCC . n 
C 1 303 LYS 303 303 303 LYS LYS CCC . n 
C 1 304 GLY 304 304 304 GLY GLY CCC . n 
C 1 305 LEU 305 305 305 LEU LEU CCC . n 
C 1 306 ASN 306 306 306 ASN ASN CCC . n 
C 1 307 LEU 307 307 307 LEU LEU CCC . n 
C 1 308 ASN 308 308 308 ASN ASN CCC . n 
C 1 309 ALA 309 309 309 ALA ALA CCC . n 
C 1 310 ILE 310 310 310 ILE ILE CCC . n 
C 1 311 GLY 311 311 311 GLY GLY CCC . n 
C 1 312 VAL 312 312 312 VAL VAL CCC . n 
C 1 313 GLU 313 313 313 GLU GLU CCC . n 
C 1 314 VAL 314 314 314 VAL VAL CCC . n 
C 1 315 SER 315 315 315 SER SER CCC . n 
C 1 316 ASP 316 316 316 ASP ASP CCC . n 
C 1 317 SER 317 317 317 SER SER CCC . n 
C 1 318 GLY 318 318 318 GLY GLY CCC . n 
C 1 319 LYS 319 319 319 LYS LYS CCC . n 
C 1 320 ILE 320 320 320 ILE ILE CCC . n 
C 1 321 ILE 321 321 321 ILE ILE CCC . n 
C 1 322 ALA 322 322 322 ALA ALA CCC . n 
C 1 323 PRO 323 323 323 PRO PRO CCC . n 
C 1 324 LYS 324 324 324 LYS LYS CCC . n 
C 1 325 ASP 325 325 325 ASP ASP CCC . n 
C 1 326 ALA 326 326 326 ALA ALA CCC . n 
C 1 327 THR 327 327 327 THR THR CCC . n 
C 1 328 SER 328 328 328 SER SER CCC . n 
C 1 329 VAL 329 329 329 VAL VAL CCC . n 
C 1 330 PRO 330 330 330 PRO PRO CCC . n 
C 1 331 SER 331 331 331 SER SER CCC . n 
C 1 332 ILE 332 332 332 ILE ILE CCC . n 
C 1 333 PHE 333 333 333 PHE PHE CCC . n 
C 1 334 ALA 334 334 334 ALA ALA CCC . n 
C 1 335 VAL 335 335 335 VAL VAL CCC . n 
C 1 336 GLY 336 336 336 GLY GLY CCC . n 
C 1 337 ASP 337 337 337 ASP ASP CCC . n 
C 1 338 ILE 338 338 338 ILE ILE CCC . n 
C 1 339 VAL 339 339 339 VAL VAL CCC . n 
C 1 340 GLU 340 340 340 GLU GLU CCC . n 
C 1 341 GLY 341 341 341 GLY GLY CCC . n 
C 1 342 ARG 342 342 342 ARG ARG CCC . n 
C 1 343 PRO 343 343 343 PRO PRO CCC . n 
C 1 344 GLU 344 344 344 GLU GLU CCC . n 
C 1 345 LEU 345 345 345 LEU LEU CCC . n 
C 1 346 THR 346 346 346 THR THR CCC . n 
C 1 347 PRO 347 347 347 PRO PRO CCC . n 
C 1 348 VAL 348 348 348 VAL VAL CCC . n 
C 1 349 ALA 349 349 349 ALA ALA CCC . n 
C 1 350 VAL 350 350 350 VAL VAL CCC . n 
C 1 351 LYS 351 351 351 LYS LYS CCC . n 
C 1 352 ALA 352 352 352 ALA ALA CCC . n 
C 1 353 GLY 353 353 353 GLY GLY CCC . n 
C 1 354 ILE 354 354 354 ILE ILE CCC . n 
C 1 355 LEU 355 355 355 LEU LEU CCC . n 
C 1 356 LEU 356 356 356 LEU LEU CCC . n 
C 1 357 ALA 357 357 357 ALA ALA CCC . n 
C 1 358 ARG 358 358 358 ARG ARG CCC . n 
C 1 359 ARG 359 359 359 ARG ARG CCC . n 
C 1 360 LEU 360 360 360 LEU LEU CCC . n 
C 1 361 PHE 361 361 361 PHE PHE CCC . n 
C 1 362 ALA 362 362 362 ALA ALA CCC . n 
C 1 363 GLY 363 363 363 GLY GLY CCC . n 
C 1 364 SER 364 364 364 SER SER CCC . n 
C 1 365 ASN 365 365 365 ASN ASN CCC . n 
C 1 366 GLU 366 366 366 GLU GLU CCC . n 
C 1 367 PHE 367 367 367 PHE PHE CCC . n 
C 1 368 ILE 368 368 368 ILE ILE CCC . n 
C 1 369 ASP 369 369 369 ASP ASP CCC . n 
C 1 370 TYR 370 370 370 TYR TYR CCC . n 
C 1 371 ASP 371 371 371 ASP ASP CCC . n 
C 1 372 PHE 372 372 372 PHE PHE CCC . n 
C 1 373 VAL 373 373 373 VAL VAL CCC . n 
C 1 374 PRO 374 374 374 PRO PRO CCC . n 
C 1 375 THR 375 375 375 THR THR CCC . n 
C 1 376 THR 376 376 376 THR THR CCC . n 
C 1 377 VAL 377 377 377 VAL VAL CCC . n 
C 1 378 PHE 378 378 378 PHE PHE CCC . n 
C 1 379 THR 379 379 379 THR THR CCC . n 
C 1 380 PRO 380 380 380 PRO PRO CCC . n 
C 1 381 ILE 381 381 381 ILE ILE CCC . n 
C 1 382 GLU 382 382 382 GLU GLU CCC . n 
C 1 383 TYR 383 383 383 TYR TYR CCC . n 
C 1 384 GLY 384 384 384 GLY GLY CCC . n 
C 1 385 HIS 385 385 385 HIS HIS CCC . n 
C 1 386 VAL 386 386 386 VAL VAL CCC . n 
C 1 387 GLY 387 387 387 GLY GLY CCC . n 
C 1 388 LEU 388 388 388 LEU LEU CCC . n 
C 1 389 SER 389 389 389 SER SER CCC . n 
C 1 390 SER 390 390 390 SER SER CCC . n 
C 1 391 GLU 391 391 391 GLU GLU CCC . n 
C 1 392 ALA 392 392 392 ALA ALA CCC . n 
C 1 393 ALA 393 393 393 ALA ALA CCC . n 
C 1 394 ILE 394 394 394 ILE ILE CCC . n 
C 1 395 ALA 395 395 395 ALA ALA CCC . n 
C 1 396 LYS 396 396 396 LYS LYS CCC . n 
C 1 397 TYR 397 397 397 TYR TYR CCC . n 
C 1 398 GLY 398 398 398 GLY GLY CCC . n 
C 1 399 GLU 399 399 399 GLU GLU CCC . n 
C 1 400 ASP 400 400 400 ASP ASP CCC . n 
C 1 401 ASP 401 401 401 ASP ASP CCC . n 
C 1 402 ILE 402 402 402 ILE ILE CCC . n 
C 1 403 GLU 403 403 403 GLU GLU CCC . n 
C 1 404 GLU 404 404 404 GLU GLU CCC . n 
C 1 405 TYR 405 405 405 TYR TYR CCC . n 
C 1 406 LEU 406 406 406 LEU LEU CCC . n 
C 1 407 SER 407 407 407 SER SER CCC . n 
C 1 408 GLU 408 408 408 GLU GLU CCC . n 
C 1 409 PHE 409 409 409 PHE PHE CCC . n 
C 1 410 SER 410 410 410 SER SER CCC . n 
C 1 411 THR 411 411 411 THR THR CCC . n 
C 1 412 LEU 412 412 412 LEU LEU CCC . n 
C 1 413 GLU 413 413 413 GLU GLU CCC . n 
C 1 414 ILE 414 414 414 ILE ILE CCC . n 
C 1 415 ALA 415 415 415 ALA ALA CCC . n 
C 1 416 ALA 416 416 416 ALA ALA CCC . n 
C 1 417 ALA 417 417 417 ALA ALA CCC . n 
C 1 418 HIS 418 418 418 HIS HIS CCC . n 
C 1 419 ARG 419 419 419 ARG ARG CCC . n 
C 1 420 GLU 420 420 420 GLU GLU CCC . n 
C 1 421 LYS 421 421 421 LYS LYS CCC . n 
C 1 422 PRO 422 422 422 PRO PRO CCC . n 
C 1 423 GLU 423 423 423 GLU GLU CCC . n 
C 1 424 HIS 424 424 424 HIS HIS CCC . n 
C 1 425 LEU 425 425 425 LEU LEU CCC . n 
C 1 426 ARG 426 426 426 ARG ARG CCC . n 
C 1 427 GLU 427 427 427 GLU GLU CCC . n 
C 1 428 ASN 428 428 428 ASN ASN CCC . n 
C 1 429 GLU 429 429 429 GLU GLU CCC . n 
C 1 430 MET 430 430 430 MET MET CCC . n 
C 1 431 ASP 431 431 431 ASP ASP CCC . n 
C 1 432 PHE 432 432 432 PHE PHE CCC . n 
C 1 433 ALA 433 433 433 ALA ALA CCC . n 
C 1 434 LEU 434 434 434 LEU LEU CCC . n 
C 1 435 PRO 435 435 435 PRO PRO CCC . n 
C 1 436 LEU 436 436 436 LEU LEU CCC . n 
C 1 437 ASN 437 437 437 ASN ASN CCC . n 
C 1 438 CYS 438 438 438 CYS CYS CCC . n 
C 1 439 LEU 439 439 439 LEU LEU CCC . n 
C 1 440 ALA 440 440 440 ALA ALA CCC . n 
C 1 441 LYS 441 441 441 LYS LYS CCC . n 
C 1 442 LEU 442 442 442 LEU LEU CCC . n 
C 1 443 VAL 443 443 443 VAL VAL CCC . n 
C 1 444 VAL 444 444 444 VAL VAL CCC . n 
C 1 445 VAL 445 445 445 VAL VAL CCC . n 
C 1 446 LYS 446 446 446 LYS LYS CCC . n 
C 1 447 SER 447 447 447 SER SER CCC . n 
C 1 448 GLN 448 448 448 GLN GLN CCC . n 
C 1 449 GLY 449 449 449 GLY GLY CCC . n 
C 1 450 GLU 450 450 450 GLU GLU CCC . n 
C 1 451 LYS 451 451 451 LYS LYS CCC . n 
C 1 452 VAL 452 452 452 VAL VAL CCC . n 
C 1 453 VAL 453 453 453 VAL VAL CCC . n 
C 1 454 GLY 454 454 454 GLY GLY CCC . n 
C 1 455 PHE 455 455 455 PHE PHE CCC . n 
C 1 456 HIS 456 456 456 HIS HIS CCC . n 
C 1 457 PHE 457 457 457 PHE PHE CCC . n 
C 1 458 VAL 458 458 458 VAL VAL CCC . n 
C 1 459 GLY 459 459 459 GLY GLY CCC . n 
C 1 460 PRO 460 460 460 PRO PRO CCC . n 
C 1 461 ASN 461 461 461 ASN ASN CCC . n 
C 1 462 ALA 462 462 462 ALA ALA CCC . n 
C 1 463 GLY 463 463 463 GLY GLY CCC . n 
C 1 464 GLU 464 464 464 GLU GLU CCC . n 
C 1 465 ILE 465 465 465 ILE ILE CCC . n 
C 1 466 THR 466 466 466 THR THR CCC . n 
C 1 467 GLN 467 467 467 GLN GLN CCC . n 
C 1 468 GLY 468 468 468 GLY GLY CCC . n 
C 1 469 PHE 469 469 469 PHE PHE CCC . n 
C 1 470 SER 470 470 470 SER SER CCC . n 
C 1 471 LEU 471 471 471 LEU LEU CCC . n 
C 1 472 ALA 472 472 472 ALA ALA CCC . n 
C 1 473 VAL 473 473 473 VAL VAL CCC . n 
C 1 474 LYS 474 474 474 LYS LYS CCC . n 
C 1 475 LEU 475 475 475 LEU LEU CCC . n 
C 1 476 GLY 476 476 476 GLY GLY CCC . n 
C 1 477 ALA 477 477 477 ALA ALA CCC . n 
C 1 478 THR 478 478 478 THR THR CCC . n 
C 1 479 LYS 479 479 479 LYS LYS CCC . n 
C 1 480 LYS 480 480 480 LYS LYS CCC . n 
C 1 481 ASP 481 481 481 ASP ASP CCC . n 
C 1 482 PHE 482 482 482 PHE PHE CCC . n 
C 1 483 ASP 483 483 483 ASP ASP CCC . n 
C 1 484 ASP 484 484 484 ASP ASP CCC . n 
C 1 485 MET 485 485 485 MET MET CCC . n 
C 1 486 ILE 486 486 486 ILE ILE CCC . n 
C 1 487 GLY 487 487 487 GLY GLY CCC . n 
C 1 488 ILE 488 488 488 ILE ILE CCC . n 
C 1 489 HIS 489 489 489 HIS HIS CCC . n 
C 1 490 PRO 490 490 490 PRO PRO CCC . n 
C 1 491 THR 491 491 491 THR THR CCC . n 
C 1 492 ASP 492 492 492 ASP ASP CCC . n 
C 1 493 ALA 493 493 493 ALA ALA CCC . n 
C 1 494 GLU 494 494 494 GLU GLU CCC . n 
C 1 495 VAL 495 495 495 VAL VAL CCC . n 
C 1 496 PHE 496 496 496 PHE PHE CCC . n 
C 1 497 GLY 497 497 497 GLY GLY CCC . n 
C 1 498 ILE 498 498 498 ILE ILE CCC . n 
C 1 499 LEU 499 499 499 LEU LEU CCC . n 
C 1 500 GLU 500 500 500 GLU GLU CCC . n 
C 1 501 VAL 501 501 501 VAL VAL CCC . n 
C 1 502 THR 502 502 502 THR THR CCC . n 
C 1 503 LYS 503 503 503 LYS LYS CCC . n 
C 1 504 ARG 504 504 504 ARG ARG CCC . n 
C 1 505 SER 505 505 505 SER SER CCC . n 
C 1 506 GLY 506 506 506 GLY GLY CCC . n 
C 1 507 GLU 507 507 507 GLU GLU CCC . n 
C 1 508 SER 508 508 508 SER SER CCC . n 
C 1 509 PHE 509 509 509 PHE PHE CCC . n 
C 1 510 VAL 510 510 510 VAL VAL CCC . n 
C 1 511 SER 511 511 511 SER SER CCC . n 
C 1 512 SER 512 512 512 SER SER CCC . n 
C 1 513 GLY 513 513 513 GLY GLY CCC . n 
C 1 514 GLY 514 514 514 GLY GLY CCC . n 
C 1 515 CYS 515 515 515 CYS CYS CCC . n 
C 1 516 GLY 516 516 516 GLY GLY CCC . n 
C 1 517 GLY 517 517 517 GLY GLY CCC . n 
C 1 518 GLY 518 518 518 GLY GLY CCC . n 
C 1 519 LYS 519 519 519 LYS LYS CCC . n 
C 1 520 CYS 520 520 520 CYS CYS CCC . n 
C 1 521 GLY 521 521 521 GLY GLY CCC . n 
D 1 1   MET 1   1   ?   ?   ?   DDD . n 
D 1 2   LYS 2   2   ?   ?   ?   DDD . n 
D 1 3   PHE 3   3   ?   ?   ?   DDD . n 
D 1 4   THR 4   4   ?   ?   ?   DDD . n 
D 1 5   LEU 5   5   ?   ?   ?   DDD . n 
D 1 6   VAL 6   6   ?   ?   ?   DDD . n 
D 1 7   THR 7   7   ?   ?   ?   DDD . n 
D 1 8   ILE 8   8   ?   ?   ?   DDD . n 
D 1 9   LEU 9   9   ?   ?   ?   DDD . n 
D 1 10  PHE 10  10  ?   ?   ?   DDD . n 
D 1 11  LEU 11  11  ?   ?   ?   DDD . n 
D 1 12  ILE 12  12  ?   ?   ?   DDD . n 
D 1 13  PHE 13  13  ?   ?   ?   DDD . n 
D 1 14  MET 14  14  ?   ?   ?   DDD . n 
D 1 15  LYS 15  15  ?   ?   ?   DDD . n 
D 1 16  LYS 16  16  ?   ?   ?   DDD . n 
D 1 17  ALA 17  17  ?   ?   ?   DDD . n 
D 1 18  LYS 18  18  ?   ?   ?   DDD . n 
D 1 19  ILE 19  19  ?   ?   ?   DDD . n 
D 1 20  VAL 20  20  ?   ?   ?   DDD . n 
D 1 21  MET 21  21  ?   ?   ?   DDD . n 
D 1 22  ALA 22  22  ?   ?   ?   DDD . n 
D 1 23  ASP 23  23  ?   ?   ?   DDD . n 
D 1 24  LEU 24  24  24  LEU LEU DDD . n 
D 1 25  THR 25  25  25  THR THR DDD . n 
D 1 26  PHE 26  26  26  PHE PHE DDD . n 
D 1 27  MET 27  27  27  MET MET DDD . n 
D 1 28  TYR 28  28  28  TYR TYR DDD . n 
D 1 29  ASP 29  29  29  ASP ASP DDD . n 
D 1 30  LEU 30  30  30  LEU LEU DDD . n 
D 1 31  VAL 31  31  31  VAL VAL DDD . n 
D 1 32  VAL 32  32  32  VAL VAL DDD . n 
D 1 33  ILE 33  33  33  ILE ILE DDD . n 
D 1 34  GLY 34  34  34  GLY GLY DDD . n 
D 1 35  GLY 35  35  35  GLY GLY DDD . n 
D 1 36  GLY 36  36  36  GLY GLY DDD . n 
D 1 37  SER 37  37  37  SER SER DDD . n 
D 1 38  GLY 38  38  38  GLY GLY DDD . n 
D 1 39  GLY 39  39  39  GLY GLY DDD . n 
D 1 40  MET 40  40  40  MET MET DDD . n 
D 1 41  ALA 41  41  41  ALA ALA DDD . n 
D 1 42  ALA 42  42  42  ALA ALA DDD . n 
D 1 43  ALA 43  43  43  ALA ALA DDD . n 
D 1 44  LYS 44  44  44  LYS LYS DDD . n 
D 1 45  GLU 45  45  45  GLU GLU DDD . n 
D 1 46  ALA 46  46  46  ALA ALA DDD . n 
D 1 47  ALA 47  47  47  ALA ALA DDD . n 
D 1 48  LYS 48  48  48  LYS LYS DDD . n 
D 1 49  TYR 49  49  49  TYR TYR DDD . n 
D 1 50  GLY 50  50  50  GLY GLY DDD . n 
D 1 51  LYS 51  51  51  LYS LYS DDD . n 
D 1 52  LYS 52  52  52  LYS LYS DDD . n 
D 1 53  VAL 53  53  53  VAL VAL DDD . n 
D 1 54  ALA 54  54  54  ALA ALA DDD . n 
D 1 55  LEU 55  55  55  LEU LEU DDD . n 
D 1 56  PHE 56  56  56  PHE PHE DDD . n 
D 1 57  ASP 57  57  57  ASP ASP DDD . n 
D 1 58  PHE 58  58  58  PHE PHE DDD . n 
D 1 59  VAL 59  59  59  VAL VAL DDD . n 
D 1 60  LYS 60  60  60  LYS LYS DDD . n 
D 1 61  PRO 61  61  61  PRO PRO DDD . n 
D 1 62  SER 62  62  62  SER SER DDD . n 
D 1 63  THR 63  63  63  THR THR DDD . n 
D 1 64  GLN 64  64  64  GLN GLN DDD . n 
D 1 65  GLY 65  65  65  GLY GLY DDD . n 
D 1 66  THR 66  66  66  THR THR DDD . n 
D 1 67  LYS 67  67  67  LYS LYS DDD . n 
D 1 68  TRP 68  68  68  TRP TRP DDD . n 
D 1 69  GLY 69  69  69  GLY GLY DDD . n 
D 1 70  LEU 70  70  70  LEU LEU DDD . n 
D 1 71  GLY 71  71  71  GLY GLY DDD . n 
D 1 72  GLY 72  72  72  GLY GLY DDD . n 
D 1 73  THR 73  73  73  THR THR DDD . n 
D 1 74  CYS 74  74  74  CYS CYS DDD . n 
D 1 75  VAL 75  75  75  VAL VAL DDD . n 
D 1 76  ASN 76  76  76  ASN ASN DDD . n 
D 1 77  VAL 77  77  77  VAL VAL DDD . n 
D 1 78  GLY 78  78  78  GLY GLY DDD . n 
D 1 79  CYS 79  79  79  CYS CYS DDD . n 
D 1 80  VAL 80  80  80  VAL VAL DDD . n 
D 1 81  PRO 81  81  81  PRO PRO DDD . n 
D 1 82  LYS 82  82  82  LYS LYS DDD . n 
D 1 83  LYS 83  83  83  LYS LYS DDD . n 
D 1 84  LEU 84  84  84  LEU LEU DDD . n 
D 1 85  MET 85  85  85  MET MET DDD . n 
D 1 86  HIS 86  86  86  HIS HIS DDD . n 
D 1 87  TYR 87  87  87  TYR TYR DDD . n 
D 1 88  SER 88  88  88  SER SER DDD . n 
D 1 89  ALA 89  89  89  ALA ALA DDD . n 
D 1 90  LEU 90  90  90  LEU LEU DDD . n 
D 1 91  ILE 91  91  91  ILE ILE DDD . n 
D 1 92  ALA 92  92  92  ALA ALA DDD . n 
D 1 93  SER 93  93  93  SER SER DDD . n 
D 1 94  SER 94  94  94  SER SER DDD . n 
D 1 95  ILE 95  95  95  ILE ILE DDD . n 
D 1 96  HIS 96  96  96  HIS HIS DDD . n 
D 1 97  HIS 97  97  97  HIS HIS DDD . n 
D 1 98  ASP 98  98  98  ASP ASP DDD . n 
D 1 99  ALA 99  99  99  ALA ALA DDD . n 
D 1 100 GLN 100 100 100 GLN GLN DDD . n 
D 1 101 MET 101 101 101 MET MET DDD . n 
D 1 102 PHE 102 102 102 PHE PHE DDD . n 
D 1 103 GLY 103 103 103 GLY GLY DDD . n 
D 1 104 HIS 104 104 104 HIS HIS DDD . n 
D 1 105 LYS 105 105 105 LYS LYS DDD . n 
D 1 106 THR 106 106 106 THR THR DDD . n 
D 1 107 SER 107 107 107 SER SER DDD . n 
D 1 108 SER 108 108 108 SER SER DDD . n 
D 1 109 SER 109 109 109 SER SER DDD . n 
D 1 110 PHE 110 110 110 PHE PHE DDD . n 
D 1 111 GLU 111 111 111 GLU GLU DDD . n 
D 1 112 TRP 112 112 112 TRP TRP DDD . n 
D 1 113 GLY 113 113 113 GLY GLY DDD . n 
D 1 114 LYS 114 114 114 LYS LYS DDD . n 
D 1 115 LEU 115 115 115 LEU LEU DDD . n 
D 1 116 VAL 116 116 116 VAL VAL DDD . n 
D 1 117 GLU 117 117 117 GLU GLU DDD . n 
D 1 118 THR 118 118 118 THR THR DDD . n 
D 1 119 LEU 119 119 119 LEU LEU DDD . n 
D 1 120 ARG 120 120 120 ARG ARG DDD . n 
D 1 121 ASN 121 121 121 ASN ASN DDD . n 
D 1 122 HIS 122 122 122 HIS HIS DDD . n 
D 1 123 ILE 123 123 123 ILE ILE DDD . n 
D 1 124 ARG 124 124 124 ARG ARG DDD . n 
D 1 125 MET 125 125 125 MET MET DDD . n 
D 1 126 LEU 126 126 126 LEU LEU DDD . n 
D 1 127 ASN 127 127 127 ASN ASN DDD . n 
D 1 128 PHE 128 128 128 PHE PHE DDD . n 
D 1 129 SER 129 129 129 SER SER DDD . n 
D 1 130 TYR 130 130 130 TYR TYR DDD . n 
D 1 131 ARG 131 131 131 ARG ARG DDD . n 
D 1 132 THR 132 132 132 THR THR DDD . n 
D 1 133 GLY 133 133 133 GLY GLY DDD . n 
D 1 134 LEU 134 134 134 LEU LEU DDD . n 
D 1 135 ARG 135 135 135 ARG ARG DDD . n 
D 1 136 VAL 136 136 136 VAL VAL DDD . n 
D 1 137 GLY 137 137 137 GLY GLY DDD . n 
D 1 138 ASN 138 138 138 ASN ASN DDD . n 
D 1 139 VAL 139 139 139 VAL VAL DDD . n 
D 1 140 GLU 140 140 140 GLU GLU DDD . n 
D 1 141 TYR 141 141 141 TYR TYR DDD . n 
D 1 142 ILE 142 142 142 ILE ILE DDD . n 
D 1 143 ASN 143 143 143 ASN ASN DDD . n 
D 1 144 ALA 144 144 144 ALA ALA DDD . n 
D 1 145 LEU 145 145 145 LEU LEU DDD . n 
D 1 146 ALA 146 146 146 ALA ALA DDD . n 
D 1 147 LYS 147 147 147 LYS LYS DDD . n 
D 1 148 LEU 148 148 148 LEU LEU DDD . n 
D 1 149 ILE 149 149 149 ILE ILE DDD . n 
D 1 150 ASP 150 150 150 ASP ASP DDD . n 
D 1 151 PRO 151 151 151 PRO PRO DDD . n 
D 1 152 HIS 152 152 152 HIS HIS DDD . n 
D 1 153 SER 153 153 153 SER SER DDD . n 
D 1 154 VAL 154 154 154 VAL VAL DDD . n 
D 1 155 GLU 155 155 155 GLU GLU DDD . n 
D 1 156 TYR 156 156 156 TYR TYR DDD . n 
D 1 157 GLU 157 157 157 GLU GLU DDD . n 
D 1 158 ASP 158 158 158 ASP ASP DDD . n 
D 1 159 ASN 159 159 159 ASN ASN DDD . n 
D 1 160 GLY 160 160 160 GLY GLY DDD . n 
D 1 161 GLN 161 161 161 GLN GLN DDD . n 
D 1 162 LYS 162 162 162 LYS LYS DDD . n 
D 1 163 LYS 163 163 163 LYS LYS DDD . n 
D 1 164 THR 164 164 164 THR THR DDD . n 
D 1 165 ILE 165 165 165 ILE ILE DDD . n 
D 1 166 THR 166 166 166 THR THR DDD . n 
D 1 167 SER 167 167 167 SER SER DDD . n 
D 1 168 ARG 168 168 168 ARG ARG DDD . n 
D 1 169 TYR 169 169 169 TYR TYR DDD . n 
D 1 170 ILE 170 170 170 ILE ILE DDD . n 
D 1 171 LEU 171 171 171 LEU LEU DDD . n 
D 1 172 LEU 172 172 172 LEU LEU DDD . n 
D 1 173 ALA 173 173 173 ALA ALA DDD . n 
D 1 174 THR 174 174 174 THR THR DDD . n 
D 1 175 GLY 175 175 175 GLY GLY DDD . n 
D 1 176 GLY 176 176 176 GLY GLY DDD . n 
D 1 177 ARG 177 177 177 ARG ARG DDD . n 
D 1 178 PRO 178 178 178 PRO PRO DDD . n 
D 1 179 SER 179 179 179 SER SER DDD . n 
D 1 180 ILE 180 180 180 ILE ILE DDD . n 
D 1 181 PRO 181 181 181 PRO PRO DDD . n 
D 1 182 GLU 182 182 182 GLU GLU DDD . n 
D 1 183 THR 183 183 183 THR THR DDD . n 
D 1 184 VAL 184 184 184 VAL VAL DDD . n 
D 1 185 PRO 185 185 185 PRO PRO DDD . n 
D 1 186 GLY 186 186 186 GLY GLY DDD . n 
D 1 187 ALA 187 187 187 ALA ALA DDD . n 
D 1 188 ILE 188 188 188 ILE ILE DDD . n 
D 1 189 GLN 189 189 189 GLN GLN DDD . n 
D 1 190 TYR 190 190 190 TYR TYR DDD . n 
D 1 191 SER 191 191 191 SER SER DDD . n 
D 1 192 ILE 192 192 192 ILE ILE DDD . n 
D 1 193 THR 193 193 193 THR THR DDD . n 
D 1 194 SER 194 194 194 SER SER DDD . n 
D 1 195 ASP 195 195 195 ASP ASP DDD . n 
D 1 196 ASP 196 196 196 ASP ASP DDD . n 
D 1 197 ILE 197 197 197 ILE ILE DDD . n 
D 1 198 PHE 198 198 198 PHE PHE DDD . n 
D 1 199 PHE 199 199 199 PHE PHE DDD . n 
D 1 200 LEU 200 200 200 LEU LEU DDD . n 
D 1 201 SER 201 201 201 SER SER DDD . n 
D 1 202 LYS 202 202 202 LYS LYS DDD . n 
D 1 203 SER 203 203 203 SER SER DDD . n 
D 1 204 PRO 204 204 204 PRO PRO DDD . n 
D 1 205 GLY 205 205 205 GLY GLY DDD . n 
D 1 206 LYS 206 206 206 LYS LYS DDD . n 
D 1 207 THR 207 207 207 THR THR DDD . n 
D 1 208 LEU 208 208 208 LEU LEU DDD . n 
D 1 209 VAL 209 209 209 VAL VAL DDD . n 
D 1 210 ILE 210 210 210 ILE ILE DDD . n 
D 1 211 GLY 211 211 211 GLY GLY DDD . n 
D 1 212 ALA 212 212 212 ALA ALA DDD . n 
D 1 213 SER 213 213 213 SER SER DDD . n 
D 1 214 TYR 214 214 214 TYR TYR DDD . n 
D 1 215 ILE 215 215 215 ILE ILE DDD . n 
D 1 216 GLY 216 216 216 GLY GLY DDD . n 
D 1 217 LEU 217 217 217 LEU LEU DDD . n 
D 1 218 GLU 218 218 218 GLU GLU DDD . n 
D 1 219 THR 219 219 219 THR THR DDD . n 
D 1 220 ALA 220 220 220 ALA ALA DDD . n 
D 1 221 GLY 221 221 221 GLY GLY DDD . n 
D 1 222 PHE 222 222 222 PHE PHE DDD . n 
D 1 223 LEU 223 223 223 LEU LEU DDD . n 
D 1 224 ASN 224 224 224 ASN ASN DDD . n 
D 1 225 GLU 225 225 225 GLU GLU DDD . n 
D 1 226 LEU 226 226 226 LEU LEU DDD . n 
D 1 227 GLY 227 227 227 GLY GLY DDD . n 
D 1 228 PHE 228 228 228 PHE PHE DDD . n 
D 1 229 ASP 229 229 229 ASP ASP DDD . n 
D 1 230 THR 230 230 230 THR THR DDD . n 
D 1 231 THR 231 231 231 THR THR DDD . n 
D 1 232 VAL 232 232 232 VAL VAL DDD . n 
D 1 233 ALA 233 233 233 ALA ALA DDD . n 
D 1 234 MET 234 234 234 MET MET DDD . n 
D 1 235 ARG 235 235 235 ARG ARG DDD . n 
D 1 236 SER 236 236 236 SER SER DDD . n 
D 1 237 ILE 237 237 237 ILE ILE DDD . n 
D 1 238 PRO 238 238 238 PRO PRO DDD . n 
D 1 239 LEU 239 239 239 LEU LEU DDD . n 
D 1 240 ARG 240 240 240 ARG ARG DDD . n 
D 1 241 GLY 241 241 241 GLY GLY DDD . n 
D 1 242 PHE 242 242 242 PHE PHE DDD . n 
D 1 243 ASP 243 243 243 ASP ASP DDD . n 
D 1 244 ARG 244 244 244 ARG ARG DDD . n 
D 1 245 GLN 245 245 245 GLN GLN DDD . n 
D 1 246 CYS 246 246 246 CYS CYS DDD . n 
D 1 247 SER 247 247 247 SER SER DDD . n 
D 1 248 GLU 248 248 248 GLU GLU DDD . n 
D 1 249 LYS 249 249 249 LYS LYS DDD . n 
D 1 250 ILE 250 250 250 ILE ILE DDD . n 
D 1 251 VAL 251 251 251 VAL VAL DDD . n 
D 1 252 GLU 252 252 252 GLU GLU DDD . n 
D 1 253 TYR 253 253 253 TYR TYR DDD . n 
D 1 254 MET 254 254 254 MET MET DDD . n 
D 1 255 LYS 255 255 255 LYS LYS DDD . n 
D 1 256 ALA 256 256 256 ALA ALA DDD . n 
D 1 257 THR 257 257 257 THR THR DDD . n 
D 1 258 GLY 258 258 258 GLY GLY DDD . n 
D 1 259 THR 259 259 259 THR THR DDD . n 
D 1 260 LYS 260 260 260 LYS LYS DDD . n 
D 1 261 PHE 261 261 261 PHE PHE DDD . n 
D 1 262 LEU 262 262 262 LEU LEU DDD . n 
D 1 263 VAL 263 263 263 VAL VAL DDD . n 
D 1 264 GLY 264 264 264 GLY GLY DDD . n 
D 1 265 VAL 265 265 265 VAL VAL DDD . n 
D 1 266 VAL 266 266 266 VAL VAL DDD . n 
D 1 267 PRO 267 267 267 PRO PRO DDD . n 
D 1 268 ILE 268 268 268 ILE ILE DDD . n 
D 1 269 ASN 269 269 269 ASN ASN DDD . n 
D 1 270 ILE 270 270 270 ILE ILE DDD . n 
D 1 271 GLU 271 271 271 GLU GLU DDD . n 
D 1 272 LYS 272 272 272 LYS LYS DDD . n 
D 1 273 VAL 273 273 273 VAL VAL DDD . n 
D 1 274 ASN 274 274 274 ASN ASN DDD . n 
D 1 275 GLU 275 275 275 GLU GLU DDD . n 
D 1 276 ASN 276 276 276 ASN ASN DDD . n 
D 1 277 ILE 277 277 277 ILE ILE DDD . n 
D 1 278 LYS 278 278 278 LYS LYS DDD . n 
D 1 279 VAL 279 279 279 VAL VAL DDD . n 
D 1 280 SER 280 280 280 SER SER DDD . n 
D 1 281 PHE 281 281 281 PHE PHE DDD . n 
D 1 282 SER 282 282 282 SER SER DDD . n 
D 1 283 ASP 283 283 283 ASP ASP DDD . n 
D 1 284 GLY 284 284 284 GLY GLY DDD . n 
D 1 285 SER 285 285 285 SER SER DDD . n 
D 1 286 VAL 286 286 286 VAL VAL DDD . n 
D 1 287 GLU 287 287 287 GLU GLU DDD . n 
D 1 288 GLU 288 288 288 GLU GLU DDD . n 
D 1 289 PHE 289 289 289 PHE PHE DDD . n 
D 1 290 GLU 290 290 290 GLU GLU DDD . n 
D 1 291 THR 291 291 291 THR THR DDD . n 
D 1 292 VAL 292 292 292 VAL VAL DDD . n 
D 1 293 LEU 293 293 293 LEU LEU DDD . n 
D 1 294 TYR 294 294 294 TYR TYR DDD . n 
D 1 295 ALA 295 295 295 ALA ALA DDD . n 
D 1 296 THR 296 296 296 THR THR DDD . n 
D 1 297 GLY 297 297 297 GLY GLY DDD . n 
D 1 298 ARG 298 298 298 ARG ARG DDD . n 
D 1 299 ASN 299 299 299 ASN ASN DDD . n 
D 1 300 PRO 300 300 300 PRO PRO DDD . n 
D 1 301 ASP 301 301 301 ASP ASP DDD . n 
D 1 302 VAL 302 302 302 VAL VAL DDD . n 
D 1 303 LYS 303 303 303 LYS LYS DDD . n 
D 1 304 GLY 304 304 304 GLY GLY DDD . n 
D 1 305 LEU 305 305 305 LEU LEU DDD . n 
D 1 306 ASN 306 306 306 ASN ASN DDD . n 
D 1 307 LEU 307 307 307 LEU LEU DDD . n 
D 1 308 ASN 308 308 308 ASN ASN DDD . n 
D 1 309 ALA 309 309 309 ALA ALA DDD . n 
D 1 310 ILE 310 310 310 ILE ILE DDD . n 
D 1 311 GLY 311 311 311 GLY GLY DDD . n 
D 1 312 VAL 312 312 312 VAL VAL DDD . n 
D 1 313 GLU 313 313 313 GLU GLU DDD . n 
D 1 314 VAL 314 314 314 VAL VAL DDD . n 
D 1 315 SER 315 315 315 SER SER DDD . n 
D 1 316 ASP 316 316 316 ASP ASP DDD . n 
D 1 317 SER 317 317 317 SER SER DDD . n 
D 1 318 GLY 318 318 318 GLY GLY DDD . n 
D 1 319 LYS 319 319 319 LYS LYS DDD . n 
D 1 320 ILE 320 320 320 ILE ILE DDD . n 
D 1 321 ILE 321 321 321 ILE ILE DDD . n 
D 1 322 ALA 322 322 322 ALA ALA DDD . n 
D 1 323 PRO 323 323 323 PRO PRO DDD . n 
D 1 324 LYS 324 324 324 LYS LYS DDD . n 
D 1 325 ASP 325 325 325 ASP ASP DDD . n 
D 1 326 ALA 326 326 326 ALA ALA DDD . n 
D 1 327 THR 327 327 327 THR THR DDD . n 
D 1 328 SER 328 328 328 SER SER DDD . n 
D 1 329 VAL 329 329 329 VAL VAL DDD . n 
D 1 330 PRO 330 330 330 PRO PRO DDD . n 
D 1 331 SER 331 331 331 SER SER DDD . n 
D 1 332 ILE 332 332 332 ILE ILE DDD . n 
D 1 333 PHE 333 333 333 PHE PHE DDD . n 
D 1 334 ALA 334 334 334 ALA ALA DDD . n 
D 1 335 VAL 335 335 335 VAL VAL DDD . n 
D 1 336 GLY 336 336 336 GLY GLY DDD . n 
D 1 337 ASP 337 337 337 ASP ASP DDD . n 
D 1 338 ILE 338 338 338 ILE ILE DDD . n 
D 1 339 VAL 339 339 339 VAL VAL DDD . n 
D 1 340 GLU 340 340 340 GLU GLU DDD . n 
D 1 341 GLY 341 341 341 GLY GLY DDD . n 
D 1 342 ARG 342 342 342 ARG ARG DDD . n 
D 1 343 PRO 343 343 343 PRO PRO DDD . n 
D 1 344 GLU 344 344 344 GLU GLU DDD . n 
D 1 345 LEU 345 345 345 LEU LEU DDD . n 
D 1 346 THR 346 346 346 THR THR DDD . n 
D 1 347 PRO 347 347 347 PRO PRO DDD . n 
D 1 348 VAL 348 348 348 VAL VAL DDD . n 
D 1 349 ALA 349 349 349 ALA ALA DDD . n 
D 1 350 VAL 350 350 350 VAL VAL DDD . n 
D 1 351 LYS 351 351 351 LYS LYS DDD . n 
D 1 352 ALA 352 352 352 ALA ALA DDD . n 
D 1 353 GLY 353 353 353 GLY GLY DDD . n 
D 1 354 ILE 354 354 354 ILE ILE DDD . n 
D 1 355 LEU 355 355 355 LEU LEU DDD . n 
D 1 356 LEU 356 356 356 LEU LEU DDD . n 
D 1 357 ALA 357 357 357 ALA ALA DDD . n 
D 1 358 ARG 358 358 358 ARG ARG DDD . n 
D 1 359 ARG 359 359 359 ARG ARG DDD . n 
D 1 360 LEU 360 360 360 LEU LEU DDD . n 
D 1 361 PHE 361 361 361 PHE PHE DDD . n 
D 1 362 ALA 362 362 362 ALA ALA DDD . n 
D 1 363 GLY 363 363 363 GLY GLY DDD . n 
D 1 364 SER 364 364 364 SER SER DDD . n 
D 1 365 ASN 365 365 365 ASN ASN DDD . n 
D 1 366 GLU 366 366 366 GLU GLU DDD . n 
D 1 367 PHE 367 367 367 PHE PHE DDD . n 
D 1 368 ILE 368 368 368 ILE ILE DDD . n 
D 1 369 ASP 369 369 369 ASP ASP DDD . n 
D 1 370 TYR 370 370 370 TYR TYR DDD . n 
D 1 371 ASP 371 371 371 ASP ASP DDD . n 
D 1 372 PHE 372 372 372 PHE PHE DDD . n 
D 1 373 VAL 373 373 373 VAL VAL DDD . n 
D 1 374 PRO 374 374 374 PRO PRO DDD . n 
D 1 375 THR 375 375 375 THR THR DDD . n 
D 1 376 THR 376 376 376 THR THR DDD . n 
D 1 377 VAL 377 377 377 VAL VAL DDD . n 
D 1 378 PHE 378 378 378 PHE PHE DDD . n 
D 1 379 THR 379 379 379 THR THR DDD . n 
D 1 380 PRO 380 380 380 PRO PRO DDD . n 
D 1 381 ILE 381 381 381 ILE ILE DDD . n 
D 1 382 GLU 382 382 382 GLU GLU DDD . n 
D 1 383 TYR 383 383 383 TYR TYR DDD . n 
D 1 384 GLY 384 384 384 GLY GLY DDD . n 
D 1 385 HIS 385 385 385 HIS HIS DDD . n 
D 1 386 VAL 386 386 386 VAL VAL DDD . n 
D 1 387 GLY 387 387 387 GLY GLY DDD . n 
D 1 388 LEU 388 388 388 LEU LEU DDD . n 
D 1 389 SER 389 389 389 SER SER DDD . n 
D 1 390 SER 390 390 390 SER SER DDD . n 
D 1 391 GLU 391 391 391 GLU GLU DDD . n 
D 1 392 ALA 392 392 392 ALA ALA DDD . n 
D 1 393 ALA 393 393 393 ALA ALA DDD . n 
D 1 394 ILE 394 394 394 ILE ILE DDD . n 
D 1 395 ALA 395 395 395 ALA ALA DDD . n 
D 1 396 LYS 396 396 396 LYS LYS DDD . n 
D 1 397 TYR 397 397 397 TYR TYR DDD . n 
D 1 398 GLY 398 398 398 GLY GLY DDD . n 
D 1 399 GLU 399 399 399 GLU GLU DDD . n 
D 1 400 ASP 400 400 400 ASP ASP DDD . n 
D 1 401 ASP 401 401 401 ASP ASP DDD . n 
D 1 402 ILE 402 402 402 ILE ILE DDD . n 
D 1 403 GLU 403 403 403 GLU GLU DDD . n 
D 1 404 GLU 404 404 404 GLU GLU DDD . n 
D 1 405 TYR 405 405 405 TYR TYR DDD . n 
D 1 406 LEU 406 406 406 LEU LEU DDD . n 
D 1 407 SER 407 407 407 SER SER DDD . n 
D 1 408 GLU 408 408 408 GLU GLU DDD . n 
D 1 409 PHE 409 409 409 PHE PHE DDD . n 
D 1 410 SER 410 410 410 SER SER DDD . n 
D 1 411 THR 411 411 411 THR THR DDD . n 
D 1 412 LEU 412 412 412 LEU LEU DDD . n 
D 1 413 GLU 413 413 413 GLU GLU DDD . n 
D 1 414 ILE 414 414 414 ILE ILE DDD . n 
D 1 415 ALA 415 415 415 ALA ALA DDD . n 
D 1 416 ALA 416 416 416 ALA ALA DDD . n 
D 1 417 ALA 417 417 417 ALA ALA DDD . n 
D 1 418 HIS 418 418 418 HIS HIS DDD . n 
D 1 419 ARG 419 419 419 ARG ARG DDD . n 
D 1 420 GLU 420 420 420 GLU GLU DDD . n 
D 1 421 LYS 421 421 421 LYS LYS DDD . n 
D 1 422 PRO 422 422 422 PRO PRO DDD . n 
D 1 423 GLU 423 423 423 GLU GLU DDD . n 
D 1 424 HIS 424 424 424 HIS HIS DDD . n 
D 1 425 LEU 425 425 425 LEU LEU DDD . n 
D 1 426 ARG 426 426 426 ARG ARG DDD . n 
D 1 427 GLU 427 427 427 GLU GLU DDD . n 
D 1 428 ASN 428 428 428 ASN ASN DDD . n 
D 1 429 GLU 429 429 429 GLU GLU DDD . n 
D 1 430 MET 430 430 430 MET MET DDD . n 
D 1 431 ASP 431 431 431 ASP ASP DDD . n 
D 1 432 PHE 432 432 432 PHE PHE DDD . n 
D 1 433 ALA 433 433 433 ALA ALA DDD . n 
D 1 434 LEU 434 434 434 LEU LEU DDD . n 
D 1 435 PRO 435 435 435 PRO PRO DDD . n 
D 1 436 LEU 436 436 436 LEU LEU DDD . n 
D 1 437 ASN 437 437 437 ASN ASN DDD . n 
D 1 438 CYS 438 438 438 CYS CYS DDD . n 
D 1 439 LEU 439 439 439 LEU LEU DDD . n 
D 1 440 ALA 440 440 440 ALA ALA DDD . n 
D 1 441 LYS 441 441 441 LYS LYS DDD . n 
D 1 442 LEU 442 442 442 LEU LEU DDD . n 
D 1 443 VAL 443 443 443 VAL VAL DDD . n 
D 1 444 VAL 444 444 444 VAL VAL DDD . n 
D 1 445 VAL 445 445 445 VAL VAL DDD . n 
D 1 446 LYS 446 446 446 LYS LYS DDD . n 
D 1 447 SER 447 447 447 SER SER DDD . n 
D 1 448 GLN 448 448 448 GLN GLN DDD . n 
D 1 449 GLY 449 449 449 GLY GLY DDD . n 
D 1 450 GLU 450 450 450 GLU GLU DDD . n 
D 1 451 LYS 451 451 451 LYS LYS DDD . n 
D 1 452 VAL 452 452 452 VAL VAL DDD . n 
D 1 453 VAL 453 453 453 VAL VAL DDD . n 
D 1 454 GLY 454 454 454 GLY GLY DDD . n 
D 1 455 PHE 455 455 455 PHE PHE DDD . n 
D 1 456 HIS 456 456 456 HIS HIS DDD . n 
D 1 457 PHE 457 457 457 PHE PHE DDD . n 
D 1 458 VAL 458 458 458 VAL VAL DDD . n 
D 1 459 GLY 459 459 459 GLY GLY DDD . n 
D 1 460 PRO 460 460 460 PRO PRO DDD . n 
D 1 461 ASN 461 461 461 ASN ASN DDD . n 
D 1 462 ALA 462 462 462 ALA ALA DDD . n 
D 1 463 GLY 463 463 463 GLY GLY DDD . n 
D 1 464 GLU 464 464 464 GLU GLU DDD . n 
D 1 465 ILE 465 465 465 ILE ILE DDD . n 
D 1 466 THR 466 466 466 THR THR DDD . n 
D 1 467 GLN 467 467 467 GLN GLN DDD . n 
D 1 468 GLY 468 468 468 GLY GLY DDD . n 
D 1 469 PHE 469 469 469 PHE PHE DDD . n 
D 1 470 SER 470 470 470 SER SER DDD . n 
D 1 471 LEU 471 471 471 LEU LEU DDD . n 
D 1 472 ALA 472 472 472 ALA ALA DDD . n 
D 1 473 VAL 473 473 473 VAL VAL DDD . n 
D 1 474 LYS 474 474 474 LYS LYS DDD . n 
D 1 475 LEU 475 475 475 LEU LEU DDD . n 
D 1 476 GLY 476 476 476 GLY GLY DDD . n 
D 1 477 ALA 477 477 477 ALA ALA DDD . n 
D 1 478 THR 478 478 478 THR THR DDD . n 
D 1 479 LYS 479 479 479 LYS LYS DDD . n 
D 1 480 LYS 480 480 480 LYS LYS DDD . n 
D 1 481 ASP 481 481 481 ASP ASP DDD . n 
D 1 482 PHE 482 482 482 PHE PHE DDD . n 
D 1 483 ASP 483 483 483 ASP ASP DDD . n 
D 1 484 ASP 484 484 484 ASP ASP DDD . n 
D 1 485 MET 485 485 485 MET MET DDD . n 
D 1 486 ILE 486 486 486 ILE ILE DDD . n 
D 1 487 GLY 487 487 487 GLY GLY DDD . n 
D 1 488 ILE 488 488 488 ILE ILE DDD . n 
D 1 489 HIS 489 489 489 HIS HIS DDD . n 
D 1 490 PRO 490 490 490 PRO PRO DDD . n 
D 1 491 THR 491 491 491 THR THR DDD . n 
D 1 492 ASP 492 492 492 ASP ASP DDD . n 
D 1 493 ALA 493 493 493 ALA ALA DDD . n 
D 1 494 GLU 494 494 494 GLU GLU DDD . n 
D 1 495 VAL 495 495 495 VAL VAL DDD . n 
D 1 496 PHE 496 496 496 PHE PHE DDD . n 
D 1 497 GLY 497 497 497 GLY GLY DDD . n 
D 1 498 ILE 498 498 498 ILE ILE DDD . n 
D 1 499 LEU 499 499 499 LEU LEU DDD . n 
D 1 500 GLU 500 500 500 GLU GLU DDD . n 
D 1 501 VAL 501 501 501 VAL VAL DDD . n 
D 1 502 THR 502 502 502 THR THR DDD . n 
D 1 503 LYS 503 503 503 LYS LYS DDD . n 
D 1 504 ARG 504 504 504 ARG ARG DDD . n 
D 1 505 SER 505 505 505 SER SER DDD . n 
D 1 506 GLY 506 506 506 GLY GLY DDD . n 
D 1 507 GLU 507 507 507 GLU GLU DDD . n 
D 1 508 SER 508 508 508 SER SER DDD . n 
D 1 509 PHE 509 509 509 PHE PHE DDD . n 
D 1 510 VAL 510 510 510 VAL VAL DDD . n 
D 1 511 SER 511 511 511 SER SER DDD . n 
D 1 512 SER 512 512 512 SER SER DDD . n 
D 1 513 GLY 513 513 513 GLY GLY DDD . n 
D 1 514 GLY 514 514 514 GLY GLY DDD . n 
D 1 515 CYS 515 515 515 CYS CYS DDD . n 
D 1 516 GLY 516 516 516 GLY GLY DDD . n 
D 1 517 GLY 517 517 517 GLY GLY DDD . n 
D 1 518 GLY 518 518 518 GLY GLY DDD . n 
D 1 519 LYS 519 519 519 LYS LYS DDD . n 
D 1 520 CYS 520 520 ?   ?   ?   DDD . n 
D 1 521 GLY 521 521 ?   ?   ?   DDD . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FAD 
_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 
E 2 FAD 1  601 581 FAD FAD AAA . 
F 3 PEG 1  602 585 PEG PEG AAA . 
G 2 FAD 1  601 581 FAD FAD BBB . 
H 3 PEG 1  602 585 PEG PEG BBB . 
I 3 PEG 1  603 586 PEG PEG BBB . 
J 2 FAD 1  601 581 FAD FAD CCC . 
K 3 PEG 1  602 585 PEG PEG CCC . 
L 2 FAD 1  601 581 FAD FAD DDD . 
M 3 PEG 1  602 585 PEG PEG DDD . 
N 4 HOH 1  701 130 HOH HOH AAA . 
N 4 HOH 2  702 204 HOH HOH AAA . 
N 4 HOH 3  703 249 HOH HOH AAA . 
N 4 HOH 4  704 71  HOH HOH AAA . 
N 4 HOH 5  705 282 HOH HOH AAA . 
N 4 HOH 6  706 55  HOH HOH AAA . 
N 4 HOH 7  707 200 HOH HOH AAA . 
N 4 HOH 8  708 240 HOH HOH AAA . 
N 4 HOH 9  709 303 HOH HOH AAA . 
N 4 HOH 10 710 29  HOH HOH AAA . 
N 4 HOH 11 711 255 HOH HOH AAA . 
N 4 HOH 12 712 17  HOH HOH AAA . 
N 4 HOH 13 713 91  HOH HOH AAA . 
N 4 HOH 14 714 305 HOH HOH AAA . 
N 4 HOH 15 715 310 HOH HOH AAA . 
N 4 HOH 16 716 76  HOH HOH AAA . 
N 4 HOH 17 717 99  HOH HOH AAA . 
N 4 HOH 18 718 6   HOH HOH AAA . 
N 4 HOH 19 719 46  HOH HOH AAA . 
N 4 HOH 20 720 48  HOH HOH AAA . 
N 4 HOH 21 721 281 HOH HOH AAA . 
N 4 HOH 22 722 144 HOH HOH AAA . 
N 4 HOH 23 723 186 HOH HOH AAA . 
N 4 HOH 24 724 23  HOH HOH AAA . 
N 4 HOH 25 725 75  HOH HOH AAA . 
N 4 HOH 26 726 77  HOH HOH AAA . 
N 4 HOH 27 727 64  HOH HOH AAA . 
N 4 HOH 28 728 237 HOH HOH AAA . 
N 4 HOH 29 729 1   HOH HOH AAA . 
N 4 HOH 30 730 65  HOH HOH AAA . 
N 4 HOH 31 731 82  HOH HOH AAA . 
N 4 HOH 32 732 296 HOH HOH AAA . 
N 4 HOH 33 733 174 HOH HOH AAA . 
N 4 HOH 34 734 167 HOH HOH AAA . 
N 4 HOH 35 735 4   HOH HOH AAA . 
N 4 HOH 36 736 84  HOH HOH AAA . 
N 4 HOH 37 737 121 HOH HOH AAA . 
N 4 HOH 38 738 294 HOH HOH AAA . 
N 4 HOH 39 739 253 HOH HOH AAA . 
N 4 HOH 40 740 131 HOH HOH AAA . 
N 4 HOH 41 741 228 HOH HOH AAA . 
N 4 HOH 42 742 317 HOH HOH AAA . 
N 4 HOH 43 743 31  HOH HOH AAA . 
N 4 HOH 44 744 20  HOH HOH AAA . 
N 4 HOH 45 745 14  HOH HOH AAA . 
N 4 HOH 46 746 3   HOH HOH AAA . 
N 4 HOH 47 747 298 HOH HOH AAA . 
N 4 HOH 48 748 231 HOH HOH AAA . 
N 4 HOH 49 749 122 HOH HOH AAA . 
N 4 HOH 50 750 109 HOH HOH AAA . 
N 4 HOH 51 751 295 HOH HOH AAA . 
N 4 HOH 52 752 304 HOH HOH AAA . 
N 4 HOH 53 753 176 HOH HOH AAA . 
N 4 HOH 54 754 164 HOH HOH AAA . 
N 4 HOH 55 755 254 HOH HOH AAA . 
N 4 HOH 56 756 175 HOH HOH AAA . 
N 4 HOH 57 757 92  HOH HOH AAA . 
N 4 HOH 58 758 210 HOH HOH AAA . 
N 4 HOH 59 759 140 HOH HOH AAA . 
N 4 HOH 60 760 196 HOH HOH AAA . 
N 4 HOH 61 761 205 HOH HOH AAA . 
N 4 HOH 62 762 258 HOH HOH AAA . 
N 4 HOH 63 763 100 HOH HOH AAA . 
N 4 HOH 64 764 37  HOH HOH AAA . 
N 4 HOH 65 765 50  HOH HOH AAA . 
N 4 HOH 66 766 222 HOH HOH AAA . 
N 4 HOH 67 767 13  HOH HOH AAA . 
N 4 HOH 68 768 316 HOH HOH AAA . 
N 4 HOH 69 769 169 HOH HOH AAA . 
N 4 HOH 70 770 151 HOH HOH AAA . 
N 4 HOH 71 771 149 HOH HOH AAA . 
N 4 HOH 72 772 95  HOH HOH AAA . 
N 4 HOH 73 773 257 HOH HOH AAA . 
N 4 HOH 74 774 129 HOH HOH AAA . 
N 4 HOH 75 775 213 HOH HOH AAA . 
N 4 HOH 76 776 125 HOH HOH AAA . 
N 4 HOH 77 777 190 HOH HOH AAA . 
N 4 HOH 78 778 107 HOH HOH AAA . 
N 4 HOH 79 779 74  HOH HOH AAA . 
N 4 HOH 80 780 173 HOH HOH AAA . 
N 4 HOH 81 781 216 HOH HOH AAA . 
N 4 HOH 82 782 182 HOH HOH AAA . 
N 4 HOH 83 783 232 HOH HOH AAA . 
N 4 HOH 84 784 226 HOH HOH AAA . 
N 4 HOH 85 785 133 HOH HOH AAA . 
N 4 HOH 86 786 315 HOH HOH AAA . 
N 4 HOH 87 787 313 HOH HOH AAA . 
N 4 HOH 88 788 111 HOH HOH AAA . 
N 4 HOH 89 789 314 HOH HOH AAA . 
O 4 HOH 1  701 302 HOH HOH BBB . 
O 4 HOH 2  702 321 HOH HOH BBB . 
O 4 HOH 3  703 323 HOH HOH BBB . 
O 4 HOH 4  704 276 HOH HOH BBB . 
O 4 HOH 5  705 66  HOH HOH BBB . 
O 4 HOH 6  706 203 HOH HOH BBB . 
O 4 HOH 7  707 106 HOH HOH BBB . 
O 4 HOH 8  708 87  HOH HOH BBB . 
O 4 HOH 9  709 215 HOH HOH BBB . 
O 4 HOH 10 710 171 HOH HOH BBB . 
O 4 HOH 11 711 212 HOH HOH BBB . 
O 4 HOH 12 712 85  HOH HOH BBB . 
O 4 HOH 13 713 198 HOH HOH BBB . 
O 4 HOH 14 714 248 HOH HOH BBB . 
O 4 HOH 15 715 26  HOH HOH BBB . 
O 4 HOH 16 716 93  HOH HOH BBB . 
O 4 HOH 17 717 32  HOH HOH BBB . 
O 4 HOH 18 718 96  HOH HOH BBB . 
O 4 HOH 19 719 101 HOH HOH BBB . 
O 4 HOH 20 720 260 HOH HOH BBB . 
O 4 HOH 21 721 279 HOH HOH BBB . 
O 4 HOH 22 722 277 HOH HOH BBB . 
O 4 HOH 23 723 234 HOH HOH BBB . 
O 4 HOH 24 724 15  HOH HOH BBB . 
O 4 HOH 25 725 318 HOH HOH BBB . 
O 4 HOH 26 726 250 HOH HOH BBB . 
O 4 HOH 27 727 311 HOH HOH BBB . 
O 4 HOH 28 728 44  HOH HOH BBB . 
O 4 HOH 29 729 293 HOH HOH BBB . 
O 4 HOH 30 730 45  HOH HOH BBB . 
O 4 HOH 31 731 147 HOH HOH BBB . 
O 4 HOH 32 732 104 HOH HOH BBB . 
O 4 HOH 33 733 265 HOH HOH BBB . 
O 4 HOH 34 734 42  HOH HOH BBB . 
O 4 HOH 35 735 189 HOH HOH BBB . 
O 4 HOH 36 736 211 HOH HOH BBB . 
O 4 HOH 37 737 165 HOH HOH BBB . 
O 4 HOH 38 738 252 HOH HOH BBB . 
O 4 HOH 39 739 9   HOH HOH BBB . 
O 4 HOH 40 740 297 HOH HOH BBB . 
O 4 HOH 41 741 51  HOH HOH BBB . 
O 4 HOH 42 742 236 HOH HOH BBB . 
O 4 HOH 43 743 30  HOH HOH BBB . 
O 4 HOH 44 744 224 HOH HOH BBB . 
O 4 HOH 45 745 80  HOH HOH BBB . 
O 4 HOH 46 746 283 HOH HOH BBB . 
O 4 HOH 47 747 233 HOH HOH BBB . 
O 4 HOH 48 748 105 HOH HOH BBB . 
O 4 HOH 49 749 72  HOH HOH BBB . 
O 4 HOH 50 750 57  HOH HOH BBB . 
O 4 HOH 51 751 161 HOH HOH BBB . 
O 4 HOH 52 752 179 HOH HOH BBB . 
O 4 HOH 53 753 155 HOH HOH BBB . 
O 4 HOH 54 754 112 HOH HOH BBB . 
O 4 HOH 55 755 47  HOH HOH BBB . 
O 4 HOH 56 756 120 HOH HOH BBB . 
O 4 HOH 57 757 264 HOH HOH BBB . 
O 4 HOH 58 758 245 HOH HOH BBB . 
O 4 HOH 59 759 16  HOH HOH BBB . 
O 4 HOH 60 760 278 HOH HOH BBB . 
O 4 HOH 61 761 114 HOH HOH BBB . 
O 4 HOH 62 762 221 HOH HOH BBB . 
O 4 HOH 63 763 25  HOH HOH BBB . 
O 4 HOH 64 764 33  HOH HOH BBB . 
O 4 HOH 65 765 41  HOH HOH BBB . 
O 4 HOH 66 766 218 HOH HOH BBB . 
O 4 HOH 67 767 54  HOH HOH BBB . 
O 4 HOH 68 768 10  HOH HOH BBB . 
O 4 HOH 69 769 188 HOH HOH BBB . 
O 4 HOH 70 770 59  HOH HOH BBB . 
O 4 HOH 71 771 181 HOH HOH BBB . 
O 4 HOH 72 772 12  HOH HOH BBB . 
O 4 HOH 73 773 61  HOH HOH BBB . 
O 4 HOH 74 774 219 HOH HOH BBB . 
O 4 HOH 75 775 63  HOH HOH BBB . 
O 4 HOH 76 776 145 HOH HOH BBB . 
O 4 HOH 77 777 275 HOH HOH BBB . 
O 4 HOH 78 778 280 HOH HOH BBB . 
O 4 HOH 79 779 148 HOH HOH BBB . 
O 4 HOH 80 780 22  HOH HOH BBB . 
O 4 HOH 81 781 81  HOH HOH BBB . 
O 4 HOH 82 782 98  HOH HOH BBB . 
O 4 HOH 83 783 322 HOH HOH BBB . 
O 4 HOH 84 784 266 HOH HOH BBB . 
O 4 HOH 85 785 306 HOH HOH BBB . 
O 4 HOH 86 786 268 HOH HOH BBB . 
O 4 HOH 87 787 89  HOH HOH BBB . 
O 4 HOH 88 788 308 HOH HOH BBB . 
O 4 HOH 89 789 320 HOH HOH BBB . 
O 4 HOH 90 790 243 HOH HOH BBB . 
O 4 HOH 91 791 307 HOH HOH BBB . 
O 4 HOH 92 792 274 HOH HOH BBB . 
O 4 HOH 93 793 309 HOH HOH BBB . 
O 4 HOH 94 794 319 HOH HOH BBB . 
P 4 HOH 1  701 289 HOH HOH CCC . 
P 4 HOH 2  702 73  HOH HOH CCC . 
P 4 HOH 3  703 194 HOH HOH CCC . 
P 4 HOH 4  704 67  HOH HOH CCC . 
P 4 HOH 5  705 324 HOH HOH CCC . 
P 4 HOH 6  706 242 HOH HOH CCC . 
P 4 HOH 7  707 284 HOH HOH CCC . 
P 4 HOH 8  708 126 HOH HOH CCC . 
P 4 HOH 9  709 166 HOH HOH CCC . 
P 4 HOH 10 710 136 HOH HOH CCC . 
P 4 HOH 11 711 36  HOH HOH CCC . 
P 4 HOH 12 712 191 HOH HOH CCC . 
P 4 HOH 13 713 287 HOH HOH CCC . 
P 4 HOH 14 714 24  HOH HOH CCC . 
P 4 HOH 15 715 259 HOH HOH CCC . 
P 4 HOH 16 716 90  HOH HOH CCC . 
P 4 HOH 17 717 159 HOH HOH CCC . 
P 4 HOH 18 718 162 HOH HOH CCC . 
P 4 HOH 19 719 127 HOH HOH CCC . 
P 4 HOH 20 720 2   HOH HOH CCC . 
P 4 HOH 21 721 28  HOH HOH CCC . 
P 4 HOH 22 722 220 HOH HOH CCC . 
P 4 HOH 23 723 5   HOH HOH CCC . 
P 4 HOH 24 724 113 HOH HOH CCC . 
P 4 HOH 25 725 288 HOH HOH CCC . 
P 4 HOH 26 726 79  HOH HOH CCC . 
P 4 HOH 27 727 235 HOH HOH CCC . 
P 4 HOH 28 728 177 HOH HOH CCC . 
P 4 HOH 29 729 168 HOH HOH CCC . 
P 4 HOH 30 730 35  HOH HOH CCC . 
P 4 HOH 31 731 39  HOH HOH CCC . 
P 4 HOH 32 732 187 HOH HOH CCC . 
P 4 HOH 33 733 102 HOH HOH CCC . 
P 4 HOH 34 734 141 HOH HOH CCC . 
P 4 HOH 35 735 143 HOH HOH CCC . 
P 4 HOH 36 736 183 HOH HOH CCC . 
P 4 HOH 37 737 312 HOH HOH CCC . 
P 4 HOH 38 738 271 HOH HOH CCC . 
P 4 HOH 39 739 217 HOH HOH CCC . 
P 4 HOH 40 740 273 HOH HOH CCC . 
P 4 HOH 41 741 261 HOH HOH CCC . 
P 4 HOH 42 742 60  HOH HOH CCC . 
P 4 HOH 43 743 118 HOH HOH CCC . 
P 4 HOH 44 744 7   HOH HOH CCC . 
P 4 HOH 45 745 209 HOH HOH CCC . 
P 4 HOH 46 746 103 HOH HOH CCC . 
P 4 HOH 47 747 137 HOH HOH CCC . 
P 4 HOH 48 748 132 HOH HOH CCC . 
P 4 HOH 49 749 134 HOH HOH CCC . 
P 4 HOH 50 750 206 HOH HOH CCC . 
P 4 HOH 51 751 272 HOH HOH CCC . 
P 4 HOH 52 752 124 HOH HOH CCC . 
P 4 HOH 53 753 290 HOH HOH CCC . 
P 4 HOH 54 754 69  HOH HOH CCC . 
P 4 HOH 55 755 86  HOH HOH CCC . 
P 4 HOH 56 756 21  HOH HOH CCC . 
P 4 HOH 57 757 270 HOH HOH CCC . 
P 4 HOH 58 758 300 HOH HOH CCC . 
P 4 HOH 59 759 325 HOH HOH CCC . 
P 4 HOH 60 760 208 HOH HOH CCC . 
P 4 HOH 61 761 241 HOH HOH CCC . 
P 4 HOH 62 762 299 HOH HOH CCC . 
P 4 HOH 63 763 238 HOH HOH CCC . 
P 4 HOH 64 764 291 HOH HOH CCC . 
Q 4 HOH 1  701 38  HOH HOH DDD . 
Q 4 HOH 2  702 110 HOH HOH DDD . 
Q 4 HOH 3  703 18  HOH HOH DDD . 
Q 4 HOH 4  704 58  HOH HOH DDD . 
Q 4 HOH 5  705 88  HOH HOH DDD . 
Q 4 HOH 6  706 256 HOH HOH DDD . 
Q 4 HOH 7  707 94  HOH HOH DDD . 
Q 4 HOH 8  708 292 HOH HOH DDD . 
Q 4 HOH 9  709 8   HOH HOH DDD . 
Q 4 HOH 10 710 34  HOH HOH DDD . 
Q 4 HOH 11 711 262 HOH HOH DDD . 
Q 4 HOH 12 712 139 HOH HOH DDD . 
Q 4 HOH 13 713 184 HOH HOH DDD . 
Q 4 HOH 14 714 185 HOH HOH DDD . 
Q 4 HOH 15 715 53  HOH HOH DDD . 
Q 4 HOH 16 716 62  HOH HOH DDD . 
Q 4 HOH 17 717 157 HOH HOH DDD . 
Q 4 HOH 18 718 244 HOH HOH DDD . 
Q 4 HOH 19 719 195 HOH HOH DDD . 
Q 4 HOH 20 720 56  HOH HOH DDD . 
Q 4 HOH 21 721 49  HOH HOH DDD . 
Q 4 HOH 22 722 123 HOH HOH DDD . 
Q 4 HOH 23 723 227 HOH HOH DDD . 
Q 4 HOH 24 724 119 HOH HOH DDD . 
Q 4 HOH 25 725 152 HOH HOH DDD . 
Q 4 HOH 26 726 301 HOH HOH DDD . 
Q 4 HOH 27 727 70  HOH HOH DDD . 
Q 4 HOH 28 728 108 HOH HOH DDD . 
Q 4 HOH 29 729 170 HOH HOH DDD . 
Q 4 HOH 30 730 172 HOH HOH DDD . 
Q 4 HOH 31 731 11  HOH HOH DDD . 
Q 4 HOH 32 732 285 HOH HOH DDD . 
Q 4 HOH 33 733 286 HOH HOH DDD . 
Q 4 HOH 34 734 180 HOH HOH DDD . 
Q 4 HOH 35 735 142 HOH HOH DDD . 
Q 4 HOH 36 736 192 HOH HOH DDD . 
Q 4 HOH 37 737 83  HOH HOH DDD . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.613 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H9C 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     73.872 
_cell.length_a_esd                 ? 
_cell.length_b                     72.543 
_cell.length_b_esd                 ? 
_cell.length_c                     188.458 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9H9C 
_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                   9H9C 
_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             2.34 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.42 
_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Tris/HCl, 0.1 M KSCN, PEG 2000 MME, 5 mM DTT' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294.15 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-09-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_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                        'ELETTRA BEAMLINE 11.2C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11.2C 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H9C 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.4 
_reflns.d_resolution_low                               39.91 
_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                                     78143 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.53 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.72 
_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                                ? 
_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                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.12 
_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                                    2.4 
_reflns_shell.d_res_low                                     2.486 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7744 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.79 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.78 
_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]                            0.360 
_refine.aniso_B[1][2]                            -0.000 
_refine.aniso_B[1][3]                            -0.404 
_refine.aniso_B[2][2]                            -1.098 
_refine.aniso_B[2][3]                            -0.000 
_refine.aniso_B[3][3]                            0.747 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.311 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.908 
_refine.correlation_coeff_Fo_to_Fc_free          0.877 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_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                                 9H9C 
_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                            2.400 
_refine.ls_d_res_low                             39.91 
_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                     78128 
_refine.ls_number_reflns_R_free                  3930 
_refine.ls_number_reflns_R_work                  74198 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.681 
_refine.ls_percent_reflns_R_free                 5.030 
_refine.ls_R_factor_all                          0.225 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2568 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2232 
_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                    'MASK BULK SOLVENT' 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.634 
_refine.pdbx_overall_ESU_R_Free                  0.288 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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                 ? 
_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                             21.060 
_refine.overall_SU_ML                            0.253 
_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        15073 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         247 
_refine_hist.number_atoms_solvent             284 
_refine_hist.number_atoms_total               15604 
_refine_hist.d_res_high                       2.400 
_refine_hist.d_res_low                        39.91 
# 
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  0.013  15707 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.015  14913 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.533  1.638  21289 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.274  1.577  34477 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 7.470  5.000  2005  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 32.701 22.924 684   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 15.034 15.000 2625  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 6.872  15.000 10    ? r_dihedral_angle_other_3_deg   ? ? 
'X-RAY DIFFRACTION' ? 18.173 15.000 66    ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.073  0.200  2076  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  19074 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  3382  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.199  0.200  2838  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.187  0.200  13005 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.162  0.200  7533  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.078  0.200  6908  ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.151  0.200  468   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.061  0.200  3     ? r_symmetry_xyhbond_nbd_other   ? ? 
'X-RAY DIFFRACTION' ? 0.282  0.200  52    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.331  0.200  143   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.217  0.200  8     ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 2.007  3.110  7972  ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.006  3.110  7971  ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 3.229  4.658  9966  ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.229  4.658  9967  ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 2.078  3.317  7735  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.079  3.317  7736  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 3.369  4.862  11314 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.369  4.862  11315 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 5.265  35.349 16689 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 5.264  35.349 16674 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.051  0.050  15090 ? r_ncsr_local_group_1           ? ? 
'X-RAY DIFFRACTION' ? 0.043  0.050  15274 ? r_ncsr_local_group_2           ? ? 
'X-RAY DIFFRACTION' ? 0.048  0.050  15151 ? r_ncsr_local_group_3           ? ? 
'X-RAY DIFFRACTION' ? 0.050  0.050  15087 ? r_ncsr_local_group_4           ? ? 
'X-RAY DIFFRACTION' ? 0.041  0.050  15152 ? r_ncsr_local_group_5           ? ? 
'X-RAY DIFFRACTION' ? 0.048  0.050  15218 ? r_ncsr_local_group_6           ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1  ? ? 0.05142 ? 0.05009 1  'Local ncs' ? AAA ? ? ? 1 
'X-RAY DIFFRACTION' 2  ? ? 0.05142 ? 0.05009 2  'Local ncs' ? BBB ? ? ? 1 
'X-RAY DIFFRACTION' 3  ? ? 0.04344 ? 0.05009 3  'Local ncs' ? AAA ? ? ? 2 
'X-RAY DIFFRACTION' 4  ? ? 0.04344 ? 0.05009 4  'Local ncs' ? CCC ? ? ? 2 
'X-RAY DIFFRACTION' 5  ? ? 0.04773 ? 0.05009 5  'Local ncs' ? AAA ? ? ? 3 
'X-RAY DIFFRACTION' 6  ? ? 0.04773 ? 0.05009 6  'Local ncs' ? DDD ? ? ? 3 
'X-RAY DIFFRACTION' 7  ? ? 0.04968 ? 0.05009 7  'Local ncs' ? BBB ? ? ? 4 
'X-RAY DIFFRACTION' 8  ? ? 0.04968 ? 0.05009 8  'Local ncs' ? CCC ? ? ? 4 
'X-RAY DIFFRACTION' 9  ? ? 0.04104 ? 0.05009 9  'Local ncs' ? BBB ? ? ? 5 
'X-RAY DIFFRACTION' 10 ? ? 0.04104 ? 0.05009 10 'Local ncs' ? DDD ? ? ? 5 
'X-RAY DIFFRACTION' 11 ? ? 0.04778 ? 0.05009 11 'Local ncs' ? CCC ? ? ? 6 
'X-RAY DIFFRACTION' 12 ? ? 0.04778 ? 0.05009 12 'Local ncs' ? DDD ? ? ? 6 
# 
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' 2.400  2.462  . . 266 5492 99.9826  . . . . 0.257 . . . . . . . . . . . 0.292 
'X-RAY DIFFRACTION' 2.462  2.529  . . 270 5287 100.0000 . . . . 0.246 . . . . . . . . . . . 0.311 
'X-RAY DIFFRACTION' 2.529  2.602  . . 265 5165 100.0000 . . . . 0.253 . . . . . . . . . . . 0.305 
'X-RAY DIFFRACTION' 2.602  2.682  . . 197 5047 98.6827  . . . . 0.357 . . . . . . . . . . . 0.357 
'X-RAY DIFFRACTION' 2.682  2.770  . . 249 4864 99.9218  . . . . 0.245 . . . . . . . . . . . 0.276 
'X-RAY DIFFRACTION' 2.770  2.866  . . 295 4678 100.0000 . . . . 0.228 . . . . . . . . . . . 0.282 
'X-RAY DIFFRACTION' 2.866  2.974  . . 259 4523 99.9791  . . . . 0.222 . . . . . . . . . . . 0.306 
'X-RAY DIFFRACTION' 2.974  3.095  . . 281 4326 99.9133  . . . . 0.217 . . . . . . . . . . . 0.274 
'X-RAY DIFFRACTION' 3.095  3.231  . . 243 4198 99.9325  . . . . 0.208 . . . . . . . . . . . 0.259 
'X-RAY DIFFRACTION' 3.231  3.388  . . 205 4014 99.9053  . . . . 0.204 . . . . . . . . . . . 0.253 
'X-RAY DIFFRACTION' 3.388  3.570  . . 237 3785 98.8935  . . . . 0.268 . . . . . . . . . . . 0.293 
'X-RAY DIFFRACTION' 3.570  3.785  . . 235 3552 99.1881  . . . . 0.238 . . . . . . . . . . . 0.262 
'X-RAY DIFFRACTION' 3.785  4.043  . . 166 3412 99.1136  . . . . 0.237 . . . . . . . . . . . 0.243 
'X-RAY DIFFRACTION' 4.043  4.364  . . 172 3198 99.8814  . . . . 0.174 . . . . . . . . . . . 0.204 
'X-RAY DIFFRACTION' 4.364  4.774  . . 173 2915 99.9029  . . . . 0.166 . . . . . . . . . . . 0.205 
'X-RAY DIFFRACTION' 4.774  5.328  . . 97  2724 99.7878  . . . . 0.191 . . . . . . . . . . . 0.208 
'X-RAY DIFFRACTION' 5.328  6.135  . . 134 2386 99.8415  . . . . 0.197 . . . . . . . . . . . 0.208 
'X-RAY DIFFRACTION' 6.135  7.470  . . 82  2044 99.8122  . . . . 0.193 . . . . . . . . . . . 0.248 
'X-RAY DIFFRACTION' 7.470  10.384 . . 81  1607 99.7636  . . . . 0.176 . . . . . . . . . . . 0.198 
'X-RAY DIFFRACTION' 10.384 39.90  . . 23  981  99.0138  . . . . 0.247 . . . . . . . . . . . 0.273 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1  1 AAA 
2  1 BBB 
3  2 AAA 
4  2 CCC 
5  3 AAA 
6  3 DDD 
7  4 BBB 
8  4 CCC 
9  5 BBB 
10 5 DDD 
11 6 CCC 
12 6 DDD 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
1 1  1 A LEU 24 . A GLY 517 . AAA LEU 24 AAA GLY 517 ? ? 
1 2  1 B LEU 24 . B GLY 517 . BBB LEU 24 BBB GLY 517 ? ? 
2 3  2 A LEU 24 . A GLY 521 . AAA LEU 24 AAA GLY 521 ? ? 
2 4  2 C LEU 24 . C GLY 521 . CCC LEU 24 CCC GLY 521 ? ? 
3 5  3 A LEU 24 . A GLY 518 . AAA LEU 24 AAA GLY 518 ? ? 
3 6  3 D LEU 24 . D GLY 518 . DDD LEU 24 DDD GLY 518 ? ? 
4 7  4 B LEU 24 . B GLY 517 . BBB LEU 24 BBB GLY 517 ? ? 
4 8  4 C LEU 24 . C GLY 517 . CCC LEU 24 CCC GLY 517 ? ? 
5 9  5 B LEU 24 . B GLY 517 . BBB LEU 24 BBB GLY 517 ? ? 
5 10 5 D LEU 24 . D GLY 517 . DDD LEU 24 DDD GLY 517 ? ? 
6 11 6 C LEU 24 . C GLY 518 . CCC LEU 24 CCC GLY 518 ? ? 
6 12 6 D LEU 24 . D GLY 518 . DDD LEU 24 DDD GLY 518 ? ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 'Local NCS retraints between domains:       1       2' 
2 'Local NCS retraints between domains:       3       4' 
3 'Local NCS retraints between domains:       5       6' 
4 'Local NCS retraints between domains:       7       8' 
5 'Local NCS retraints between domains:       9      10' 
6 'Local NCS retraints between domains:      11      12' 
# 
_struct.entry_id                     9H9C 
_struct.title                        
;Crystal structure of thioredoxin reductase from Cryptosporidium parvum in the "activated in" conformation
;
_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        9H9C 
_struct_keywords.text            'reductase, FLAVOPROTEIN' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
J N N 2 ? 
K N N 3 ? 
L N N 2 ? 
M N N 3 ? 
N N N 4 ? 
O N N 4 ? 
P N N 4 ? 
Q N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q8IS93_CRYPV 
_struct_ref.pdbx_db_accession          Q8IS93 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKFTLVTILFLIFMKKAKIVMADLTFMYDLVVIGGGSGGMAAAKEAAKYGKKVALFDFVKPSTQGTKWGLGGTCVNVGCV
PKKLMHYSALIASSIHHDAQMFGHKTSSSFEWGKLVETLRNHIRMLNFSYRTGLRVGNVEYINALAKLIDPHSVEYEDNG
QKKTITSRYILLATGGRPSIPETVPGAIQYSITSDDIFFLSKSPGKTLVIGASYIGLETAGFLNELGFDTTVAMRSIPLR
GFDRQCSEKIVEYMKATGTKFLVGVVPINIEKVNENIKVSFSDGSVEEFETVLYATGRNPDVKGLNLNAIGVEVSDSGKI
IAPKDATSVPSIFAVGDIVEGRPELTPVAVKAGILLARRLFAGSNEFIDYDFVPTTVFTPIEYGHVGLSSEAAIAKYGED
DIEEYLSEFSTLEIAAAHREKPEHLRENEMDFALPLNCLAKLVVVKSQGEKVVGFHFVGPNAGEITQGFSLAVKLGATKK
DFDDMIGIHPTDAEVFGILEVTKRSGESFVSSGGCGGGKCG
;
_struct_ref.pdbx_align_begin           1 
# 
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 9H9C AAA 1 ? 521 ? Q8IS93 1 ? 521 ? 1 521 
2 1 9H9C BBB 1 ? 521 ? Q8IS93 1 ? 521 ? 1 521 
3 1 9H9C CCC 1 ? 521 ? Q8IS93 1 ? 521 ? 1 521 
4 1 9H9C DDD 1 ? 521 ? Q8IS93 1 ? 521 ? 1 521 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 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)' 11310 ? 
1 MORE         -65   ? 
1 'SSA (A^2)'  37840 ? 
2 'ABSA (A^2)' 11140 ? 
2 MORE         -68   ? 
2 'SSA (A^2)'  37690 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,N,O 
2 1 C,D,J,K,L,M,P,Q   
# 
_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 GLY A 36  ? LYS A 48  ? GLY AAA 36  LYS AAA 48  1 ? 13 
HELX_P HELX_P2  AA2 GLY A 71  ? GLY A 78  ? GLY AAA 71  GLY AAA 78  1 ? 8  
HELX_P HELX_P3  AA3 GLY A 78  ? ASP A 98  ? GLY AAA 78  ASP AAA 98  1 ? 21 
HELX_P HELX_P4  AA4 GLU A 111 ? GLY A 137 ? GLU AAA 111 GLY AAA 137 1 ? 27 
HELX_P HELX_P5  AA5 GLY A 186 ? SER A 191 ? GLY AAA 186 SER AAA 191 1 ? 6  
HELX_P HELX_P6  AA6 THR A 193 ? PHE A 198 ? THR AAA 193 PHE AAA 198 1 ? 6  
HELX_P HELX_P7  AA7 SER A 213 ? LEU A 226 ? SER AAA 213 LEU AAA 226 1 ? 14 
HELX_P HELX_P8  AA8 ASP A 243 ? THR A 257 ? ASP AAA 243 THR AAA 257 1 ? 15 
HELX_P HELX_P9  AA9 VAL A 302 ? LEU A 305 ? VAL AAA 302 LEU AAA 305 5 ? 4  
HELX_P HELX_P10 AB1 ASN A 306 ? GLY A 311 ? ASN AAA 306 GLY AAA 311 1 ? 6  
HELX_P HELX_P11 AB2 GLY A 336 ? VAL A 339 ? GLY AAA 336 VAL AAA 339 5 ? 4  
HELX_P HELX_P12 AB3 LEU A 345 ? ALA A 362 ? LEU AAA 345 ALA AAA 362 1 ? 18 
HELX_P HELX_P13 AB4 SER A 389 ? GLY A 398 ? SER AAA 389 GLY AAA 398 1 ? 10 
HELX_P HELX_P14 AB5 THR A 411 ? HIS A 418 ? THR AAA 411 HIS AAA 418 1 ? 8  
HELX_P HELX_P15 AB6 PRO A 422 ? ARG A 426 ? PRO AAA 422 ARG AAA 426 5 ? 5  
HELX_P HELX_P16 AB7 SER A 447 ? GLY A 449 ? SER AAA 447 GLY AAA 449 5 ? 3  
HELX_P HELX_P17 AB8 ASN A 461 ? LEU A 475 ? ASN AAA 461 LEU AAA 475 1 ? 15 
HELX_P HELX_P18 AB9 THR A 478 ? ASP A 484 ? THR AAA 478 ASP AAA 484 1 ? 7  
HELX_P HELX_P19 AC1 ASP A 492 ? ILE A 498 ? ASP AAA 492 ILE AAA 498 5 ? 7  
HELX_P HELX_P20 AC2 GLY B 36  ? LYS B 48  ? GLY BBB 36  LYS BBB 48  1 ? 13 
HELX_P HELX_P21 AC3 GLY B 71  ? GLY B 78  ? GLY BBB 71  GLY BBB 78  1 ? 8  
HELX_P HELX_P22 AC4 GLY B 78  ? ASP B 98  ? GLY BBB 78  ASP BBB 98  1 ? 21 
HELX_P HELX_P23 AC5 GLU B 111 ? GLY B 137 ? GLU BBB 111 GLY BBB 137 1 ? 27 
HELX_P HELX_P24 AC6 GLY B 186 ? SER B 191 ? GLY BBB 186 SER BBB 191 1 ? 6  
HELX_P HELX_P25 AC7 THR B 193 ? PHE B 198 ? THR BBB 193 PHE BBB 198 1 ? 6  
HELX_P HELX_P26 AC8 SER B 213 ? LEU B 226 ? SER BBB 213 LEU BBB 226 1 ? 14 
HELX_P HELX_P27 AC9 ASP B 243 ? THR B 257 ? ASP BBB 243 THR BBB 257 1 ? 15 
HELX_P HELX_P28 AD1 VAL B 302 ? LEU B 305 ? VAL BBB 302 LEU BBB 305 5 ? 4  
HELX_P HELX_P29 AD2 ASN B 306 ? GLY B 311 ? ASN BBB 306 GLY BBB 311 1 ? 6  
HELX_P HELX_P30 AD3 GLY B 336 ? VAL B 339 ? GLY BBB 336 VAL BBB 339 5 ? 4  
HELX_P HELX_P31 AD4 LEU B 345 ? ALA B 362 ? LEU BBB 345 ALA BBB 362 1 ? 18 
HELX_P HELX_P32 AD5 SER B 389 ? GLY B 398 ? SER BBB 389 GLY BBB 398 1 ? 10 
HELX_P HELX_P33 AD6 THR B 411 ? HIS B 418 ? THR BBB 411 HIS BBB 418 1 ? 8  
HELX_P HELX_P34 AD7 PRO B 422 ? ARG B 426 ? PRO BBB 422 ARG BBB 426 5 ? 5  
HELX_P HELX_P35 AD8 SER B 447 ? GLY B 449 ? SER BBB 447 GLY BBB 449 5 ? 3  
HELX_P HELX_P36 AD9 ASN B 461 ? LEU B 475 ? ASN BBB 461 LEU BBB 475 1 ? 15 
HELX_P HELX_P37 AE1 THR B 478 ? ASP B 484 ? THR BBB 478 ASP BBB 484 1 ? 7  
HELX_P HELX_P38 AE2 ASP B 492 ? ILE B 498 ? ASP BBB 492 ILE BBB 498 5 ? 7  
HELX_P HELX_P39 AE3 GLY C 36  ? LYS C 48  ? GLY CCC 36  LYS CCC 48  1 ? 13 
HELX_P HELX_P40 AE4 GLY C 71  ? GLY C 78  ? GLY CCC 71  GLY CCC 78  1 ? 8  
HELX_P HELX_P41 AE5 GLY C 78  ? ASP C 98  ? GLY CCC 78  ASP CCC 98  1 ? 21 
HELX_P HELX_P42 AE6 GLU C 111 ? GLY C 137 ? GLU CCC 111 GLY CCC 137 1 ? 27 
HELX_P HELX_P43 AE7 GLY C 186 ? SER C 191 ? GLY CCC 186 SER CCC 191 1 ? 6  
HELX_P HELX_P44 AE8 THR C 193 ? PHE C 198 ? THR CCC 193 PHE CCC 198 1 ? 6  
HELX_P HELX_P45 AE9 SER C 213 ? LEU C 226 ? SER CCC 213 LEU CCC 226 1 ? 14 
HELX_P HELX_P46 AF1 ASP C 243 ? THR C 257 ? ASP CCC 243 THR CCC 257 1 ? 15 
HELX_P HELX_P47 AF2 VAL C 302 ? LEU C 305 ? VAL CCC 302 LEU CCC 305 5 ? 4  
HELX_P HELX_P48 AF3 ASN C 306 ? GLY C 311 ? ASN CCC 306 GLY CCC 311 1 ? 6  
HELX_P HELX_P49 AF4 LEU C 345 ? ALA C 362 ? LEU CCC 345 ALA CCC 362 1 ? 18 
HELX_P HELX_P50 AF5 SER C 389 ? GLY C 398 ? SER CCC 389 GLY CCC 398 1 ? 10 
HELX_P HELX_P51 AF6 THR C 411 ? HIS C 418 ? THR CCC 411 HIS CCC 418 1 ? 8  
HELX_P HELX_P52 AF7 PRO C 422 ? ARG C 426 ? PRO CCC 422 ARG CCC 426 5 ? 5  
HELX_P HELX_P53 AF8 SER C 447 ? GLY C 449 ? SER CCC 447 GLY CCC 449 5 ? 3  
HELX_P HELX_P54 AF9 ASN C 461 ? LEU C 475 ? ASN CCC 461 LEU CCC 475 1 ? 15 
HELX_P HELX_P55 AG1 THR C 478 ? ASP C 484 ? THR CCC 478 ASP CCC 484 1 ? 7  
HELX_P HELX_P56 AG2 ASP C 492 ? ILE C 498 ? ASP CCC 492 ILE CCC 498 5 ? 7  
HELX_P HELX_P57 AG3 GLY D 36  ? LYS D 48  ? GLY DDD 36  LYS DDD 48  1 ? 13 
HELX_P HELX_P58 AG4 GLY D 71  ? GLY D 78  ? GLY DDD 71  GLY DDD 78  1 ? 8  
HELX_P HELX_P59 AG5 GLY D 78  ? ASP D 98  ? GLY DDD 78  ASP DDD 98  1 ? 21 
HELX_P HELX_P60 AG6 GLU D 111 ? GLY D 137 ? GLU DDD 111 GLY DDD 137 1 ? 27 
HELX_P HELX_P61 AG7 GLY D 186 ? SER D 191 ? GLY DDD 186 SER DDD 191 1 ? 6  
HELX_P HELX_P62 AG8 THR D 193 ? PHE D 198 ? THR DDD 193 PHE DDD 198 1 ? 6  
HELX_P HELX_P63 AG9 SER D 213 ? LEU D 226 ? SER DDD 213 LEU DDD 226 1 ? 14 
HELX_P HELX_P64 AH1 ASP D 243 ? THR D 257 ? ASP DDD 243 THR DDD 257 1 ? 15 
HELX_P HELX_P65 AH2 VAL D 302 ? LEU D 305 ? VAL DDD 302 LEU DDD 305 5 ? 4  
HELX_P HELX_P66 AH3 ASN D 306 ? GLY D 311 ? ASN DDD 306 GLY DDD 311 1 ? 6  
HELX_P HELX_P67 AH4 GLY D 336 ? VAL D 339 ? GLY DDD 336 VAL DDD 339 5 ? 4  
HELX_P HELX_P68 AH5 LEU D 345 ? ALA D 362 ? LEU DDD 345 ALA DDD 362 1 ? 18 
HELX_P HELX_P69 AH6 SER D 389 ? GLY D 398 ? SER DDD 389 GLY DDD 398 1 ? 10 
HELX_P HELX_P70 AH7 THR D 411 ? HIS D 418 ? THR DDD 411 HIS DDD 418 1 ? 8  
HELX_P HELX_P71 AH8 PRO D 422 ? ARG D 426 ? PRO DDD 422 ARG DDD 426 5 ? 5  
HELX_P HELX_P72 AH9 SER D 447 ? GLY D 449 ? SER DDD 447 GLY DDD 449 5 ? 3  
HELX_P HELX_P73 AI1 ASN D 461 ? LEU D 475 ? ASN DDD 461 LEU DDD 475 1 ? 15 
HELX_P HELX_P74 AI2 THR D 478 ? ASP D 484 ? THR DDD 478 ASP DDD 484 1 ? 7  
HELX_P HELX_P75 AI3 ASP D 492 ? ILE D 498 ? ASP DDD 492 ILE DDD 498 5 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 74  SG ? ? ? 1_555 A CYS 79  SG ? ? AAA CYS 74  AAA CYS 79  1_555 ? ? ? ? ? ? ? 2.104 ? ? 
disulf2 disulf ? ? A CYS 520 SG B ? ? 1_555 B CYS 74  SG B ? AAA CYS 520 BBB CYS 74  1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf3 disulf ? ? B CYS 74  SG A ? ? 1_555 B CYS 79  SG ? ? BBB CYS 74  BBB CYS 79  1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf4 disulf ? ? C CYS 74  SG A ? ? 1_555 C CYS 79  SG ? ? CCC CYS 74  CCC CYS 79  1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf5 disulf ? ? C CYS 74  SG B ? ? 1_555 C CYS 79  SG ? ? CCC CYS 74  CCC CYS 79  1_555 ? ? ? ? ? ? ? 2.080 ? ? 
disulf6 disulf ? ? C CYS 515 SG ? ? ? 1_555 C CYS 520 SG A ? CCC CYS 515 CCC CYS 520 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
disulf7 disulf ? ? C CYS 520 SG B ? ? 1_555 D CYS 74  SG B ? CCC CYS 520 DDD CYS 74  1_555 ? ? ? ? ? ? ? 2.052 ? ? 
disulf8 disulf ? ? D CYS 74  SG A ? ? 1_555 D CYS 79  SG ? ? DDD CYS 74  DDD CYS 79  1_555 ? ? ? ? ? ? ? 2.057 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 74  ? CYS A 79  ? CYS AAA 74  ? 1_555 CYS AAA 79  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 520 B CYS B 74  B CYS AAA 520 ? 1_555 CYS BBB 74  ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS B 74  A CYS B 79  ? CYS BBB 74  ? 1_555 CYS BBB 79  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS C 74  A CYS C 79  ? CYS CCC 74  ? 1_555 CYS CCC 79  ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS C 74  B CYS C 79  ? CYS CCC 74  ? 1_555 CYS CCC 79  ? 1_555 SG SG . . . None 'Disulfide bridge' 
6 CYS C 515 ? CYS C 520 A CYS CCC 515 ? 1_555 CYS CCC 520 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7 CYS C 520 B CYS D 74  B CYS CCC 520 ? 1_555 CYS DDD 74  ? 1_555 SG SG . . . None 'Disulfide bridge' 
8 CYS D 74  A CYS D 79  ? CYS DDD 74  ? 1_555 CYS DDD 79  ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
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 HIS 489 A . ? HIS 489 AAA PRO 490 A ? PRO 490 AAA 1 -7.35 
2 HIS 489 B . ? HIS 489 BBB PRO 490 B ? PRO 490 BBB 1 -8.91 
3 HIS 489 C . ? HIS 489 CCC PRO 490 C ? PRO 490 CCC 1 -8.20 
4 HIS 489 D . ? HIS 489 DDD PRO 490 D ? PRO 490 DDD 1 -8.78 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 3 ? 
AA7 ? 6 ? 
AA8 ? 6 ? 
AA9 ? 5 ? 
AB1 ? 2 ? 
AB2 ? 4 ? 
AB3 ? 3 ? 
AB4 ? 6 ? 
AB5 ? 6 ? 
AB6 ? 5 ? 
AB7 ? 2 ? 
AB8 ? 2 ? 
AB9 ? 4 ? 
AC1 ? 3 ? 
AC2 ? 6 ? 
AC3 ? 6 ? 
AC4 ? 5 ? 
AC5 ? 2 ? 
AC6 ? 4 ? 
AC7 ? 3 ? 
AC8 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AA9 4 5 ? parallel      
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? anti-parallel 
AB5 5 6 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB6 4 5 ? parallel      
AB7 1 2 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? parallel      
AB9 3 4 ? parallel      
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC2 4 5 ? anti-parallel 
AC2 5 6 ? anti-parallel 
AC3 1 2 ? parallel      
AC3 2 3 ? parallel      
AC3 3 4 ? parallel      
AC3 4 5 ? anti-parallel 
AC3 5 6 ? anti-parallel 
AC4 1 2 ? parallel      
AC4 2 3 ? parallel      
AC4 3 4 ? parallel      
AC4 4 5 ? parallel      
AC5 1 2 ? anti-parallel 
AC6 1 2 ? parallel      
AC6 2 3 ? parallel      
AC6 3 4 ? parallel      
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC8 3 4 ? anti-parallel 
AC8 4 5 ? anti-parallel 
AC8 5 6 ? 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 GLU A 140 ? ILE A 142 ? GLU AAA 140 ILE AAA 142 
AA1 2 VAL A 53  ? PHE A 56  ? VAL AAA 53  PHE AAA 56  
AA1 3 TYR A 28  ? ILE A 33  ? TYR AAA 28  ILE AAA 33  
AA1 4 LYS A 163 ? LEU A 172 ? LYS AAA 163 LEU AAA 172 
AA1 5 SER A 153 ? TYR A 156 ? SER AAA 153 TYR AAA 156 
AA1 6 ALA A 146 ? ASP A 150 ? ALA AAA 146 ASP AAA 150 
AA2 1 GLU A 140 ? ILE A 142 ? GLU AAA 140 ILE AAA 142 
AA2 2 VAL A 53  ? PHE A 56  ? VAL AAA 53  PHE AAA 56  
AA2 3 TYR A 28  ? ILE A 33  ? TYR AAA 28  ILE AAA 33  
AA2 4 LYS A 163 ? LEU A 172 ? LYS AAA 163 LEU AAA 172 
AA2 5 ILE A 332 ? ALA A 334 ? ILE AAA 332 ALA AAA 334 
AA3 1 HIS A 104 ? PHE A 110 ? HIS AAA 104 PHE AAA 110 
AA3 2 HIS B 104 ? PHE B 110 ? HIS BBB 104 PHE BBB 110 
AA4 1 GLY A 176 ? PRO A 178 ? GLY AAA 176 PRO AAA 178 
AA4 2 ARG A 298 ? PRO A 300 ? ARG AAA 298 PRO AAA 300 
AA5 1 LYS A 260 ? VAL A 263 ? LYS AAA 260 VAL AAA 263 
AA5 2 THR A 230 ? MET A 234 ? THR AAA 230 MET AAA 234 
AA5 3 THR A 207 ? ILE A 210 ? THR AAA 207 ILE AAA 210 
AA5 4 THR A 291 ? TYR A 294 ? THR AAA 291 TYR AAA 294 
AA6 1 PRO A 267 ? VAL A 273 ? PRO AAA 267 VAL AAA 273 
AA6 2 ASN A 276 ? PHE A 281 ? ASN AAA 276 PHE AAA 281 
AA6 3 VAL A 286 ? PHE A 289 ? VAL AAA 286 PHE AAA 289 
AA7 1 THR A 375 ? VAL A 377 ? THR AAA 375 VAL AAA 377 
AA7 2 GLU A 382 ? GLY A 387 ? GLU AAA 382 GLY AAA 387 
AA7 3 LYS A 451 ? GLY A 459 ? LYS AAA 451 GLY AAA 459 
AA7 4 CYS A 438 ? VAL A 445 ? CYS AAA 438 VAL AAA 445 
AA7 5 ILE A 402 ? PHE A 409 ? ILE AAA 402 PHE AAA 409 
AA7 6 VAL A 501 ? THR A 502 ? VAL AAA 501 THR AAA 502 
AA8 1 VAL B 139 ? ILE B 142 ? VAL BBB 139 ILE BBB 142 
AA8 2 VAL B 53  ? PHE B 56  ? VAL BBB 53  PHE BBB 56  
AA8 3 TYR B 28  ? ILE B 33  ? TYR BBB 28  ILE BBB 33  
AA8 4 LYS B 163 ? LEU B 172 ? LYS BBB 163 LEU BBB 172 
AA8 5 SER B 153 ? TYR B 156 ? SER BBB 153 TYR BBB 156 
AA8 6 ALA B 146 ? ASP B 150 ? ALA BBB 146 ASP BBB 150 
AA9 1 VAL B 139 ? ILE B 142 ? VAL BBB 139 ILE BBB 142 
AA9 2 VAL B 53  ? PHE B 56  ? VAL BBB 53  PHE BBB 56  
AA9 3 TYR B 28  ? ILE B 33  ? TYR BBB 28  ILE BBB 33  
AA9 4 LYS B 163 ? LEU B 172 ? LYS BBB 163 LEU BBB 172 
AA9 5 ILE B 332 ? ALA B 334 ? ILE BBB 332 ALA BBB 334 
AB1 1 GLY B 176 ? PRO B 178 ? GLY BBB 176 PRO BBB 178 
AB1 2 ARG B 298 ? PRO B 300 ? ARG BBB 298 PRO BBB 300 
AB2 1 LYS B 260 ? VAL B 263 ? LYS BBB 260 VAL BBB 263 
AB2 2 THR B 230 ? MET B 234 ? THR BBB 230 MET BBB 234 
AB2 3 THR B 207 ? ILE B 210 ? THR BBB 207 ILE BBB 210 
AB2 4 THR B 291 ? TYR B 294 ? THR BBB 291 TYR BBB 294 
AB3 1 PRO B 267 ? VAL B 273 ? PRO BBB 267 VAL BBB 273 
AB3 2 ASN B 276 ? PHE B 281 ? ASN BBB 276 PHE BBB 281 
AB3 3 VAL B 286 ? PHE B 289 ? VAL BBB 286 PHE BBB 289 
AB4 1 THR B 375 ? VAL B 377 ? THR BBB 375 VAL BBB 377 
AB4 2 GLU B 382 ? GLY B 387 ? GLU BBB 382 GLY BBB 387 
AB4 3 LYS B 451 ? GLY B 459 ? LYS BBB 451 GLY BBB 459 
AB4 4 CYS B 438 ? VAL B 445 ? CYS BBB 438 VAL BBB 445 
AB4 5 ILE B 402 ? PHE B 409 ? ILE BBB 402 PHE BBB 409 
AB4 6 VAL B 501 ? THR B 502 ? VAL BBB 501 THR BBB 502 
AB5 1 GLU C 140 ? ILE C 142 ? GLU CCC 140 ILE CCC 142 
AB5 2 VAL C 53  ? PHE C 56  ? VAL CCC 53  PHE CCC 56  
AB5 3 TYR C 28  ? ILE C 33  ? TYR CCC 28  ILE CCC 33  
AB5 4 LYS C 163 ? LEU C 172 ? LYS CCC 163 LEU CCC 172 
AB5 5 SER C 153 ? TYR C 156 ? SER CCC 153 TYR CCC 156 
AB5 6 ALA C 146 ? ASP C 150 ? ALA CCC 146 ASP CCC 150 
AB6 1 GLU C 140 ? ILE C 142 ? GLU CCC 140 ILE CCC 142 
AB6 2 VAL C 53  ? PHE C 56  ? VAL CCC 53  PHE CCC 56  
AB6 3 TYR C 28  ? ILE C 33  ? TYR CCC 28  ILE CCC 33  
AB6 4 LYS C 163 ? LEU C 172 ? LYS CCC 163 LEU CCC 172 
AB6 5 ILE C 332 ? ALA C 334 ? ILE CCC 332 ALA CCC 334 
AB7 1 HIS C 104 ? PHE C 110 ? HIS CCC 104 PHE CCC 110 
AB7 2 HIS D 104 ? PHE D 110 ? HIS DDD 104 PHE DDD 110 
AB8 1 GLY C 176 ? PRO C 178 ? GLY CCC 176 PRO CCC 178 
AB8 2 ARG C 298 ? PRO C 300 ? ARG CCC 298 PRO CCC 300 
AB9 1 LYS C 260 ? VAL C 263 ? LYS CCC 260 VAL CCC 263 
AB9 2 THR C 230 ? MET C 234 ? THR CCC 230 MET CCC 234 
AB9 3 THR C 207 ? ILE C 210 ? THR CCC 207 ILE CCC 210 
AB9 4 THR C 291 ? TYR C 294 ? THR CCC 291 TYR CCC 294 
AC1 1 PRO C 267 ? VAL C 273 ? PRO CCC 267 VAL CCC 273 
AC1 2 ASN C 276 ? PHE C 281 ? ASN CCC 276 PHE CCC 281 
AC1 3 VAL C 286 ? PHE C 289 ? VAL CCC 286 PHE CCC 289 
AC2 1 THR C 375 ? VAL C 377 ? THR CCC 375 VAL CCC 377 
AC2 2 GLU C 382 ? GLY C 387 ? GLU CCC 382 GLY CCC 387 
AC2 3 LYS C 451 ? GLY C 459 ? LYS CCC 451 GLY CCC 459 
AC2 4 CYS C 438 ? VAL C 445 ? CYS CCC 438 VAL CCC 445 
AC2 5 ILE C 402 ? PHE C 409 ? ILE CCC 402 PHE CCC 409 
AC2 6 VAL C 501 ? THR C 502 ? VAL CCC 501 THR CCC 502 
AC3 1 GLU D 140 ? ILE D 142 ? GLU DDD 140 ILE DDD 142 
AC3 2 VAL D 53  ? PHE D 56  ? VAL DDD 53  PHE DDD 56  
AC3 3 TYR D 28  ? ILE D 33  ? TYR DDD 28  ILE DDD 33  
AC3 4 LYS D 163 ? LEU D 172 ? LYS DDD 163 LEU DDD 172 
AC3 5 SER D 153 ? TYR D 156 ? SER DDD 153 TYR DDD 156 
AC3 6 ALA D 146 ? ASP D 150 ? ALA DDD 146 ASP DDD 150 
AC4 1 GLU D 140 ? ILE D 142 ? GLU DDD 140 ILE DDD 142 
AC4 2 VAL D 53  ? PHE D 56  ? VAL DDD 53  PHE DDD 56  
AC4 3 TYR D 28  ? ILE D 33  ? TYR DDD 28  ILE DDD 33  
AC4 4 LYS D 163 ? LEU D 172 ? LYS DDD 163 LEU DDD 172 
AC4 5 ILE D 332 ? ALA D 334 ? ILE DDD 332 ALA DDD 334 
AC5 1 GLY D 176 ? PRO D 178 ? GLY DDD 176 PRO DDD 178 
AC5 2 ARG D 298 ? PRO D 300 ? ARG DDD 298 PRO DDD 300 
AC6 1 LYS D 260 ? VAL D 263 ? LYS DDD 260 VAL DDD 263 
AC6 2 THR D 230 ? MET D 234 ? THR DDD 230 MET DDD 234 
AC6 3 THR D 207 ? ILE D 210 ? THR DDD 207 ILE DDD 210 
AC6 4 THR D 291 ? TYR D 294 ? THR DDD 291 TYR DDD 294 
AC7 1 PRO D 267 ? VAL D 273 ? PRO DDD 267 VAL DDD 273 
AC7 2 ASN D 276 ? PHE D 281 ? ASN DDD 276 PHE DDD 281 
AC7 3 VAL D 286 ? PHE D 289 ? VAL DDD 286 PHE DDD 289 
AC8 1 THR D 375 ? VAL D 377 ? THR DDD 375 VAL DDD 377 
AC8 2 GLU D 382 ? GLY D 387 ? GLU DDD 382 GLY DDD 387 
AC8 3 LYS D 451 ? GLY D 459 ? LYS DDD 451 GLY DDD 459 
AC8 4 CYS D 438 ? VAL D 445 ? CYS DDD 438 VAL DDD 445 
AC8 5 ILE D 402 ? PHE D 409 ? ILE DDD 402 PHE DDD 409 
AC8 6 VAL D 501 ? THR D 502 ? VAL DDD 501 THR DDD 502 
# 
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 O GLU A 140 ? O GLU AAA 140 N LEU A 55  ? N LEU AAA 55  
AA1 2 3 O ALA A 54  ? O ALA AAA 54  N VAL A 32  ? N VAL AAA 32  
AA1 3 4 N ILE A 33  ? N ILE AAA 33  O LEU A 171 ? O LEU AAA 171 
AA1 4 5 O LYS A 163 ? O LYS AAA 163 N TYR A 156 ? N TYR AAA 156 
AA1 5 6 O SER A 153 ? O SER AAA 153 N ILE A 149 ? N ILE AAA 149 
AA2 1 2 O GLU A 140 ? O GLU AAA 140 N LEU A 55  ? N LEU AAA 55  
AA2 2 3 O ALA A 54  ? O ALA AAA 54  N VAL A 32  ? N VAL AAA 32  
AA2 3 4 N ILE A 33  ? N ILE AAA 33  O LEU A 171 ? O LEU AAA 171 
AA2 4 5 N ILE A 170 ? N ILE AAA 170 O PHE A 333 ? O PHE AAA 333 
AA3 1 2 N SER A 107 ? N SER AAA 107 O SER B 107 ? O SER BBB 107 
AA4 1 2 N ARG A 177 ? N ARG AAA 177 O ASN A 299 ? O ASN AAA 299 
AA5 1 2 O LYS A 260 ? O LYS AAA 260 N VAL A 232 ? N VAL AAA 232 
AA5 2 3 O THR A 231 ? O THR AAA 231 N VAL A 209 ? N VAL AAA 209 
AA5 3 4 N LEU A 208 ? N LEU AAA 208 O LEU A 293 ? O LEU AAA 293 
AA6 1 2 N ILE A 268 ? N ILE AAA 268 O SER A 280 ? O SER AAA 280 
AA6 2 3 N ILE A 277 ? N ILE AAA 277 O PHE A 289 ? O PHE AAA 289 
AA7 1 2 N VAL A 377 ? N VAL AAA 377 O TYR A 383 ? O TYR AAA 383 
AA7 2 3 N GLY A 384 ? N GLY AAA 384 O PHE A 457 ? O PHE AAA 457 
AA7 3 4 O GLY A 454 ? O GLY AAA 454 N VAL A 443 ? N VAL AAA 443 
AA7 4 5 O ALA A 440 ? O ALA AAA 440 N SER A 407 ? N SER AAA 407 
AA7 5 6 N LEU A 406 ? N LEU AAA 406 O VAL A 501 ? O VAL AAA 501 
AA8 1 2 O GLU B 140 ? O GLU BBB 140 N LEU B 55  ? N LEU BBB 55  
AA8 2 3 O ALA B 54  ? O ALA BBB 54  N VAL B 32  ? N VAL BBB 32  
AA8 3 4 N ILE B 33  ? N ILE BBB 33  O LEU B 171 ? O LEU BBB 171 
AA8 4 5 O LYS B 163 ? O LYS BBB 163 N TYR B 156 ? N TYR BBB 156 
AA8 5 6 O SER B 153 ? O SER BBB 153 N ILE B 149 ? N ILE BBB 149 
AA9 1 2 O GLU B 140 ? O GLU BBB 140 N LEU B 55  ? N LEU BBB 55  
AA9 2 3 O ALA B 54  ? O ALA BBB 54  N VAL B 32  ? N VAL BBB 32  
AA9 3 4 N ILE B 33  ? N ILE BBB 33  O LEU B 171 ? O LEU BBB 171 
AA9 4 5 N ILE B 170 ? N ILE BBB 170 O PHE B 333 ? O PHE BBB 333 
AB1 1 2 N ARG B 177 ? N ARG BBB 177 O ASN B 299 ? O ASN BBB 299 
AB2 1 2 O LYS B 260 ? O LYS BBB 260 N VAL B 232 ? N VAL BBB 232 
AB2 2 3 O THR B 231 ? O THR BBB 231 N VAL B 209 ? N VAL BBB 209 
AB2 3 4 N LEU B 208 ? N LEU BBB 208 O LEU B 293 ? O LEU BBB 293 
AB3 1 2 N ILE B 268 ? N ILE BBB 268 O SER B 280 ? O SER BBB 280 
AB3 2 3 N ILE B 277 ? N ILE BBB 277 O PHE B 289 ? O PHE BBB 289 
AB4 1 2 N VAL B 377 ? N VAL BBB 377 O TYR B 383 ? O TYR BBB 383 
AB4 2 3 N GLY B 384 ? N GLY BBB 384 O PHE B 457 ? O PHE BBB 457 
AB4 3 4 O GLY B 454 ? O GLY BBB 454 N VAL B 443 ? N VAL BBB 443 
AB4 4 5 O ALA B 440 ? O ALA BBB 440 N SER B 407 ? N SER BBB 407 
AB4 5 6 N LEU B 406 ? N LEU BBB 406 O VAL B 501 ? O VAL BBB 501 
AB5 1 2 O GLU C 140 ? O GLU CCC 140 N LEU C 55  ? N LEU CCC 55  
AB5 2 3 O ALA C 54  ? O ALA CCC 54  N VAL C 32  ? N VAL CCC 32  
AB5 3 4 N ILE C 33  ? N ILE CCC 33  O LEU C 171 ? O LEU CCC 171 
AB5 4 5 O LYS C 163 ? O LYS CCC 163 N TYR C 156 ? N TYR CCC 156 
AB5 5 6 O SER C 153 ? O SER CCC 153 N ILE C 149 ? N ILE CCC 149 
AB6 1 2 O GLU C 140 ? O GLU CCC 140 N LEU C 55  ? N LEU CCC 55  
AB6 2 3 O ALA C 54  ? O ALA CCC 54  N VAL C 32  ? N VAL CCC 32  
AB6 3 4 N ILE C 33  ? N ILE CCC 33  O LEU C 171 ? O LEU CCC 171 
AB6 4 5 N ILE C 170 ? N ILE CCC 170 O PHE C 333 ? O PHE CCC 333 
AB7 1 2 N SER C 107 ? N SER CCC 107 O SER D 107 ? O SER DDD 107 
AB8 1 2 N ARG C 177 ? N ARG CCC 177 O ASN C 299 ? O ASN CCC 299 
AB9 1 2 O LYS C 260 ? O LYS CCC 260 N VAL C 232 ? N VAL CCC 232 
AB9 2 3 O THR C 231 ? O THR CCC 231 N VAL C 209 ? N VAL CCC 209 
AB9 3 4 N LEU C 208 ? N LEU CCC 208 O LEU C 293 ? O LEU CCC 293 
AC1 1 2 N ILE C 268 ? N ILE CCC 268 O SER C 280 ? O SER CCC 280 
AC1 2 3 N ILE C 277 ? N ILE CCC 277 O PHE C 289 ? O PHE CCC 289 
AC2 1 2 N VAL C 377 ? N VAL CCC 377 O TYR C 383 ? O TYR CCC 383 
AC2 2 3 N GLY C 384 ? N GLY CCC 384 O PHE C 457 ? O PHE CCC 457 
AC2 3 4 O GLY C 454 ? O GLY CCC 454 N VAL C 443 ? N VAL CCC 443 
AC2 4 5 O ALA C 440 ? O ALA CCC 440 N SER C 407 ? N SER CCC 407 
AC2 5 6 N LEU C 406 ? N LEU CCC 406 O VAL C 501 ? O VAL CCC 501 
AC3 1 2 O GLU D 140 ? O GLU DDD 140 N LEU D 55  ? N LEU DDD 55  
AC3 2 3 O ALA D 54  ? O ALA DDD 54  N VAL D 32  ? N VAL DDD 32  
AC3 3 4 N ILE D 33  ? N ILE DDD 33  O LEU D 171 ? O LEU DDD 171 
AC3 4 5 O LYS D 163 ? O LYS DDD 163 N TYR D 156 ? N TYR DDD 156 
AC3 5 6 O SER D 153 ? O SER DDD 153 N ILE D 149 ? N ILE DDD 149 
AC4 1 2 O GLU D 140 ? O GLU DDD 140 N LEU D 55  ? N LEU DDD 55  
AC4 2 3 O ALA D 54  ? O ALA DDD 54  N VAL D 32  ? N VAL DDD 32  
AC4 3 4 N ILE D 33  ? N ILE DDD 33  O LEU D 171 ? O LEU DDD 171 
AC4 4 5 N ILE D 170 ? N ILE DDD 170 O PHE D 333 ? O PHE DDD 333 
AC5 1 2 N ARG D 177 ? N ARG DDD 177 O ASN D 299 ? O ASN DDD 299 
AC6 1 2 O LYS D 260 ? O LYS DDD 260 N VAL D 232 ? N VAL DDD 232 
AC6 2 3 O THR D 231 ? O THR DDD 231 N VAL D 209 ? N VAL DDD 209 
AC6 3 4 N LEU D 208 ? N LEU DDD 208 O LEU D 293 ? O LEU DDD 293 
AC7 1 2 N ILE D 268 ? N ILE DDD 268 O SER D 280 ? O SER DDD 280 
AC7 2 3 N ILE D 277 ? N ILE DDD 277 O PHE D 289 ? O PHE DDD 289 
AC8 1 2 N VAL D 377 ? N VAL DDD 377 O TYR D 383 ? O TYR DDD 383 
AC8 2 3 N GLY D 384 ? N GLY DDD 384 O PHE D 457 ? O PHE DDD 457 
AC8 3 4 O GLY D 454 ? O GLY DDD 454 N VAL D 443 ? N VAL DDD 443 
AC8 4 5 O ALA D 440 ? O ALA DDD 440 N SER D 407 ? N SER DDD 407 
AC8 5 6 N LEU D 406 ? N LEU DDD 406 O VAL D 501 ? O VAL DDD 501 
# 
_pdbx_entry_details.entry_id                   9H9C 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   BBB 
_pdbx_validate_close_contact.auth_comp_id_1   GLY 
_pdbx_validate_close_contact.auth_seq_id_1    133 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   BBB 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    701 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.06 
# 
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 SER AAA 62  ? ? -59.90  172.63  
2  1 VAL AAA 77  ? ? -146.29 28.33   
3  1 ALA AAA 173 ? ? -148.74 59.67   
4  1 SER AAA 236 ? ? -142.76 -79.87  
5  1 ASN AAA 274 ? ? 67.10   -119.25 
6  1 ALA AAA 322 ? ? -161.26 63.24   
7  1 ASP AAA 325 ? ? 79.05   -23.52  
8  1 PHE AAA 378 ? ? -93.87  59.82   
9  1 ASN AAA 428 ? ? -168.82 -163.48 
10 1 ILE AAA 498 ? ? -140.36 29.19   
11 1 SER BBB 62  ? ? -59.58  171.55  
12 1 VAL BBB 77  ? ? -145.77 31.80   
13 1 ALA BBB 173 ? ? -150.41 58.55   
14 1 SER BBB 236 ? ? -140.39 -82.99  
15 1 ASN BBB 274 ? ? 65.91   -116.12 
16 1 ALA BBB 322 ? ? -162.74 63.59   
17 1 ASP BBB 325 ? ? 78.78   -23.12  
18 1 ASN BBB 428 ? ? -166.18 -161.62 
19 1 GLU BBB 500 ? ? -140.53 -25.39  
20 1 VAL CCC 77  ? ? -146.08 26.93   
21 1 ALA CCC 173 ? ? -151.09 59.08   
22 1 SER CCC 236 ? ? -143.52 -81.47  
23 1 ASN CCC 274 ? ? 66.57   -116.69 
24 1 ALA CCC 322 ? ? -162.16 62.76   
25 1 ASP CCC 325 ? ? 77.66   -22.84  
26 1 ASN CCC 428 ? ? -167.18 -160.50 
27 1 VAL DDD 77  ? ? -145.26 30.65   
28 1 ALA DDD 173 ? ? -152.09 60.15   
29 1 SER DDD 236 ? ? -141.57 -82.28  
30 1 ASN DDD 274 ? ? 66.67   -118.02 
31 1 ASN DDD 306 ? ? 70.06   43.36   
32 1 ALA DDD 322 ? ? -161.71 62.71   
33 1 ASP DDD 325 ? ? 79.40   -23.29  
34 1 PHE DDD 378 ? ? -91.73  59.78   
35 1 ASN DDD 428 ? ? -166.36 -161.87 
36 1 ILE DDD 498 ? ? -140.05 29.27   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 15.0579 2.3599   31.8469 0.0776 ? 0.0127  ? 0.0143  ? 0.1456 ? -0.0117 ? 0.0222 ? 0.6909 ? -0.2498 
? -0.2954 ? 0.1607 ? 0.2061 ? 0.2680 ? 0.0673  ? -0.0582 ? -0.0122 ? -0.0603 ? -0.0449 ? -0.0156 ? -0.0788 ? -0.0641 ? -0.0224 ? 
2 'X-RAY DIFFRACTION' ? refined 38.1928 -19.1211 15.6179 0.0741 ? -0.0121 ? 0.0170  ? 0.1383 ? -0.0247 ? 0.0425 ? 0.3894 ? -0.2565 
? -0.2395 ? 0.4055 ? 0.3319 ? 0.2834 ? 0.0353  ? 0.0883  ? -0.0904 ? -0.0747 ? -0.0390 ? -0.0085 ? -0.0722 ? -0.0120 ? 0.0037  ? 
3 'X-RAY DIFFRACTION' ? refined 51.6735 0.3405   63.2229 0.0126 ? 0.0290  ? 0.0040  ? 0.2321 ? -0.0175 ? 0.0080 ? 0.8329 ? 0.2858  
? 0.4177  ? 0.1879 ? 0.1403 ? 0.2180 ? -0.0570 ? 0.0419  ? -0.0769 ? 0.0074  ? 0.0922  ? -0.0287 ? -0.0317 ? -0.0188 ? -0.0352 ? 
4 'X-RAY DIFFRACTION' ? refined 74.5803 22.7503  78.3284 0.0432 ? 0.0933  ? -0.0351 ? 0.2315 ? -0.0976 ? 0.0444 ? 0.9321 ? 0.1153  
? 0.1567  ? 0.5546 ? 0.2005 ? 0.1046 ? -0.0988 ? -0.2639 ? 0.1263  ? -0.0133 ? 0.0877  ? -0.0675 ? -0.0410 ? -0.0526 ? 0.0111  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? AAA 24 ? ? ? AAA 521 ? ALL ? 
2 'X-RAY DIFFRACTION' 2 ? ? BBB 24 ? ? ? BBB 518 ? ALL ? 
3 'X-RAY DIFFRACTION' 3 ? ? CCC 24 ? ? ? CCC 521 ? ALL ? 
4 'X-RAY DIFFRACTION' 4 ? ? DDD 24 ? ? ? DDD 519 ? 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 AAA MET 1   ? A MET 1   
2  1 Y 1 AAA LYS 2   ? A LYS 2   
3  1 Y 1 AAA PHE 3   ? A PHE 3   
4  1 Y 1 AAA THR 4   ? A THR 4   
5  1 Y 1 AAA LEU 5   ? A LEU 5   
6  1 Y 1 AAA VAL 6   ? A VAL 6   
7  1 Y 1 AAA THR 7   ? A THR 7   
8  1 Y 1 AAA ILE 8   ? A ILE 8   
9  1 Y 1 AAA LEU 9   ? A LEU 9   
10 1 Y 1 AAA PHE 10  ? A PHE 10  
11 1 Y 1 AAA LEU 11  ? A LEU 11  
12 1 Y 1 AAA ILE 12  ? A ILE 12  
13 1 Y 1 AAA PHE 13  ? A PHE 13  
14 1 Y 1 AAA MET 14  ? A MET 14  
15 1 Y 1 AAA LYS 15  ? A LYS 15  
16 1 Y 1 AAA LYS 16  ? A LYS 16  
17 1 Y 1 AAA ALA 17  ? A ALA 17  
18 1 Y 1 AAA LYS 18  ? A LYS 18  
19 1 Y 1 AAA ILE 19  ? A ILE 19  
20 1 Y 1 AAA VAL 20  ? A VAL 20  
21 1 Y 1 AAA MET 21  ? A MET 21  
22 1 Y 1 AAA ALA 22  ? A ALA 22  
23 1 Y 1 AAA ASP 23  ? A ASP 23  
24 1 Y 1 BBB MET 1   ? B MET 1   
25 1 Y 1 BBB LYS 2   ? B LYS 2   
26 1 Y 1 BBB PHE 3   ? B PHE 3   
27 1 Y 1 BBB THR 4   ? B THR 4   
28 1 Y 1 BBB LEU 5   ? B LEU 5   
29 1 Y 1 BBB VAL 6   ? B VAL 6   
30 1 Y 1 BBB THR 7   ? B THR 7   
31 1 Y 1 BBB ILE 8   ? B ILE 8   
32 1 Y 1 BBB LEU 9   ? B LEU 9   
33 1 Y 1 BBB PHE 10  ? B PHE 10  
34 1 Y 1 BBB LEU 11  ? B LEU 11  
35 1 Y 1 BBB ILE 12  ? B ILE 12  
36 1 Y 1 BBB PHE 13  ? B PHE 13  
37 1 Y 1 BBB MET 14  ? B MET 14  
38 1 Y 1 BBB LYS 15  ? B LYS 15  
39 1 Y 1 BBB LYS 16  ? B LYS 16  
40 1 Y 1 BBB ALA 17  ? B ALA 17  
41 1 Y 1 BBB LYS 18  ? B LYS 18  
42 1 Y 1 BBB ILE 19  ? B ILE 19  
43 1 Y 1 BBB VAL 20  ? B VAL 20  
44 1 Y 1 BBB MET 21  ? B MET 21  
45 1 Y 1 BBB ALA 22  ? B ALA 22  
46 1 Y 1 BBB ASP 23  ? B ASP 23  
47 1 Y 1 BBB LYS 519 ? B LYS 519 
48 1 Y 1 BBB CYS 520 ? B CYS 520 
49 1 Y 1 BBB GLY 521 ? B GLY 521 
50 1 Y 1 CCC MET 1   ? C MET 1   
51 1 Y 1 CCC LYS 2   ? C LYS 2   
52 1 Y 1 CCC PHE 3   ? C PHE 3   
53 1 Y 1 CCC THR 4   ? C THR 4   
54 1 Y 1 CCC LEU 5   ? C LEU 5   
55 1 Y 1 CCC VAL 6   ? C VAL 6   
56 1 Y 1 CCC THR 7   ? C THR 7   
57 1 Y 1 CCC ILE 8   ? C ILE 8   
58 1 Y 1 CCC LEU 9   ? C LEU 9   
59 1 Y 1 CCC PHE 10  ? C PHE 10  
60 1 Y 1 CCC LEU 11  ? C LEU 11  
61 1 Y 1 CCC ILE 12  ? C ILE 12  
62 1 Y 1 CCC PHE 13  ? C PHE 13  
63 1 Y 1 CCC MET 14  ? C MET 14  
64 1 Y 1 CCC LYS 15  ? C LYS 15  
65 1 Y 1 CCC LYS 16  ? C LYS 16  
66 1 Y 1 CCC ALA 17  ? C ALA 17  
67 1 Y 1 CCC LYS 18  ? C LYS 18  
68 1 Y 1 CCC ILE 19  ? C ILE 19  
69 1 Y 1 CCC VAL 20  ? C VAL 20  
70 1 Y 1 CCC MET 21  ? C MET 21  
71 1 Y 1 CCC ALA 22  ? C ALA 22  
72 1 Y 1 CCC ASP 23  ? C ASP 23  
73 1 Y 1 DDD MET 1   ? D MET 1   
74 1 Y 1 DDD LYS 2   ? D LYS 2   
75 1 Y 1 DDD PHE 3   ? D PHE 3   
76 1 Y 1 DDD THR 4   ? D THR 4   
77 1 Y 1 DDD LEU 5   ? D LEU 5   
78 1 Y 1 DDD VAL 6   ? D VAL 6   
79 1 Y 1 DDD THR 7   ? D THR 7   
80 1 Y 1 DDD ILE 8   ? D ILE 8   
81 1 Y 1 DDD LEU 9   ? D LEU 9   
82 1 Y 1 DDD PHE 10  ? D PHE 10  
83 1 Y 1 DDD LEU 11  ? D LEU 11  
84 1 Y 1 DDD ILE 12  ? D ILE 12  
85 1 Y 1 DDD PHE 13  ? D PHE 13  
86 1 Y 1 DDD MET 14  ? D MET 14  
87 1 Y 1 DDD LYS 15  ? D LYS 15  
88 1 Y 1 DDD LYS 16  ? D LYS 16  
89 1 Y 1 DDD ALA 17  ? D ALA 17  
90 1 Y 1 DDD LYS 18  ? D LYS 18  
91 1 Y 1 DDD ILE 19  ? D ILE 19  
92 1 Y 1 DDD VAL 20  ? D VAL 20  
93 1 Y 1 DDD MET 21  ? D MET 21  
94 1 Y 1 DDD ALA 22  ? D ALA 22  
95 1 Y 1 DDD ASP 23  ? D ASP 23  
96 1 Y 1 DDD CYS 520 ? D CYS 520 
97 1 Y 1 DDD GLY 521 ? D GLY 521 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
GLN N      N N N 174 
GLN CA     C N S 175 
GLN C      C N N 176 
GLN O      O N N 177 
GLN CB     C N N 178 
GLN CG     C N N 179 
GLN CD     C N N 180 
GLN OE1    O N N 181 
GLN NE2    N N N 182 
GLN OXT    O N N 183 
GLN H      H N N 184 
GLN H2     H N N 185 
GLN HA     H N N 186 
GLN HB2    H N N 187 
GLN HB3    H N N 188 
GLN HG2    H N N 189 
GLN HG3    H N N 190 
GLN HE21   H N N 191 
GLN HE22   H N N 192 
GLN HXT    H N N 193 
GLU N      N N N 194 
GLU CA     C N S 195 
GLU C      C N N 196 
GLU O      O N N 197 
GLU CB     C N N 198 
GLU CG     C N N 199 
GLU CD     C N N 200 
GLU OE1    O N N 201 
GLU OE2    O N N 202 
GLU OXT    O N N 203 
GLU H      H N N 204 
GLU H2     H N N 205 
GLU HA     H N N 206 
GLU HB2    H N N 207 
GLU HB3    H N N 208 
GLU HG2    H N N 209 
GLU HG3    H N N 210 
GLU HE2    H N N 211 
GLU HXT    H N N 212 
GLY N      N N N 213 
GLY CA     C N N 214 
GLY C      C N N 215 
GLY O      O N N 216 
GLY OXT    O N N 217 
GLY H      H N N 218 
GLY H2     H N N 219 
GLY HA2    H N N 220 
GLY HA3    H N N 221 
GLY HXT    H N N 222 
HIS N      N N N 223 
HIS CA     C N S 224 
HIS C      C N N 225 
HIS O      O N N 226 
HIS CB     C N N 227 
HIS CG     C Y N 228 
HIS ND1    N Y N 229 
HIS CD2    C Y N 230 
HIS CE1    C Y N 231 
HIS NE2    N Y N 232 
HIS OXT    O N N 233 
HIS H      H N N 234 
HIS H2     H N N 235 
HIS HA     H N N 236 
HIS HB2    H N N 237 
HIS HB3    H N N 238 
HIS HD1    H N N 239 
HIS HD2    H N N 240 
HIS HE1    H N N 241 
HIS HE2    H N N 242 
HIS HXT    H N N 243 
HOH O      O N N 244 
HOH H1     H N N 245 
HOH H2     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 
PEG C1     C N N 336 
PEG O1     O N N 337 
PEG C2     C N N 338 
PEG O2     O N N 339 
PEG C3     C N N 340 
PEG C4     C N N 341 
PEG O4     O N N 342 
PEG H11    H N N 343 
PEG H12    H N N 344 
PEG HO1    H N N 345 
PEG H21    H N N 346 
PEG H22    H N N 347 
PEG H31    H N N 348 
PEG H32    H N N 349 
PEG H41    H N N 350 
PEG H42    H N N 351 
PEG HO4    H N N 352 
PHE N      N N N 353 
PHE CA     C N S 354 
PHE C      C N N 355 
PHE O      O N N 356 
PHE CB     C N N 357 
PHE CG     C Y N 358 
PHE CD1    C Y N 359 
PHE CD2    C Y N 360 
PHE CE1    C Y N 361 
PHE CE2    C Y N 362 
PHE CZ     C Y N 363 
PHE OXT    O N N 364 
PHE H      H N N 365 
PHE H2     H N N 366 
PHE HA     H N N 367 
PHE HB2    H N N 368 
PHE HB3    H N N 369 
PHE HD1    H N N 370 
PHE HD2    H N N 371 
PHE HE1    H N N 372 
PHE HE2    H N N 373 
PHE HZ     H N N 374 
PHE HXT    H N N 375 
PRO N      N N N 376 
PRO CA     C N S 377 
PRO C      C N N 378 
PRO O      O N N 379 
PRO CB     C N N 380 
PRO CG     C N N 381 
PRO CD     C N N 382 
PRO OXT    O N N 383 
PRO H      H N N 384 
PRO HA     H N N 385 
PRO HB2    H N N 386 
PRO HB3    H N N 387 
PRO HG2    H N N 388 
PRO HG3    H N N 389 
PRO HD2    H N N 390 
PRO HD3    H N N 391 
PRO HXT    H N N 392 
SER N      N N N 393 
SER CA     C N S 394 
SER C      C N N 395 
SER O      O N N 396 
SER CB     C N N 397 
SER OG     O N N 398 
SER OXT    O N N 399 
SER H      H N N 400 
SER H2     H N N 401 
SER HA     H N N 402 
SER HB2    H N N 403 
SER HB3    H N N 404 
SER HG     H N N 405 
SER HXT    H N N 406 
THR N      N N N 407 
THR CA     C N S 408 
THR C      C N N 409 
THR O      O N N 410 
THR CB     C N R 411 
THR OG1    O N N 412 
THR CG2    C N N 413 
THR OXT    O N N 414 
THR H      H N N 415 
THR H2     H N N 416 
THR HA     H N N 417 
THR HB     H N N 418 
THR HG1    H N N 419 
THR HG21   H N N 420 
THR HG22   H N N 421 
THR HG23   H N N 422 
THR HXT    H N N 423 
TRP N      N N N 424 
TRP CA     C N S 425 
TRP C      C N N 426 
TRP O      O N N 427 
TRP CB     C N N 428 
TRP CG     C Y N 429 
TRP CD1    C Y N 430 
TRP CD2    C Y N 431 
TRP NE1    N Y N 432 
TRP CE2    C Y N 433 
TRP CE3    C Y N 434 
TRP CZ2    C Y N 435 
TRP CZ3    C Y N 436 
TRP CH2    C Y N 437 
TRP OXT    O N N 438 
TRP H      H N N 439 
TRP H2     H N N 440 
TRP HA     H N N 441 
TRP HB2    H N N 442 
TRP HB3    H N N 443 
TRP HD1    H N N 444 
TRP HE1    H N N 445 
TRP HE3    H N N 446 
TRP HZ2    H N N 447 
TRP HZ3    H N N 448 
TRP HH2    H N N 449 
TRP HXT    H N N 450 
TYR N      N N N 451 
TYR CA     C N S 452 
TYR C      C N N 453 
TYR O      O N N 454 
TYR CB     C N N 455 
TYR CG     C Y N 456 
TYR CD1    C Y N 457 
TYR CD2    C Y N 458 
TYR CE1    C Y N 459 
TYR CE2    C Y N 460 
TYR CZ     C Y N 461 
TYR OH     O N N 462 
TYR OXT    O N N 463 
TYR H      H N N 464 
TYR H2     H N N 465 
TYR HA     H N N 466 
TYR HB2    H N N 467 
TYR HB3    H N N 468 
TYR HD1    H N N 469 
TYR HD2    H N N 470 
TYR HE1    H N N 471 
TYR HE2    H N N 472 
TYR HH     H N N 473 
TYR HXT    H N N 474 
VAL N      N N N 475 
VAL CA     C N S 476 
VAL C      C N N 477 
VAL O      O N N 478 
VAL CB     C N N 479 
VAL CG1    C N N 480 
VAL CG2    C N N 481 
VAL OXT    O N N 482 
VAL H      H N N 483 
VAL H2     H N N 484 
VAL HA     H N N 485 
VAL HB     H N N 486 
VAL HG11   H N N 487 
VAL HG12   H N N 488 
VAL HG13   H N N 489 
VAL HG21   H N N 490 
VAL HG22   H N N 491 
VAL HG23   H N N 492 
VAL HXT    H N N 493 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     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 
PEG C1    O1     sing N N 328 
PEG C1    C2     sing N N 329 
PEG C1    H11    sing N N 330 
PEG C1    H12    sing N N 331 
PEG O1    HO1    sing N N 332 
PEG C2    O2     sing N N 333 
PEG C2    H21    sing N N 334 
PEG C2    H22    sing N N 335 
PEG O2    C3     sing N N 336 
PEG C3    C4     sing N N 337 
PEG C3    H31    sing N N 338 
PEG C3    H32    sing N N 339 
PEG C4    O4     sing N N 340 
PEG C4    H41    sing N N 341 
PEG C4    H42    sing N N 342 
PEG O4    HO4    sing N N 343 
PHE N     CA     sing N N 344 
PHE N     H      sing N N 345 
PHE N     H2     sing N N 346 
PHE CA    C      sing N N 347 
PHE CA    CB     sing N N 348 
PHE CA    HA     sing N N 349 
PHE C     O      doub N N 350 
PHE C     OXT    sing N N 351 
PHE CB    CG     sing N N 352 
PHE CB    HB2    sing N N 353 
PHE CB    HB3    sing N N 354 
PHE CG    CD1    doub Y N 355 
PHE CG    CD2    sing Y N 356 
PHE CD1   CE1    sing Y N 357 
PHE CD1   HD1    sing N N 358 
PHE CD2   CE2    doub Y N 359 
PHE CD2   HD2    sing N N 360 
PHE CE1   CZ     doub Y N 361 
PHE CE1   HE1    sing N N 362 
PHE CE2   CZ     sing Y N 363 
PHE CE2   HE2    sing N N 364 
PHE CZ    HZ     sing N N 365 
PHE OXT   HXT    sing N N 366 
PRO N     CA     sing N N 367 
PRO N     CD     sing N N 368 
PRO N     H      sing N N 369 
PRO CA    C      sing N N 370 
PRO CA    CB     sing N N 371 
PRO CA    HA     sing N N 372 
PRO C     O      doub N N 373 
PRO C     OXT    sing N N 374 
PRO CB    CG     sing N N 375 
PRO CB    HB2    sing N N 376 
PRO CB    HB3    sing N N 377 
PRO CG    CD     sing N N 378 
PRO CG    HG2    sing N N 379 
PRO CG    HG3    sing N N 380 
PRO CD    HD2    sing N N 381 
PRO CD    HD3    sing N N 382 
PRO OXT   HXT    sing N N 383 
SER N     CA     sing N N 384 
SER N     H      sing N N 385 
SER N     H2     sing N N 386 
SER CA    C      sing N N 387 
SER CA    CB     sing N N 388 
SER CA    HA     sing N N 389 
SER C     O      doub N N 390 
SER C     OXT    sing N N 391 
SER CB    OG     sing N N 392 
SER CB    HB2    sing N N 393 
SER CB    HB3    sing N N 394 
SER OG    HG     sing N N 395 
SER OXT   HXT    sing N N 396 
THR N     CA     sing N N 397 
THR N     H      sing N N 398 
THR N     H2     sing N N 399 
THR CA    C      sing N N 400 
THR CA    CB     sing N N 401 
THR CA    HA     sing N N 402 
THR C     O      doub N N 403 
THR C     OXT    sing N N 404 
THR CB    OG1    sing N N 405 
THR CB    CG2    sing N N 406 
THR CB    HB     sing N N 407 
THR OG1   HG1    sing N N 408 
THR CG2   HG21   sing N N 409 
THR CG2   HG22   sing N N 410 
THR CG2   HG23   sing N N 411 
THR OXT   HXT    sing N N 412 
TRP N     CA     sing N N 413 
TRP N     H      sing N N 414 
TRP N     H2     sing N N 415 
TRP CA    C      sing N N 416 
TRP CA    CB     sing N N 417 
TRP CA    HA     sing N N 418 
TRP C     O      doub N N 419 
TRP C     OXT    sing N N 420 
TRP CB    CG     sing N N 421 
TRP CB    HB2    sing N N 422 
TRP CB    HB3    sing N N 423 
TRP CG    CD1    doub Y N 424 
TRP CG    CD2    sing Y N 425 
TRP CD1   NE1    sing Y N 426 
TRP CD1   HD1    sing N N 427 
TRP CD2   CE2    doub Y N 428 
TRP CD2   CE3    sing Y N 429 
TRP NE1   CE2    sing Y N 430 
TRP NE1   HE1    sing N N 431 
TRP CE2   CZ2    sing Y N 432 
TRP CE3   CZ3    doub Y N 433 
TRP CE3   HE3    sing N N 434 
TRP CZ2   CH2    doub Y N 435 
TRP CZ2   HZ2    sing N N 436 
TRP CZ3   CH2    sing Y N 437 
TRP CZ3   HZ3    sing N N 438 
TRP CH2   HH2    sing N N 439 
TRP OXT   HXT    sing N N 440 
TYR N     CA     sing N N 441 
TYR N     H      sing N N 442 
TYR N     H2     sing N N 443 
TYR CA    C      sing N N 444 
TYR CA    CB     sing N N 445 
TYR CA    HA     sing N N 446 
TYR C     O      doub N N 447 
TYR C     OXT    sing N N 448 
TYR CB    CG     sing N N 449 
TYR CB    HB2    sing N N 450 
TYR CB    HB3    sing N N 451 
TYR CG    CD1    doub Y N 452 
TYR CG    CD2    sing Y N 453 
TYR CD1   CE1    sing Y N 454 
TYR CD1   HD1    sing N N 455 
TYR CD2   CE2    doub Y N 456 
TYR CD2   HD2    sing N N 457 
TYR CE1   CZ     doub Y N 458 
TYR CE1   HE1    sing N N 459 
TYR CE2   CZ     sing Y N 460 
TYR CE2   HE2    sing N N 461 
TYR CZ    OH     sing N N 462 
TYR OH    HH     sing N N 463 
TYR OXT   HXT    sing N N 464 
VAL N     CA     sing N N 465 
VAL N     H      sing N N 466 
VAL N     H2     sing N N 467 
VAL CA    C      sing N N 468 
VAL CA    CB     sing N N 469 
VAL CA    HA     sing N N 470 
VAL C     O      doub N N 471 
VAL C     OXT    sing N N 472 
VAL CB    CG1    sing N N 473 
VAL CB    CG2    sing N N 474 
VAL CB    HB     sing N N 475 
VAL CG1   HG11   sing N N 476 
VAL CG1   HG12   sing N N 477 
VAL CG1   HG13   sing N N 478 
VAL CG2   HG21   sing N N 479 
VAL CG2   HG22   sing N N 480 
VAL CG2   HG23   sing N N 481 
VAL OXT   HXT    sing N N 482 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R01AI177493 
_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   9G92 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H9C 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.013537 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000145 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013785 
_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]   0.005307 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C 6  6  2.310  20.844 1.020 10.208 1.589 0.569  0.865 51.651 0.216   
H 1  1  0.493  10.511 0.323 26.126 0.140 3.142  0.041 57.800 0.003   
N 7  7  12.222 0.006  3.135 9.893  2.014 28.997 1.167 0.583  -11.538 
O 8  8  3.049  13.277 2.287 5.701  1.546 0.324  0.867 32.909 0.251   
P 15 15 6.435  1.907  4.179 27.157 1.780 0.526  1.491 68.164 1.273   
S 16 16 6.905  1.468  5.203 22.215 1.438 0.254  1.586 56.172 1.056   
# 
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_site.calc_flag 
_atom_site.pdbx_tls_group_id 
ATOM   1     N N     . LEU A 1 24  ? -18.674 9.769   7.508   1.000 79.647  0 24  LEU AAA N     1 ? 1 
ATOM   2     C CA    . LEU A 1 24  ? -19.002 11.088  8.133   1.000 78.580  0 24  LEU AAA CA    1 ? 1 
ATOM   3     C C     . LEU A 1 24  ? -19.468 10.904  9.570   1.000 77.058  0 24  LEU AAA C     1 ? 1 
ATOM   4     O O     . LEU A 1 24  ? -19.283 11.856  10.355  1.000 77.357  0 24  LEU AAA O     1 ? 1 
ATOM   5     C CB    . LEU A 1 24  ? -20.100 11.783  7.332   1.000 80.964  0 24  LEU AAA CB    1 ? 1 
ATOM   6     C CG    . LEU A 1 24  ? -19.666 12.319  5.974   1.000 82.932  0 24  LEU AAA CG    1 ? 1 
ATOM   7     C CD1   . LEU A 1 24  ? -20.819 12.189  4.992   1.000 83.168  0 24  LEU AAA CD1   1 ? 1 
ATOM   8     C CD2   . LEU A 1 24  ? -19.155 13.753  6.102   1.000 82.176  0 24  LEU AAA CD2   1 ? 1 
ATOM   9     N N     . THR A 1 25  ? -20.076 9.756   9.891   1.000 75.676  0 25  THR AAA N     1 ? 1 
ATOM   10    C CA    . THR A 1 25  ? -20.463 9.349   11.282  1.000 73.151  0 25  THR AAA CA    1 ? 1 
ATOM   11    C C     . THR A 1 25  ? -19.377 9.835   12.285  1.000 71.233  0 25  THR AAA C     1 ? 1 
ATOM   12    O O     . THR A 1 25  ? -19.706 10.434  13.356  1.000 72.288  0 25  THR AAA O     1 ? 1 
ATOM   13    C CB    . THR A 1 25  ? -20.778 7.836   11.298  1.000 71.465  0 25  THR AAA CB    1 ? 1 
ATOM   14    O OG1   . THR A 1 25  ? -21.338 7.499   12.565  1.000 64.803  0 25  THR AAA OG1   1 ? 1 
ATOM   15    C CG2   . THR A 1 25  ? -19.587 6.931   11.029  1.000 70.549  0 25  THR AAA CG2   1 ? 1 
ATOM   16    N N     . PHE A 1 26  ? -18.099 9.632   11.919  1.000 63.369  0 26  PHE AAA N     1 ? 1 
ATOM   17    C CA    . PHE A 1 26  ? -16.880 10.084  12.638  1.000 58.258  0 26  PHE AAA CA    1 ? 1 
ATOM   18    C C     . PHE A 1 26  ? -15.923 10.693  11.625  1.000 53.636  0 26  PHE AAA C     1 ? 1 
ATOM   19    O O     . PHE A 1 26  ? -15.714 10.063  10.608  1.000 51.695  0 26  PHE AAA O     1 ? 1 
ATOM   20    C CB    . PHE A 1 26  ? -16.231 8.882   13.339  1.000 57.369  0 26  PHE AAA CB    1 ? 1 
ATOM   21    C CG    . PHE A 1 26  ? -17.127 8.206   14.345  1.000 56.786  0 26  PHE AAA CG    1 ? 1 
ATOM   22    C CD1   . PHE A 1 26  ? -17.573 8.910   15.447  1.000 55.002  0 26  PHE AAA CD1   1 ? 1 
ATOM   23    C CD2   . PHE A 1 26  ? -17.560 6.897   14.180  1.000 58.625  0 26  PHE AAA CD2   1 ? 1 
ATOM   24    C CE1   . PHE A 1 26  ? -18.400 8.307   16.383  1.000 55.435  0 26  PHE AAA CE1   1 ? 1 
ATOM   25    C CE2   . PHE A 1 26  ? -18.389 6.305   15.121  1.000 56.827  0 26  PHE AAA CE2   1 ? 1 
ATOM   26    C CZ    . PHE A 1 26  ? -18.823 7.013   16.201  1.000 54.404  0 26  PHE AAA CZ    1 ? 1 
ATOM   27    N N     . MET A 1 27  ? -15.356 11.867  11.900  1.000 53.966  0 27  MET AAA N     1 ? 1 
ATOM   28    C CA    . MET A 1 27  ? -14.298 12.487  11.048  1.000 53.498  0 27  MET AAA CA    1 ? 1 
ATOM   29    C C     . MET A 1 27  ? -13.120 11.510  10.902  1.000 51.571  0 27  MET AAA C     1 ? 1 
ATOM   30    O O     . MET A 1 27  ? -12.650 11.326  9.772   1.000 54.220  0 27  MET AAA O     1 ? 1 
ATOM   31    C CB    . MET A 1 27  ? -13.798 13.808  11.636  1.000 55.962  0 27  MET AAA CB    1 ? 1 
ATOM   32    C CG    . MET A 1 27  ? -14.831 14.921  11.626  1.000 59.261  0 27  MET AAA CG    1 ? 1 
ATOM   33    S SD    . MET A 1 27  ? -14.374 16.366  12.626  1.000 65.275  0 27  MET AAA SD    1 ? 1 
ATOM   34    C CE    . MET A 1 27  ? -13.057 17.084  11.633  1.000 63.733  0 27  MET AAA CE    1 ? 1 
ATOM   35    N N     . TYR A 1 28  ? -12.682 10.864  11.989  1.000 49.119  0 28  TYR AAA N     1 ? 1 
ATOM   36    C CA    . TYR A 1 28  ? -11.471 9.987   12.005  1.000 47.811  0 28  TYR AAA CA    1 ? 1 
ATOM   37    C C     . TYR A 1 28  ? -11.821 8.564   12.451  1.000 47.444  0 28  TYR AAA C     1 ? 1 
ATOM   38    O O     . TYR A 1 28  ? -12.849 8.362   13.137  1.000 47.508  0 28  TYR AAA O     1 ? 1 
ATOM   39    C CB    . TYR A 1 28  ? -10.394 10.564  12.921  1.000 46.593  0 28  TYR AAA CB    1 ? 1 
ATOM   40    C CG    . TYR A 1 28  ? -9.813  11.870  12.456  1.000 46.047  0 28  TYR AAA CG    1 ? 1 
ATOM   41    C CD1   . TYR A 1 28  ? -10.426 13.078  12.745  1.000 46.707  0 28  TYR AAA CD1   1 ? 1 
ATOM   42    C CD2   . TYR A 1 28  ? -8.626  11.893  11.753  1.000 45.847  0 28  TYR AAA CD2   1 ? 1 
ATOM   43    C CE1   . TYR A 1 28  ? -9.883  14.280  12.322  1.000 47.540  0 28  TYR AAA CE1   1 ? 1 
ATOM   44    C CE2   . TYR A 1 28  ? -8.080  13.080  11.301  1.000 46.651  0 28  TYR AAA CE2   1 ? 1 
ATOM   45    C CZ    . TYR A 1 28  ? -8.705  14.276  11.589  1.000 48.362  0 28  TYR AAA CZ    1 ? 1 
ATOM   46    O OH    . TYR A 1 28  ? -8.155  15.435  11.133  1.000 50.173  0 28  TYR AAA OH    1 ? 1 
ATOM   47    N N     . ASP A 1 29  ? -10.987 7.596   12.048  1.000 48.233  0 29  ASP AAA N     1 ? 1 
ATOM   48    C CA    . ASP A 1 29  ? -11.057 6.184   12.520  1.000 47.154  0 29  ASP AAA CA    1 ? 1 
ATOM   49    C C     . ASP A 1 29  ? -10.352 6.107   13.887  1.000 46.988  0 29  ASP AAA C     1 ? 1 
ATOM   50    O O     . ASP A 1 29  ? -10.855 5.394   14.800  1.000 42.840  0 29  ASP AAA O     1 ? 1 
ATOM   51    C CB    . ASP A 1 29  ? -10.471 5.231   11.485  1.000 47.663  0 29  ASP AAA CB    1 ? 1 
ATOM   52    C CG    . ASP A 1 29  ? -11.267 5.183   10.178  1.000 50.970  0 29  ASP AAA CG    1 ? 1 
ATOM   53    O OD1   . ASP A 1 29  ? -12.387 4.628   10.182  1.000 53.040  0 29  ASP AAA OD1   1 ? 1 
ATOM   54    O OD2   . ASP A 1 29  ? -10.764 5.712   9.164   1.000 50.340  0 29  ASP AAA OD2   1 ? 1 
ATOM   55    N N     . LEU A 1 30  ? -9.254  6.861   14.033  1.000 45.689  0 30  LEU AAA N     1 ? 1 
ATOM   56    C CA    . LEU A 1 30  ? -8.340  6.807   15.193  1.000 46.709  0 30  LEU AAA CA    1 ? 1 
ATOM   57    C C     . LEU A 1 30  ? -7.692  8.175   15.432  1.000 46.848  0 30  LEU AAA C     1 ? 1 
ATOM   58    O O     . LEU A 1 30  ? -7.089  8.757   14.484  1.000 46.651  0 30  LEU AAA O     1 ? 1 
ATOM   59    C CB    . LEU A 1 30  ? -7.257  5.763   14.935  1.000 47.040  0 30  LEU AAA CB    1 ? 1 
ATOM   60    C CG    . LEU A 1 30  ? -6.222  5.661   16.045  1.000 48.547  0 30  LEU AAA CG    1 ? 1 
ATOM   61    C CD1   . LEU A 1 30  ? -6.858  5.115   17.328  1.000 49.203  0 30  LEU AAA CD1   1 ? 1 
ATOM   62    C CD2   . LEU A 1 30  ? -5.037  4.815   15.589  1.000 50.385  0 30  LEU AAA CD2   1 ? 1 
ATOM   63    N N     . VAL A 1 31  ? -7.808  8.651   16.666  1.000 43.672  0 31  VAL AAA N     1 ? 1 
ATOM   64    C CA    . VAL A 1 31  ? -7.116  9.865   17.163  1.000 44.643  0 31  VAL AAA CA    1 ? 1 
ATOM   65    C C     . VAL A 1 31  ? -6.224  9.420   18.325  1.000 42.687  0 31  VAL AAA C     1 ? 1 
ATOM   66    O O     . VAL A 1 31  ? -6.733  8.729   19.229  1.000 42.599  0 31  VAL AAA O     1 ? 1 
ATOM   67    C CB    . VAL A 1 31  ? -8.099  10.966  17.592  1.000 44.116  0 31  VAL AAA CB    1 ? 1 
ATOM   68    C CG1   . VAL A 1 31  ? -7.374  12.080  18.315  1.000 45.901  0 31  VAL AAA CG1   1 ? 1 
ATOM   69    C CG2   . VAL A 1 31  ? -8.850  11.535  16.417  1.000 45.016  0 31  VAL AAA CG2   1 ? 1 
ATOM   70    N N     . VAL A 1 32  ? -4.947  9.759   18.241  1.000 40.578  0 32  VAL AAA N     1 ? 1 
ATOM   71    C CA    . VAL A 1 32  ? -3.903  9.359   19.221  1.000 39.954  0 32  VAL AAA CA    1 ? 1 
ATOM   72    C C     . VAL A 1 32  ? -3.483  10.637  19.927  1.000 39.299  0 32  VAL AAA C     1 ? 1 
ATOM   73    O O     . VAL A 1 32  ? -3.039  11.557  19.239  1.000 41.207  0 32  VAL AAA O     1 ? 1 
ATOM   74    C CB    . VAL A 1 32  ? -2.701  8.675   18.527  1.000 39.670  0 32  VAL AAA CB    1 ? 1 
ATOM   75    C CG1   . VAL A 1 32  ? -1.626  8.293   19.542  1.000 39.215  0 32  VAL AAA CG1   1 ? 1 
ATOM   76    C CG2   . VAL A 1 32  ? -3.140  7.469   17.705  1.000 38.419  0 32  VAL AAA CG2   1 ? 1 
ATOM   77    N N     . ILE A 1 33  ? -3.616  10.686  21.242  1.000 39.252  0 33  ILE AAA N     1 ? 1 
ATOM   78    C CA    . ILE A 1 33  ? -3.063  11.802  22.058  1.000 40.173  0 33  ILE AAA CA    1 ? 1 
ATOM   79    C C     . ILE A 1 33  ? -1.722  11.354  22.670  1.000 37.675  0 33  ILE AAA C     1 ? 1 
ATOM   80    O O     . ILE A 1 33  ? -1.721  10.626  23.686  1.000 35.060  0 33  ILE AAA O     1 ? 1 
ATOM   81    C CB    . ILE A 1 33  ? -4.071  12.285  23.111  1.000 41.452  0 33  ILE AAA CB    1 ? 1 
ATOM   82    C CG1   . ILE A 1 33  ? -5.431  12.585  22.472  1.000 43.525  0 33  ILE AAA CG1   1 ? 1 
ATOM   83    C CG2   . ILE A 1 33  ? -3.502  13.493  23.829  1.000 43.770  0 33  ILE AAA CG2   1 ? 1 
ATOM   84    C CD1   . ILE A 1 33  ? -6.549  12.881  23.471  1.000 42.608  0 33  ILE AAA CD1   1 ? 1 
ATOM   85    N N     . GLY A 1 34  ? -0.627  11.830  22.078  1.000 35.548  0 34  GLY AAA N     1 ? 1 
ATOM   86    C CA    . GLY A 1 34  ? 0.748   11.528  22.518  1.000 34.340  0 34  GLY AAA CA    1 ? 1 
ATOM   87    C C     . GLY A 1 34  ? 1.556   10.917  21.408  1.000 31.442  0 34  GLY AAA C     1 ? 1 
ATOM   88    O O     . GLY A 1 34  ? 1.142   9.891   20.872  1.000 29.701  0 34  GLY AAA O     1 ? 1 
ATOM   89    N N     . GLY A 1 35  ? 2.656   11.570  21.072  1.000 32.619  0 35  GLY AAA N     1 ? 1 
ATOM   90    C CA    . GLY A 1 35  ? 3.553   11.178  19.970  1.000 34.651  0 35  GLY AAA CA    1 ? 1 
ATOM   91    C C     . GLY A 1 35  ? 4.857   10.643  20.507  1.000 36.214  0 35  GLY AAA C     1 ? 1 
ATOM   92    O O     . GLY A 1 35  ? 5.904   11.075  19.997  1.000 35.780  0 35  GLY AAA O     1 ? 1 
ATOM   93    N N     . GLY A 1 36  ? 4.787   9.787   21.544  1.000 35.096  0 36  GLY AAA N     1 ? 1 
ATOM   94    C CA    . GLY A 1 36  ? 5.917   8.970   21.998  1.000 33.707  0 36  GLY AAA CA    1 ? 1 
ATOM   95    C C     . GLY A 1 36  ? 5.840   7.550   21.450  1.000 34.514  0 36  GLY AAA C     1 ? 1 
ATOM   96    O O     . GLY A 1 36  ? 5.212   7.316   20.390  1.000 30.941  0 36  GLY AAA O     1 ? 1 
ATOM   97    N N     . SER A 1 37  ? 6.441   6.598   22.169  1.000 34.920  0 37  SER AAA N     1 ? 1 
ATOM   98    C CA    . SER A 1 37  ? 6.689   5.242   21.620  1.000 35.680  0 37  SER AAA CA    1 ? 1 
ATOM   99    C C     . SER A 1 37  ? 5.349   4.571   21.305  1.000 34.626  0 37  SER AAA C     1 ? 1 
ATOM   100   O O     . SER A 1 37  ? 5.228   3.997   20.214  1.000 36.178  0 37  SER AAA O     1 ? 1 
ATOM   101   C CB    . SER A 1 37  ? 7.555   4.462   22.538  1.000 34.248  0 37  SER AAA CB    1 ? 1 
ATOM   102   O OG    . SER A 1 37  ? 8.838   5.051   22.515  1.000 34.893  0 37  SER AAA OG    1 ? 1 
ATOM   103   N N     . GLY A 1 38  ? 4.388   4.674   22.217  1.000 33.054  0 38  GLY AAA N     1 ? 1 
ATOM   104   C CA    . GLY A 1 38  ? 3.062   4.017   22.117  1.000 32.155  0 38  GLY AAA CA    1 ? 1 
ATOM   105   C C     . GLY A 1 38  ? 2.253   4.633   21.013  1.000 31.404  0 38  GLY AAA C     1 ? 1 
ATOM   106   O O     . GLY A 1 38  ? 1.812   3.887   20.152  1.000 33.051  0 38  GLY AAA O     1 ? 1 
ATOM   107   N N     . GLY A 1 39  ? 2.103   5.956   21.042  1.000 31.759  0 39  GLY AAA N     1 ? 1 
ATOM   108   C CA    . GLY A 1 39  ? 1.251   6.746   20.133  1.000 32.990  0 39  GLY AAA CA    1 ? 1 
ATOM   109   C C     . GLY A 1 39  ? 1.685   6.655   18.671  1.000 34.297  0 39  GLY AAA C     1 ? 1 
ATOM   110   O O     . GLY A 1 39  ? 0.854   6.324   17.832  1.000 33.896  0 39  GLY AAA O     1 ? 1 
ATOM   111   N N     . MET A 1 40  ? 2.953   6.912   18.369  1.000 35.084  0 40  MET AAA N     1 ? 1 
ATOM   112   C CA    . MET A 1 40  ? 3.469   6.903   16.989  1.000 36.684  0 40  MET AAA CA    1 ? 1 
ATOM   113   C C     . MET A 1 40  ? 3.376   5.487   16.438  1.000 35.886  0 40  MET AAA C     1 ? 1 
ATOM   114   O O     . MET A 1 40  ? 3.050   5.361   15.270  1.000 36.719  0 40  MET AAA O     1 ? 1 
ATOM   115   C CB    . MET A 1 40  ? 4.908   7.427   16.924  1.000 39.013  0 40  MET AAA CB    1 ? 1 
ATOM   116   C CG    . MET A 1 40  ? 4.942   8.936   17.056  1.000 41.281  0 40  MET AAA CG    1 ? 1 
ATOM   117   S SD    . MET A 1 40  ? 6.488   9.641   16.602  1.000 47.226  0 40  MET AAA SD    1 ? 1 
ATOM   118   C CE    . MET A 1 40  ? 7.641   8.636   17.538  1.000 46.343  0 40  MET AAA CE    1 ? 1 
ATOM   119   N N     . ALA A 1 41  ? 3.599   4.469   17.253  1.000 33.990  0 41  ALA AAA N     1 ? 1 
ATOM   120   C CA    . ALA A 1 41  ? 3.513   3.053   16.825  1.000 33.167  0 41  ALA AAA CA    1 ? 1 
ATOM   121   C C     . ALA A 1 41  ? 2.048   2.718   16.479  1.000 33.519  0 41  ALA AAA C     1 ? 1 
ATOM   122   O O     . ALA A 1 41  ? 1.815   2.210   15.377  1.000 32.109  0 41  ALA AAA O     1 ? 1 
ATOM   123   C CB    . ALA A 1 41  ? 4.053   2.149   17.911  1.000 31.808  0 41  ALA AAA CB    1 ? 1 
ATOM   124   N N     . ALA A 1 42  ? 1.092   3.005   17.374  1.000 33.124  0 42  ALA AAA N     1 ? 1 
ATOM   125   C CA    . ALA A 1 42  ? -0.345  2.748   17.121  1.000 34.337  0 42  ALA AAA CA    1 ? 1 
ATOM   126   C C     . ALA A 1 42  ? -0.776  3.464   15.823  1.000 36.265  0 42  ALA AAA C     1 ? 1 
ATOM   127   O O     . ALA A 1 42  ? -1.343  2.785   14.951  1.000 33.932  0 42  ALA AAA O     1 ? 1 
ATOM   128   C CB    . ALA A 1 42  ? -1.169  3.187   18.283  1.000 33.803  0 42  ALA AAA CB    1 ? 1 
ATOM   129   N N     . ALA A 1 43  ? -0.434  4.756   15.698  1.000 38.448  0 43  ALA AAA N     1 ? 1 
ATOM   130   C CA    . ALA A 1 43  ? -0.851  5.700   14.636  1.000 40.373  0 43  ALA AAA CA    1 ? 1 
ATOM   131   C C     . ALA A 1 43  ? -0.370  5.242   13.250  1.000 43.412  0 43  ALA AAA C     1 ? 1 
ATOM   132   O O     . ALA A 1 43  ? -1.236  5.147   12.338  1.000 47.131  0 43  ALA AAA O     1 ? 1 
ATOM   133   C CB    . ALA A 1 43  ? -0.329  7.082   14.962  1.000 40.898  0 43  ALA AAA CB    1 ? 1 
ATOM   134   N N     . LYS A 1 44  ? 0.937   4.977   13.089  1.000 41.970  0 44  LYS AAA N     1 ? 1 
ATOM   135   C CA    . LYS A 1 44  ? 1.549   4.477   11.823  1.000 43.037  0 44  LYS AAA CA    1 ? 1 
ATOM   136   C C     . LYS A 1 44  ? 0.952   3.115   11.446  1.000 41.940  0 44  LYS AAA C     1 ? 1 
ATOM   137   O O     . LYS A 1 44  ? 0.765   2.877   10.244  1.000 42.635  0 44  LYS AAA O     1 ? 1 
ATOM   138   C CB    . LYS A 1 44  ? 3.073   4.307   11.928  1.000 45.340  0 44  LYS AAA CB    1 ? 1 
ATOM   139   C CG    . LYS A 1 44  ? 3.880   5.585   11.799  1.000 49.143  0 44  LYS AAA CG    1 ? 1 
ATOM   140   C CD    . LYS A 1 44  ? 5.383   5.331   11.765  1.000 52.307  0 44  LYS AAA CD    1 ? 1 
ATOM   141   C CE    . LYS A 1 44  ? 6.068   5.522   13.105  1.000 53.351  0 44  LYS AAA CE    1 ? 1 
ATOM   142   N NZ    . LYS A 1 44  ? 7.521   5.791   12.925  1.000 53.370  0 44  LYS AAA NZ    1 ? 1 
ATOM   143   N N     . GLU A 1 45  ? 0.708   2.228   12.416  1.000 40.865  0 45  GLU AAA N     1 ? 1 
ATOM   144   C CA    . GLU A 1 45  ? 0.158   0.878   12.138  1.000 40.777  0 45  GLU AAA CA    1 ? 1 
ATOM   145   C C     . GLU A 1 45  ? -1.304  1.001   11.702  1.000 42.971  0 45  GLU AAA C     1 ? 1 
ATOM   146   O O     . GLU A 1 45  ? -1.690  0.277   10.766  1.000 45.147  0 45  GLU AAA O     1 ? 1 
ATOM   147   C CB    . GLU A 1 45  ? 0.267   -0.045  13.345  1.000 39.671  0 45  GLU AAA CB    1 ? 1 
ATOM   148   C CG    . GLU A 1 45  ? -0.024  -1.492  12.992  1.000 41.041  0 45  GLU AAA CG    1 ? 1 
ATOM   149   C CD    . GLU A 1 45  ? 1.109   -2.211  12.266  1.000 40.634  0 45  GLU AAA CD    1 ? 1 
ATOM   150   O OE1   . GLU A 1 45  ? 2.113   -1.518  11.938  1.000 41.596  0 45  GLU AAA OE1   1 ? 1 
ATOM   151   O OE2   . GLU A 1 45  ? 1.020   -3.456  12.112  1.000 38.561  0 45  GLU AAA OE2   1 ? 1 
ATOM   152   N N     . ALA A 1 46  ? -2.090  1.877   12.334  1.000 42.144  0 46  ALA AAA N     1 ? 1 
ATOM   153   C CA    . ALA A 1 46  ? -3.497  2.105   11.959  1.000 46.385  0 46  ALA AAA CA    1 ? 1 
ATOM   154   C C     . ALA A 1 46  ? -3.525  2.626   10.521  1.000 50.765  0 46  ALA AAA C     1 ? 1 
ATOM   155   O O     . ALA A 1 46  ? -4.259  2.050   9.706   1.000 54.688  0 46  ALA AAA O     1 ? 1 
ATOM   156   C CB    . ALA A 1 46  ? -4.148  3.073   12.904  1.000 47.127  0 46  ALA AAA CB    1 ? 1 
ATOM   157   N N     . ALA A 1 47  ? -2.718  3.647   10.230  1.000 52.470  0 47  ALA AAA N     1 ? 1 
ATOM   158   C CA    . ALA A 1 47  ? -2.623  4.329   8.920   1.000 54.438  0 47  ALA AAA CA    1 ? 1 
ATOM   159   C C     . ALA A 1 47  ? -2.230  3.347   7.812   1.000 54.805  0 47  ALA AAA C     1 ? 1 
ATOM   160   O O     . ALA A 1 47  ? -2.702  3.552   6.670   1.000 54.850  0 47  ALA AAA O     1 ? 1 
ATOM   161   C CB    . ALA A 1 47  ? -1.644  5.463   9.009   1.000 56.928  0 47  ALA AAA CB    1 ? 1 
ATOM   162   N N     . LYS A 1 48  ? -1.433  2.322   8.144   1.000 56.173  0 48  LYS AAA N     1 ? 1 
ATOM   163   C CA    . LYS A 1 48  ? -1.040  1.202   7.237   1.000 58.842  0 48  LYS AAA CA    1 ? 1 
ATOM   164   C C     . LYS A 1 48  ? -2.273  0.541   6.602   1.000 57.960  0 48  LYS AAA C     1 ? 1 
ATOM   165   O O     . LYS A 1 48  ? -2.130  0.036   5.474   1.000 57.705  0 48  LYS AAA O     1 ? 1 
ATOM   166   C CB    . LYS A 1 48  ? -0.266  0.108   7.987   1.000 61.597  0 48  LYS AAA CB    1 ? 1 
ATOM   167   C CG    . LYS A 1 48  ? 1.230   0.021   7.729   1.000 66.141  0 48  LYS AAA CG    1 ? 1 
ATOM   168   C CD    . LYS A 1 48  ? 1.813   -1.344  8.109   1.000 70.451  0 48  LYS AAA CD    1 ? 1 
ATOM   169   C CE    . LYS A 1 48  ? 1.396   -2.434  7.130   1.000 74.325  0 48  LYS AAA CE    1 ? 1 
ATOM   170   N NZ    . LYS A 1 48  ? 2.469   -3.434  6.869   1.000 74.871  0 48  LYS AAA NZ    1 ? 1 
ATOM   171   N N     . TYR A 1 49  ? -3.419  0.503   7.303   1.000 55.127  0 49  TYR AAA N     1 ? 1 
ATOM   172   C CA    . TYR A 1 49  ? -4.636  -0.244  6.885   1.000 56.269  0 49  TYR AAA CA    1 ? 1 
ATOM   173   C C     . TYR A 1 49  ? -5.636  0.701   6.189   1.000 56.215  0 49  TYR AAA C     1 ? 1 
ATOM   174   O O     . TYR A 1 49  ? -6.848  0.347   6.100   1.000 55.466  0 49  TYR AAA O     1 ? 1 
ATOM   175   C CB    . TYR A 1 49  ? -5.216  -1.007  8.081   1.000 54.211  0 49  TYR AAA CB    1 ? 1 
ATOM   176   C CG    . TYR A 1 49  ? -4.272  -2.051  8.616   1.000 53.644  0 49  TYR AAA CG    1 ? 1 
ATOM   177   C CD1   . TYR A 1 49  ? -3.834  -3.088  7.815   1.000 54.562  0 49  TYR AAA CD1   1 ? 1 
ATOM   178   C CD2   . TYR A 1 49  ? -3.755  -1.973  9.899   1.000 54.543  0 49  TYR AAA CD2   1 ? 1 
ATOM   179   C CE1   . TYR A 1 49  ? -2.946  -4.041  8.289   1.000 55.044  0 49  TYR AAA CE1   1 ? 1 
ATOM   180   C CE2   . TYR A 1 49  ? -2.859  -2.917  10.385  1.000 53.358  0 49  TYR AAA CE2   1 ? 1 
ATOM   181   C CZ    . TYR A 1 49  ? -2.446  -3.955  9.573   1.000 54.091  0 49  TYR AAA CZ    1 ? 1 
ATOM   182   O OH    . TYR A 1 49  ? -1.571  -4.908  10.015  1.000 53.883  0 49  TYR AAA OH    1 ? 1 
ATOM   183   N N     . GLY A 1 50  ? -5.149  1.850   5.695   1.000 55.028  0 50  GLY AAA N     1 ? 1 
ATOM   184   C CA    . GLY A 1 50  ? -5.955  2.854   4.966   1.000 56.073  0 50  GLY AAA CA    1 ? 1 
ATOM   185   C C     . GLY A 1 50  ? -6.850  3.681   5.885   1.000 53.329  0 50  GLY AAA C     1 ? 1 
ATOM   186   O O     . GLY A 1 50  ? -7.749  4.354   5.376   1.000 54.978  0 50  GLY AAA O     1 ? 1 
ATOM   187   N N     . LYS A 1 51  ? -6.588  3.671   7.182   1.000 51.021  0 51  LYS AAA N     1 ? 1 
ATOM   188   C CA    . LYS A 1 51  ? -7.424  4.371   8.174   1.000 51.757  0 51  LYS AAA CA    1 ? 1 
ATOM   189   C C     . LYS A 1 51  ? -6.963  5.819   8.261   1.000 49.733  0 51  LYS AAA C     1 ? 1 
ATOM   190   O O     . LYS A 1 51  ? -5.776  6.086   8.032   1.000 46.932  0 51  LYS AAA O     1 ? 1 
ATOM   191   C CB    . LYS A 1 51  ? -7.381  3.655   9.529   1.000 52.176  0 51  LYS AAA CB    1 ? 1 
ATOM   192   C CG    . LYS A 1 51  ? -7.883  2.225   9.508   1.000 52.574  0 51  LYS AAA CG    1 ? 1 
ATOM   193   C CD    . LYS A 1 51  ? -9.104  2.013   8.651   1.000 53.770  0 51  LYS AAA CD    1 ? 1 
ATOM   194   C CE    . LYS A 1 51  ? -9.801  0.713   8.979   1.000 54.303  0 51  LYS AAA CE    1 ? 1 
ATOM   195   N NZ    . LYS A 1 51  ? -10.406 0.151   7.755   1.000 56.423  0 51  LYS AAA NZ    1 ? 1 
ATOM   196   N N     . LYS A 1 52  ? -7.912  6.715   8.524   1.000 49.220  0 52  LYS AAA N     1 ? 1 
ATOM   197   C CA    . LYS A 1 52  ? -7.636  8.152   8.735   1.000 50.890  0 52  LYS AAA CA    1 ? 1 
ATOM   198   C C     . LYS A 1 52  ? -7.235  8.325   10.214  1.000 45.486  0 52  LYS AAA C     1 ? 1 
ATOM   199   O O     . LYS A 1 52  ? -8.021  7.903   11.112  1.000 41.429  0 52  LYS AAA O     1 ? 1 
ATOM   200   C CB    . LYS A 1 52  ? -8.867  8.976   8.348   1.000 57.034  0 52  LYS AAA CB    1 ? 1 
ATOM   201   C CG    . LYS A 1 52  ? -8.553  10.405  7.936   1.000 62.405  0 52  LYS AAA CG    1 ? 1 
ATOM   202   C CD    . LYS A 1 52  ? -9.717  11.367  8.042   1.000 66.286  0 52  LYS AAA CD    1 ? 1 
ATOM   203   C CE    . LYS A 1 52  ? -9.221  12.796  7.968   1.000 69.135  0 52  LYS AAA CE    1 ? 1 
ATOM   204   N NZ    . LYS A 1 52  ? -10.291 13.772  8.271   1.000 70.901  0 52  LYS AAA NZ    1 ? 1 
ATOM   205   N N     . VAL A 1 53  ? -6.061  8.910   10.425  1.000 41.305  0 53  VAL AAA N     1 ? 1 
ATOM   206   C CA    . VAL A 1 53  ? -5.343  8.925   11.727  1.000 41.224  0 53  VAL AAA CA    1 ? 1 
ATOM   207   C C     . VAL A 1 53  ? -4.875  10.358  11.969  1.000 39.306  0 53  VAL AAA C     1 ? 1 
ATOM   208   O O     . VAL A 1 53  ? -4.273  10.929  11.040  1.000 38.281  0 53  VAL AAA O     1 ? 1 
ATOM   209   C CB    . VAL A 1 53  ? -4.156  7.938   11.778  1.000 40.923  0 53  VAL AAA CB    1 ? 1 
ATOM   210   C CG1   . VAL A 1 53  ? -3.605  7.791   13.193  1.000 40.866  0 53  VAL AAA CG1   1 ? 1 
ATOM   211   C CG2   . VAL A 1 53  ? -4.521  6.571   11.230  1.000 42.359  0 53  VAL AAA CG2   1 ? 1 
ATOM   212   N N     . ALA A 1 54  ? -5.169  10.889  13.162  1.000 37.505  0 54  ALA AAA N     1 ? 1 
ATOM   213   C CA    . ALA A 1 54  ? -4.593  12.148  13.687  1.000 38.745  0 54  ALA AAA CA    1 ? 1 
ATOM   214   C C     . ALA A 1 54  ? -3.799  11.833  14.949  1.000 39.332  0 54  ALA AAA C     1 ? 1 
ATOM   215   O O     . ALA A 1 54  ? -4.285  10.992  15.759  1.000 39.493  0 54  ALA AAA O     1 ? 1 
ATOM   216   C CB    . ALA A 1 54  ? -5.656  13.164  13.987  1.000 39.140  0 54  ALA AAA CB    1 ? 1 
ATOM   217   N N     . LEU A 1 55  ? -2.623  12.449  15.083  1.000 39.304  0 55  LEU AAA N     1 ? 1 
ATOM   218   C CA    . LEU A 1 55  ? -1.759  12.289  16.269  1.000 38.062  0 55  LEU AAA CA    1 ? 1 
ATOM   219   C C     . LEU A 1 55  ? -1.467  13.675  16.812  1.000 38.417  0 55  LEU AAA C     1 ? 1 
ATOM   220   O O     . LEU A 1 55  ? -1.062  14.546  16.026  1.000 40.148  0 55  LEU AAA O     1 ? 1 
ATOM   221   C CB    . LEU A 1 55  ? -0.479  11.526  15.918  1.000 37.469  0 55  LEU AAA CB    1 ? 1 
ATOM   222   C CG    . LEU A 1 55  ? 0.428   11.195  17.111  1.000 37.662  0 55  LEU AAA CG    1 ? 1 
ATOM   223   C CD1   . LEU A 1 55  ? 1.166   9.869   16.925  1.000 37.607  0 55  LEU AAA CD1   1 ? 1 
ATOM   224   C CD2   . LEU A 1 55  ? 1.431   12.319  17.358  1.000 37.946  0 55  LEU AAA CD2   1 ? 1 
ATOM   225   N N     . PHE A 1 56  ? -1.684  13.830  18.110  1.000 38.870  0 56  PHE AAA N     1 ? 1 
ATOM   226   C CA    . PHE A 1 56  ? -1.337  15.023  18.919  1.000 40.301  0 56  PHE AAA CA    1 ? 1 
ATOM   227   C C     . PHE A 1 56  ? -0.062  14.711  19.701  1.000 37.811  0 56  PHE AAA C     1 ? 1 
ATOM   228   O O     . PHE A 1 56  ? 0.033   13.645  20.306  1.000 37.899  0 56  PHE AAA O     1 ? 1 
ATOM   229   C CB    . PHE A 1 56  ? -2.510  15.429  19.824  1.000 40.097  0 56  PHE AAA CB    1 ? 1 
ATOM   230   C CG    . PHE A 1 56  ? -3.729  15.886  19.059  1.000 42.557  0 56  PHE AAA CG    1 ? 1 
ATOM   231   C CD1   . PHE A 1 56  ? -3.843  17.198  18.621  1.000 44.769  0 56  PHE AAA CD1   1 ? 1 
ATOM   232   C CD2   . PHE A 1 56  ? -4.741  15.005  18.726  1.000 43.679  0 56  PHE AAA CD2   1 ? 1 
ATOM   233   C CE1   . PHE A 1 56  ? -4.940  17.608  17.873  1.000 44.798  0 56  PHE AAA CE1   1 ? 1 
ATOM   234   C CE2   . PHE A 1 56  ? -5.837  15.426  17.989  1.000 46.522  0 56  PHE AAA CE2   1 ? 1 
ATOM   235   C CZ    . PHE A 1 56  ? -5.927  16.720  17.545  1.000 45.754  0 56  PHE AAA CZ    1 ? 1 
ATOM   236   N N     . ASP A 1 57  ? 0.907   15.607  19.623  1.000 37.581  0 57  ASP AAA N     1 ? 1 
ATOM   237   C CA    . ASP A 1 57  ? 2.087   15.654  20.516  1.000 37.079  0 57  ASP AAA CA    1 ? 1 
ATOM   238   C C     . ASP A 1 57  ? 2.400   17.120  20.782  1.000 37.469  0 57  ASP AAA C     1 ? 1 
ATOM   239   O O     . ASP A 1 57  ? 2.538   17.839  19.791  1.000 37.950  0 57  ASP AAA O     1 ? 1 
ATOM   240   C CB    . ASP A 1 57  ? 3.331   14.965  19.941  1.000 36.246  0 57  ASP AAA CB    1 ? 1 
ATOM   241   C CG    . ASP A 1 57  ? 4.375   14.767  21.030  1.000 35.135  0 57  ASP AAA CG    1 ? 1 
ATOM   242   O OD1   . ASP A 1 57  ? 4.085   13.986  21.955  1.000 34.569  0 57  ASP AAA OD1   1 ? 1 
ATOM   243   O OD2   . ASP A 1 57  ? 5.415   15.461  21.010  1.000 33.039  0 57  ASP AAA OD2   1 ? 1 
ATOM   244   N N     . PHE A 1 58  ? 2.490   17.520  22.055  1.000 37.187  0 58  PHE AAA N     1 ? 1 
ATOM   245   C CA    . PHE A 1 58  ? 3.036   18.831  22.486  1.000 38.281  0 58  PHE AAA CA    1 ? 1 
ATOM   246   C C     . PHE A 1 58  ? 3.863   18.605  23.754  1.000 37.627  0 58  PHE AAA C     1 ? 1 
ATOM   247   O O     . PHE A 1 58  ? 3.451   17.842  24.638  1.000 37.133  0 58  PHE AAA O     1 ? 1 
ATOM   248   C CB    . PHE A 1 58  ? 1.912   19.864  22.686  1.000 38.164  0 58  PHE AAA CB    1 ? 1 
ATOM   249   C CG    . PHE A 1 58  ? 2.375   21.240  23.113  1.000 38.791  0 58  PHE AAA CG    1 ? 1 
ATOM   250   C CD1   . PHE A 1 58  ? 2.526   21.560  24.463  1.000 39.804  0 58  PHE AAA CD1   1 ? 1 
ATOM   251   C CD2   . PHE A 1 58  ? 2.666   22.228  22.169  1.000 40.356  0 58  PHE AAA CD2   1 ? 1 
ATOM   252   C CE1   . PHE A 1 58  ? 2.916   22.836  24.863  1.000 40.867  0 58  PHE AAA CE1   1 ? 1 
ATOM   253   C CE2   . PHE A 1 58  ? 3.092   23.489  22.554  1.000 39.942  0 58  PHE AAA CE2   1 ? 1 
ATOM   254   C CZ    . PHE A 1 58  ? 3.219   23.794  23.899  1.000 42.706  0 58  PHE AAA CZ    1 ? 1 
ATOM   255   N N     . VAL A 1 59  ? 4.985   19.292  23.859  1.000 38.212  0 59  VAL AAA N     1 ? 1 
ATOM   256   C CA    . VAL A 1 59  ? 5.901   19.136  25.022  1.000 39.582  0 59  VAL AAA CA    1 ? 1 
ATOM   257   C C     . VAL A 1 59  ? 5.675   20.293  25.995  1.000 39.335  0 59  VAL AAA C     1 ? 1 
ATOM   258   O O     . VAL A 1 59  ? 6.100   21.404  25.688  1.000 38.581  0 59  VAL AAA O     1 ? 1 
ATOM   259   C CB    . VAL A 1 59  ? 7.366   19.029  24.559  1.000 38.881  0 59  VAL AAA CB    1 ? 1 
ATOM   260   C CG1   . VAL A 1 59  ? 8.310   18.814  25.740  1.000 38.566  0 59  VAL AAA CG1   1 ? 1 
ATOM   261   C CG2   . VAL A 1 59  ? 7.509   17.900  23.530  1.000 39.595  0 59  VAL AAA CG2   1 ? 1 
ATOM   262   N N     . LYS A 1 60  ? 5.018   20.033  27.125  1.000 40.694  0 60  LYS AAA N     1 ? 1 
ATOM   263   C CA    . LYS A 1 60  ? 4.992   20.971  28.283  1.000 41.438  0 60  LYS AAA CA    1 ? 1 
ATOM   264   C C     . LYS A 1 60  ? 6.424   21.064  28.815  1.000 43.337  0 60  LYS AAA C     1 ? 1 
ATOM   265   O O     . LYS A 1 60  ? 7.085   20.047  29.039  1.000 44.558  0 60  LYS AAA O     1 ? 1 
ATOM   266   C CB    . LYS A 1 60  ? 3.953   20.529  29.316  1.000 41.307  0 60  LYS AAA CB    1 ? 1 
ATOM   267   C CG    . LYS A 1 60  ? 2.508   20.713  28.849  1.000 42.184  0 60  LYS AAA CG    1 ? 1 
ATOM   268   C CD    . LYS A 1 60  ? 1.438   20.284  29.836  1.000 40.942  0 60  LYS AAA CD    1 ? 1 
ATOM   269   C CE    . LYS A 1 60  ? 1.489   18.812  30.171  1.000 40.050  0 60  LYS AAA CE    1 ? 1 
ATOM   270   N NZ    . LYS A 1 60  ? 1.157   17.994  28.991  1.000 39.277  0 60  LYS AAA NZ    1 ? 1 
ATOM   271   N N     . PRO A 1 61  ? 6.989   22.285  29.007  1.000 44.874  0 61  PRO AAA N     1 ? 1 
ATOM   272   C CA    . PRO A 1 61  ? 8.357   22.403  29.519  1.000 43.866  0 61  PRO AAA CA    1 ? 1 
ATOM   273   C C     . PRO A 1 61  ? 8.510   21.777  30.920  1.000 43.088  0 61  PRO AAA C     1 ? 1 
ATOM   274   O O     . PRO A 1 61  ? 7.561   21.753  31.697  1.000 39.407  0 61  PRO AAA O     1 ? 1 
ATOM   275   C CB    . PRO A 1 61  ? 8.644   23.912  29.547  1.000 44.643  0 61  PRO AAA CB    1 ? 1 
ATOM   276   C CG    . PRO A 1 61  ? 7.587   24.518  28.643  1.000 46.370  0 61  PRO AAA CG    1 ? 1 
ATOM   277   C CD    . PRO A 1 61  ? 6.379   23.598  28.728  1.000 45.689  0 61  PRO AAA CD    1 ? 1 
ATOM   278   N N     . SER A 1 62  ? 9.700   21.254  31.196  1.000 42.780  0 62  SER AAA N     1 ? 1 
ATOM   279   C CA    . SER A 1 62  ? 10.057  20.662  32.502  1.000 42.984  0 62  SER AAA CA    1 ? 1 
ATOM   280   C C     . SER A 1 62  ? 9.913   21.728  33.599  1.000 42.272  0 62  SER AAA C     1 ? 1 
ATOM   281   O O     . SER A 1 62  ? 9.748   22.921  33.289  1.000 44.831  0 62  SER AAA O     1 ? 1 
ATOM   282   C CB    . SER A 1 62  ? 11.459  20.095  32.469  1.000 41.915  0 62  SER AAA CB    1 ? 1 
ATOM   283   O OG    . SER A 1 62  ? 12.405  21.137  32.430  1.000 39.825  0 62  SER AAA OG    1 ? 1 
ATOM   284   N N     . THR A 1 63  ? 10.052  21.313  34.846  1.000 40.720  0 63  THR AAA N     1 ? 1 
ATOM   285   C CA    . THR A 1 63  ? 10.100  22.226  36.018  1.000 42.566  0 63  THR AAA CA    1 ? 1 
ATOM   286   C C     . THR A 1 63  ? 11.225  23.261  35.842  1.000 41.543  0 63  THR AAA C     1 ? 1 
ATOM   287   O O     . THR A 1 63  ? 11.146  24.281  36.501  1.000 41.518  0 63  THR AAA O     1 ? 1 
ATOM   288   C CB    . THR A 1 63  ? 10.219  21.411  37.313  1.000 41.814  0 63  THR AAA CB    1 ? 1 
ATOM   289   O OG1   . THR A 1 63  ? 11.428  20.632  37.267  1.000 36.945  0 63  THR AAA OG1   1 ? 1 
ATOM   290   C CG2   . THR A 1 63  ? 8.991   20.534  37.504  1.000 41.221  0 63  THR AAA CG2   1 ? 1 
ATOM   291   N N     . GLN A 1 64  ? 12.206  23.037  34.966  1.000 41.776  0 64  GLN AAA N     1 ? 1 
ATOM   292   C CA    . GLN A 1 64  ? 13.358  23.965  34.770  1.000 43.915  0 64  GLN AAA CA    1 ? 1 
ATOM   293   C C     . GLN A 1 64  ? 13.338  24.586  33.356  1.000 45.521  0 64  GLN AAA C     1 ? 1 
ATOM   294   O O     . GLN A 1 64  ? 14.383  25.135  32.948  1.000 47.948  0 64  GLN AAA O     1 ? 1 
ATOM   295   C CB    . GLN A 1 64  ? 14.681  23.251  35.101  1.000 42.785  0 64  GLN AAA CB    1 ? 1 
ATOM   296   C CG    . GLN A 1 64  ? 14.835  22.910  36.586  1.000 41.181  0 64  GLN AAA CG    1 ? 1 
ATOM   297   C CD    . GLN A 1 64  ? 14.917  24.133  37.483  1.000 42.792  0 64  GLN AAA CD    1 ? 1 
ATOM   298   O OE1   . GLN A 1 64  ? 15.354  25.208  37.078  1.000 43.825  0 64  GLN AAA OE1   1 ? 1 
ATOM   299   N NE2   . GLN A 1 64  ? 14.474  23.995  38.728  1.000 42.427  0 64  GLN AAA NE2   1 ? 1 
ATOM   300   N N     . GLY A 1 65  ? 12.203  24.550  32.648  1.000 44.600  0 65  GLY AAA N     1 ? 1 
ATOM   301   C CA    . GLY A 1 65  ? 12.019  25.234  31.354  1.000 43.289  0 65  GLY AAA CA    1 ? 1 
ATOM   302   C C     . GLY A 1 65  ? 12.580  24.453  30.171  1.000 42.159  0 65  GLY AAA C     1 ? 1 
ATOM   303   O O     . GLY A 1 65  ? 12.603  25.002  29.068  1.000 43.151  0 65  GLY AAA O     1 ? 1 
ATOM   304   N N     . THR A 1 66  ? 12.992  23.193  30.333  1.000 39.681  0 66  THR AAA N     1 ? 1 
ATOM   305   C CA    . THR A 1 66  ? 13.535  22.388  29.203  1.000 37.793  0 66  THR AAA CA    1 ? 1 
ATOM   306   C C     . THR A 1 66  ? 12.366  21.854  28.366  1.000 37.621  0 66  THR AAA C     1 ? 1 
ATOM   307   O O     . THR A 1 66  ? 11.424  21.322  28.942  1.000 37.112  0 66  THR AAA O     1 ? 1 
ATOM   308   C CB    . THR A 1 66  ? 14.434  21.237  29.665  1.000 36.506  0 66  THR AAA CB    1 ? 1 
ATOM   309   O OG1   . THR A 1 66  ? 15.300  21.741  30.682  1.000 32.961  0 66  THR AAA OG1   1 ? 1 
ATOM   310   C CG2   . THR A 1 66  ? 15.213  20.631  28.514  1.000 37.496  0 66  THR AAA CG2   1 ? 1 
ATOM   311   N N     . LYS A 1 67  ? 12.471  21.965  27.046  1.000 40.561  0 67  LYS AAA N     1 ? 1 
ATOM   312   C CA    . LYS A 1 67  ? 11.518  21.414  26.051  1.000 42.115  0 67  LYS AAA CA    1 ? 1 
ATOM   313   C C     . LYS A 1 67  ? 12.280  20.846  24.851  1.000 39.228  0 67  LYS AAA C     1 ? 1 
ATOM   314   O O     . LYS A 1 67  ? 13.501  21.040  24.772  1.000 39.809  0 67  LYS AAA O     1 ? 1 
ATOM   315   C CB    . LYS A 1 67  ? 10.518  22.490  25.624  1.000 46.068  0 67  LYS AAA CB    1 ? 1 
ATOM   316   C CG    . LYS A 1 67  ? 11.061  23.595  24.735  1.000 50.824  0 67  LYS AAA CG    1 ? 1 
ATOM   317   C CD    . LYS A 1 67  ? 10.048  24.723  24.586  1.000 54.849  0 67  LYS AAA CD    1 ? 1 
ATOM   318   C CE    . LYS A 1 67  ? 10.489  25.766  23.588  1.000 57.208  0 67  LYS AAA CE    1 ? 1 
ATOM   319   N NZ    . LYS A 1 67  ? 9.318   26.410  22.945  1.000 60.041  0 67  LYS AAA NZ    1 ? 1 
ATOM   320   N N     . TRP A 1 68  ? 11.568  20.137  23.971  1.000 37.643  0 68  TRP AAA N     1 ? 1 
ATOM   321   C CA    . TRP A 1 68  ? 12.152  19.259  22.920  1.000 35.652  0 68  TRP AAA CA    1 ? 1 
ATOM   322   C C     . TRP A 1 68  ? 11.082  18.943  21.868  1.000 37.929  0 68  TRP AAA C     1 ? 1 
ATOM   323   O O     . TRP A 1 68  ? 9.871   19.321  22.073  1.000 39.964  0 68  TRP AAA O     1 ? 1 
ATOM   324   C CB    . TRP A 1 68  ? 12.728  17.977  23.555  1.000 32.823  0 68  TRP AAA CB    1 ? 1 
ATOM   325   C CG    . TRP A 1 68  ? 11.805  17.253  24.498  1.000 30.726  0 68  TRP AAA CG    1 ? 1 
ATOM   326   C CD1   . TRP A 1 68  ? 10.810  16.369  24.179  1.000 29.497  0 68  TRP AAA CD1   1 ? 1 
ATOM   327   C CD2   . TRP A 1 68  ? 11.790  17.341  25.935  1.000 29.547  0 68  TRP AAA CD2   1 ? 1 
ATOM   328   N NE1   . TRP A 1 68  ? 10.179  15.916  25.302  1.000 27.682  0 68  TRP AAA NE1   1 ? 1 
ATOM   329   C CE2   . TRP A 1 68  ? 10.766  16.484  26.393  1.000 27.978  0 68  TRP AAA CE2   1 ? 1 
ATOM   330   C CE3   . TRP A 1 68  ? 12.531  18.071  26.877  1.000 28.785  0 68  TRP AAA CE3   1 ? 1 
ATOM   331   C CZ2   . TRP A 1 68  ? 10.488  16.328  27.744  1.000 28.536  0 68  TRP AAA CZ2   1 ? 1 
ATOM   332   C CZ3   . TRP A 1 68  ? 12.225  17.934  28.212  1.000 28.526  0 68  TRP AAA CZ3   1 ? 1 
ATOM   333   C CH2   . TRP A 1 68  ? 11.223  17.067  28.641  1.000 27.939  0 68  TRP AAA CH2   1 ? 1 
ATOM   334   N N     . GLY A 1 69  ? 11.494  18.266  20.798  1.000 36.725  0 69  GLY AAA N     1 ? 1 
ATOM   335   C CA    . GLY A 1 69  ? 10.641  17.944  19.650  1.000 37.656  0 69  GLY AAA CA    1 ? 1 
ATOM   336   C C     . GLY A 1 69  ? 9.874   16.646  19.824  1.000 37.695  0 69  GLY AAA C     1 ? 1 
ATOM   337   O O     . GLY A 1 69  ? 9.752   16.150  20.930  1.000 38.377  0 69  GLY AAA O     1 ? 1 
ATOM   338   N N     . LEU A 1 70  ? 9.344   16.171  18.712  1.000 40.216  0 70  LEU AAA N     1 ? 1 
ATOM   339   C CA    . LEU A 1 70  ? 8.515   14.957  18.556  1.000 40.986  0 70  LEU AAA CA    1 ? 1 
ATOM   340   C C     . LEU A 1 70  ? 9.310   13.711  18.929  1.000 40.135  0 70  LEU AAA C     1 ? 1 
ATOM   341   O O     . LEU A 1 70  ? 10.523  13.669  18.668  1.000 43.599  0 70  LEU AAA O     1 ? 1 
ATOM   342   C CB    . LEU A 1 70  ? 8.068   14.895  17.087  1.000 41.806  0 70  LEU AAA CB    1 ? 1 
ATOM   343   C CG    . LEU A 1 70  ? 7.273   13.653  16.687  1.000 42.661  0 70  LEU AAA CG    1 ? 1 
ATOM   344   C CD1   . LEU A 1 70  ? 5.929   13.587  17.410  1.000 41.762  0 70  LEU AAA CD1   1 ? 1 
ATOM   345   C CD2   . LEU A 1 70  ? 7.034   13.648  15.187  1.000 42.606  0 70  LEU AAA CD2   1 ? 1 
ATOM   346   N N     . GLY A 1 71  ? 8.626   12.695  19.442  1.000 39.710  0 71  GLY AAA N     1 ? 1 
ATOM   347   C CA    . GLY A 1 71  ? 9.199   11.349  19.668  1.000 38.579  0 71  GLY AAA CA    1 ? 1 
ATOM   348   C C     . GLY A 1 71  ? 9.015   10.870  21.093  1.000 36.438  0 71  GLY AAA C     1 ? 1 
ATOM   349   O O     . GLY A 1 71  ? 9.134   9.661   21.322  1.000 36.927  0 71  GLY AAA O     1 ? 1 
ATOM   350   N N     . GLY A 1 72  ? 8.756   11.793  22.012  1.000 35.390  0 72  GLY AAA N     1 ? 1 
ATOM   351   C CA    . GLY A 1 72  ? 8.321   11.484  23.386  1.000 34.846  0 72  GLY AAA CA    1 ? 1 
ATOM   352   C C     . GLY A 1 72  ? 9.517   11.189  24.274  1.000 33.842  0 72  GLY AAA C     1 ? 1 
ATOM   353   O O     . GLY A 1 72  ? 10.633  11.615  23.921  1.000 31.637  0 72  GLY AAA O     1 ? 1 
ATOM   354   N N     . THR A 1 73  ? 9.301   10.492  25.385  1.000 33.681  0 73  THR AAA N     1 ? 1 
ATOM   355   C CA    . THR A 1 73  ? 10.307  10.371  26.474  1.000 33.145  0 73  THR AAA CA    1 ? 1 
ATOM   356   C C     . THR A 1 73  ? 11.552  9.606   25.968  1.000 31.681  0 73  THR AAA C     1 ? 1 
ATOM   357   O O     . THR A 1 73  ? 12.690  10.058  26.217  1.000 29.366  0 73  THR AAA O     1 ? 1 
ATOM   358   C CB    . THR A 1 73  ? 9.687   9.710   27.711  1.000 32.488  0 73  THR AAA CB    1 ? 1 
ATOM   359   O OG1   . THR A 1 73  ? 8.557   10.499  28.074  1.000 31.821  0 73  THR AAA OG1   1 ? 1 
ATOM   360   C CG2   . THR A 1 73  ? 10.696  9.557   28.835  1.000 31.648  0 73  THR AAA CG2   1 ? 1 
ATOM   361   N N     . CYS A 1 74  ? 11.352  8.471   25.313  1.000 31.123  0 74  CYS AAA N     1 ? 1 
ATOM   362   C CA    . CYS A 1 74  ? 12.471  7.602   24.926  1.000 33.503  0 74  CYS AAA CA    1 ? 1 
ATOM   363   C C     . CYS A 1 74  ? 13.438  8.365   23.992  1.000 33.362  0 74  CYS AAA C     1 ? 1 
ATOM   364   O O     . CYS A 1 74  ? 14.675  8.287   24.248  1.000 30.901  0 74  CYS AAA O     1 ? 1 
ATOM   365   C CB    . CYS A 1 74  ? 12.001  6.303   24.303  1.000 36.053  0 74  CYS AAA CB    1 ? 1 
ATOM   366   S SG    . CYS A 1 74  ? 13.399  5.160   24.074  1.000 43.593  0 74  CYS AAA SG    1 ? 1 
ATOM   367   N N     . VAL A 1 75  ? 12.920  9.090   22.986  1.000 31.745  0 75  VAL AAA N     1 ? 1 
ATOM   368   C CA    . VAL A 1 75  ? 13.757  9.766   21.950  1.000 31.116  0 75  VAL AAA CA    1 ? 1 
ATOM   369   C C     . VAL A 1 75  ? 14.527  10.933  22.577  1.000 29.363  0 75  VAL AAA C     1 ? 1 
ATOM   370   O O     . VAL A 1 75  ? 15.732  11.118  22.244  1.000 27.773  0 75  VAL AAA O     1 ? 1 
ATOM   371   C CB    . VAL A 1 75  ? 12.885  10.254  20.780  1.000 31.591  0 75  VAL AAA CB    1 ? 1 
ATOM   372   C CG1   . VAL A 1 75  ? 13.619  11.246  19.908  1.000 32.491  0 75  VAL AAA CG1   1 ? 1 
ATOM   373   C CG2   . VAL A 1 75  ? 12.379  9.096   19.956  1.000 31.785  0 75  VAL AAA CG2   1 ? 1 
ATOM   374   N N     . ASN A 1 76  ? 13.843  11.710  23.415  1.000 28.490  0 76  ASN AAA N     1 ? 1 
ATOM   375   C CA    . ASN A 1 76  ? 14.285  13.066  23.821  1.000 28.526  0 76  ASN AAA CA    1 ? 1 
ATOM   376   C C     . ASN A 1 76  ? 14.988  13.047  25.184  1.000 28.845  0 76  ASN AAA C     1 ? 1 
ATOM   377   O O     . ASN A 1 76  ? 15.961  13.787  25.331  1.000 29.721  0 76  ASN AAA O     1 ? 1 
ATOM   378   C CB    . ASN A 1 76  ? 13.100  14.039  23.780  1.000 28.039  0 76  ASN AAA CB    1 ? 1 
ATOM   379   C CG    . ASN A 1 76  ? 12.638  14.251  22.357  1.000 28.364  0 76  ASN AAA CG    1 ? 1 
ATOM   380   O OD1   . ASN A 1 76  ? 13.264  14.993  21.584  1.000 27.463  0 76  ASN AAA OD1   1 ? 1 
ATOM   381   N ND2   . ASN A 1 76  ? 11.573  13.553  21.989  1.000 28.181  0 76  ASN AAA ND2   1 ? 1 
ATOM   382   N N     . VAL A 1 77  ? 14.471  12.318  26.171  1.000 28.639  0 77  VAL AAA N     1 ? 1 
ATOM   383   C CA    . VAL A 1 77  ? 14.853  12.524  27.596  1.000 28.004  0 77  VAL AAA CA    1 ? 1 
ATOM   384   C C     . VAL A 1 77  ? 14.825  11.172  28.309  1.000 27.503  0 77  VAL AAA C     1 ? 1 
ATOM   385   O O     . VAL A 1 77  ? 14.663  11.166  29.498  1.000 26.342  0 77  VAL AAA O     1 ? 1 
ATOM   386   C CB    . VAL A 1 77  ? 13.943  13.562  28.302  1.000 28.793  0 77  VAL AAA CB    1 ? 1 
ATOM   387   C CG1   . VAL A 1 77  ? 14.245  14.972  27.878  1.000 29.499  0 77  VAL AAA CG1   1 ? 1 
ATOM   388   C CG2   . VAL A 1 77  ? 12.455  13.287  28.136  1.000 29.698  0 77  VAL AAA CG2   1 ? 1 
ATOM   389   N N     . GLY A 1 78  ? 15.061  10.075  27.599  1.000 28.011  0 78  GLY AAA N     1 ? 1 
ATOM   390   C CA    . GLY A 1 78  ? 15.009  8.721   28.166  1.000 27.519  0 78  GLY AAA CA    1 ? 1 
ATOM   391   C C     . GLY A 1 78  ? 16.031  7.818   27.509  1.000 28.641  0 78  GLY AAA C     1 ? 1 
ATOM   392   O O     . GLY A 1 78  ? 17.244  8.164   27.543  1.000 28.905  0 78  GLY AAA O     1 ? 1 
ATOM   393   N N     . CYS A 1 79  ? 15.582  6.706   26.935  1.000 28.307  0 79  CYS AAA N     1 ? 1 
ATOM   394   C CA    . CYS A 1 79  ? 16.457  5.597   26.497  1.000 30.022  0 79  CYS AAA CA    1 ? 1 
ATOM   395   C C     . CYS A 1 79  ? 17.573  6.133   25.610  1.000 29.527  0 79  CYS AAA C     1 ? 1 
ATOM   396   O O     . CYS A 1 79  ? 18.718  5.741   25.842  1.000 28.711  0 79  CYS AAA O     1 ? 1 
ATOM   397   C CB    . CYS A 1 79  ? 15.715  4.501   25.752  1.000 31.900  0 79  CYS AAA CB    1 ? 1 
ATOM   398   S SG    . CYS A 1 79  ? 13.932  4.517   26.005  1.000 34.761  0 79  CYS AAA SG    1 ? 1 
ATOM   399   N N     . VAL A 1 80  ? 17.253  6.991   24.633  1.000 28.506  0 80  VAL AAA N     1 ? 1 
ATOM   400   C CA    . VAL A 1 80  ? 18.261  7.380   23.607  1.000 28.452  0 80  VAL AAA CA    1 ? 1 
ATOM   401   C C     . VAL A 1 80  ? 19.390  8.187   24.245  1.000 27.309  0 80  VAL AAA C     1 ? 1 
ATOM   402   O O     . VAL A 1 80  ? 20.518  7.755   24.220  1.000 26.375  0 80  VAL AAA O     1 ? 1 
ATOM   403   C CB    . VAL A 1 80  ? 17.643  8.114   22.405  1.000 29.171  0 80  VAL AAA CB    1 ? 1 
ATOM   404   C CG1   . VAL A 1 80  ? 18.722  8.744   21.536  1.000 28.174  0 80  VAL AAA CG1   1 ? 1 
ATOM   405   C CG2   . VAL A 1 80  ? 16.748  7.175   21.599  1.000 29.533  0 80  VAL AAA CG2   1 ? 1 
ATOM   406   N N     . PRO A 1 81  ? 19.153  9.370   24.825  1.000 27.694  0 81  PRO AAA N     1 ? 1 
ATOM   407   C CA    . PRO A 1 81  ? 20.235  10.127  25.442  1.000 28.495  0 81  PRO AAA CA    1 ? 1 
ATOM   408   C C     . PRO A 1 81  ? 20.908  9.371   26.597  1.000 29.168  0 81  PRO AAA C     1 ? 1 
ATOM   409   O O     . PRO A 1 81  ? 22.104  9.511   26.716  1.000 31.666  0 81  PRO AAA O     1 ? 1 
ATOM   410   C CB    . PRO A 1 81  ? 19.592  11.442  25.958  1.000 28.371  0 81  PRO AAA CB    1 ? 1 
ATOM   411   C CG    . PRO A 1 81  ? 18.088  11.200  25.900  1.000 28.809  0 81  PRO AAA CG    1 ? 1 
ATOM   412   C CD    . PRO A 1 81  ? 17.856  10.061  24.911  1.000 28.660  0 81  PRO AAA CD    1 ? 1 
ATOM   413   N N     . LYS A 1 82  ? 20.163  8.605   27.399  1.000 28.390  0 82  LYS AAA N     1 ? 1 
ATOM   414   C CA    . LYS A 1 82  ? 20.750  7.839   28.531  1.000 29.385  0 82  LYS AAA CA    1 ? 1 
ATOM   415   C C     . LYS A 1 82  ? 21.801  6.877   27.955  1.000 28.139  0 82  LYS AAA C     1 ? 1 
ATOM   416   O O     . LYS A 1 82  ? 22.948  6.831   28.472  1.000 27.548  0 82  LYS AAA O     1 ? 1 
ATOM   417   C CB    . LYS A 1 82  ? 19.651  7.107   29.299  1.000 31.562  0 82  LYS AAA CB    1 ? 1 
ATOM   418   C CG    . LYS A 1 82  ? 20.096  6.081   30.327  1.000 33.726  0 82  LYS AAA CG    1 ? 1 
ATOM   419   C CD    . LYS A 1 82  ? 20.367  4.693   29.803  1.000 34.995  0 82  LYS AAA CD    1 ? 1 
ATOM   420   C CE    . LYS A 1 82  ? 19.166  3.971   29.215  1.000 37.068  0 82  LYS AAA CE    1 ? 1 
ATOM   421   N NZ    . LYS A 1 82  ? 18.080  3.661   30.187  1.000 35.763  0 82  LYS AAA NZ    1 ? 1 
ATOM   422   N N     . LYS A 1 83  ? 21.468  6.194   26.863  1.000 27.072  0 83  LYS AAA N     1 ? 1 
ATOM   423   C CA    . LYS A 1 83  ? 22.340  5.172   26.233  1.000 27.342  0 83  LYS AAA CA    1 ? 1 
ATOM   424   C C     . LYS A 1 83  ? 23.580  5.858   25.628  1.000 28.187  0 83  LYS AAA C     1 ? 1 
ATOM   425   O O     . LYS A 1 83  ? 24.693  5.287   25.738  1.000 27.181  0 83  LYS AAA O     1 ? 1 
ATOM   426   C CB    . LYS A 1 83  ? 21.519  4.365   25.232  1.000 27.282  0 83  LYS AAA CB    1 ? 1 
ATOM   427   C CG    . LYS A 1 83  ? 22.276  3.230   24.554  1.000 28.811  0 83  LYS AAA CG    1 ? 1 
ATOM   428   C CD    . LYS A 1 83  ? 22.346  1.972   25.361  1.000 28.962  0 83  LYS AAA CD    1 ? 1 
ATOM   429   C CE    . LYS A 1 83  ? 23.474  1.058   24.924  1.000 28.414  0 83  LYS AAA CE    1 ? 1 
ATOM   430   N NZ    . LYS A 1 83  ? 23.014  -0.240  24.455  1.000 27.110  0 83  LYS AAA NZ    1 ? 1 
ATOM   431   N N     . LEU A 1 84  ? 23.432  7.061   25.062  1.000 27.537  0 84  LEU AAA N     1 ? 1 
ATOM   432   C CA    . LEU A 1 84  ? 24.597  7.798   24.522  1.000 28.250  0 84  LEU AAA CA    1 ? 1 
ATOM   433   C C     . LEU A 1 84  ? 25.479  8.258   25.688  1.000 29.268  0 84  LEU AAA C     1 ? 1 
ATOM   434   O O     . LEU A 1 84  ? 26.721  8.145   25.589  1.000 29.482  0 84  LEU AAA O     1 ? 1 
ATOM   435   C CB    . LEU A 1 84  ? 24.071  8.965   23.689  1.000 28.052  0 84  LEU AAA CB    1 ? 1 
ATOM   436   C CG    . LEU A 1 84  ? 23.313  8.564   22.413  1.000 28.193  0 84  LEU AAA CG    1 ? 1 
ATOM   437   C CD1   . LEU A 1 84  ? 22.777  9.806   21.687  1.000 28.563  0 84  LEU AAA CD1   1 ? 1 
ATOM   438   C CD2   . LEU A 1 84  ? 24.190  7.741   21.466  1.000 27.146  0 84  LEU AAA CD2   1 ? 1 
ATOM   439   N N     . MET A 1 85  ? 24.892  8.734   26.789  1.000 28.843  0 85  MET AAA N     1 ? 1 
ATOM   440   C CA    . MET A 1 85  ? 25.713  9.126   27.953  1.000 30.098  0 85  MET AAA CA    1 ? 1 
ATOM   441   C C     . MET A 1 85  ? 26.442  7.881   28.494  1.000 26.974  0 85  MET AAA C     1 ? 1 
ATOM   442   O O     . MET A 1 85  ? 27.623  7.988   28.816  1.000 27.532  0 85  MET AAA O     1 ? 1 
ATOM   443   C CB    . MET A 1 85  ? 24.859  9.755   29.042  1.000 34.032  0 85  MET AAA CB    1 ? 1 
ATOM   444   C CG    . MET A 1 85  ? 24.203  11.041  28.582  1.000 37.575  0 85  MET AAA CG    1 ? 1 
ATOM   445   S SD    . MET A 1 85  ? 25.015  12.458  29.388  1.000 44.274  0 85  MET AAA SD    1 ? 1 
ATOM   446   C CE    . MET A 1 85  ? 24.512  13.834  28.380  1.000 43.325  0 85  MET AAA CE    1 ? 1 
ATOM   447   N N     . HIS A 1 86  ? 25.776  6.738   28.587  1.000 24.163  0 86  HIS AAA N     1 ? 1 
ATOM   448   C CA    . HIS A 1 86  ? 26.361  5.459   29.073  1.000 22.735  0 86  HIS AAA CA    1 ? 1 
ATOM   449   C C     . HIS A 1 86  ? 27.566  5.117   28.192  1.000 22.780  0 86  HIS AAA C     1 ? 1 
ATOM   450   O O     . HIS A 1 86  ? 28.643  4.783   28.754  1.000 22.457  0 86  HIS AAA O     1 ? 1 
ATOM   451   C CB    . HIS A 1 86  ? 25.277  4.380   29.080  1.000 21.427  0 86  HIS AAA CB    1 ? 1 
ATOM   452   C CG    . HIS A 1 86  ? 25.743  3.002   29.413  1.000 20.510  0 86  HIS AAA CG    1 ? 1 
ATOM   453   N ND1   . HIS A 1 86  ? 26.313  2.673   30.628  1.000 19.989  0 86  HIS AAA ND1   1 ? 1 
ATOM   454   C CD2   . HIS A 1 86  ? 25.652  1.841   28.718  1.000 20.034  0 86  HIS AAA CD2   1 ? 1 
ATOM   455   C CE1   . HIS A 1 86  ? 26.533  1.370   30.685  1.000 18.977  0 86  HIS AAA CE1   1 ? 1 
ATOM   456   N NE2   . HIS A 1 86  ? 26.145  0.838   29.523  1.000 19.411  0 86  HIS AAA NE2   1 ? 1 
ATOM   457   N N     . TYR A 1 87  ? 27.414  5.269   26.874  1.000 22.453  0 87  TYR AAA N     1 ? 1 
ATOM   458   C CA    . TYR A 1 87  ? 28.470  4.972   25.894  1.000 23.901  0 87  TYR AAA CA    1 ? 1 
ATOM   459   C C     . TYR A 1 87  ? 29.679  5.881   26.171  1.000 23.131  0 87  TYR AAA C     1 ? 1 
ATOM   460   O O     . TYR A 1 87  ? 30.792  5.367   26.275  1.000 21.761  0 87  TYR AAA O     1 ? 1 
ATOM   461   C CB    . TYR A 1 87  ? 27.939  5.072   24.459  1.000 25.655  0 87  TYR AAA CB    1 ? 1 
ATOM   462   C CG    . TYR A 1 87  ? 28.905  4.479   23.474  1.000 28.925  0 87  TYR AAA CG    1 ? 1 
ATOM   463   C CD1   . TYR A 1 87  ? 29.238  3.128   23.506  1.000 31.224  0 87  TYR AAA CD1   1 ? 1 
ATOM   464   C CD2   . TYR A 1 87  ? 29.545  5.277   22.538  1.000 32.063  0 87  TYR AAA CD2   1 ? 1 
ATOM   465   C CE1   . TYR A 1 87  ? 30.176  2.590   22.630  1.000 34.057  0 87  TYR AAA CE1   1 ? 1 
ATOM   466   C CE2   . TYR A 1 87  ? 30.471  4.761   21.650  1.000 31.610  0 87  TYR AAA CE2   1 ? 1 
ATOM   467   C CZ    . TYR A 1 87  ? 30.769  3.412   21.676  1.000 34.829  0 87  TYR AAA CZ    1 ? 1 
ATOM   468   O OH    . TYR A 1 87  ? 31.690  2.920   20.801  1.000 37.201  0 87  TYR AAA OH    1 ? 1 
ATOM   469   N N     . SER A 1 88  ? 29.456  7.179   26.364  1.000 22.532  0 88  SER AAA N     1 ? 1 
ATOM   470   C CA    . SER A 1 88  ? 30.522  8.131   26.752  1.000 23.927  0 88  SER AAA CA    1 ? 1 
ATOM   471   C C     . SER A 1 88  ? 31.206  7.641   28.015  1.000 24.335  0 88  SER AAA C     1 ? 1 
ATOM   472   O O     . SER A 1 88  ? 32.424  7.766   28.088  1.000 24.787  0 88  SER AAA O     1 ? 1 
ATOM   473   C CB    . SER A 1 88  ? 29.997  9.535   26.973  1.000 24.862  0 88  SER AAA CB    1 ? 1 
ATOM   474   O OG    . SER A 1 88  ? 31.067  10.444  27.233  1.000 24.755  0 88  SER AAA OG    1 ? 1 
ATOM   475   N N     . ALA A 1 89  ? 30.435  7.135   28.983  1.000 24.225  0 89  ALA AAA N     1 ? 1 
ATOM   476   C CA    . ALA A 1 89  ? 30.951  6.608   30.274  1.000 24.466  0 89  ALA AAA CA    1 ? 1 
ATOM   477   C C     . ALA A 1 89  ? 31.842  5.385   30.035  1.000 23.666  0 89  ALA AAA C     1 ? 1 
ATOM   478   O O     . ALA A 1 89  ? 32.948  5.355   30.600  1.000 24.089  0 89  ALA AAA O     1 ? 1 
ATOM   479   C CB    . ALA A 1 89  ? 29.787  6.283   31.206  1.000 24.298  0 89  ALA AAA CB    1 ? 1 
ATOM   480   N N     . LEU A 1 90  ? 31.376  4.442   29.204  1.000 24.206  0 90  LEU AAA N     1 ? 1 
ATOM   481   C CA    . LEU A 1 90  ? 32.110  3.191   28.859  1.000 25.210  0 90  LEU AAA CA    1 ? 1 
ATOM   482   C C     . LEU A 1 90  ? 33.411  3.620   28.208  1.000 25.751  0 90  LEU AAA C     1 ? 1 
ATOM   483   O O     . LEU A 1 90  ? 34.436  2.959   28.457  1.000 26.120  0 90  LEU AAA O     1 ? 1 
ATOM   484   C CB    . LEU A 1 90  ? 31.310  2.273   27.922  1.000 26.120  0 90  LEU AAA CB    1 ? 1 
ATOM   485   C CG    . LEU A 1 90  ? 30.098  1.592   28.585  1.000 27.612  0 90  LEU AAA CG    1 ? 1 
ATOM   486   C CD1   . LEU A 1 90  ? 29.267  0.773   27.594  1.000 27.465  0 90  LEU AAA CD1   1 ? 1 
ATOM   487   C CD2   . LEU A 1 90  ? 30.524  0.723   29.741  1.000 26.773  0 90  LEU AAA CD2   1 ? 1 
ATOM   488   N N     . ILE A 1 91  ? 33.367  4.697   27.424  1.000 25.972  0 91  ILE AAA N     1 ? 1 
ATOM   489   C CA    . ILE A 1 91  ? 34.583  5.171   26.714  1.000 26.562  0 91  ILE AAA CA    1 ? 1 
ATOM   490   C C     . ILE A 1 91  ? 35.561  5.703   27.773  1.000 26.919  0 91  ILE AAA C     1 ? 1 
ATOM   491   O O     . ILE A 1 91  ? 36.743  5.278   27.739  1.000 26.748  0 91  ILE AAA O     1 ? 1 
ATOM   492   C CB    . ILE A 1 91  ? 34.256  6.210   25.623  1.000 26.123  0 91  ILE AAA CB    1 ? 1 
ATOM   493   C CG1   . ILE A 1 91  ? 33.516  5.552   24.466  1.000 25.020  0 91  ILE AAA CG1   1 ? 1 
ATOM   494   C CG2   . ILE A 1 91  ? 35.543  6.898   25.162  1.000 26.184  0 91  ILE AAA CG2   1 ? 1 
ATOM   495   C CD1   . ILE A 1 91  ? 33.212  6.495   23.342  1.000 25.398  0 91  ILE AAA CD1   1 ? 1 
ATOM   496   N N     . ALA A 1 92  ? 35.097  6.590   28.660  1.000 26.408  0 92  ALA AAA N     1 ? 1 
ATOM   497   C CA    . ALA A 1 92  ? 35.894  7.090   29.808  1.000 27.466  0 92  ALA AAA CA    1 ? 1 
ATOM   498   C C     . ALA A 1 92  ? 36.561  5.916   30.545  1.000 28.087  0 92  ALA AAA C     1 ? 1 
ATOM   499   O O     . ALA A 1 92  ? 37.803  5.929   30.725  1.000 26.944  0 92  ALA AAA O     1 ? 1 
ATOM   500   C CB    . ALA A 1 92  ? 34.997  7.861   30.745  1.000 27.603  0 92  ALA AAA CB    1 ? 1 
ATOM   501   N N     . SER A 1 93  ? 35.751  4.931   30.963  1.000 28.508  0 93  SER AAA N     1 ? 1 
ATOM   502   C CA    . SER A 1 93  ? 36.203  3.727   31.710  1.000 28.754  0 93  SER AAA CA    1 ? 1 
ATOM   503   C C     . SER A 1 93  ? 37.313  2.995   30.944  1.000 28.412  0 93  SER AAA C     1 ? 1 
ATOM   504   O O     . SER A 1 93  ? 38.367  2.715   31.489  1.000 29.852  0 93  SER AAA O     1 ? 1 
ATOM   505   C CB    . SER A 1 93  ? 35.028  2.825   31.983  1.000 28.714  0 93  SER AAA CB    1 ? 1 
ATOM   506   O OG    . SER A 1 93  ? 34.443  3.158   33.212  1.000 30.669  0 93  SER AAA OG    1 ? 1 
ATOM   507   N N     A SER A 1 94  ? 37.053  2.681   29.686  0.500 29.114  0 94  SER AAA N     1 ? 1 
ATOM   508   N N     B SER A 1 94  ? 37.053  2.681   29.686  0.500 29.114  0 94  SER AAA N     1 ? 1 
ATOM   509   C CA    A SER A 1 94  ? 37.990  1.984   28.777  0.500 29.408  0 94  SER AAA CA    1 ? 1 
ATOM   510   C CA    B SER A 1 94  ? 37.990  1.984   28.777  0.500 29.408  0 94  SER AAA CA    1 ? 1 
ATOM   511   C C     A SER A 1 94  ? 39.309  2.762   28.689  0.500 30.413  0 94  SER AAA C     1 ? 1 
ATOM   512   C C     B SER A 1 94  ? 39.309  2.762   28.689  0.500 30.413  0 94  SER AAA C     1 ? 1 
ATOM   513   O O     A SER A 1 94  ? 40.373  2.127   28.733  0.500 31.084  0 94  SER AAA O     1 ? 1 
ATOM   514   O O     B SER A 1 94  ? 40.373  2.127   28.733  0.500 31.084  0 94  SER AAA O     1 ? 1 
ATOM   515   C CB    A SER A 1 94  ? 37.332  1.799   27.441  0.500 29.083  0 94  SER AAA CB    1 ? 1 
ATOM   516   C CB    B SER A 1 94  ? 37.332  1.799   27.441  0.500 29.083  0 94  SER AAA CB    1 ? 1 
ATOM   517   O OG    A SER A 1 94  ? 38.303  1.804   26.417  0.500 30.182  0 94  SER AAA OG    1 ? 1 
ATOM   518   O OG    B SER A 1 94  ? 38.303  1.804   26.417  0.500 30.182  0 94  SER AAA OG    1 ? 1 
ATOM   519   N N     . ILE A 1 95  ? 39.248  4.095   28.588  1.000 31.570  0 95  ILE AAA N     1 ? 1 
ATOM   520   C CA    . ILE A 1 95  ? 40.457  4.958   28.468  1.000 32.688  0 95  ILE AAA CA    1 ? 1 
ATOM   521   C C     . ILE A 1 95  ? 41.199  4.990   29.810  1.000 33.340  0 95  ILE AAA C     1 ? 1 
ATOM   522   O O     . ILE A 1 95  ? 42.414  4.823   29.787  1.000 32.333  0 95  ILE AAA O     1 ? 1 
ATOM   523   C CB    . ILE A 1 95  ? 40.117  6.382   28.026  1.000 34.116  0 95  ILE AAA CB    1 ? 1 
ATOM   524   C CG1   . ILE A 1 95  ? 39.654  6.435   26.574  1.000 35.680  0 95  ILE AAA CG1   1 ? 1 
ATOM   525   C CG2   . ILE A 1 95  ? 41.320  7.303   28.246  1.000 34.576  0 95  ILE AAA CG2   1 ? 1 
ATOM   526   C CD1   . ILE A 1 95  ? 39.203  7.814   26.122  1.000 36.366  0 95  ILE AAA CD1   1 ? 1 
ATOM   527   N N     . HIS A 1 96  ? 40.510  5.196   30.934  1.000 33.658  0 96  HIS AAA N     1 ? 1 
ATOM   528   C CA    . HIS A 1 96  ? 41.143  5.192   32.286  1.000 32.904  0 96  HIS AAA CA    1 ? 1 
ATOM   529   C C     . HIS A 1 96  ? 41.761  3.821   32.594  1.000 31.104  0 96  HIS AAA C     1 ? 1 
ATOM   530   O O     . HIS A 1 96  ? 42.979  3.786   32.908  1.000 28.900  0 96  HIS AAA O     1 ? 1 
ATOM   531   C CB    . HIS A 1 96  ? 40.167  5.600   33.385  1.000 35.261  0 96  HIS AAA CB    1 ? 1 
ATOM   532   C CG    . HIS A 1 96  ? 40.806  5.661   34.737  1.000 38.086  0 96  HIS AAA CG    1 ? 1 
ATOM   533   N ND1   . HIS A 1 96  ? 40.518  4.717   35.751  1.000 42.146  0 96  HIS AAA ND1   1 ? 1 
ATOM   534   C CD2   . HIS A 1 96  ? 41.719  6.517   35.258  1.000 41.768  0 96  HIS AAA CD2   1 ? 1 
ATOM   535   C CE1   . HIS A 1 96  ? 41.236  4.993   36.825  1.000 43.613  0 96  HIS AAA CE1   1 ? 1 
ATOM   536   N NE2   . HIS A 1 96  ? 42.014  6.078   36.532  1.000 45.288  0 96  HIS AAA NE2   1 ? 1 
ATOM   537   N N     . HIS A 1 97  ? 40.987  2.739   32.462  1.000 29.124  0 97  HIS AAA N     1 ? 1 
ATOM   538   C CA    . HIS A 1 97  ? 41.329  1.405   33.034  1.000 28.929  0 97  HIS AAA CA    1 ? 1 
ATOM   539   C C     . HIS A 1 97  ? 42.138  0.565   32.050  1.000 26.845  0 97  HIS AAA C     1 ? 1 
ATOM   540   O O     . HIS A 1 97  ? 42.935  -0.230  32.552  1.000 26.053  0 97  HIS AAA O     1 ? 1 
ATOM   541   C CB    . HIS A 1 97  ? 40.070  0.591   33.413  1.000 27.541  0 97  HIS AAA CB    1 ? 1 
ATOM   542   C CG    . HIS A 1 97  ? 39.392  1.138   34.601  1.000 28.823  0 97  HIS AAA CG    1 ? 1 
ATOM   543   N ND1   . HIS A 1 97  ? 40.010  1.150   35.847  1.000 30.181  0 97  HIS AAA ND1   1 ? 1 
ATOM   544   C CD2   . HIS A 1 97  ? 38.165  1.678   34.771  1.000 29.259  0 97  HIS AAA CD2   1 ? 1 
ATOM   545   C CE1   . HIS A 1 97  ? 39.177  1.661   36.739  1.000 29.697  0 97  HIS AAA CE1   1 ? 1 
ATOM   546   N NE2   . HIS A 1 97  ? 38.045  1.981   36.117  1.000 29.530  0 97  HIS AAA NE2   1 ? 1 
ATOM   547   N N     . ASP A 1 98  ? 41.841  0.645   30.748  1.000 25.542  0 98  ASP AAA N     1 ? 1 
ATOM   548   C CA    . ASP A 1 98  ? 42.132  -0.467  29.803  1.000 25.865  0 98  ASP AAA CA    1 ? 1 
ATOM   549   C C     . ASP A 1 98  ? 43.138  -0.035  28.732  1.000 26.157  0 98  ASP AAA C     1 ? 1 
ATOM   550   O O     . ASP A 1 98  ? 43.940  -0.888  28.327  1.000 27.143  0 98  ASP AAA O     1 ? 1 
ATOM   551   C CB    . ASP A 1 98  ? 40.879  -0.954  29.071  1.000 25.904  0 98  ASP AAA CB    1 ? 1 
ATOM   552   C CG    . ASP A 1 98  ? 39.791  -1.583  29.930  1.000 26.080  0 98  ASP AAA CG    1 ? 1 
ATOM   553   O OD1   . ASP A 1 98  ? 40.023  -1.841  31.124  1.000 25.903  0 98  ASP AAA OD1   1 ? 1 
ATOM   554   O OD2   . ASP A 1 98  ? 38.717  -1.831  29.395  1.000 27.492  0 98  ASP AAA OD2   1 ? 1 
ATOM   555   N N     . ALA A 1 99  ? 43.073  1.203   28.256  1.000 26.180  0 99  ALA AAA N     1 ? 1 
ATOM   556   C CA    . ALA A 1 99  ? 43.792  1.643   27.036  1.000 28.631  0 99  ALA AAA CA    1 ? 1 
ATOM   557   C C     . ALA A 1 99  ? 45.290  1.374   27.179  1.000 29.103  0 99  ALA AAA C     1 ? 1 
ATOM   558   O O     . ALA A 1 99  ? 45.848  0.752   26.299  1.000 29.749  0 99  ALA AAA O     1 ? 1 
ATOM   559   C CB    . ALA A 1 99  ? 43.513  3.093   26.725  1.000 28.443  0 99  ALA AAA CB    1 ? 1 
ATOM   560   N N     . GLN A 1 100 ? 45.906  1.841   28.239  1.000 30.555  0 100 GLN AAA N     1 ? 1 
ATOM   561   C CA    . GLN A 1 100 ? 47.364  1.677   28.455  1.000 34.530  0 100 GLN AAA CA    1 ? 1 
ATOM   562   C C     . GLN A 1 100 ? 47.712  0.175   28.490  1.000 32.825  0 100 GLN AAA C     1 ? 1 
ATOM   563   O O     . GLN A 1 100 ? 48.678  -0.238  27.794  1.000 34.240  0 100 GLN AAA O     1 ? 1 
ATOM   564   C CB    . GLN A 1 100 ? 47.764  2.446   29.719  1.000 39.474  0 100 GLN AAA CB    1 ? 1 
ATOM   565   C CG    . GLN A 1 100 ? 49.174  2.158   30.204  1.000 46.764  0 100 GLN AAA CG    1 ? 1 
ATOM   566   C CD    . GLN A 1 100 ? 50.150  3.195   29.737  1.000 51.845  0 100 GLN AAA CD    1 ? 1 
ATOM   567   O OE1   . GLN A 1 100 ? 50.297  4.237   30.372  1.000 55.641  0 100 GLN AAA OE1   1 ? 1 
ATOM   568   N NE2   . GLN A 1 100 ? 50.844  2.877   28.660  1.000 56.725  0 100 GLN AAA NE2   1 ? 1 
ATOM   569   N N     . MET A 1 101 ? 46.951  -0.631  29.232  1.000 30.825  0 101 MET AAA N     1 ? 1 
ATOM   570   C CA    . MET A 1 101 ? 47.197  -2.093  29.387  1.000 29.646  0 101 MET AAA CA    1 ? 1 
ATOM   571   C C     . MET A 1 101 ? 47.158  -2.773  27.998  1.000 27.816  0 101 MET AAA C     1 ? 1 
ATOM   572   O O     . MET A 1 101 ? 47.865  -3.802  27.796  1.000 27.715  0 101 MET AAA O     1 ? 1 
ATOM   573   C CB    . MET A 1 101 ? 46.152  -2.739  30.299  1.000 29.641  0 101 MET AAA CB    1 ? 1 
ATOM   574   C CG    . MET A 1 101 ? 46.303  -2.403  31.777  1.000 31.693  0 101 MET AAA CG    1 ? 1 
ATOM   575   S SD    . MET A 1 101 ? 47.850  -2.989  32.530  1.000 33.376  0 101 MET AAA SD    1 ? 1 
ATOM   576   C CE    . MET A 1 101 ? 47.679  -4.775  32.472  1.000 32.380  0 101 MET AAA CE    1 ? 1 
ATOM   577   N N     . PHE A 1 102 ? 46.314  -2.284  27.093  1.000 25.709  0 102 PHE AAA N     1 ? 1 
ATOM   578   C CA    . PHE A 1 102 ? 46.128  -2.897  25.746  1.000 26.095  0 102 PHE AAA CA    1 ? 1 
ATOM   579   C C     . PHE A 1 102 ? 46.989  -2.149  24.723  1.000 24.429  0 102 PHE AAA C     1 ? 1 
ATOM   580   O O     . PHE A 1 102 ? 46.747  -2.317  23.541  1.000 23.430  0 102 PHE AAA O     1 ? 1 
ATOM   581   C CB    . PHE A 1 102 ? 44.638  -3.010  25.373  1.000 25.459  0 102 PHE AAA CB    1 ? 1 
ATOM   582   C CG    . PHE A 1 102 ? 43.978  -4.136  26.101  1.000 24.917  0 102 PHE AAA CG    1 ? 1 
ATOM   583   C CD1   . PHE A 1 102 ? 43.500  -3.946  27.388  1.000 24.847  0 102 PHE AAA CD1   1 ? 1 
ATOM   584   C CD2   . PHE A 1 102 ? 43.950  -5.406  25.555  1.000 24.542  0 102 PHE AAA CD2   1 ? 1 
ATOM   585   C CE1   . PHE A 1 102 ? 42.953  -5.004  28.094  1.000 24.448  0 102 PHE AAA CE1   1 ? 1 
ATOM   586   C CE2   . PHE A 1 102 ? 43.420  -6.464  26.275  1.000 24.464  0 102 PHE AAA CE2   1 ? 1 
ATOM   587   C CZ    . PHE A 1 102 ? 42.952  -6.271  27.557  1.000 24.491  0 102 PHE AAA CZ    1 ? 1 
ATOM   588   N N     . GLY A 1 103 ? 47.979  -1.397  25.199  1.000 24.983  0 103 GLY AAA N     1 ? 1 
ATOM   589   C CA    . GLY A 1 103 ? 49.095  -0.857  24.391  1.000 26.665  0 103 GLY AAA CA    1 ? 1 
ATOM   590   C C     . GLY A 1 103 ? 48.882  0.583   23.968  1.000 27.009  0 103 GLY AAA C     1 ? 1 
ATOM   591   O O     . GLY A 1 103 ? 49.742  1.110   23.295  1.000 27.753  0 103 GLY AAA O     1 ? 1 
ATOM   592   N N     . HIS A 1 104 ? 47.770  1.187   24.348  1.000 28.529  0 104 HIS AAA N     1 ? 1 
ATOM   593   C CA    . HIS A 1 104 ? 47.361  2.545   23.910  1.000 30.557  0 104 HIS AAA CA    1 ? 1 
ATOM   594   C C     . HIS A 1 104 ? 47.597  3.539   25.048  1.000 33.951  0 104 HIS AAA C     1 ? 1 
ATOM   595   O O     . HIS A 1 104 ? 46.730  3.648   25.917  1.000 33.067  0 104 HIS AAA O     1 ? 1 
ATOM   596   C CB    . HIS A 1 104 ? 45.908  2.522   23.442  1.000 30.348  0 104 HIS AAA CB    1 ? 1 
ATOM   597   C CG    . HIS A 1 104 ? 45.652  1.605   22.302  1.000 29.642  0 104 HIS AAA CG    1 ? 1 
ATOM   598   N ND1   . HIS A 1 104 ? 45.893  1.989   20.999  1.000 30.070  0 104 HIS AAA ND1   1 ? 1 
ATOM   599   C CD2   . HIS A 1 104 ? 45.168  0.351   22.261  1.000 30.130  0 104 HIS AAA CD2   1 ? 1 
ATOM   600   C CE1   . HIS A 1 104 ? 45.586  0.987   20.187  1.000 30.129  0 104 HIS AAA CE1   1 ? 1 
ATOM   601   N NE2   . HIS A 1 104 ? 45.165  -0.046  20.943  1.000 30.620  0 104 HIS AAA NE2   1 ? 1 
ATOM   602   N N     . LYS A 1 105 ? 48.785  4.155   25.064  1.000 37.467  0 105 LYS AAA N     1 ? 1 
ATOM   603   C CA    . LYS A 1 105 ? 49.151  5.301   25.940  1.000 41.488  0 105 LYS AAA CA    1 ? 1 
ATOM   604   C C     . LYS A 1 105 ? 48.371  6.531   25.444  1.000 41.099  0 105 LYS AAA C     1 ? 1 
ATOM   605   O O     . LYS A 1 105 ? 48.527  6.946   24.264  1.000 43.101  0 105 LYS AAA O     1 ? 1 
ATOM   606   C CB    . LYS A 1 105 ? 50.665  5.540   25.898  1.000 44.612  0 105 LYS AAA CB    1 ? 1 
ATOM   607   C CG    . LYS A 1 105 ? 51.169  6.684   26.766  1.000 49.504  0 105 LYS AAA CG    1 ? 1 
ATOM   608   C CD    . LYS A 1 105 ? 51.147  6.395   28.257  1.000 53.826  0 105 LYS AAA CD    1 ? 1 
ATOM   609   C CE    . LYS A 1 105 ? 52.297  7.082   28.990  1.000 57.550  0 105 LYS AAA CE    1 ? 1 
ATOM   610   N NZ    . LYS A 1 105 ? 53.612  6.427   28.720  1.000 58.340  0 105 LYS AAA NZ    1 ? 1 
ATOM   611   N N     . THR A 1 106 ? 47.527  7.079   26.297  1.000 41.651  0 106 THR AAA N     1 ? 1 
ATOM   612   C CA    . THR A 1 106 ? 46.553  8.133   25.928  1.000 42.707  0 106 THR AAA CA    1 ? 1 
ATOM   613   C C     . THR A 1 106 ? 46.624  9.299   26.906  1.000 42.268  0 106 THR AAA C     1 ? 1 
ATOM   614   O O     . THR A 1 106 ? 46.846  9.054   28.095  1.000 42.234  0 106 THR AAA O     1 ? 1 
ATOM   615   C CB    . THR A 1 106 ? 45.123  7.586   25.949  1.000 42.034  0 106 THR AAA CB    1 ? 1 
ATOM   616   O OG1   . THR A 1 106 ? 44.846  7.402   27.327  1.000 43.222  0 106 THR AAA OG1   1 ? 1 
ATOM   617   C CG2   . THR A 1 106 ? 44.940  6.295   25.183  1.000 41.666  0 106 THR AAA CG2   1 ? 1 
ATOM   618   N N     . SER A 1 107 ? 46.408  10.516  26.426  1.000 42.713  0 107 SER AAA N     1 ? 1 
ATOM   619   C CA    . SER A 1 107 ? 45.964  11.640  27.282  1.000 42.054  0 107 SER AAA CA    1 ? 1 
ATOM   620   C C     . SER A 1 107 ? 44.581  12.049  26.793  1.000 40.935  0 107 SER AAA C     1 ? 1 
ATOM   621   O O     . SER A 1 107 ? 44.323  11.980  25.587  1.000 40.359  0 107 SER AAA O     1 ? 1 
ATOM   622   C CB    . SER A 1 107 ? 46.959  12.778  27.289  1.000 44.037  0 107 SER AAA CB    1 ? 1 
ATOM   623   O OG    . SER A 1 107 ? 47.221  13.252  25.981  1.000 42.991  0 107 SER AAA OG    1 ? 1 
ATOM   624   N N     . SER A 1 108 ? 43.727  12.423  27.721  1.000 40.659  0 108 SER AAA N     1 ? 1 
ATOM   625   C CA    . SER A 1 108 ? 42.286  12.629  27.491  1.000 44.283  0 108 SER AAA CA    1 ? 1 
ATOM   626   C C     . SER A 1 108 ? 41.815  13.738  28.418  1.000 45.287  0 108 SER AAA C     1 ? 1 
ATOM   627   O O     . SER A 1 108 ? 42.290  13.766  29.566  1.000 46.232  0 108 SER AAA O     1 ? 1 
ATOM   628   C CB    . SER A 1 108 ? 41.518  11.342  27.764  1.000 44.569  0 108 SER AAA CB    1 ? 1 
ATOM   629   O OG    . SER A 1 108 ? 40.160  11.476  27.393  1.000 42.858  0 108 SER AAA OG    1 ? 1 
ATOM   630   N N     . SER A 1 109 ? 40.881  14.576  27.970  1.000 43.704  0 109 SER AAA N     1 ? 1 
ATOM   631   C CA    . SER A 1 109 ? 40.086  15.439  28.879  1.000 41.792  0 109 SER AAA CA    1 ? 1 
ATOM   632   C C     . SER A 1 109 ? 38.634  15.414  28.413  1.000 40.615  0 109 SER AAA C     1 ? 1 
ATOM   633   O O     . SER A 1 109 ? 38.400  15.346  27.169  1.000 41.078  0 109 SER AAA O     1 ? 1 
ATOM   634   C CB    . SER A 1 109 ? 40.631  16.856  28.974  1.000 41.054  0 109 SER AAA CB    1 ? 1 
ATOM   635   O OG    . SER A 1 109 ? 40.920  17.399  27.697  1.000 40.517  0 109 SER AAA OG    1 ? 1 
ATOM   636   N N     . PHE A 1 110 ? 37.713  15.503  29.367  1.000 38.928  0 110 PHE AAA N     1 ? 1 
ATOM   637   C CA    . PHE A 1 110 ? 36.250  15.397  29.117  1.000 37.842  0 110 PHE AAA CA    1 ? 1 
ATOM   638   C C     . PHE A 1 110 ? 35.655  16.791  28.950  1.000 36.172  0 110 PHE AAA C     1 ? 1 
ATOM   639   O O     . PHE A 1 110 ? 35.973  17.641  29.777  1.000 37.040  0 110 PHE AAA O     1 ? 1 
ATOM   640   C CB    . PHE A 1 110 ? 35.535  14.679  30.260  1.000 37.202  0 110 PHE AAA CB    1 ? 1 
ATOM   641   C CG    . PHE A 1 110 ? 34.055  14.629  30.039  1.000 36.444  0 110 PHE AAA CG    1 ? 1 
ATOM   642   C CD1   . PHE A 1 110 ? 33.538  13.987  28.931  1.000 35.240  0 110 PHE AAA CD1   1 ? 1 
ATOM   643   C CD2   . PHE A 1 110 ? 33.188  15.271  30.906  1.000 36.702  0 110 PHE AAA CD2   1 ? 1 
ATOM   644   C CE1   . PHE A 1 110 ? 32.163  13.927  28.716  1.000 35.923  0 110 PHE AAA CE1   1 ? 1 
ATOM   645   C CE2   . PHE A 1 110 ? 31.812  15.222  30.693  1.000 36.635  0 110 PHE AAA CE2   1 ? 1 
ATOM   646   C CZ    . PHE A 1 110 ? 31.299  14.553  29.592  1.000 36.650  0 110 PHE AAA CZ    1 ? 1 
ATOM   647   N N     . GLU A 1 111 ? 34.813  16.994  27.942  1.000 34.208  0 111 GLU AAA N     1 ? 1 
ATOM   648   C CA    . GLU A 1 111 ? 34.127  18.272  27.709  1.000 34.984  0 111 GLU AAA CA    1 ? 1 
ATOM   649   C C     . GLU A 1 111 ? 32.617  18.013  27.655  1.000 33.516  0 111 GLU AAA C     1 ? 1 
ATOM   650   O O     . GLU A 1 111 ? 32.142  17.515  26.632  1.000 32.865  0 111 GLU AAA O     1 ? 1 
ATOM   651   C CB    . GLU A 1 111 ? 34.757  18.945  26.477  1.000 36.215  0 111 GLU AAA CB    1 ? 1 
ATOM   652   C CG    . GLU A 1 111 ? 36.198  19.418  26.735  1.000 38.461  0 111 GLU AAA CG    1 ? 1 
ATOM   653   C CD    . GLU A 1 111 ? 36.430  20.477  27.841  1.000 40.743  0 111 GLU AAA CD    1 ? 1 
ATOM   654   O OE1   . GLU A 1 111 ? 37.636  20.709  28.204  1.000 39.833  0 111 GLU AAA OE1   1 ? 1 
ATOM   655   O OE2   . GLU A 1 111 ? 35.414  21.114  28.365  1.000 38.960  0 111 GLU AAA OE2   1 ? 1 
ATOM   656   N N     . TRP A 1 112 ? 31.910  18.364  28.722  1.000 33.503  0 112 TRP AAA N     1 ? 1 
ATOM   657   C CA    . TRP A 1 112 ? 30.459  18.081  28.922  1.000 33.003  0 112 TRP AAA CA    1 ? 1 
ATOM   658   C C     . TRP A 1 112 ? 29.663  18.587  27.711  1.000 32.369  0 112 TRP AAA C     1 ? 1 
ATOM   659   O O     . TRP A 1 112 ? 28.833  17.805  27.166  1.000 31.029  0 112 TRP AAA O     1 ? 1 
ATOM   660   C CB    . TRP A 1 112 ? 29.951  18.657  30.257  1.000 32.691  0 112 TRP AAA CB    1 ? 1 
ATOM   661   C CG    . TRP A 1 112 ? 28.454  18.635  30.411  1.000 33.268  0 112 TRP AAA CG    1 ? 1 
ATOM   662   C CD1   . TRP A 1 112 ? 27.577  19.654  30.144  1.000 33.443  0 112 TRP AAA CD1   1 ? 1 
ATOM   663   C CD2   . TRP A 1 112 ? 27.644  17.521  30.851  1.000 32.318  0 112 TRP AAA CD2   1 ? 1 
ATOM   664   N NE1   . TRP A 1 112 ? 26.290  19.249  30.405  1.000 32.829  0 112 TRP AAA NE1   1 ? 1 
ATOM   665   C CE2   . TRP A 1 112 ? 26.301  17.952  30.827  1.000 31.776  0 112 TRP AAA CE2   1 ? 1 
ATOM   666   C CE3   . TRP A 1 112 ? 27.922  16.205  31.254  1.000 32.184  0 112 TRP AAA CE3   1 ? 1 
ATOM   667   C CZ2   . TRP A 1 112 ? 25.248  17.133  31.205  1.000 31.441  0 112 TRP AAA CZ2   1 ? 1 
ATOM   668   C CZ3   . TRP A 1 112 ? 26.877  15.390  31.626  1.000 32.073  0 112 TRP AAA CZ3   1 ? 1 
ATOM   669   C CH2   . TRP A 1 112 ? 25.556  15.841  31.567  1.000 32.337  0 112 TRP AAA CH2   1 ? 1 
ATOM   670   N N     . GLY A 1 113 ? 29.906  19.835  27.297  1.000 33.880  0 113 GLY AAA N     1 ? 1 
ATOM   671   C CA    . GLY A 1 113 ? 29.142  20.514  26.220  1.000 34.993  0 113 GLY AAA CA    1 ? 1 
ATOM   672   C C     . GLY A 1 113 ? 29.280  19.824  24.858  1.000 34.320  0 113 GLY AAA C     1 ? 1 
ATOM   673   O O     . GLY A 1 113 ? 28.378  19.944  24.035  1.000 35.464  0 113 GLY AAA O     1 ? 1 
ATOM   674   N N     . LYS A 1 114 ? 30.400  19.159  24.609  1.000 34.093  0 114 LYS AAA N     1 ? 1 
ATOM   675   C CA    . LYS A 1 114 ? 30.634  18.432  23.339  1.000 34.379  0 114 LYS AAA CA    1 ? 1 
ATOM   676   C C     . LYS A 1 114 ? 29.714  17.197  23.278  1.000 33.239  0 114 LYS AAA C     1 ? 1 
ATOM   677   O O     . LYS A 1 114 ? 29.110  16.968  22.217  1.000 31.952  0 114 LYS AAA O     1 ? 1 
ATOM   678   C CB    . LYS A 1 114 ? 32.112  18.062  23.239  1.000 34.991  0 114 LYS AAA CB    1 ? 1 
ATOM   679   C CG    . LYS A 1 114 ? 32.488  17.336  21.963  1.000 37.029  0 114 LYS AAA CG    1 ? 1 
ATOM   680   C CD    . LYS A 1 114 ? 31.901  17.951  20.704  1.000 39.381  0 114 LYS AAA CD    1 ? 1 
ATOM   681   C CE    . LYS A 1 114 ? 32.336  17.140  19.510  1.000 41.655  0 114 LYS AAA CE    1 ? 1 
ATOM   682   N NZ    . LYS A 1 114 ? 32.166  17.876  18.240  1.000 44.820  0 114 LYS AAA NZ    1 ? 1 
ATOM   683   N N     . LEU A 1 115 ? 29.593  16.462  24.387  1.000 31.168  0 115 LEU AAA N     1 ? 1 
ATOM   684   C CA    . LEU A 1 115 ? 28.743  15.244  24.516  1.000 30.707  0 115 LEU AAA CA    1 ? 1 
ATOM   685   C C     . LEU A 1 115 ? 27.281  15.647  24.358  1.000 30.401  0 115 LEU AAA C     1 ? 1 
ATOM   686   O O     . LEU A 1 115 ? 26.559  15.021  23.562  1.000 28.456  0 115 LEU AAA O     1 ? 1 
ATOM   687   C CB    . LEU A 1 115 ? 28.991  14.580  25.876  1.000 29.387  0 115 LEU AAA CB    1 ? 1 
ATOM   688   C CG    . LEU A 1 115 ? 28.032  13.456  26.241  1.000 28.721  0 115 LEU AAA CG    1 ? 1 
ATOM   689   C CD1   . LEU A 1 115 ? 28.133  12.312  25.249  1.000 28.263  0 115 LEU AAA CD1   1 ? 1 
ATOM   690   C CD2   . LEU A 1 115 ? 28.258  12.983  27.672  1.000 28.550  0 115 LEU AAA CD2   1 ? 1 
ATOM   691   N N     . VAL A 1 116 ? 26.884  16.691  25.081  1.000 32.610  0 116 VAL AAA N     1 ? 1 
ATOM   692   C CA    . VAL A 1 116 ? 25.542  17.313  24.968  1.000 33.802  0 116 VAL AAA CA    1 ? 1 
ATOM   693   C C     . VAL A 1 116 ? 25.304  17.600  23.488  1.000 34.108  0 116 VAL AAA C     1 ? 1 
ATOM   694   O O     . VAL A 1 116 ? 24.318  17.129  22.960  1.000 33.190  0 116 VAL AAA O     1 ? 1 
ATOM   695   C CB    . VAL A 1 116 ? 25.434  18.567  25.859  1.000 35.240  0 116 VAL AAA CB    1 ? 1 
ATOM   696   C CG1   . VAL A 1 116 ? 24.265  19.455  25.491  1.000 36.660  0 116 VAL AAA CG1   1 ? 1 
ATOM   697   C CG2   . VAL A 1 116 ? 25.334  18.202  27.320  1.000 35.536  0 116 VAL AAA CG2   1 ? 1 
ATOM   698   N N     . GLU A 1 117 ? 26.238  18.269  22.826  1.000 37.721  0 117 GLU AAA N     1 ? 1 
ATOM   699   C CA    . GLU A 1 117 ? 26.088  18.668  21.402  1.000 41.490  0 117 GLU AAA CA    1 ? 1 
ATOM   700   C C     . GLU A 1 117 ? 25.883  17.409  20.537  1.000 38.549  0 117 GLU AAA C     1 ? 1 
ATOM   701   O O     . GLU A 1 117 ? 24.967  17.397  19.720  1.000 36.949  0 117 GLU AAA O     1 ? 1 
ATOM   702   C CB    . GLU A 1 117 ? 27.265  19.582  21.037  1.000 45.149  0 117 GLU AAA CB    1 ? 1 
ATOM   703   C CG    . GLU A 1 117 ? 27.412  19.924  19.560  1.000 47.610  0 117 GLU AAA CG    1 ? 1 
ATOM   704   C CD    . GLU A 1 117 ? 28.745  20.629  19.365  1.000 53.168  0 117 GLU AAA CD    1 ? 1 
ATOM   705   O OE1   . GLU A 1 117 ? 29.734  19.938  18.947  1.000 51.972  0 117 GLU AAA OE1   1 ? 1 
ATOM   706   O OE2   . GLU A 1 117 ? 28.799  21.859  19.699  1.000 57.718  0 117 GLU AAA OE2   1 ? 1 
ATOM   707   N N     . THR A 1 118 ? 26.650  16.344  20.739  1.000 38.339  0 118 THR AAA N     1 ? 1 
ATOM   708   C CA    . THR A 1 118 ? 26.488  15.052  19.991  1.000 38.084  0 118 THR AAA CA    1 ? 1 
ATOM   709   C C     . THR A 1 118 ? 25.097  14.433  20.269  1.000 36.336  0 118 THR AAA C     1 ? 1 
ATOM   710   O O     . THR A 1 118 ? 24.486  13.951  19.328  1.000 33.421  0 118 THR AAA O     1 ? 1 
ATOM   711   C CB    . THR A 1 118 ? 27.658  14.114  20.322  1.000 37.865  0 118 THR AAA CB    1 ? 1 
ATOM   712   O OG1   . THR A 1 118 ? 28.795  14.702  19.676  1.000 36.832  0 118 THR AAA OG1   1 ? 1 
ATOM   713   C CG2   . THR A 1 118 ? 27.443  12.670  19.900  1.000 37.158  0 118 THR AAA CG2   1 ? 1 
ATOM   714   N N     . LEU A 1 119 ? 24.614  14.451  21.516  1.000 36.581  0 119 LEU AAA N     1 ? 1 
ATOM   715   C CA    . LEU A 1 119 ? 23.228  14.013  21.875  1.000 37.994  0 119 LEU AAA CA    1 ? 1 
ATOM   716   C C     . LEU A 1 119 ? 22.196  14.858  21.133  1.000 37.300  0 119 LEU AAA C     1 ? 1 
ATOM   717   O O     . LEU A 1 119 ? 21.379  14.263  20.438  1.000 36.949  0 119 LEU AAA O     1 ? 1 
ATOM   718   C CB    . LEU A 1 119 ? 22.964  14.145  23.380  1.000 38.081  0 119 LEU AAA CB    1 ? 1 
ATOM   719   C CG    . LEU A 1 119 ? 23.245  12.894  24.194  1.000 37.582  0 119 LEU AAA CG    1 ? 1 
ATOM   720   C CD1   . LEU A 1 119 ? 24.712  12.513  24.113  1.000 36.519  0 119 LEU AAA CD1   1 ? 1 
ATOM   721   C CD2   . LEU A 1 119 ? 22.846  13.143  25.636  1.000 37.780  0 119 LEU AAA CD2   1 ? 1 
ATOM   722   N N     . ARG A 1 120 ? 22.239  16.173  21.326  1.000 40.927  0 120 ARG AAA N     1 ? 1 
ATOM   723   C CA    . ARG A 1 120 ? 21.299  17.168  20.733  1.000 48.015  0 120 ARG AAA CA    1 ? 1 
ATOM   724   C C     . ARG A 1 120 ? 21.218  16.936  19.222  1.000 46.058  0 120 ARG AAA C     1 ? 1 
ATOM   725   O O     . ARG A 1 120 ? 20.092  16.833  18.745  1.000 43.610  0 120 ARG AAA O     1 ? 1 
ATOM   726   C CB    . ARG A 1 120 ? 21.702  18.626  21.020  1.000 54.573  0 120 ARG AAA CB    1 ? 1 
ATOM   727   C CG    . ARG A 1 120 ? 21.042  19.240  22.251  1.000 60.673  0 120 ARG AAA CG    1 ? 1 
ATOM   728   C CD    . ARG A 1 120 ? 21.127  20.759  22.299  1.000 69.222  0 120 ARG AAA CD    1 ? 1 
ATOM   729   N NE    . ARG A 1 120 ? 22.330  21.292  22.957  1.000 76.313  0 120 ARG AAA NE    1 ? 1 
ATOM   730   C CZ    . ARG A 1 120 ? 23.473  21.686  22.364  1.000 75.054  0 120 ARG AAA CZ    1 ? 1 
ATOM   731   N NH1   . ARG A 1 120 ? 23.635  21.629  21.048  1.000 72.240  0 120 ARG AAA NH1   1 ? 1 
ATOM   732   N NH2   . ARG A 1 120 ? 24.467  22.124  23.120  1.000 75.631  0 120 ARG AAA NH2   1 ? 1 
ATOM   733   N N     . ASN A 1 121 ? 22.355  16.830  18.517  1.000 43.244  0 121 ASN AAA N     1 ? 1 
ATOM   734   C CA    . ASN A 1 121 ? 22.389  16.636  17.036  1.000 43.161  0 121 ASN AAA CA    1 ? 1 
ATOM   735   C C     . ASN A 1 121 ? 21.672  15.340  16.664  1.000 39.651  0 121 ASN AAA C     1 ? 1 
ATOM   736   O O     . ASN A 1 121 ? 20.879  15.361  15.762  1.000 38.716  0 121 ASN AAA O     1 ? 1 
ATOM   737   C CB    . ASN A 1 121 ? 23.808  16.616  16.444  1.000 44.285  0 121 ASN AAA CB    1 ? 1 
ATOM   738   C CG    . ASN A 1 121 ? 24.520  17.955  16.529  1.000 46.500  0 121 ASN AAA CG    1 ? 1 
ATOM   739   O OD1   . ASN A 1 121 ? 23.917  18.964  16.916  1.000 48.939  0 121 ASN AAA OD1   1 ? 1 
ATOM   740   N ND2   . ASN A 1 121 ? 25.817  17.964  16.228  1.000 45.200  0 121 ASN AAA ND2   1 ? 1 
ATOM   741   N N     . HIS A 1 122 ? 21.933  14.256  17.369  1.000 38.404  0 122 HIS AAA N     1 ? 1 
ATOM   742   C CA    . HIS A 1 122 ? 21.354  12.938  17.026  1.000 36.470  0 122 HIS AAA CA    1 ? 1 
ATOM   743   C C     . HIS A 1 122 ? 19.847  12.955  17.313  1.000 36.824  0 122 HIS AAA C     1 ? 1 
ATOM   744   O O     . HIS A 1 122 ? 19.067  12.513  16.461  1.000 35.605  0 122 HIS AAA O     1 ? 1 
ATOM   745   C CB    . HIS A 1 122 ? 22.127  11.834  17.753  1.000 35.250  0 122 HIS AAA CB    1 ? 1 
ATOM   746   C CG    . HIS A 1 122 ? 21.752  10.511  17.213  1.000 35.121  0 122 HIS AAA CG    1 ? 1 
ATOM   747   N ND1   . HIS A 1 122 ? 20.812  9.715   17.820  1.000 36.708  0 122 HIS AAA ND1   1 ? 1 
ATOM   748   C CD2   . HIS A 1 122 ? 22.141  9.864   16.095  1.000 34.956  0 122 HIS AAA CD2   1 ? 1 
ATOM   749   C CE1   . HIS A 1 122 ? 20.639  8.621   17.106  1.000 34.777  0 122 HIS AAA CE1   1 ? 1 
ATOM   750   N NE2   . HIS A 1 122 ? 21.473  8.675   16.065  1.000 34.252  0 122 HIS AAA NE2   1 ? 1 
ATOM   751   N N     . ILE A 1 123 ? 19.440  13.504  18.453  1.000 37.289  0 123 ILE AAA N     1 ? 1 
ATOM   752   C CA    . ILE A 1 123 ? 18.000  13.650  18.836  1.000 37.983  0 123 ILE AAA CA    1 ? 1 
ATOM   753   C C     . ILE A 1 123 ? 17.287  14.583  17.851  1.000 40.074  0 123 ILE AAA C     1 ? 1 
ATOM   754   O O     . ILE A 1 123 ? 16.161  14.255  17.471  1.000 42.357  0 123 ILE AAA O     1 ? 1 
ATOM   755   C CB    . ILE A 1 123 ? 17.883  14.119  20.303  1.000 36.377  0 123 ILE AAA CB    1 ? 1 
ATOM   756   C CG1   . ILE A 1 123 ? 18.312  12.992  21.233  1.000 36.654  0 123 ILE AAA CG1   1 ? 1 
ATOM   757   C CG2   . ILE A 1 123 ? 16.499  14.644  20.626  1.000 35.153  0 123 ILE AAA CG2   1 ? 1 
ATOM   758   C CD1   . ILE A 1 123 ? 18.589  13.410  22.657  1.000 37.448  0 123 ILE AAA CD1   1 ? 1 
ATOM   759   N N     . ARG A 1 124 ? 17.911  15.682  17.421  1.000 43.630  0 124 ARG AAA N     1 ? 1 
ATOM   760   C CA    . ARG A 1 124 ? 17.302  16.599  16.414  1.000 47.260  0 124 ARG AAA CA    1 ? 1 
ATOM   761   C C     . ARG A 1 124 ? 17.032  15.800  15.135  1.000 42.955  0 124 ARG AAA C     1 ? 1 
ATOM   762   O O     . ARG A 1 124 ? 15.889  15.806  14.665  1.000 39.167  0 124 ARG AAA O     1 ? 1 
ATOM   763   C CB    . ARG A 1 124 ? 18.181  17.821  16.151  1.000 52.640  0 124 ARG AAA CB    1 ? 1 
ATOM   764   C CG    . ARG A 1 124 ? 17.422  19.043  15.640  1.000 58.043  0 124 ARG AAA CG    1 ? 1 
ATOM   765   C CD    . ARG A 1 124 ? 18.314  20.274  15.471  1.000 62.748  0 124 ARG AAA CD    1 ? 1 
ATOM   766   N NE    . ARG A 1 124 ? 19.110  20.596  16.663  1.000 64.443  0 124 ARG AAA NE    1 ? 1 
ATOM   767   C CZ    . ARG A 1 124 ? 20.444  20.443  16.784  1.000 67.403  0 124 ARG AAA CZ    1 ? 1 
ATOM   768   N NH1   . ARG A 1 124 ? 21.192  19.971  15.790  1.000 66.854  0 124 ARG AAA NH1   1 ? 1 
ATOM   769   N NH2   . ARG A 1 124 ? 21.026  20.764  17.928  1.000 68.215  0 124 ARG AAA NH2   1 ? 1 
ATOM   770   N N     . MET A 1 125 ? 18.024  15.064  14.643  1.000 42.296  0 125 MET AAA N     1 ? 1 
ATOM   771   C CA    . MET A 1 125 ? 17.876  14.210  13.436  1.000 41.962  0 125 MET AAA CA    1 ? 1 
ATOM   772   C C     . MET A 1 125 ? 16.651  13.291  13.641  1.000 41.236  0 125 MET AAA C     1 ? 1 
ATOM   773   O O     . MET A 1 125 ? 15.872  13.167  12.699  1.000 41.353  0 125 MET AAA O     1 ? 1 
ATOM   774   C CB    . MET A 1 125 ? 19.174  13.432  13.192  1.000 41.127  0 125 MET AAA CB    1 ? 1 
ATOM   775   C CG    . MET A 1 125 ? 19.179  12.546  11.948  1.000 43.702  0 125 MET AAA CG    1 ? 1 
ATOM   776   S SD    . MET A 1 125 ? 18.344  10.927  12.128  1.000 48.788  0 125 MET AAA SD    1 ? 1 
ATOM   777   C CE    . MET A 1 125 ? 19.251  10.202  13.492  1.000 47.259  0 125 MET AAA CE    1 ? 1 
ATOM   778   N N     . LEU A 1 126 ? 16.464  12.702  14.839  1.000 37.645  0 126 LEU AAA N     1 ? 1 
ATOM   779   C CA    . LEU A 1 126 ? 15.346  11.769  15.173  1.000 34.977  0 126 LEU AAA CA    1 ? 1 
ATOM   780   C C     . LEU A 1 126 ? 14.021  12.541  15.245  1.000 34.240  0 126 LEU AAA C     1 ? 1 
ATOM   781   O O     . LEU A 1 126 ? 13.032  12.023  14.764  1.000 32.734  0 126 LEU AAA O     1 ? 1 
ATOM   782   C CB    . LEU A 1 126 ? 15.614  11.039  16.496  1.000 33.109  0 126 LEU AAA CB    1 ? 1 
ATOM   783   C CG    . LEU A 1 126 ? 16.617  9.887   16.459  1.000 32.060  0 126 LEU AAA CG    1 ? 1 
ATOM   784   C CD1   . LEU A 1 126 ? 16.981  9.443   17.877  1.000 31.753  0 126 LEU AAA CD1   1 ? 1 
ATOM   785   C CD2   . LEU A 1 126 ? 16.127  8.700   15.657  1.000 31.067  0 126 LEU AAA CD2   1 ? 1 
ATOM   786   N N     . ASN A 1 127 ? 13.992  13.733  15.829  1.000 35.724  0 127 ASN AAA N     1 ? 1 
ATOM   787   C CA    . ASN A 1 127 ? 12.759  14.569  15.799  1.000 37.240  0 127 ASN AAA CA    1 ? 1 
ATOM   788   C C     . ASN A 1 127 ? 12.299  14.688  14.342  1.000 39.153  0 127 ASN AAA C     1 ? 1 
ATOM   789   O O     . ASN A 1 127 ? 11.138  14.389  14.058  1.000 38.512  0 127 ASN AAA O     1 ? 1 
ATOM   790   C CB    . ASN A 1 127 ? 12.930  15.963  16.399  1.000 37.880  0 127 ASN AAA CB    1 ? 1 
ATOM   791   C CG    . ASN A 1 127 ? 13.375  15.995  17.850  1.000 37.517  0 127 ASN AAA CG    1 ? 1 
ATOM   792   O OD1   . ASN A 1 127 ? 14.196  16.831  18.222  1.000 37.190  0 127 ASN AAA OD1   1 ? 1 
ATOM   793   N ND2   . ASN A 1 127 ? 12.855  15.098  18.667  1.000 36.468  0 127 ASN AAA ND2   1 ? 1 
ATOM   794   N N     . PHE A 1 128 ? 13.204  15.080  13.440  1.000 42.091  0 128 PHE AAA N     1 ? 1 
ATOM   795   C CA    . PHE A 1 128 ? 12.916  15.355  12.007  1.000 44.894  0 128 PHE AAA CA    1 ? 1 
ATOM   796   C C     . PHE A 1 128 ? 12.489  14.045  11.335  1.000 44.170  0 128 PHE AAA C     1 ? 1 
ATOM   797   O O     . PHE A 1 128 ? 11.432  13.986  10.686  1.000 40.899  0 128 PHE AAA O     1 ? 1 
ATOM   798   C CB    . PHE A 1 128 ? 14.157  16.046  11.432  1.000 46.321  0 128 PHE AAA CB    1 ? 1 
ATOM   799   C CG    . PHE A 1 128 ? 14.213  16.285  9.954   1.000 50.490  0 128 PHE AAA CG    1 ? 1 
ATOM   800   C CD1   . PHE A 1 128 ? 13.093  16.679  9.224   1.000 51.988  0 128 PHE AAA CD1   1 ? 1 
ATOM   801   C CD2   . PHE A 1 128 ? 15.438  16.241  9.305   1.000 51.302  0 128 PHE AAA CD2   1 ? 1 
ATOM   802   C CE1   . PHE A 1 128 ? 13.185  16.900  7.857   1.000 49.743  0 128 PHE AAA CE1   1 ? 1 
ATOM   803   C CE2   . PHE A 1 128 ? 15.530  16.511  7.945   1.000 48.957  0 128 PHE AAA CE2   1 ? 1 
ATOM   804   C CZ    . PHE A 1 128 ? 14.405  16.821  7.232   1.000 49.019  0 128 PHE AAA CZ    1 ? 1 
ATOM   805   N N     . SER A 1 129 ? 13.272  13.000  11.556  1.000 42.427  0 129 SER AAA N     1 ? 1 
ATOM   806   C CA    . SER A 1 129 ? 13.032  11.647  11.016  1.000 45.261  0 129 SER AAA CA    1 ? 1 
ATOM   807   C C     . SER A 1 129 ? 11.609  11.186  11.361  1.000 45.173  0 129 SER AAA C     1 ? 1 
ATOM   808   O O     . SER A 1 129 ? 10.942  10.620  10.484  1.000 43.836  0 129 SER AAA O     1 ? 1 
ATOM   809   C CB    . SER A 1 129 ? 14.132  10.723  11.529  1.000 45.311  0 129 SER AAA CB    1 ? 1 
ATOM   810   O OG    . SER A 1 129 ? 13.889  9.368   11.203  1.000 44.742  0 129 SER AAA OG    1 ? 1 
ATOM   811   N N     . TYR A 1 130 ? 11.128  11.426  12.585  1.000 48.733  0 130 TYR AAA N     1 ? 1 
ATOM   812   C CA    . TYR A 1 130 ? 9.769   10.993  13.015  1.000 50.124  0 130 TYR AAA CA    1 ? 1 
ATOM   813   C C     . TYR A 1 130 ? 8.688   11.888  12.377  1.000 49.846  0 130 TYR AAA C     1 ? 1 
ATOM   814   O O     . TYR A 1 130 ? 7.663   11.352  11.985  1.000 48.510  0 130 TYR AAA O     1 ? 1 
ATOM   815   C CB    . TYR A 1 130 ? 9.664   10.927  14.544  1.000 52.933  0 130 TYR AAA CB    1 ? 1 
ATOM   816   C CG    . TYR A 1 130 ? 10.325  9.724   15.162  1.000 54.190  0 130 TYR AAA CG    1 ? 1 
ATOM   817   C CD1   . TYR A 1 130 ? 9.936   8.450   14.789  1.000 57.631  0 130 TYR AAA CD1   1 ? 1 
ATOM   818   C CD2   . TYR A 1 130 ? 11.326  9.847   16.116  1.000 55.048  0 130 TYR AAA CD2   1 ? 1 
ATOM   819   C CE1   . TYR A 1 130 ? 10.558  7.326   15.301  1.000 60.904  0 130 TYR AAA CE1   1 ? 1 
ATOM   820   C CE2   . TYR A 1 130 ? 11.934  8.730   16.670  1.000 57.942  0 130 TYR AAA CE2   1 ? 1 
ATOM   821   C CZ    . TYR A 1 130 ? 11.545  7.464   16.262  1.000 60.834  0 130 TYR AAA CZ    1 ? 1 
ATOM   822   O OH    . TYR A 1 130 ? 12.121  6.337   16.776  1.000 63.126  0 130 TYR AAA OH    1 ? 1 
ATOM   823   N N     . ARG A 1 131 ? 8.884   13.204  12.290  1.000 54.857  0 131 ARG AAA N     1 ? 1 
ATOM   824   C CA    . ARG A 1 131 ? 7.929   14.114  11.581  1.000 59.890  0 131 ARG AAA CA    1 ? 1 
ATOM   825   C C     . ARG A 1 131 ? 7.679   13.562  10.171  1.000 56.318  0 131 ARG AAA C     1 ? 1 
ATOM   826   O O     . ARG A 1 131 ? 6.492   13.420  9.789   1.000 53.522  0 131 ARG AAA O     1 ? 1 
ATOM   827   C CB    . ARG A 1 131 ? 8.443   15.548  11.440  1.000 62.993  0 131 ARG AAA CB    1 ? 1 
ATOM   828   C CG    . ARG A 1 131 ? 7.884   16.528  12.460  1.000 67.309  0 131 ARG AAA CG    1 ? 1 
ATOM   829   C CD    . ARG A 1 131 ? 8.602   17.867  12.451  1.000 73.482  0 131 ARG AAA CD    1 ? 1 
ATOM   830   N NE    . ARG A 1 131 ? 8.581   18.509  11.135  1.000 81.109  0 131 ARG AAA NE    1 ? 1 
ATOM   831   C CZ    . ARG A 1 131 ? 9.441   19.430  10.719  1.000 82.144  0 131 ARG AAA CZ    1 ? 1 
ATOM   832   N NH1   . ARG A 1 131 ? 10.401  19.866  11.519  1.000 82.113  0 131 ARG AAA NH1   1 ? 1 
ATOM   833   N NH2   . ARG A 1 131 ? 9.339   19.908  9.492   1.000 82.956  0 131 ARG AAA NH2   1 ? 1 
ATOM   834   N N     . THR A 1 132 ? 8.767   13.268  9.445   1.000 53.447  0 132 THR AAA N     1 ? 1 
ATOM   835   C CA    . THR A 1 132 ? 8.739   12.751  8.055   1.000 55.274  0 132 THR AAA CA    1 ? 1 
ATOM   836   C C     . THR A 1 132 ? 8.025   11.390  8.040   1.000 55.785  0 132 THR AAA C     1 ? 1 
ATOM   837   O O     . THR A 1 132 ? 7.156   11.184  7.154   1.000 55.313  0 132 THR AAA O     1 ? 1 
ATOM   838   C CB    . THR A 1 132 ? 10.156  12.680  7.471   1.000 55.959  0 132 THR AAA CB    1 ? 1 
ATOM   839   O OG1   . THR A 1 132 ? 10.655  14.013  7.427   1.000 56.929  0 132 THR AAA OG1   1 ? 1 
ATOM   840   C CG2   . THR A 1 132 ? 10.219  12.056  6.092   1.000 58.856  0 132 THR AAA CG2   1 ? 1 
ATOM   841   N N     . GLY A 1 133 ? 8.396   10.501  8.975   1.000 54.372  0 133 GLY AAA N     1 ? 1 
ATOM   842   C CA    . GLY A 1 133 ? 7.890   9.119   9.065   1.000 53.361  0 133 GLY AAA CA    1 ? 1 
ATOM   843   C C     . GLY A 1 133 ? 6.381   9.113   9.199   1.000 53.552  0 133 GLY AAA C     1 ? 1 
ATOM   844   O O     . GLY A 1 133 ? 5.739   8.202   8.639   1.000 56.777  0 133 GLY AAA O     1 ? 1 
ATOM   845   N N     . LEU A 1 134 ? 5.834   10.094  9.921   1.000 50.932  0 134 LEU AAA N     1 ? 1 
ATOM   846   C CA    . LEU A 1 134 ? 4.370   10.266  10.117  1.000 50.319  0 134 LEU AAA CA    1 ? 1 
ATOM   847   C C     . LEU A 1 134 ? 3.744   10.770  8.811   1.000 51.268  0 134 LEU AAA C     1 ? 1 
ATOM   848   O O     . LEU A 1 134 ? 2.762   10.161  8.372   1.000 53.438  0 134 LEU AAA O     1 ? 1 
ATOM   849   C CB    . LEU A 1 134 ? 4.105   11.238  11.270  1.000 49.166  0 134 LEU AAA CB    1 ? 1 
ATOM   850   C CG    . LEU A 1 134 ? 4.286   10.671  12.681  1.000 49.249  0 134 LEU AAA CG    1 ? 1 
ATOM   851   C CD1   . LEU A 1 134 ? 3.880   11.698  13.716  1.000 48.764  0 134 LEU AAA CD1   1 ? 1 
ATOM   852   C CD2   . LEU A 1 134 ? 3.520   9.369   12.890  1.000 47.814  0 134 LEU AAA CD2   1 ? 1 
ATOM   853   N N     . ARG A 1 135 ? 4.281   11.830  8.214   1.000 52.315  0 135 ARG AAA N     1 ? 1 
ATOM   854   C CA    . ARG A 1 135 ? 3.724   12.403  6.956   1.000 56.107  0 135 ARG AAA CA    1 ? 1 
ATOM   855   C C     . ARG A 1 135 ? 3.759   11.331  5.848   1.000 51.608  0 135 ARG AAA C     1 ? 1 
ATOM   856   O O     . ARG A 1 135 ? 2.707   11.074  5.245   1.000 48.014  0 135 ARG AAA O     1 ? 1 
ATOM   857   C CB    . ARG A 1 135 ? 4.458   13.692  6.574   1.000 61.537  0 135 ARG AAA CB    1 ? 1 
ATOM   858   C CG    . ARG A 1 135 ? 3.663   14.630  5.670   1.000 66.052  0 135 ARG AAA CG    1 ? 1 
ATOM   859   C CD    . ARG A 1 135 ? 4.354   15.981  5.454   1.000 69.070  0 135 ARG AAA CD    1 ? 1 
ATOM   860   N NE    . ARG A 1 135 ? 5.641   15.806  4.787   1.000 69.623  0 135 ARG AAA NE    1 ? 1 
ATOM   861   C CZ    . ARG A 1 135 ? 6.846   15.844  5.375   1.000 73.192  0 135 ARG AAA CZ    1 ? 1 
ATOM   862   N NH1   . ARG A 1 135 ? 6.966   16.064  6.682   1.000 70.382  0 135 ARG AAA NH1   1 ? 1 
ATOM   863   N NH2   . ARG A 1 135 ? 7.932   15.632  4.639   1.000 73.854  0 135 ARG AAA NH2   1 ? 1 
ATOM   864   N N     . VAL A 1 136 ? 4.916   10.700  5.622   1.000 50.690  0 136 VAL AAA N     1 ? 1 
ATOM   865   C CA    . VAL A 1 136 ? 5.100   9.575   4.655   1.000 49.915  0 136 VAL AAA CA    1 ? 1 
ATOM   866   C C     . VAL A 1 136 ? 4.108   8.458   4.999   1.000 47.934  0 136 VAL AAA C     1 ? 1 
ATOM   867   O O     . VAL A 1 136 ? 3.528   7.908   4.083   1.000 49.481  0 136 VAL AAA O     1 ? 1 
ATOM   868   C CB    . VAL A 1 136 ? 6.574   9.098   4.622   1.000 51.241  0 136 VAL AAA CB    1 ? 1 
ATOM   869   C CG1   . VAL A 1 136 ? 6.755   7.679   4.078   1.000 50.018  0 136 VAL AAA CG1   1 ? 1 
ATOM   870   C CG2   . VAL A 1 136 ? 7.460   10.083  3.847   1.000 50.029  0 136 VAL AAA CG2   1 ? 1 
ATOM   871   N N     . GLY A 1 137 ? 3.907   8.156   6.280   1.000 49.127  0 137 GLY AAA N     1 ? 1 
ATOM   872   C CA    . GLY A 1 137 ? 3.027   7.068   6.759   1.000 48.587  0 137 GLY AAA CA    1 ? 1 
ATOM   873   C C     . GLY A 1 137 ? 1.546   7.448   6.790   1.000 49.618  0 137 GLY AAA C     1 ? 1 
ATOM   874   O O     . GLY A 1 137 ? 0.766   6.635   7.328   1.000 50.908  0 137 GLY AAA O     1 ? 1 
ATOM   875   N N     . ASN A 1 138 ? 1.179   8.634   6.293   1.000 49.519  0 138 ASN AAA N     1 ? 1 
ATOM   876   C CA    . ASN A 1 138 ? -0.228  9.113   6.137   1.000 52.851  0 138 ASN AAA CA    1 ? 1 
ATOM   877   C C     . ASN A 1 138 ? -0.880  9.316   7.525   1.000 51.245  0 138 ASN AAA C     1 ? 1 
ATOM   878   O O     . ASN A 1 138 ? -2.074  8.986   7.716   1.000 52.034  0 138 ASN AAA O     1 ? 1 
ATOM   879   C CB    . ASN A 1 138 ? -1.045  8.172   5.243   1.000 55.304  0 138 ASN AAA CB    1 ? 1 
ATOM   880   C CG    . ASN A 1 138 ? -2.436  8.696   4.932   1.000 58.744  0 138 ASN AAA CG    1 ? 1 
ATOM   881   O OD1   . ASN A 1 138 ? -2.634  9.896   4.718   1.000 61.140  0 138 ASN AAA OD1   1 ? 1 
ATOM   882   N ND2   . ASN A 1 138 ? -3.429  7.817   4.955   1.000 60.659  0 138 ASN AAA ND2   1 ? 1 
ATOM   883   N N     . VAL A 1 139 ? -0.128  9.857   8.471   1.000 48.478  0 139 VAL AAA N     1 ? 1 
ATOM   884   C CA    . VAL A 1 139 ? -0.632  10.279  9.806   1.000 46.520  0 139 VAL AAA CA    1 ? 1 
ATOM   885   C C     . VAL A 1 139 ? -0.625  11.800  9.827   1.000 46.000  0 139 VAL AAA C     1 ? 1 
ATOM   886   O O     . VAL A 1 139 ? 0.443   12.371  9.478   1.000 46.689  0 139 VAL AAA O     1 ? 1 
ATOM   887   C CB    . VAL A 1 139 ? 0.228   9.703   10.948  1.000 45.963  0 139 VAL AAA CB    1 ? 1 
ATOM   888   C CG1   . VAL A 1 139 ? -0.262  10.192  12.313  1.000 46.513  0 139 VAL AAA CG1   1 ? 1 
ATOM   889   C CG2   . VAL A 1 139 ? 0.283   8.169   10.897  1.000 45.757  0 139 VAL AAA CG2   1 ? 1 
ATOM   890   N N     . GLU A 1 140 ? -1.755  12.416  10.203  1.000 45.146  0 140 GLU AAA N     1 ? 1 
ATOM   891   C CA    . GLU A 1 140 ? -1.862  13.881  10.419  1.000 48.234  0 140 GLU AAA CA    1 ? 1 
ATOM   892   C C     . GLU A 1 140 ? -1.315  14.219  11.813  1.000 46.453  0 140 GLU AAA C     1 ? 1 
ATOM   893   O O     . GLU A 1 140 ? -2.018  13.967  12.825  1.000 47.087  0 140 GLU AAA O     1 ? 1 
ATOM   894   C CB    . GLU A 1 140 ? -3.304  14.363  10.250  1.000 53.178  0 140 GLU AAA CB    1 ? 1 
ATOM   895   C CG    . GLU A 1 140 ? -3.432  15.876  10.160  1.000 56.890  0 140 GLU AAA CG    1 ? 1 
ATOM   896   C CD    . GLU A 1 140 ? -4.857  16.427  10.121  1.000 61.977  0 140 GLU AAA CD    1 ? 1 
ATOM   897   O OE1   . GLU A 1 140 ? -5.838  15.628  9.930   1.000 62.659  0 140 GLU AAA OE1   1 ? 1 
ATOM   898   O OE2   . GLU A 1 140 ? -5.006  17.672  10.303  1.000 61.764  0 140 GLU AAA OE2   1 ? 1 
ATOM   899   N N     . TYR A 1 141 ? -0.110  14.793  11.841  1.000 44.737  0 141 TYR AAA N     1 ? 1 
ATOM   900   C CA    . TYR A 1 141 ? 0.604   15.261  13.050  1.000 45.389  0 141 TYR AAA CA    1 ? 1 
ATOM   901   C C     . TYR A 1 141 ? 0.138   16.683  13.366  1.000 44.916  0 141 TYR AAA C     1 ? 1 
ATOM   902   O O     . TYR A 1 141 ? 0.231   17.518  12.481  1.000 43.022  0 141 TYR AAA O     1 ? 1 
ATOM   903   C CB    . TYR A 1 141 ? 2.125   15.218  12.844  1.000 43.476  0 141 TYR AAA CB    1 ? 1 
ATOM   904   C CG    . TYR A 1 141 ? 2.931   15.928  13.906  1.000 43.134  0 141 TYR AAA CG    1 ? 1 
ATOM   905   C CD1   . TYR A 1 141 ? 2.689   15.700  15.252  1.000 42.920  0 141 TYR AAA CD1   1 ? 1 
ATOM   906   C CD2   . TYR A 1 141 ? 3.944   16.815  13.578  1.000 43.944  0 141 TYR AAA CD2   1 ? 1 
ATOM   907   C CE1   . TYR A 1 141 ? 3.423   16.325  16.246  1.000 42.288  0 141 TYR AAA CE1   1 ? 1 
ATOM   908   C CE2   . TYR A 1 141 ? 4.685   17.455  14.556  1.000 43.004  0 141 TYR AAA CE2   1 ? 1 
ATOM   909   C CZ    . TYR A 1 141 ? 4.445   17.190  15.892  1.000 42.854  0 141 TYR AAA CZ    1 ? 1 
ATOM   910   O OH    . TYR A 1 141 ? 5.171   17.835  16.853  1.000 41.195  0 141 TYR AAA OH    1 ? 1 
ATOM   911   N N     . ILE A 1 142 ? -0.277  16.946  14.607  1.000 45.833  0 142 ILE AAA N     1 ? 1 
ATOM   912   C CA    . ILE A 1 142 ? -0.656  18.303  15.102  1.000 48.129  0 142 ILE AAA CA    1 ? 1 
ATOM   913   C C     . ILE A 1 142 ? 0.123   18.577  16.392  1.000 49.269  0 142 ILE AAA C     1 ? 1 
ATOM   914   O O     . ILE A 1 142 ? -0.076  17.813  17.388  1.000 46.327  0 142 ILE AAA O     1 ? 1 
ATOM   915   C CB    . ILE A 1 142 ? -2.180  18.360  15.337  1.000 50.034  0 142 ILE AAA CB    1 ? 1 
ATOM   916   C CG1   . ILE A 1 142 ? -2.953  18.098  14.043  1.000 51.420  0 142 ILE AAA CG1   1 ? 1 
ATOM   917   C CG2   . ILE A 1 142 ? -2.591  19.669  15.981  1.000 49.130  0 142 ILE AAA CG2   1 ? 1 
ATOM   918   C CD1   . ILE A 1 142 ? -4.413  17.808  14.241  1.000 53.312  0 142 ILE AAA CD1   1 ? 1 
ATOM   919   N N     . ASN A 1 143 ? 0.956   19.621  16.395  1.000 51.220  0 143 ASN AAA N     1 ? 1 
ATOM   920   C CA    . ASN A 1 143 ? 1.800   20.030  17.551  1.000 49.376  0 143 ASN AAA CA    1 ? 1 
ATOM   921   C C     . ASN A 1 143 ? 0.929   20.900  18.457  1.000 49.404  0 143 ASN AAA C     1 ? 1 
ATOM   922   O O     . ASN A 1 143 ? 1.136   22.118  18.453  1.000 49.013  0 143 ASN AAA O     1 ? 1 
ATOM   923   C CB    . ASN A 1 143 ? 3.099   20.713  17.088  1.000 49.675  0 143 ASN AAA CB    1 ? 1 
ATOM   924   C CG    . ASN A 1 143 ? 4.132   20.977  18.182  1.000 50.917  0 143 ASN AAA CG    1 ? 1 
ATOM   925   O OD1   . ASN A 1 143 ? 4.148   20.351  19.242  1.000 49.700  0 143 ASN AAA OD1   1 ? 1 
ATOM   926   N ND2   . ASN A 1 143 ? 5.048   21.904  17.948  1.000 49.610  0 143 ASN AAA ND2   1 ? 1 
ATOM   927   N N     . ALA A 1 144 ? -0.022  20.297  19.181  1.000 50.671  0 144 ALA AAA N     1 ? 1 
ATOM   928   C CA    . ALA A 1 144 ? -0.881  20.974  20.195  1.000 49.851  0 144 ALA AAA CA    1 ? 1 
ATOM   929   C C     . ALA A 1 144 ? -1.290  20.010  21.314  1.000 47.597  0 144 ALA AAA C     1 ? 1 
ATOM   930   O O     . ALA A 1 144 ? -1.309  18.799  21.087  1.000 51.083  0 144 ALA AAA O     1 ? 1 
ATOM   931   C CB    . ALA A 1 144 ? -2.106  21.565  19.546  1.000 50.642  0 144 ALA AAA CB    1 ? 1 
ATOM   932   N N     . LEU A 1 145 ? -1.598  20.545  22.488  1.000 45.372  0 145 LEU AAA N     1 ? 1 
ATOM   933   C CA    . LEU A 1 145 ? -2.232  19.785  23.593  1.000 46.826  0 145 LEU AAA CA    1 ? 1 
ATOM   934   C C     . LEU A 1 145 ? -3.693  19.489  23.254  1.000 47.908  0 145 LEU AAA C     1 ? 1 
ATOM   935   O O     . LEU A 1 145 ? -4.436  20.432  22.908  1.000 49.474  0 145 LEU AAA O     1 ? 1 
ATOM   936   C CB    . LEU A 1 145 ? -2.165  20.582  24.905  1.000 46.374  0 145 LEU AAA CB    1 ? 1 
ATOM   937   C CG    . LEU A 1 145 ? -0.798  20.620  25.570  1.000 44.022  0 145 LEU AAA CG    1 ? 1 
ATOM   938   C CD1   . LEU A 1 145 ? -0.837  21.522  26.784  1.000 45.317  0 145 LEU AAA CD1   1 ? 1 
ATOM   939   C CD2   . LEU A 1 145 ? -0.319  19.217  25.933  1.000 42.530  0 145 LEU AAA CD2   1 ? 1 
ATOM   940   N N     . ALA A 1 146 ? -4.083  18.225  23.406  1.000 46.914  0 146 ALA AAA N     1 ? 1 
ATOM   941   C CA    . ALA A 1 146 ? -5.448  17.716  23.156  1.000 47.544  0 146 ALA AAA CA    1 ? 1 
ATOM   942   C C     . ALA A 1 146 ? -6.089  17.377  24.501  1.000 47.040  0 146 ALA AAA C     1 ? 1 
ATOM   943   O O     . ALA A 1 146 ? -5.344  17.060  25.403  1.000 45.149  0 146 ALA AAA O     1 ? 1 
ATOM   944   C CB    . ALA A 1 146 ? -5.379  16.517  22.237  1.000 48.277  0 146 ALA AAA CB    1 ? 1 
ATOM   945   N N     . LYS A 1 147 ? -7.413  17.489  24.626  1.000 50.921  0 147 LYS AAA N     1 ? 1 
ATOM   946   C CA    . LYS A 1 147 ? -8.187  16.974  25.788  1.000 53.405  0 147 LYS AAA CA    1 ? 1 
ATOM   947   C C     . LYS A 1 147 ? -9.480  16.276  25.315  1.000 50.384  0 147 LYS AAA C     1 ? 1 
ATOM   948   O O     . LYS A 1 147 ? -9.917  16.495  24.172  1.000 48.904  0 147 LYS AAA O     1 ? 1 
ATOM   949   C CB    . LYS A 1 147 ? -8.429  18.098  26.797  1.000 57.076  0 147 LYS AAA CB    1 ? 1 
ATOM   950   C CG    . LYS A 1 147 ? -9.322  19.231  26.334  1.000 61.499  0 147 LYS AAA CG    1 ? 1 
ATOM   951   C CD    . LYS A 1 147 ? -9.956  20.007  27.481  1.000 64.263  0 147 LYS AAA CD    1 ? 1 
ATOM   952   C CE    . LYS A 1 147 ? -9.168  21.236  27.881  1.000 67.743  0 147 LYS AAA CE    1 ? 1 
ATOM   953   N NZ    . LYS A 1 147 ? -10.000 22.137  28.713  1.000 72.349  0 147 LYS AAA NZ    1 ? 1 
ATOM   954   N N     . LEU A 1 148 ? -10.037 15.394  26.145  1.000 47.160  0 148 LEU AAA N     1 ? 1 
ATOM   955   C CA    . LEU A 1 148 ? -11.291 14.649  25.827  1.000 48.165  0 148 LEU AAA CA    1 ? 1 
ATOM   956   C C     . LEU A 1 148 ? -12.500 15.546  26.072  1.000 45.742  0 148 LEU AAA C     1 ? 1 
ATOM   957   O O     . LEU A 1 148 ? -12.512 16.239  27.082  1.000 45.508  0 148 LEU AAA O     1 ? 1 
ATOM   958   C CB    . LEU A 1 148 ? -11.341 13.378  26.688  1.000 48.479  0 148 LEU AAA CB    1 ? 1 
ATOM   959   C CG    . LEU A 1 148 ? -10.200 12.380  26.456  1.000 48.213  0 148 LEU AAA CG    1 ? 1 
ATOM   960   C CD1   . LEU A 1 148 ? -10.265 11.263  27.468  1.000 47.839  0 148 LEU AAA CD1   1 ? 1 
ATOM   961   C CD2   . LEU A 1 148 ? -10.253 11.805  25.045  1.000 47.728  0 148 LEU AAA CD2   1 ? 1 
ATOM   962   N N     . ILE A 1 149 ? -13.440 15.576  25.136  1.000 51.048  0 149 ILE AAA N     1 ? 1 
ATOM   963   C CA    . ILE A 1 149 ? -14.748 16.297  25.261  1.000 51.461  0 149 ILE AAA CA    1 ? 1 
ATOM   964   C C     . ILE A 1 149 ? -15.825 15.257  25.573  1.000 51.995  0 149 ILE AAA C     1 ? 1 
ATOM   965   O O     . ILE A 1 149 ? -16.606 15.531  26.485  1.000 53.565  0 149 ILE AAA O     1 ? 1 
ATOM   966   C CB    . ILE A 1 149 ? -15.052 17.127  23.997  1.000 54.388  0 149 ILE AAA CB    1 ? 1 
ATOM   967   C CG1   . ILE A 1 149 ? -14.135 18.357  23.905  1.000 54.906  0 149 ILE AAA CG1   1 ? 1 
ATOM   968   C CG2   . ILE A 1 149 ? -16.528 17.514  23.906  1.000 54.875  0 149 ILE AAA CG2   1 ? 1 
ATOM   969   C CD1   . ILE A 1 149 ? -14.262 19.335  25.065  1.000 53.874  0 149 ILE AAA CD1   1 ? 1 
ATOM   970   N N     . ASP A 1 150 ? -15.809 14.100  24.897  1.000 51.770  0 150 ASP AAA N     1 ? 1 
ATOM   971   C CA    . ASP A 1 150 ? -16.710 12.943  25.161  1.000 52.901  0 150 ASP AAA CA    1 ? 1 
ATOM   972   C C     . ASP A 1 150 ? -16.106 11.661  24.572  1.000 50.347  0 150 ASP AAA C     1 ? 1 
ATOM   973   O O     . ASP A 1 150 ? -15.048 11.693  23.964  1.000 46.926  0 150 ASP AAA O     1 ? 1 
ATOM   974   C CB    . ASP A 1 150 ? -18.122 13.284  24.665  1.000 54.379  0 150 ASP AAA CB    1 ? 1 
ATOM   975   C CG    . ASP A 1 150 ? -18.297 13.353  23.157  1.000 55.771  0 150 ASP AAA CG    1 ? 1 
ATOM   976   O OD1   . ASP A 1 150 ? -17.647 12.564  22.432  1.000 57.283  0 150 ASP AAA OD1   1 ? 1 
ATOM   977   O OD2   . ASP A 1 150 ? -19.110 14.184  22.715  1.000 60.496  0 150 ASP AAA OD2   1 ? 1 
ATOM   978   N N     . PRO A 1 151 ? -16.751 10.481  24.714  1.000 50.288  0 151 PRO AAA N     1 ? 1 
ATOM   979   C CA    . PRO A 1 151 ? -16.196 9.230   24.191  1.000 50.270  0 151 PRO AAA CA    1 ? 1 
ATOM   980   C C     . PRO A 1 151 ? -15.728 9.207   22.731  1.000 47.982  0 151 PRO AAA C     1 ? 1 
ATOM   981   O O     . PRO A 1 151 ? -15.084 8.251   22.382  1.000 47.982  0 151 PRO AAA O     1 ? 1 
ATOM   982   C CB    . PRO A 1 151 ? -17.377 8.244   24.305  1.000 50.945  0 151 PRO AAA CB    1 ? 1 
ATOM   983   C CG    . PRO A 1 151 ? -18.140 8.756   25.514  1.000 50.218  0 151 PRO AAA CG    1 ? 1 
ATOM   984   C CD    . PRO A 1 151 ? -18.050 10.266  25.377  1.000 50.046  0 151 PRO AAA CD    1 ? 1 
ATOM   985   N N     . HIS A 1 152 ? -16.058 10.208  21.912  1.000 48.747  0 152 HIS AAA N     1 ? 1 
ATOM   986   C CA    . HIS A 1 152 ? -15.695 10.235  20.463  1.000 49.619  0 152 HIS AAA CA    1 ? 1 
ATOM   987   C C     . HIS A 1 152 ? -15.126 11.589  20.027  1.000 49.960  0 152 HIS AAA C     1 ? 1 
ATOM   988   O O     . HIS A 1 152 ? -14.989 11.764  18.793  1.000 50.248  0 152 HIS AAA O     1 ? 1 
ATOM   989   C CB    . HIS A 1 152 ? -16.899 9.870   19.573  1.000 49.317  0 152 HIS AAA CB    1 ? 1 
ATOM   990   C CG    . HIS A 1 152 ? -17.327 8.456   19.722  1.000 51.060  0 152 HIS AAA CG    1 ? 1 
ATOM   991   N ND1   . HIS A 1 152 ? -16.568 7.408   19.249  1.000 50.359  0 152 HIS AAA ND1   1 ? 1 
ATOM   992   C CD2   . HIS A 1 152 ? -18.406 7.906   20.322  1.000 54.759  0 152 HIS AAA CD2   1 ? 1 
ATOM   993   C CE1   . HIS A 1 152 ? -17.168 6.266   19.531  1.000 52.722  0 152 HIS AAA CE1   1 ? 1 
ATOM   994   N NE2   . HIS A 1 152 ? -18.287 6.539   20.203  1.000 54.909  0 152 HIS AAA NE2   1 ? 1 
ATOM   995   N N     . SER A 1 153 ? -14.814 12.509  20.949  1.000 48.059  0 153 SER AAA N     1 ? 1 
ATOM   996   C CA    . SER A 1 153 ? -14.445 13.904  20.588  1.000 48.757  0 153 SER AAA CA    1 ? 1 
ATOM   997   C C     . SER A 1 153 ? -13.241 14.380  21.396  1.000 46.387  0 153 SER AAA C     1 ? 1 
ATOM   998   O O     . SER A 1 153 ? -13.232 14.140  22.619  1.000 44.202  0 153 SER AAA O     1 ? 1 
ATOM   999   C CB    . SER A 1 153 ? -15.609 14.838  20.771  1.000 47.167  0 153 SER AAA CB    1 ? 1 
ATOM   1000  O OG    . SER A 1 153 ? -16.749 14.264  20.193  1.000 51.752  0 153 SER AAA OG    1 ? 1 
ATOM   1001  N N     . VAL A 1 154 ? -12.317 15.087  20.735  1.000 45.765  0 154 VAL AAA N     1 ? 1 
ATOM   1002  C CA    . VAL A 1 154 ? -11.089 15.655  21.366  1.000 49.039  0 154 VAL AAA CA    1 ? 1 
ATOM   1003  C C     . VAL A 1 154 ? -10.982 17.124  20.950  1.000 50.532  0 154 VAL AAA C     1 ? 1 
ATOM   1004  O O     . VAL A 1 154 ? -11.381 17.421  19.817  1.000 53.940  0 154 VAL AAA O     1 ? 1 
ATOM   1005  C CB    . VAL A 1 154 ? -9.840  14.830  20.981  1.000 46.719  0 154 VAL AAA CB    1 ? 1 
ATOM   1006  C CG1   . VAL A 1 154 ? -9.433  15.085  19.569  1.000 49.186  0 154 VAL AAA CG1   1 ? 1 
ATOM   1007  C CG2   . VAL A 1 154 ? -8.659  15.096  21.869  1.000 48.303  0 154 VAL AAA CG2   1 ? 1 
ATOM   1008  N N     . GLU A 1 155 ? -10.470 17.993  21.831  1.000 52.309  0 155 GLU AAA N     1 ? 1 
ATOM   1009  C CA    . GLU A 1 155 ? -10.356 19.465  21.633  1.000 55.396  0 155 GLU AAA CA    1 ? 1 
ATOM   1010  C C     . GLU A 1 155 ? -8.889  19.883  21.656  1.000 54.018  0 155 GLU AAA C     1 ? 1 
ATOM   1011  O O     . GLU A 1 155 ? -8.188  19.436  22.558  1.000 55.150  0 155 GLU AAA O     1 ? 1 
ATOM   1012  C CB    . GLU A 1 155 ? -11.098 20.202  22.753  1.000 59.979  0 155 GLU AAA CB    1 ? 1 
ATOM   1013  C CG    . GLU A 1 155 ? -11.184 21.706  22.568  1.000 62.130  0 155 GLU AAA CG    1 ? 1 
ATOM   1014  C CD    . GLU A 1 155 ? -12.006 22.427  23.633  1.000 62.757  0 155 GLU AAA CD    1 ? 1 
ATOM   1015  O OE1   . GLU A 1 155 ? -11.807 22.129  24.839  1.000 57.570  0 155 GLU AAA OE1   1 ? 1 
ATOM   1016  O OE2   . GLU A 1 155 ? -12.851 23.288  23.248  1.000 63.149  0 155 GLU AAA OE2   1 ? 1 
ATOM   1017  N N     . TYR A 1 156 ? -8.462  20.761  20.747  1.000 53.653  0 156 TYR AAA N     1 ? 1 
ATOM   1018  C CA    . TYR A 1 156 ? -7.115  21.397  20.752  1.000 56.756  0 156 TYR AAA CA    1 ? 1 
ATOM   1019  C C     . TYR A 1 156 ? -7.203  22.856  20.278  1.000 63.269  0 156 TYR AAA C     1 ? 1 
ATOM   1020  O O     . TYR A 1 156 ? -8.108  23.195  19.486  1.000 64.662  0 156 TYR AAA O     1 ? 1 
ATOM   1021  C CB    . TYR A 1 156 ? -6.130  20.602  19.887  1.000 54.010  0 156 TYR AAA CB    1 ? 1 
ATOM   1022  C CG    . TYR A 1 156 ? -6.423  20.646  18.406  1.000 52.320  0 156 TYR AAA CG    1 ? 1 
ATOM   1023  C CD1   . TYR A 1 156 ? -7.430  19.865  17.849  1.000 51.690  0 156 TYR AAA CD1   1 ? 1 
ATOM   1024  C CD2   . TYR A 1 156 ? -5.692  21.470  17.568  1.000 50.081  0 156 TYR AAA CD2   1 ? 1 
ATOM   1025  C CE1   . TYR A 1 156 ? -7.731  19.937  16.501  1.000 52.741  0 156 TYR AAA CE1   1 ? 1 
ATOM   1026  C CE2   . TYR A 1 156 ? -5.944  21.506  16.210  1.000 50.952  0 156 TYR AAA CE2   1 ? 1 
ATOM   1027  C CZ    . TYR A 1 156 ? -6.981  20.760  15.677  1.000 52.231  0 156 TYR AAA CZ    1 ? 1 
ATOM   1028  O OH    . TYR A 1 156 ? -7.226  20.817  14.337  1.000 51.973  0 156 TYR AAA OH    1 ? 1 
ATOM   1029  N N     . GLU A 1 157 ? -6.266  23.699  20.729  1.000 69.278  0 157 GLU AAA N     1 ? 1 
ATOM   1030  C CA    . GLU A 1 157 ? -6.117  25.096  20.242  1.000 72.730  0 157 GLU AAA CA    1 ? 1 
ATOM   1031  C C     . GLU A 1 157 ? -5.255  25.095  18.976  1.000 78.443  0 157 GLU AAA C     1 ? 1 
ATOM   1032  O O     . GLU A 1 157 ? -4.369  24.218  18.836  1.000 79.860  0 157 GLU AAA O     1 ? 1 
ATOM   1033  C CB    . GLU A 1 157 ? -5.602  26.026  21.335  1.000 77.722  0 157 GLU AAA CB    1 ? 1 
ATOM   1034  C CG    . GLU A 1 157 ? -4.095  26.184  21.382  1.000 82.514  0 157 GLU AAA CG    1 ? 1 
ATOM   1035  C CD    . GLU A 1 157 ? -3.611  26.883  22.644  1.000 87.583  0 157 GLU AAA CD    1 ? 1 
ATOM   1036  O OE1   . GLU A 1 157 ? -4.305  26.764  23.688  1.000 87.462  0 157 GLU AAA OE1   1 ? 1 
ATOM   1037  O OE2   . GLU A 1 157 ? -2.541  27.553  22.592  1.000 87.953  0 157 GLU AAA OE2   1 ? 1 
ATOM   1038  N N     . ASP A 1 158 ? -5.519  26.057  18.094  1.000 82.480  0 158 ASP AAA N     1 ? 1 
ATOM   1039  C CA    . ASP A 1 158 ? -4.892  26.207  16.754  1.000 85.295  0 158 ASP AAA CA    1 ? 1 
ATOM   1040  C C     . ASP A 1 158 ? -5.048  27.669  16.320  1.000 88.353  0 158 ASP AAA C     1 ? 1 
ATOM   1041  O O     . ASP A 1 158 ? -6.186  28.049  15.963  1.000 88.224  0 158 ASP AAA O     1 ? 1 
ATOM   1042  C CB    . ASP A 1 158 ? -5.532  25.225  15.769  1.000 83.929  0 158 ASP AAA CB    1 ? 1 
ATOM   1043  C CG    . ASP A 1 158 ? -5.086  25.405  14.333  1.000 85.529  0 158 ASP AAA CG    1 ? 1 
ATOM   1044  O OD1   . ASP A 1 158 ? -3.875  25.609  14.112  1.000 86.601  0 158 ASP AAA OD1   1 ? 1 
ATOM   1045  O OD2   . ASP A 1 158 ? -5.954  25.355  13.446  1.000 85.703  0 158 ASP AAA OD2   1 ? 1 
ATOM   1046  N N     . ASN A 1 159 ? -3.971  28.464  16.382  1.000 90.254  0 159 ASN AAA N     1 ? 1 
ATOM   1047  C CA    . ASN A 1 159 ? -4.021  29.947  16.246  1.000 95.194  0 159 ASN AAA CA    1 ? 1 
ATOM   1048  C C     . ASN A 1 159 ? -4.960  30.500  17.327  1.000 98.193  0 159 ASN AAA C     1 ? 1 
ATOM   1049  O O     . ASN A 1 159 ? -5.796  31.360  17.004  1.000 102.491 0 159 ASN AAA O     1 ? 1 
ATOM   1050  C CB    . ASN A 1 159 ? -4.434  30.389  14.833  1.000 95.499  0 159 ASN AAA CB    1 ? 1 
ATOM   1051  C CG    . ASN A 1 159 ? -3.372  30.112  13.787  1.000 98.097  0 159 ASN AAA CG    1 ? 1 
ATOM   1052  O OD1   . ASN A 1 159 ? -2.472  30.920  13.576  1.000 94.455  0 159 ASN AAA OD1   1 ? 1 
ATOM   1053  N ND2   . ASN A 1 159 ? -3.463  28.975  13.118  1.000 100.812 0 159 ASN AAA ND2   1 ? 1 
ATOM   1054  N N     . GLY A 1 160 ? -4.831  30.004  18.565  1.000 103.410 0 160 GLY AAA N     1 ? 1 
ATOM   1055  C CA    . GLY A 1 160 ? -5.636  30.434  19.729  1.000 101.383 0 160 GLY AAA CA    1 ? 1 
ATOM   1056  C C     . GLY A 1 160 ? -7.129  30.273  19.491  1.000 99.787  0 160 GLY AAA C     1 ? 1 
ATOM   1057  O O     . GLY A 1 160 ? -7.891  31.120  19.982  1.000 94.866  0 160 GLY AAA O     1 ? 1 
ATOM   1058  N N     . GLN A 1 161 ? -7.532  29.236  18.752  1.000 100.953 0 161 GLN AAA N     1 ? 1 
ATOM   1059  C CA    . GLN A 1 161 ? -8.949  28.919  18.444  1.000 100.104 0 161 GLN AAA CA    1 ? 1 
ATOM   1060  C C     . GLN A 1 161 ? -9.198  27.433  18.708  1.000 97.666  0 161 GLN AAA C     1 ? 1 
ATOM   1061  O O     . GLN A 1 161 ? -8.774  26.600  17.874  1.000 97.241  0 161 GLN AAA O     1 ? 1 
ATOM   1062  C CB    . GLN A 1 161 ? -9.276  29.294  17.000  1.000 101.739 0 161 GLN AAA CB    1 ? 1 
ATOM   1063  C CG    . GLN A 1 161 ? -9.340  30.798  16.781  1.000 105.105 0 161 GLN AAA CG    1 ? 1 
ATOM   1064  C CD    . GLN A 1 161 ? -10.140 31.161  15.556  1.000 110.030 0 161 GLN AAA CD    1 ? 1 
ATOM   1065  O OE1   . GLN A 1 161 ? -10.287 30.364  14.629  1.000 108.378 0 161 GLN AAA OE1   1 ? 1 
ATOM   1066  N NE2   . GLN A 1 161 ? -10.656 32.383  15.534  1.000 112.319 0 161 GLN AAA NE2   1 ? 1 
ATOM   1067  N N     . LYS A 1 162 ? -9.849  27.120  19.831  1.000 94.257  0 162 LYS AAA N     1 ? 1 
ATOM   1068  C CA    . LYS A 1 162 ? -10.366 25.763  20.150  1.000 90.030  0 162 LYS AAA CA    1 ? 1 
ATOM   1069  C C     . LYS A 1 162 ? -10.984 25.123  18.903  1.000 81.675  0 162 LYS AAA C     1 ? 1 
ATOM   1070  O O     . LYS A 1 162 ? -11.801 25.769  18.256  1.000 80.470  0 162 LYS AAA O     1 ? 1 
ATOM   1071  C CB    . LYS A 1 162 ? -11.414 25.831  21.258  1.000 94.134  0 162 LYS AAA CB    1 ? 1 
ATOM   1072  C CG    . LYS A 1 162 ? -10.877 26.307  22.599  1.000 97.912  0 162 LYS AAA CG    1 ? 1 
ATOM   1073  C CD    . LYS A 1 162 ? -9.752  25.461  23.153  1.000 95.992  0 162 LYS AAA CD    1 ? 1 
ATOM   1074  C CE    . LYS A 1 162 ? -9.663  25.497  24.669  1.000 91.888  0 162 LYS AAA CE    1 ? 1 
ATOM   1075  N NZ    . LYS A 1 162 ? -9.045  24.270  25.222  1.000 91.115  0 162 LYS AAA NZ    1 ? 1 
ATOM   1076  N N     . LYS A 1 163 ? -10.569 23.898  18.593  1.000 74.694  0 163 LYS AAA N     1 ? 1 
ATOM   1077  C CA    . LYS A 1 163 ? -11.169 23.037  17.547  1.000 70.401  0 163 LYS AAA CA    1 ? 1 
ATOM   1078  C C     . LYS A 1 163 ? -11.518 21.687  18.167  1.000 63.480  0 163 LYS AAA C     1 ? 1 
ATOM   1079  O O     . LYS A 1 163 ? -10.868 21.298  19.125  1.000 61.466  0 163 LYS AAA O     1 ? 1 
ATOM   1080  C CB    . LYS A 1 163 ? -10.205 22.872  16.377  1.000 70.481  0 163 LYS AAA CB    1 ? 1 
ATOM   1081  C CG    . LYS A 1 163 ? -9.948  24.140  15.588  1.000 73.307  0 163 LYS AAA CG    1 ? 1 
ATOM   1082  C CD    . LYS A 1 163 ? -9.437  23.823  14.200  1.000 74.618  0 163 LYS AAA CD    1 ? 1 
ATOM   1083  C CE    . LYS A 1 163 ? -9.326  25.055  13.324  1.000 78.546  0 163 LYS AAA CE    1 ? 1 
ATOM   1084  N NZ    . LYS A 1 163 ? -9.081  24.686  11.912  1.000 77.893  0 163 LYS AAA NZ    1 ? 1 
ATOM   1085  N N     . THR A 1 164 ? -12.542 21.034  17.644  1.000 61.946  0 164 THR AAA N     1 ? 1 
ATOM   1086  C CA    . THR A 1 164 ? -13.048 19.722  18.105  1.000 62.917  0 164 THR AAA CA    1 ? 1 
ATOM   1087  C C     . THR A 1 164 ? -13.044 18.803  16.880  1.000 60.222  0 164 THR AAA C     1 ? 1 
ATOM   1088  O O     . THR A 1 164 ? -13.377 19.282  15.786  1.000 60.573  0 164 THR AAA O     1 ? 1 
ATOM   1089  C CB    . THR A 1 164 ? -14.418 19.864  18.788  1.000 67.466  0 164 THR AAA CB    1 ? 1 
ATOM   1090  O OG1   . THR A 1 164 ? -14.263 20.690  19.951  1.000 67.108  0 164 THR AAA OG1   1 ? 1 
ATOM   1091  C CG2   . THR A 1 164 ? -15.029 18.531  19.184  1.000 69.464  0 164 THR AAA CG2   1 ? 1 
ATOM   1092  N N     . ILE A 1 165 ? -12.593 17.562  17.048  1.000 55.284  0 165 ILE AAA N     1 ? 1 
ATOM   1093  C CA    . ILE A 1 165 ? -12.601 16.541  15.964  1.000 53.725  0 165 ILE AAA CA    1 ? 1 
ATOM   1094  C C     . ILE A 1 165 ? -13.128 15.226  16.544  1.000 50.185  0 165 ILE AAA C     1 ? 1 
ATOM   1095  O O     . ILE A 1 165 ? -12.953 14.987  17.776  1.000 47.168  0 165 ILE AAA O     1 ? 1 
ATOM   1096  C CB    . ILE A 1 165 ? -11.204 16.389  15.340  1.000 54.112  0 165 ILE AAA CB    1 ? 1 
ATOM   1097  C CG1   . ILE A 1 165 ? -10.188 15.839  16.346  1.000 52.593  0 165 ILE AAA CG1   1 ? 1 
ATOM   1098  C CG2   . ILE A 1 165 ? -10.734 17.702  14.726  1.000 55.009  0 165 ILE AAA CG2   1 ? 1 
ATOM   1099  C CD1   . ILE A 1 165 ? -8.968  15.276  15.682  1.000 54.420  0 165 ILE AAA CD1   1 ? 1 
ATOM   1100  N N     . THR A 1 166 ? -13.736 14.405  15.690  1.000 48.600  0 166 THR AAA N     1 ? 1 
ATOM   1101  C CA    . THR A 1 166 ? -14.502 13.210  16.116  1.000 48.486  0 166 THR AAA CA    1 ? 1 
ATOM   1102  C C     . THR A 1 166 ? -13.799 11.964  15.587  1.000 47.286  0 166 THR AAA C     1 ? 1 
ATOM   1103  O O     . THR A 1 166 ? -13.268 12.020  14.449  1.000 46.412  0 166 THR AAA O     1 ? 1 
ATOM   1104  C CB    . THR A 1 166 ? -15.962 13.296  15.671  1.000 48.790  0 166 THR AAA CB    1 ? 1 
ATOM   1105  O OG1   . THR A 1 166 ? -15.929 13.396  14.247  1.000 49.722  0 166 THR AAA OG1   1 ? 1 
ATOM   1106  C CG2   . THR A 1 166 ? -16.700 14.450  16.321  1.000 48.855  0 166 THR AAA CG2   1 ? 1 
ATOM   1107  N N     . SER A 1 167 ? -13.814 10.887  16.378  1.000 45.446  0 167 SER AAA N     1 ? 1 
ATOM   1108  C CA    . SER A 1 167 ? -13.138 9.612   16.023  1.000 45.348  0 167 SER AAA CA    1 ? 1 
ATOM   1109  C C     . SER A 1 167 ? -13.957 8.406   16.480  1.000 45.144  0 167 SER AAA C     1 ? 1 
ATOM   1110  O O     . SER A 1 167 ? -14.593 8.496   17.543  1.000 45.814  0 167 SER AAA O     1 ? 1 
ATOM   1111  C CB    . SER A 1 167 ? -11.741 9.584   16.597  1.000 44.809  0 167 SER AAA CB    1 ? 1 
ATOM   1112  O OG    . SER A 1 167 ? -10.900 8.787   15.783  1.000 44.569  0 167 SER AAA OG    1 ? 1 
ATOM   1113  N N     . ARG A 1 168 ? -13.914 7.322   15.706  1.000 48.487  0 168 ARG AAA N     1 ? 1 
ATOM   1114  C CA    . ARG A 1 168 ? -14.455 5.989   16.087  1.000 50.556  0 168 ARG AAA CA    1 ? 1 
ATOM   1115  C C     . ARG A 1 168 ? -13.756 5.580   17.385  1.000 45.549  0 168 ARG AAA C     1 ? 1 
ATOM   1116  O O     . ARG A 1 168 ? -14.443 5.228   18.361  1.000 43.913  0 168 ARG AAA O     1 ? 1 
ATOM   1117  C CB    . ARG A 1 168 ? -14.299 5.012   14.903  1.000 58.375  0 168 ARG AAA CB    1 ? 1 
ATOM   1118  C CG    . ARG A 1 168 ? -14.988 3.655   15.030  1.000 67.247  0 168 ARG AAA CG    1 ? 1 
ATOM   1119  C CD    . ARG A 1 168 ? -16.286 3.570   15.840  1.000 78.060  0 168 ARG AAA CD    1 ? 1 
ATOM   1120  N NE    . ARG A 1 168 ? -16.712 2.213   16.191  1.000 85.130  0 168 ARG AAA NE    1 ? 1 
ATOM   1121  C CZ    . ARG A 1 168 ? -17.378 1.863   17.308  1.000 83.970  0 168 ARG AAA CZ    1 ? 1 
ATOM   1122  N NH1   . ARG A 1 168 ? -17.718 2.761   18.221  1.000 81.459  0 168 ARG AAA NH1   1 ? 1 
ATOM   1123  N NH2   . ARG A 1 168 ? -17.721 0.600   17.505  1.000 84.408  0 168 ARG AAA NH2   1 ? 1 
ATOM   1124  N N     . TYR A 1 169 ? -12.430 5.714   17.411  1.000 45.534  0 169 TYR AAA N     1 ? 1 
ATOM   1125  C CA    . TYR A 1 169 ? -11.530 5.235   18.495  1.000 43.506  0 169 TYR AAA CA    1 ? 1 
ATOM   1126  C C     . TYR A 1 169 ? -10.616 6.382   18.939  1.000 42.710  0 169 TYR AAA C     1 ? 1 
ATOM   1127  O O     . TYR A 1 169 ? -10.175 7.189   18.108  1.000 42.695  0 169 TYR AAA O     1 ? 1 
ATOM   1128  C CB    . TYR A 1 169 ? -10.765 3.995   18.020  1.000 43.220  0 169 TYR AAA CB    1 ? 1 
ATOM   1129  C CG    . TYR A 1 169 ? -11.627 2.807   17.653  1.000 44.401  0 169 TYR AAA CG    1 ? 1 
ATOM   1130  C CD1   . TYR A 1 169 ? -12.470 2.217   18.586  1.000 46.030  0 169 TYR AAA CD1   1 ? 1 
ATOM   1131  C CD2   . TYR A 1 169 ? -11.606 2.261   16.375  1.000 45.638  0 169 TYR AAA CD2   1 ? 1 
ATOM   1132  C CE1   . TYR A 1 169 ? -13.269 1.129   18.265  1.000 46.900  0 169 TYR AAA CE1   1 ? 1 
ATOM   1133  C CE2   . TYR A 1 169 ? -12.385 1.165   16.035  1.000 46.188  0 169 TYR AAA CE2   1 ? 1 
ATOM   1134  C CZ    . TYR A 1 169 ? -13.218 0.596   16.987  1.000 47.071  0 169 TYR AAA CZ    1 ? 1 
ATOM   1135  O OH    . TYR A 1 169 ? -14.003 -0.468  16.677  1.000 46.919  0 169 TYR AAA OH    1 ? 1 
ATOM   1136  N N     . ILE A 1 170 ? -10.348 6.479   20.242  1.000 43.776  0 170 ILE AAA N     1 ? 1 
ATOM   1137  C CA    . ILE A 1 170 ? -9.337  7.428   20.797  1.000 43.569  0 170 ILE AAA CA    1 ? 1 
ATOM   1138  C C     . ILE A 1 170 ? -8.319  6.615   21.589  1.000 41.865  0 170 ILE AAA C     1 ? 1 
ATOM   1139  O O     . ILE A 1 170 ? -8.752  5.702   22.307  1.000 41.699  0 170 ILE AAA O     1 ? 1 
ATOM   1140  C CB    . ILE A 1 170 ? -9.986  8.529   21.648  1.000 43.530  0 170 ILE AAA CB    1 ? 1 
ATOM   1141  C CG1   . ILE A 1 170 ? -11.002 9.332   20.842  1.000 45.332  0 170 ILE AAA CG1   1 ? 1 
ATOM   1142  C CG2   . ILE A 1 170 ? -8.919  9.417   22.279  1.000 43.532  0 170 ILE AAA CG2   1 ? 1 
ATOM   1143  C CD1   . ILE A 1 170 ? -11.864 10.240  21.683  1.000 45.408  0 170 ILE AAA CD1   1 ? 1 
ATOM   1144  N N     . LEU A 1 171 ? -7.028  6.896   21.385  1.000 39.167  0 171 LEU AAA N     1 ? 1 
ATOM   1145  C CA    . LEU A 1 171 ? -5.921  6.242   22.121  1.000 38.038  0 171 LEU AAA CA    1 ? 1 
ATOM   1146  C C     . LEU A 1 171 ? -5.192  7.295   22.946  1.000 36.946  0 171 LEU AAA C     1 ? 1 
ATOM   1147  O O     . LEU A 1 171 ? -4.718  8.269   22.351  1.000 36.738  0 171 LEU AAA O     1 ? 1 
ATOM   1148  C CB    . LEU A 1 171 ? -4.955  5.577   21.143  1.000 39.084  0 171 LEU AAA CB    1 ? 1 
ATOM   1149  C CG    . LEU A 1 171 ? -3.660  5.049   21.758  1.000 39.616  0 171 LEU AAA CG    1 ? 1 
ATOM   1150  C CD1   . LEU A 1 171 ? -3.972  4.063   22.872  1.000 40.287  0 171 LEU AAA CD1   1 ? 1 
ATOM   1151  C CD2   . LEU A 1 171 ? -2.815  4.369   20.682  1.000 40.071  0 171 LEU AAA CD2   1 ? 1 
ATOM   1152  N N     . LEU A 1 172 ? -5.115  7.083   24.259  1.000 35.000  0 172 LEU AAA N     1 ? 1 
ATOM   1153  C CA    . LEU A 1 172 ? -4.296  7.907   25.183  1.000 34.273  0 172 LEU AAA CA    1 ? 1 
ATOM   1154  C C     . LEU A 1 172 ? -2.933  7.251   25.329  1.000 32.816  0 172 LEU AAA C     1 ? 1 
ATOM   1155  O O     . LEU A 1 172 ? -2.882  6.038   25.670  1.000 31.554  0 172 LEU AAA O     1 ? 1 
ATOM   1156  C CB    . LEU A 1 172 ? -5.034  8.003   26.518  1.000 34.349  0 172 LEU AAA CB    1 ? 1 
ATOM   1157  C CG    . LEU A 1 172 ? -6.499  8.447   26.418  1.000 34.479  0 172 LEU AAA CG    1 ? 1 
ATOM   1158  C CD1   . LEU A 1 172 ? -7.169  8.387   27.791  1.000 36.546  0 172 LEU AAA CD1   1 ? 1 
ATOM   1159  C CD2   . LEU A 1 172 ? -6.558  9.854   25.888  1.000 33.149  0 172 LEU AAA CD2   1 ? 1 
ATOM   1160  N N     . ALA A 1 173 ? -1.874  8.003   25.039  1.000 32.754  0 173 ALA AAA N     1 ? 1 
ATOM   1161  C CA    . ALA A 1 173 ? -0.465  7.596   25.269  1.000 33.039  0 173 ALA AAA CA    1 ? 1 
ATOM   1162  C C     . ALA A 1 173 ? 0.368   8.837   25.574  1.000 33.183  0 173 ALA AAA C     1 ? 1 
ATOM   1163  O O     . ALA A 1 173 ? 1.307   9.115   24.834  1.000 31.884  0 173 ALA AAA O     1 ? 1 
ATOM   1164  C CB    . ALA A 1 173 ? 0.047   6.875   24.065  1.000 34.842  0 173 ALA AAA CB    1 ? 1 
ATOM   1165  N N     . THR A 1 174 ? -0.005  9.545   26.645  1.000 33.613  0 174 THR AAA N     1 ? 1 
ATOM   1166  C CA    . THR A 1 174 ? 0.547   10.872  27.028  1.000 33.800  0 174 THR AAA CA    1 ? 1 
ATOM   1167  C C     . THR A 1 174 ? 1.798   10.731  27.903  1.000 32.244  0 174 THR AAA C     1 ? 1 
ATOM   1168  O O     . THR A 1 174 ? 2.455   11.748  28.157  1.000 30.291  0 174 THR AAA O     1 ? 1 
ATOM   1169  C CB    . THR A 1 174 ? -0.546  11.711  27.697  1.000 34.115  0 174 THR AAA CB    1 ? 1 
ATOM   1170  O OG1   . THR A 1 174 ? -1.124  10.936  28.741  1.000 32.592  0 174 THR AAA OG1   1 ? 1 
ATOM   1171  C CG2   . THR A 1 174 ? -1.586  12.132  26.690  1.000 36.550  0 174 THR AAA CG2   1 ? 1 
ATOM   1172  N N     . GLY A 1 175 ? 2.126   9.507   28.313  1.000 33.288  0 175 GLY AAA N     1 ? 1 
ATOM   1173  C CA    . GLY A 1 175 ? 3.316   9.185   29.125  1.000 31.562  0 175 GLY AAA CA    1 ? 1 
ATOM   1174  C C     . GLY A 1 175 ? 3.254   9.811   30.507  1.000 32.484  0 175 GLY AAA C     1 ? 1 
ATOM   1175  O O     . GLY A 1 175 ? 2.199   10.324  30.903  1.000 32.038  0 175 GLY AAA O     1 ? 1 
ATOM   1176  N N     . GLY A 1 176 ? 4.370   9.751   31.229  1.000 33.125  0 176 GLY AAA N     1 ? 1 
ATOM   1177  C CA    . GLY A 1 176 ? 4.563   10.452  32.492  1.000 32.545  0 176 GLY AAA CA    1 ? 1 
ATOM   1178  C C     . GLY A 1 176 ? 5.517   11.623  32.367  1.000 33.149  0 176 GLY AAA C     1 ? 1 
ATOM   1179  O O     . GLY A 1 176 ? 5.939   11.971  31.242  1.000 31.811  0 176 GLY AAA O     1 ? 1 
ATOM   1180  N N     . ARG A 1 177 ? 5.760   12.255  33.527  1.000 33.357  0 177 ARG AAA N     1 ? 1 
ATOM   1181  C CA    . ARG A 1 177 ? 6.802   13.275  33.760  1.000 33.797  0 177 ARG AAA CA    1 ? 1 
ATOM   1182  C C     . ARG A 1 177 ? 7.464   12.993  35.097  1.000 33.988  0 177 ARG AAA C     1 ? 1 
ATOM   1183  O O     . ARG A 1 177 ? 6.868   12.367  35.974  1.000 32.108  0 177 ARG AAA O     1 ? 1 
ATOM   1184  C CB    . ARG A 1 177 ? 6.220   14.675  33.585  1.000 33.551  0 177 ARG AAA CB    1 ? 1 
ATOM   1185  C CG    . ARG A 1 177 ? 5.718   14.922  32.163  1.000 34.886  0 177 ARG AAA CG    1 ? 1 
ATOM   1186  C CD    . ARG A 1 177 ? 6.807   14.825  31.109  1.000 34.858  0 177 ARG AAA CD    1 ? 1 
ATOM   1187  N NE    . ARG A 1 177 ? 7.725   15.957  31.214  1.000 34.985  0 177 ARG AAA NE    1 ? 1 
ATOM   1188  C CZ    . ARG A 1 177 ? 7.491   17.160  30.721  1.000 33.129  0 177 ARG AAA CZ    1 ? 1 
ATOM   1189  N NH1   . ARG A 1 177 ? 6.363   17.409  30.068  1.000 34.128  0 177 ARG AAA NH1   1 ? 1 
ATOM   1190  N NH2   . ARG A 1 177 ? 8.406   18.100  30.837  1.000 33.102  0 177 ARG AAA NH2   1 ? 1 
ATOM   1191  N N     . PRO A 1 178 ? 8.729   13.434  35.279  1.000 33.854  0 178 PRO AAA N     1 ? 1 
ATOM   1192  C CA    . PRO A 1 178 ? 9.412   13.241  36.549  1.000 36.134  0 178 PRO AAA CA    1 ? 1 
ATOM   1193  C C     . PRO A 1 178 ? 8.563   13.802  37.701  1.000 39.174  0 178 PRO AAA C     1 ? 1 
ATOM   1194  O O     . PRO A 1 178 ? 7.882   14.833  37.523  1.000 33.371  0 178 PRO AAA O     1 ? 1 
ATOM   1195  C CB    . PRO A 1 178 ? 10.710  14.038  36.421  1.000 36.566  0 178 PRO AAA CB    1 ? 1 
ATOM   1196  C CG    . PRO A 1 178 ? 10.929  14.114  34.909  1.000 35.421  0 178 PRO AAA CG    1 ? 1 
ATOM   1197  C CD    . PRO A 1 178 ? 9.547   14.139  34.291  1.000 34.182  0 178 PRO AAA CD    1 ? 1 
ATOM   1198  N N     . SER A 1 179 ? 8.605   13.105  38.840  1.000 41.548  0 179 SER AAA N     1 ? 1 
ATOM   1199  C CA    . SER A 1 179 ? 7.954   13.562  40.081  1.000 45.855  0 179 SER AAA CA    1 ? 1 
ATOM   1200  C C     . SER A 1 179 ? 8.997   14.164  41.033  1.000 46.082  0 179 SER AAA C     1 ? 1 
ATOM   1201  O O     . SER A 1 179 ? 10.063  13.532  41.238  1.000 39.012  0 179 SER AAA O     1 ? 1 
ATOM   1202  C CB    . SER A 1 179 ? 7.166   12.480  40.731  1.000 47.382  0 179 SER AAA CB    1 ? 1 
ATOM   1203  O OG    . SER A 1 179 ? 6.295   13.070  41.702  1.000 49.175  0 179 SER AAA OG    1 ? 1 
ATOM   1204  N N     . ILE A 1 180 ? 8.695   15.370  41.521  1.000 48.052  0 180 ILE AAA N     1 ? 1 
ATOM   1205  C CA    . ILE A 1 180 ? 9.469   16.073  42.574  1.000 49.666  0 180 ILE AAA CA    1 ? 1 
ATOM   1206  C C     . ILE A 1 180 ? 8.571   16.244  43.793  1.000 49.569  0 180 ILE AAA C     1 ? 1 
ATOM   1207  O O     . ILE A 1 180 ? 7.482   16.797  43.677  1.000 49.834  0 180 ILE AAA O     1 ? 1 
ATOM   1208  C CB    . ILE A 1 180 ? 9.968   17.438  42.075  1.000 51.382  0 180 ILE AAA CB    1 ? 1 
ATOM   1209  C CG1   . ILE A 1 180 ? 10.749  17.326  40.767  1.000 48.514  0 180 ILE AAA CG1   1 ? 1 
ATOM   1210  C CG2   . ILE A 1 180 ? 10.777  18.118  43.170  1.000 53.726  0 180 ILE AAA CG2   1 ? 1 
ATOM   1211  C CD1   . ILE A 1 180 ? 11.193  18.645  40.218  1.000 48.292  0 180 ILE AAA CD1   1 ? 1 
ATOM   1212  N N     . PRO A 1 181 ? 9.009   15.806  44.995  1.000 51.108  0 181 PRO AAA N     1 ? 1 
ATOM   1213  C CA    . PRO A 1 181 ? 8.242   16.002  46.226  1.000 50.395  0 181 PRO AAA CA    1 ? 1 
ATOM   1214  C C     . PRO A 1 181 ? 7.959   17.475  46.571  1.000 49.267  0 181 PRO AAA C     1 ? 1 
ATOM   1215  O O     . PRO A 1 181 ? 8.900   18.205  46.777  1.000 46.660  0 181 PRO AAA O     1 ? 1 
ATOM   1216  C CB    . PRO A 1 181 ? 9.107   15.336  47.306  1.000 49.881  0 181 PRO AAA CB    1 ? 1 
ATOM   1217  C CG    . PRO A 1 181 ? 10.501  15.278  46.720  1.000 50.487  0 181 PRO AAA CG    1 ? 1 
ATOM   1218  C CD    . PRO A 1 181 ? 10.285  15.109  45.233  1.000 51.189  0 181 PRO AAA CD    1 ? 1 
ATOM   1219  N N     . GLU A 1 182 ? 6.665   17.838  46.636  1.000 51.589  0 182 GLU AAA N     1 ? 1 
ATOM   1220  C CA    . GLU A 1 182 ? 6.126   19.196  46.956  1.000 56.044  0 182 GLU AAA CA    1 ? 1 
ATOM   1221  C C     . GLU A 1 182 ? 6.362   19.483  48.450  1.000 54.998  0 182 GLU AAA C     1 ? 1 
ATOM   1222  O O     . GLU A 1 182 ? 6.529   20.662  48.803  1.000 56.997  0 182 GLU AAA O     1 ? 1 
ATOM   1223  C CB    . GLU A 1 182 ? 4.638   19.314  46.599  1.000 60.759  0 182 GLU AAA CB    1 ? 1 
ATOM   1224  C CG    . GLU A 1 182 ? 4.343   19.153  45.114  1.000 71.185  0 182 GLU AAA CG    1 ? 1 
ATOM   1225  C CD    . GLU A 1 182 ? 3.425   20.177  44.447  1.000 78.137  0 182 GLU AAA CD    1 ? 1 
ATOM   1226  O OE1   . GLU A 1 182 ? 2.849   21.048  45.163  1.000 73.987  0 182 GLU AAA OE1   1 ? 1 
ATOM   1227  O OE2   . GLU A 1 182 ? 3.302   20.109  43.190  1.000 79.532  0 182 GLU AAA OE2   1 ? 1 
ATOM   1228  N N     . THR A 1 183 ? 6.457   18.427  49.263  1.000 49.229  0 183 THR AAA N     1 ? 1 
ATOM   1229  C CA    . THR A 1 183 ? 6.612   18.454  50.737  1.000 54.243  0 183 THR AAA CA    1 ? 1 
ATOM   1230  C C     . THR A 1 183 ? 8.031   18.922  51.118  1.000 55.097  0 183 THR AAA C     1 ? 1 
ATOM   1231  O O     . THR A 1 183 ? 8.151   19.624  52.150  1.000 59.529  0 183 THR AAA O     1 ? 1 
ATOM   1232  C CB    . THR A 1 183 ? 6.269   17.074  51.325  1.000 55.989  0 183 THR AAA CB    1 ? 1 
ATOM   1233  O OG1   . THR A 1 183 ? 7.216   16.113  50.851  1.000 55.135  0 183 THR AAA OG1   1 ? 1 
ATOM   1234  C CG2   . THR A 1 183 ? 4.877   16.596  50.954  1.000 54.987  0 183 THR AAA CG2   1 ? 1 
ATOM   1235  N N     . VAL A 1 184 ? 9.069   18.584  50.336  1.000 49.096  0 184 VAL AAA N     1 ? 1 
ATOM   1236  C CA    . VAL A 1 184 ? 10.481  18.998  50.622  1.000 45.997  0 184 VAL AAA CA    1 ? 1 
ATOM   1237  C C     . VAL A 1 184 ? 10.708  20.418  50.116  1.000 44.806  0 184 VAL AAA C     1 ? 1 
ATOM   1238  O O     . VAL A 1 184 ? 10.686  20.661  48.918  1.000 47.352  0 184 VAL AAA O     1 ? 1 
ATOM   1239  C CB    . VAL A 1 184 ? 11.513  18.025  50.023  1.000 42.518  0 184 VAL AAA CB    1 ? 1 
ATOM   1240  C CG1   . VAL A 1 184 ? 12.913  18.583  50.146  1.000 41.588  0 184 VAL AAA CG1   1 ? 1 
ATOM   1241  C CG2   . VAL A 1 184 ? 11.419  16.631  50.642  1.000 40.929  0 184 VAL AAA CG2   1 ? 1 
ATOM   1242  N N     . PRO A 1 185 ? 10.929  21.403  51.009  1.000 46.241  0 185 PRO AAA N     1 ? 1 
ATOM   1243  C CA    . PRO A 1 185 ? 11.149  22.793  50.594  1.000 45.149  0 185 PRO AAA CA    1 ? 1 
ATOM   1244  C C     . PRO A 1 185 ? 12.422  23.020  49.767  1.000 42.313  0 185 PRO AAA C     1 ? 1 
ATOM   1245  O O     . PRO A 1 185 ? 13.448  22.500  50.132  1.000 40.528  0 185 PRO AAA O     1 ? 1 
ATOM   1246  C CB    . PRO A 1 185 ? 11.266  23.585  51.912  1.000 46.013  0 185 PRO AAA CB    1 ? 1 
ATOM   1247  C CG    . PRO A 1 185 ? 10.685  22.654  52.968  1.000 47.280  0 185 PRO AAA CG    1 ? 1 
ATOM   1248  C CD    . PRO A 1 185 ? 10.958  21.248  52.473  1.000 46.635  0 185 PRO AAA CD    1 ? 1 
ATOM   1249  N N     . GLY A 1 186 ? 12.301  23.826  48.707  1.000 40.543  0 186 GLY AAA N     1 ? 1 
ATOM   1250  C CA    . GLY A 1 186 ? 13.367  24.151  47.739  1.000 41.638  0 186 GLY AAA CA    1 ? 1 
ATOM   1251  C C     . GLY A 1 186 ? 13.456  23.167  46.571  1.000 41.408  0 186 GLY AAA C     1 ? 1 
ATOM   1252  O O     . GLY A 1 186 ? 14.094  23.531  45.572  1.000 41.458  0 186 GLY AAA O     1 ? 1 
ATOM   1253  N N     . ALA A 1 187 ? 12.860  21.967  46.678  1.000 41.201  0 187 ALA AAA N     1 ? 1 
ATOM   1254  C CA    . ALA A 1 187 ? 13.006  20.844  45.714  1.000 40.507  0 187 ALA AAA CA    1 ? 1 
ATOM   1255  C C     . ALA A 1 187 ? 12.566  21.282  44.312  1.000 41.586  0 187 ALA AAA C     1 ? 1 
ATOM   1256  O O     . ALA A 1 187 ? 13.397  21.162  43.371  1.000 41.117  0 187 ALA AAA O     1 ? 1 
ATOM   1257  C CB    . ALA A 1 187 ? 12.222  19.643  46.190  1.000 39.941  0 187 ALA AAA CB    1 ? 1 
ATOM   1258  N N     . ILE A 1 188 ? 11.327  21.791  44.181  1.000 42.804  0 188 ILE AAA N     1 ? 1 
ATOM   1259  C CA    . ILE A 1 188 ? 10.720  22.189  42.876  1.000 44.055  0 188 ILE AAA CA    1 ? 1 
ATOM   1260  C C     . ILE A 1 188 ? 11.572  23.295  42.246  1.000 44.197  0 188 ILE AAA C     1 ? 1 
ATOM   1261  O O     . ILE A 1 188 ? 11.744  23.299  41.018  1.000 47.081  0 188 ILE AAA O     1 ? 1 
ATOM   1262  C CB    . ILE A 1 188 ? 9.229   22.571  43.070  1.000 44.754  0 188 ILE AAA CB    1 ? 1 
ATOM   1263  C CG1   . ILE A 1 188 ? 8.356   21.310  43.020  1.000 44.316  0 188 ILE AAA CG1   1 ? 1 
ATOM   1264  C CG2   . ILE A 1 188 ? 8.765   23.628  42.068  1.000 43.064  0 188 ILE AAA CG2   1 ? 1 
ATOM   1265  C CD1   . ILE A 1 188 ? 6.984   21.474  43.640  1.000 45.191  0 188 ILE AAA CD1   1 ? 1 
ATOM   1266  N N     . GLN A 1 189 ? 12.066  24.213  43.070  1.000 46.704  0 189 GLN AAA N     1 ? 1 
ATOM   1267  C CA    . GLN A 1 189 ? 12.695  25.471  42.597  1.000 48.424  0 189 GLN AAA CA    1 ? 1 
ATOM   1268  C C     . GLN A 1 189 ? 14.115  25.172  42.086  1.000 46.759  0 189 GLN AAA C     1 ? 1 
ATOM   1269  O O     . GLN A 1 189 ? 14.497  25.746  41.041  1.000 43.554  0 189 GLN AAA O     1 ? 1 
ATOM   1270  C CB    . GLN A 1 189 ? 12.710  26.531  43.711  1.000 48.974  0 189 GLN AAA CB    1 ? 1 
ATOM   1271  C CG    . GLN A 1 189 ? 12.854  27.946  43.163  1.000 50.427  0 189 GLN AAA CG    1 ? 1 
ATOM   1272  C CD    . GLN A 1 189 ? 13.154  29.008  44.204  1.000 50.924  0 189 GLN AAA CD    1 ? 1 
ATOM   1273  O OE1   . GLN A 1 189 ? 12.660  28.979  45.330  1.000 45.951  0 189 GLN AAA OE1   1 ? 1 
ATOM   1274  N NE2   . GLN A 1 189 ? 13.993  29.963  43.823  1.000 51.420  0 189 GLN AAA NE2   1 ? 1 
ATOM   1275  N N     . TYR A 1 190 ? 14.877  24.347  42.815  1.000 45.831  0 190 TYR AAA N     1 ? 1 
ATOM   1276  C CA    . TYR A 1 190 ? 16.360  24.292  42.688  1.000 46.015  0 190 TYR AAA CA    1 ? 1 
ATOM   1277  C C     . TYR A 1 190 ? 16.854  22.985  42.046  1.000 42.254  0 190 TYR AAA C     1 ? 1 
ATOM   1278  O O     . TYR A 1 190 ? 17.963  23.010  41.507  1.000 42.306  0 190 TYR AAA O     1 ? 1 
ATOM   1279  C CB    . TYR A 1 190 ? 16.992  24.521  44.062  1.000 48.467  0 190 TYR AAA CB    1 ? 1 
ATOM   1280  C CG    . TYR A 1 190 ? 16.836  25.921  44.591  1.000 52.177  0 190 TYR AAA CG    1 ? 1 
ATOM   1281  C CD1   . TYR A 1 190 ? 17.230  27.018  43.832  1.000 53.209  0 190 TYR AAA CD1   1 ? 1 
ATOM   1282  C CD2   . TYR A 1 190 ? 16.278  26.158  45.848  1.000 54.433  0 190 TYR AAA CD2   1 ? 1 
ATOM   1283  C CE1   . TYR A 1 190 ? 17.096  28.309  44.315  1.000 53.918  0 190 TYR AAA CE1   1 ? 1 
ATOM   1284  C CE2   . TYR A 1 190 ? 16.166  27.444  46.355  1.000 54.186  0 190 TYR AAA CE2   1 ? 1 
ATOM   1285  C CZ    . TYR A 1 190 ? 16.574  28.519  45.583  1.000 56.139  0 190 TYR AAA CZ    1 ? 1 
ATOM   1286  O OH    . TYR A 1 190 ? 16.446  29.785  46.079  1.000 60.731  0 190 TYR AAA OH    1 ? 1 
ATOM   1287  N N     . SER A 1 191 ? 16.064  21.905  42.105  1.000 39.823  0 191 SER AAA N     1 ? 1 
ATOM   1288  C CA    . SER A 1 191 ? 16.436  20.558  41.619  1.000 37.453  0 191 SER AAA CA    1 ? 1 
ATOM   1289  C C     . SER A 1 191 ? 16.097  20.385  40.138  1.000 34.684  0 191 SER AAA C     1 ? 1 
ATOM   1290  O O     . SER A 1 191 ? 15.130  20.942  39.684  1.000 34.112  0 191 SER AAA O     1 ? 1 
ATOM   1291  C CB    . SER A 1 191 ? 15.793  19.483  42.424  1.000 37.405  0 191 SER AAA CB    1 ? 1 
ATOM   1292  O OG    . SER A 1 191 ? 14.460  19.327  42.018  1.000 41.255  0 191 SER AAA OG    1 ? 1 
ATOM   1293  N N     . ILE A 1 192 ? 16.894  19.575  39.445  1.000 34.670  0 192 ILE AAA N     1 ? 1 
ATOM   1294  C CA    . ILE A 1 192 ? 16.631  19.134  38.044  1.000 33.858  0 192 ILE AAA CA    1 ? 1 
ATOM   1295  C C     . ILE A 1 192 ? 16.068  17.699  38.091  1.000 32.693  0 192 ILE AAA C     1 ? 1 
ATOM   1296  O O     . ILE A 1 192 ? 16.018  17.100  39.179  1.000 31.340  0 192 ILE AAA O     1 ? 1 
ATOM   1297  C CB    . ILE A 1 192 ? 17.895  19.253  37.179  1.000 35.171  0 192 ILE AAA CB    1 ? 1 
ATOM   1298  C CG1   . ILE A 1 192 ? 19.014  18.326  37.652  1.000 35.443  0 192 ILE AAA CG1   1 ? 1 
ATOM   1299  C CG2   . ILE A 1 192 ? 18.393  20.687  37.142  1.000 37.413  0 192 ILE AAA CG2   1 ? 1 
ATOM   1300  C CD1   . ILE A 1 192 ? 20.146  18.143  36.661  1.000 34.617  0 192 ILE AAA CD1   1 ? 1 
ATOM   1301  N N     . THR A 1 193 ? 15.635  17.191  36.941  1.000 31.490  0 193 THR AAA N     1 ? 1 
ATOM   1302  C CA    . THR A 1 193 ? 15.164  15.811  36.711  1.000 29.686  0 193 THR AAA CA    1 ? 1 
ATOM   1303  C C     . THR A 1 193 ? 15.816  15.293  35.432  1.000 29.436  0 193 THR AAA C     1 ? 1 
ATOM   1304  O O     . THR A 1 193 ? 16.628  16.002  34.866  1.000 28.658  0 193 THR AAA O     1 ? 1 
ATOM   1305  C CB    . THR A 1 193 ? 13.634  15.808  36.621  1.000 29.527  0 193 THR AAA CB    1 ? 1 
ATOM   1306  O OG1   . THR A 1 193 ? 13.228  16.490  35.422  1.000 28.026  0 193 THR AAA OG1   1 ? 1 
ATOM   1307  C CG2   . THR A 1 193 ? 13.010  16.435  37.859  1.000 29.716  0 193 THR AAA CG2   1 ? 1 
ATOM   1308  N N     . SER A 1 194 ? 15.424  14.097  34.990  1.000 30.027  0 194 SER AAA N     1 ? 1 
ATOM   1309  C CA    . SER A 1 194 ? 15.882  13.436  33.745  1.000 28.374  0 194 SER AAA CA    1 ? 1 
ATOM   1310  C C     . SER A 1 194 ? 15.467  14.287  32.536  1.000 27.311  0 194 SER AAA C     1 ? 1 
ATOM   1311  O O     . SER A 1 194 ? 16.121  14.175  31.479  1.000 26.672  0 194 SER AAA O     1 ? 1 
ATOM   1312  C CB    . SER A 1 194 ? 15.378  11.999  33.640  1.000 27.976  0 194 SER AAA CB    1 ? 1 
ATOM   1313  O OG    . SER A 1 194 ? 13.991  11.945  33.907  1.000 28.476  0 194 SER AAA OG    1 ? 1 
ATOM   1314  N N     . ASP A 1 195 ? 14.440  15.107  32.666  1.000 25.368  0 195 ASP AAA N     1 ? 1 
ATOM   1315  C CA    . ASP A 1 195 ? 14.038  16.053  31.596  1.000 25.821  0 195 ASP AAA CA    1 ? 1 
ATOM   1316  C C     . ASP A 1 195 ? 15.161  17.079  31.297  1.000 27.207  0 195 ASP AAA C     1 ? 1 
ATOM   1317  O O     . ASP A 1 195 ? 15.170  17.657  30.193  1.000 28.626  0 195 ASP AAA O     1 ? 1 
ATOM   1318  C CB    . ASP A 1 195 ? 12.740  16.755  31.993  1.000 25.656  0 195 ASP AAA CB    1 ? 1 
ATOM   1319  C CG    . ASP A 1 195 ? 11.492  15.900  31.892  1.000 25.199  0 195 ASP AAA CG    1 ? 1 
ATOM   1320  O OD1   . ASP A 1 195 ? 11.595  14.699  31.582  1.000 24.009  0 195 ASP AAA OD1   1 ? 1 
ATOM   1321  O OD2   . ASP A 1 195 ? 10.424  16.477  32.076  1.000 28.307  0 195 ASP AAA OD2   1 ? 1 
ATOM   1322  N N     . ASP A 1 196 ? 16.064  17.359  32.233  1.000 28.020  0 196 ASP AAA N     1 ? 1 
ATOM   1323  C CA    . ASP A 1 196 ? 17.036  18.476  32.089  1.000 30.366  0 196 ASP AAA CA    1 ? 1 
ATOM   1324  C C     . ASP A 1 196 ? 18.486  17.957  31.940  1.000 30.541  0 196 ASP AAA C     1 ? 1 
ATOM   1325  O O     . ASP A 1 196 ? 19.284  18.666  31.272  1.000 29.423  0 196 ASP AAA O     1 ? 1 
ATOM   1326  C CB    . ASP A 1 196 ? 16.940  19.424  33.274  1.000 31.306  0 196 ASP AAA CB    1 ? 1 
ATOM   1327  C CG    . ASP A 1 196 ? 15.495  19.748  33.652  1.000 33.605  0 196 ASP AAA CG    1 ? 1 
ATOM   1328  O OD1   . ASP A 1 196 ? 14.806  20.390  32.824  1.000 33.803  0 196 ASP AAA OD1   1 ? 1 
ATOM   1329  O OD2   . ASP A 1 196 ? 15.067  19.379  34.784  1.000 32.834  0 196 ASP AAA OD2   1 ? 1 
ATOM   1330  N N     . ILE A 1 197 ? 18.790  16.778  32.503  1.000 29.368  0 197 ILE AAA N     1 ? 1 
ATOM   1331  C CA    . ILE A 1 197 ? 20.188  16.297  32.705  1.000 30.446  0 197 ILE AAA CA    1 ? 1 
ATOM   1332  C C     . ILE A 1 197 ? 20.947  16.144  31.376  1.000 29.610  0 197 ILE AAA C     1 ? 1 
ATOM   1333  O O     . ILE A 1 197 ? 22.155  16.394  31.365  1.000 28.789  0 197 ILE AAA O     1 ? 1 
ATOM   1334  C CB    . ILE A 1 197 ? 20.233  14.992  33.527  1.000 30.065  0 197 ILE AAA CB    1 ? 1 
ATOM   1335  C CG1   . ILE A 1 197 ? 21.676  14.572  33.838  1.000 28.373  0 197 ILE AAA CG1   1 ? 1 
ATOM   1336  C CG2   . ILE A 1 197 ? 19.460  13.888  32.845  1.000 29.830  0 197 ILE AAA CG2   1 ? 1 
ATOM   1337  C CD1   . ILE A 1 197 ? 22.495  15.656  34.496  1.000 28.417  0 197 ILE AAA CD1   1 ? 1 
ATOM   1338  N N     . PHE A 1 198 ? 20.294  15.772  30.286  1.000 30.717  0 198 PHE AAA N     1 ? 1 
ATOM   1339  C CA    . PHE A 1 198 ? 21.018  15.447  29.028  1.000 31.675  0 198 PHE AAA CA    1 ? 1 
ATOM   1340  C C     . PHE A 1 198 ? 21.388  16.722  28.266  1.000 34.470  0 198 PHE AAA C     1 ? 1 
ATOM   1341  O O     . PHE A 1 198 ? 22.197  16.583  27.344  1.000 38.157  0 198 PHE AAA O     1 ? 1 
ATOM   1342  C CB    . PHE A 1 198 ? 20.203  14.477  28.179  1.000 30.714  0 198 PHE AAA CB    1 ? 1 
ATOM   1343  C CG    . PHE A 1 198 ? 19.849  13.227  28.937  1.000 29.252  0 198 PHE AAA CG    1 ? 1 
ATOM   1344  C CD1   . PHE A 1 198 ? 20.853  12.390  29.383  1.000 28.674  0 198 PHE AAA CD1   1 ? 1 
ATOM   1345  C CD2   . PHE A 1 198 ? 18.534  12.908  29.239  1.000 28.128  0 198 PHE AAA CD2   1 ? 1 
ATOM   1346  C CE1   . PHE A 1 198 ? 20.542  11.250  30.104  1.000 27.933  0 198 PHE AAA CE1   1 ? 1 
ATOM   1347  C CE2   . PHE A 1 198 ? 18.236  11.754  29.946  1.000 27.173  0 198 PHE AAA CE2   1 ? 1 
ATOM   1348  C CZ    . PHE A 1 198 ? 19.233  10.919  30.356  1.000 27.010  0 198 PHE AAA CZ    1 ? 1 
ATOM   1349  N N     . PHE A 1 199 ? 20.842  17.889  28.643  1.000 36.264  0 199 PHE AAA N     1 ? 1 
ATOM   1350  C CA    . PHE A 1 199 ? 20.917  19.163  27.875  1.000 37.343  0 199 PHE AAA CA    1 ? 1 
ATOM   1351  C C     . PHE A 1 199 ? 21.473  20.308  28.725  1.000 36.660  0 199 PHE AAA C     1 ? 1 
ATOM   1352  O O     . PHE A 1 199 ? 21.483  21.434  28.225  1.000 35.357  0 199 PHE AAA O     1 ? 1 
ATOM   1353  C CB    . PHE A 1 199 ? 19.542  19.555  27.331  1.000 38.147  0 199 PHE AAA CB    1 ? 1 
ATOM   1354  C CG    . PHE A 1 199 ? 18.886  18.437  26.582  1.000 40.056  0 199 PHE AAA CG    1 ? 1 
ATOM   1355  C CD1   . PHE A 1 199 ? 19.511  17.922  25.465  1.000 41.739  0 199 PHE AAA CD1   1 ? 1 
ATOM   1356  C CD2   . PHE A 1 199 ? 17.680  17.883  27.005  1.000 43.389  0 199 PHE AAA CD2   1 ? 1 
ATOM   1357  C CE1   . PHE A 1 199 ? 18.931  16.894  24.738  1.000 42.945  0 199 PHE AAA CE1   1 ? 1 
ATOM   1358  C CE2   . PHE A 1 199 ? 17.110  16.835  26.294  1.000 44.565  0 199 PHE AAA CE2   1 ? 1 
ATOM   1359  C CZ    . PHE A 1 199 ? 17.734  16.359  25.149  1.000 44.765  0 199 PHE AAA CZ    1 ? 1 
ATOM   1360  N N     . LEU A 1 200 ? 21.925  20.068  29.954  1.000 36.566  0 200 LEU AAA N     1 ? 1 
ATOM   1361  C CA    . LEU A 1 200 ? 22.501  21.165  30.763  1.000 39.290  0 200 LEU AAA CA    1 ? 1 
ATOM   1362  C C     . LEU A 1 200 ? 23.528  21.938  29.933  1.000 41.662  0 200 LEU AAA C     1 ? 1 
ATOM   1363  O O     . LEU A 1 200 ? 24.426  21.295  29.397  1.000 42.792  0 200 LEU AAA O     1 ? 1 
ATOM   1364  C CB    . LEU A 1 200 ? 23.197  20.575  31.980  1.000 39.976  0 200 LEU AAA CB    1 ? 1 
ATOM   1365  C CG    . LEU A 1 200 ? 22.297  20.041  33.082  1.000 38.798  0 200 LEU AAA CG    1 ? 1 
ATOM   1366  C CD1   . LEU A 1 200 ? 23.158  19.607  34.253  1.000 39.103  0 200 LEU AAA CD1   1 ? 1 
ATOM   1367  C CD2   . LEU A 1 200 ? 21.255  21.071  33.485  1.000 38.707  0 200 LEU AAA CD2   1 ? 1 
ATOM   1368  N N     . SER A 1 201 ? 23.415  23.264  29.838  1.000 44.741  0 201 SER AAA N     1 ? 1 
ATOM   1369  C CA    A SER A 1 201 ? 24.434  24.121  29.163  0.500 45.415  0 201 SER AAA CA    1 ? 1 
ATOM   1370  C CA    B SER A 1 201 ? 24.426  24.139  29.174  0.500 45.206  0 201 SER AAA CA    1 ? 1 
ATOM   1371  C C     . SER A 1 201 ? 25.747  24.070  29.955  1.000 45.687  0 201 SER AAA C     1 ? 1 
ATOM   1372  O O     . SER A 1 201 ? 26.811  24.211  29.342  1.000 48.002  0 201 SER AAA O     1 ? 1 
ATOM   1373  C CB    A SER A 1 201 ? 23.956  25.533  28.970  0.500 45.755  0 201 SER AAA CB    1 ? 1 
ATOM   1374  C CB    B SER A 1 201 ? 23.958  25.573  29.042  0.500 45.355  0 201 SER AAA CB    1 ? 1 
ATOM   1375  O OG    A SER A 1 201 ? 23.516  26.088  30.196  0.500 46.009  0 201 SER AAA OG    1 ? 1 
ATOM   1376  O OG    B SER A 1 201 ? 22.646  25.667  28.507  0.500 44.873  0 201 SER AAA OG    1 ? 1 
ATOM   1377  N N     . LYS A 1 202 ? 25.664  23.854  31.266  1.000 48.353  0 202 LYS AAA N     1 ? 1 
ATOM   1378  C CA    . LYS A 1 202 ? 26.843  23.753  32.167  1.000 49.587  0 202 LYS AAA CA    1 ? 1 
ATOM   1379  C C     . LYS A 1 202 ? 27.000  22.326  32.712  1.000 47.041  0 202 LYS AAA C     1 ? 1 
ATOM   1380  O O     . LYS A 1 202 ? 25.954  21.685  32.990  1.000 42.578  0 202 LYS AAA O     1 ? 1 
ATOM   1381  C CB    . LYS A 1 202 ? 26.644  24.740  33.310  1.000 52.785  0 202 LYS AAA CB    1 ? 1 
ATOM   1382  C CG    . LYS A 1 202 ? 27.857  24.988  34.202  1.000 56.065  0 202 LYS AAA CG    1 ? 1 
ATOM   1383  C CD    . LYS A 1 202 ? 27.491  25.328  35.640  1.000 59.552  0 202 LYS AAA CD    1 ? 1 
ATOM   1384  C CE    . LYS A 1 202 ? 26.481  24.363  36.239  1.000 61.726  0 202 LYS AAA CE    1 ? 1 
ATOM   1385  N NZ    . LYS A 1 202 ? 26.729  24.091  37.678  1.000 63.483  0 202 LYS AAA NZ    1 ? 1 
ATOM   1386  N N     . SER A 1 203 ? 28.245  21.851  32.854  1.000 44.662  0 203 SER AAA N     1 ? 1 
ATOM   1387  C CA    . SER A 1 203 ? 28.519  20.533  33.484  1.000 44.307  0 203 SER AAA CA    1 ? 1 
ATOM   1388  C C     . SER A 1 203 ? 27.967  20.572  34.912  1.000 45.083  0 203 SER AAA C     1 ? 1 
ATOM   1389  O O     . SER A 1 203 ? 28.010  21.596  35.603  1.000 44.624  0 203 SER AAA O     1 ? 1 
ATOM   1390  C CB    . SER A 1 203 ? 29.970  20.112  33.428  1.000 43.794  0 203 SER AAA CB    1 ? 1 
ATOM   1391  O OG    . SER A 1 203 ? 30.769  20.971  34.195  1.000 46.312  0 203 SER AAA OG    1 ? 1 
ATOM   1392  N N     . PRO A 1 204 ? 27.396  19.445  35.393  1.000 44.069  0 204 PRO AAA N     1 ? 1 
ATOM   1393  C CA    . PRO A 1 204 ? 26.689  19.444  36.673  1.000 41.235  0 204 PRO AAA CA    1 ? 1 
ATOM   1394  C C     . PRO A 1 204 ? 27.566  19.518  37.934  1.000 37.647  0 204 PRO AAA C     1 ? 1 
ATOM   1395  O O     . PRO A 1 204 ? 27.012  19.751  38.987  1.000 35.722  0 204 PRO AAA O     1 ? 1 
ATOM   1396  C CB    . PRO A 1 204 ? 25.918  18.121  36.597  1.000 42.653  0 204 PRO AAA CB    1 ? 1 
ATOM   1397  C CG    . PRO A 1 204 ? 26.811  17.233  35.766  1.000 43.175  0 204 PRO AAA CG    1 ? 1 
ATOM   1398  C CD    . PRO A 1 204 ? 27.379  18.145  34.712  1.000 42.540  0 204 PRO AAA CD    1 ? 1 
ATOM   1399  N N     . GLY A 1 205 ? 28.890  19.334  37.779  1.000 34.433  0 205 GLY AAA N     1 ? 1 
ATOM   1400  C CA    . GLY A 1 205 ? 29.883  19.223  38.866  1.000 32.268  0 205 GLY AAA CA    1 ? 1 
ATOM   1401  C C     . GLY A 1 205 ? 29.435  18.246  39.932  1.000 31.497  0 205 GLY AAA C     1 ? 1 
ATOM   1402  O O     . GLY A 1 205 ? 28.811  17.195  39.561  1.000 30.766  0 205 GLY AAA O     1 ? 1 
ATOM   1403  N N     . LYS A 1 206 ? 29.700  18.566  41.201  1.000 30.217  0 206 LYS AAA N     1 ? 1 
ATOM   1404  C CA    . LYS A 1 206 ? 29.350  17.703  42.347  1.000 31.067  0 206 LYS AAA CA    1 ? 1 
ATOM   1405  C C     . LYS A 1 206 ? 27.825  17.487  42.363  1.000 30.709  0 206 LYS AAA C     1 ? 1 
ATOM   1406  O O     . LYS A 1 206 ? 27.070  18.473  42.430  1.000 31.390  0 206 LYS AAA O     1 ? 1 
ATOM   1407  C CB    . LYS A 1 206 ? 29.883  18.334  43.632  1.000 33.374  0 206 LYS AAA CB    1 ? 1 
ATOM   1408  C CG    . LYS A 1 206 ? 29.376  17.692  44.917  1.000 35.084  0 206 LYS AAA CG    1 ? 1 
ATOM   1409  C CD    . LYS A 1 206 ? 30.177  18.065  46.153  1.000 36.613  0 206 LYS AAA CD    1 ? 1 
ATOM   1410  C CE    . LYS A 1 206 ? 29.818  17.210  47.347  1.000 37.109  0 206 LYS AAA CE    1 ? 1 
ATOM   1411  N NZ    . LYS A 1 206 ? 30.171  17.867  48.632  1.000 39.209  0 206 LYS AAA NZ    1 ? 1 
ATOM   1412  N N     . THR A 1 207 ? 27.357  16.243  42.299  1.000 29.144  0 207 THR AAA N     1 ? 1 
ATOM   1413  C CA    . THR A 1 207 ? 25.920  15.954  42.057  1.000 28.202  0 207 THR AAA CA    1 ? 1 
ATOM   1414  C C     . THR A 1 207 ? 25.354  15.059  43.151  1.000 27.974  0 207 THR AAA C     1 ? 1 
ATOM   1415  O O     . THR A 1 207 ? 26.020  14.083  43.535  1.000 30.571  0 207 THR AAA O     1 ? 1 
ATOM   1416  C CB    . THR A 1 207 ? 25.709  15.310  40.682  1.000 27.582  0 207 THR AAA CB    1 ? 1 
ATOM   1417  O OG1   . THR A 1 207 ? 26.250  16.155  39.651  1.000 28.630  0 207 THR AAA OG1   1 ? 1 
ATOM   1418  C CG2   . THR A 1 207 ? 24.250  15.017  40.417  1.000 27.400  0 207 THR AAA CG2   1 ? 1 
ATOM   1419  N N     . LEU A 1 208 ? 24.149  15.389  43.606  1.000 27.528  0 208 LEU AAA N     1 ? 1 
ATOM   1420  C CA    . LEU A 1 208 ? 23.278  14.510  44.424  1.000 26.894  0 208 LEU AAA CA    1 ? 1 
ATOM   1421  C C     . LEU A 1 208 ? 22.127  13.995  43.552  1.000 26.309  0 208 LEU AAA C     1 ? 1 
ATOM   1422  O O     . LEU A 1 208 ? 21.432  14.822  42.913  1.000 25.951  0 208 LEU AAA O     1 ? 1 
ATOM   1423  C CB    . LEU A 1 208 ? 22.741  15.304  45.622  1.000 27.783  0 208 LEU AAA CB    1 ? 1 
ATOM   1424  C CG    . LEU A 1 208 ? 21.735  14.567  46.512  1.000 27.115  0 208 LEU AAA CG    1 ? 1 
ATOM   1425  C CD1   . LEU A 1 208 ? 22.375  13.414  47.233  1.000 26.771  0 208 LEU AAA CD1   1 ? 1 
ATOM   1426  C CD2   . LEU A 1 208 ? 21.125  15.491  47.539  1.000 28.071  0 208 LEU AAA CD2   1 ? 1 
ATOM   1427  N N     . VAL A 1 209 ? 21.940  12.682  43.546  1.000 25.592  0 209 VAL AAA N     1 ? 1 
ATOM   1428  C CA    . VAL A 1 209 ? 20.805  11.997  42.880  1.000 26.656  0 209 VAL AAA CA    1 ? 1 
ATOM   1429  C C     . VAL A 1 209 ? 19.972  11.406  44.022  1.000 27.844  0 209 VAL AAA C     1 ? 1 
ATOM   1430  O O     . VAL A 1 209 ? 20.505  10.629  44.802  1.000 28.760  0 209 VAL AAA O     1 ? 1 
ATOM   1431  C CB    . VAL A 1 209 ? 21.269  10.930  41.860  1.000 25.268  0 209 VAL AAA CB    1 ? 1 
ATOM   1432  C CG1   . VAL A 1 209 ? 20.126  10.125  41.292  1.000 24.943  0 209 VAL AAA CG1   1 ? 1 
ATOM   1433  C CG2   . VAL A 1 209 ? 22.085  11.517  40.732  1.000 25.315  0 209 VAL AAA CG2   1 ? 1 
ATOM   1434  N N     . ILE A 1 210 ? 18.695  11.753  44.093  1.000 29.984  0 210 ILE AAA N     1 ? 1 
ATOM   1435  C CA    . ILE A 1 210 ? 17.720  11.155  45.049  1.000 31.006  0 210 ILE AAA CA    1 ? 1 
ATOM   1436  C C     . ILE A 1 210 ? 16.931  10.096  44.282  1.000 29.104  0 210 ILE AAA C     1 ? 1 
ATOM   1437  O O     . ILE A 1 210 ? 16.298  10.444  43.306  1.000 28.828  0 210 ILE AAA O     1 ? 1 
ATOM   1438  C CB    . ILE A 1 210 ? 16.811  12.233  45.698  1.000 33.316  0 210 ILE AAA CB    1 ? 1 
ATOM   1439  C CG1   . ILE A 1 210 ? 17.610  13.393  46.307  1.000 34.437  0 210 ILE AAA CG1   1 ? 1 
ATOM   1440  C CG2   . ILE A 1 210 ? 15.879  11.630  46.748  1.000 33.333  0 210 ILE AAA CG2   1 ? 1 
ATOM   1441  C CD1   . ILE A 1 210 ? 17.638  14.658  45.485  1.000 34.734  0 210 ILE AAA CD1   1 ? 1 
ATOM   1442  N N     . GLY A 1 211 ? 17.019  8.852   44.732  1.000 28.978  0 211 GLY AAA N     1 ? 1 
ATOM   1443  C CA    . GLY A 1 211 ? 16.342  7.681   44.174  1.000 28.961  0 211 GLY AAA CA    1 ? 1 
ATOM   1444  C C     . GLY A 1 211 ? 17.350  6.649   43.717  1.000 30.462  0 211 GLY AAA C     1 ? 1 
ATOM   1445  O O     . GLY A 1 211 ? 18.249  6.974   42.910  1.000 31.637  0 211 GLY AAA O     1 ? 1 
ATOM   1446  N N     . ALA A 1 212 ? 17.216  5.430   44.233  1.000 29.989  0 212 ALA AAA N     1 ? 1 
ATOM   1447  C CA    . ALA A 1 212 ? 18.003  4.249   43.828  1.000 28.653  0 212 ALA AAA CA    1 ? 1 
ATOM   1448  C C     . ALA A 1 212 ? 17.121  3.355   42.933  1.000 29.045  0 212 ALA AAA C     1 ? 1 
ATOM   1449  O O     . ALA A 1 212 ? 17.322  2.141   42.896  1.000 30.951  0 212 ALA AAA O     1 ? 1 
ATOM   1450  C CB    . ALA A 1 212 ? 18.491  3.570   45.092  1.000 29.103  0 212 ALA AAA CB    1 ? 1 
ATOM   1451  N N     . SER A 1 213 ? 16.134  3.964   42.271  1.000 30.024  0 213 SER AAA N     1 ? 1 
ATOM   1452  C CA    . SER A 1 213 ? 15.453  3.513   41.018  1.000 29.751  0 213 SER AAA CA    1 ? 1 
ATOM   1453  C C     . SER A 1 213 ? 16.480  3.314   39.892  1.000 27.241  0 213 SER AAA C     1 ? 1 
ATOM   1454  O O     . SER A 1 213 ? 17.585  3.895   39.966  1.000 25.856  0 213 SER AAA O     1 ? 1 
ATOM   1455  C CB    . SER A 1 213 ? 14.429  4.547   40.595  1.000 29.518  0 213 SER AAA CB    1 ? 1 
ATOM   1456  O OG    . SER A 1 213 ? 15.125  5.773   40.314  1.000 30.859  0 213 SER AAA OG    1 ? 1 
ATOM   1457  N N     . TYR A 1 214 ? 16.099  2.622   38.829  1.000 27.170  0 214 TYR AAA N     1 ? 1 
ATOM   1458  C CA    . TYR A 1 214 ? 17.000  2.370   37.675  1.000 28.887  0 214 TYR AAA CA    1 ? 1 
ATOM   1459  C C     . TYR A 1 214 ? 17.438  3.707   37.064  1.000 29.512  0 214 TYR AAA C     1 ? 1 
ATOM   1460  O O     . TYR A 1 214 ? 18.617  3.837   36.655  1.000 30.507  0 214 TYR AAA O     1 ? 1 
ATOM   1461  C CB    . TYR A 1 214 ? 16.336  1.396   36.695  1.000 30.662  0 214 TYR AAA CB    1 ? 1 
ATOM   1462  C CG    . TYR A 1 214 ? 15.442  1.954   35.610  1.000 31.705  0 214 TYR AAA CG    1 ? 1 
ATOM   1463  C CD1   . TYR A 1 214 ? 15.975  2.333   34.381  1.000 31.988  0 214 TYR AAA CD1   1 ? 1 
ATOM   1464  C CD2   . TYR A 1 214 ? 14.066  2.003   35.757  1.000 31.776  0 214 TYR AAA CD2   1 ? 1 
ATOM   1465  C CE1   . TYR A 1 214 ? 15.179  2.771   33.339  1.000 32.630  0 214 TYR AAA CE1   1 ? 1 
ATOM   1466  C CE2   . TYR A 1 214 ? 13.256  2.444   34.719  1.000 32.084  0 214 TYR AAA CE2   1 ? 1 
ATOM   1467  C CZ    . TYR A 1 214 ? 13.810  2.816   33.503  1.000 31.827  0 214 TYR AAA CZ    1 ? 1 
ATOM   1468  O OH    . TYR A 1 214 ? 13.063  3.262   32.450  1.000 33.743  0 214 TYR AAA OH    1 ? 1 
ATOM   1469  N N     . ILE A 1 215 ? 16.555  4.709   37.029  1.000 29.142  0 215 ILE AAA N     1 ? 1 
ATOM   1470  C CA    . ILE A 1 215 ? 16.888  6.010   36.397  1.000 28.858  0 215 ILE AAA CA    1 ? 1 
ATOM   1471  C C     . ILE A 1 215 ? 18.006  6.637   37.220  1.000 27.878  0 215 ILE AAA C     1 ? 1 
ATOM   1472  O O     . ILE A 1 215 ? 19.018  7.034   36.634  1.000 29.068  0 215 ILE AAA O     1 ? 1 
ATOM   1473  C CB    . ILE A 1 215 ? 15.621  6.888   36.229  1.000 28.759  0 215 ILE AAA CB    1 ? 1 
ATOM   1474  C CG1   . ILE A 1 215 ? 14.741  6.303   35.125  1.000 28.154  0 215 ILE AAA CG1   1 ? 1 
ATOM   1475  C CG2   . ILE A 1 215 ? 16.001  8.335   35.942  1.000 29.457  0 215 ILE AAA CG2   1 ? 1 
ATOM   1476  C CD1   . ILE A 1 215 ? 13.289  6.738   35.123  1.000 29.241  0 215 ILE AAA CD1   1 ? 1 
ATOM   1477  N N     . GLY A 1 216 ? 17.819  6.679   38.539  1.000 29.020  0 216 GLY AAA N     1 ? 1 
ATOM   1478  C CA    . GLY A 1 216 ? 18.771  7.224   39.513  1.000 27.449  0 216 GLY AAA CA    1 ? 1 
ATOM   1479  C C     . GLY A 1 216 ? 20.127  6.557   39.425  1.000 26.616  0 216 GLY AAA C     1 ? 1 
ATOM   1480  O O     . GLY A 1 216 ? 21.137  7.280   39.344  1.000 27.214  0 216 GLY AAA O     1 ? 1 
ATOM   1481  N N     . LEU A 1 217 ? 20.168  5.231   39.472  1.000 25.752  0 217 LEU AAA N     1 ? 1 
ATOM   1482  C CA    . LEU A 1 217 ? 21.439  4.457   39.469  1.000 25.607  0 217 LEU AAA CA    1 ? 1 
ATOM   1483  C C     . LEU A 1 217 ? 22.138  4.666   38.128  1.000 26.360  0 217 LEU AAA C     1 ? 1 
ATOM   1484  O O     . LEU A 1 217 ? 23.364  4.930   38.160  1.000 27.594  0 217 LEU AAA O     1 ? 1 
ATOM   1485  C CB    . LEU A 1 217 ? 21.192  2.973   39.758  1.000 24.662  0 217 LEU AAA CB    1 ? 1 
ATOM   1486  C CG    . LEU A 1 217 ? 20.818  2.622   41.207  1.000 25.732  0 217 LEU AAA CG    1 ? 1 
ATOM   1487  C CD1   . LEU A 1 217 ? 20.987  1.133   41.507  1.000 26.367  0 217 LEU AAA CD1   1 ? 1 
ATOM   1488  C CD2   . LEU A 1 217 ? 21.633  3.405   42.210  1.000 25.913  0 217 LEU AAA CD2   1 ? 1 
ATOM   1489  N N     . GLU A 1 218 ? 21.418  4.539   37.006  1.000 25.839  0 218 GLU AAA N     1 ? 1 
ATOM   1490  C CA    . GLU A 1 218 ? 22.010  4.745   35.655  1.000 26.702  0 218 GLU AAA CA    1 ? 1 
ATOM   1491  C C     . GLU A 1 218 ? 22.619  6.144   35.589  1.000 26.593  0 218 GLU AAA C     1 ? 1 
ATOM   1492  O O     . GLU A 1 218 ? 23.749  6.287   35.143  1.000 26.853  0 218 GLU AAA O     1 ? 1 
ATOM   1493  C CB    . GLU A 1 218 ? 20.990  4.625   34.531  1.000 28.007  0 218 GLU AAA CB    1 ? 1 
ATOM   1494  C CG    . GLU A 1 218 ? 20.469  3.226   34.310  1.000 28.050  0 218 GLU AAA CG    1 ? 1 
ATOM   1495  C CD    . GLU A 1 218 ? 19.428  3.129   33.212  1.000 28.437  0 218 GLU AAA CD    1 ? 1 
ATOM   1496  O OE1   . GLU A 1 218 ? 18.758  4.107   32.945  1.000 28.523  0 218 GLU AAA OE1   1 ? 1 
ATOM   1497  O OE2   . GLU A 1 218 ? 19.296  2.047   32.636  1.000 31.180  0 218 GLU AAA OE2   1 ? 1 
ATOM   1498  N N     . THR A 1 219 ? 21.869  7.146   36.039  1.000 26.522  0 219 THR AAA N     1 ? 1 
ATOM   1499  C CA    . THR A 1 219 ? 22.285  8.567   35.976  1.000 24.814  0 219 THR AAA CA    1 ? 1 
ATOM   1500  C C     . THR A 1 219 ? 23.536  8.783   36.837  1.000 25.111  0 219 THR AAA C     1 ? 1 
ATOM   1501  O O     . THR A 1 219 ? 24.532  9.417   36.365  1.000 22.608  0 219 THR AAA O     1 ? 1 
ATOM   1502  C CB    . THR A 1 219 ? 21.138  9.472   36.356  1.000 24.013  0 219 THR AAA CB    1 ? 1 
ATOM   1503  O OG1   . THR A 1 219 ? 20.039  9.070   35.539  1.000 23.218  0 219 THR AAA OG1   1 ? 1 
ATOM   1504  C CG2   . THR A 1 219 ? 21.493  10.932  36.152  1.000 25.327  0 219 THR AAA CG2   1 ? 1 
ATOM   1505  N N     . ALA A 1 220 ? 23.496  8.295   38.074  1.000 25.340  0 220 ALA AAA N     1 ? 1 
ATOM   1506  C CA    . ALA A 1 220 ? 24.624  8.459   39.016  1.000 26.048  0 220 ALA AAA CA    1 ? 1 
ATOM   1507  C C     . ALA A 1 220 ? 25.849  7.729   38.447  1.000 24.588  0 220 ALA AAA C     1 ? 1 
ATOM   1508  O O     . ALA A 1 220 ? 26.970  8.250   38.535  1.000 23.307  0 220 ALA AAA O     1 ? 1 
ATOM   1509  C CB    . ALA A 1 220 ? 24.211  7.918   40.374  1.000 26.738  0 220 ALA AAA CB    1 ? 1 
ATOM   1510  N N     . GLY A 1 221 ? 25.608  6.520   37.932  1.000 24.172  0 221 GLY AAA N     1 ? 1 
ATOM   1511  C CA    . GLY A 1 221 ? 26.626  5.645   37.330  1.000 24.733  0 221 GLY AAA CA    1 ? 1 
ATOM   1512  C C     . GLY A 1 221 ? 27.364  6.343   36.210  1.000 25.068  0 221 GLY AAA C     1 ? 1 
ATOM   1513  O O     . GLY A 1 221 ? 28.624  6.277   36.233  1.000 25.574  0 221 GLY AAA O     1 ? 1 
ATOM   1514  N N     . PHE A 1 222 ? 26.673  6.988   35.267  1.000 24.875  0 222 PHE AAA N     1 ? 1 
ATOM   1515  C CA    . PHE A 1 222 ? 27.396  7.653   34.150  1.000 27.457  0 222 PHE AAA CA    1 ? 1 
ATOM   1516  C C     . PHE A 1 222 ? 28.034  8.963   34.645  1.000 27.261  0 222 PHE AAA C     1 ? 1 
ATOM   1517  O O     . PHE A 1 222 ? 29.164  9.287   34.212  1.000 28.173  0 222 PHE AAA O     1 ? 1 
ATOM   1518  C CB    . PHE A 1 222 ? 26.577  7.691   32.847  1.000 28.060  0 222 PHE AAA CB    1 ? 1 
ATOM   1519  C CG    . PHE A 1 222 ? 25.408  8.637   32.797  1.000 29.186  0 222 PHE AAA CG    1 ? 1 
ATOM   1520  C CD1   . PHE A 1 222 ? 25.594  10.004  32.844  1.000 30.871  0 222 PHE AAA CD1   1 ? 1 
ATOM   1521  C CD2   . PHE A 1 222 ? 24.132  8.161   32.619  1.000 29.545  0 222 PHE AAA CD2   1 ? 1 
ATOM   1522  C CE1   . PHE A 1 222 ? 24.514  10.872  32.796  1.000 31.605  0 222 PHE AAA CE1   1 ? 1 
ATOM   1523  C CE2   . PHE A 1 222 ? 23.055  9.027   32.558  1.000 30.398  0 222 PHE AAA CE2   1 ? 1 
ATOM   1524  C CZ    . PHE A 1 222 ? 23.243  10.381  32.672  1.000 30.792  0 222 PHE AAA CZ    1 ? 1 
ATOM   1525  N N     . LEU A 1 223 ? 27.417  9.701   35.557  1.000 27.860  0 223 LEU AAA N     1 ? 1 
ATOM   1526  C CA    . LEU A 1 223 ? 28.057  10.955  36.039  1.000 29.208  0 223 LEU AAA CA    1 ? 1 
ATOM   1527  C C     . LEU A 1 223 ? 29.359  10.614  36.770  1.000 29.907  0 223 LEU AAA C     1 ? 1 
ATOM   1528  O O     . LEU A 1 223 ? 30.356  11.343  36.580  1.000 31.044  0 223 LEU AAA O     1 ? 1 
ATOM   1529  C CB    . LEU A 1 223 ? 27.090  11.753  36.925  1.000 29.324  0 223 LEU AAA CB    1 ? 1 
ATOM   1530  C CG    . LEU A 1 223 ? 25.918  12.389  36.184  1.000 30.153  0 223 LEU AAA CG    1 ? 1 
ATOM   1531  C CD1   . LEU A 1 223 ? 25.032  13.143  37.141  1.000 30.767  0 223 LEU AAA CD1   1 ? 1 
ATOM   1532  C CD2   . LEU A 1 223 ? 26.372  13.318  35.067  1.000 30.613  0 223 LEU AAA CD2   1 ? 1 
ATOM   1533  N N     . ASN A 1 224 ? 29.383  9.531   37.547  1.000 29.651  0 224 ASN AAA N     1 ? 1 
ATOM   1534  C CA    . ASN A 1 224 ? 30.619  9.093   38.249  1.000 31.391  0 224 ASN AAA CA    1 ? 1 
ATOM   1535  C C     . ASN A 1 224 ? 31.666  8.656   37.216  1.000 32.773  0 224 ASN AAA C     1 ? 1 
ATOM   1536  O O     . ASN A 1 224 ? 32.817  9.111   37.317  1.000 32.940  0 224 ASN AAA O     1 ? 1 
ATOM   1537  C CB    . ASN A 1 224 ? 30.343  7.995   39.265  1.000 31.061  0 224 ASN AAA CB    1 ? 1 
ATOM   1538  C CG    . ASN A 1 224 ? 31.577  7.560   40.014  1.000 30.227  0 224 ASN AAA CG    1 ? 1 
ATOM   1539  O OD1   . ASN A 1 224 ? 32.002  8.232   40.920  1.000 30.531  0 224 ASN AAA OD1   1 ? 1 
ATOM   1540  N ND2   . ASN A 1 224 ? 32.123  6.410   39.664  1.000 30.455  0 224 ASN AAA ND2   1 ? 1 
ATOM   1541  N N     . GLU A 1 225 ? 31.289  7.807   36.262  1.000 33.630  0 225 GLU AAA N     1 ? 1 
ATOM   1542  C CA    . GLU A 1 225 ? 32.214  7.317   35.212  0.940 34.066  0 225 GLU AAA CA    1 ? 1 
ATOM   1543  C C     . GLU A 1 225 ? 32.799  8.510   34.453  1.000 33.955  0 225 GLU AAA C     1 ? 1 
ATOM   1544  O O     . GLU A 1 225 ? 33.974  8.413   33.992  1.000 32.133  0 225 GLU AAA O     1 ? 1 
ATOM   1545  C CB    . GLU A 1 225 ? 31.522  6.343   34.257  0.940 36.778  0 225 GLU AAA CB    1 ? 1 
ATOM   1546  C CG    . GLU A 1 225 ? 31.762  4.882   34.581  0.940 38.306  0 225 GLU AAA CG    1 ? 1 
ATOM   1547  C CD    . GLU A 1 225 ? 31.092  3.856   33.688  0.940 39.483  0 225 GLU AAA CD    1 ? 1 
ATOM   1548  O OE1   . GLU A 1 225 ? 29.843  3.786   33.708  0.940 41.092  0 225 GLU AAA OE1   1 ? 1 
ATOM   1549  O OE2   . GLU A 1 225 ? 31.832  3.094   33.003  0.940 41.927  0 225 GLU AAA OE2   1 ? 1 
ATOM   1550  N N     . LEU A 1 226 ? 32.049  9.609   34.348  1.000 33.776  0 226 LEU AAA N     1 ? 1 
ATOM   1551  C CA    . LEU A 1 226 ? 32.465  10.800  33.558  1.000 35.265  0 226 LEU AAA CA    1 ? 1 
ATOM   1552  C C     . LEU A 1 226 ? 33.283  11.768  34.419  1.000 36.904  0 226 LEU AAA C     1 ? 1 
ATOM   1553  O O     . LEU A 1 226 ? 33.624  12.873  33.904  1.000 33.935  0 226 LEU AAA O     1 ? 1 
ATOM   1554  C CB    . LEU A 1 226 ? 31.231  11.498  32.986  1.000 34.157  0 226 LEU AAA CB    1 ? 1 
ATOM   1555  C CG    . LEU A 1 226 ? 30.583  10.832  31.773  1.000 33.764  0 226 LEU AAA CG    1 ? 1 
ATOM   1556  C CD1   . LEU A 1 226 ? 29.315  11.589  31.394  1.000 33.543  0 226 LEU AAA CD1   1 ? 1 
ATOM   1557  C CD2   . LEU A 1 226 ? 31.554  10.730  30.601  1.000 32.018  0 226 LEU AAA CD2   1 ? 1 
ATOM   1558  N N     . GLY A 1 227 ? 33.547  11.391  35.680  1.000 37.549  0 227 GLY AAA N     1 ? 1 
ATOM   1559  C CA    . GLY A 1 227 ? 34.502  12.078  36.568  1.000 38.763  0 227 GLY AAA CA    1 ? 1 
ATOM   1560  C C     . GLY A 1 227 ? 33.844  13.035  37.551  1.000 39.719  0 227 GLY AAA C     1 ? 1 
ATOM   1561  O O     . GLY A 1 227 ? 34.573  13.736  38.241  1.000 42.722  0 227 GLY AAA O     1 ? 1 
ATOM   1562  N N     . PHE A 1 228 ? 32.510  13.085  37.628  1.000 39.509  0 228 PHE AAA N     1 ? 1 
ATOM   1563  C CA    . PHE A 1 228 ? 31.782  14.010  38.546  1.000 37.242  0 228 PHE AAA CA    1 ? 1 
ATOM   1564  C C     . PHE A 1 228 ? 31.674  13.384  39.941  1.000 35.679  0 228 PHE AAA C     1 ? 1 
ATOM   1565  O O     . PHE A 1 228 ? 31.516  12.156  40.031  1.000 35.945  0 228 PHE AAA O     1 ? 1 
ATOM   1566  C CB    . PHE A 1 228 ? 30.433  14.386  37.945  1.000 35.748  0 228 PHE AAA CB    1 ? 1 
ATOM   1567  C CG    . PHE A 1 228 ? 30.571  15.131  36.651  1.000 35.398  0 228 PHE AAA CG    1 ? 1 
ATOM   1568  C CD1   . PHE A 1 228 ? 31.135  16.391  36.623  1.000 35.726  0 228 PHE AAA CD1   1 ? 1 
ATOM   1569  C CD2   . PHE A 1 228 ? 30.176  14.556  35.449  1.000 35.811  0 228 PHE AAA CD2   1 ? 1 
ATOM   1570  C CE1   . PHE A 1 228 ? 31.251  17.087  35.429  1.000 36.784  0 228 PHE AAA CE1   1 ? 1 
ATOM   1571  C CE2   . PHE A 1 228 ? 30.283  15.255  34.257  1.000 34.507  0 228 PHE AAA CE2   1 ? 1 
ATOM   1572  C CZ    . PHE A 1 228 ? 30.841  16.510  34.247  1.000 36.046  0 228 PHE AAA CZ    1 ? 1 
ATOM   1573  N N     . ASP A 1 229 ? 31.793  14.213  40.982  1.000 35.618  0 229 ASP AAA N     1 ? 1 
ATOM   1574  C CA    . ASP A 1 229 ? 31.608  13.862  42.416  1.000 34.131  0 229 ASP AAA CA    1 ? 1 
ATOM   1575  C C     . ASP A 1 229 ? 30.122  13.543  42.622  1.000 32.976  0 229 ASP AAA C     1 ? 1 
ATOM   1576  O O     . ASP A 1 229 ? 29.272  14.443  42.514  1.000 32.655  0 229 ASP AAA O     1 ? 1 
ATOM   1577  C CB    . ASP A 1 229 ? 32.108  14.982  43.325  1.000 35.598  0 229 ASP AAA CB    1 ? 1 
ATOM   1578  C CG    . ASP A 1 229 ? 32.045  14.705  44.834  1.000 37.280  0 229 ASP AAA CG    1 ? 1 
ATOM   1579  O OD1   . ASP A 1 229 ? 31.214  13.885  45.266  1.000 34.968  0 229 ASP AAA OD1   1 ? 1 
ATOM   1580  O OD2   . ASP A 1 229 ? 32.820  15.360  45.595  1.000 40.222  0 229 ASP AAA OD2   1 ? 1 
ATOM   1581  N N     . THR A 1 230 ? 29.814  12.280  42.867  1.000 30.892  0 230 THR AAA N     1 ? 1 
ATOM   1582  C CA    . THR A 1 230 ? 28.450  11.750  42.747  1.000 30.670  0 230 THR AAA CA    1 ? 1 
ATOM   1583  C C     . THR A 1 230 ? 28.005  11.096  44.050  1.000 28.526  0 230 THR AAA C     1 ? 1 
ATOM   1584  O O     . THR A 1 230 ? 28.757  10.281  44.577  1.000 26.867  0 230 THR AAA O     1 ? 1 
ATOM   1585  C CB    . THR A 1 230 ? 28.382  10.821  41.524  1.000 31.908  0 230 THR AAA CB    1 ? 1 
ATOM   1586  O OG1   . THR A 1 230 ? 28.680  11.624  40.373  1.000 34.005  0 230 THR AAA OG1   1 ? 1 
ATOM   1587  C CG2   . THR A 1 230 ? 27.024  10.173  41.382  1.000 32.484  0 230 THR AAA CG2   1 ? 1 
ATOM   1588  N N     . THR A 1 231 ? 26.761  11.373  44.459  1.000 28.034  0 231 THR AAA N     1 ? 1 
ATOM   1589  C CA    . THR A 1 231 ? 26.146  10.846  45.698  1.000 28.466  0 231 THR AAA CA    1 ? 1 
ATOM   1590  C C     . THR A 1 231 ? 24.725  10.414  45.377  1.000 28.747  0 231 THR AAA C     1 ? 1 
ATOM   1591  O O     . THR A 1 231 ? 24.029  11.191  44.709  1.000 29.763  0 231 THR AAA O     1 ? 1 
ATOM   1592  C CB    . THR A 1 231 ? 26.242  11.885  46.834  1.000 29.509  0 231 THR AAA CB    1 ? 1 
ATOM   1593  O OG1   . THR A 1 231 ? 27.620  12.190  47.015  1.000 28.995  0 231 THR AAA OG1   1 ? 1 
ATOM   1594  C CG2   . THR A 1 231 ? 25.697  11.410  48.160  1.000 29.891  0 231 THR AAA CG2   1 ? 1 
ATOM   1595  N N     . VAL A 1 232 ? 24.327  9.225   45.815  1.000 27.712  0 232 VAL AAA N     1 ? 1 
ATOM   1596  C CA    . VAL A 1 232 ? 22.931  8.747   45.730  1.000 28.407  0 232 VAL AAA CA    1 ? 1 
ATOM   1597  C C     . VAL A 1 232 ? 22.344  8.705   47.142  1.000 30.704  0 232 VAL AAA C     1 ? 1 
ATOM   1598  O O     . VAL A 1 232 ? 22.927  8.003   47.996  1.000 33.871  0 232 VAL AAA O     1 ? 1 
ATOM   1599  C CB    . VAL A 1 232 ? 22.862  7.362   45.065  1.000 28.373  0 232 VAL AAA CB    1 ? 1 
ATOM   1600  C CG1   . VAL A 1 232 ? 21.471  6.743   45.223  1.000 26.445  0 232 VAL AAA CG1   1 ? 1 
ATOM   1601  C CG2   . VAL A 1 232 ? 23.305  7.415   43.587  1.000 27.586  0 232 VAL AAA CG2   1 ? 1 
ATOM   1602  N N     . ALA A 1 233 ? 21.243  9.436   47.372  1.000 30.004  0 233 ALA AAA N     1 ? 1 
ATOM   1603  C CA    . ALA A 1 233 ? 20.380  9.344   48.569  1.000 31.320  0 233 ALA AAA CA    1 ? 1 
ATOM   1604  C C     . ALA A 1 233 ? 19.304  8.274   48.307  1.000 32.085  0 233 ALA AAA C     1 ? 1 
ATOM   1605  O O     . ALA A 1 233 ? 18.424  8.502   47.493  1.000 29.950  0 233 ALA AAA O     1 ? 1 
ATOM   1606  C CB    . ALA A 1 233 ? 19.762  10.678  48.892  1.000 31.280  0 233 ALA AAA CB    1 ? 1 
ATOM   1607  N N     . MET A 1 234 ? 19.486  7.118   48.933  1.000 32.616  0 234 MET AAA N     1 ? 1 
ATOM   1608  C CA    . MET A 1 234 ? 18.690  5.891   48.810  1.000 33.626  0 234 MET AAA CA    1 ? 1 
ATOM   1609  C C     . MET A 1 234 ? 17.836  5.789   50.072  1.000 35.617  0 234 MET AAA C     1 ? 1 
ATOM   1610  O O     . MET A 1 234 ? 18.402  5.631   51.179  1.000 36.451  0 234 MET AAA O     1 ? 1 
ATOM   1611  C CB    . MET A 1 234 ? 19.651  4.705   48.689  1.000 34.969  0 234 MET AAA CB    1 ? 1 
ATOM   1612  C CG    . MET A 1 234 ? 18.995  3.375   48.733  1.000 35.464  0 234 MET AAA CG    1 ? 1 
ATOM   1613  S SD    . MET A 1 234 ? 20.018  2.066   48.019  1.000 35.890  0 234 MET AAA SD    1 ? 1 
ATOM   1614  C CE    . MET A 1 234 ? 21.451  2.059   49.094  1.000 40.055  0 234 MET AAA CE    1 ? 1 
ATOM   1615  N N     . ARG A 1 235 ? 16.524  5.970   49.921  1.000 37.319  0 235 ARG AAA N     1 ? 1 
ATOM   1616  C CA    . ARG A 1 235 ? 15.561  5.908   51.044  1.000 39.399  0 235 ARG AAA CA    1 ? 1 
ATOM   1617  C C     . ARG A 1 235 ? 15.680  4.554   51.770  1.000 40.299  0 235 ARG AAA C     1 ? 1 
ATOM   1618  O O     . ARG A 1 235 ? 15.713  4.542   53.037  1.000 44.831  0 235 ARG AAA O     1 ? 1 
ATOM   1619  C CB    . ARG A 1 235 ? 14.135  6.156   50.546  1.000 41.007  0 235 ARG AAA CB    1 ? 1 
ATOM   1620  C CG    . ARG A 1 235 ? 13.175  6.385   51.696  1.000 44.953  0 235 ARG AAA CG    1 ? 1 
ATOM   1621  C CD    . ARG A 1 235 ? 11.857  7.076   51.327  1.000 47.162  0 235 ARG AAA CD    1 ? 1 
ATOM   1622  N NE    . ARG A 1 235 ? 11.317  7.683   52.540  1.000 49.040  0 235 ARG AAA NE    1 ? 1 
ATOM   1623  C CZ    . ARG A 1 235 ? 10.752  6.998   53.543  1.000 51.216  0 235 ARG AAA CZ    1 ? 1 
ATOM   1624  N NH1   . ARG A 1 235 ? 10.589  5.681   53.458  1.000 50.792  0 235 ARG AAA NH1   1 ? 1 
ATOM   1625  N NH2   . ARG A 1 235 ? 10.313  7.637   54.617  1.000 51.611  0 235 ARG AAA NH2   1 ? 1 
ATOM   1626  N N     . SER A 1 236 ? 15.753  3.440   51.030  1.000 36.352  0 236 SER AAA N     1 ? 1 
ATOM   1627  C CA    . SER A 1 236 ? 15.823  2.079   51.615  1.000 34.058  0 236 SER AAA CA    1 ? 1 
ATOM   1628  C C     . SER A 1 236 ? 16.757  1.196   50.780  1.000 33.420  0 236 SER AAA C     1 ? 1 
ATOM   1629  O O     . SER A 1 236 ? 17.906  1.008   51.185  1.000 32.370  0 236 SER AAA O     1 ? 1 
ATOM   1630  C CB    . SER A 1 236 ? 14.432  1.476   51.767  1.000 32.578  0 236 SER AAA CB    1 ? 1 
ATOM   1631  O OG    . SER A 1 236 ? 13.693  1.566   50.565  1.000 30.747  0 236 SER AAA OG    1 ? 1 
ATOM   1632  N N     . ILE A 1 237 ? 16.268  0.669   49.654  1.000 33.084  0 237 ILE AAA N     1 ? 1 
ATOM   1633  C CA    . ILE A 1 237 ? 16.951  -0.423  48.898  1.000 32.162  0 237 ILE AAA CA    1 ? 1 
ATOM   1634  C C     . ILE A 1 237 ? 17.108  0.001   47.454  1.000 29.962  0 237 ILE AAA C     1 ? 1 
ATOM   1635  O O     . ILE A 1 237 ? 16.329  0.798   46.956  1.000 31.657  0 237 ILE AAA O     1 ? 1 
ATOM   1636  C CB    . ILE A 1 237 ? 16.193  -1.758  49.044  1.000 31.522  0 237 ILE AAA CB    1 ? 1 
ATOM   1637  C CG1   . ILE A 1 237 ? 14.783  -1.676  48.458  1.000 32.090  0 237 ILE AAA CG1   1 ? 1 
ATOM   1638  C CG2   . ILE A 1 237 ? 16.222  -2.229  50.497  1.000 31.891  0 237 ILE AAA CG2   1 ? 1 
ATOM   1639  C CD1   . ILE A 1 237 ? 14.052  -3.014  48.383  1.000 33.618  0 237 ILE AAA CD1   1 ? 1 
ATOM   1640  N N     . PRO A 1 238 ? 18.128  -0.528  46.753  1.000 29.933  0 238 PRO AAA N     1 ? 1 
ATOM   1641  C CA    . PRO A 1 238 ? 18.293  -0.281  45.311  1.000 28.759  0 238 PRO AAA CA    1 ? 1 
ATOM   1642  C C     . PRO A 1 238 ? 17.355  -1.100  44.414  1.000 27.582  0 238 PRO AAA C     1 ? 1 
ATOM   1643  O O     . PRO A 1 238 ? 17.188  -2.270  44.655  1.000 28.398  0 238 PRO AAA O     1 ? 1 
ATOM   1644  C CB    . PRO A 1 238 ? 19.763  -0.675  45.071  1.000 27.847  0 238 PRO AAA CB    1 ? 1 
ATOM   1645  C CG    . PRO A 1 238 ? 20.041  -1.748  46.102  1.000 28.182  0 238 PRO AAA CG    1 ? 1 
ATOM   1646  C CD    . PRO A 1 238 ? 19.206  -1.371  47.321  1.000 29.753  0 238 PRO AAA CD    1 ? 1 
ATOM   1647  N N     . LEU A 1 239 ? 16.808  -0.476  43.373  1.000 26.624  0 239 LEU AAA N     1 ? 1 
ATOM   1648  C CA    . LEU A 1 239 ? 16.019  -1.168  42.333  1.000 26.871  0 239 LEU AAA CA    1 ? 1 
ATOM   1649  C C     . LEU A 1 239 ? 14.921  -2.033  42.970  1.000 27.988  0 239 LEU AAA C     1 ? 1 
ATOM   1650  O O     . LEU A 1 239 ? 14.905  -3.271  42.751  1.000 27.740  0 239 LEU AAA O     1 ? 1 
ATOM   1651  C CB    . LEU A 1 239 ? 16.990  -2.047  41.553  1.000 27.721  0 239 LEU AAA CB    1 ? 1 
ATOM   1652  C CG    . LEU A 1 239 ? 18.159  -1.340  40.873  1.000 27.992  0 239 LEU AAA CG    1 ? 1 
ATOM   1653  C CD1   . LEU A 1 239 ? 18.953  -2.349  40.086  1.000 27.521  0 239 LEU AAA CD1   1 ? 1 
ATOM   1654  C CD2   . LEU A 1 239 ? 17.659  -0.259  39.925  1.000 29.225  0 239 LEU AAA CD2   1 ? 1 
ATOM   1655  N N     . ARG A 1 240 ? 14.049  -1.419  43.759  1.000 28.563  0 240 ARG AAA N     1 ? 1 
ATOM   1656  C CA    . ARG A 1 240 ? 12.862  -2.086  44.342  1.000 29.416  0 240 ARG AAA CA    1 ? 1 
ATOM   1657  C C     . ARG A 1 240 ? 12.085  -2.869  43.276  1.000 29.534  0 240 ARG AAA C     1 ? 1 
ATOM   1658  O O     . ARG A 1 240 ? 11.713  -2.266  42.260  1.000 28.097  0 240 ARG AAA O     1 ? 1 
ATOM   1659  C CB    . ARG A 1 240 ? 11.955  -1.041  44.991  1.000 30.454  0 240 ARG AAA CB    1 ? 1 
ATOM   1660  C CG    . ARG A 1 240 ? 10.933  -1.643  45.942  1.000 33.082  0 240 ARG AAA CG    1 ? 1 
ATOM   1661  C CD    . ARG A 1 240 ? 10.121  -0.580  46.633  1.000 33.398  0 240 ARG AAA CD    1 ? 1 
ATOM   1662  N NE    . ARG A 1 240 ? 10.910  -0.054  47.742  1.000 34.076  0 240 ARG AAA NE    1 ? 1 
ATOM   1663  C CZ    . ARG A 1 240 ? 11.023  -0.610  48.944  1.000 34.615  0 240 ARG AAA CZ    1 ? 1 
ATOM   1664  N NH1   . ARG A 1 240 ? 10.410  -1.749  49.198  1.000 36.266  0 240 ARG AAA NH1   1 ? 1 
ATOM   1665  N NH2   . ARG A 1 240 ? 11.780  -0.054  49.874  1.000 34.186  0 240 ARG AAA NH2   1 ? 1 
ATOM   1666  N N     . GLY A 1 241 ? 11.812  -4.158  43.543  1.000 32.163  0 241 GLY AAA N     1 ? 1 
ATOM   1667  C CA    . GLY A 1 241 ? 11.050  -5.081  42.671  1.000 32.976  0 241 GLY AAA CA    1 ? 1 
ATOM   1668  C C     . GLY A 1 241 ? 11.993  -6.018  41.935  1.000 33.001  0 241 GLY AAA C     1 ? 1 
ATOM   1669  O O     . GLY A 1 241 ? 11.564  -7.152  41.585  1.000 34.036  0 241 GLY AAA O     1 ? 1 
ATOM   1670  N N     . PHE A 1 242 ? 13.246  -5.601  41.761  1.000 31.714  0 242 PHE AAA N     1 ? 1 
ATOM   1671  C CA    . PHE A 1 242 ? 14.287  -6.387  41.057  1.000 29.975  0 242 PHE AAA CA    1 ? 1 
ATOM   1672  C C     . PHE A 1 242 ? 14.930  -7.362  42.045  1.000 28.835  0 242 PHE AAA C     1 ? 1 
ATOM   1673  O O     . PHE A 1 242 ? 14.922  -7.127  43.304  1.000 26.276  0 242 PHE AAA O     1 ? 1 
ATOM   1674  C CB    . PHE A 1 242 ? 15.343  -5.455  40.461  1.000 31.303  0 242 PHE AAA CB    1 ? 1 
ATOM   1675  C CG    . PHE A 1 242 ? 14.913  -4.626  39.271  1.000 32.755  0 242 PHE AAA CG    1 ? 1 
ATOM   1676  C CD1   . PHE A 1 242 ? 13.883  -3.706  39.365  1.000 34.316  0 242 PHE AAA CD1   1 ? 1 
ATOM   1677  C CD2   . PHE A 1 242 ? 15.588  -4.708  38.065  1.000 33.798  0 242 PHE AAA CD2   1 ? 1 
ATOM   1678  C CE1   . PHE A 1 242 ? 13.526  -2.931  38.268  1.000 36.041  0 242 PHE AAA CE1   1 ? 1 
ATOM   1679  C CE2   . PHE A 1 242 ? 15.230  -3.929  36.980  1.000 33.504  0 242 PHE AAA CE2   1 ? 1 
ATOM   1680  C CZ    . PHE A 1 242 ? 14.218  -3.023  37.087  1.000 33.764  0 242 PHE AAA CZ    1 ? 1 
ATOM   1681  N N     . ASP A 1 243 ? 15.502  -8.429  41.486  1.000 27.829  0 243 ASP AAA N     1 ? 1 
ATOM   1682  C CA    . ASP A 1 243 ? 16.282  -9.444  42.244  1.000 28.203  0 243 ASP AAA CA    1 ? 1 
ATOM   1683  C C     . ASP A 1 243 ? 17.271  -8.773  43.211  1.000 27.554  0 243 ASP AAA C     1 ? 1 
ATOM   1684  O O     . ASP A 1 243 ? 18.029  -7.922  42.752  1.000 25.120  0 243 ASP AAA O     1 ? 1 
ATOM   1685  C CB    . ASP A 1 243 ? 17.042  -10.325 41.281  1.000 28.276  0 243 ASP AAA CB    1 ? 1 
ATOM   1686  C CG    . ASP A 1 243 ? 17.790  -11.419 41.992  1.000 30.140  0 243 ASP AAA CG    1 ? 1 
ATOM   1687  O OD1   . ASP A 1 243 ? 17.126  -12.389 42.488  1.000 29.714  0 243 ASP AAA OD1   1 ? 1 
ATOM   1688  O OD2   . ASP A 1 243 ? 19.027  -11.280 42.066  1.000 31.358  0 243 ASP AAA OD2   1 ? 1 
ATOM   1689  N N     . ARG A 1 244 ? 17.230  -9.143  44.495  1.000 27.892  0 244 ARG AAA N     1 ? 1 
ATOM   1690  C CA    . ARG A 1 244 ? 18.023  -8.492  45.571  1.000 29.406  0 244 ARG AAA CA    1 ? 1 
ATOM   1691  C C     . ARG A 1 244 ? 19.513  -8.730  45.299  1.000 28.512  0 244 ARG AAA C     1 ? 1 
ATOM   1692  O O     . ARG A 1 244 ? 20.258  -7.729  45.282  1.000 30.494  0 244 ARG AAA O     1 ? 1 
ATOM   1693  C CB    . ARG A 1 244 ? 17.656  -9.015  46.971  1.000 31.122  0 244 ARG AAA CB    1 ? 1 
ATOM   1694  C CG    . ARG A 1 244 ? 16.274  -8.605  47.478  1.000 31.685  0 244 ARG AAA CG    1 ? 1 
ATOM   1695  C CD    . ARG A 1 244 ? 16.125  -7.099  47.662  1.000 31.881  0 244 ARG AAA CD    1 ? 1 
ATOM   1696  N NE    . ARG A 1 244 ? 15.793  -6.420  46.420  1.000 32.373  0 244 ARG AAA NE    1 ? 1 
ATOM   1697  C CZ    . ARG A 1 244 ? 16.267  -5.234  46.019  1.000 32.888  0 244 ARG AAA CZ    1 ? 1 
ATOM   1698  N NH1   . ARG A 1 244 ? 17.107  -4.517  46.750  1.000 31.748  0 244 ARG AAA NH1   1 ? 1 
ATOM   1699  N NH2   . ARG A 1 244 ? 15.903  -4.770  44.837  1.000 33.884  0 244 ARG AAA NH2   1 ? 1 
ATOM   1700  N N     . GLN A 1 245 ? 19.920  -9.982  45.065  1.000 26.926  0 245 GLN AAA N     1 ? 1 
ATOM   1701  C CA    . GLN A 1 245 ? 21.335  -10.363 44.859  1.000 26.260  0 245 GLN AAA CA    1 ? 1 
ATOM   1702  C C     . GLN A 1 245 ? 21.949  -9.474  43.778  1.000 25.967  0 245 GLN AAA C     1 ? 1 
ATOM   1703  O O     . GLN A 1 245 ? 23.014  -8.881  44.055  1.000 26.659  0 245 GLN AAA O     1 ? 1 
ATOM   1704  C CB    . GLN A 1 245 ? 21.452  -11.841 44.518  1.000 27.068  0 245 GLN AAA CB    1 ? 1 
ATOM   1705  C CG    . GLN A 1 245 ? 22.889  -12.310 44.606  1.000 28.879  0 245 GLN AAA CG    1 ? 1 
ATOM   1706  C CD    . GLN A 1 245 ? 23.057  -13.757 44.204  1.000 31.153  0 245 GLN AAA CD    1 ? 1 
ATOM   1707  O OE1   . GLN A 1 245 ? 22.119  -14.407 43.721  1.000 32.768  0 245 GLN AAA OE1   1 ? 1 
ATOM   1708  N NE2   . GLN A 1 245 ? 24.271  -14.260 44.392  1.000 30.830  0 245 GLN AAA NE2   1 ? 1 
ATOM   1709  N N     . CYS A 1 246 ? 21.322  -9.398  42.595  1.000 25.042  0 246 CYS AAA N     1 ? 1 
ATOM   1710  C CA    . CYS A 1 246 ? 21.791  -8.589  41.430  1.000 24.430  0 246 CYS AAA CA    1 ? 1 
ATOM   1711  C C     . CYS A 1 246 ? 21.757  -7.098  41.761  1.000 24.072  0 246 CYS AAA C     1 ? 1 
ATOM   1712  O O     . CYS A 1 246 ? 22.763  -6.409  41.458  1.000 23.972  0 246 CYS AAA O     1 ? 1 
ATOM   1713  C CB    . CYS A 1 246 ? 20.947  -8.807  40.182  1.000 24.155  0 246 CYS AAA CB    1 ? 1 
ATOM   1714  S SG    . CYS A 1 246 ? 21.082  -10.489 39.541  1.000 26.371  0 246 CYS AAA SG    1 ? 1 
ATOM   1715  N N     . SER A 1 247 ? 20.655  -6.600  42.322  1.000 23.111  0 247 SER AAA N     1 ? 1 
ATOM   1716  C CA    . SER A 1 247 ? 20.539  -5.163  42.658  1.000 24.447  0 247 SER AAA CA    1 ? 1 
ATOM   1717  C C     . SER A 1 247 ? 21.701  -4.757  43.585  1.000 24.631  0 247 SER AAA C     1 ? 1 
ATOM   1718  O O     . SER A 1 247 ? 22.251  -3.673  43.413  1.000 23.030  0 247 SER AAA O     1 ? 1 
ATOM   1719  C CB    . SER A 1 247 ? 19.186  -4.844  43.245  1.000 25.225  0 247 SER AAA CB    1 ? 1 
ATOM   1720  O OG    . SER A 1 247 ? 18.170  -5.172  42.313  1.000 25.690  0 247 SER AAA OG    1 ? 1 
ATOM   1721  N N     . GLU A 1 248 ? 22.099  -5.636  44.502  1.000 25.963  0 248 GLU AAA N     1 ? 1 
ATOM   1722  C CA    . GLU A 1 248 ? 23.118  -5.309  45.538  1.000 27.222  0 248 GLU AAA CA    1 ? 1 
ATOM   1723  C C     . GLU A 1 248 ? 24.534  -5.430  44.951  1.000 25.990  0 248 GLU AAA C     1 ? 1 
ATOM   1724  O O     . GLU A 1 248 ? 25.403  -4.580  45.291  1.000 23.388  0 248 GLU AAA O     1 ? 1 
ATOM   1725  C CB    . GLU A 1 248 ? 22.940  -6.191  46.779  1.000 28.986  0 248 GLU AAA CB    1 ? 1 
ATOM   1726  C CG    . GLU A 1 248 ? 21.774  -5.769  47.656  1.000 31.761  0 248 GLU AAA CG    1 ? 1 
ATOM   1727  C CD    . GLU A 1 248 ? 21.340  -6.862  48.622  1.000 35.405  0 248 GLU AAA CD    1 ? 1 
ATOM   1728  O OE1   . GLU A 1 248 ? 22.220  -7.738  48.915  1.000 37.877  0 248 GLU AAA OE1   1 ? 1 
ATOM   1729  O OE2   . GLU A 1 248 ? 20.147  -6.845  49.080  1.000 33.691  0 248 GLU AAA OE2   1 ? 1 
ATOM   1730  N N     . LYS A 1 249 ? 24.756  -6.408  44.069  1.000 25.875  0 249 LYS AAA N     1 ? 1 
ATOM   1731  C CA    . LYS A 1 249 ? 26.011  -6.445  43.263  1.000 25.858  0 249 LYS AAA CA    1 ? 1 
ATOM   1732  C C     . LYS A 1 249 ? 26.202  -5.095  42.547  1.000 24.022  0 249 LYS AAA C     1 ? 1 
ATOM   1733  O O     . LYS A 1 249 ? 27.317  -4.539  42.651  1.000 23.501  0 249 LYS AAA O     1 ? 1 
ATOM   1734  C CB    . LYS A 1 249 ? 26.052  -7.577  42.240  1.000 25.911  0 249 LYS AAA CB    1 ? 1 
ATOM   1735  C CG    . LYS A 1 249 ? 27.436  -7.676  41.642  1.000 26.655  0 249 LYS AAA CG    1 ? 1 
ATOM   1736  C CD    . LYS A 1 249 ? 27.659  -8.816  40.683  1.000 27.854  0 249 LYS AAA CD    1 ? 1 
ATOM   1737  C CE    . LYS A 1 249 ? 29.057  -8.884  40.096  1.000 27.611  0 249 LYS AAA CE    1 ? 1 
ATOM   1738  N NZ    . LYS A 1 249 ? 30.084  -8.650  41.137  1.000 30.108  0 249 LYS AAA NZ    1 ? 1 
ATOM   1739  N N     . ILE A 1 250 ? 25.163  -4.547  41.904  1.000 22.004  0 250 ILE AAA N     1 ? 1 
ATOM   1740  C CA    . ILE A 1 250 ? 25.330  -3.249  41.193  1.000 23.372  0 250 ILE AAA CA    1 ? 1 
ATOM   1741  C C     . ILE A 1 250 ? 25.836  -2.174  42.168  1.000 23.975  0 250 ILE AAA C     1 ? 1 
ATOM   1742  O O     . ILE A 1 250 ? 26.874  -1.521  41.875  1.000 22.663  0 250 ILE AAA O     1 ? 1 
ATOM   1743  C CB    . ILE A 1 250 ? 24.057  -2.840  40.457  1.000 24.072  0 250 ILE AAA CB    1 ? 1 
ATOM   1744  C CG1   . ILE A 1 250 ? 23.798  -3.797  39.297  1.000 25.595  0 250 ILE AAA CG1   1 ? 1 
ATOM   1745  C CG2   . ILE A 1 250 ? 24.124  -1.422  39.945  1.000 23.905  0 250 ILE AAA CG2   1 ? 1 
ATOM   1746  C CD1   . ILE A 1 250 ? 22.325  -3.943  38.983  1.000 26.686  0 250 ILE AAA CD1   1 ? 1 
ATOM   1747  N N     . VAL A 1 251 ? 25.143  -2.018  43.292  1.000 23.888  0 251 VAL AAA N     1 ? 1 
ATOM   1748  C CA    . VAL A 1 251 ? 25.484  -0.970  44.294  1.000 24.990  0 251 VAL AAA CA    1 ? 1 
ATOM   1749  C C     . VAL A 1 251 ? 26.899  -1.222  44.824  1.000 26.353  0 251 VAL AAA C     1 ? 1 
ATOM   1750  O O     . VAL A 1 251 ? 27.662  -0.255  44.885  1.000 27.001  0 251 VAL AAA O     1 ? 1 
ATOM   1751  C CB    . VAL A 1 251 ? 24.409  -0.917  45.397  1.000 24.900  0 251 VAL AAA CB    1 ? 1 
ATOM   1752  C CG1   . VAL A 1 251 ? 24.858  -0.211  46.669  1.000 24.780  0 251 VAL AAA CG1   1 ? 1 
ATOM   1753  C CG2   . VAL A 1 251 ? 23.145  -0.302  44.837  1.000 23.944  0 251 VAL AAA CG2   1 ? 1 
ATOM   1754  N N     . GLU A 1 252 ? 27.252  -2.474  45.127  1.000 28.273  0 252 GLU AAA N     1 ? 1 
ATOM   1755  C CA    . GLU A 1 252 ? 28.637  -2.860  45.517  1.000 29.222  0 252 GLU AAA CA    1 ? 1 
ATOM   1756  C C     . GLU A 1 252 ? 29.633  -2.345  44.464  1.000 27.489  0 252 GLU AAA C     1 ? 1 
ATOM   1757  O O     . GLU A 1 252 ? 30.638  -1.689  44.861  1.000 28.356  0 252 GLU AAA O     1 ? 1 
ATOM   1758  C CB    . GLU A 1 252 ? 28.693  -4.364  45.773  1.000 32.676  0 252 GLU AAA CB    1 ? 1 
ATOM   1759  C CG    . GLU A 1 252 ? 30.053  -4.860  46.259  1.000 37.154  0 252 GLU AAA CG    1 ? 1 
ATOM   1760  C CD    . GLU A 1 252 ? 30.538  -6.246  45.805  1.000 39.072  0 252 GLU AAA CD    1 ? 1 
ATOM   1761  O OE1   . GLU A 1 252 ? 30.988  -7.020  46.691  1.000 43.082  0 252 GLU AAA OE1   1 ? 1 
ATOM   1762  O OE2   . GLU A 1 252 ? 30.472  -6.555  44.582  1.000 39.818  0 252 GLU AAA OE2   1 ? 1 
ATOM   1763  N N     . TYR A 1 253 ? 29.369  -2.556  43.170  1.000 26.424  0 253 TYR AAA N     1 ? 1 
ATOM   1764  C CA    . TYR A 1 253 ? 30.287  -2.132  42.075  1.000 25.223  0 253 TYR AAA CA    1 ? 1 
ATOM   1765  C C     . TYR A 1 253 ? 30.338  -0.602  42.024  1.000 24.533  0 253 TYR AAA C     1 ? 1 
ATOM   1766  O O     . TYR A 1 253 ? 31.446  -0.005  41.966  1.000 25.282  0 253 TYR AAA O     1 ? 1 
ATOM   1767  C CB    . TYR A 1 253 ? 29.881  -2.754  40.719  1.000 25.584  0 253 TYR AAA CB    1 ? 1 
ATOM   1768  C CG    . TYR A 1 253 ? 30.830  -2.417  39.587  1.000 25.537  0 253 TYR AAA CG    1 ? 1 
ATOM   1769  C CD1   . TYR A 1 253 ? 30.653  -1.270  38.824  1.000 24.765  0 253 TYR AAA CD1   1 ? 1 
ATOM   1770  C CD2   . TYR A 1 253 ? 31.963  -3.193  39.334  1.000 25.936  0 253 TYR AAA CD2   1 ? 1 
ATOM   1771  C CE1   . TYR A 1 253 ? 31.534  -0.938  37.807  1.000 25.270  0 253 TYR AAA CE1   1 ? 1 
ATOM   1772  C CE2   . TYR A 1 253 ? 32.854  -2.871  38.319  1.000 26.133  0 253 TYR AAA CE2   1 ? 1 
ATOM   1773  C CZ    . TYR A 1 253 ? 32.637  -1.734  37.547  1.000 26.213  0 253 TYR AAA CZ    1 ? 1 
ATOM   1774  O OH    . TYR A 1 253 ? 33.471  -1.410  36.506  1.000 26.755  0 253 TYR AAA OH    1 ? 1 
ATOM   1775  N N     . MET A 1 254 ? 29.175  0.054   42.056  1.000 23.784  0 254 MET AAA N     1 ? 1 
ATOM   1776  C CA    . MET A 1 254 ? 29.117  1.528   41.951  1.000 23.746  0 254 MET AAA CA    1 ? 1 
ATOM   1777  C C     . MET A 1 254 ? 29.901  2.178   43.105  1.000 24.310  0 254 MET AAA C     1 ? 1 
ATOM   1778  O O     . MET A 1 254 ? 30.590  3.181   42.852  1.000 23.044  0 254 MET AAA O     1 ? 1 
ATOM   1779  C CB    . MET A 1 254 ? 27.664  1.984   41.957  1.000 23.712  0 254 MET AAA CB    1 ? 1 
ATOM   1780  C CG    . MET A 1 254 ? 26.922  1.486   40.696  1.000 23.133  0 254 MET AAA CG    1 ? 1 
ATOM   1781  S SD    . MET A 1 254 ? 25.285  2.281   40.513  1.000 21.029  0 254 MET AAA SD    1 ? 1 
ATOM   1782  C CE    . MET A 1 254 ? 25.695  4.012   40.581  1.000 21.686  0 254 MET AAA CE    1 ? 1 
ATOM   1783  N N     . LYS A 1 255 ? 29.785  1.637   44.320  1.000 26.046  0 255 LYS AAA N     1 ? 1 
ATOM   1784  C CA    . LYS A 1 255 ? 30.537  2.078   45.526  1.000 28.501  0 255 LYS AAA CA    1 ? 1 
ATOM   1785  C C     . LYS A 1 255 ? 32.050  1.945   45.291  1.000 29.030  0 255 LYS AAA C     1 ? 1 
ATOM   1786  O O     . LYS A 1 255 ? 32.760  2.913   45.578  1.000 28.479  0 255 LYS AAA O     1 ? 1 
ATOM   1787  C CB    . LYS A 1 255 ? 30.186  1.254   46.761  1.000 31.534  0 255 LYS AAA CB    1 ? 1 
ATOM   1788  C CG    . LYS A 1 255 ? 29.059  1.813   47.626  1.000 35.670  0 255 LYS AAA CG    1 ? 1 
ATOM   1789  C CD    . LYS A 1 255 ? 28.631  0.879   48.762  1.000 37.588  0 255 LYS AAA CD    1 ? 1 
ATOM   1790  C CE    . LYS A 1 255 ? 27.688  1.565   49.734  1.000 41.086  0 255 LYS AAA CE    1 ? 1 
ATOM   1791  N NZ    . LYS A 1 255 ? 26.574  0.704   50.227  1.000 43.000  0 255 LYS AAA NZ    1 ? 1 
ATOM   1792  N N     . ALA A 1 256 ? 32.504  0.805   44.745  1.000 27.623  0 256 ALA AAA N     1 ? 1 
ATOM   1793  C CA    . ALA A 1 256 ? 33.935  0.504   44.512  1.000 26.272  0 256 ALA AAA CA    1 ? 1 
ATOM   1794  C C     . ALA A 1 256 ? 34.492  1.404   43.417  1.000 25.551  0 256 ALA AAA C     1 ? 1 
ATOM   1795  O O     . ALA A 1 256 ? 35.722  1.504   43.354  1.000 25.637  0 256 ALA AAA O     1 ? 1 
ATOM   1796  C CB    . ALA A 1 256 ? 34.142  -0.962  44.184  1.000 25.988  0 256 ALA AAA CB    1 ? 1 
ATOM   1797  N N     . THR A 1 257 ? 33.648  2.042   42.598  1.000 24.749  0 257 THR AAA N     1 ? 1 
ATOM   1798  C CA    . THR A 1 257 ? 34.129  2.930   41.504  1.000 23.945  0 257 THR AAA CA    1 ? 1 
ATOM   1799  C C     . THR A 1 257 ? 33.895  4.401   41.827  1.000 23.493  0 257 THR AAA C     1 ? 1 
ATOM   1800  O O     . THR A 1 257 ? 34.169  5.207   40.929  1.000 23.604  0 257 THR AAA O     1 ? 1 
ATOM   1801  C CB    . THR A 1 257 ? 33.529  2.581   40.135  1.000 23.816  0 257 THR AAA CB    1 ? 1 
ATOM   1802  O OG1   . THR A 1 257 ? 32.099  2.594   40.184  1.000 24.280  0 257 THR AAA OG1   1 ? 1 
ATOM   1803  C CG2   . THR A 1 257 ? 34.006  1.239   39.643  1.000 23.813  0 257 THR AAA CG2   1 ? 1 
ATOM   1804  N N     . GLY A 1 258 ? 33.359  4.744   42.997  1.000 23.657  0 258 GLY AAA N     1 ? 1 
ATOM   1805  C CA    . GLY A 1 258 ? 33.393  6.131   43.500  1.000 24.237  0 258 GLY AAA CA    1 ? 1 
ATOM   1806  C C     . GLY A 1 258 ? 32.016  6.760   43.744  1.000 24.326  0 258 GLY AAA C     1 ? 1 
ATOM   1807  O O     . GLY A 1 258 ? 31.949  7.924   44.172  1.000 23.078  0 258 GLY AAA O     1 ? 1 
ATOM   1808  N N     . THR A 1 259 ? 30.919  6.064   43.497  1.000 24.987  0 259 THR AAA N     1 ? 1 
ATOM   1809  C CA    . THR A 1 259 ? 29.581  6.616   43.854  1.000 25.828  0 259 THR AAA CA    1 ? 1 
ATOM   1810  C C     . THR A 1 259 ? 29.389  6.473   45.374  1.000 28.193  0 259 THR AAA C     1 ? 1 
ATOM   1811  O O     . THR A 1 259 ? 29.621  5.371   45.917  1.000 29.073  0 259 THR AAA O     1 ? 1 
ATOM   1812  C CB    . THR A 1 259 ? 28.490  6.007   42.985  1.000 24.734  0 259 THR AAA CB    1 ? 1 
ATOM   1813  O OG1   . THR A 1 259 ? 28.898  6.157   41.608  1.000 23.797  0 259 THR AAA OG1   1 ? 1 
ATOM   1814  C CG2   . THR A 1 259 ? 27.144  6.661   43.255  1.000 25.072  0 259 THR AAA CG2   1 ? 1 
ATOM   1815  N N     . LYS A 1 260 ? 28.995  7.555   46.053  1.000 29.631  0 260 LYS AAA N     1 ? 1 
ATOM   1816  C CA    . LYS A 1 260 ? 28.719  7.500   47.517  1.000 31.368  0 260 LYS AAA CA    1 ? 1 
ATOM   1817  C C     . LYS A 1 260 ? 27.213  7.313   47.689  1.000 31.113  0 260 LYS AAA C     1 ? 1 
ATOM   1818  O O     . LYS A 1 260 ? 26.480  7.886   46.901  1.000 33.639  0 260 LYS AAA O     1 ? 1 
ATOM   1819  C CB    . LYS A 1 260 ? 29.220  8.749   48.244  1.000 32.118  0 260 LYS AAA CB    1 ? 1 
ATOM   1820  C CG    . LYS A 1 260 ? 30.741  8.829   48.353  1.000 33.759  0 260 LYS AAA CG    1 ? 1 
ATOM   1821  C CD    . LYS A 1 260 ? 31.339  10.225  48.519  1.000 34.028  0 260 LYS AAA CD    1 ? 1 
ATOM   1822  C CE    . LYS A 1 260 ? 31.099  11.139  47.331  1.000 34.472  0 260 LYS AAA CE    1 ? 1 
ATOM   1823  N NZ    . LYS A 1 260 ? 31.214  12.567  47.728  1.000 35.226  0 260 LYS AAA NZ    1 ? 1 
ATOM   1824  N N     . PHE A 1 261 ? 26.826  6.475   48.641  1.000 31.434  0 261 PHE AAA N     1 ? 1 
ATOM   1825  C CA    . PHE A 1 261 ? 25.435  6.127   49.014  1.000 33.057  0 261 PHE AAA CA    1 ? 1 
ATOM   1826  C C     . PHE A 1 261 ? 25.163  6.498   50.473  1.000 33.385  0 261 PHE AAA C     1 ? 1 
ATOM   1827  O O     . PHE A 1 261 ? 25.839  5.975   51.352  1.000 32.661  0 261 PHE AAA O     1 ? 1 
ATOM   1828  C CB    . PHE A 1 261 ? 25.173  4.638   48.812  1.000 32.471  0 261 PHE AAA CB    1 ? 1 
ATOM   1829  C CG    . PHE A 1 261 ? 25.124  4.217   47.375  1.000 31.979  0 261 PHE AAA CG    1 ? 1 
ATOM   1830  C CD1   . PHE A 1 261 ? 26.289  4.000   46.651  1.000 33.163  0 261 PHE AAA CD1   1 ? 1 
ATOM   1831  C CD2   . PHE A 1 261 ? 23.909  4.074   46.738  1.000 31.860  0 261 PHE AAA CD2   1 ? 1 
ATOM   1832  C CE1   . PHE A 1 261 ? 26.238  3.604   45.333  1.000 30.394  0 261 PHE AAA CE1   1 ? 1 
ATOM   1833  C CE2   . PHE A 1 261 ? 23.864  3.678   45.418  1.000 31.153  0 261 PHE AAA CE2   1 ? 1 
ATOM   1834  C CZ    . PHE A 1 261 ? 25.028  3.418   44.735  1.000 30.546  0 261 PHE AAA CZ    1 ? 1 
ATOM   1835  N N     . LEU A 1 262 ? 24.183  7.383   50.668  1.000 35.324  0 262 LEU AAA N     1 ? 1 
ATOM   1836  C CA    . LEU A 1 262 ? 23.491  7.677   51.945  1.000 37.985  0 262 LEU AAA CA    1 ? 1 
ATOM   1837  C C     . LEU A 1 262 ? 22.278  6.752   52.065  1.000 38.619  0 262 LEU AAA C     1 ? 1 
ATOM   1838  O O     . LEU A 1 262 ? 21.294  6.986   51.362  1.000 36.154  0 262 LEU AAA O     1 ? 1 
ATOM   1839  C CB    . LEU A 1 262 ? 23.066  9.149   51.919  1.000 39.270  0 262 LEU AAA CB    1 ? 1 
ATOM   1840  C CG    . LEU A 1 262 ? 24.172  10.138  51.559  1.000 40.168  0 262 LEU AAA CG    1 ? 1 
ATOM   1841  C CD1   . LEU A 1 262 ? 23.633  11.560  51.575  1.000 40.519  0 262 LEU AAA CD1   1 ? 1 
ATOM   1842  C CD2   . LEU A 1 262 ? 25.361  9.997   52.524  1.000 40.650  0 262 LEU AAA CD2   1 ? 1 
ATOM   1843  N N     . VAL A 1 263 ? 22.363  5.737   52.917  1.000 41.954  0 263 VAL AAA N     1 ? 1 
ATOM   1844  C CA    . VAL A 1 263 ? 21.317  4.674   53.062  1.000 43.982  0 263 VAL AAA CA    1 ? 1 
ATOM   1845  C C     . VAL A 1 263 ? 20.328  5.078   54.177  1.000 42.954  0 263 VAL AAA C     1 ? 1 
ATOM   1846  O O     . VAL A 1 263 ? 20.794  5.424   55.257  1.000 41.076  0 263 VAL AAA O     1 ? 1 
ATOM   1847  C CB    . VAL A 1 263 ? 21.991  3.320   53.343  1.000 46.545  0 263 VAL AAA CB    1 ? 1 
ATOM   1848  C CG1   . VAL A 1 263 ? 20.978  2.178   53.251  1.000 47.997  0 263 VAL AAA CG1   1 ? 1 
ATOM   1849  C CG2   . VAL A 1 263 ? 23.193  3.083   52.425  1.000 46.532  0 263 VAL AAA CG2   1 ? 1 
ATOM   1850  N N     . GLY A 1 264 ? 19.015  5.104   53.893  1.000 42.286  0 264 GLY AAA N     1 ? 1 
ATOM   1851  C CA    . GLY A 1 264 ? 17.942  5.459   54.841  1.000 43.007  0 264 GLY AAA CA    1 ? 1 
ATOM   1852  C C     . GLY A 1 264 ? 17.900  6.945   55.145  1.000 44.110  0 264 GLY AAA C     1 ? 1 
ATOM   1853  O O     . GLY A 1 264 ? 17.386  7.325   56.213  1.000 43.565  0 264 GLY AAA O     1 ? 1 
ATOM   1854  N N     . VAL A 1 265 ? 18.454  7.758   54.245  1.000 46.463  0 265 VAL AAA N     1 ? 1 
ATOM   1855  C CA    . VAL A 1 265 ? 18.627  9.228   54.391  1.000 46.693  0 265 VAL AAA CA    1 ? 1 
ATOM   1856  C C     . VAL A 1 265 ? 18.100  9.892   53.124  1.000 46.083  0 265 VAL AAA C     1 ? 1 
ATOM   1857  O O     . VAL A 1 265 ? 18.400  9.407   52.049  1.000 49.029  0 265 VAL AAA O     1 ? 1 
ATOM   1858  C CB    . VAL A 1 265 ? 20.099  9.596   54.643  1.000 50.446  0 265 VAL AAA CB    1 ? 1 
ATOM   1859  C CG1   . VAL A 1 265 ? 20.325  11.114  54.556  1.000 52.287  0 265 VAL AAA CG1   1 ? 1 
ATOM   1860  C CG2   . VAL A 1 265 ? 20.616  9.031   55.972  1.000 50.536  0 265 VAL AAA CG2   1 ? 1 
ATOM   1861  N N     . VAL A 1 266 ? 17.299  10.938  53.267  1.000 46.977  0 266 VAL AAA N     1 ? 1 
ATOM   1862  C CA    . VAL A 1 266 ? 16.768  11.742  52.128  1.000 43.996  0 266 VAL AAA CA    1 ? 1 
ATOM   1863  C C     . VAL A 1 266 ? 16.831  13.216  52.518  1.000 42.136  0 266 VAL AAA C     1 ? 1 
ATOM   1864  O O     . VAL A 1 266 ? 16.862  13.575  53.708  1.000 42.291  0 266 VAL AAA O     1 ? 1 
ATOM   1865  C CB    . VAL A 1 266 ? 15.325  11.317  51.759  1.000 47.655  0 266 VAL AAA CB    1 ? 1 
ATOM   1866  C CG1   . VAL A 1 266 ? 15.268  9.850   51.307  1.000 52.490  0 266 VAL AAA CG1   1 ? 1 
ATOM   1867  C CG2   . VAL A 1 266 ? 14.322  11.555  52.881  1.000 45.730  0 266 VAL AAA CG2   1 ? 1 
ATOM   1868  N N     . PRO A 1 267 ? 16.833  14.125  51.523  1.000 38.468  0 267 PRO AAA N     1 ? 1 
ATOM   1869  C CA    . PRO A 1 267 ? 16.724  15.552  51.792  1.000 36.665  0 267 PRO AAA CA    1 ? 1 
ATOM   1870  C C     . PRO A 1 267 ? 15.417  15.903  52.509  1.000 35.330  0 267 PRO AAA C     1 ? 1 
ATOM   1871  O O     . PRO A 1 267 ? 14.376  15.331  52.166  1.000 34.002  0 267 PRO AAA O     1 ? 1 
ATOM   1872  C CB    . PRO A 1 267 ? 16.713  16.220  50.399  1.000 36.612  0 267 PRO AAA CB    1 ? 1 
ATOM   1873  C CG    . PRO A 1 267 ? 17.297  15.183  49.494  1.000 37.548  0 267 PRO AAA CG    1 ? 1 
ATOM   1874  C CD    . PRO A 1 267 ? 16.929  13.833  50.082  1.000 37.560  0 267 PRO AAA CD    1 ? 1 
ATOM   1875  N N     . ILE A 1 268 ? 15.505  16.852  53.451  1.000 35.801  0 268 ILE AAA N     1 ? 1 
ATOM   1876  C CA    . ILE A 1 268 ? 14.326  17.511  54.095  1.000 35.639  0 268 ILE AAA CA    1 ? 1 
ATOM   1877  C C     . ILE A 1 268 ? 14.322  19.008  53.762  1.000 35.267  0 268 ILE AAA C     1 ? 1 
ATOM   1878  O O     . ILE A 1 268 ? 13.300  19.636  53.981  1.000 34.106  0 268 ILE AAA O     1 ? 1 
ATOM   1879  C CB    . ILE A 1 268 ? 14.316  17.242  55.612  1.000 37.071  0 268 ILE AAA CB    1 ? 1 
ATOM   1880  C CG1   . ILE A 1 268 ? 15.585  17.757  56.309  1.000 37.026  0 268 ILE AAA CG1   1 ? 1 
ATOM   1881  C CG2   . ILE A 1 268 ? 14.038  15.755  55.885  1.000 36.276  0 268 ILE AAA CG2   1 ? 1 
ATOM   1882  C CD1   . ILE A 1 268 ? 15.554  17.597  57.804  1.000 37.352  0 268 ILE AAA CD1   1 ? 1 
ATOM   1883  N N     . ASN A 1 269 ? 15.421  19.547  53.230  1.000 35.467  0 269 ASN AAA N     1 ? 1 
ATOM   1884  C CA    . ASN A 1 269 ? 15.501  20.983  52.860  1.000 37.460  0 269 ASN AAA CA    1 ? 1 
ATOM   1885  C C     . ASN A 1 269 ? 16.560  21.188  51.779  1.000 37.078  0 269 ASN AAA C     1 ? 1 
ATOM   1886  O O     . ASN A 1 269 ? 17.626  20.573  51.875  1.000 38.423  0 269 ASN AAA O     1 ? 1 
ATOM   1887  C CB    . ASN A 1 269 ? 15.738  21.920  54.054  1.000 37.096  0 269 ASN AAA CB    1 ? 1 
ATOM   1888  C CG    . ASN A 1 269 ? 15.606  23.380  53.690  1.000 37.769  0 269 ASN AAA CG    1 ? 1 
ATOM   1889  O OD1   . ASN A 1 269 ? 16.591  24.124  53.720  1.000 41.817  0 269 ASN AAA OD1   1 ? 1 
ATOM   1890  N ND2   . ASN A 1 269 ? 14.398  23.791  53.337  1.000 38.351  0 269 ASN AAA ND2   1 ? 1 
ATOM   1891  N N     . ILE A 1 270 ? 16.284  22.104  50.852  1.000 38.548  0 270 ILE AAA N     1 ? 1 
ATOM   1892  C CA    . ILE A 1 270 ? 17.133  22.427  49.675  1.000 41.981  0 270 ILE AAA CA    1 ? 1 
ATOM   1893  C C     . ILE A 1 270 ? 17.167  23.956  49.494  1.000 44.902  0 270 ILE AAA C     1 ? 1 
ATOM   1894  O O     . ILE A 1 270 ? 16.114  24.534  49.218  1.000 45.115  0 270 ILE AAA O     1 ? 1 
ATOM   1895  C CB    . ILE A 1 270 ? 16.615  21.638  48.449  1.000 43.033  0 270 ILE AAA CB    1 ? 1 
ATOM   1896  C CG1   . ILE A 1 270 ? 16.880  20.139  48.645  1.000 43.634  0 270 ILE AAA CG1   1 ? 1 
ATOM   1897  C CG2   . ILE A 1 270 ? 17.224  22.153  47.145  1.000 43.290  0 270 ILE AAA CG2   1 ? 1 
ATOM   1898  C CD1   . ILE A 1 270 ? 16.273  19.230  47.601  1.000 44.444  0 270 ILE AAA CD1   1 ? 1 
ATOM   1899  N N     . GLU A 1 271 ? 18.334  24.588  49.666  1.000 47.324  0 271 GLU AAA N     1 ? 1 
ATOM   1900  C CA    . GLU A 1 271 ? 18.489  26.072  49.632  1.000 52.473  0 271 GLU AAA CA    1 ? 1 
ATOM   1901  C C     . GLU A 1 271 ? 19.701  26.430  48.771  1.000 53.285  0 271 GLU AAA C     1 ? 1 
ATOM   1902  O O     . GLU A 1 271 ? 20.640  25.637  48.737  1.000 48.752  0 271 GLU AAA O     1 ? 1 
ATOM   1903  C CB    . GLU A 1 271 ? 18.649  26.693  51.031  1.000 54.987  0 271 GLU AAA CB    1 ? 1 
ATOM   1904  C CG    . GLU A 1 271 ? 19.309  25.774  52.046  1.000 57.954  0 271 GLU AAA CG    1 ? 1 
ATOM   1905  C CD    . GLU A 1 271 ? 19.470  26.314  53.466  1.000 57.625  0 271 GLU AAA CD    1 ? 1 
ATOM   1906  O OE1   . GLU A 1 271 ? 19.441  27.539  53.637  1.000 59.107  0 271 GLU AAA OE1   1 ? 1 
ATOM   1907  O OE2   . GLU A 1 271 ? 19.601  25.508  54.406  1.000 54.729  0 271 GLU AAA OE2   1 ? 1 
ATOM   1908  N N     . LYS A 1 272 ? 19.660  27.588  48.110  1.000 58.946  0 272 LYS AAA N     1 ? 1 
ATOM   1909  C CA    . LYS A 1 272 ? 20.787  28.173  47.341  1.000 62.741  0 272 LYS AAA CA    1 ? 1 
ATOM   1910  C C     . LYS A 1 272 ? 21.695  28.966  48.294  1.000 65.950  0 272 LYS AAA C     1 ? 1 
ATOM   1911  O O     . LYS A 1 272 ? 21.249  29.991  48.826  1.000 70.795  0 272 LYS AAA O     1 ? 1 
ATOM   1912  C CB    . LYS A 1 272 ? 20.262  29.054  46.206  1.000 65.887  0 272 LYS AAA CB    1 ? 1 
ATOM   1913  C CG    . LYS A 1 272 ? 21.266  29.344  45.106  1.000 70.678  0 272 LYS AAA CG    1 ? 1 
ATOM   1914  C CD    . LYS A 1 272 ? 20.656  29.495  43.742  1.000 74.864  0 272 LYS AAA CD    1 ? 1 
ATOM   1915  C CE    . LYS A 1 272 ? 21.638  30.011  42.719  1.000 79.086  0 272 LYS AAA CE    1 ? 1 
ATOM   1916  N NZ    . LYS A 1 272 ? 20.942  30.665  41.583  1.000 84.252  0 272 LYS AAA NZ    1 ? 1 
ATOM   1917  N N     . VAL A 1 273 ? 22.918  28.489  48.520  1.000 67.124  0 273 VAL AAA N     1 ? 1 
ATOM   1918  C CA    . VAL A 1 273 ? 24.012  29.245  49.207  1.000 72.099  0 273 VAL AAA CA    1 ? 1 
ATOM   1919  C C     . VAL A 1 273 ? 25.041  29.669  48.143  1.000 74.728  0 273 VAL AAA C     1 ? 1 
ATOM   1920  O O     . VAL A 1 273 ? 25.911  28.847  47.796  1.000 81.224  0 273 VAL AAA O     1 ? 1 
ATOM   1921  C CB    . VAL A 1 273 ? 24.647  28.411  50.345  1.000 72.922  0 273 VAL AAA CB    1 ? 1 
ATOM   1922  C CG1   . VAL A 1 273 ? 25.914  29.059  50.914  1.000 71.540  0 273 VAL AAA CG1   1 ? 1 
ATOM   1923  C CG2   . VAL A 1 273 ? 23.635  28.106  51.451  1.000 70.680  0 273 VAL AAA CG2   1 ? 1 
ATOM   1924  N N     . ASN A 1 274 ? 24.935  30.908  47.660  1.000 74.860  0 274 ASN AAA N     1 ? 1 
ATOM   1925  C CA    . ASN A 1 274 ? 25.726  31.462  46.526  1.000 73.029  0 274 ASN AAA CA    1 ? 1 
ATOM   1926  C C     . ASN A 1 274 ? 25.299  30.721  45.252  1.000 70.718  0 274 ASN AAA C     1 ? 1 
ATOM   1927  O O     . ASN A 1 274 ? 24.120  30.812  44.883  1.000 64.532  0 274 ASN AAA O     1 ? 1 
ATOM   1928  C CB    . ASN A 1 274 ? 27.245  31.406  46.775  1.000 76.263  0 274 ASN AAA CB    1 ? 1 
ATOM   1929  C CG    . ASN A 1 274 ? 27.715  32.248  47.937  1.000 78.663  0 274 ASN AAA CG    1 ? 1 
ATOM   1930  O OD1   . ASN A 1 274 ? 28.297  31.728  48.885  1.000 76.662  0 274 ASN AAA OD1   1 ? 1 
ATOM   1931  N ND2   . ASN A 1 274 ? 27.479  33.545  47.863  1.000 78.403  0 274 ASN AAA ND2   1 ? 1 
ATOM   1932  N N     . GLU A 1 275 ? 26.239  30.030  44.598  1.000 69.010  0 275 GLU AAA N     1 ? 1 
ATOM   1933  C CA    . GLU A 1 275 ? 25.993  29.289  43.330  1.000 69.093  0 275 GLU AAA CA    1 ? 1 
ATOM   1934  C C     . GLU A 1 275 ? 25.863  27.795  43.645  1.000 62.481  0 275 GLU AAA C     1 ? 1 
ATOM   1935  O O     . GLU A 1 275 ? 25.527  27.042  42.717  1.000 61.572  0 275 GLU AAA O     1 ? 1 
ATOM   1936  C CB    . GLU A 1 275 ? 27.088  29.562  42.292  1.000 73.354  0 275 GLU AAA CB    1 ? 1 
ATOM   1937  C CG    . GLU A 1 275 ? 28.480  29.091  42.701  1.000 77.383  0 275 GLU AAA CG    1 ? 1 
ATOM   1938  C CD    . GLU A 1 275 ? 29.310  30.054  43.537  1.000 80.647  0 275 GLU AAA CD    1 ? 1 
ATOM   1939  O OE1   . GLU A 1 275 ? 28.890  31.217  43.712  1.000 81.702  0 275 GLU AAA OE1   1 ? 1 
ATOM   1940  O OE2   . GLU A 1 275 ? 30.370  29.630  44.047  1.000 85.195  0 275 GLU AAA OE2   1 ? 1 
ATOM   1941  N N     . ASN A 1 276 ? 26.093  27.374  44.891  1.000 56.982  0 276 ASN AAA N     1 ? 1 
ATOM   1942  C CA    . ASN A 1 276 ? 25.946  25.950  45.323  1.000 54.120  0 276 ASN AAA CA    1 ? 1 
ATOM   1943  C C     . ASN A 1 276 ? 24.548  25.724  45.909  1.000 51.946  0 276 ASN AAA C     1 ? 1 
ATOM   1944  O O     . ASN A 1 276 ? 23.857  26.704  46.167  1.000 49.762  0 276 ASN AAA O     1 ? 1 
ATOM   1945  C CB    . ASN A 1 276 ? 27.019  25.514  46.326  1.000 54.102  0 276 ASN AAA CB    1 ? 1 
ATOM   1946  C CG    . ASN A 1 276 ? 28.398  25.367  45.705  1.000 56.127  0 276 ASN AAA CG    1 ? 1 
ATOM   1947  O OD1   . ASN A 1 276 ? 28.548  25.034  44.527  1.000 52.487  0 276 ASN AAA OD1   1 ? 1 
ATOM   1948  N ND2   . ASN A 1 276 ? 29.421  25.594  46.507  1.000 55.893  0 276 ASN AAA ND2   1 ? 1 
ATOM   1949  N N     . ILE A 1 277 ? 24.157  24.461  46.076  1.000 48.261  0 277 ILE AAA N     1 ? 1 
ATOM   1950  C CA    . ILE A 1 277 ? 22.892  24.038  46.751  1.000 45.549  0 277 ILE AAA CA    1 ? 1 
ATOM   1951  C C     . ILE A 1 277 ? 23.245  23.301  48.051  1.000 44.374  0 277 ILE AAA C     1 ? 1 
ATOM   1952  O O     . ILE A 1 277 ? 23.808  22.196  47.991  1.000 43.039  0 277 ILE AAA O     1 ? 1 
ATOM   1953  C CB    . ILE A 1 277 ? 22.011  23.201  45.799  1.000 43.207  0 277 ILE AAA CB    1 ? 1 
ATOM   1954  C CG1   . ILE A 1 277 ? 21.685  23.989  44.523  1.000 43.463  0 277 ILE AAA CG1   1 ? 1 
ATOM   1955  C CG2   . ILE A 1 277 ? 20.767  22.699  46.517  1.000 40.499  0 277 ILE AAA CG2   1 ? 1 
ATOM   1956  C CD1   . ILE A 1 277 ? 21.229  23.151  43.356  1.000 42.526  0 277 ILE AAA CD1   1 ? 1 
ATOM   1957  N N     . LYS A 1 278 ? 22.956  23.935  49.186  1.000 45.471  0 278 LYS AAA N     1 ? 1 
ATOM   1958  C CA    . LYS A 1 278 ? 23.050  23.352  50.549  1.000 44.186  0 278 LYS AAA CA    1 ? 1 
ATOM   1959  C C     . LYS A 1 278 ? 21.827  22.449  50.756  1.000 42.484  0 278 LYS AAA C     1 ? 1 
ATOM   1960  O O     . LYS A 1 278 ? 20.670  22.944  50.696  1.000 43.329  0 278 LYS AAA O     1 ? 1 
ATOM   1961  C CB    . LYS A 1 278 ? 23.120  24.483  51.577  1.000 45.434  0 278 LYS AAA CB    1 ? 1 
ATOM   1962  C CG    . LYS A 1 278 ? 23.467  24.083  53.004  1.000 47.138  0 278 LYS AAA CG    1 ? 1 
ATOM   1963  C CD    . LYS A 1 278 ? 23.254  25.214  54.018  1.000 48.392  0 278 LYS AAA CD    1 ? 1 
ATOM   1964  C CE    . LYS A 1 278 ? 23.871  24.879  55.366  1.000 49.751  0 278 LYS AAA CE    1 ? 1 
ATOM   1965  N NZ    . LYS A 1 278 ? 23.400  25.733  56.484  1.000 49.339  0 278 LYS AAA NZ    1 ? 1 
ATOM   1966  N N     . VAL A 1 279 ? 22.069  21.165  50.957  1.000 38.253  0 279 VAL AAA N     1 ? 1 
ATOM   1967  C CA    . VAL A 1 279 ? 21.001  20.157  51.165  1.000 37.460  0 279 VAL AAA CA    1 ? 1 
ATOM   1968  C C     . VAL A 1 279 ? 21.044  19.724  52.629  1.000 38.547  0 279 VAL AAA C     1 ? 1 
ATOM   1969  O O     . VAL A 1 279 ? 22.114  19.347  53.107  1.000 40.516  0 279 VAL AAA O     1 ? 1 
ATOM   1970  C CB    . VAL A 1 279 ? 21.138  18.971  50.185  1.000 35.180  0 279 VAL AAA CB    1 ? 1 
ATOM   1971  C CG1   . VAL A 1 279 ? 20.248  17.791  50.568  1.000 35.174  0 279 VAL AAA CG1   1 ? 1 
ATOM   1972  C CG2   . VAL A 1 279 ? 20.839  19.426  48.769  1.000 33.009  0 279 VAL AAA CG2   1 ? 1 
ATOM   1973  N N     . SER A 1 280 ? 19.905  19.798  53.317  1.000 38.419  0 280 SER AAA N     1 ? 1 
ATOM   1974  C CA    . SER A 1 280 ? 19.789  19.348  54.719  1.000 38.489  0 280 SER AAA CA    1 ? 1 
ATOM   1975  C C     . SER A 1 280 ? 19.085  18.007  54.697  1.000 37.384  0 280 SER AAA C     1 ? 1 
ATOM   1976  O O     . SER A 1 280 ? 18.047  17.914  54.072  1.000 37.339  0 280 SER AAA O     1 ? 1 
ATOM   1977  C CB    . SER A 1 280 ? 19.097  20.373  55.590  1.000 41.034  0 280 SER AAA CB    1 ? 1 
ATOM   1978  O OG    . SER A 1 280 ? 19.885  21.555  55.716  1.000 40.567  0 280 SER AAA OG    1 ? 1 
ATOM   1979  N N     . PHE A 1 281 ? 19.705  16.993  55.286  1.000 39.339  0 281 PHE AAA N     1 ? 1 
ATOM   1980  C CA    . PHE A 1 281 ? 19.260  15.580  55.223  1.000 39.955  0 281 PHE AAA CA    1 ? 1 
ATOM   1981  C C     . PHE A 1 281 ? 18.500  15.197  56.501  1.000 40.992  0 281 PHE AAA C     1 ? 1 
ATOM   1982  O O     . PHE A 1 281 ? 18.725  15.811  57.569  1.000 41.447  0 281 PHE AAA O     1 ? 1 
ATOM   1983  C CB    . PHE A 1 281 ? 20.459  14.656  55.016  1.000 39.788  0 281 PHE AAA CB    1 ? 1 
ATOM   1984  C CG    . PHE A 1 281 ? 21.053  14.727  53.637  1.000 38.586  0 281 PHE AAA CG    1 ? 1 
ATOM   1985  C CD1   . PHE A 1 281 ? 20.469  14.036  52.598  1.000 35.903  0 281 PHE AAA CD1   1 ? 1 
ATOM   1986  C CD2   . PHE A 1 281 ? 22.204  15.471  53.391  1.000 38.007  0 281 PHE AAA CD2   1 ? 1 
ATOM   1987  C CE1   . PHE A 1 281 ? 20.971  14.138  51.319  1.000 36.306  0 281 PHE AAA CE1   1 ? 1 
ATOM   1988  C CE2   . PHE A 1 281 ? 22.752  15.511  52.124  1.000 37.056  0 281 PHE AAA CE2   1 ? 1 
ATOM   1989  C CZ    . PHE A 1 281 ? 22.133  14.849  51.090  1.000 36.885  0 281 PHE AAA CZ    1 ? 1 
ATOM   1990  N N     . SER A 1 282 ? 17.639  14.187  56.361  1.000 40.465  0 282 SER AAA N     1 ? 1 
ATOM   1991  C CA    . SER A 1 282 ? 16.724  13.642  57.394  1.000 40.369  0 282 SER AAA CA    1 ? 1 
ATOM   1992  C C     . SER A 1 282 ? 17.494  13.160  58.639  1.000 43.097  0 282 SER AAA C     1 ? 1 
ATOM   1993  O O     . SER A 1 282 ? 16.838  13.012  59.686  1.000 41.658  0 282 SER AAA O     1 ? 1 
ATOM   1994  C CB    . SER A 1 282 ? 15.905  12.519  56.807  1.000 38.476  0 282 SER AAA CB    1 ? 1 
ATOM   1995  O OG    . SER A 1 282 ? 16.711  11.361  56.588  1.000 38.983  0 282 SER AAA OG    1 ? 1 
ATOM   1996  N N     . ASP A 1 283 ? 18.810  12.895  58.528  1.000 42.980  0 283 ASP AAA N     1 ? 1 
ATOM   1997  C CA    . ASP A 1 283 ? 19.648  12.442  59.667  1.000 44.336  0 283 ASP AAA CA    1 ? 1 
ATOM   1998  C C     . ASP A 1 283 ? 20.340  13.649  60.343  1.000 43.119  0 283 ASP AAA C     1 ? 1 
ATOM   1999  O O     . ASP A 1 283 ? 21.233  13.412  61.169  1.000 41.968  0 283 ASP AAA O     1 ? 1 
ATOM   2000  C CB    . ASP A 1 283 ? 20.634  11.349  59.223  1.000 44.922  0 283 ASP AAA CB    1 ? 1 
ATOM   2001  C CG    . ASP A 1 283 ? 21.780  11.812  58.330  1.000 44.350  0 283 ASP AAA CG    1 ? 1 
ATOM   2002  O OD1   . ASP A 1 283 ? 21.688  12.956  57.788  1.000 41.523  0 283 ASP AAA OD1   1 ? 1 
ATOM   2003  O OD2   . ASP A 1 283 ? 22.766  11.018  58.178  1.000 44.042  0 283 ASP AAA OD2   1 ? 1 
ATOM   2004  N N     . GLY A 1 284 ? 19.961  14.887  60.005  1.000 41.726  0 284 GLY AAA N     1 ? 1 
ATOM   2005  C CA    . GLY A 1 284 ? 20.564  16.120  60.554  1.000 42.352  0 284 GLY AAA CA    1 ? 1 
ATOM   2006  C C     . GLY A 1 284 ? 21.909  16.482  59.930  1.000 43.866  0 284 GLY AAA C     1 ? 1 
ATOM   2007  O O     . GLY A 1 284 ? 22.544  17.441  60.397  1.000 45.872  0 284 GLY AAA O     1 ? 1 
ATOM   2008  N N     . SER A 1 285 ? 22.384  15.743  58.925  1.000 43.780  0 285 SER AAA N     1 ? 1 
ATOM   2009  C CA    . SER A 1 285 ? 23.640  16.068  58.200  1.000 41.664  0 285 SER AAA CA    1 ? 1 
ATOM   2010  C C     . SER A 1 285 ? 23.334  17.092  57.101  1.000 40.671  0 285 SER AAA C     1 ? 1 
ATOM   2011  O O     . SER A 1 285 ? 22.159  17.209  56.678  1.000 39.890  0 285 SER AAA O     1 ? 1 
ATOM   2012  C CB    . SER A 1 285 ? 24.346  14.833  57.690  1.000 39.580  0 285 SER AAA CB    1 ? 1 
ATOM   2013  O OG    . SER A 1 285 ? 23.660  14.298  56.590  1.000 40.630  0 285 SER AAA OG    1 ? 1 
ATOM   2014  N N     . VAL A 1 286 ? 24.354  17.847  56.711  1.000 41.413  0 286 VAL AAA N     1 ? 1 
ATOM   2015  C CA    . VAL A 1 286 ? 24.258  18.968  55.734  1.000 45.489  0 286 VAL AAA CA    1 ? 1 
ATOM   2016  C C     . VAL A 1 286 ? 25.408  18.781  54.732  1.000 46.848  0 286 VAL AAA C     1 ? 1 
ATOM   2017  O O     . VAL A 1 286 ? 26.479  18.259  55.142  1.000 50.374  0 286 VAL AAA O     1 ? 1 
ATOM   2018  C CB    . VAL A 1 286 ? 24.295  20.341  56.451  1.000 45.941  0 286 VAL AAA CB    1 ? 1 
ATOM   2019  C CG1   . VAL A 1 286 ? 24.517  21.506  55.505  1.000 46.286  0 286 VAL AAA CG1   1 ? 1 
ATOM   2020  C CG2   . VAL A 1 286 ? 23.038  20.579  57.280  1.000 45.658  0 286 VAL AAA CG2   1 ? 1 
ATOM   2021  N N     . GLU A 1 287 ? 25.212  19.146  53.462  1.000 45.905  0 287 GLU AAA N     1 ? 1 
ATOM   2022  C CA    . GLU A 1 287 ? 26.280  19.017  52.424  1.000 46.622  0 287 GLU AAA CA    1 ? 1 
ATOM   2023  C C     . GLU A 1 287 ? 25.918  19.887  51.219  1.000 43.202  0 287 GLU AAA C     1 ? 1 
ATOM   2024  O O     . GLU A 1 287 ? 24.714  19.996  50.896  1.000 38.698  0 287 GLU AAA O     1 ? 1 
ATOM   2025  C CB    . GLU A 1 287 ? 26.461  17.551  51.999  1.000 47.080  0 287 GLU AAA CB    1 ? 1 
ATOM   2026  C CG    . GLU A 1 287 ? 27.805  17.257  51.368  1.000 48.955  0 287 GLU AAA CG    1 ? 1 
ATOM   2027  C CD    . GLU A 1 287 ? 28.040  15.792  51.039  1.000 50.460  0 287 GLU AAA CD    1 ? 1 
ATOM   2028  O OE1   . GLU A 1 287 ? 27.290  14.945  51.595  1.000 51.992  0 287 GLU AAA OE1   1 ? 1 
ATOM   2029  O OE2   . GLU A 1 287 ? 28.981  15.493  50.268  1.000 48.405  0 287 GLU AAA OE2   1 ? 1 
ATOM   2030  N N     . GLU A 1 288 ? 26.935  20.484  50.605  1.000 44.306  0 288 GLU AAA N     1 ? 1 
ATOM   2031  C CA    . GLU A 1 288 ? 26.791  21.359  49.409  1.000 45.649  0 288 GLU AAA CA    1 ? 1 
ATOM   2032  C C     . GLU A 1 288 ? 26.975  20.524  48.143  1.000 42.555  0 288 GLU AAA C     1 ? 1 
ATOM   2033  O O     . GLU A 1 288 ? 27.832  19.616  48.130  1.000 41.460  0 288 GLU AAA O     1 ? 1 
ATOM   2034  C CB    . GLU A 1 288 ? 27.752  22.538  49.476  1.000 48.412  0 288 GLU AAA CB    1 ? 1 
ATOM   2035  C CG    . GLU A 1 288 ? 27.426  23.482  50.629  1.000 52.724  0 288 GLU AAA CG    1 ? 1 
ATOM   2036  C CD    . GLU A 1 288 ? 28.006  24.876  50.496  1.000 57.677  0 288 GLU AAA CD    1 ? 1 
ATOM   2037  O OE1   . GLU A 1 288 ? 28.452  25.255  49.374  1.000 62.408  0 288 GLU AAA OE1   1 ? 1 
ATOM   2038  O OE2   . GLU A 1 288 ? 27.992  25.581  51.509  1.000 65.334  0 288 GLU AAA OE2   1 ? 1 
ATOM   2039  N N     . PHE A 1 289 ? 26.134  20.790  47.144  1.000 40.296  0 289 PHE AAA N     1 ? 1 
ATOM   2040  C CA    . PHE A 1 289 ? 26.229  20.208  45.786  1.000 41.380  0 289 PHE AAA CA    1 ? 1 
ATOM   2041  C C     . PHE A 1 289 ? 26.051  21.329  44.765  1.000 40.587  0 289 PHE AAA C     1 ? 1 
ATOM   2042  O O     . PHE A 1 289 ? 25.451  22.325  45.076  1.000 43.080  0 289 PHE AAA O     1 ? 1 
ATOM   2043  C CB    . PHE A 1 289 ? 25.184  19.106  45.569  1.000 40.078  0 289 PHE AAA CB    1 ? 1 
ATOM   2044  C CG    . PHE A 1 289 ? 25.197  18.033  46.630  1.000 40.527  0 289 PHE AAA CG    1 ? 1 
ATOM   2045  C CD1   . PHE A 1 289 ? 24.469  18.194  47.805  1.000 39.896  0 289 PHE AAA CD1   1 ? 1 
ATOM   2046  C CD2   . PHE A 1 289 ? 25.958  16.880  46.469  1.000 39.288  0 289 PHE AAA CD2   1 ? 1 
ATOM   2047  C CE1   . PHE A 1 289 ? 24.507  17.218  48.786  1.000 41.089  0 289 PHE AAA CE1   1 ? 1 
ATOM   2048  C CE2   . PHE A 1 289 ? 25.955  15.891  47.441  1.000 39.921  0 289 PHE AAA CE2   1 ? 1 
ATOM   2049  C CZ    . PHE A 1 289 ? 25.241  16.063  48.603  1.000 39.513  0 289 PHE AAA CZ    1 ? 1 
ATOM   2050  N N     . GLU A 1 290 ? 26.578  21.145  43.573  1.000 39.519  0 290 GLU AAA N     1 ? 1 
ATOM   2051  C CA    . GLU A 1 290 ? 26.377  22.073  42.440  1.000 41.345  0 290 GLU AAA CA    1 ? 1 
ATOM   2052  C C     . GLU A 1 290 ? 25.051  21.754  41.747  1.000 40.647  0 290 GLU AAA C     1 ? 1 
ATOM   2053  O O     . GLU A 1 290 ? 24.404  22.692  41.265  1.000 39.988  0 290 GLU AAA O     1 ? 1 
ATOM   2054  C CB    . GLU A 1 290 ? 27.571  21.886  41.530  1.000 44.058  0 290 GLU AAA CB    1 ? 1 
ATOM   2055  C CG    . GLU A 1 290 ? 27.750  22.940  40.500  1.000 49.139  0 290 GLU AAA CG    1 ? 1 
ATOM   2056  C CD    . GLU A 1 290 ? 29.153  22.872  39.875  1.000 51.546  0 290 GLU AAA CD    1 ? 1 
ATOM   2057  O OE1   . GLU A 1 290 ? 29.250  23.201  38.642  1.000 54.503  0 290 GLU AAA OE1   1 ? 1 
ATOM   2058  O OE2   . GLU A 1 290 ? 30.162  22.506  40.618  1.000 49.133  0 290 GLU AAA OE2   1 ? 1 
ATOM   2059  N N     . THR A 1 291 ? 24.648  20.476  41.725  1.000 37.358  0 291 THR AAA N     1 ? 1 
ATOM   2060  C CA    . THR A 1 291 ? 23.436  19.984  41.034  1.000 35.542  0 291 THR AAA CA    1 ? 1 
ATOM   2061  C C     . THR A 1 291 ? 22.701  18.997  41.943  1.000 34.504  0 291 THR AAA C     1 ? 1 
ATOM   2062  O O     . THR A 1 291 ? 23.340  18.109  42.515  1.000 33.649  0 291 THR AAA O     1 ? 1 
ATOM   2063  C CB    . THR A 1 291 ? 23.790  19.327  39.698  1.000 35.587  0 291 THR AAA CB    1 ? 1 
ATOM   2064  O OG1   . THR A 1 291 ? 24.514  20.234  38.864  1.000 34.849  0 291 THR AAA OG1   1 ? 1 
ATOM   2065  C CG2   . THR A 1 291 ? 22.561  18.885  38.949  1.000 35.901  0 291 THR AAA CG2   1 ? 1 
ATOM   2066  N N     . VAL A 1 292 ? 21.387  19.141  42.036  1.000 33.957  0 292 VAL AAA N     1 ? 1 
ATOM   2067  C CA    . VAL A 1 292 ? 20.509  18.160  42.735  1.000 32.967  0 292 VAL AAA CA    1 ? 1 
ATOM   2068  C C     . VAL A 1 292 ? 19.460  17.672  41.744  1.000 31.153  0 292 VAL AAA C     1 ? 1 
ATOM   2069  O O     . VAL A 1 292 ? 18.738  18.508  41.185  1.000 30.564  0 292 VAL AAA O     1 ? 1 
ATOM   2070  C CB    . VAL A 1 292 ? 19.866  18.740  44.007  1.000 32.856  0 292 VAL AAA CB    1 ? 1 
ATOM   2071  C CG1   . VAL A 1 292 ? 18.882  17.763  44.633  1.000 32.559  0 292 VAL AAA CG1   1 ? 1 
ATOM   2072  C CG2   . VAL A 1 292 ? 20.919  19.145  45.027  1.000 32.110  0 292 VAL AAA CG2   1 ? 1 
ATOM   2073  N N     . LEU A 1 293 ? 19.408  16.352  41.565  1.000 30.306  0 293 LEU AAA N     1 ? 1 
ATOM   2074  C CA    . LEU A 1 293 ? 18.562  15.673  40.557  1.000 29.209  0 293 LEU AAA CA    1 ? 1 
ATOM   2075  C C     . LEU A 1 293 ? 17.632  14.726  41.294  1.000 27.898  0 293 LEU AAA C     1 ? 1 
ATOM   2076  O O     . LEU A 1 293 ? 18.140  13.840  41.966  1.000 27.174  0 293 LEU AAA O     1 ? 1 
ATOM   2077  C CB    . LEU A 1 293 ? 19.446  14.914  39.560  1.000 29.462  0 293 LEU AAA CB    1 ? 1 
ATOM   2078  C CG    . LEU A 1 293 ? 18.708  14.426  38.315  1.000 30.589  0 293 LEU AAA CG    1 ? 1 
ATOM   2079  C CD1   . LEU A 1 293 ? 19.627  14.332  37.124  1.000 31.671  0 293 LEU AAA CD1   1 ? 1 
ATOM   2080  C CD2   . LEU A 1 293 ? 18.040  13.085  38.559  1.000 30.717  0 293 LEU AAA CD2   1 ? 1 
ATOM   2081  N N     . TYR A 1 294 ? 16.330  14.893  41.106  1.000 27.875  0 294 TYR AAA N     1 ? 1 
ATOM   2082  C CA    . TYR A 1 294 ? 15.269  14.010  41.651  1.000 29.004  0 294 TYR AAA CA    1 ? 1 
ATOM   2083  C C     . TYR A 1 294 ? 14.975  12.907  40.659  1.000 28.491  0 294 TYR AAA C     1 ? 1 
ATOM   2084  O O     . TYR A 1 294 ? 14.439  13.202  39.600  1.000 29.041  0 294 TYR AAA O     1 ? 1 
ATOM   2085  C CB    . TYR A 1 294 ? 14.010  14.803  42.046  1.000 29.098  0 294 TYR AAA CB    1 ? 1 
ATOM   2086  C CG    . TYR A 1 294 ? 14.056  15.207  43.506  1.000 30.022  0 294 TYR AAA CG    1 ? 1 
ATOM   2087  C CD1   . TYR A 1 294 ? 13.727  14.305  44.505  1.000 30.483  0 294 TYR AAA CD1   1 ? 1 
ATOM   2088  C CD2   . TYR A 1 294 ? 14.466  16.468  43.889  1.000 30.677  0 294 TYR AAA CD2   1 ? 1 
ATOM   2089  C CE1   . TYR A 1 294 ? 13.778  14.657  45.840  1.000 30.657  0 294 TYR AAA CE1   1 ? 1 
ATOM   2090  C CE2   . TYR A 1 294 ? 14.575  16.817  45.221  1.000 31.167  0 294 TYR AAA CE2   1 ? 1 
ATOM   2091  C CZ    . TYR A 1 294 ? 14.231  15.912  46.206  1.000 31.881  0 294 TYR AAA CZ    1 ? 1 
ATOM   2092  O OH    . TYR A 1 294 ? 14.321  16.278  47.534  1.000 33.420  0 294 TYR AAA OH    1 ? 1 
ATOM   2093  N N     . ALA A 1 295 ? 15.279  11.664  41.037  1.000 28.729  0 295 ALA AAA N     1 ? 1 
ATOM   2094  C CA    . ALA A 1 295 ? 14.925  10.447  40.271  1.000 29.152  0 295 ALA AAA CA    1 ? 1 
ATOM   2095  C C     . ALA A 1 295 ? 14.072  9.544   41.155  1.000 30.547  0 295 ALA AAA C     1 ? 1 
ATOM   2096  O O     . ALA A 1 295 ? 14.414  8.362   41.324  1.000 29.638  0 295 ALA AAA O     1 ? 1 
ATOM   2097  C CB    . ALA A 1 295 ? 16.178  9.761   39.796  1.000 29.137  0 295 ALA AAA CB    1 ? 1 
ATOM   2098  N N     . THR A 1 296 ? 12.999  10.088  41.704  1.000 33.467  0 296 THR AAA N     1 ? 1 
ATOM   2099  C CA    . THR A 1 296 ? 12.214  9.414   42.760  1.000 37.663  0 296 THR AAA CA    1 ? 1 
ATOM   2100  C C     . THR A 1 296 ? 11.076  8.653   42.087  1.000 40.709  0 296 THR AAA C     1 ? 1 
ATOM   2101  O O     . THR A 1 296 ? 10.534  7.696   42.715  1.000 45.530  0 296 THR AAA O     1 ? 1 
ATOM   2102  C CB    . THR A 1 296 ? 11.793  10.403  43.853  1.000 37.085  0 296 THR AAA CB    1 ? 1 
ATOM   2103  O OG1   . THR A 1 296 ? 11.374  11.631  43.255  1.000 33.593  0 296 THR AAA OG1   1 ? 1 
ATOM   2104  C CG2   . THR A 1 296 ? 12.919  10.667  44.833  1.000 38.059  0 296 THR AAA CG2   1 ? 1 
ATOM   2105  N N     . GLY A 1 297 ? 10.732  9.079   40.870  1.000 38.149  0 297 GLY AAA N     1 ? 1 
ATOM   2106  C CA    . GLY A 1 297 ? 9.796   8.365   39.995  1.000 37.140  0 297 GLY AAA CA    1 ? 1 
ATOM   2107  C C     . GLY A 1 297 ? 9.092   9.351   39.086  1.000 34.626  0 297 GLY AAA C     1 ? 1 
ATOM   2108  O O     . GLY A 1 297 ? 9.670   10.459  38.869  1.000 30.899  0 297 GLY AAA O     1 ? 1 
ATOM   2109  N N     . ARG A 1 298 ? 7.910   8.952   38.588  1.000 31.228  0 298 ARG AAA N     1 ? 1 
ATOM   2110  C CA    . ARG A 1 298 ? 7.208   9.607   37.467  1.000 30.049  0 298 ARG AAA CA    1 ? 1 
ATOM   2111  C C     . ARG A 1 298 ? 5.710   9.457   37.695  1.000 31.013  0 298 ARG AAA C     1 ? 1 
ATOM   2112  O O     . ARG A 1 298 ? 5.271   8.346   38.054  1.000 29.624  0 298 ARG AAA O     1 ? 1 
ATOM   2113  C CB    . ARG A 1 298 ? 7.633   9.016   36.116  1.000 27.654  0 298 ARG AAA CB    1 ? 1 
ATOM   2114  C CG    . ARG A 1 298 ? 9.082   9.306   35.722  1.000 26.822  0 298 ARG AAA CG    1 ? 1 
ATOM   2115  C CD    . ARG A 1 298 ? 9.571   8.500   34.522  1.000 25.674  0 298 ARG AAA CD    1 ? 1 
ATOM   2116  N NE    . ARG A 1 298 ? 8.925   8.970   33.286  1.000 24.710  0 298 ARG AAA NE    1 ? 1 
ATOM   2117  C CZ    . ARG A 1 298 ? 9.330   10.008  32.570  1.000 25.577  0 298 ARG AAA CZ    1 ? 1 
ATOM   2118  N NH1   . ARG A 1 298 ? 10.396  10.707  32.913  1.000 25.159  0 298 ARG AAA NH1   1 ? 1 
ATOM   2119  N NH2   . ARG A 1 298 ? 8.702   10.347  31.458  1.000 26.985  0 298 ARG AAA NH2   1 ? 1 
ATOM   2120  N N     . ASN A 1 299 ? 4.957   10.541  37.495  1.000 31.724  0 299 ASN AAA N     1 ? 1 
ATOM   2121  C CA    . ASN A 1 299 ? 3.473   10.551  37.538  1.000 32.272  0 299 ASN AAA CA    1 ? 1 
ATOM   2122  C C     . ASN A 1 299 ? 2.934   10.595  36.120  1.000 34.006  0 299 ASN AAA C     1 ? 1 
ATOM   2123  O O     . ASN A 1 299 ? 3.494   11.295  35.275  1.000 30.620  0 299 ASN AAA O     1 ? 1 
ATOM   2124  C CB    . ASN A 1 299 ? 2.914   11.778  38.257  1.000 31.319  0 299 ASN AAA CB    1 ? 1 
ATOM   2125  C CG    . ASN A 1 299 ? 3.360   11.832  39.704  1.000 30.284  0 299 ASN AAA CG    1 ? 1 
ATOM   2126  O OD1   . ASN A 1 299 ? 3.882   12.846  40.155  1.000 29.456  0 299 ASN AAA OD1   1 ? 1 
ATOM   2127  N ND2   . ASN A 1 299 ? 3.196   10.715  40.395  1.000 29.100  0 299 ASN AAA ND2   1 ? 1 
ATOM   2128  N N     . PRO A 1 300 ? 1.825   9.871   35.839  1.000 36.103  0 300 PRO AAA N     1 ? 1 
ATOM   2129  C CA    . PRO A 1 300 ? 1.189   9.925   34.518  1.000 33.929  0 300 PRO AAA CA    1 ? 1 
ATOM   2130  C C     . PRO A 1 300 ? 0.624   11.316  34.222  1.000 34.182  0 300 PRO AAA C     1 ? 1 
ATOM   2131  O O     . PRO A 1 300 ? -0.050  11.840  35.008  1.000 31.581  0 300 PRO AAA O     1 ? 1 
ATOM   2132  C CB    . PRO A 1 300 ? 0.102   8.854   34.584  1.000 33.923  0 300 PRO AAA CB    1 ? 1 
ATOM   2133  C CG    . PRO A 1 300 ? -0.203  8.764   36.092  1.000 35.830  0 300 PRO AAA CG    1 ? 1 
ATOM   2134  C CD    . PRO A 1 300 ? 1.142   8.965   36.785  1.000 35.697  0 300 PRO AAA CD    1 ? 1 
ATOM   2135  N N     . ASP A 1 301 ? 0.931   11.849  33.043  1.000 36.914  0 301 ASP AAA N     1 ? 1 
ATOM   2136  C CA    . ASP A 1 301 ? 0.506   13.193  32.581  1.000 38.942  0 301 ASP AAA CA    1 ? 1 
ATOM   2137  C C     . ASP A 1 301 ? -0.899  13.074  31.998  1.000 38.524  0 301 ASP AAA C     1 ? 1 
ATOM   2138  O O     . ASP A 1 301 ? -1.052  13.044  30.774  1.000 37.145  0 301 ASP AAA O     1 ? 1 
ATOM   2139  C CB    . ASP A 1 301 ? 1.527   13.756  31.594  1.000 40.219  0 301 ASP AAA CB    1 ? 1 
ATOM   2140  C CG    . ASP A 1 301 ? 1.222   15.177  31.178  1.000 43.566  0 301 ASP AAA CG    1 ? 1 
ATOM   2141  O OD1   . ASP A 1 301 ? 0.710   15.937  32.074  1.000 44.801  0 301 ASP AAA OD1   1 ? 1 
ATOM   2142  O OD2   . ASP A 1 301 ? 1.475   15.510  29.964  1.000 43.906  0 301 ASP AAA OD2   1 ? 1 
ATOM   2143  N N     . VAL A 1 302 ? -1.898  13.007  32.871  1.000 41.885  0 302 VAL AAA N     1 ? 1 
ATOM   2144  C CA    . VAL A 1 302 ? -3.320  12.755  32.476  1.000 43.162  0 302 VAL AAA CA    1 ? 1 
ATOM   2145  C C     . VAL A 1 302 ? -4.234  13.860  33.007  1.000 47.138  0 302 VAL AAA C     1 ? 1 
ATOM   2146  O O     . VAL A 1 302 ? -5.438  13.856  32.649  1.000 53.184  0 302 VAL AAA O     1 ? 1 
ATOM   2147  C CB    . VAL A 1 302 ? -3.782  11.367  32.944  1.000 41.011  0 302 VAL AAA CB    1 ? 1 
ATOM   2148  C CG1   . VAL A 1 302 ? -3.008  10.281  32.212  1.000 40.562  0 302 VAL AAA CG1   1 ? 1 
ATOM   2149  C CG2   . VAL A 1 302 ? -3.672  11.195  34.450  1.000 39.103  0 302 VAL AAA CG2   1 ? 1 
ATOM   2150  N N     . LYS A 1 303 ? -3.691  14.800  33.776  1.000 49.876  0 303 LYS AAA N     1 ? 1 
ATOM   2151  C CA    . LYS A 1 303 ? -4.490  15.846  34.462  1.000 49.811  0 303 LYS AAA CA    1 ? 1 
ATOM   2152  C C     . LYS A 1 303 ? -5.118  16.754  33.407  1.000 49.042  0 303 LYS AAA C     1 ? 1 
ATOM   2153  O O     . LYS A 1 303 ? -6.273  17.143  33.605  1.000 56.183  0 303 LYS AAA O     1 ? 1 
ATOM   2154  C CB    . LYS A 1 303 ? -3.627  16.533  35.530  1.000 51.569  0 303 LYS AAA CB    1 ? 1 
ATOM   2155  C CG    . LYS A 1 303 ? -3.270  15.592  36.687  1.000 52.866  0 303 LYS AAA CG    1 ? 1 
ATOM   2156  C CD    . LYS A 1 303 ? -2.534  16.215  37.863  1.000 55.236  0 303 LYS AAA CD    1 ? 1 
ATOM   2157  C CE    . LYS A 1 303 ? -2.844  15.499  39.173  1.000 55.591  0 303 LYS AAA CE    1 ? 1 
ATOM   2158  N NZ    . LYS A 1 303 ? -2.212  16.135  40.357  1.000 54.875  0 303 LYS AAA NZ    1 ? 1 
ATOM   2159  N N     . GLY A 1 304 ? -4.432  17.032  32.306  1.000 50.200  0 304 GLY AAA N     1 ? 1 
ATOM   2160  C CA    . GLY A 1 304 ? -4.960  17.867  31.200  1.000 49.911  0 304 GLY AAA CA    1 ? 1 
ATOM   2161  C C     . GLY A 1 304 ? -6.039  17.177  30.369  1.000 48.431  0 304 GLY AAA C     1 ? 1 
ATOM   2162  O O     . GLY A 1 304 ? -6.648  17.851  29.538  1.000 52.286  0 304 GLY AAA O     1 ? 1 
ATOM   2163  N N     . LEU A 1 305 ? -6.299  15.886  30.588  1.000 45.807  0 305 LEU AAA N     1 ? 1 
ATOM   2164  C CA    . LEU A 1 305 ? -7.075  15.061  29.620  1.000 47.000  0 305 LEU AAA CA    1 ? 1 
ATOM   2165  C C     . LEU A 1 305 ? -8.584  15.136  29.879  1.000 45.191  0 305 LEU AAA C     1 ? 1 
ATOM   2166  O O     . LEU A 1 305 ? -9.321  14.735  28.965  1.000 44.515  0 305 LEU AAA O     1 ? 1 
ATOM   2167  C CB    . LEU A 1 305 ? -6.585  13.610  29.660  1.000 44.944  0 305 LEU AAA CB    1 ? 1 
ATOM   2168  C CG    . LEU A 1 305 ? -5.220  13.370  29.023  1.000 43.226  0 305 LEU AAA CG    1 ? 1 
ATOM   2169  C CD1   . LEU A 1 305 ? -4.797  11.923  29.189  1.000 40.673  0 305 LEU AAA CD1   1 ? 1 
ATOM   2170  C CD2   . LEU A 1 305 ? -5.261  13.736  27.554  1.000 43.433  0 305 LEU AAA CD2   1 ? 1 
ATOM   2171  N N     . ASN A 1 306 ? -9.021  15.604  31.046  1.000 45.794  0 306 ASN AAA N     1 ? 1 
ATOM   2172  C CA    . ASN A 1 306 ? -10.460 15.708  31.403  1.000 49.030  0 306 ASN AAA CA    1 ? 1 
ATOM   2173  C C     . ASN A 1 306 ? -11.066 14.297  31.539  1.000 50.786  0 306 ASN AAA C     1 ? 1 
ATOM   2174  O O     . ASN A 1 306 ? -12.193 14.063  31.028  1.000 52.934  0 306 ASN AAA O     1 ? 1 
ATOM   2175  C CB    . ASN A 1 306 ? -11.202 16.536  30.351  1.000 53.077  0 306 ASN AAA CB    1 ? 1 
ATOM   2176  C CG    . ASN A 1 306 ? -12.524 17.080  30.834  1.000 56.268  0 306 ASN AAA CG    1 ? 1 
ATOM   2177  O OD1   . ASN A 1 306 ? -12.731 17.255  32.033  1.000 60.869  0 306 ASN AAA OD1   1 ? 1 
ATOM   2178  N ND2   . ASN A 1 306 ? -13.428 17.336  29.900  1.000 58.671  0 306 ASN AAA ND2   1 ? 1 
ATOM   2179  N N     . LEU A 1 307 ? -10.358 13.390  32.213  1.000 52.024  0 307 LEU AAA N     1 ? 1 
ATOM   2180  C CA    . LEU A 1 307 ? -10.727 11.954  32.352  1.000 54.227  0 307 LEU AAA CA    1 ? 1 
ATOM   2181  C C     . LEU A 1 307 ? -11.956 11.821  33.255  1.000 54.641  0 307 LEU AAA C     1 ? 1 
ATOM   2182  O O     . LEU A 1 307 ? -12.842 11.013  32.905  1.000 56.686  0 307 LEU AAA O     1 ? 1 
ATOM   2183  C CB    . LEU A 1 307 ? -9.554  11.153  32.934  1.000 53.610  0 307 LEU AAA CB    1 ? 1 
ATOM   2184  C CG    . LEU A 1 307 ? -8.282  11.083  32.077  1.000 56.631  0 307 LEU AAA CG    1 ? 1 
ATOM   2185  C CD1   . LEU A 1 307 ? -7.251  10.198  32.746  1.000 57.014  0 307 LEU AAA CD1   1 ? 1 
ATOM   2186  C CD2   . LEU A 1 307 ? -8.548  10.564  30.673  1.000 54.958  0 307 LEU AAA CD2   1 ? 1 
ATOM   2187  N N     . ASN A 1 308 ? -11.995 12.564  34.367  1.000 54.507  0 308 ASN AAA N     1 ? 1 
ATOM   2188  C CA    . ASN A 1 308 ? -13.056 12.455  35.408  1.000 54.853  0 308 ASN AAA CA    1 ? 1 
ATOM   2189  C C     . ASN A 1 308 ? -14.431 12.647  34.767  1.000 50.910  0 308 ASN AAA C     1 ? 1 
ATOM   2190  O O     . ASN A 1 308 ? -15.310 11.783  34.967  1.000 46.306  0 308 ASN AAA O     1 ? 1 
ATOM   2191  C CB    . ASN A 1 308 ? -12.881 13.450  36.563  1.000 56.213  0 308 ASN AAA CB    1 ? 1 
ATOM   2192  C CG    . ASN A 1 308 ? -13.707 13.063  37.777  1.000 60.935  0 308 ASN AAA CG    1 ? 1 
ATOM   2193  O OD1   . ASN A 1 308 ? -14.676 12.316  37.671  1.000 58.913  0 308 ASN AAA OD1   1 ? 1 
ATOM   2194  N ND2   . ASN A 1 308 ? -13.333 13.546  38.955  1.000 68.054  0 308 ASN AAA ND2   1 ? 1 
ATOM   2195  N N     . ALA A 1 309 ? -14.577 13.736  34.010  1.000 49.745  0 309 ALA AAA N     1 ? 1 
ATOM   2196  C CA    . ALA A 1 309 ? -15.840 14.174  33.380  1.000 50.682  0 309 ALA AAA CA    1 ? 1 
ATOM   2197  C C     . ALA A 1 309 ? -16.317 13.161  32.318  1.000 49.296  0 309 ALA AAA C     1 ? 1 
ATOM   2198  O O     . ALA A 1 309 ? -17.544 13.072  32.102  1.000 44.456  0 309 ALA AAA O     1 ? 1 
ATOM   2199  C CB    . ALA A 1 309 ? -15.651 15.564  32.811  1.000 52.177  0 309 ALA AAA CB    1 ? 1 
ATOM   2200  N N     . ILE A 1 310 ? -15.410 12.415  31.670  1.000 49.427  0 310 ILE AAA N     1 ? 1 
ATOM   2201  C CA    . ILE A 1 310 ? -15.768 11.500  30.541  1.000 48.759  0 310 ILE AAA CA    1 ? 1 
ATOM   2202  C C     . ILE A 1 310 ? -16.101 10.107  31.080  1.000 47.121  0 310 ILE AAA C     1 ? 1 
ATOM   2203  O O     . ILE A 1 310 ? -16.756 9.354   30.348  1.000 47.607  0 310 ILE AAA O     1 ? 1 
ATOM   2204  C CB    . ILE A 1 310 ? -14.636 11.461  29.496  1.000 52.792  0 310 ILE AAA CB    1 ? 1 
ATOM   2205  C CG1   . ILE A 1 310 ? -14.291 12.871  29.014  1.000 55.499  0 310 ILE AAA CG1   1 ? 1 
ATOM   2206  C CG2   . ILE A 1 310 ? -14.949 10.519  28.343  1.000 53.091  0 310 ILE AAA CG2   1 ? 1 
ATOM   2207  C CD1   . ILE A 1 310 ? -15.495 13.734  28.743  1.000 57.638  0 310 ILE AAA CD1   1 ? 1 
ATOM   2208  N N     . GLY A 1 311 ? -15.677 9.786   32.306  1.000 45.739  0 311 GLY AAA N     1 ? 1 
ATOM   2209  C CA    . GLY A 1 311 ? -15.869 8.464   32.933  1.000 44.584  0 311 GLY AAA CA    1 ? 1 
ATOM   2210  C C     . GLY A 1 311 ? -14.700 7.512   32.692  1.000 43.495  0 311 GLY AAA C     1 ? 1 
ATOM   2211  O O     . GLY A 1 311 ? -14.937 6.303   32.767  1.000 45.611  0 311 GLY AAA O     1 ? 1 
ATOM   2212  N N     . VAL A 1 312 ? -13.482 8.006   32.450  1.000 41.990  0 312 VAL AAA N     1 ? 1 
ATOM   2213  C CA    . VAL A 1 312 ? -12.273 7.130   32.305  1.000 40.107  0 312 VAL AAA CA    1 ? 1 
ATOM   2214  C C     . VAL A 1 312 ? -11.707 6.862   33.699  1.000 37.947  0 312 VAL AAA C     1 ? 1 
ATOM   2215  O O     . VAL A 1 312 ? -11.192 7.795   34.300  1.000 35.225  0 312 VAL AAA O     1 ? 1 
ATOM   2216  C CB    . VAL A 1 312 ? -11.190 7.714   31.383  1.000 38.874  0 312 VAL AAA CB    1 ? 1 
ATOM   2217  C CG1   . VAL A 1 312 ? -9.914  6.898   31.484  1.000 38.412  0 312 VAL AAA CG1   1 ? 1 
ATOM   2218  C CG2   . VAL A 1 312 ? -11.659 7.794   29.938  1.000 39.554  0 312 VAL AAA CG2   1 ? 1 
ATOM   2219  N N     . GLU A 1 313 ? -11.782 5.613   34.157  1.000 37.892  0 313 GLU AAA N     1 ? 1 
ATOM   2220  C CA    . GLU A 1 313 ? -11.468 5.248   35.558  1.000 40.016  0 313 GLU AAA CA    1 ? 1 
ATOM   2221  C C     . GLU A 1 313 ? -9.936  5.257   35.721  1.000 40.022  0 313 GLU AAA C     1 ? 1 
ATOM   2222  O O     . GLU A 1 313 ? -9.189  4.779   34.812  1.000 38.364  0 313 GLU AAA O     1 ? 1 
ATOM   2223  C CB    . GLU A 1 313 ? -12.067 3.889   35.938  1.000 42.036  0 313 GLU AAA CB    1 ? 1 
ATOM   2224  C CG    . GLU A 1 313 ? -13.594 3.788   35.933  1.000 44.855  0 313 GLU AAA CG    1 ? 1 
ATOM   2225  C CD    . GLU A 1 313 ? -14.506 4.775   36.662  1.000 47.179  0 313 GLU AAA CD    1 ? 1 
ATOM   2226  O OE1   . GLU A 1 313 ? -14.310 5.023   37.882  1.000 49.896  0 313 GLU AAA OE1   1 ? 1 
ATOM   2227  O OE2   . GLU A 1 313 ? -15.486 5.228   36.029  1.000 47.659  0 313 GLU AAA OE2   1 ? 1 
ATOM   2228  N N     . VAL A 1 314 ? -9.476  5.744   36.870  1.000 39.275  0 314 VAL AAA N     1 ? 1 
ATOM   2229  C CA    . VAL A 1 314 ? -8.033  5.822   37.235  1.000 39.335  0 314 VAL AAA CA    1 ? 1 
ATOM   2230  C C     . VAL A 1 314 ? -7.842  5.126   38.579  1.000 39.250  0 314 VAL AAA C     1 ? 1 
ATOM   2231  O O     . VAL A 1 314 ? -8.797  5.106   39.379  1.000 43.086  0 314 VAL AAA O     1 ? 1 
ATOM   2232  C CB    . VAL A 1 314 ? -7.527  7.282   37.249  1.000 39.745  0 314 VAL AAA CB    1 ? 1 
ATOM   2233  C CG1   . VAL A 1 314 ? -7.628  7.903   35.849  1.000 38.509  0 314 VAL AAA CG1   1 ? 1 
ATOM   2234  C CG2   . VAL A 1 314 ? -8.242  8.133   38.312  1.000 39.261  0 314 VAL AAA CG2   1 ? 1 
ATOM   2235  N N     . SER A 1 315 ? -6.651  4.580   38.821  1.000 37.072  0 315 SER AAA N     1 ? 1 
ATOM   2236  C CA    . SER A 1 315 ? -6.262  3.943   40.099  1.000 37.880  0 315 SER AAA CA    1 ? 1 
ATOM   2237  C C     . SER A 1 315 ? -5.910  5.035   41.120  1.000 38.412  0 315 SER AAA C     1 ? 1 
ATOM   2238  O O     . SER A 1 315 ? -5.977  6.233   40.793  1.000 35.286  0 315 SER AAA O     1 ? 1 
ATOM   2239  C CB    . SER A 1 315 ? -5.101  2.991   39.890  1.000 38.028  0 315 SER AAA CB    1 ? 1 
ATOM   2240  O OG    . SER A 1 315 ? -3.900  3.724   39.672  1.000 37.082  0 315 SER AAA OG    1 ? 1 
ATOM   2241  N N     . ASP A 1 316 ? -5.525  4.622   42.322  1.000 42.487  0 316 ASP AAA N     1 ? 1 
ATOM   2242  C CA    . ASP A 1 316 ? -5.125  5.531   43.435  1.000 44.689  0 316 ASP AAA CA    1 ? 1 
ATOM   2243  C C     . ASP A 1 316 ? -3.853  6.285   43.043  1.000 43.536  0 316 ASP AAA C     1 ? 1 
ATOM   2244  O O     . ASP A 1 316 ? -3.682  7.387   43.520  1.000 45.050  0 316 ASP AAA O     1 ? 1 
ATOM   2245  C CB    . ASP A 1 316 ? -4.996  4.753   44.753  1.000 45.955  0 316 ASP AAA CB    1 ? 1 
ATOM   2246  C CG    . ASP A 1 316 ? -6.346  4.244   45.278  1.000 46.581  0 316 ASP AAA CG    1 ? 1 
ATOM   2247  O OD1   . ASP A 1 316 ? -7.357  4.988   45.148  1.000 48.913  0 316 ASP AAA OD1   1 ? 1 
ATOM   2248  O OD2   . ASP A 1 316 ? -6.400  3.096   45.794  1.000 45.546  0 316 ASP AAA OD2   1 ? 1 
ATOM   2249  N N     . SER A 1 317 ? -3.018  5.717   42.169  1.000 43.873  0 317 SER AAA N     1 ? 1 
ATOM   2250  C CA    . SER A 1 317 ? -1.751  6.334   41.686  1.000 40.984  0 317 SER AAA CA    1 ? 1 
ATOM   2251  C C     . SER A 1 317 ? -2.014  7.350   40.566  1.000 37.789  0 317 SER AAA C     1 ? 1 
ATOM   2252  O O     . SER A 1 317 ? -1.038  8.048   40.174  1.000 37.661  0 317 SER AAA O     1 ? 1 
ATOM   2253  C CB    . SER A 1 317 ? -0.764  5.287   41.235  1.000 42.119  0 317 SER AAA CB    1 ? 1 
ATOM   2254  O OG    . SER A 1 317 ? -1.242  4.613   40.082  1.000 42.426  0 317 SER AAA OG    1 ? 1 
ATOM   2255  N N     . GLY A 1 318 ? -3.256  7.454   40.075  1.000 34.332  0 318 GLY AAA N     1 ? 1 
ATOM   2256  C CA    . GLY A 1 318 ? -3.612  8.316   38.925  1.000 33.166  0 318 GLY AAA CA    1 ? 1 
ATOM   2257  C C     . GLY A 1 318 ? -3.399  7.625   37.571  1.000 31.168  0 318 GLY AAA C     1 ? 1 
ATOM   2258  O O     . GLY A 1 318 ? -3.625  8.238   36.568  1.000 30.600  0 318 GLY AAA O     1 ? 1 
ATOM   2259  N N     . LYS A 1 319 ? -2.985  6.372   37.550  1.000 31.532  0 319 LYS AAA N     1 ? 1 
ATOM   2260  C CA    . LYS A 1 319 ? -2.808  5.597   36.297  1.000 33.151  0 319 LYS AAA CA    1 ? 1 
ATOM   2261  C C     . LYS A 1 319 ? -4.181  5.129   35.791  1.000 35.089  0 319 LYS AAA C     1 ? 1 
ATOM   2262  O O     . LYS A 1 319 ? -5.045  4.819   36.615  1.000 35.552  0 319 LYS AAA O     1 ? 1 
ATOM   2263  C CB    . LYS A 1 319 ? -1.824  4.444   36.498  1.000 31.290  0 319 LYS AAA CB    1 ? 1 
ATOM   2264  C CG    . LYS A 1 319 ? -0.362  4.859   36.504  1.000 31.031  0 319 LYS AAA CG    1 ? 1 
ATOM   2265  C CD    . LYS A 1 319 ? 0.592   3.709   36.177  1.000 30.312  0 319 LYS AAA CD    1 ? 1 
ATOM   2266  C CE    . LYS A 1 319 ? 2.032   4.157   36.114  1.000 29.254  0 319 LYS AAA CE    1 ? 1 
ATOM   2267  N NZ    . LYS A 1 319 ? 2.926   3.019   35.812  1.000 28.267  0 319 LYS AAA NZ    1 ? 1 
ATOM   2268  N N     . ILE A 1 320 ? -4.355  5.082   34.473  1.000 36.531  0 320 ILE AAA N     1 ? 1 
ATOM   2269  C CA    . ILE A 1 320 ? -5.617  4.632   33.823  1.000 37.642  0 320 ILE AAA CA    1 ? 1 
ATOM   2270  C C     . ILE A 1 320 ? -5.737  3.114   33.994  1.000 38.257  0 320 ILE AAA C     1 ? 1 
ATOM   2271  O O     . ILE A 1 320 ? -4.734  2.402   33.756  1.000 37.236  0 320 ILE AAA O     1 ? 1 
ATOM   2272  C CB    . ILE A 1 320 ? -5.618  5.026   32.341  1.000 38.977  0 320 ILE AAA CB    1 ? 1 
ATOM   2273  C CG1   . ILE A 1 320 ? -5.531  6.543   32.185  1.000 41.090  0 320 ILE AAA CG1   1 ? 1 
ATOM   2274  C CG2   . ILE A 1 320 ? -6.834  4.438   31.644  1.000 39.853  0 320 ILE AAA CG2   1 ? 1 
ATOM   2275  C CD1   . ILE A 1 320 ? -5.478  7.023   30.761  1.000 43.546  0 320 ILE AAA CD1   1 ? 1 
ATOM   2276  N N     . ILE A 1 321 ? -6.926  2.645   34.366  1.000 37.703  0 321 ILE AAA N     1 ? 1 
ATOM   2277  C CA    . ILE A 1 321 ? -7.240  1.199   34.467  1.000 38.810  0 321 ILE AAA CA    1 ? 1 
ATOM   2278  C C     . ILE A 1 321 ? -7.613  0.739   33.055  1.000 38.295  0 321 ILE AAA C     1 ? 1 
ATOM   2279  O O     . ILE A 1 321 ? -8.604  1.256   32.502  1.000 36.191  0 321 ILE AAA O     1 ? 1 
ATOM   2280  C CB    . ILE A 1 321 ? -8.319  0.935   35.541  1.000 41.448  0 321 ILE AAA CB    1 ? 1 
ATOM   2281  C CG1   . ILE A 1 321 ? -7.760  1.180   36.950  1.000 41.687  0 321 ILE AAA CG1   1 ? 1 
ATOM   2282  C CG2   . ILE A 1 321 ? -8.881  -0.476  35.433  1.000 43.468  0 321 ILE AAA CG2   1 ? 1 
ATOM   2283  C CD1   . ILE A 1 321 ? -8.828  1.371   38.018  1.000 42.470  0 321 ILE AAA CD1   1 ? 1 
ATOM   2284  N N     . ALA A 1 322 ? -6.771  -0.123  32.472  1.000 36.024  0 322 ALA AAA N     1 ? 1 
ATOM   2285  C CA    . ALA A 1 322 ? -6.914  -0.645  31.089  1.000 34.681  0 322 ALA AAA CA    1 ? 1 
ATOM   2286  C C     . ALA A 1 322 ? -6.078  -1.916  30.932  1.000 33.014  0 322 ALA AAA C     1 ? 1 
ATOM   2287  O O     . ALA A 1 322 ? -5.142  -1.948  30.162  1.000 28.059  0 322 ALA AAA O     1 ? 1 
ATOM   2288  C CB    . ALA A 1 322 ? -6.522  0.412   30.092  1.000 33.375  0 322 ALA AAA CB    1 ? 1 
ATOM   2289  N N     . PRO A 1 323 ? -6.405  -2.991  31.686  1.000 34.411  0 323 PRO AAA N     1 ? 1 
ATOM   2290  C CA    . PRO A 1 323 ? -5.577  -4.191  31.733  1.000 35.216  0 323 PRO AAA CA    1 ? 1 
ATOM   2291  C C     . PRO A 1 323 ? -5.404  -4.827  30.346  1.000 35.301  0 323 PRO AAA C     1 ? 1 
ATOM   2292  O O     . PRO A 1 323 ? -4.391  -5.494  30.135  1.000 33.961  0 323 PRO AAA O     1 ? 1 
ATOM   2293  C CB    . PRO A 1 323 ? -6.297  -5.157  32.706  1.000 34.628  0 323 PRO AAA CB    1 ? 1 
ATOM   2294  C CG    . PRO A 1 323 ? -7.687  -4.589  32.882  1.000 33.512  0 323 PRO AAA CG    1 ? 1 
ATOM   2295  C CD    . PRO A 1 323 ? -7.602  -3.111  32.548  1.000 33.626  0 323 PRO AAA CD    1 ? 1 
ATOM   2296  N N     . LYS A 1 324 ? -6.348  -4.576  29.436  1.000 37.663  0 324 LYS AAA N     1 ? 1 
ATOM   2297  C CA    . LYS A 1 324 ? -6.322  -5.047  28.016  1.000 36.565  0 324 LYS AAA CA    1 ? 1 
ATOM   2298  C C     . LYS A 1 324 ? -6.345  -3.842  27.069  1.000 34.151  0 324 LYS AAA C     1 ? 1 
ATOM   2299  O O     . LYS A 1 324 ? -6.884  -3.973  25.973  1.000 36.904  0 324 LYS AAA O     1 ? 1 
ATOM   2300  C CB    . LYS A 1 324 ? -7.533  -5.945  27.767  1.000 39.579  0 324 LYS AAA CB    1 ? 1 
ATOM   2301  C CG    . LYS A 1 324 ? -7.483  -7.294  28.459  1.000 44.625  0 324 LYS AAA CG    1 ? 1 
ATOM   2302  C CD    . LYS A 1 324 ? -8.774  -7.650  29.151  1.000 48.805  0 324 LYS AAA CD    1 ? 1 
ATOM   2303  C CE    . LYS A 1 324 ? -8.657  -8.909  29.989  1.000 53.505  0 324 LYS AAA CE    1 ? 1 
ATOM   2304  N NZ    . LYS A 1 324 ? -9.959  -9.622  30.126  1.000 55.393  0 324 LYS AAA NZ    1 ? 1 
ATOM   2305  N N     . ASP A 1 325 ? -5.801  -2.699  27.476  1.000 31.706  0 325 ASP AAA N     1 ? 1 
ATOM   2306  C CA    . ASP A 1 325 ? -5.696  -1.456  26.662  1.000 32.534  0 325 ASP AAA CA    1 ? 1 
ATOM   2307  C C     . ASP A 1 325 ? -7.035  -0.704  26.642  1.000 33.449  0 325 ASP AAA C     1 ? 1 
ATOM   2308  O O     . ASP A 1 325 ? -7.004  0.513   26.437  1.000 33.287  0 325 ASP AAA O     1 ? 1 
ATOM   2309  C CB    . ASP A 1 325 ? -5.176  -1.741  25.239  1.000 34.516  0 325 ASP AAA CB    1 ? 1 
ATOM   2310  C CG    . ASP A 1 325 ? -3.877  -2.572  25.182  1.000 34.385  0 325 ASP AAA CG    1 ? 1 
ATOM   2311  O OD1   . ASP A 1 325 ? -3.082  -2.535  26.147  1.000 31.748  0 325 ASP AAA OD1   1 ? 1 
ATOM   2312  O OD2   . ASP A 1 325 ? -3.684  -3.282  24.180  1.000 37.549  0 325 ASP AAA OD2   1 ? 1 
ATOM   2313  N N     . ALA A 1 326 ? -8.167  -1.378  26.874  1.000 34.920  0 326 ALA AAA N     1 ? 1 
ATOM   2314  C CA    . ALA A 1 326 ? -9.524  -0.776  26.882  1.000 36.175  0 326 ALA AAA CA    1 ? 1 
ATOM   2315  C C     . ALA A 1 326 ? -9.778  -0.157  28.267  1.000 35.216  0 326 ALA AAA C     1 ? 1 
ATOM   2316  O O     . ALA A 1 326 ? -9.718  -0.881  29.257  1.000 35.212  0 326 ALA AAA O     1 ? 1 
ATOM   2317  C CB    . ALA A 1 326 ? -10.577 -1.822  26.512  1.000 35.652  0 326 ALA AAA CB    1 ? 1 
ATOM   2318  N N     . THR A 1 327 ? -10.035 1.147   28.320  1.000 35.565  0 327 THR AAA N     1 ? 1 
ATOM   2319  C CA    . THR A 1 327 ? -10.478 1.873   29.532  1.000 37.295  0 327 THR AAA CA    1 ? 1 
ATOM   2320  C C     . THR A 1 327 ? -11.926 1.502   29.894  1.000 38.148  0 327 THR AAA C     1 ? 1 
ATOM   2321  O O     . THR A 1 327 ? -12.555 0.693   29.180  1.000 38.983  0 327 THR AAA O     1 ? 1 
ATOM   2322  C CB    . THR A 1 327 ? -10.375 3.396   29.356  1.000 37.019  0 327 THR AAA CB    1 ? 1 
ATOM   2323  O OG1   . THR A 1 327 ? -11.417 3.831   28.481  1.000 39.858  0 327 THR AAA OG1   1 ? 1 
ATOM   2324  C CG2   . THR A 1 327 ? -9.027  3.845   28.839  1.000 36.747  0 327 THR AAA CG2   1 ? 1 
ATOM   2325  N N     . SER A 1 328 ? -12.451 2.117   30.952  1.000 38.117  0 328 SER AAA N     1 ? 1 
ATOM   2326  C CA    . SER A 1 328 ? -13.870 2.002   31.384  1.000 38.251  0 328 SER AAA CA    1 ? 1 
ATOM   2327  C C     . SER A 1 328 ? -14.815 2.582   30.322  1.000 38.253  0 328 SER AAA C     1 ? 1 
ATOM   2328  O O     . SER A 1 328 ? -16.015 2.246   30.385  1.000 34.259  0 328 SER AAA O     1 ? 1 
ATOM   2329  C CB    . SER A 1 328 ? -14.080 2.663   32.706  1.000 38.700  0 328 SER AAA CB    1 ? 1 
ATOM   2330  O OG    . SER A 1 328 ? -13.537 3.985   32.688  1.000 39.792  0 328 SER AAA OG    1 ? 1 
ATOM   2331  N N     . VAL A 1 329 ? -14.299 3.430   29.411  1.000 38.484  0 329 VAL AAA N     1 ? 1 
ATOM   2332  C CA    . VAL A 1 329 ? -15.059 3.995   28.263  1.000 38.912  0 329 VAL AAA CA    1 ? 1 
ATOM   2333  C C     . VAL A 1 329 ? -14.635 3.251   26.991  1.000 41.581  0 329 VAL AAA C     1 ? 1 
ATOM   2334  O O     . VAL A 1 329 ? -13.477 3.331   26.552  1.000 41.822  0 329 VAL AAA O     1 ? 1 
ATOM   2335  C CB    . VAL A 1 329 ? -14.842 5.512   28.160  1.000 39.242  0 329 VAL AAA CB    1 ? 1 
ATOM   2336  C CG1   . VAL A 1 329 ? -15.423 6.085   26.853  1.000 39.385  0 329 VAL AAA CG1   1 ? 1 
ATOM   2337  C CG2   . VAL A 1 329 ? -15.405 6.218   29.399  1.000 39.847  0 329 VAL AAA CG2   1 ? 1 
ATOM   2338  N N     . PRO A 1 330 ? -15.547 2.483   26.356  1.000 41.816  0 330 PRO AAA N     1 ? 1 
ATOM   2339  C CA    . PRO A 1 330 ? -15.123 1.450   25.407  1.000 42.124  0 330 PRO AAA CA    1 ? 1 
ATOM   2340  C C     . PRO A 1 330 ? -14.583 1.924   24.045  1.000 43.291  0 330 PRO AAA C     1 ? 1 
ATOM   2341  O O     . PRO A 1 330 ? -13.970 1.093   23.346  1.000 47.537  0 330 PRO AAA O     1 ? 1 
ATOM   2342  C CB    . PRO A 1 330 ? -16.368 0.587   25.199  1.000 43.409  0 330 PRO AAA CB    1 ? 1 
ATOM   2343  C CG    . PRO A 1 330 ? -17.546 1.437   25.695  1.000 44.041  0 330 PRO AAA CG    1 ? 1 
ATOM   2344  C CD    . PRO A 1 330 ? -17.002 2.556   26.557  1.000 41.633  0 330 PRO AAA CD    1 ? 1 
ATOM   2345  N N     . SER A 1 331 ? -14.736 3.214   23.723  1.000 40.402  0 331 SER AAA N     1 ? 1 
ATOM   2346  C CA    . SER A 1 331 ? -14.202 3.852   22.489  1.000 39.271  0 331 SER AAA CA    1 ? 1 
ATOM   2347  C C     . SER A 1 331 ? -12.804 4.431   22.768  1.000 39.443  0 331 SER AAA C     1 ? 1 
ATOM   2348  O O     . SER A 1 331 ? -12.164 4.969   21.824  1.000 39.849  0 331 SER AAA O     1 ? 1 
ATOM   2349  C CB    . SER A 1 331 ? -15.134 4.918   21.983  1.000 37.306  0 331 SER AAA CB    1 ? 1 
ATOM   2350  O OG    . SER A 1 331 ? -15.281 5.903   22.995  1.000 37.169  0 331 SER AAA OG    1 ? 1 
ATOM   2351  N N     . ILE A 1 332 ? -12.373 4.393   24.031  1.000 38.114  0 332 ILE AAA N     1 ? 1 
ATOM   2352  C CA    . ILE A 1 332 ? -11.116 5.032   24.485  1.000 37.366  0 332 ILE AAA CA    1 ? 1 
ATOM   2353  C C     . ILE A 1 332 ? -10.169 3.965   25.020  1.000 35.501  0 332 ILE AAA C     1 ? 1 
ATOM   2354  O O     . ILE A 1 332 ? -10.498 3.267   25.969  1.000 35.676  0 332 ILE AAA O     1 ? 1 
ATOM   2355  C CB    . ILE A 1 332 ? -11.391 6.135   25.519  1.000 38.214  0 332 ILE AAA CB    1 ? 1 
ATOM   2356  C CG1   . ILE A 1 332 ? -12.216 7.257   24.883  1.000 37.315  0 332 ILE AAA CG1   1 ? 1 
ATOM   2357  C CG2   . ILE A 1 332 ? -10.062 6.622   26.116  1.000 37.692  0 332 ILE AAA CG2   1 ? 1 
ATOM   2358  C CD1   . ILE A 1 332 ? -12.451 8.444   25.799  1.000 38.451  0 332 ILE AAA CD1   1 ? 1 
ATOM   2359  N N     . PHE A 1 333 ? -8.998  3.913   24.415  1.000 37.046  0 333 PHE AAA N     1 ? 1 
ATOM   2360  C CA    . PHE A 1 333 ? -7.926  2.935   24.689  1.000 35.598  0 333 PHE AAA CA    1 ? 1 
ATOM   2361  C C     . PHE A 1 333 ? -6.760  3.708   25.288  1.000 34.371  0 333 PHE AAA C     1 ? 1 
ATOM   2362  O O     . PHE A 1 333 ? -6.748  4.964   25.229  1.000 34.750  0 333 PHE AAA O     1 ? 1 
ATOM   2363  C CB    . PHE A 1 333 ? -7.593  2.172   23.410  1.000 35.770  0 333 PHE AAA CB    1 ? 1 
ATOM   2364  C CG    . PHE A 1 333 ? -8.736  1.334   22.913  1.000 38.038  0 333 PHE AAA CG    1 ? 1 
ATOM   2365  C CD1   . PHE A 1 333 ? -9.715  1.882   22.097  1.000 38.340  0 333 PHE AAA CD1   1 ? 1 
ATOM   2366  C CD2   . PHE A 1 333 ? -8.874  0.005   23.310  1.000 38.172  0 333 PHE AAA CD2   1 ? 1 
ATOM   2367  C CE1   . PHE A 1 333 ? -10.757 1.092   21.623  1.000 38.821  0 333 PHE AAA CE1   1 ? 1 
ATOM   2368  C CE2   . PHE A 1 333 ? -9.959  -0.759  22.891  1.000 37.869  0 333 PHE AAA CE2   1 ? 1 
ATOM   2369  C CZ    . PHE A 1 333 ? -10.869 -0.230  22.012  1.000 38.414  0 333 PHE AAA CZ    1 ? 1 
ATOM   2370  N N     . ALA A 1 334 ? -5.834  2.973   25.899  1.000 32.689  0 334 ALA AAA N     1 ? 1 
ATOM   2371  C CA    . ALA A 1 334 ? -4.610  3.547   26.488  1.000 31.270  0 334 ALA AAA CA    1 ? 1 
ATOM   2372  C C     . ALA A 1 334 ? -3.479  2.529   26.396  1.000 28.753  0 334 ALA AAA C     1 ? 1 
ATOM   2373  O O     . ALA A 1 334 ? -3.746  1.311   26.467  1.000 27.501  0 334 ALA AAA O     1 ? 1 
ATOM   2374  C CB    . ALA A 1 334 ? -4.908  3.965   27.900  1.000 31.204  0 334 ALA AAA CB    1 ? 1 
ATOM   2375  N N     . VAL A 1 335 ? -2.267  3.026   26.178  1.000 28.436  0 335 VAL AAA N     1 ? 1 
ATOM   2376  C CA    . VAL A 1 335 ? -1.017  2.207   26.170  1.000 28.208  0 335 VAL AAA CA    1 ? 1 
ATOM   2377  C C     . VAL A 1 335 ? 0.107   3.027   26.783  1.000 26.708  0 335 VAL AAA C     1 ? 1 
ATOM   2378  O O     . VAL A 1 335 ? -0.111  4.242   27.018  1.000 25.170  0 335 VAL AAA O     1 ? 1 
ATOM   2379  C CB    . VAL A 1 335 ? -0.645  1.757   24.749  1.000 29.179  0 335 VAL AAA CB    1 ? 1 
ATOM   2380  C CG1   . VAL A 1 335 ? -1.747  0.890   24.129  1.000 30.634  0 335 VAL AAA CG1   1 ? 1 
ATOM   2381  C CG2   . VAL A 1 335 ? -0.289  2.942   23.859  1.000 28.814  0 335 VAL AAA CG2   1 ? 1 
ATOM   2382  N N     . GLY A 1 336 ? 1.256   2.379   26.993  1.000 26.746  0 336 GLY AAA N     1 ? 1 
ATOM   2383  C CA    . GLY A 1 336 ? 2.463   3.003   27.568  1.000 27.230  0 336 GLY AAA CA    1 ? 1 
ATOM   2384  C C     . GLY A 1 336 ? 2.394   3.236   29.083  1.000 27.548  0 336 GLY AAA C     1 ? 1 
ATOM   2385  O O     . GLY A 1 336 ? 1.552   2.613   29.798  1.000 27.152  0 336 GLY AAA O     1 ? 1 
ATOM   2386  N N     . ASP A 1 337 ? 3.197   4.194   29.530  1.000 28.492  0 337 ASP AAA N     1 ? 1 
ATOM   2387  C CA    . ASP A 1 337 ? 3.515   4.471   30.951  1.000 29.747  0 337 ASP AAA CA    1 ? 1 
ATOM   2388  C C     . ASP A 1 337 ? 2.264   4.863   31.745  1.000 31.163  0 337 ASP AAA C     1 ? 1 
ATOM   2389  O O     . ASP A 1 337 ? 2.330   4.715   33.006  1.000 30.077  0 337 ASP AAA O     1 ? 1 
ATOM   2390  C CB    . ASP A 1 337 ? 4.528   5.607   31.103  1.000 30.836  0 337 ASP AAA CB    1 ? 1 
ATOM   2391  C CG    . ASP A 1 337 ? 5.954   5.278   30.690  1.000 31.202  0 337 ASP AAA CG    1 ? 1 
ATOM   2392  O OD1   . ASP A 1 337 ? 6.215   4.118   30.248  1.000 31.140  0 337 ASP AAA OD1   1 ? 1 
ATOM   2393  O OD2   . ASP A 1 337 ? 6.785   6.213   30.781  1.000 31.768  0 337 ASP AAA OD2   1 ? 1 
ATOM   2394  N N     . ILE A 1 338 ? 1.199   5.364   31.101  1.000 30.253  0 338 ILE AAA N     1 ? 1 
ATOM   2395  C CA    . ILE A 1 338 ? -0.011  5.853   31.850  1.000 30.858  0 338 ILE AAA CA    1 ? 1 
ATOM   2396  C C     . ILE A 1 338 ? -0.900  4.686   32.312  1.000 31.901  0 338 ILE AAA C     1 ? 1 
ATOM   2397  O O     . ILE A 1 338 ? -1.833  4.937   33.114  1.000 33.614  0 338 ILE AAA O     1 ? 1 
ATOM   2398  C CB    . ILE A 1 338 ? -0.829  6.868   31.022  1.000 30.578  0 338 ILE AAA CB    1 ? 1 
ATOM   2399  C CG1   . ILE A 1 338 ? -1.526  6.206   29.832  1.000 30.517  0 338 ILE AAA CG1   1 ? 1 
ATOM   2400  C CG2   . ILE A 1 338 ? 0.050   8.060   30.620  1.000 30.551  0 338 ILE AAA CG2   1 ? 1 
ATOM   2401  C CD1   . ILE A 1 338 ? -2.210  7.186   28.900  1.000 31.304  0 338 ILE AAA CD1   1 ? 1 
ATOM   2402  N N     . VAL A 1 339 ? -0.654  3.454   31.861  1.000 33.160  0 339 VAL AAA N     1 ? 1 
ATOM   2403  C CA    . VAL A 1 339 ? -1.571  2.321   32.167  1.000 34.609  0 339 VAL AAA CA    1 ? 1 
ATOM   2404  C C     . VAL A 1 339 ? -1.075  1.592   33.416  1.000 35.236  0 339 VAL AAA C     1 ? 1 
ATOM   2405  O O     . VAL A 1 339 ? 0.100   1.228   33.497  1.000 33.555  0 339 VAL AAA O     1 ? 1 
ATOM   2406  C CB    . VAL A 1 339 ? -1.745  1.375   30.959  1.000 35.460  0 339 VAL AAA CB    1 ? 1 
ATOM   2407  C CG1   . VAL A 1 339 ? -2.647  0.190   31.292  1.000 36.548  0 339 VAL AAA CG1   1 ? 1 
ATOM   2408  C CG2   . VAL A 1 339 ? -2.276  2.124   29.742  1.000 34.254  0 339 VAL AAA CG2   1 ? 1 
ATOM   2409  N N     . GLU A 1 340 ? -1.970  1.379   34.362  1.000 38.714  0 340 GLU AAA N     1 ? 1 
ATOM   2410  C CA    . GLU A 1 340 ? -1.667  0.666   35.620  1.000 40.524  0 340 GLU AAA CA    1 ? 1 
ATOM   2411  C C     . GLU A 1 340 ? -1.382  -0.812  35.337  1.000 39.323  0 340 GLU AAA C     1 ? 1 
ATOM   2412  O O     . GLU A 1 340 ? -2.112  -1.427  34.497  1.000 34.680  0 340 GLU AAA O     1 ? 1 
ATOM   2413  C CB    . GLU A 1 340 ? -2.821  0.764   36.612  1.000 48.168  0 340 GLU AAA CB    1 ? 1 
ATOM   2414  C CG    . GLU A 1 340 ? -2.675  -0.232  37.752  1.000 55.330  0 340 GLU AAA CG    1 ? 1 
ATOM   2415  C CD    . GLU A 1 340 ? -3.061  0.301   39.115  1.000 60.640  0 340 GLU AAA CD    1 ? 1 
ATOM   2416  O OE1   . GLU A 1 340 ? -4.100  -0.179  39.654  1.000 68.428  0 340 GLU AAA OE1   1 ? 1 
ATOM   2417  O OE2   . GLU A 1 340 ? -2.323  1.183   39.626  1.000 63.181  0 340 GLU AAA OE2   1 ? 1 
ATOM   2418  N N     . GLY A 1 341 ? -0.356  -1.348  36.027  1.000 36.551  0 341 GLY AAA N     1 ? 1 
ATOM   2419  C CA    . GLY A 1 341 ? -0.056  -2.785  36.095  1.000 35.108  0 341 GLY AAA CA    1 ? 1 
ATOM   2420  C C     . GLY A 1 341 ? 0.780   -3.274  34.930  1.000 34.353  0 341 GLY AAA C     1 ? 1 
ATOM   2421  O O     . GLY A 1 341 ? 0.812   -4.500  34.698  1.000 34.248  0 341 GLY AAA O     1 ? 1 
ATOM   2422  N N     . ARG A 1 342 ? 1.443   -2.382  34.204  1.000 33.206  0 342 ARG AAA N     1 ? 1 
ATOM   2423  C CA    . ARG A 1 342 ? 2.397   -2.810  33.154  1.000 33.999  0 342 ARG AAA CA    1 ? 1 
ATOM   2424  C C     . ARG A 1 342 ? 3.709   -2.034  33.294  1.000 31.632  0 342 ARG AAA C     1 ? 1 
ATOM   2425  O O     . ARG A 1 342 ? 3.741   -0.879  33.703  1.000 28.155  0 342 ARG AAA O     1 ? 1 
ATOM   2426  C CB    . ARG A 1 342 ? 1.795   -2.682  31.746  1.000 33.862  0 342 ARG AAA CB    1 ? 1 
ATOM   2427  C CG    . ARG A 1 342 ? 1.595   -1.247  31.259  1.000 34.209  0 342 ARG AAA CG    1 ? 1 
ATOM   2428  C CD    . ARG A 1 342 ? 1.000   -1.229  29.845  1.000 34.139  0 342 ARG AAA CD    1 ? 1 
ATOM   2429  N NE    . ARG A 1 342 ? -0.354  -1.775  29.784  1.000 34.259  0 342 ARG AAA NE    1 ? 1 
ATOM   2430  C CZ    . ARG A 1 342 ? -1.106  -1.849  28.697  1.000 33.761  0 342 ARG AAA CZ    1 ? 1 
ATOM   2431  N NH1   . ARG A 1 342 ? -0.635  -1.443  27.539  1.000 34.151  0 342 ARG AAA NH1   1 ? 1 
ATOM   2432  N NH2   . ARG A 1 342 ? -2.339  -2.335  28.755  1.000 33.281  0 342 ARG AAA NH2   1 ? 1 
ATOM   2433  N N     . PRO A 1 343 ? 4.829   -2.677  32.906  1.000 31.535  0 343 PRO AAA N     1 ? 1 
ATOM   2434  C CA    . PRO A 1 343 ? 6.142   -2.049  32.960  1.000 32.028  0 343 PRO AAA CA    1 ? 1 
ATOM   2435  C C     . PRO A 1 343 ? 6.208   -0.794  32.084  1.000 32.344  0 343 PRO AAA C     1 ? 1 
ATOM   2436  O O     . PRO A 1 343 ? 5.675   -0.783  31.033  1.000 32.098  0 343 PRO AAA O     1 ? 1 
ATOM   2437  C CB    . PRO A 1 343 ? 7.096   -3.130  32.439  1.000 31.088  0 343 PRO AAA CB    1 ? 1 
ATOM   2438  C CG    . PRO A 1 343 ? 6.335   -4.425  32.568  1.000 31.517  0 343 PRO AAA CG    1 ? 1 
ATOM   2439  C CD    . PRO A 1 343 ? 4.885   -4.047  32.379  1.000 31.269  0 343 PRO AAA CD    1 ? 1 
ATOM   2440  N N     . GLU A 1 344 ? 6.857   0.242   32.590  1.000 32.746  0 344 GLU AAA N     1 ? 1 
ATOM   2441  C CA    . GLU A 1 344 ? 7.074   1.520   31.874  1.000 33.604  0 344 GLU AAA CA    1 ? 1 
ATOM   2442  C C     . GLU A 1 344 ? 8.330   1.370   31.015  1.000 32.090  0 344 GLU AAA C     1 ? 1 
ATOM   2443  O O     . GLU A 1 344 ? 9.341   1.999   31.368  1.000 32.568  0 344 GLU AAA O     1 ? 1 
ATOM   2444  C CB    . GLU A 1 344 ? 7.250   2.665   32.888  1.000 36.520  0 344 GLU AAA CB    1 ? 1 
ATOM   2445  C CG    . GLU A 1 344 ? 6.052   2.906   33.805  1.000 37.798  0 344 GLU AAA CG    1 ? 1 
ATOM   2446  C CD    . GLU A 1 344 ? 6.240   3.919   34.921  1.000 41.248  0 344 GLU AAA CD    1 ? 1 
ATOM   2447  O OE1   . GLU A 1 344 ? 7.303   4.626   34.989  1.000 43.242  0 344 GLU AAA OE1   1 ? 1 
ATOM   2448  O OE2   . GLU A 1 344 ? 5.320   3.995   35.741  1.000 42.128  0 344 GLU AAA OE2   1 ? 1 
ATOM   2449  N N     . LEU A 1 345 ? 8.254   0.599   29.929  1.000 30.024  0 345 LEU AAA N     1 ? 1 
ATOM   2450  C CA    . LEU A 1 345 ? 9.384   0.353   28.983  1.000 27.582  0 345 LEU AAA CA    1 ? 1 
ATOM   2451  C C     . LEU A 1 345 ? 8.941   0.694   27.557  1.000 26.529  0 345 LEU AAA C     1 ? 1 
ATOM   2452  O O     . LEU A 1 345 ? 7.714   0.541   27.258  1.000 24.566  0 345 LEU AAA O     1 ? 1 
ATOM   2453  C CB    . LEU A 1 345 ? 9.771   -1.132  29.060  1.000 28.273  0 345 LEU AAA CB    1 ? 1 
ATOM   2454  C CG    . LEU A 1 345 ? 10.281  -1.638  30.407  1.000 29.127  0 345 LEU AAA CG    1 ? 1 
ATOM   2455  C CD1   . LEU A 1 345 ? 10.417  -3.157  30.403  1.000 28.722  0 345 LEU AAA CD1   1 ? 1 
ATOM   2456  C CD2   . LEU A 1 345 ? 11.599  -0.977  30.748  1.000 29.128  0 345 LEU AAA CD2   1 ? 1 
ATOM   2457  N N     . THR A 1 346 ? 9.877   1.075   26.679  1.000 24.798  0 346 THR AAA N     1 ? 1 
ATOM   2458  C CA    . THR A 1 346 ? 9.546   1.539   25.310  1.000 24.952  0 346 THR AAA CA    1 ? 1 
ATOM   2459  C C     . THR A 1 346 ? 8.969   0.392   24.494  1.000 24.923  0 346 THR AAA C     1 ? 1 
ATOM   2460  O O     . THR A 1 346 ? 7.912   0.548   23.898  1.000 25.454  0 346 THR AAA O     1 ? 1 
ATOM   2461  C CB    . THR A 1 346 ? 10.746  2.212   24.638  1.000 24.968  0 346 THR AAA CB    1 ? 1 
ATOM   2462  O OG1   . THR A 1 346 ? 10.652  3.589   24.948  1.000 25.572  0 346 THR AAA OG1   1 ? 1 
ATOM   2463  C CG2   . THR A 1 346 ? 10.794  2.119   23.132  1.000 24.708  0 346 THR AAA CG2   1 ? 1 
ATOM   2464  N N     . PRO A 1 347 ? 9.640   -0.792  24.407  1.000 24.777  0 347 PRO AAA N     1 ? 1 
ATOM   2465  C CA    . PRO A 1 347 ? 9.113   -1.910  23.617  1.000 24.323  0 347 PRO AAA CA    1 ? 1 
ATOM   2466  C C     . PRO A 1 347 ? 7.700   -2.348  24.020  1.000 25.081  0 347 PRO AAA C     1 ? 1 
ATOM   2467  O O     . PRO A 1 347 ? 6.995   -2.774  23.178  1.000 27.103  0 347 PRO AAA O     1 ? 1 
ATOM   2468  C CB    . PRO A 1 347 ? 10.170  -3.000  23.819  1.000 23.800  0 347 PRO AAA CB    1 ? 1 
ATOM   2469  C CG    . PRO A 1 347 ? 11.429  -2.207  24.085  1.000 23.979  0 347 PRO AAA CG    1 ? 1 
ATOM   2470  C CD    . PRO A 1 347 ? 10.945  -1.106  25.004  1.000 23.629  0 347 PRO AAA CD    1 ? 1 
ATOM   2471  N N     . VAL A 1 348 ? 7.315   -2.211  25.282  1.000 26.492  0 348 VAL AAA N     1 ? 1 
ATOM   2472  C CA    . VAL A 1 348 ? 5.954   -2.552  25.787  1.000 27.515  0 348 VAL AAA CA    1 ? 1 
ATOM   2473  C C     . VAL A 1 348 ? 4.956   -1.538  25.224  1.000 27.869  0 348 VAL AAA C     1 ? 1 
ATOM   2474  O O     . VAL A 1 348 ? 3.883   -1.972  24.772  1.000 30.950  0 348 VAL AAA O     1 ? 1 
ATOM   2475  C CB    . VAL A 1 348 ? 5.914   -2.556  27.319  1.000 27.586  0 348 VAL AAA CB    1 ? 1 
ATOM   2476  C CG1   . VAL A 1 348 ? 4.534   -2.885  27.875  1.000 27.773  0 348 VAL AAA CG1   1 ? 1 
ATOM   2477  C CG2   . VAL A 1 348 ? 6.947   -3.505  27.867  1.000 28.569  0 348 VAL AAA CG2   1 ? 1 
ATOM   2478  N N     . ALA A 1 349 ? 5.300   -0.258  25.254  1.000 26.840  0 349 ALA AAA N     1 ? 1 
ATOM   2479  C CA    . ALA A 1 349 ? 4.504   0.832   24.663  1.000 27.439  0 349 ALA AAA CA    1 ? 1 
ATOM   2480  C C     . ALA A 1 349 ? 4.266   0.543   23.169  1.000 28.354  0 349 ALA AAA C     1 ? 1 
ATOM   2481  O O     . ALA A 1 349 ? 3.098   0.491   22.725  1.000 29.210  0 349 ALA AAA O     1 ? 1 
ATOM   2482  C CB    . ALA A 1 349 ? 5.220   2.135   24.892  1.000 26.502  0 349 ALA AAA CB    1 ? 1 
ATOM   2483  N N     . VAL A 1 350 ? 5.340   0.373   22.413  1.000 28.969  0 350 VAL AAA N     1 ? 1 
ATOM   2484  C CA    . VAL A 1 350 ? 5.342   0.114   20.938  1.000 29.568  0 350 VAL AAA CA    1 ? 1 
ATOM   2485  C C     . VAL A 1 350 ? 4.467   -1.109  20.627  1.000 29.369  0 350 VAL AAA C     1 ? 1 
ATOM   2486  O O     . VAL A 1 350 ? 3.561   -0.969  19.816  1.000 27.077  0 350 VAL AAA O     1 ? 1 
ATOM   2487  C CB    . VAL A 1 350 ? 6.777   -0.083  20.407  1.000 29.408  0 350 VAL AAA CB    1 ? 1 
ATOM   2488  C CG1   . VAL A 1 350 ? 6.806   -0.594  18.975  1.000 29.242  0 350 VAL AAA CG1   1 ? 1 
ATOM   2489  C CG2   . VAL A 1 350 ? 7.574   1.218   20.512  1.000 30.017  0 350 VAL AAA CG2   1 ? 1 
ATOM   2490  N N     . LYS A 1 351 ? 4.756   -2.271  21.209  1.000 29.923  0 351 LYS AAA N     1 ? 1 
ATOM   2491  C CA    . LYS A 1 351 ? 4.052   -3.513  20.801  1.000 31.266  0 351 LYS AAA CA    1 ? 1 
ATOM   2492  C C     . LYS A 1 351 ? 2.571   -3.403  21.186  1.000 30.779  0 351 LYS AAA C     1 ? 1 
ATOM   2493  O O     . LYS A 1 351 ? 1.734   -3.857  20.438  1.000 33.292  0 351 LYS AAA O     1 ? 1 
ATOM   2494  C CB    . LYS A 1 351 ? 4.689   -4.777  21.373  1.000 31.845  0 351 LYS AAA CB    1 ? 1 
ATOM   2495  C CG    . LYS A 1 351 ? 4.046   -6.042  20.829  1.000 35.348  0 351 LYS AAA CG    1 ? 1 
ATOM   2496  C CD    . LYS A 1 351 ? 4.789   -7.337  21.150  1.000 38.481  0 351 LYS AAA CD    1 ? 1 
ATOM   2497  C CE    . LYS A 1 351 ? 6.069   -7.543  20.357  1.000 38.851  0 351 LYS AAA CE    1 ? 1 
ATOM   2498  N NZ    . LYS A 1 351 ? 5.785   -7.795  18.917  1.000 39.860  0 351 LYS AAA NZ    1 ? 1 
ATOM   2499  N N     . ALA A 1 352 ? 2.242   -2.815  22.317  1.000 31.859  0 352 ALA AAA N     1 ? 1 
ATOM   2500  C CA    . ALA A 1 352 ? 0.828   -2.607  22.715  1.000 32.982  0 352 ALA AAA CA    1 ? 1 
ATOM   2501  C C     . ALA A 1 352 ? 0.145   -1.720  21.662  1.000 33.247  0 352 ALA AAA C     1 ? 1 
ATOM   2502  O O     . ALA A 1 352 ? -0.991  -2.037  21.297  1.000 31.605  0 352 ALA AAA O     1 ? 1 
ATOM   2503  C CB    . ALA A 1 352 ? 0.714   -2.020  24.102  1.000 32.321  0 352 ALA AAA CB    1 ? 1 
ATOM   2504  N N     . GLY A 1 353 ? 0.842   -0.676  21.195  1.000 33.397  0 353 GLY AAA N     1 ? 1 
ATOM   2505  C CA    . GLY A 1 353 ? 0.325   0.264   20.192  1.000 34.809  0 353 GLY AAA CA    1 ? 1 
ATOM   2506  C C     . GLY A 1 353 ? 0.048   -0.442  18.876  1.000 36.397  0 353 GLY AAA C     1 ? 1 
ATOM   2507  O O     . GLY A 1 353 ? -1.058  -0.249  18.293  1.000 38.934  0 353 GLY AAA O     1 ? 1 
ATOM   2508  N N     . ILE A 1 354 ? 1.002   -1.251  18.423  1.000 35.323  0 354 ILE AAA N     1 ? 1 
ATOM   2509  C CA    . ILE A 1 354 ? 0.897   -2.017  17.154  1.000 34.937  0 354 ILE AAA CA    1 ? 1 
ATOM   2510  C C     . ILE A 1 354 ? -0.211  -3.072  17.282  1.000 33.407  0 354 ILE AAA C     1 ? 1 
ATOM   2511  O O     . ILE A 1 354 ? -1.023  -3.135  16.353  1.000 31.105  0 354 ILE AAA O     1 ? 1 
ATOM   2512  C CB    . ILE A 1 354 ? 2.256   -2.628  16.758  1.000 36.414  0 354 ILE AAA CB    1 ? 1 
ATOM   2513  C CG1   . ILE A 1 354 ? 3.306   -1.549  16.464  1.000 36.329  0 354 ILE AAA CG1   1 ? 1 
ATOM   2514  C CG2   . ILE A 1 354 ? 2.071   -3.571  15.565  1.000 37.045  0 354 ILE AAA CG2   1 ? 1 
ATOM   2515  C CD1   . ILE A 1 354 ? 4.705   -2.104  16.205  1.000 36.146  0 354 ILE AAA CD1   1 ? 1 
ATOM   2516  N N     . LEU A 1 355 ? -0.240  -3.866  18.359  1.000 33.231  0 355 LEU AAA N     1 ? 1 
ATOM   2517  C CA    . LEU A 1 355 ? -1.228  -4.967  18.527  1.000 34.436  0 355 LEU AAA CA    1 ? 1 
ATOM   2518  C C     . LEU A 1 355 ? -2.634  -4.353  18.631  1.000 36.382  0 355 LEU AAA C     1 ? 1 
ATOM   2519  O O     . LEU A 1 355 ? -3.566  -4.921  18.026  1.000 38.461  0 355 LEU AAA O     1 ? 1 
ATOM   2520  C CB    . LEU A 1 355 ? -0.899  -5.828  19.753  1.000 34.344  0 355 LEU AAA CB    1 ? 1 
ATOM   2521  C CG    . LEU A 1 355 ? 0.384   -6.674  19.698  1.000 35.739  0 355 LEU AAA CG    1 ? 1 
ATOM   2522  C CD1   . LEU A 1 355 ? 0.400   -7.674  20.841  1.000 34.869  0 355 LEU AAA CD1   1 ? 1 
ATOM   2523  C CD2   . LEU A 1 355 ? 0.623   -7.381  18.337  1.000 34.962  0 355 LEU AAA CD2   1 ? 1 
ATOM   2524  N N     . LEU A 1 356 ? -2.786  -3.223  19.322  1.000 35.517  0 356 LEU AAA N     1 ? 1 
ATOM   2525  C CA    . LEU A 1 356 ? -4.083  -2.512  19.436  1.000 37.234  0 356 LEU AAA CA    1 ? 1 
ATOM   2526  C C     . LEU A 1 356 ? -4.544  -2.126  18.023  1.000 37.574  0 356 LEU AAA C     1 ? 1 
ATOM   2527  O O     . LEU A 1 356 ? -5.629  -2.554  17.621  1.000 38.959  0 356 LEU AAA O     1 ? 1 
ATOM   2528  C CB    . LEU A 1 356 ? -3.944  -1.287  20.352  1.000 37.142  0 356 LEU AAA CB    1 ? 1 
ATOM   2529  C CG    . LEU A 1 356 ? -5.154  -0.351  20.387  1.000 38.963  0 356 LEU AAA CG    1 ? 1 
ATOM   2530  C CD1   . LEU A 1 356 ? -6.407  -1.032  20.914  1.000 38.644  0 356 LEU AAA CD1   1 ? 1 
ATOM   2531  C CD2   . LEU A 1 356 ? -4.867  0.871   21.241  1.000 40.386  0 356 LEU AAA CD2   1 ? 1 
ATOM   2532  N N     . ALA A 1 357 ? -3.740  -1.365  17.296  1.000 38.287  0 357 ALA AAA N     1 ? 1 
ATOM   2533  C CA    . ALA A 1 357 ? -3.989  -1.004  15.872  1.000 40.356  0 357 ALA AAA CA    1 ? 1 
ATOM   2534  C C     . ALA A 1 357 ? -4.461  -2.232  15.074  1.000 40.693  0 357 ALA AAA C     1 ? 1 
ATOM   2535  O O     . ALA A 1 357 ? -5.489  -2.123  14.387  1.000 42.412  0 357 ALA AAA O     1 ? 1 
ATOM   2536  C CB    . ALA A 1 357 ? -2.759  -0.376  15.257  1.000 40.234  0 357 ALA AAA CB    1 ? 1 
ATOM   2537  N N     . ARG A 1 358 ? -3.790  -3.374  15.194  1.000 40.836  0 358 ARG AAA N     1 ? 1 
ATOM   2538  C CA    . ARG A 1 358 ? -4.151  -4.613  14.454  1.000 42.791  0 358 ARG AAA CA    1 ? 1 
ATOM   2539  C C     . ARG A 1 358 ? -5.498  -5.175  14.923  1.000 44.744  0 358 ARG AAA C     1 ? 1 
ATOM   2540  O O     . ARG A 1 358 ? -6.264  -5.593  14.054  1.000 47.718  0 358 ARG AAA O     1 ? 1 
ATOM   2541  C CB    . ARG A 1 358 ? -3.088  -5.693  14.616  1.000 42.404  0 358 ARG AAA CB    1 ? 1 
ATOM   2542  C CG    . ARG A 1 358 ? -1.862  -5.429  13.769  1.000 43.526  0 358 ARG AAA CG    1 ? 1 
ATOM   2543  C CD    . ARG A 1 358 ? -0.756  -6.434  14.003  1.000 42.716  0 358 ARG AAA CD    1 ? 1 
ATOM   2544  N NE    . ARG A 1 358 ? 0.458   -5.913  13.388  1.000 44.654  0 358 ARG AAA NE    1 ? 1 
ATOM   2545  C CZ    . ARG A 1 358 ? 1.673   -6.420  13.584  1.000 44.082  0 358 ARG AAA CZ    1 ? 1 
ATOM   2546  N NH1   . ARG A 1 358 ? 1.819   -7.462  14.390  1.000 42.823  0 358 ARG AAA NH1   1 ? 1 
ATOM   2547  N NH2   . ARG A 1 358 ? 2.725   -5.863  13.000  1.000 42.733  0 358 ARG AAA NH2   1 ? 1 
ATOM   2548  N N     . ARG A 1 359 ? -5.763  -5.228  16.230  1.000 44.134  0 359 ARG AAA N     1 ? 1 
ATOM   2549  C CA    . ARG A 1 359 ? -7.032  -5.768  16.782  1.000 42.513  0 359 ARG AAA CA    1 ? 1 
ATOM   2550  C C     . ARG A 1 359 ? -8.193  -4.906  16.264  1.000 43.754  0 359 ARG AAA C     1 ? 1 
ATOM   2551  O O     . ARG A 1 359 ? -9.284  -5.485  15.954  1.000 43.528  0 359 ARG AAA O     1 ? 1 
ATOM   2552  C CB    . ARG A 1 359 ? -7.012  -5.804  18.317  1.000 41.153  0 359 ARG AAA CB    1 ? 1 
ATOM   2553  C CG    . ARG A 1 359 ? -6.101  -6.869  18.914  1.000 39.809  0 359 ARG AAA CG    1 ? 1 
ATOM   2554  C CD    . ARG A 1 359 ? -6.453  -7.233  20.351  1.000 38.794  0 359 ARG AAA CD    1 ? 1 
ATOM   2555  N NE    . ARG A 1 359 ? -6.505  -6.051  21.226  1.000 37.341  0 359 ARG AAA NE    1 ? 1 
ATOM   2556  C CZ    . ARG A 1 359 ? -5.447  -5.411  21.704  1.000 34.409  0 359 ARG AAA CZ    1 ? 1 
ATOM   2557  N NH1   . ARG A 1 359 ? -4.227  -5.830  21.430  1.000 33.685  0 359 ARG AAA NH1   1 ? 1 
ATOM   2558  N NH2   . ARG A 1 359 ? -5.610  -4.350  22.469  1.000 35.216  0 359 ARG AAA NH2   1 ? 1 
ATOM   2559  N N     . LEU A 1 360 ? -7.987  -3.588  16.188  1.000 42.574  0 360 LEU AAA N     1 ? 1 
ATOM   2560  C CA    . LEU A 1 360 ? -9.056  -2.623  15.817  1.000 44.687  0 360 LEU AAA CA    1 ? 1 
ATOM   2561  C C     . LEU A 1 360 ? -9.364  -2.755  14.318  1.000 46.038  0 360 LEU AAA C     1 ? 1 
ATOM   2562  O O     . LEU A 1 360 ? -10.579 -2.654  13.977  1.000 48.112  0 360 LEU AAA O     1 ? 1 
ATOM   2563  C CB    . LEU A 1 360 ? -8.640  -1.190  16.168  1.000 43.008  0 360 LEU AAA CB    1 ? 1 
ATOM   2564  C CG    . LEU A 1 360 ? -8.566  -0.843  17.661  1.000 42.060  0 360 LEU AAA CG    1 ? 1 
ATOM   2565  C CD1   . LEU A 1 360 ? -8.123  0.601   17.867  1.000 39.938  0 360 LEU AAA CD1   1 ? 1 
ATOM   2566  C CD2   . LEU A 1 360 ? -9.871  -1.125  18.413  1.000 42.147  0 360 LEU AAA CD2   1 ? 1 
ATOM   2567  N N     . PHE A 1 361 ? -8.345  -2.995  13.470  1.000 43.920  0 361 PHE AAA N     1 ? 1 
ATOM   2568  C CA    . PHE A 1 361 ? -8.422  -2.720  12.010  1.000 44.015  0 361 PHE AAA CA    1 ? 1 
ATOM   2569  C C     . PHE A 1 361 ? -7.938  -3.880  11.129  1.000 45.246  0 361 PHE AAA C     1 ? 1 
ATOM   2570  O O     . PHE A 1 361 ? -8.130  -3.735  9.893   1.000 45.102  0 361 PHE AAA O     1 ? 1 
ATOM   2571  C CB    . PHE A 1 361 ? -7.633  -1.455  11.658  1.000 43.849  0 361 PHE AAA CB    1 ? 1 
ATOM   2572  C CG    . PHE A 1 361 ? -8.100  -0.204  12.364  1.000 44.102  0 361 PHE AAA CG    1 ? 1 
ATOM   2573  C CD1   . PHE A 1 361 ? -9.417  0.234   12.234  1.000 43.834  0 361 PHE AAA CD1   1 ? 1 
ATOM   2574  C CD2   . PHE A 1 361 ? -7.228  0.536   13.159  1.000 42.607  0 361 PHE AAA CD2   1 ? 1 
ATOM   2575  C CE1   . PHE A 1 361 ? -9.849  1.372   12.892  1.000 43.057  0 361 PHE AAA CE1   1 ? 1 
ATOM   2576  C CE2   . PHE A 1 361 ? -7.659  1.684   13.804  1.000 42.592  0 361 PHE AAA CE2   1 ? 1 
ATOM   2577  C CZ    . PHE A 1 361 ? -8.972  2.093   13.675  1.000 44.106  0 361 PHE AAA CZ    1 ? 1 
ATOM   2578  N N     . ALA A 1 362 ? -7.337  -4.954  11.670  1.000 45.136  0 362 ALA AAA N     1 ? 1 
ATOM   2579  C CA    . ALA A 1 362 ? -6.834  -6.121  10.897  1.000 44.999  0 362 ALA AAA CA    1 ? 1 
ATOM   2580  C C     . ALA A 1 362 ? -7.276  -7.451  11.522  1.000 44.796  0 362 ALA AAA C     1 ? 1 
ATOM   2581  O O     . ALA A 1 362 ? -6.644  -8.459  11.272  1.000 40.944  0 362 ALA AAA O     1 ? 1 
ATOM   2582  C CB    . ALA A 1 362 ? -5.339  -6.044  10.778  1.000 47.095  0 362 ALA AAA CB    1 ? 1 
ATOM   2583  N N     . GLY A 1 363 ? -8.365  -7.456  12.286  1.000 49.171  0 363 GLY AAA N     1 ? 1 
ATOM   2584  C CA    . GLY A 1 363 ? -9.005  -8.681  12.793  1.000 50.661  0 363 GLY AAA CA    1 ? 1 
ATOM   2585  C C     . GLY A 1 363 ? -8.091  -9.529  13.662  1.000 54.965  0 363 GLY AAA C     1 ? 1 
ATOM   2586  O O     . GLY A 1 363 ? -8.401  -10.720 13.807  1.000 55.823  0 363 GLY AAA O     1 ? 1 
ATOM   2587  N N     . SER A 1 364 ? -7.029  -8.953  14.252  1.000 57.305  0 364 SER AAA N     1 ? 1 
ATOM   2588  C CA    . SER A 1 364 ? -6.104  -9.640  15.204  1.000 55.136  0 364 SER AAA CA    1 ? 1 
ATOM   2589  C C     . SER A 1 364 ? -6.794  -9.752  16.577  1.000 54.463  0 364 SER AAA C     1 ? 1 
ATOM   2590  O O     . SER A 1 364 ? -7.707  -8.938  16.860  1.000 50.916  0 364 SER AAA O     1 ? 1 
ATOM   2591  C CB    . SER A 1 364 ? -4.770  -8.904  15.288  1.000 55.685  0 364 SER AAA CB    1 ? 1 
ATOM   2592  O OG    . SER A 1 364 ? -4.000  -9.309  16.414  1.000 51.145  0 364 SER AAA OG    1 ? 1 
ATOM   2593  N N     . ASN A 1 365 ? -6.422  -10.746 17.386  1.000 55.662  0 365 ASN AAA N     1 ? 1 
ATOM   2594  C CA    . ASN A 1 365 ? -6.873  -10.814 18.803  1.000 58.240  0 365 ASN AAA CA    1 ? 1 
ATOM   2595  C C     . ASN A 1 365 ? -5.668  -11.076 19.719  1.000 55.297  0 365 ASN AAA C     1 ? 1 
ATOM   2596  O O     . ASN A 1 365 ? -5.864  -11.608 20.830  1.000 53.593  0 365 ASN AAA O     1 ? 1 
ATOM   2597  C CB    . ASN A 1 365 ? -8.024  -11.799 19.015  1.000 62.279  0 365 ASN AAA CB    1 ? 1 
ATOM   2598  C CG    . ASN A 1 365 ? -8.976  -11.279 20.077  1.000 66.921  0 365 ASN AAA CG    1 ? 1 
ATOM   2599  O OD1   . ASN A 1 365 ? -8.879  -11.676 21.236  1.000 65.998  0 365 ASN AAA OD1   1 ? 1 
ATOM   2600  N ND2   . ASN A 1 365 ? -9.844  -10.340 19.712  1.000 68.505  0 365 ASN AAA ND2   1 ? 1 
ATOM   2601  N N     . GLU A 1 366 ? -4.484  -10.627 19.294  1.000 55.439  0 366 GLU AAA N     1 ? 1 
ATOM   2602  C CA    . GLU A 1 366 ? -3.189  -10.867 19.984  1.000 53.647  0 366 GLU AAA CA    1 ? 1 
ATOM   2603  C C     . GLU A 1 366 ? -2.956  -9.743  20.991  1.000 46.883  0 366 GLU AAA C     1 ? 1 
ATOM   2604  O O     . GLU A 1 366 ? -3.084  -8.559  20.612  1.000 41.753  0 366 GLU AAA O     1 ? 1 
ATOM   2605  C CB    . GLU A 1 366 ? -2.043  -10.981 18.976  1.000 56.164  0 366 GLU AAA CB    1 ? 1 
ATOM   2606  C CG    . GLU A 1 366 ? -1.997  -12.322 18.277  1.000 59.825  0 366 GLU AAA CG    1 ? 1 
ATOM   2607  C CD    . GLU A 1 366 ? -0.604  -12.737 17.803  1.000 63.948  0 366 GLU AAA CD    1 ? 1 
ATOM   2608  O OE1   . GLU A 1 366 ? -0.390  -12.646 16.591  1.000 64.783  0 366 GLU AAA OE1   1 ? 1 
ATOM   2609  O OE2   . GLU A 1 366 ? 0.267   -13.153 18.644  1.000 64.701  0 366 GLU AAA OE2   1 ? 1 
ATOM   2610  N N     . PHE A 1 367 ? -2.660  -10.144 22.228  1.000 45.061  0 367 PHE AAA N     1 ? 1 
ATOM   2611  C CA    . PHE A 1 367 ? -2.165  -9.290  23.340  1.000 42.749  0 367 PHE AAA CA    1 ? 1 
ATOM   2612  C C     . PHE A 1 367 ? -0.729  -9.697  23.672  1.000 39.267  0 367 PHE AAA C     1 ? 1 
ATOM   2613  O O     . PHE A 1 367 ? -0.327  -10.785 23.344  1.000 37.649  0 367 PHE AAA O     1 ? 1 
ATOM   2614  C CB    . PHE A 1 367 ? -3.110  -9.371  24.541  1.000 42.642  0 367 PHE AAA CB    1 ? 1 
ATOM   2615  C CG    . PHE A 1 367 ? -4.486  -8.798  24.287  1.000 43.892  0 367 PHE AAA CG    1 ? 1 
ATOM   2616  C CD1   . PHE A 1 367 ? -5.467  -9.543  23.628  1.000 42.576  0 367 PHE AAA CD1   1 ? 1 
ATOM   2617  C CD2   . PHE A 1 367 ? -4.804  -7.502  24.682  1.000 45.048  0 367 PHE AAA CD2   1 ? 1 
ATOM   2618  C CE1   . PHE A 1 367 ? -6.728  -9.012  23.393  1.000 41.637  0 367 PHE AAA CE1   1 ? 1 
ATOM   2619  C CE2   . PHE A 1 367 ? -6.081  -6.981  24.441  1.000 45.399  0 367 PHE AAA CE2   1 ? 1 
ATOM   2620  C CZ    . PHE A 1 367 ? -7.032  -7.730  23.781  1.000 41.230  0 367 PHE AAA CZ    1 ? 1 
ATOM   2621  N N     . ILE A 1 368 ? 0.039   -8.793  24.282  1.000 41.506  0 368 ILE AAA N     1 ? 1 
ATOM   2622  C CA    . ILE A 1 368 ? 1.368   -9.095  24.907  1.000 38.721  0 368 ILE AAA CA    1 ? 1 
ATOM   2623  C C     . ILE A 1 368 ? 1.179   -10.155 26.009  1.000 37.304  0 368 ILE AAA C     1 ? 1 
ATOM   2624  O O     . ILE A 1 368 ? 0.125   -10.137 26.720  1.000 32.060  0 368 ILE AAA O     1 ? 1 
ATOM   2625  C CB    . ILE A 1 368 ? 2.018   -7.825  25.474  1.000 37.713  0 368 ILE AAA CB    1 ? 1 
ATOM   2626  C CG1   . ILE A 1 368 ? 2.401   -6.831  24.377  1.000 37.188  0 368 ILE AAA CG1   1 ? 1 
ATOM   2627  C CG2   . ILE A 1 368 ? 3.213   -8.179  26.343  1.000 38.428  0 368 ILE AAA CG2   1 ? 1 
ATOM   2628  C CD1   . ILE A 1 368 ? 2.707   -5.420  24.882  1.000 35.660  0 368 ILE AAA CD1   1 ? 1 
ATOM   2629  N N     . ASP A 1 369 ? 2.176   -11.039 26.126  1.000 37.967  0 369 ASP AAA N     1 ? 1 
ATOM   2630  C CA    . ASP A 1 369 ? 2.360   -11.966 27.270  1.000 38.791  0 369 ASP AAA CA    1 ? 1 
ATOM   2631  C C     . ASP A 1 369 ? 3.224   -11.237 28.301  1.000 37.523  0 369 ASP AAA C     1 ? 1 
ATOM   2632  O O     . ASP A 1 369 ? 4.469   -11.170 28.113  1.000 37.348  0 369 ASP AAA O     1 ? 1 
ATOM   2633  C CB    . ASP A 1 369 ? 2.928   -13.309 26.775  1.000 40.560  0 369 ASP AAA CB    1 ? 1 
ATOM   2634  C CG    . ASP A 1 369 ? 3.041   -14.388 27.844  1.000 42.770  0 369 ASP AAA CG    1 ? 1 
ATOM   2635  O OD1   . ASP A 1 369 ? 2.845   -14.060 29.042  1.000 48.602  0 369 ASP AAA OD1   1 ? 1 
ATOM   2636  O OD2   . ASP A 1 369 ? 3.311   -15.546 27.489  1.000 40.870  0 369 ASP AAA OD2   1 ? 1 
ATOM   2637  N N     . TYR A 1 370 ? 2.610   -10.688 29.344  1.000 37.456  0 370 TYR AAA N     1 ? 1 
ATOM   2638  C CA    . TYR A 1 370 ? 3.300   -9.812  30.325  1.000 37.478  0 370 TYR AAA CA    1 ? 1 
ATOM   2639  C C     . TYR A 1 370 ? 4.185   -10.631 31.263  1.000 38.482  0 370 TYR AAA C     1 ? 1 
ATOM   2640  O O     . TYR A 1 370 ? 4.919   -10.014 32.056  1.000 37.985  0 370 TYR AAA O     1 ? 1 
ATOM   2641  C CB    . TYR A 1 370 ? 2.325   -8.909  31.086  1.000 35.433  0 370 TYR AAA CB    1 ? 1 
ATOM   2642  C CG    . TYR A 1 370 ? 1.817   -7.773  30.237  1.000 36.626  0 370 TYR AAA CG    1 ? 1 
ATOM   2643  C CD1   . TYR A 1 370 ? 2.628   -6.679  29.948  1.000 34.903  0 370 TYR AAA CD1   1 ? 1 
ATOM   2644  C CD2   . TYR A 1 370 ? 0.532   -7.799  29.687  1.000 35.355  0 370 TYR AAA CD2   1 ? 1 
ATOM   2645  C CE1   . TYR A 1 370 ? 2.183   -5.638  29.144  1.000 35.967  0 370 TYR AAA CE1   1 ? 1 
ATOM   2646  C CE2   . TYR A 1 370 ? 0.073   -6.751  28.908  1.000 35.643  0 370 TYR AAA CE2   1 ? 1 
ATOM   2647  C CZ    . TYR A 1 370 ? 0.904   -5.682  28.611  1.000 36.859  0 370 TYR AAA CZ    1 ? 1 
ATOM   2648  O OH    . TYR A 1 370 ? 0.467   -4.659  27.824  1.000 38.483  0 370 TYR AAA OH    1 ? 1 
ATOM   2649  N N     . ASP A 1 371 ? 4.158   -11.959 31.140  1.000 41.346  0 371 ASP AAA N     1 ? 1 
ATOM   2650  C CA    . ASP A 1 371 ? 5.027   -12.871 31.938  1.000 42.143  0 371 ASP AAA CA    1 ? 1 
ATOM   2651  C C     . ASP A 1 371 ? 6.475   -12.830 31.413  1.000 38.143  0 371 ASP AAA C     1 ? 1 
ATOM   2652  O O     . ASP A 1 371 ? 7.351   -13.243 32.151  1.000 38.261  0 371 ASP AAA O     1 ? 1 
ATOM   2653  C CB    . ASP A 1 371 ? 4.498   -14.309 31.916  1.000 44.840  0 371 ASP AAA CB    1 ? 1 
ATOM   2654  C CG    . ASP A 1 371 ? 3.148   -14.516 32.591  1.000 48.027  0 371 ASP AAA CG    1 ? 1 
ATOM   2655  O OD1   . ASP A 1 371 ? 2.831   -13.772 33.526  1.000 49.144  0 371 ASP AAA OD1   1 ? 1 
ATOM   2656  O OD2   . ASP A 1 371 ? 2.414   -15.423 32.143  1.000 50.823  0 371 ASP AAA OD2   1 ? 1 
ATOM   2657  N N     . PHE A 1 372 ? 6.716   -12.396 30.178  1.000 36.269  0 372 PHE AAA N     1 ? 1 
ATOM   2658  C CA    . PHE A 1 372 ? 8.036   -12.494 29.493  1.000 35.376  0 372 PHE AAA CA    1 ? 1 
ATOM   2659  C C     . PHE A 1 372 ? 8.391   -11.143 28.872  1.000 34.947  0 372 PHE AAA C     1 ? 1 
ATOM   2660  O O     . PHE A 1 372 ? 8.463   -11.004 27.635  1.000 35.403  0 372 PHE AAA O     1 ? 1 
ATOM   2661  C CB    . PHE A 1 372 ? 8.013   -13.636 28.477  1.000 36.815  0 372 PHE AAA CB    1 ? 1 
ATOM   2662  C CG    . PHE A 1 372 ? 7.816   -14.991 29.108  1.000 37.551  0 372 PHE AAA CG    1 ? 1 
ATOM   2663  C CD1   . PHE A 1 372 ? 8.838   -15.577 29.840  1.000 37.554  0 372 PHE AAA CD1   1 ? 1 
ATOM   2664  C CD2   . PHE A 1 372 ? 6.590   -15.649 29.033  1.000 37.845  0 372 PHE AAA CD2   1 ? 1 
ATOM   2665  C CE1   . PHE A 1 372 ? 8.643   -16.798 30.469  1.000 38.019  0 372 PHE AAA CE1   1 ? 1 
ATOM   2666  C CE2   . PHE A 1 372 ? 6.398   -16.869 29.667  1.000 38.563  0 372 PHE AAA CE2   1 ? 1 
ATOM   2667  C CZ    . PHE A 1 372 ? 7.433   -17.442 30.378  1.000 39.159  0 372 PHE AAA CZ    1 ? 1 
ATOM   2668  N N     . VAL A 1 373 ? 8.573   -10.144 29.733  1.000 35.497  0 373 VAL AAA N     1 ? 1 
ATOM   2669  C CA    . VAL A 1 373 ? 9.016   -8.771  29.342  1.000 35.331  0 373 VAL AAA CA    1 ? 1 
ATOM   2670  C C     . VAL A 1 373 ? 10.429  -8.588  29.871  1.000 33.259  0 373 VAL AAA C     1 ? 1 
ATOM   2671  O O     . VAL A 1 373 ? 10.598  -8.368  31.050  1.000 36.709  0 373 VAL AAA O     1 ? 1 
ATOM   2672  C CB    . VAL A 1 373 ? 8.063   -7.699  29.887  1.000 35.254  0 373 VAL AAA CB    1 ? 1 
ATOM   2673  C CG1   . VAL A 1 373 ? 8.595   -6.292  29.626  1.000 35.869  0 373 VAL AAA CG1   1 ? 1 
ATOM   2674  C CG2   . VAL A 1 373 ? 6.639   -7.895  29.322  1.000 35.832  0 373 VAL AAA CG2   1 ? 1 
ATOM   2675  N N     . PRO A 1 374 ? 11.481  -8.691  29.034  1.000 31.725  0 374 PRO AAA N     1 ? 1 
ATOM   2676  C CA    . PRO A 1 374 ? 12.852  -8.501  29.504  1.000 30.288  0 374 PRO AAA CA    1 ? 1 
ATOM   2677  C C     . PRO A 1 374 ? 13.135  -7.010  29.658  1.000 31.224  0 374 PRO AAA C     1 ? 1 
ATOM   2678  O O     . PRO A 1 374 ? 12.446  -6.167  29.033  1.000 32.947  0 374 PRO AAA O     1 ? 1 
ATOM   2679  C CB    . PRO A 1 374 ? 13.708  -9.085  28.382  1.000 29.265  0 374 PRO AAA CB    1 ? 1 
ATOM   2680  C CG    . PRO A 1 374 ? 12.873  -8.821  27.124  1.000 29.872  0 374 PRO AAA CG    1 ? 1 
ATOM   2681  C CD    . PRO A 1 374 ? 11.436  -8.987  27.590  1.000 30.556  0 374 PRO AAA CD    1 ? 1 
ATOM   2682  N N     . THR A 1 375 ? 14.138  -6.690  30.464  1.000 31.948  0 375 THR AAA N     1 ? 1 
ATOM   2683  C CA    . THR A 1 375 ? 14.553  -5.294  30.717  1.000 32.100  0 375 THR AAA CA    1 ? 1 
ATOM   2684  C C     . THR A 1 375 ? 16.047  -5.336  30.951  1.000 28.711  0 375 THR AAA C     1 ? 1 
ATOM   2685  O O     . THR A 1 375 ? 16.535  -6.403  31.352  1.000 28.271  0 375 THR AAA O     1 ? 1 
ATOM   2686  C CB    . THR A 1 375 ? 13.751  -4.700  31.879  1.000 38.474  0 375 THR AAA CB    1 ? 1 
ATOM   2687  O OG1   . THR A 1 375 ? 14.288  -3.404  32.170  1.000 44.378  0 375 THR AAA OG1   1 ? 1 
ATOM   2688  C CG2   . THR A 1 375 ? 13.759  -5.569  33.118  1.000 41.168  0 375 THR AAA CG2   1 ? 1 
ATOM   2689  N N     . THR A 1 376 ? 16.743  -4.267  30.607  1.000 26.055  0 376 THR AAA N     1 ? 1 
ATOM   2690  C CA    . THR A 1 376 ? 18.136  -4.041  31.011  1.000 25.041  0 376 THR AAA CA    1 ? 1 
ATOM   2691  C C     . THR A 1 376 ? 18.261  -2.672  31.679  1.000 23.528  0 376 THR AAA C     1 ? 1 
ATOM   2692  O O     . THR A 1 376 ? 17.736  -1.679  31.135  1.000 23.741  0 376 THR AAA O     1 ? 1 
ATOM   2693  C CB    . THR A 1 376 ? 19.108  -4.158  29.840  1.000 25.498  0 376 THR AAA CB    1 ? 1 
ATOM   2694  O OG1   . THR A 1 376 ? 19.166  -5.529  29.441  1.000 29.029  0 376 THR AAA OG1   1 ? 1 
ATOM   2695  C CG2   . THR A 1 376 ? 20.498  -3.742  30.224  1.000 25.024  0 376 THR AAA CG2   1 ? 1 
ATOM   2696  N N     . VAL A 1 377 ? 19.003  -2.644  32.778  1.000 21.280  0 377 VAL AAA N     1 ? 1 
ATOM   2697  C CA    . VAL A 1 377 ? 19.404  -1.422  33.502  1.000 20.395  0 377 VAL AAA CA    1 ? 1 
ATOM   2698  C C     . VAL A 1 377 ? 20.822  -1.106  33.038  1.000 20.736  0 377 VAL AAA C     1 ? 1 
ATOM   2699  O O     . VAL A 1 377 ? 21.683  -2.026  33.125  1.000 20.734  0 377 VAL AAA O     1 ? 1 
ATOM   2700  C CB    . VAL A 1 377 ? 19.321  -1.685  35.015  1.000 20.101  0 377 VAL AAA CB    1 ? 1 
ATOM   2701  C CG1   . VAL A 1 377 ? 19.883  -0.525  35.824  1.000 20.200  0 377 VAL AAA CG1   1 ? 1 
ATOM   2702  C CG2   . VAL A 1 377 ? 17.896  -2.004  35.448  1.000 19.674  0 377 VAL AAA CG2   1 ? 1 
ATOM   2703  N N     . PHE A 1 378 ? 21.061  0.096   32.509  1.000 20.517  0 378 PHE AAA N     1 ? 1 
ATOM   2704  C CA    . PHE A 1 378 ? 22.380  0.449   31.918  1.000 21.523  0 378 PHE AAA CA    1 ? 1 
ATOM   2705  C C     . PHE A 1 378 ? 23.255  1.132   32.957  1.000 21.607  0 378 PHE AAA C     1 ? 1 
ATOM   2706  O O     . PHE A 1 378 ? 23.723  2.238   32.712  1.000 22.127  0 378 PHE AAA O     1 ? 1 
ATOM   2707  C CB    . PHE A 1 378 ? 22.204  1.256   30.621  1.000 22.009  0 378 PHE AAA CB    1 ? 1 
ATOM   2708  C CG    . PHE A 1 378 ? 21.571  0.434   29.535  1.000 21.346  0 378 PHE AAA CG    1 ? 1 
ATOM   2709  C CD1   . PHE A 1 378 ? 22.344  -0.395  28.752  1.000 21.245  0 378 PHE AAA CD1   1 ? 1 
ATOM   2710  C CD2   . PHE A 1 378 ? 20.195  0.426   29.373  1.000 21.755  0 378 PHE AAA CD2   1 ? 1 
ATOM   2711  C CE1   . PHE A 1 378 ? 21.762  -1.188  27.773  1.000 22.075  0 378 PHE AAA CE1   1 ? 1 
ATOM   2712  C CE2   . PHE A 1 378 ? 19.611  -0.358  28.385  1.000 22.082  0 378 PHE AAA CE2   1 ? 1 
ATOM   2713  C CZ    . PHE A 1 378 ? 20.396  -1.171  27.588  1.000 22.074  0 378 PHE AAA CZ    1 ? 1 
ATOM   2714  N N     . THR A 1 379 ? 23.521  0.422   34.042  1.000 22.048  0 379 THR AAA N     1 ? 1 
ATOM   2715  C CA    . THR A 1 379 ? 24.444  0.850   35.107  1.000 22.742  0 379 THR AAA CA    1 ? 1 
ATOM   2716  C C     . THR A 1 379 ? 25.853  0.501   34.650  1.000 23.313  0 379 THR AAA C     1 ? 1 
ATOM   2717  O O     . THR A 1 379 ? 26.026  -0.233  33.678  1.000 22.690  0 379 THR AAA O     1 ? 1 
ATOM   2718  C CB    . THR A 1 379 ? 24.004  0.213   36.432  1.000 23.658  0 379 THR AAA CB    1 ? 1 
ATOM   2719  O OG1   . THR A 1 379 ? 23.467  -1.093  36.175  1.000 22.979  0 379 THR AAA OG1   1 ? 1 
ATOM   2720  C CG2   . THR A 1 379 ? 22.961  1.057   37.128  1.000 23.574  0 379 THR AAA CG2   1 ? 1 
ATOM   2721  N N     . PRO A 1 380 ? 26.905  1.052   35.306  1.000 23.506  0 380 PRO AAA N     1 ? 1 
ATOM   2722  C CA    . PRO A 1 380 ? 28.287  0.897   34.828  1.000 23.309  0 380 PRO AAA CA    1 ? 1 
ATOM   2723  C C     . PRO A 1 380 ? 28.654  -0.550  34.507  1.000 22.986  0 380 PRO AAA C     1 ? 1 
ATOM   2724  O O     . PRO A 1 380 ? 29.366  -0.751  33.585  1.000 26.438  0 380 PRO AAA O     1 ? 1 
ATOM   2725  C CB    . PRO A 1 380 ? 29.110  1.493   35.978  1.000 23.276  0 380 PRO AAA CB    1 ? 1 
ATOM   2726  C CG    . PRO A 1 380 ? 28.181  2.562   36.532  1.000 23.502  0 380 PRO AAA CG    1 ? 1 
ATOM   2727  C CD    . PRO A 1 380 ? 26.813  1.934   36.476  1.000 23.149  0 380 PRO AAA CD    1 ? 1 
ATOM   2728  N N     . ILE A 1 381 ? 28.181  -1.508  35.281  1.000 22.975  0 381 ILE AAA N     1 ? 1 
ATOM   2729  C CA    . ILE A 1 381 ? 27.927  -2.909  34.837  1.000 22.157  0 381 ILE AAA CA    1 ? 1 
ATOM   2730  C C     . ILE A 1 381 ? 26.408  -3.003  34.719  1.000 22.622  0 381 ILE AAA C     1 ? 1 
ATOM   2731  O O     . ILE A 1 381 ? 25.688  -2.507  35.629  1.000 21.030  0 381 ILE AAA O     1 ? 1 
ATOM   2732  C CB    . ILE A 1 381 ? 28.478  -3.967  35.809  1.000 22.616  0 381 ILE AAA CB    1 ? 1 
ATOM   2733  C CG1   . ILE A 1 381 ? 28.014  -3.752  37.244  1.000 22.549  0 381 ILE AAA CG1   1 ? 1 
ATOM   2734  C CG2   . ILE A 1 381 ? 30.001  -4.057  35.765  1.000 22.510  0 381 ILE AAA CG2   1 ? 1 
ATOM   2735  C CD1   . ILE A 1 381 ? 28.532  -4.791  38.194  1.000 22.692  0 381 ILE AAA CD1   1 ? 1 
ATOM   2736  N N     . GLU A 1 382 ? 25.946  -3.564  33.598  1.000 22.758  0 382 GLU AAA N     1 ? 1 
ATOM   2737  C CA    . GLU A 1 382 ? 24.531  -3.566  33.188  1.000 22.351  0 382 GLU AAA CA    1 ? 1 
ATOM   2738  C C     . GLU A 1 382 ? 23.842  -4.757  33.834  1.000 21.803  0 382 GLU AAA C     1 ? 1 
ATOM   2739  O O     . GLU A 1 382 ? 24.542  -5.691  34.263  1.000 21.721  0 382 GLU AAA O     1 ? 1 
ATOM   2740  C CB    . GLU A 1 382 ? 24.436  -3.649  31.675  1.000 23.509  0 382 GLU AAA CB    1 ? 1 
ATOM   2741  C CG    . GLU A 1 382 ? 25.336  -2.644  30.984  1.000 25.363  0 382 GLU AAA CG    1 ? 1 
ATOM   2742  C CD    . GLU A 1 382 ? 25.216  -2.606  29.475  1.000 27.198  0 382 GLU AAA CD    1 ? 1 
ATOM   2743  O OE1   . GLU A 1 382 ? 24.649  -3.601  28.873  1.000 26.233  0 382 GLU AAA OE1   1 ? 1 
ATOM   2744  O OE2   . GLU A 1 382 ? 25.696  -1.568  28.895  1.000 31.159  0 382 GLU AAA OE2   1 ? 1 
ATOM   2745  N N     . TYR A 1 383 ? 22.515  -4.723  33.888  1.000 20.470  0 383 TYR AAA N     1 ? 1 
ATOM   2746  C CA    . TYR A 1 383 ? 21.738  -5.822  34.497  1.000 20.173  0 383 TYR AAA CA    1 ? 1 
ATOM   2747  C C     . TYR A 1 383 ? 20.560  -6.103  33.588  1.000 19.193  0 383 TYR AAA C     1 ? 1 
ATOM   2748  O O     . TYR A 1 383 ? 19.654  -5.245  33.438  1.000 18.221  0 383 TYR AAA O     1 ? 1 
ATOM   2749  C CB    . TYR A 1 383 ? 21.375  -5.507  35.951  1.000 20.784  0 383 TYR AAA CB    1 ? 1 
ATOM   2750  C CG    . TYR A 1 383 ? 20.376  -6.464  36.531  1.000 21.819  0 383 TYR AAA CG    1 ? 1 
ATOM   2751  C CD1   . TYR A 1 383 ? 20.484  -7.822  36.315  1.000 22.642  0 383 TYR AAA CD1   1 ? 1 
ATOM   2752  C CD2   . TYR A 1 383 ? 19.361  -6.026  37.342  1.000 22.683  0 383 TYR AAA CD2   1 ? 1 
ATOM   2753  C CE1   . TYR A 1 383 ? 19.556  -8.706  36.814  1.000 23.644  0 383 TYR AAA CE1   1 ? 1 
ATOM   2754  C CE2   . TYR A 1 383 ? 18.385  -6.895  37.823  1.000 23.513  0 383 TYR AAA CE2   1 ? 1 
ATOM   2755  C CZ    . TYR A 1 383 ? 18.466  -8.236  37.542  1.000 23.234  0 383 TYR AAA CZ    1 ? 1 
ATOM   2756  O OH    . TYR A 1 383 ? 17.550  -9.106  38.041  1.000 21.756  0 383 TYR AAA OH    1 ? 1 
ATOM   2757  N N     . GLY A 1 384 ? 20.629  -7.266  32.934  1.000 18.686  0 384 GLY AAA N     1 ? 1 
ATOM   2758  C CA    . GLY A 1 384 ? 19.513  -7.748  32.105  1.000 18.840  0 384 GLY AAA CA    1 ? 1 
ATOM   2759  C C     . GLY A 1 384 ? 18.827  -8.914  32.771  1.000 19.023  0 384 GLY AAA C     1 ? 1 
ATOM   2760  O O     . GLY A 1 384 ? 19.555  -9.742  33.402  1.000 19.385  0 384 GLY AAA O     1 ? 1 
ATOM   2761  N N     . HIS A 1 385 ? 17.507  -8.976  32.693  1.000 19.407  0 385 HIS AAA N     1 ? 1 
ATOM   2762  C CA    . HIS A 1 385 ? 16.745  -10.124 33.248  1.000 20.298  0 385 HIS AAA CA    1 ? 1 
ATOM   2763  C C     . HIS A 1 385 ? 15.428  -10.294 32.501  1.000 21.314  0 385 HIS AAA C     1 ? 1 
ATOM   2764  O O     . HIS A 1 385 ? 14.967  -9.320  31.878  1.000 22.306  0 385 HIS AAA O     1 ? 1 
ATOM   2765  C CB    . HIS A 1 385 ? 16.514  -9.913  34.766  1.000 20.383  0 385 HIS AAA CB    1 ? 1 
ATOM   2766  C CG    . HIS A 1 385 ? 15.238  -9.233  35.129  1.000 20.724  0 385 HIS AAA CG    1 ? 1 
ATOM   2767  N ND1   . HIS A 1 385 ? 15.104  -7.850  35.294  1.000 21.100  0 385 HIS AAA ND1   1 ? 1 
ATOM   2768  C CD2   . HIS A 1 385 ? 14.042  -9.785  35.440  1.000 20.921  0 385 HIS AAA CD2   1 ? 1 
ATOM   2769  C CE1   . HIS A 1 385 ? 13.878  -7.583  35.688  1.000 20.847  0 385 HIS AAA CE1   1 ? 1 
ATOM   2770  N NE2   . HIS A 1 385 ? 13.211  -8.774  35.827  1.000 21.346  0 385 HIS AAA NE2   1 ? 1 
ATOM   2771  N N     . VAL A 1 386 ? 14.835  -11.480 32.618  1.000 21.881  0 386 VAL AAA N     1 ? 1 
ATOM   2772  C CA    . VAL A 1 386 ? 13.426  -11.766 32.271  1.000 22.240  0 386 VAL AAA CA    1 ? 1 
ATOM   2773  C C     . VAL A 1 386 ? 12.911  -12.783 33.280  1.000 23.611  0 386 VAL AAA C     1 ? 1 
ATOM   2774  O O     . VAL A 1 386 ? 13.738  -13.632 33.807  1.000 22.769  0 386 VAL AAA O     1 ? 1 
ATOM   2775  C CB    . VAL A 1 386 ? 13.295  -12.315 30.840  1.000 22.470  0 386 VAL AAA CB    1 ? 1 
ATOM   2776  C CG1   . VAL A 1 386 ? 13.904  -13.696 30.682  1.000 22.460  0 386 VAL AAA CG1   1 ? 1 
ATOM   2777  C CG2   . VAL A 1 386 ? 11.847  -12.315 30.395  1.000 22.164  0 386 VAL AAA CG2   1 ? 1 
ATOM   2778  N N     . GLY A 1 387 ? 11.601  -12.712 33.533  1.000 24.466  0 387 GLY AAA N     1 ? 1 
ATOM   2779  C CA    . GLY A 1 387 ? 10.926  -13.607 34.482  1.000 25.020  0 387 GLY AAA CA    1 ? 1 
ATOM   2780  C C     . GLY A 1 387 ? 11.185  -13.174 35.897  1.000 26.334  0 387 GLY AAA C     1 ? 1 
ATOM   2781  O O     . GLY A 1 387 ? 11.365  -11.975 36.133  1.000 28.235  0 387 GLY AAA O     1 ? 1 
ATOM   2782  N N     . LEU A 1 388 ? 11.241  -14.143 36.806  1.000 28.074  0 388 LEU AAA N     1 ? 1 
ATOM   2783  C CA    . LEU A 1 388 ? 11.135  -13.920 38.266  1.000 28.296  0 388 LEU AAA CA    1 ? 1 
ATOM   2784  C C     . LEU A 1 388 ? 12.522  -13.773 38.874  1.000 27.733  0 388 LEU AAA C     1 ? 1 
ATOM   2785  O O     . LEU A 1 388 ? 13.445  -14.495 38.489  1.000 28.046  0 388 LEU AAA O     1 ? 1 
ATOM   2786  C CB    . LEU A 1 388 ? 10.361  -15.094 38.885  1.000 30.063  0 388 LEU AAA CB    1 ? 1 
ATOM   2787  C CG    . LEU A 1 388 ? 8.990   -15.385 38.230  1.000 31.367  0 388 LEU AAA CG    1 ? 1 
ATOM   2788  C CD1   . LEU A 1 388 ? 8.327   -16.623 38.840  1.000 31.962  0 388 LEU AAA CD1   1 ? 1 
ATOM   2789  C CD2   . LEU A 1 388 ? 8.032   -14.185 38.315  1.000 30.292  0 388 LEU AAA CD2   1 ? 1 
ATOM   2790  N N     . SER A 1 389 ? 12.640  -12.847 39.811  1.000 28.402  0 389 SER AAA N     1 ? 1 
ATOM   2791  C CA    . SER A 1 389 ? 13.724  -12.784 40.819  1.000 28.768  0 389 SER AAA CA    1 ? 1 
ATOM   2792  C C     . SER A 1 389 ? 13.705  -14.073 41.657  1.000 29.810  0 389 SER AAA C     1 ? 1 
ATOM   2793  O O     . SER A 1 389 ? 12.691  -14.810 41.613  1.000 31.018  0 389 SER AAA O     1 ? 1 
ATOM   2794  C CB    . SER A 1 389 ? 13.517  -11.591 41.697  1.000 28.742  0 389 SER AAA CB    1 ? 1 
ATOM   2795  O OG    . SER A 1 389 ? 12.242  -11.654 42.310  1.000 28.105  0 389 SER AAA OG    1 ? 1 
ATOM   2796  N N     . SER A 1 390 ? 14.796  -14.356 42.360  1.000 29.765  0 390 SER AAA N     1 ? 1 
ATOM   2797  C CA    . SER A 1 390 ? 14.864  -15.383 43.426  1.000 31.142  0 390 SER AAA CA    1 ? 1 
ATOM   2798  C C     . SER A 1 390 ? 13.682  -15.181 44.389  1.000 31.402  0 390 SER AAA C     1 ? 1 
ATOM   2799  O O     . SER A 1 390 ? 12.972  -16.157 44.655  1.000 32.348  0 390 SER AAA O     1 ? 1 
ATOM   2800  C CB    . SER A 1 390 ? 16.209  -15.367 44.124  1.000 30.452  0 390 SER AAA CB    1 ? 1 
ATOM   2801  O OG    . SER A 1 390 ? 17.276  -15.598 43.212  1.000 28.924  0 390 SER AAA OG    1 ? 1 
ATOM   2802  N N     . GLU A 1 391 ? 13.413  -13.942 44.793  1.000 30.192  0 391 GLU AAA N     1 ? 1 
ATOM   2803  C CA    . GLU A 1 391 ? 12.364  -13.596 45.781  1.000 30.600  0 391 GLU AAA CA    1 ? 1 
ATOM   2804  C C     . GLU A 1 391 ? 10.980  -13.983 45.217  1.000 31.624  0 391 GLU AAA C     1 ? 1 
ATOM   2805  O O     . GLU A 1 391 ? 10.219  -14.702 45.924  1.000 31.632  0 391 GLU AAA O     1 ? 1 
ATOM   2806  C CB    . GLU A 1 391 ? 12.454  -12.127 46.200  1.000 29.486  0 391 GLU AAA CB    1 ? 1 
ATOM   2807  C CG    . GLU A 1 391 ? 13.684  -11.842 47.072  1.000 30.384  0 391 GLU AAA CG    1 ? 1 
ATOM   2808  C CD    . GLU A 1 391 ? 15.014  -11.748 46.300  1.000 30.524  0 391 GLU AAA CD    1 ? 1 
ATOM   2809  O OE1   . GLU A 1 391 ? 15.022  -11.175 45.173  1.000 28.234  0 391 GLU AAA OE1   1 ? 1 
ATOM   2810  O OE2   . GLU A 1 391 ? 16.039  -12.288 46.805  1.000 30.272  0 391 GLU AAA OE2   1 ? 1 
ATOM   2811  N N     . ALA A 1 392 ? 10.628  -13.532 44.012  1.000 33.003  0 392 ALA AAA N     1 ? 1 
ATOM   2812  C CA    . ALA A 1 392 ? 9.305   -13.833 43.406  1.000 34.778  0 392 ALA AAA CA    1 ? 1 
ATOM   2813  C C     . ALA A 1 392 ? 9.201   -15.342 43.124  1.000 38.869  0 392 ALA AAA C     1 ? 1 
ATOM   2814  O O     . ALA A 1 392 ? 8.065   -15.874 43.161  1.000 46.697  0 392 ALA AAA O     1 ? 1 
ATOM   2815  C CB    . ALA A 1 392 ? 9.057   -13.009 42.179  1.000 32.551  0 392 ALA AAA CB    1 ? 1 
ATOM   2816  N N     . ALA A 1 393 ? 10.325  -16.026 42.866  1.000 38.790  0 393 ALA AAA N     1 ? 1 
ATOM   2817  C CA    . ALA A 1 393 ? 10.356  -17.478 42.573  1.000 38.622  0 393 ALA AAA CA    1 ? 1 
ATOM   2818  C C     . ALA A 1 393 ? 10.077  -18.269 43.858  1.000 39.208  0 393 ALA AAA C     1 ? 1 
ATOM   2819  O O     . ALA A 1 393 ? 9.208   -19.161 43.825  1.000 38.647  0 393 ALA AAA O     1 ? 1 
ATOM   2820  C CB    . ALA A 1 393 ? 11.676  -17.867 41.968  1.000 39.404  0 393 ALA AAA CB    1 ? 1 
ATOM   2821  N N     . ILE A 1 394 ? 10.780  -17.926 44.939  1.000 38.198  0 394 ILE AAA N     1 ? 1 
ATOM   2822  C CA    . ILE A 1 394 ? 10.601  -18.521 46.290  1.000 39.602  0 394 ILE AAA CA    1 ? 1 
ATOM   2823  C C     . ILE A 1 394 ? 9.152   -18.288 46.759  1.000 40.273  0 394 ILE AAA C     1 ? 1 
ATOM   2824  O O     . ILE A 1 394 ? 8.505   -19.284 47.118  1.000 41.716  0 394 ILE AAA O     1 ? 1 
ATOM   2825  C CB    . ILE A 1 394 ? 11.698  -18.005 47.257  1.000 39.246  0 394 ILE AAA CB    1 ? 1 
ATOM   2826  C CG1   . ILE A 1 394 ? 13.045  -18.655 46.916  1.000 38.106  0 394 ILE AAA CG1   1 ? 1 
ATOM   2827  C CG2   . ILE A 1 394 ? 11.312  -18.245 48.711  1.000 38.579  0 394 ILE AAA CG2   1 ? 1 
ATOM   2828  C CD1   . ILE A 1 394 ? 14.246  -18.140 47.689  1.000 37.415  0 394 ILE AAA CD1   1 ? 1 
ATOM   2829  N N     . ALA A 1 395 ? 8.624   -17.061 46.664  1.000 42.600  0 395 ALA AAA N     1 ? 1 
ATOM   2830  C CA    . ALA A 1 395 ? 7.233   -16.693 47.051  1.000 43.824  0 395 ALA AAA CA    1 ? 1 
ATOM   2831  C C     . ALA A 1 395 ? 6.207   -17.556 46.297  1.000 46.111  0 395 ALA AAA C     1 ? 1 
ATOM   2832  O O     . ALA A 1 395 ? 5.256   -18.014 46.939  1.000 46.240  0 395 ALA AAA O     1 ? 1 
ATOM   2833  C CB    . ALA A 1 395 ? 6.972   -15.217 46.817  1.000 42.949  0 395 ALA AAA CB    1 ? 1 
ATOM   2834  N N     . LYS A 1 396 ? 6.387   -17.774 44.989  1.000 48.770  0 396 LYS AAA N     1 ? 1 
ATOM   2835  C CA    . LYS A 1 396 ? 5.355   -18.401 44.113  1.000 47.044  0 396 LYS AAA CA    1 ? 1 
ATOM   2836  C C     . LYS A 1 396 ? 5.383   -19.925 44.226  1.000 45.052  0 396 LYS AAA C     1 ? 1 
ATOM   2837  O O     . LYS A 1 396 ? 4.288   -20.511 44.229  1.000 44.687  0 396 LYS AAA O     1 ? 1 
ATOM   2838  C CB    . LYS A 1 396 ? 5.539   -17.985 42.651  1.000 50.014  0 396 LYS AAA CB    1 ? 1 
ATOM   2839  C CG    . LYS A 1 396 ? 4.489   -18.510 41.674  1.000 52.260  0 396 LYS AAA CG    1 ? 1 
ATOM   2840  C CD    . LYS A 1 396 ? 4.810   -18.166 40.237  1.000 53.867  0 396 LYS AAA CD    1 ? 1 
ATOM   2841  C CE    . LYS A 1 396 ? 3.969   -18.891 39.205  1.000 58.167  0 396 LYS AAA CE    1 ? 1 
ATOM   2842  N NZ    . LYS A 1 396 ? 2.522   -18.557 39.287  1.000 61.485  0 396 LYS AAA NZ    1 ? 1 
ATOM   2843  N N     . TYR A 1 397 ? 6.565   -20.556 44.275  1.000 43.338  0 397 TYR AAA N     1 ? 1 
ATOM   2844  C CA    . TYR A 1 397 ? 6.723   -22.041 44.171  1.000 44.119  0 397 TYR AAA CA    1 ? 1 
ATOM   2845  C C     . TYR A 1 397 ? 7.130   -22.666 45.514  1.000 44.169  0 397 TYR AAA C     1 ? 1 
ATOM   2846  O O     . TYR A 1 397 ? 6.991   -23.883 45.644  1.000 43.556  0 397 TYR AAA O     1 ? 1 
ATOM   2847  C CB    . TYR A 1 397 ? 7.719   -22.405 43.060  1.000 44.306  0 397 TYR AAA CB    1 ? 1 
ATOM   2848  C CG    . TYR A 1 397 ? 7.234   -22.076 41.672  1.000 43.072  0 397 TYR AAA CG    1 ? 1 
ATOM   2849  C CD1   . TYR A 1 397 ? 6.260   -22.849 41.063  1.000 43.416  0 397 TYR AAA CD1   1 ? 1 
ATOM   2850  C CD2   . TYR A 1 397 ? 7.716   -20.981 40.975  1.000 42.967  0 397 TYR AAA CD2   1 ? 1 
ATOM   2851  C CE1   . TYR A 1 397 ? 5.791   -22.553 39.793  1.000 43.474  0 397 TYR AAA CE1   1 ? 1 
ATOM   2852  C CE2   . TYR A 1 397 ? 7.244   -20.662 39.710  1.000 43.333  0 397 TYR AAA CE2   1 ? 1 
ATOM   2853  C CZ    . TYR A 1 397 ? 6.281   -21.456 39.110  1.000 43.669  0 397 TYR AAA CZ    1 ? 1 
ATOM   2854  O OH    . TYR A 1 397 ? 5.808   -21.158 37.859  1.000 44.173  0 397 TYR AAA OH    1 ? 1 
ATOM   2855  N N     . GLY A 1 398 ? 7.606   -21.856 46.464  1.000 45.843  0 398 GLY AAA N     1 ? 1 
ATOM   2856  C CA    . GLY A 1 398 ? 8.199   -22.302 47.739  1.000 47.405  0 398 GLY AAA CA    1 ? 1 
ATOM   2857  C C     . GLY A 1 398 ? 9.693   -22.568 47.613  1.000 48.751  0 398 GLY AAA C     1 ? 1 
ATOM   2858  O O     . GLY A 1 398 ? 10.114  -23.048 46.568  1.000 46.916  0 398 GLY AAA O     1 ? 1 
ATOM   2859  N N     . GLU A 1 399 ? 10.442  -22.304 48.687  1.000 51.349  0 399 GLU AAA N     1 ? 1 
ATOM   2860  C CA    . GLU A 1 399 ? 11.918  -22.421 48.806  1.000 55.175  0 399 GLU AAA CA    1 ? 1 
ATOM   2861  C C     . GLU A 1 399 ? 12.407  -23.788 48.301  1.000 56.804  0 399 GLU AAA C     1 ? 1 
ATOM   2862  O O     . GLU A 1 399 ? 13.503  -23.837 47.734  1.000 54.278  0 399 GLU AAA O     1 ? 1 
ATOM   2863  C CB    . GLU A 1 399 ? 12.305  -22.224 50.275  1.000 60.246  0 399 GLU AAA CB    1 ? 1 
ATOM   2864  C CG    . GLU A 1 399 ? 13.799  -22.288 50.545  1.000 62.463  0 399 GLU AAA CG    1 ? 1 
ATOM   2865  C CD    . GLU A 1 399 ? 14.549  -21.032 50.136  1.000 65.757  0 399 GLU AAA CD    1 ? 1 
ATOM   2866  O OE1   . GLU A 1 399 ? 14.089  -19.917 50.542  1.000 66.624  0 399 GLU AAA OE1   1 ? 1 
ATOM   2867  O OE2   . GLU A 1 399 ? 15.588  -21.159 49.424  1.000 63.634  0 399 GLU AAA OE2   1 ? 1 
ATOM   2868  N N     . ASP A 1 400 ? 11.646  -24.859 48.515  1.000 57.870  0 400 ASP AAA N     1 ? 1 
ATOM   2869  C CA    . ASP A 1 400 ? 12.118  -26.250 48.279  1.000 56.460  0 400 ASP AAA CA    1 ? 1 
ATOM   2870  C C     . ASP A 1 400 ? 11.911  -26.661 46.824  1.000 51.052  0 400 ASP AAA C     1 ? 1 
ATOM   2871  O O     . ASP A 1 400 ? 12.557  -27.638 46.397  1.000 52.106  0 400 ASP AAA O     1 ? 1 
ATOM   2872  C CB    . ASP A 1 400 ? 11.373  -27.272 49.141  1.000 60.981  0 400 ASP AAA CB    1 ? 1 
ATOM   2873  C CG    . ASP A 1 400 ? 11.702  -27.149 50.601  1.000 61.721  0 400 ASP AAA CG    1 ? 1 
ATOM   2874  O OD1   . ASP A 1 400 ? 12.820  -26.653 50.921  1.000 63.239  0 400 ASP AAA OD1   1 ? 1 
ATOM   2875  O OD2   . ASP A 1 400 ? 10.807  -27.480 51.389  1.000 62.499  0 400 ASP AAA OD2   1 ? 1 
ATOM   2876  N N     . ASP A 1 401 ? 11.037  -25.976 46.096  1.000 45.723  0 401 ASP AAA N     1 ? 1 
ATOM   2877  C CA    . ASP A 1 401 ? 10.780  -26.264 44.664  1.000 44.996  0 401 ASP AAA CA    1 ? 1 
ATOM   2878  C C     . ASP A 1 401 ? 11.674  -25.349 43.800  1.000 42.462  0 401 ASP AAA C     1 ? 1 
ATOM   2879  O O     . ASP A 1 401 ? 11.495  -25.374 42.572  1.000 41.967  0 401 ASP AAA O     1 ? 1 
ATOM   2880  C CB    . ASP A 1 401 ? 9.276   -26.164 44.369  1.000 43.708  0 401 ASP AAA CB    1 ? 1 
ATOM   2881  C CG    . ASP A 1 401 ? 8.801   -26.980 43.178  1.000 44.346  0 401 ASP AAA CG    1 ? 1 
ATOM   2882  O OD1   . ASP A 1 401 ? 9.526   -27.922 42.777  1.000 46.447  0 401 ASP AAA OD1   1 ? 1 
ATOM   2883  O OD2   . ASP A 1 401 ? 7.723   -26.664 42.649  1.000 41.980  0 401 ASP AAA OD2   1 ? 1 
ATOM   2884  N N     . ILE A 1 402 ? 12.615  -24.608 44.405  1.000 41.617  0 402 ILE AAA N     1 ? 1 
ATOM   2885  C CA    . ILE A 1 402 ? 13.492  -23.605 43.725  1.000 42.762  0 402 ILE AAA CA    1 ? 1 
ATOM   2886  C C     . ILE A 1 402 ? 14.967  -24.017 43.798  1.000 44.377  0 402 ILE AAA C     1 ? 1 
ATOM   2887  O O     . ILE A 1 402 ? 15.469  -24.223 44.891  1.000 47.586  0 402 ILE AAA O     1 ? 1 
ATOM   2888  C CB    . ILE A 1 402 ? 13.290  -22.188 44.298  1.000 41.700  0 402 ILE AAA CB    1 ? 1 
ATOM   2889  C CG1   . ILE A 1 402 ? 11.909  -21.627 43.944  1.000 40.587  0 402 ILE AAA CG1   1 ? 1 
ATOM   2890  C CG2   . ILE A 1 402 ? 14.399  -21.258 43.830  1.000 39.635  0 402 ILE AAA CG2   1 ? 1 
ATOM   2891  C CD1   . ILE A 1 402 ? 11.537  -21.772 42.475  1.000 40.793  0 402 ILE AAA CD1   1 ? 1 
ATOM   2892  N N     . GLU A 1 403 ? 15.652  -24.046 42.653  1.000 45.449  0 403 GLU AAA N     1 ? 1 
ATOM   2893  C CA    . GLU A 1 403 ? 17.134  -24.087 42.594  1.000 44.027  0 403 GLU AAA CA    1 ? 1 
ATOM   2894  C C     . GLU A 1 403 ? 17.630  -22.796 41.940  1.000 41.863  0 403 GLU AAA C     1 ? 1 
ATOM   2895  O O     . GLU A 1 403 ? 17.055  -22.375 40.922  1.000 41.081  0 403 GLU AAA O     1 ? 1 
ATOM   2896  C CB    . GLU A 1 403 ? 17.619  -25.334 41.841  1.000 45.873  0 403 GLU AAA CB    1 ? 1 
ATOM   2897  C CG    . GLU A 1 403 ? 18.956  -25.879 42.330  1.000 47.123  0 403 GLU AAA CG    1 ? 1 
ATOM   2898  C CD    . GLU A 1 403 ? 18.904  -26.572 43.687  1.000 47.749  0 403 GLU AAA CD    1 ? 1 
ATOM   2899  O OE1   . GLU A 1 403 ? 18.124  -27.572 43.831  1.000 48.279  0 403 GLU AAA OE1   1 ? 1 
ATOM   2900  O OE2   . GLU A 1 403 ? 19.600  -26.089 44.606  1.000 47.064  0 403 GLU AAA OE2   1 ? 1 
ATOM   2901  N N     . GLU A 1 404 ? 18.672  -22.207 42.513  1.000 41.028  0 404 GLU AAA N     1 ? 1 
ATOM   2902  C CA    . GLU A 1 404 ? 19.410  -21.058 41.942  1.000 41.504  0 404 GLU AAA CA    1 ? 1 
ATOM   2903  C C     . GLU A 1 404 ? 20.820  -21.533 41.565  1.000 36.905  0 404 GLU AAA C     1 ? 1 
ATOM   2904  O O     . GLU A 1 404 ? 21.594  -21.897 42.457  1.000 35.506  0 404 GLU AAA O     1 ? 1 
ATOM   2905  C CB    . GLU A 1 404 ? 19.427  -19.907 42.953  1.000 45.295  0 404 GLU AAA CB    1 ? 1 
ATOM   2906  C CG    . GLU A 1 404 ? 18.048  -19.566 43.499  1.000 47.513  0 404 GLU AAA CG    1 ? 1 
ATOM   2907  C CD    . GLU A 1 404 ? 18.051  -18.498 44.584  1.000 49.704  0 404 GLU AAA CD    1 ? 1 
ATOM   2908  O OE1   . GLU A 1 404 ? 18.843  -17.543 44.477  1.000 50.740  0 404 GLU AAA OE1   1 ? 1 
ATOM   2909  O OE2   . GLU A 1 404 ? 17.261  -18.629 45.538  1.000 53.567  0 404 GLU AAA OE2   1 ? 1 
ATOM   2910  N N     . TYR A 1 405 ? 21.110  -21.564 40.270  1.000 34.075  0 405 TYR AAA N     1 ? 1 
ATOM   2911  C CA    . TYR A 1 405 ? 22.440  -21.856 39.697  1.000 30.896  0 405 TYR AAA CA    1 ? 1 
ATOM   2912  C C     . TYR A 1 405 ? 23.066  -20.522 39.320  1.000 29.282  0 405 TYR AAA C     1 ? 1 
ATOM   2913  O O     . TYR A 1 405 ? 22.393  -19.698 38.695  1.000 28.259  0 405 TYR AAA O     1 ? 1 
ATOM   2914  C CB    . TYR A 1 405 ? 22.321  -22.767 38.484  1.000 30.161  0 405 TYR AAA CB    1 ? 1 
ATOM   2915  C CG    . TYR A 1 405 ? 21.873  -24.172 38.767  1.000 30.285  0 405 TYR AAA CG    1 ? 1 
ATOM   2916  C CD1   . TYR A 1 405 ? 20.534  -24.516 38.684  1.000 29.041  0 405 TYR AAA CD1   1 ? 1 
ATOM   2917  C CD2   . TYR A 1 405 ? 22.805  -25.185 38.981  1.000 31.152  0 405 TYR AAA CD2   1 ? 1 
ATOM   2918  C CE1   . TYR A 1 405 ? 20.116  -25.819 38.864  1.000 31.060  0 405 TYR AAA CE1   1 ? 1 
ATOM   2919  C CE2   . TYR A 1 405 ? 22.400  -26.500 39.193  1.000 32.873  0 405 TYR AAA CE2   1 ? 1 
ATOM   2920  C CZ    . TYR A 1 405 ? 21.046  -26.819 39.113  1.000 32.831  0 405 TYR AAA CZ    1 ? 1 
ATOM   2921  O OH    . TYR A 1 405 ? 20.613  -28.099 39.293  1.000 34.653  0 405 TYR AAA OH    1 ? 1 
ATOM   2922  N N     . LEU A 1 406 ? 24.322  -20.305 39.703  1.000 28.594  0 406 LEU AAA N     1 ? 1 
ATOM   2923  C CA    . LEU A 1 406 ? 24.964  -19.007 39.471  1.000 28.227  0 406 LEU AAA CA    1 ? 1 
ATOM   2924  C C     . LEU A 1 406 ? 26.481  -19.150 39.420  1.000 27.365  0 406 LEU AAA C     1 ? 1 
ATOM   2925  O O     . LEU A 1 406 ? 27.031  -20.178 39.802  1.000 25.176  0 406 LEU AAA O     1 ? 1 
ATOM   2926  C CB    . LEU A 1 406 ? 24.459  -18.001 40.518  1.000 29.423  0 406 LEU AAA CB    1 ? 1 
ATOM   2927  C CG    . LEU A 1 406 ? 24.993  -18.085 41.941  1.000 29.356  0 406 LEU AAA CG    1 ? 1 
ATOM   2928  C CD1   . LEU A 1 406 ? 24.566  -16.843 42.685  1.000 29.102  0 406 LEU AAA CD1   1 ? 1 
ATOM   2929  C CD2   . LEU A 1 406 ? 24.458  -19.313 42.649  1.000 31.426  0 406 LEU AAA CD2   1 ? 1 
ATOM   2930  N N     . SER A 1 407 ? 27.088  -18.137 38.825  1.000 26.275  0 407 SER AAA N     1 ? 1 
ATOM   2931  C CA    . SER A 1 407 ? 28.547  -17.972 38.697  1.000 26.819  0 407 SER AAA CA    1 ? 1 
ATOM   2932  C C     . SER A 1 407 ? 28.855  -16.466 38.688  1.000 27.115  0 407 SER AAA C     1 ? 1 
ATOM   2933  O O     . SER A 1 407 ? 28.116  -15.711 38.032  1.000 28.859  0 407 SER AAA O     1 ? 1 
ATOM   2934  C CB    . SER A 1 407 ? 29.031  -18.684 37.455  1.000 26.219  0 407 SER AAA CB    1 ? 1 
ATOM   2935  O OG    . SER A 1 407 ? 30.414  -18.457 37.261  1.000 27.133  0 407 SER AAA OG    1 ? 1 
ATOM   2936  N N     . GLU A 1 408 ? 29.855  -16.038 39.458  1.000 27.436  0 408 GLU AAA N     1 ? 1 
ATOM   2937  C CA    . GLU A 1 408 ? 30.396  -14.659 39.459  1.000 27.042  0 408 GLU AAA CA    1 ? 1 
ATOM   2938  C C     . GLU A 1 408 ? 31.793  -14.744 38.891  1.000 25.511  0 408 GLU AAA C     1 ? 1 
ATOM   2939  O O     . GLU A 1 408 ? 32.572  -15.547 39.378  1.000 25.456  0 408 GLU AAA O     1 ? 1 
ATOM   2940  C CB    . GLU A 1 408 ? 30.431  -14.104 40.887  1.000 28.446  0 408 GLU AAA CB    1 ? 1 
ATOM   2941  C CG    . GLU A 1 408 ? 30.757  -12.631 41.020  1.000 28.995  0 408 GLU AAA CG    1 ? 1 
ATOM   2942  C CD    . GLU A 1 408 ? 30.526  -12.084 42.435  1.000 31.545  0 408 GLU AAA CD    1 ? 1 
ATOM   2943  O OE1   . GLU A 1 408 ? 30.599  -12.869 43.395  1.000 34.040  0 408 GLU AAA OE1   1 ? 1 
ATOM   2944  O OE2   . GLU A 1 408 ? 30.264  -10.855 42.605  1.000 32.297  0 408 GLU AAA OE2   1 ? 1 
ATOM   2945  N N     . PHE A 1 409 ? 32.098  -13.922 37.908  1.000 25.485  0 409 PHE AAA N     1 ? 1 
ATOM   2946  C CA    . PHE A 1 409 ? 33.397  -13.993 37.192  1.000 24.850  0 409 PHE AAA CA    1 ? 1 
ATOM   2947  C C     . PHE A 1 409 ? 33.675  -12.680 36.500  1.000 23.880  0 409 PHE AAA C     1 ? 1 
ATOM   2948  O O     . PHE A 1 409 ? 32.840  -11.786 36.472  1.000 23.677  0 409 PHE AAA O     1 ? 1 
ATOM   2949  C CB    . PHE A 1 409 ? 33.351  -15.076 36.113  1.000 26.515  0 409 PHE AAA CB    1 ? 1 
ATOM   2950  C CG    . PHE A 1 409 ? 32.240  -14.838 35.109  1.000 26.351  0 409 PHE AAA CG    1 ? 1 
ATOM   2951  C CD1   . PHE A 1 409 ? 30.921  -15.110 35.439  1.000 26.264  0 409 PHE AAA CD1   1 ? 1 
ATOM   2952  C CD2   . PHE A 1 409 ? 32.530  -14.336 33.853  1.000 26.248  0 409 PHE AAA CD2   1 ? 1 
ATOM   2953  C CE1   . PHE A 1 409 ? 29.917  -14.911 34.515  1.000 27.764  0 409 PHE AAA CE1   1 ? 1 
ATOM   2954  C CE2   . PHE A 1 409 ? 31.511  -14.114 32.937  1.000 27.046  0 409 PHE AAA CE2   1 ? 1 
ATOM   2955  C CZ    . PHE A 1 409 ? 30.208  -14.405 33.256  1.000 26.650  0 409 PHE AAA CZ    1 ? 1 
ATOM   2956  N N     . SER A 1 410 ? 34.841  -12.608 35.896  1.000 23.425  0 410 SER AAA N     1 ? 1 
ATOM   2957  C CA    . SER A 1 410 ? 35.272  -11.427 35.132  1.000 23.132  0 410 SER AAA CA    1 ? 1 
ATOM   2958  C C     . SER A 1 410 ? 35.265  -11.775 33.639  1.000 22.706  0 410 SER AAA C     1 ? 1 
ATOM   2959  O O     . SER A 1 410 ? 35.631  -12.921 33.287  1.000 22.594  0 410 SER AAA O     1 ? 1 
ATOM   2960  C CB    . SER A 1 410 ? 36.597  -11.006 35.592  1.000 23.500  0 410 SER AAA CB    1 ? 1 
ATOM   2961  O OG    . SER A 1 410 ? 37.050  -10.009 34.716  1.000 24.296  0 410 SER AAA OG    1 ? 1 
ATOM   2962  N N     . THR A 1 411 ? 34.757  -10.869 32.819  1.000 21.982  0 411 THR AAA N     1 ? 1 
ATOM   2963  C CA    . THR A 1 411 ? 35.039  -10.811 31.375  1.000 22.396  0 411 THR AAA CA    1 ? 1 
ATOM   2964  C C     . THR A 1 411 ? 36.546  -11.033 31.211  1.000 22.790  0 411 THR AAA C     1 ? 1 
ATOM   2965  O O     . THR A 1 411 ? 37.318  -10.527 32.074  1.000 20.964  0 411 THR AAA O     1 ? 1 
ATOM   2966  C CB    . THR A 1 411 ? 34.623  -9.448  30.790  1.000 22.534  0 411 THR AAA CB    1 ? 1 
ATOM   2967  O OG1   . THR A 1 411 ? 33.251  -9.304  31.081  1.000 22.717  0 411 THR AAA OG1   1 ? 1 
ATOM   2968  C CG2   . THR A 1 411 ? 34.781  -9.338  29.288  1.000 23.266  0 411 THR AAA CG2   1 ? 1 
ATOM   2969  N N     . LEU A 1 412 ? 36.926  -11.801 30.190  1.000 22.521  0 412 LEU AAA N     1 ? 1 
ATOM   2970  C CA    . LEU A 1 412 ? 38.334  -12.095 29.849  1.000 23.621  0 412 LEU AAA CA    1 ? 1 
ATOM   2971  C C     . LEU A 1 412 ? 39.147  -10.797 29.699  1.000 24.940  0 412 LEU AAA C     1 ? 1 
ATOM   2972  O O     . LEU A 1 412 ? 40.198  -10.674 30.348  1.000 25.692  0 412 LEU AAA O     1 ? 1 
ATOM   2973  C CB    . LEU A 1 412 ? 38.272  -12.856 28.530  1.000 24.680  0 412 LEU AAA CB    1 ? 1 
ATOM   2974  C CG    . LEU A 1 412 ? 39.586  -13.147 27.842  1.000 25.110  0 412 LEU AAA CG    1 ? 1 
ATOM   2975  C CD1   . LEU A 1 412 ? 40.477  -13.889 28.759  1.000 26.645  0 412 LEU AAA CD1   1 ? 1 
ATOM   2976  C CD2   . LEU A 1 412 ? 39.310  -13.929 26.599  1.000 25.879  0 412 LEU AAA CD2   1 ? 1 
ATOM   2977  N N     . GLU A 1 413 ? 38.661  -9.860  28.873  1.000 26.003  0 413 GLU AAA N     1 ? 1 
ATOM   2978  C CA    . GLU A 1 413 ? 39.349  -8.605  28.510  1.000 27.320  0 413 GLU AAA CA    1 ? 1 
ATOM   2979  C C     . GLU A 1 413 ? 39.533  -7.766  29.773  1.000 28.107  0 413 GLU AAA C     1 ? 1 
ATOM   2980  O O     . GLU A 1 413 ? 40.638  -7.198  29.973  1.000 28.255  0 413 GLU AAA O     1 ? 1 
ATOM   2981  C CB    . GLU A 1 413 ? 38.487  -7.775  27.561  1.000 29.636  0 413 GLU AAA CB    1 ? 1 
ATOM   2982  C CG    . GLU A 1 413 ? 38.136  -8.452  26.257  1.000 32.305  0 413 GLU AAA CG    1 ? 1 
ATOM   2983  C CD    . GLU A 1 413 ? 36.849  -9.239  26.193  1.000 32.812  0 413 GLU AAA CD    1 ? 1 
ATOM   2984  O OE1   . GLU A 1 413 ? 36.662  -10.134 27.055  1.000 34.002  0 413 GLU AAA OE1   1 ? 1 
ATOM   2985  O OE2   . GLU A 1 413 ? 36.047  -8.952  25.254  1.000 37.520  0 413 GLU AAA OE2   1 ? 1 
ATOM   2986  N N     . ILE A 1 414 ? 38.471  -7.661  30.565  1.000 26.406  0 414 ILE AAA N     1 ? 1 
ATOM   2987  C CA    . ILE A 1 414 ? 38.509  -6.896  31.842  1.000 27.112  0 414 ILE AAA CA    1 ? 1 
ATOM   2988  C C     . ILE A 1 414 ? 39.476  -7.582  32.805  1.000 26.009  0 414 ILE AAA C     1 ? 1 
ATOM   2989  O O     . ILE A 1 414 ? 40.288  -6.871  33.407  1.000 27.508  0 414 ILE AAA O     1 ? 1 
ATOM   2990  C CB    . ILE A 1 414 ? 37.106  -6.722  32.432  1.000 26.971  0 414 ILE AAA CB    1 ? 1 
ATOM   2991  C CG1   . ILE A 1 414 ? 36.123  -6.241  31.356  1.000 27.386  0 414 ILE AAA CG1   1 ? 1 
ATOM   2992  C CG2   . ILE A 1 414 ? 37.138  -5.798  33.641  1.000 26.303  0 414 ILE AAA CG2   1 ? 1 
ATOM   2993  C CD1   . ILE A 1 414 ? 36.363  -4.865  30.879  1.000 28.950  0 414 ILE AAA CD1   1 ? 1 
ATOM   2994  N N     . ALA A 1 415 ? 39.447  -8.906  32.907  1.000 24.800  0 415 ALA AAA N     1 ? 1 
ATOM   2995  C CA    . ALA A 1 415 ? 40.359  -9.645  33.810  1.000 23.755  0 415 ALA AAA CA    1 ? 1 
ATOM   2996  C C     . ALA A 1 415 ? 41.803  -9.248  33.472  1.000 24.569  0 415 ALA AAA C     1 ? 1 
ATOM   2997  O O     . ALA A 1 415 ? 42.548  -8.946  34.400  1.000 25.327  0 415 ALA AAA O     1 ? 1 
ATOM   2998  C CB    . ALA A 1 415 ? 40.145  -11.138 33.732  1.000 22.481  0 415 ALA AAA CB    1 ? 1 
ATOM   2999  N N     . ALA A 1 416 ? 42.175  -9.221  32.190  1.000 25.166  0 416 ALA AAA N     1 ? 1 
ATOM   3000  C CA    . ALA A 1 416 ? 43.568  -8.981  31.722  1.000 25.374  0 416 ALA AAA CA    1 ? 1 
ATOM   3001  C C     . ALA A 1 416 ? 43.957  -7.504  31.915  1.000 26.116  0 416 ALA AAA C     1 ? 1 
ATOM   3002  O O     . ALA A 1 416 ? 45.176  -7.205  32.007  1.000 26.042  0 416 ALA AAA O     1 ? 1 
ATOM   3003  C CB    . ALA A 1 416 ? 43.690  -9.409  30.274  1.000 24.903  0 416 ALA AAA CB    1 ? 1 
ATOM   3004  N N     . ALA A 1 417 ? 42.977  -6.603  32.022  1.000 27.026  0 417 ALA AAA N     1 ? 1 
ATOM   3005  C CA    . ALA A 1 417 ? 43.215  -5.162  32.249  1.000 28.791  0 417 ALA AAA CA    1 ? 1 
ATOM   3006  C C     . ALA A 1 417 ? 43.611  -4.874  33.702  1.000 31.229  0 417 ALA AAA C     1 ? 1 
ATOM   3007  O O     . ALA A 1 417 ? 44.268  -3.854  33.915  1.000 36.973  0 417 ALA AAA O     1 ? 1 
ATOM   3008  C CB    . ALA A 1 417 ? 41.983  -4.389  31.865  1.000 28.657  0 417 ALA AAA CB    1 ? 1 
ATOM   3009  N N     . HIS A 1 418 ? 43.238  -5.701  34.678  1.000 32.922  0 418 HIS AAA N     1 ? 1 
ATOM   3010  C CA    . HIS A 1 418 ? 43.569  -5.493  36.125  1.000 33.479  0 418 HIS AAA CA    1 ? 1 
ATOM   3011  C C     . HIS A 1 418 ? 43.007  -4.134  36.565  1.000 33.059  0 418 HIS AAA C     1 ? 1 
ATOM   3012  O O     . HIS A 1 418 ? 43.766  -3.278  37.015  1.000 35.817  0 418 HIS AAA O     1 ? 1 
ATOM   3013  C CB    . HIS A 1 418 ? 45.089  -5.625  36.387  1.000 35.287  0 418 HIS AAA CB    1 ? 1 
ATOM   3014  C CG    . HIS A 1 418 ? 45.596  -7.028  36.258  1.000 37.533  0 418 HIS AAA CG    1 ? 1 
ATOM   3015  N ND1   . HIS A 1 418 ? 45.476  -7.971  37.262  1.000 41.465  0 418 HIS AAA ND1   1 ? 1 
ATOM   3016  C CD2   . HIS A 1 418 ? 46.231  -7.667  35.259  1.000 40.051  0 418 HIS AAA CD2   1 ? 1 
ATOM   3017  C CE1   . HIS A 1 418 ? 45.992  -9.125  36.864  1.000 41.084  0 418 HIS AAA CE1   1 ? 1 
ATOM   3018  N NE2   . HIS A 1 418 ? 46.448  -8.966  35.645  1.000 39.490  0 418 HIS AAA NE2   1 ? 1 
ATOM   3019  N N     . ARG A 1 419 ? 41.708  -3.936  36.396  1.000 33.193  0 419 ARG AAA N     1 ? 1 
ATOM   3020  C CA    . ARG A 1 419 ? 40.960  -2.724  36.821  1.000 32.185  0 419 ARG AAA CA    1 ? 1 
ATOM   3021  C C     . ARG A 1 419 ? 41.087  -2.544  38.339  1.000 33.483  0 419 ARG AAA C     1 ? 1 
ATOM   3022  O O     . ARG A 1 419 ? 40.825  -3.507  39.094  1.000 35.186  0 419 ARG AAA O     1 ? 1 
ATOM   3023  C CB    . ARG A 1 419 ? 39.481  -2.818  36.418  1.000 33.266  0 419 ARG AAA CB    1 ? 1 
ATOM   3024  C CG    . ARG A 1 419 ? 39.220  -2.758  34.917  1.000 32.798  0 419 ARG AAA CG    1 ? 1 
ATOM   3025  C CD    . ARG A 1 419 ? 37.826  -2.244  34.568  1.000 33.349  0 419 ARG AAA CD    1 ? 1 
ATOM   3026  N NE    . ARG A 1 419 ? 37.751  -1.896  33.155  1.000 33.684  0 419 ARG AAA NE    1 ? 1 
ATOM   3027  C CZ    . ARG A 1 419 ? 36.705  -1.405  32.527  1.000 33.554  0 419 ARG AAA CZ    1 ? 1 
ATOM   3028  N NH1   . ARG A 1 419 ? 35.591  -1.170  33.195  1.000 33.845  0 419 ARG AAA NH1   1 ? 1 
ATOM   3029  N NH2   . ARG A 1 419 ? 36.805  -1.091  31.235  1.000 33.630  0 419 ARG AAA NH2   1 ? 1 
ATOM   3030  N N     . GLU A 1 420 ? 41.462  -1.339  38.770  1.000 35.479  0 420 GLU AAA N     1 ? 1 
ATOM   3031  C CA    . GLU A 1 420 ? 41.759  -0.965  40.174  1.000 37.108  0 420 GLU AAA CA    1 ? 1 
ATOM   3032  C C     . GLU A 1 420 ? 40.723  0.042   40.679  1.000 36.994  0 420 GLU AAA C     1 ? 1 
ATOM   3033  O O     . GLU A 1 420 ? 40.274  0.922   39.874  1.000 35.171  0 420 GLU AAA O     1 ? 1 
ATOM   3034  C CB    . GLU A 1 420 ? 43.156  -0.363  40.298  1.000 40.017  0 420 GLU AAA CB    1 ? 1 
ATOM   3035  C CG    . GLU A 1 420 ? 44.256  -1.379  40.019  1.000 43.597  0 420 GLU AAA CG    1 ? 1 
ATOM   3036  C CD    . GLU A 1 420 ? 45.632  -1.010  40.547  1.000 43.820  0 420 GLU AAA CD    1 ? 1 
ATOM   3037  O OE1   . GLU A 1 420 ? 45.726  -0.496  41.670  1.000 42.369  0 420 GLU AAA OE1   1 ? 1 
ATOM   3038  O OE2   . GLU A 1 420 ? 46.612  -1.218  39.804  1.000 48.132  0 420 GLU AAA OE2   1 ? 1 
ATOM   3039  N N     . LYS A 1 421 ? 40.385  -0.101  41.961  1.000 34.761  0 421 LYS AAA N     1 ? 1 
ATOM   3040  C CA    . LYS A 1 421 ? 39.679  0.902   42.782  1.000 36.612  0 421 LYS AAA CA    1 ? 1 
ATOM   3041  C C     . LYS A 1 421 ? 40.387  2.242   42.662  1.000 36.050  0 421 LYS AAA C     1 ? 1 
ATOM   3042  O O     . LYS A 1 421 ? 41.594  2.285   42.586  1.000 35.046  0 421 LYS AAA O     1 ? 1 
ATOM   3043  C CB    . LYS A 1 421 ? 39.634  0.478   44.261  1.000 36.537  0 421 LYS AAA CB    1 ? 1 
ATOM   3044  C CG    . LYS A 1 421 ? 38.652  -0.636  44.574  1.000 38.185  0 421 LYS AAA CG    1 ? 1 
ATOM   3045  C CD    . LYS A 1 421 ? 38.403  -0.950  46.016  1.000 40.064  0 421 LYS AAA CD    1 ? 1 
ATOM   3046  C CE    . LYS A 1 421 ? 37.372  -2.059  46.112  1.000 41.076  0 421 LYS AAA CE    1 ? 1 
ATOM   3047  N NZ    . LYS A 1 421 ? 37.254  -2.663  47.458  1.000 41.966  0 421 LYS AAA NZ    1 ? 1 
ATOM   3048  N N     . PRO A 1 422 ? 39.668  3.383   42.686  1.000 40.332  0 422 PRO AAA N     1 ? 1 
ATOM   3049  C CA    . PRO A 1 422 ? 40.328  4.682   42.829  1.000 44.275  0 422 PRO AAA CA    1 ? 1 
ATOM   3050  C C     . PRO A 1 422 ? 41.042  4.682   44.192  1.000 51.352  0 422 PRO AAA C     1 ? 1 
ATOM   3051  O O     . PRO A 1 422 ? 40.557  4.009   45.117  1.000 53.094  0 422 PRO AAA O     1 ? 1 
ATOM   3052  C CB    . PRO A 1 422 ? 39.200  5.721   42.755  1.000 42.547  0 422 PRO AAA CB    1 ? 1 
ATOM   3053  C CG    . PRO A 1 422 ? 38.010  4.954   42.195  1.000 41.824  0 422 PRO AAA CG    1 ? 1 
ATOM   3054  C CD    . PRO A 1 422 ? 38.199  3.501   42.605  1.000 40.105  0 422 PRO AAA CD    1 ? 1 
ATOM   3055  N N     . GLU A 1 423 ? 42.141  5.428   44.293  1.000 57.779  0 423 GLU AAA N     1 ? 1 
ATOM   3056  C CA    . GLU A 1 423 ? 43.073  5.377   45.444  1.000 60.954  0 423 GLU AAA CA    1 ? 1 
ATOM   3057  C C     . GLU A 1 423 ? 42.387  5.870   46.722  1.000 57.394  0 423 GLU AAA C     1 ? 1 
ATOM   3058  O O     . GLU A 1 423 ? 42.796  5.395   47.811  1.000 54.886  0 423 GLU AAA O     1 ? 1 
ATOM   3059  C CB    . GLU A 1 423 ? 44.335  6.169   45.103  1.000 67.687  0 423 GLU AAA CB    1 ? 1 
ATOM   3060  C CG    . GLU A 1 423 ? 44.104  7.653   44.854  1.000 72.500  0 423 GLU AAA CG    1 ? 1 
ATOM   3061  C CD    . GLU A 1 423 ? 45.406  8.459   44.836  1.000 77.050  0 423 GLU AAA CD    1 ? 1 
ATOM   3062  O OE1   . GLU A 1 423 ? 46.156  8.381   45.845  1.000 72.063  0 423 GLU AAA OE1   1 ? 1 
ATOM   3063  O OE2   . GLU A 1 423 ? 45.688  9.144   43.812  1.000 78.244  0 423 GLU AAA OE2   1 ? 1 
ATOM   3064  N N     . HIS A 1 424 ? 41.331  6.685   46.614  1.000 56.437  0 424 HIS AAA N     1 ? 1 
ATOM   3065  C CA    . HIS A 1 424 ? 40.599  7.200   47.808  1.000 57.787  0 424 HIS AAA CA    1 ? 1 
ATOM   3066  C C     . HIS A 1 424 ? 39.748  6.115   48.493  1.000 55.372  0 424 HIS AAA C     1 ? 1 
ATOM   3067  O O     . HIS A 1 424 ? 39.285  6.409   49.605  1.000 54.507  0 424 HIS AAA O     1 ? 1 
ATOM   3068  C CB    . HIS A 1 424 ? 39.782  8.464   47.482  1.000 60.216  0 424 HIS AAA CB    1 ? 1 
ATOM   3069  C CG    . HIS A 1 424 ? 38.664  8.293   46.502  1.000 60.043  0 424 HIS AAA CG    1 ? 1 
ATOM   3070  N ND1   . HIS A 1 424 ? 37.409  7.864   46.885  1.000 56.935  0 424 HIS AAA ND1   1 ? 1 
ATOM   3071  C CD2   . HIS A 1 424 ? 38.582  8.582   45.185  1.000 58.728  0 424 HIS AAA CD2   1 ? 1 
ATOM   3072  C CE1   . HIS A 1 424 ? 36.609  7.859   45.835  1.000 56.461  0 424 HIS AAA CE1   1 ? 1 
ATOM   3073  N NE2   . HIS A 1 424 ? 37.309  8.276   44.773  1.000 56.685  0 424 HIS AAA NE2   1 ? 1 
ATOM   3074  N N     . LEU A 1 425 ? 39.568  4.913   47.907  1.000 52.461  0 425 LEU AAA N     1 ? 1 
ATOM   3075  C CA    . LEU A 1 425 ? 38.724  3.833   48.511  1.000 50.861  0 425 LEU AAA CA    1 ? 1 
ATOM   3076  C C     . LEU A 1 425 ? 39.568  2.627   48.945  1.000 51.276  0 425 LEU AAA C     1 ? 1 
ATOM   3077  O O     . LEU A 1 425 ? 38.976  1.607   49.425  1.000 44.939  0 425 LEU AAA O     1 ? 1 
ATOM   3078  C CB    . LEU A 1 425 ? 37.658  3.405   47.504  1.000 51.247  0 425 LEU AAA CB    1 ? 1 
ATOM   3079  C CG    . LEU A 1 425 ? 36.541  4.434   47.300  1.000 51.066  0 425 LEU AAA CG    1 ? 1 
ATOM   3080  C CD1   . LEU A 1 425 ? 35.751  4.144   46.035  1.000 47.756  0 425 LEU AAA CD1   1 ? 1 
ATOM   3081  C CD2   . LEU A 1 425 ? 35.629  4.522   48.527  1.000 50.915  0 425 LEU AAA CD2   1 ? 1 
ATOM   3082  N N     . ARG A 1 426 ? 40.894  2.726   48.791  1.000 47.604  0 426 ARG AAA N     1 ? 1 
ATOM   3083  C CA    . ARG A 1 426 ? 41.826  1.629   49.146  1.000 47.952  0 426 ARG AAA CA    1 ? 1 
ATOM   3084  C C     . ARG A 1 426 ? 41.971  1.564   50.669  1.000 51.125  0 426 ARG AAA C     1 ? 1 
ATOM   3085  O O     . ARG A 1 426 ? 42.145  2.627   51.274  1.000 47.675  0 426 ARG AAA O     1 ? 1 
ATOM   3086  C CB    . ARG A 1 426 ? 43.178  1.871   48.466  1.000 46.511  0 426 ARG AAA CB    1 ? 1 
ATOM   3087  C CG    . ARG A 1 426 ? 43.163  1.681   46.954  1.000 42.977  0 426 ARG AAA CG    1 ? 1 
ATOM   3088  C CD    . ARG A 1 426 ? 42.942  0.217   46.547  1.000 40.477  0 426 ARG AAA CD    1 ? 1 
ATOM   3089  N NE    . ARG A 1 426 ? 43.998  -0.601  47.114  1.000 41.319  0 426 ARG AAA NE    1 ? 1 
ATOM   3090  C CZ    . ARG A 1 426 ? 45.231  -0.746  46.596  1.000 39.593  0 426 ARG AAA CZ    1 ? 1 
ATOM   3091  N NH1   . ARG A 1 426 ? 45.561  -0.156  45.458  1.000 39.581  0 426 ARG AAA NH1   1 ? 1 
ATOM   3092  N NH2   . ARG A 1 426 ? 46.109  -1.506  47.212  1.000 38.673  0 426 ARG AAA NH2   1 ? 1 
ATOM   3093  N N     . GLU A 1 427 ? 41.916  0.361   51.249  1.000 56.118  0 427 GLU AAA N     1 ? 1 
ATOM   3094  C CA    . GLU A 1 427 ? 42.026  0.097   52.715  1.000 60.505  0 427 GLU AAA CA    1 ? 1 
ATOM   3095  C C     . GLU A 1 427 ? 43.372  -0.578  53.040  1.000 60.598  0 427 GLU AAA C     1 ? 1 
ATOM   3096  O O     . GLU A 1 427 ? 43.748  -0.578  54.223  1.000 64.423  0 427 GLU AAA O     1 ? 1 
ATOM   3097  C CB    . GLU A 1 427 ? 40.836  -0.746  53.215  1.000 64.359  0 427 GLU AAA CB    1 ? 1 
ATOM   3098  C CG    . GLU A 1 427 ? 39.796  0.039   54.012  1.000 65.378  0 427 GLU AAA CG    1 ? 1 
ATOM   3099  C CD    . GLU A 1 427 ? 38.436  -0.627  54.267  1.000 64.965  0 427 GLU AAA CD    1 ? 1 
ATOM   3100  O OE1   . GLU A 1 427 ? 37.433  0.037   54.029  1.000 59.726  0 427 GLU AAA OE1   1 ? 1 
ATOM   3101  O OE2   . GLU A 1 427 ? 38.372  -1.797  54.741  1.000 63.162  0 427 GLU AAA OE2   1 ? 1 
ATOM   3102  N N     . ASN A 1 428 ? 44.067  -1.179  52.068  1.000 56.345  0 428 ASN AAA N     1 ? 1 
ATOM   3103  C CA    . ASN A 1 428 ? 45.261  -2.034  52.306  1.000 54.712  0 428 ASN AAA CA    1 ? 1 
ATOM   3104  C C     . ASN A 1 428 ? 45.970  -2.332  50.987  1.000 51.240  0 428 ASN AAA C     1 ? 1 
ATOM   3105  O O     . ASN A 1 428 ? 45.680  -1.616  49.992  1.000 50.152  0 428 ASN AAA O     1 ? 1 
ATOM   3106  C CB    . ASN A 1 428 ? 44.865  -3.324  53.037  1.000 56.718  0 428 ASN AAA CB    1 ? 1 
ATOM   3107  C CG    . ASN A 1 428 ? 43.727  -4.078  52.380  1.000 52.437  0 428 ASN AAA CG    1 ? 1 
ATOM   3108  O OD1   . ASN A 1 428 ? 43.791  -4.433  51.203  1.000 50.558  0 428 ASN AAA OD1   1 ? 1 
ATOM   3109  N ND2   . ASN A 1 428 ? 42.710  -4.372  53.157  1.000 51.321  0 428 ASN AAA ND2   1 ? 1 
ATOM   3110  N N     . GLU A 1 429 ? 46.845  -3.345  50.975  1.000 48.488  0 429 GLU AAA N     1 ? 1 
ATOM   3111  C CA    . GLU A 1 429 ? 47.642  -3.720  49.778  1.000 51.446  0 429 GLU AAA CA    1 ? 1 
ATOM   3112  C C     . GLU A 1 429 ? 46.966  -4.826  48.960  1.000 49.240  0 429 GLU AAA C     1 ? 1 
ATOM   3113  O O     . GLU A 1 429 ? 47.583  -5.193  47.919  1.000 52.055  0 429 GLU AAA O     1 ? 1 
ATOM   3114  C CB    . GLU A 1 429 ? 49.057  -4.153  50.193  1.000 54.781  0 429 GLU AAA CB    1 ? 1 
ATOM   3115  C CG    . GLU A 1 429 ? 49.761  -3.133  51.057  1.000 57.742  0 429 GLU AAA CG    1 ? 1 
ATOM   3116  C CD    . GLU A 1 429 ? 49.551  -1.680  50.677  1.000 59.008  0 429 GLU AAA CD    1 ? 1 
ATOM   3117  O OE1   . GLU A 1 429 ? 49.812  -1.363  49.518  1.000 60.647  0 429 GLU AAA OE1   1 ? 1 
ATOM   3118  O OE2   . GLU A 1 429 ? 49.112  -0.873  51.552  1.000 62.126  0 429 GLU AAA OE2   1 ? 1 
ATOM   3119  N N     . MET A 1 430 ? 45.805  -5.335  49.390  1.000 46.740  0 430 MET AAA N     1 ? 1 
ATOM   3120  C CA    . MET A 1 430 ? 45.144  -6.498  48.738  1.000 48.828  0 430 MET AAA CA    1 ? 1 
ATOM   3121  C C     . MET A 1 430 ? 43.673  -6.185  48.375  1.000 49.438  0 430 MET AAA C     1 ? 1 
ATOM   3122  O O     . MET A 1 430 ? 42.983  -7.114  47.865  1.000 46.487  0 430 MET AAA O     1 ? 1 
ATOM   3123  C CB    . MET A 1 430 ? 45.225  -7.764  49.596  1.000 50.501  0 430 MET AAA CB    1 ? 1 
ATOM   3124  C CG    . MET A 1 430 ? 44.716  -7.561  50.988  1.000 57.048  0 430 MET AAA CG    1 ? 1 
ATOM   3125  S SD    . MET A 1 430 ? 44.491  -9.050  51.989  1.000 58.023  0 430 MET AAA SD    1 ? 1 
ATOM   3126  C CE    . MET A 1 430 ? 43.428  -8.233  53.190  1.000 61.551  0 430 MET AAA CE    1 ? 1 
ATOM   3127  N N     . ASP A 1 431 ? 43.233  -4.929  48.513  1.000 45.177  0 431 ASP AAA N     1 ? 1 
ATOM   3128  C CA    . ASP A 1 431 ? 41.873  -4.456  48.117  1.000 42.023  0 431 ASP AAA CA    1 ? 1 
ATOM   3129  C C     . ASP A 1 431 ? 41.982  -3.610  46.827  1.000 38.265  0 431 ASP AAA C     1 ? 1 
ATOM   3130  O O     . ASP A 1 431 ? 41.151  -2.713  46.636  1.000 36.082  0 431 ASP AAA O     1 ? 1 
ATOM   3131  C CB    . ASP A 1 431 ? 41.211  -3.742  49.300  1.000 43.866  0 431 ASP AAA CB    1 ? 1 
ATOM   3132  C CG    . ASP A 1 431 ? 41.638  -2.297  49.505  1.000 44.945  0 431 ASP AAA CG    1 ? 1 
ATOM   3133  O OD1   . ASP A 1 431 ? 42.858  -2.032  49.430  1.000 48.651  0 431 ASP AAA OD1   1 ? 1 
ATOM   3134  O OD2   . ASP A 1 431 ? 40.767  -1.447  49.794  1.000 46.262  0 431 ASP AAA OD2   1 ? 1 
ATOM   3135  N N     . PHE A 1 432 ? 42.954  -3.917  45.954  1.000 35.043  0 432 PHE AAA N     1 ? 1 
ATOM   3136  C CA    . PHE A 1 432 ? 43.292  -3.121  44.753  1.000 34.292  0 432 PHE AAA CA    1 ? 1 
ATOM   3137  C C     . PHE A 1 432 ? 42.195  -3.280  43.686  1.000 33.301  0 432 PHE AAA C     1 ? 1 
ATOM   3138  O O     . PHE A 1 432 ? 41.885  -2.287  43.027  1.000 33.841  0 432 PHE AAA O     1 ? 1 
ATOM   3139  C CB    . PHE A 1 432 ? 44.682  -3.485  44.220  1.000 33.352  0 432 PHE AAA CB    1 ? 1 
ATOM   3140  C CG    . PHE A 1 432 ? 44.948  -4.954  43.989  1.000 34.718  0 432 PHE AAA CG    1 ? 1 
ATOM   3141  C CD1   . PHE A 1 432 ? 44.663  -5.538  42.766  1.000 35.202  0 432 PHE AAA CD1   1 ? 1 
ATOM   3142  C CD2   . PHE A 1 432 ? 45.503  -5.760  44.974  1.000 35.068  0 432 PHE AAA CD2   1 ? 1 
ATOM   3143  C CE1   . PHE A 1 432 ? 44.916  -6.892  42.539  1.000 35.574  0 432 PHE AAA CE1   1 ? 1 
ATOM   3144  C CE2   . PHE A 1 432 ? 45.726  -7.111  44.761  1.000 34.779  0 432 PHE AAA CE2   1 ? 1 
ATOM   3145  C CZ    . PHE A 1 432 ? 45.432  -7.678  43.545  1.000 35.255  0 432 PHE AAA CZ    1 ? 1 
ATOM   3146  N N     . ALA A 1 433 ? 41.661  -4.500  43.522  1.000 33.193  0 433 ALA AAA N     1 ? 1 
ATOM   3147  C CA    . ALA A 1 433 ? 40.809  -4.937  42.389  1.000 31.655  0 433 ALA AAA CA    1 ? 1 
ATOM   3148  C C     . ALA A 1 433 ? 39.400  -4.383  42.542  1.000 31.623  0 433 ALA AAA C     1 ? 1 
ATOM   3149  O O     . ALA A 1 433 ? 38.899  -4.344  43.687  1.000 31.775  0 433 ALA AAA O     1 ? 1 
ATOM   3150  C CB    . ALA A 1 433 ? 40.765  -6.440  42.269  1.000 30.499  0 433 ALA AAA CB    1 ? 1 
ATOM   3151  N N     . LEU A 1 434 ? 38.789  -4.014  41.405  1.000 30.608  0 434 LEU AAA N     1 ? 1 
ATOM   3152  C CA    . LEU A 1 434 ? 37.328  -3.851  41.299  1.000 29.623  0 434 LEU AAA CA    1 ? 1 
ATOM   3153  C C     . LEU A 1 434 ? 36.660  -5.192  41.532  1.000 28.575  0 434 LEU AAA C     1 ? 1 
ATOM   3154  O O     . LEU A 1 434 ? 37.267  -6.242  41.322  1.000 30.176  0 434 LEU AAA O     1 ? 1 
ATOM   3155  C CB    . LEU A 1 434 ? 36.994  -3.347  39.908  1.000 28.690  0 434 LEU AAA CB    1 ? 1 
ATOM   3156  C CG    . LEU A 1 434 ? 37.377  -1.919  39.620  1.000 28.667  0 434 LEU AAA CG    1 ? 1 
ATOM   3157  C CD1   . LEU A 1 434 ? 36.713  -1.518  38.288  1.000 30.005  0 434 LEU AAA CD1   1 ? 1 
ATOM   3158  C CD2   . LEU A 1 434 ? 36.979  -1.019  40.781  1.000 28.383  0 434 LEU AAA CD2   1 ? 1 
ATOM   3159  N N     . PRO A 1 435 ? 35.391  -5.210  41.990  1.000 25.891  0 435 PRO AAA N     1 ? 1 
ATOM   3160  C CA    . PRO A 1 435 ? 34.651  -6.464  42.026  1.000 25.965  0 435 PRO AAA CA    1 ? 1 
ATOM   3161  C C     . PRO A 1 435 ? 34.642  -7.131  40.644  1.000 25.810  0 435 PRO AAA C     1 ? 1 
ATOM   3162  O O     . PRO A 1 435 ? 34.667  -6.433  39.617  1.000 25.488  0 435 PRO AAA O     1 ? 1 
ATOM   3163  C CB    . PRO A 1 435 ? 33.232  -6.028  42.432  1.000 25.090  0 435 PRO AAA CB    1 ? 1 
ATOM   3164  C CG    . PRO A 1 435 ? 33.514  -4.821  43.283  1.000 24.778  0 435 PRO AAA CG    1 ? 1 
ATOM   3165  C CD    . PRO A 1 435 ? 34.622  -4.093  42.537  1.000 24.779  0 435 PRO AAA CD    1 ? 1 
ATOM   3166  N N     . LEU A 1 436 ? 34.495  -8.449  40.654  1.000 24.909  0 436 LEU AAA N     1 ? 1 
ATOM   3167  C CA    . LEU A 1 436 ? 34.260  -9.213  39.418  1.000 24.236  0 436 LEU AAA CA    1 ? 1 
ATOM   3168  C C     . LEU A 1 436 ? 33.095  -8.548  38.682  1.000 22.788  0 436 LEU AAA C     1 ? 1 
ATOM   3169  O O     . LEU A 1 436 ? 32.136  -8.154  39.372  1.000 21.527  0 436 LEU AAA O     1 ? 1 
ATOM   3170  C CB    . LEU A 1 436 ? 34.013  -10.667 39.774  1.000 24.501  0 436 LEU AAA CB    1 ? 1 
ATOM   3171  C CG    . LEU A 1 436 ? 35.152  -11.357 40.522  1.000 26.675  0 436 LEU AAA CG    1 ? 1 
ATOM   3172  C CD1   . LEU A 1 436 ? 34.676  -12.716 41.035  1.000 27.299  0 436 LEU AAA CD1   1 ? 1 
ATOM   3173  C CD2   . LEU A 1 436 ? 36.422  -11.515 39.683  1.000 26.496  0 436 LEU AAA CD2   1 ? 1 
ATOM   3174  N N     . ASN A 1 437 ? 33.205  -8.376  37.346  1.000 21.859  0 437 ASN AAA N     1 ? 1 
ATOM   3175  C CA    . ASN A 1 437 ? 32.219  -7.498  36.644  1.000 21.904  0 437 ASN AAA CA    1 ? 1 
ATOM   3176  C C     . ASN A 1 437 ? 30.907  -8.248  36.354  1.000 21.624  0 437 ASN AAA C     1 ? 1 
ATOM   3177  O O     . ASN A 1 437 ? 29.919  -7.577  36.142  1.000 21.846  0 437 ASN AAA O     1 ? 1 
ATOM   3178  C CB    . ASN A 1 437 ? 32.831  -6.797  35.438  1.000 21.306  0 437 ASN AAA CB    1 ? 1 
ATOM   3179  C CG    . ASN A 1 437 ? 33.143  -7.745  34.308  1.000 21.311  0 437 ASN AAA CG    1 ? 1 
ATOM   3180  O OD1   . ASN A 1 437 ? 33.520  -8.880  34.525  1.000 22.789  0 437 ASN AAA OD1   1 ? 1 
ATOM   3181  N ND2   . ASN A 1 437 ? 33.040  -7.272  33.093  1.000 21.913  0 437 ASN AAA ND2   1 ? 1 
ATOM   3182  N N     . CYS A 1 438 ? 30.902  -9.582  36.362  1.000 22.030  0 438 CYS AAA N     1 ? 1 
ATOM   3183  C CA    . CYS A 1 438 ? 29.780  -10.413 35.868  1.000 22.747  0 438 CYS AAA CA    1 ? 1 
ATOM   3184  C C     . CYS A 1 438 ? 29.175  -11.308 36.943  1.000 22.537  0 438 CYS AAA C     1 ? 1 
ATOM   3185  O O     . CYS A 1 438 ? 29.920  -11.822 37.797  1.000 21.549  0 438 CYS AAA O     1 ? 1 
ATOM   3186  C CB    . CYS A 1 438 ? 30.181  -11.326 34.717  1.000 23.856  0 438 CYS AAA CB    1 ? 1 
ATOM   3187  S SG    . CYS A 1 438 ? 30.755  -10.417 33.252  1.000 24.378  0 438 CYS AAA SG    1 ? 1 
ATOM   3188  N N     . LEU A 1 439 ? 27.868  -11.489 36.832  1.000 22.860  0 439 LEU AAA N     1 ? 1 
ATOM   3189  C CA    . LEU A 1 439 ? 27.074  -12.454 37.634  1.000 24.893  0 439 LEU AAA CA    1 ? 1 
ATOM   3190  C C     . LEU A 1 439 ? 25.979  -13.053 36.752  1.000 23.978  0 439 LEU AAA C     1 ? 1 
ATOM   3191  O O     . LEU A 1 439 ? 25.138  -12.302 36.270  1.000 22.692  0 439 LEU AAA O     1 ? 1 
ATOM   3192  C CB    . LEU A 1 439 ? 26.434  -11.778 38.849  1.000 26.152  0 439 LEU AAA CB    1 ? 1 
ATOM   3193  C CG    . LEU A 1 439 ? 25.597  -12.741 39.691  1.000 28.601  0 439 LEU AAA CG    1 ? 1 
ATOM   3194  C CD1   . LEU A 1 439 ? 26.513  -13.705 40.397  1.000 30.056  0 439 LEU AAA CD1   1 ? 1 
ATOM   3195  C CD2   . LEU A 1 439 ? 24.702  -12.063 40.705  1.000 28.930  0 439 LEU AAA CD2   1 ? 1 
ATOM   3196  N N     . ALA A 1 440 ? 26.015  -14.365 36.594  1.000 23.799  0 440 ALA AAA N     1 ? 1 
ATOM   3197  C CA    . ALA A 1 440 ? 25.022  -15.142 35.823  1.000 24.376  0 440 ALA AAA CA    1 ? 1 
ATOM   3198  C C     . ALA A 1 440 ? 24.187  -15.974 36.793  1.000 23.918  0 440 ALA AAA C     1 ? 1 
ATOM   3199  O O     . ALA A 1 440 ? 24.795  -16.622 37.684  1.000 23.989  0 440 ALA AAA O     1 ? 1 
ATOM   3200  C CB    . ALA A 1 440 ? 25.744  -16.009 34.825  1.000 23.954  0 440 ALA AAA CB    1 ? 1 
ATOM   3201  N N     . LYS A 1 441 ? 22.868  -15.910 36.654  1.000 23.717  0 441 LYS AAA N     1 ? 1 
ATOM   3202  C CA    . LYS A 1 441 ? 21.946  -16.688 37.519  1.000 25.200  0 441 LYS AAA CA    1 ? 1 
ATOM   3203  C C     . LYS A 1 441 ? 20.710  -17.166 36.762  1.000 25.080  0 441 LYS AAA C     1 ? 1 
ATOM   3204  O O     . LYS A 1 441 ? 20.014  -16.336 36.124  1.000 25.413  0 441 LYS AAA O     1 ? 1 
ATOM   3205  C CB    . LYS A 1 441 ? 21.494  -15.828 38.694  1.000 26.041  0 441 LYS AAA CB    1 ? 1 
ATOM   3206  C CG    . LYS A 1 441 ? 20.514  -16.524 39.603  1.000 26.397  0 441 LYS AAA CG    1 ? 1 
ATOM   3207  C CD    . LYS A 1 441 ? 20.471  -15.967 40.974  1.000 26.928  0 441 LYS AAA CD    1 ? 1 
ATOM   3208  C CE    . LYS A 1 441 ? 19.820  -14.621 41.045  1.000 26.069  0 441 LYS AAA CE    1 ? 1 
ATOM   3209  N NZ    . LYS A 1 441 ? 19.804  -14.138 42.441  1.000 27.157  0 441 LYS AAA NZ    1 ? 1 
ATOM   3210  N N     . LEU A 1 442 ? 20.460  -18.463 36.853  1.000 25.613  0 442 LEU AAA N     1 ? 1 
ATOM   3211  C CA    . LEU A 1 442 ? 19.192  -19.123 36.472  1.000 26.175  0 442 LEU AAA CA    1 ? 1 
ATOM   3212  C C     . LEU A 1 442 ? 18.411  -19.518 37.729  1.000 26.587  0 442 LEU AAA C     1 ? 1 
ATOM   3213  O O     . LEU A 1 442 ? 18.969  -20.093 38.669  1.000 25.999  0 442 LEU AAA O     1 ? 1 
ATOM   3214  C CB    . LEU A 1 442 ? 19.516  -20.370 35.648  1.000 26.824  0 442 LEU AAA CB    1 ? 1 
ATOM   3215  C CG    . LEU A 1 442 ? 20.211  -20.096 34.319  1.000 27.352  0 442 LEU AAA CG    1 ? 1 
ATOM   3216  C CD1   . LEU A 1 442 ? 20.564  -21.416 33.664  1.000 29.099  0 442 LEU AAA CD1   1 ? 1 
ATOM   3217  C CD2   . LEU A 1 442 ? 19.373  -19.236 33.389  1.000 26.693  0 442 LEU AAA CD2   1 ? 1 
ATOM   3218  N N     . VAL A 1 443 ? 17.129  -19.238 37.699  1.000 28.009  0 443 VAL AAA N     1 ? 1 
ATOM   3219  C CA    . VAL A 1 443 ? 16.155  -19.645 38.740  1.000 29.133  0 443 VAL AAA CA    1 ? 1 
ATOM   3220  C C     . VAL A 1 443 ? 15.233  -20.667 38.076  1.000 30.030  0 443 VAL AAA C     1 ? 1 
ATOM   3221  O O     . VAL A 1 443 ? 14.595  -20.313 37.037  1.000 29.008  0 443 VAL AAA O     1 ? 1 
ATOM   3222  C CB    . VAL A 1 443 ? 15.435  -18.396 39.279  1.000 28.740  0 443 VAL AAA CB    1 ? 1 
ATOM   3223  C CG1   . VAL A 1 443 ? 14.522  -18.754 40.424  1.000 29.012  0 443 VAL AAA CG1   1 ? 1 
ATOM   3224  C CG2   . VAL A 1 443 ? 16.434  -17.330 39.685  1.000 27.979  0 443 VAL AAA CG2   1 ? 1 
ATOM   3225  N N     . VAL A 1 444 ? 15.214  -21.886 38.619  1.000 32.159  0 444 VAL AAA N     1 ? 1 
ATOM   3226  C CA    . VAL A 1 444 ? 14.507  -23.059 38.027  1.000 32.533  0 444 VAL AAA CA    1 ? 1 
ATOM   3227  C C     . VAL A 1 444 ? 13.546  -23.673 39.059  1.000 32.747  0 444 VAL AAA C     1 ? 1 
ATOM   3228  O O     . VAL A 1 444 ? 13.824  -23.641 40.288  1.000 30.142  0 444 VAL AAA O     1 ? 1 
ATOM   3229  C CB    . VAL A 1 444 ? 15.512  -24.096 37.469  1.000 32.537  0 444 VAL AAA CB    1 ? 1 
ATOM   3230  C CG1   . VAL A 1 444 ? 16.536  -23.428 36.581  1.000 32.530  0 444 VAL AAA CG1   1 ? 1 
ATOM   3231  C CG2   . VAL A 1 444 ? 16.198  -24.893 38.552  1.000 33.904  0 444 VAL AAA CG2   1 ? 1 
ATOM   3232  N N     . VAL A 1 445 ? 12.474  -24.274 38.536  1.000 33.497  0 445 VAL AAA N     1 ? 1 
ATOM   3233  C CA    . VAL A 1 445 ? 11.490  -25.067 39.324  1.000 36.517  0 445 VAL AAA CA    1 ? 1 
ATOM   3234  C C     . VAL A 1 445 ? 11.830  -26.560 39.186  1.000 38.465  0 445 VAL AAA C     1 ? 1 
ATOM   3235  O O     . VAL A 1 445 ? 11.777  -27.110 38.067  1.000 39.622  0 445 VAL AAA O     1 ? 1 
ATOM   3236  C CB    . VAL A 1 445 ? 10.061  -24.742 38.875  1.000 36.339  0 445 VAL AAA CB    1 ? 1 
ATOM   3237  C CG1   . VAL A 1 445 ? 9.042   -25.526 39.660  1.000 37.106  0 445 VAL AAA CG1   1 ? 1 
ATOM   3238  C CG2   . VAL A 1 445 ? 9.793   -23.239 38.966  1.000 35.472  0 445 VAL AAA CG2   1 ? 1 
ATOM   3239  N N     . LYS A 1 446 ? 12.122  -27.203 40.307  1.000 41.009  0 446 LYS AAA N     1 ? 1 
ATOM   3240  C CA    . LYS A 1 446 ? 12.488  -28.644 40.372  1.000 44.480  0 446 LYS AAA CA    1 ? 1 
ATOM   3241  C C     . LYS A 1 446 ? 11.332  -29.522 39.885  1.000 42.517  0 446 LYS AAA C     1 ? 1 
ATOM   3242  O O     . LYS A 1 446 ? 11.593  -30.402 39.076  1.000 41.977  0 446 LYS AAA O     1 ? 1 
ATOM   3243  C CB    . LYS A 1 446 ? 12.907  -28.990 41.797  1.000 46.530  0 446 LYS AAA CB    1 ? 1 
ATOM   3244  C CG    . LYS A 1 446 ? 14.096  -28.179 42.280  1.000 47.273  0 446 LYS AAA CG    1 ? 1 
ATOM   3245  C CD    . LYS A 1 446 ? 15.126  -29.037 42.926  1.000 51.143  0 446 LYS AAA CD    1 ? 1 
ATOM   3246  C CE    . LYS A 1 446 ? 14.884  -29.244 44.398  1.000 52.775  0 446 LYS AAA CE    1 ? 1 
ATOM   3247  N NZ    . LYS A 1 446 ? 16.085  -29.812 45.048  1.000 55.974  0 446 LYS AAA NZ    1 ? 1 
ATOM   3248  N N     . SER A 1 447 ? 10.100  -29.229 40.290  1.000 43.357  0 447 SER AAA N     1 ? 1 
ATOM   3249  C CA    . SER A 1 447 ? 8.903   -30.064 39.983  1.000 45.672  0 447 SER AAA CA    1 ? 1 
ATOM   3250  C C     . SER A 1 447 ? 8.526   -29.941 38.502  1.000 46.262  0 447 SER AAA C     1 ? 1 
ATOM   3251  O O     . SER A 1 447 ? 7.513   -30.545 38.118  1.000 48.248  0 447 SER AAA O     1 ? 1 
ATOM   3252  C CB    . SER A 1 447 ? 7.739   -29.732 40.880  1.000 44.021  0 447 SER AAA CB    1 ? 1 
ATOM   3253  O OG    . SER A 1 447 ? 7.348   -28.379 40.703  1.000 43.390  0 447 SER AAA OG    1 ? 1 
ATOM   3254  N N     . GLN A 1 448 ? 9.288   -29.193 37.693  1.000 46.687  0 448 GLN AAA N     1 ? 1 
ATOM   3255  C CA    . GLN A 1 448 ? 9.016   -29.069 36.230  1.000 47.592  0 448 GLN AAA CA    1 ? 1 
ATOM   3256  C C     . GLN A 1 448 ? 10.280  -29.404 35.427  1.000 45.513  0 448 GLN AAA C     1 ? 1 
ATOM   3257  O O     . GLN A 1 448 ? 10.473  -28.774 34.365  1.000 41.408  0 448 GLN AAA O     1 ? 1 
ATOM   3258  C CB    . GLN A 1 448 ? 8.456   -27.680 35.920  1.000 47.588  0 448 GLN AAA CB    1 ? 1 
ATOM   3259  C CG    . GLN A 1 448 ? 7.155   -27.404 36.666  1.000 49.809  0 448 GLN AAA CG    1 ? 1 
ATOM   3260  C CD    . GLN A 1 448 ? 6.615   -26.038 36.343  1.000 52.381  0 448 GLN AAA CD    1 ? 1 
ATOM   3261  O OE1   . GLN A 1 448 ? 6.662   -25.606 35.197  1.000 57.972  0 448 GLN AAA OE1   1 ? 1 
ATOM   3262  N NE2   . GLN A 1 448 ? 6.115   -25.332 37.342  1.000 53.201  0 448 GLN AAA NE2   1 ? 1 
ATOM   3263  N N     . GLY A 1 449 ? 11.056  -30.390 35.898  1.000 43.088  0 449 GLY AAA N     1 ? 1 
ATOM   3264  C CA    . GLY A 1 449 ? 12.320  -30.813 35.284  1.000 44.439  0 449 GLY AAA CA    1 ? 1 
ATOM   3265  C C     . GLY A 1 449 ? 13.303  -29.650 35.174  1.000 43.207  0 449 GLY AAA C     1 ? 1 
ATOM   3266  O O     . GLY A 1 449 ? 13.927  -29.518 34.113  1.000 43.044  0 449 GLY AAA O     1 ? 1 
ATOM   3267  N N     . GLU A 1 450 ? 13.394  -28.836 36.232  1.000 42.369  0 450 GLU AAA N     1 ? 1 
ATOM   3268  C CA    . GLU A 1 450 ? 14.232  -27.611 36.339  1.000 40.188  0 450 GLU AAA CA    1 ? 1 
ATOM   3269  C C     . GLU A 1 450 ? 13.891  -26.627 35.204  1.000 38.069  0 450 GLU AAA C     1 ? 1 
ATOM   3270  O O     . GLU A 1 450 ? 14.820  -26.151 34.555  1.000 33.841  0 450 GLU AAA O     1 ? 1 
ATOM   3271  C CB    . GLU A 1 450 ? 15.705  -27.991 36.388  1.000 40.477  0 450 GLU AAA CB    1 ? 1 
ATOM   3272  C CG    . GLU A 1 450 ? 16.090  -28.731 37.651  1.000 42.448  0 450 GLU AAA CG    1 ? 1 
ATOM   3273  C CD    . GLU A 1 450 ? 17.588  -28.722 37.954  1.000 43.735  0 450 GLU AAA CD    1 ? 1 
ATOM   3274  O OE1   . GLU A 1 450 ? 18.379  -29.134 37.096  1.000 45.678  0 450 GLU AAA OE1   1 ? 1 
ATOM   3275  O OE2   . GLU A 1 450 ? 17.967  -28.313 39.037  1.000 45.993  0 450 GLU AAA OE2   1 ? 1 
ATOM   3276  N N     . LYS A 1 451 ? 12.597  -26.292 35.005  1.000 37.864  0 451 LYS AAA N     1 ? 1 
ATOM   3277  C CA    . LYS A 1 451 ? 12.212  -25.258 34.000  1.000 36.453  0 451 LYS AAA CA    1 ? 1 
ATOM   3278  C C     . LYS A 1 451 ? 12.811  -23.911 34.425  1.000 33.197  0 451 LYS AAA C     1 ? 1 
ATOM   3279  O O     . LYS A 1 451 ? 12.759  -23.609 35.625  1.000 29.639  0 451 LYS AAA O     1 ? 1 
ATOM   3280  C CB    . LYS A 1 451 ? 10.701  -25.113 33.841  1.000 39.761  0 451 LYS AAA CB    1 ? 1 
ATOM   3281  C CG    . LYS A 1 451 ? 10.253  -24.243 32.670  1.000 42.051  0 451 LYS AAA CG    1 ? 1 
ATOM   3282  C CD    . LYS A 1 451 ? 8.786   -23.872 32.759  1.000 45.540  0 451 LYS AAA CD    1 ? 1 
ATOM   3283  C CE    . LYS A 1 451 ? 8.159   -23.528 31.428  1.000 46.424  0 451 LYS AAA CE    1 ? 1 
ATOM   3284  N NZ    . LYS A 1 451 ? 6.960   -22.688 31.679  1.000 47.195  0 451 LYS AAA NZ    1 ? 1 
ATOM   3285  N N     . VAL A 1 452 ? 13.358  -23.132 33.482  1.000 31.484  0 452 VAL AAA N     1 ? 1 
ATOM   3286  C CA    . VAL A 1 452 ? 13.907  -21.778 33.806  1.000 30.353  0 452 VAL AAA CA    1 ? 1 
ATOM   3287  C C     . VAL A 1 452 ? 12.732  -20.786 33.880  1.000 28.938  0 452 VAL AAA C     1 ? 1 
ATOM   3288  O O     . VAL A 1 452 ? 12.012  -20.648 32.902  1.000 26.416  0 452 VAL AAA O     1 ? 1 
ATOM   3289  C CB    . VAL A 1 452 ? 14.976  -21.339 32.802  1.000 29.273  0 452 VAL AAA CB    1 ? 1 
ATOM   3290  C CG1   . VAL A 1 452 ? 15.545  -19.978 33.133  1.000 28.858  0 452 VAL AAA CG1   1 ? 1 
ATOM   3291  C CG2   . VAL A 1 452 ? 16.074  -22.349 32.720  1.000 30.791  0 452 VAL AAA CG2   1 ? 1 
ATOM   3292  N N     . VAL A 1 453 ? 12.531  -20.174 35.039  1.000 29.346  0 453 VAL AAA N     1 ? 1 
ATOM   3293  C CA    . VAL A 1 453 ? 11.429  -19.196 35.262  1.000 30.831  0 453 VAL AAA CA    1 ? 1 
ATOM   3294  C C     . VAL A 1 453 ? 12.049  -17.821 35.518  1.000 29.221  0 453 VAL AAA C     1 ? 1 
ATOM   3295  O O     . VAL A 1 453 ? 11.294  -16.834 35.464  1.000 30.226  0 453 VAL AAA O     1 ? 1 
ATOM   3296  C CB    . VAL A 1 453 ? 10.483  -19.620 36.416  1.000 32.479  0 453 VAL AAA CB    1 ? 1 
ATOM   3297  C CG1   . VAL A 1 453 ? 9.713   -20.899 36.090  1.000 32.409  0 453 VAL AAA CG1   1 ? 1 
ATOM   3298  C CG2   . VAL A 1 453 ? 11.238  -19.756 37.745  1.000 32.994  0 453 VAL AAA CG2   1 ? 1 
ATOM   3299  N N     . GLY A 1 454 ? 13.358  -17.761 35.772  1.000 27.947  0 454 GLY AAA N     1 ? 1 
ATOM   3300  C CA    . GLY A 1 454 ? 14.098  -16.499 35.988  1.000 26.250  0 454 GLY AAA CA    1 ? 1 
ATOM   3301  C C     . GLY A 1 454 ? 15.499  -16.584 35.412  1.000 25.567  0 454 GLY AAA C     1 ? 1 
ATOM   3302  O O     . GLY A 1 454 ? 16.212  -17.569 35.710  1.000 25.202  0 454 GLY AAA O     1 ? 1 
ATOM   3303  N N     . PHE A 1 455 ? 15.840  -15.621 34.546  1.000 23.991  0 455 PHE AAA N     1 ? 1 
ATOM   3304  C CA    . PHE A 1 455 ? 17.164  -15.435 33.923  1.000 22.975  0 455 PHE AAA CA    1 ? 1 
ATOM   3305  C C     . PHE A 1 455 ? 17.689  -14.043 34.282  1.000 22.311  0 455 PHE AAA C     1 ? 1 
ATOM   3306  O O     . PHE A 1 455 ? 16.947  -13.069 34.092  1.000 22.211  0 455 PHE AAA O     1 ? 1 
ATOM   3307  C CB    . PHE A 1 455 ? 17.078  -15.664 32.418  1.000 22.685  0 455 PHE AAA CB    1 ? 1 
ATOM   3308  C CG    . PHE A 1 455 ? 18.327  -15.260 31.680  1.000 22.603  0 455 PHE AAA CG    1 ? 1 
ATOM   3309  C CD1   . PHE A 1 455 ? 18.623  -13.928 31.464  1.000 22.500  0 455 PHE AAA CD1   1 ? 1 
ATOM   3310  C CD2   . PHE A 1 455 ? 19.172  -16.207 31.160  1.000 23.339  0 455 PHE AAA CD2   1 ? 1 
ATOM   3311  C CE1   . PHE A 1 455 ? 19.765  -13.534 30.797  1.000 21.935  0 455 PHE AAA CE1   1 ? 1 
ATOM   3312  C CE2   . PHE A 1 455 ? 20.314  -15.822 30.478  1.000 23.623  0 455 PHE AAA CE2   1 ? 1 
ATOM   3313  C CZ    . PHE A 1 455 ? 20.604  -14.485 30.296  1.000 22.943  0 455 PHE AAA CZ    1 ? 1 
ATOM   3314  N N     . HIS A 1 456 ? 18.957  -13.953 34.740  1.000 21.191  0 456 HIS AAA N     1 ? 1 
ATOM   3315  C CA    . HIS A 1 456 ? 19.554  -12.724 35.316  1.000 19.692  0 456 HIS AAA CA    1 ? 1 
ATOM   3316  C C     . HIS A 1 456 ? 21.002  -12.626 34.894  1.000 19.302  0 456 HIS AAA C     1 ? 1 
ATOM   3317  O O     . HIS A 1 456 ? 21.738  -13.600 35.114  1.000 20.470  0 456 HIS AAA O     1 ? 1 
ATOM   3318  C CB    . HIS A 1 456 ? 19.466  -12.788 36.841  1.000 20.111  0 456 HIS AAA CB    1 ? 1 
ATOM   3319  C CG    . HIS A 1 456 ? 18.074  -12.829 37.344  1.000 20.232  0 456 HIS AAA CG    1 ? 1 
ATOM   3320  N ND1   . HIS A 1 456 ? 17.363  -11.686 37.615  1.000 20.662  0 456 HIS AAA ND1   1 ? 1 
ATOM   3321  C CD2   . HIS A 1 456 ? 17.230  -13.855 37.523  1.000 20.899  0 456 HIS AAA CD2   1 ? 1 
ATOM   3322  C CE1   . HIS A 1 456 ? 16.126  -12.000 37.961  1.000 20.956  0 456 HIS AAA CE1   1 ? 1 
ATOM   3323  N NE2   . HIS A 1 456 ? 16.020  -13.327 37.904  1.000 21.530  0 456 HIS AAA NE2   1 ? 1 
ATOM   3324  N N     . PHE A 1 457 ? 21.435  -11.489 34.362  1.000 18.032  0 457 PHE AAA N     1 ? 1 
ATOM   3325  C CA    . PHE A 1 457 ? 22.853  -11.341 33.972  1.000 17.765  0 457 PHE AAA CA    1 ? 1 
ATOM   3326  C C     . PHE A 1 457 ? 23.296  -9.929  34.276  1.000 18.437  0 457 PHE AAA C     1 ? 1 
ATOM   3327  O O     . PHE A 1 457 ? 22.691  -8.987  33.739  1.000 20.313  0 457 PHE AAA O     1 ? 1 
ATOM   3328  C CB    . PHE A 1 457 ? 23.103  -11.664 32.503  1.000 17.254  0 457 PHE AAA CB    1 ? 1 
ATOM   3329  C CG    . PHE A 1 457 ? 24.548  -11.471 32.131  1.000 16.498  0 457 PHE AAA CG    1 ? 1 
ATOM   3330  C CD1   . PHE A 1 457 ? 25.475  -12.452 32.440  1.000 16.423  0 457 PHE AAA CD1   1 ? 1 
ATOM   3331  C CD2   . PHE A 1 457 ? 24.998  -10.290 31.558  1.000 15.649  0 457 PHE AAA CD2   1 ? 1 
ATOM   3332  C CE1   . PHE A 1 457 ? 26.816  -12.263 32.165  1.000 15.919  0 457 PHE AAA CE1   1 ? 1 
ATOM   3333  C CE2   . PHE A 1 457 ? 26.342  -10.117 31.278  1.000 15.458  0 457 PHE AAA CE2   1 ? 1 
ATOM   3334  C CZ    . PHE A 1 457 ? 27.245  -11.096 31.580  1.000 15.513  0 457 PHE AAA CZ    1 ? 1 
ATOM   3335  N N     . VAL A 1 458 ? 24.276  -9.811  35.172  1.000 19.072  0 458 VAL AAA N     1 ? 1 
ATOM   3336  C CA    . VAL A 1 458 ? 24.981  -8.551  35.478  1.000 19.209  0 458 VAL AAA CA    1 ? 1 
ATOM   3337  C C     . VAL A 1 458 ? 26.313  -8.619  34.752  1.000 18.862  0 458 VAL AAA C     1 ? 1 
ATOM   3338  O O     . VAL A 1 458 ? 26.986  -9.657  34.887  1.000 19.260  0 458 VAL AAA O     1 ? 1 
ATOM   3339  C CB    . VAL A 1 458 ? 25.174  -8.388  36.994  1.000 20.093  0 458 VAL AAA CB    1 ? 1 
ATOM   3340  C CG1   . VAL A 1 458 ? 25.951  -7.120  37.338  1.000 20.031  0 458 VAL AAA CG1   1 ? 1 
ATOM   3341  C CG2   . VAL A 1 458 ? 23.831  -8.374  37.704  1.000 20.838  0 458 VAL AAA CG2   1 ? 1 
ATOM   3342  N N     . GLY A 1 459 ? 26.676  -7.557  34.045  1.000 18.960  0 459 GLY AAA N     1 ? 1 
ATOM   3343  C CA    . GLY A 1 459 ? 27.962  -7.437  33.326  1.000 19.556  0 459 GLY AAA CA    1 ? 1 
ATOM   3344  C C     . GLY A 1 459 ? 27.827  -6.645  32.034  1.000 19.925  0 459 GLY AAA C     1 ? 1 
ATOM   3345  O O     . GLY A 1 459 ? 26.797  -6.018  31.799  1.000 21.051  0 459 GLY AAA O     1 ? 1 
ATOM   3346  N N     . PRO A 1 460 ? 28.858  -6.624  31.172  1.000 20.120  0 460 PRO AAA N     1 ? 1 
ATOM   3347  C CA    . PRO A 1 460 ? 28.810  -5.865  29.929  1.000 20.323  0 460 PRO AAA CA    1 ? 1 
ATOM   3348  C C     . PRO A 1 460 ? 27.759  -6.360  28.939  1.000 19.146  0 460 PRO AAA C     1 ? 1 
ATOM   3349  O O     . PRO A 1 460 ? 27.514  -7.484  28.921  1.000 18.960  0 460 PRO AAA O     1 ? 1 
ATOM   3350  C CB    . PRO A 1 460 ? 30.224  -5.995  29.311  1.000 20.531  0 460 PRO AAA CB    1 ? 1 
ATOM   3351  C CG    . PRO A 1 460 ? 31.075  -6.450  30.485  1.000 21.338  0 460 PRO AAA CG    1 ? 1 
ATOM   3352  C CD    . PRO A 1 460 ? 30.148  -7.298  31.347  1.000 20.812  0 460 PRO AAA CD    1 ? 1 
ATOM   3353  N N     . ASN A 1 461 ? 27.210  -5.460  28.140  1.000 18.949  0 461 ASN AAA N     1 ? 1 
ATOM   3354  C CA    . ASN A 1 461 ? 26.312  -5.831  27.019  1.000 19.598  0 461 ASN AAA CA    1 ? 1 
ATOM   3355  C C     . ASN A 1 461 ? 25.190  -6.759  27.536  1.000 19.110  0 461 ASN AAA C     1 ? 1 
ATOM   3356  O O     . ASN A 1 461 ? 24.902  -7.825  26.898  1.000 18.829  0 461 ASN AAA O     1 ? 1 
ATOM   3357  C CB    . ASN A 1 461 ? 27.141  -6.491  25.930  1.000 19.802  0 461 ASN AAA CB    1 ? 1 
ATOM   3358  C CG    . ASN A 1 461 ? 28.449  -5.766  25.696  1.000 20.595  0 461 ASN AAA CG    1 ? 1 
ATOM   3359  O OD1   . ASN A 1 461 ? 28.446  -4.548  25.405  1.000 20.644  0 461 ASN AAA OD1   1 ? 1 
ATOM   3360  N ND2   . ASN A 1 461 ? 29.547  -6.506  25.863  1.000 19.456  0 461 ASN AAA ND2   1 ? 1 
ATOM   3361  N N     . ALA A 1 462 ? 24.591  -6.428  28.664  1.000 18.341  0 462 ALA AAA N     1 ? 1 
ATOM   3362  C CA    . ALA A 1 462 ? 23.654  -7.354  29.335  1.000 19.063  0 462 ALA AAA CA    1 ? 1 
ATOM   3363  C C     . ALA A 1 462 ? 22.353  -7.441  28.533  1.000 18.920  0 462 ALA AAA C     1 ? 1 
ATOM   3364  O O     . ALA A 1 462 ? 21.726  -8.494  28.542  1.000 18.060  0 462 ALA AAA O     1 ? 1 
ATOM   3365  C CB    . ALA A 1 462 ? 23.409  -6.930  30.765  1.000 19.369  0 462 ALA AAA CB    1 ? 1 
ATOM   3366  N N     . GLY A 1 463 ? 21.909  -6.349  27.946  1.000 20.188  0 463 GLY AAA N     1 ? 1 
ATOM   3367  C CA    . GLY A 1 463 ? 20.739  -6.350  27.041  1.000 22.227  0 463 GLY AAA CA    1 ? 1 
ATOM   3368  C C     . GLY A 1 463 ? 21.002  -7.198  25.799  1.000 23.732  0 463 GLY AAA C     1 ? 1 
ATOM   3369  O O     . GLY A 1 463 ? 20.153  -7.989  25.427  1.000 24.500  0 463 GLY AAA O     1 ? 1 
ATOM   3370  N N     . GLU A 1 464 ? 22.184  -7.067  25.200  1.000 25.732  0 464 GLU AAA N     1 ? 1 
ATOM   3371  C CA    . GLU A 1 464 ? 22.579  -7.879  24.027  1.000 26.570  0 464 GLU AAA CA    1 ? 1 
ATOM   3372  C C     . GLU A 1 464 ? 22.523  -9.362  24.426  1.000 24.847  0 464 GLU AAA C     1 ? 1 
ATOM   3373  O O     . GLU A 1 464 ? 22.075  -10.188 23.596  1.000 26.847  0 464 GLU AAA O     1 ? 1 
ATOM   3374  C CB    . GLU A 1 464 ? 23.958  -7.446  23.488  1.000 29.025  0 464 GLU AAA CB    1 ? 1 
ATOM   3375  C CG    . GLU A 1 464 ? 24.082  -5.953  23.114  1.000 31.120  0 464 GLU AAA CG    1 ? 1 
ATOM   3376  C CD    . GLU A 1 464 ? 23.207  -5.404  21.980  1.000 33.413  0 464 GLU AAA CD    1 ? 1 
ATOM   3377  O OE1   . GLU A 1 464 ? 22.515  -6.193  21.309  1.000 36.379  0 464 GLU AAA OE1   1 ? 1 
ATOM   3378  O OE2   . GLU A 1 464 ? 23.274  -4.181  21.690  1.000 34.449  0 464 GLU AAA OE2   1 ? 1 
ATOM   3379  N N     . ILE A 1 465 ? 22.901  -9.711  25.648  1.000 22.615  0 465 ILE AAA N     1 ? 1 
ATOM   3380  C CA    . ILE A 1 465 ? 22.988  -11.123 26.103  1.000 21.764  0 465 ILE AAA CA    1 ? 1 
ATOM   3381  C C     . ILE A 1 465 ? 21.578  -11.622 26.407  1.000 23.407  0 465 ILE AAA C     1 ? 1 
ATOM   3382  O O     . ILE A 1 465 ? 21.246  -12.777 26.060  1.000 23.600  0 465 ILE AAA O     1 ? 1 
ATOM   3383  C CB    . ILE A 1 465 ? 23.951  -11.265 27.296  1.000 21.680  0 465 ILE AAA CB    1 ? 1 
ATOM   3384  C CG1   . ILE A 1 465 ? 25.396  -11.098 26.806  1.000 21.389  0 465 ILE AAA CG1   1 ? 1 
ATOM   3385  C CG2   . ILE A 1 465 ? 23.766  -12.616 27.954  1.000 22.227  0 465 ILE AAA CG2   1 ? 1 
ATOM   3386  C CD1   . ILE A 1 465 ? 26.424  -10.917 27.878  1.000 21.425  0 465 ILE AAA CD1   1 ? 1 
ATOM   3387  N N     . THR A 1 466 ? 20.717  -10.759 26.933  1.000 23.384  0 466 THR AAA N     1 ? 1 
ATOM   3388  C CA    . THR A 1 466 ? 19.459  -11.216 27.539  1.000 23.182  0 466 THR AAA CA    1 ? 1 
ATOM   3389  C C     . THR A 1 466 ? 18.408  -11.423 26.473  1.000 22.790  0 466 THR AAA C     1 ? 1 
ATOM   3390  O O     . THR A 1 466 ? 17.500  -12.229 26.712  1.000 22.470  0 466 THR AAA O     1 ? 1 
ATOM   3391  C CB    . THR A 1 466 ? 18.955  -10.219 28.588  1.000 23.107  0 466 THR AAA CB    1 ? 1 
ATOM   3392  O OG1   . THR A 1 466 ? 19.877  -10.267 29.673  1.000 23.003  0 466 THR AAA OG1   1 ? 1 
ATOM   3393  C CG2   . THR A 1 466 ? 17.557  -10.529 29.062  1.000 22.112  0 466 THR AAA CG2   1 ? 1 
ATOM   3394  N N     . GLN A 1 467 ? 18.456  -10.649 25.398  1.000 23.163  0 467 GLN AAA N     1 ? 1 
ATOM   3395  C CA    . GLN A 1 467 ? 17.381  -10.657 24.376  1.000 22.224  0 467 GLN AAA CA    1 ? 1 
ATOM   3396  C C     . GLN A 1 467 ? 17.126  -12.091 23.966  1.000 22.177  0 467 GLN AAA C     1 ? 1 
ATOM   3397  O O     . GLN A 1 467 ? 15.975  -12.561 24.124  1.000 24.773  0 467 GLN AAA O     1 ? 1 
ATOM   3398  C CB    . GLN A 1 467 ? 17.769  -9.835  23.155  1.000 23.415  0 467 GLN AAA CB    1 ? 1 
ATOM   3399  C CG    . GLN A 1 467 ? 16.647  -9.643  22.163  1.000 23.161  0 467 GLN AAA CG    1 ? 1 
ATOM   3400  C CD    . GLN A 1 467 ? 15.489  -8.854  22.728  1.000 23.981  0 467 GLN AAA CD    1 ? 1 
ATOM   3401  O OE1   . GLN A 1 467 ? 15.504  -7.631  22.751  1.000 24.287  0 467 GLN AAA OE1   1 ? 1 
ATOM   3402  N NE2   . GLN A 1 467 ? 14.458  -9.557  23.179  1.000 24.080  0 467 GLN AAA NE2   1 ? 1 
ATOM   3403  N N     . GLY A 1 468 ? 18.155  -12.794 23.505  1.000 20.710  0 468 GLY AAA N     1 ? 1 
ATOM   3404  C CA    . GLY A 1 468 ? 18.027  -14.160 22.995  1.000 20.381  0 468 GLY AAA CA    1 ? 1 
ATOM   3405  C C     . GLY A 1 468 ? 17.545  -15.140 24.041  1.000 19.988  0 468 GLY AAA C     1 ? 1 
ATOM   3406  O O     . GLY A 1 468 ? 16.691  -15.995 23.767  1.000 20.068  0 468 GLY AAA O     1 ? 1 
ATOM   3407  N N     . PHE A 1 469 ? 18.150  -15.080 25.199  1.000 19.599  0 469 PHE AAA N     1 ? 1 
ATOM   3408  C CA    . PHE A 1 469 ? 17.852  -15.970 26.334  1.000 19.641  0 469 PHE AAA CA    1 ? 1 
ATOM   3409  C C     . PHE A 1 469 ? 16.416  -15.743 26.744  1.000 20.636  0 469 PHE AAA C     1 ? 1 
ATOM   3410  O O     . PHE A 1 469 ? 15.733  -16.743 27.016  1.000 22.592  0 469 PHE AAA O     1 ? 1 
ATOM   3411  C CB    . PHE A 1 469 ? 18.853  -15.725 27.449  1.000 19.536  0 469 PHE AAA CB    1 ? 1 
ATOM   3412  C CG    . PHE A 1 469 ? 20.152  -16.471 27.229  1.000 19.749  0 469 PHE AAA CG    1 ? 1 
ATOM   3413  C CD1   . PHE A 1 469 ? 20.162  -17.841 27.141  1.000 20.009  0 469 PHE AAA CD1   1 ? 1 
ATOM   3414  C CD2   . PHE A 1 469 ? 21.352  -15.797 27.132  1.000 19.848  0 469 PHE AAA CD2   1 ? 1 
ATOM   3415  C CE1   . PHE A 1 469 ? 21.352  -18.514 26.956  1.000 20.981  0 469 PHE AAA CE1   1 ? 1 
ATOM   3416  C CE2   . PHE A 1 469 ? 22.547  -16.471 26.947  1.000 19.992  0 469 PHE AAA CE2   1 ? 1 
ATOM   3417  C CZ    . PHE A 1 469 ? 22.545  -17.834 26.879  1.000 20.380  0 469 PHE AAA CZ    1 ? 1 
ATOM   3418  N N     . SER A 1 470 ? 15.945  -14.497 26.719  1.000 20.439  0 470 SER AAA N     1 ? 1 
ATOM   3419  C CA    . SER A 1 470 ? 14.532  -14.182 27.050  1.000 21.662  0 470 SER AAA CA    1 ? 1 
ATOM   3420  C C     . SER A 1 470 ? 13.587  -14.983 26.150  1.000 23.240  0 470 SER AAA C     1 ? 1 
ATOM   3421  O O     . SER A 1 470 ? 12.629  -15.541 26.670  1.000 23.711  0 470 SER AAA O     1 ? 1 
ATOM   3422  C CB    . SER A 1 470 ? 14.241  -12.698 27.007  1.000 21.430  0 470 SER AAA CB    1 ? 1 
ATOM   3423  O OG    . SER A 1 470 ? 14.084  -12.221 25.674  1.000 21.193  0 470 SER AAA OG    1 ? 1 
ATOM   3424  N N     . LEU A 1 471 ? 13.849  -15.028 24.841  1.000 25.225  0 471 LEU AAA N     1 ? 1 
ATOM   3425  C CA    . LEU A 1 471 ? 13.055  -15.821 23.889  1.000 26.253  0 471 LEU AAA CA    1 ? 1 
ATOM   3426  C C     . LEU A 1 471 ? 13.119  -17.298 24.266  1.000 28.288  0 471 LEU AAA C     1 ? 1 
ATOM   3427  O O     . LEU A 1 471 ? 12.037  -17.938 24.257  1.000 28.543  0 471 LEU AAA O     1 ? 1 
ATOM   3428  C CB    . LEU A 1 471 ? 13.580  -15.619 22.471  1.000 26.233  0 471 LEU AAA CB    1 ? 1 
ATOM   3429  C CG    . LEU A 1 471 ? 12.885  -16.459 21.405  1.000 26.553  0 471 LEU AAA CG    1 ? 1 
ATOM   3430  C CD1   . LEU A 1 471 ? 11.393  -16.208 21.459  1.000 27.190  0 471 LEU AAA CD1   1 ? 1 
ATOM   3431  C CD2   . LEU A 1 471 ? 13.453  -16.116 20.045  1.000 26.686  0 471 LEU AAA CD2   1 ? 1 
ATOM   3432  N N     . ALA A 1 472 ? 14.330  -17.830 24.497  1.000 28.492  0 472 ALA AAA N     1 ? 1 
ATOM   3433  C CA    . ALA A 1 472 ? 14.533  -19.252 24.868  1.000 29.001  0 472 ALA AAA CA    1 ? 1 
ATOM   3434  C C     . ALA A 1 472 ? 13.727  -19.537 26.142  1.000 29.108  0 472 ALA AAA C     1 ? 1 
ATOM   3435  O O     . ALA A 1 472 ? 13.101  -20.608 26.240  1.000 28.667  0 472 ALA AAA O     1 ? 1 
ATOM   3436  C CB    . ALA A 1 472 ? 15.996  -19.571 25.089  1.000 28.072  0 472 ALA AAA CB    1 ? 1 
ATOM   3437  N N     . VAL A 1 473 ? 13.765  -18.629 27.103  1.000 28.499  0 473 VAL AAA N     1 ? 1 
ATOM   3438  C CA    . VAL A 1 473 ? 13.092  -18.891 28.404  1.000 30.204  0 473 VAL AAA CA    1 ? 1 
ATOM   3439  C C     . VAL A 1 473 ? 11.573  -18.892 28.146  1.000 30.830  0 473 VAL AAA C     1 ? 1 
ATOM   3440  O O     . VAL A 1 473 ? 10.895  -19.762 28.692  1.000 30.347  0 473 VAL AAA O     1 ? 1 
ATOM   3441  C CB    . VAL A 1 473 ? 13.527  -17.899 29.494  1.000 30.426  0 473 VAL AAA CB    1 ? 1 
ATOM   3442  C CG1   . VAL A 1 473 ? 12.608  -17.934 30.706  1.000 31.703  0 473 VAL AAA CG1   1 ? 1 
ATOM   3443  C CG2   . VAL A 1 473 ? 14.948  -18.142 29.929  1.000 29.444  0 473 VAL AAA CG2   1 ? 1 
ATOM   3444  N N     . LYS A 1 474 ? 11.084  -18.015 27.276  1.000 30.942  0 474 LYS AAA N     1 ? 1 
ATOM   3445  C CA    . LYS A 1 474 ? 9.646   -17.943 26.907  1.000 32.817  0 474 LYS AAA CA    1 ? 1 
ATOM   3446  C C     . LYS A 1 474 ? 9.193   -19.244 26.220  1.000 35.580  0 474 LYS AAA C     1 ? 1 
ATOM   3447  O O     . LYS A 1 474 ? 8.028   -19.686 26.468  1.000 31.610  0 474 LYS AAA O     1 ? 1 
ATOM   3448  C CB    . LYS A 1 474 ? 9.409   -16.735 26.015  1.000 34.412  0 474 LYS AAA CB    1 ? 1 
ATOM   3449  C CG    . LYS A 1 474 ? 7.956   -16.505 25.636  1.000 37.161  0 474 LYS AAA CG    1 ? 1 
ATOM   3450  C CD    . LYS A 1 474 ? 7.832   -15.303 24.722  1.000 37.009  0 474 LYS AAA CD    1 ? 1 
ATOM   3451  C CE    . LYS A 1 474 ? 6.429   -14.763 24.609  1.000 34.683  0 474 LYS AAA CE    1 ? 1 
ATOM   3452  N NZ    . LYS A 1 474 ? 6.335   -13.970 23.368  1.000 34.912  0 474 LYS AAA NZ    1 ? 1 
ATOM   3453  N N     . LEU A 1 475 ? 10.082  -19.876 25.430  1.000 36.730  0 475 LEU AAA N     1 ? 1 
ATOM   3454  C CA    . LEU A 1 475 ? 9.788   -21.142 24.693  1.000 38.502  0 475 LEU AAA CA    1 ? 1 
ATOM   3455  C C     . LEU A 1 475 ? 9.873   -22.364 25.630  1.000 37.947  0 475 LEU AAA C     1 ? 1 
ATOM   3456  O O     . LEU A 1 475 ? 9.551   -23.463 25.157  1.000 39.395  0 475 LEU AAA O     1 ? 1 
ATOM   3457  C CB    . LEU A 1 475 ? 10.746  -21.292 23.501  1.000 40.032  0 475 LEU AAA CB    1 ? 1 
ATOM   3458  C CG    . LEU A 1 475 ? 10.500  -20.351 22.318  1.000 41.198  0 475 LEU AAA CG    1 ? 1 
ATOM   3459  C CD1   . LEU A 1 475 ? 11.581  -20.530 21.245  1.000 40.506  0 475 LEU AAA CD1   1 ? 1 
ATOM   3460  C CD2   . LEU A 1 475 ? 9.106   -20.567 21.731  1.000 41.150  0 475 LEU AAA CD2   1 ? 1 
ATOM   3461  N N     . GLY A 1 476 ? 10.293  -22.192 26.890  1.000 35.958  0 476 GLY AAA N     1 ? 1 
ATOM   3462  C CA    . GLY A 1 476 ? 10.188  -23.216 27.945  1.000 34.892  0 476 GLY AAA CA    1 ? 1 
ATOM   3463  C C     . GLY A 1 476 ? 11.480  -23.948 28.196  1.000 33.909  0 476 GLY AAA C     1 ? 1 
ATOM   3464  O O     . GLY A 1 476 ? 11.382  -25.099 28.640  1.000 34.225  0 476 GLY AAA O     1 ? 1 
ATOM   3465  N N     . ALA A 1 477 ? 12.622  -23.297 27.997  1.000 32.276  0 477 ALA AAA N     1 ? 1 
ATOM   3466  C CA    . ALA A 1 477 ? 13.985  -23.848 28.188  1.000 31.666  0 477 ALA AAA CA    1 ? 1 
ATOM   3467  C C     . ALA A 1 477 ? 14.175  -24.354 29.624  1.000 30.682  0 477 ALA AAA C     1 ? 1 
ATOM   3468  O O     . ALA A 1 477 ? 13.782  -23.675 30.564  1.000 33.184  0 477 ALA AAA O     1 ? 1 
ATOM   3469  C CB    . ALA A 1 477 ? 15.019  -22.787 27.862  1.000 31.378  0 477 ALA AAA CB    1 ? 1 
ATOM   3470  N N     . THR A 1 478 ? 14.741  -25.544 29.770  1.000 29.647  0 478 THR AAA N     1 ? 1 
ATOM   3471  C CA    . THR A 1 478 ? 15.074  -26.178 31.065  1.000 30.007  0 478 THR AAA CA    1 ? 1 
ATOM   3472  C C     . THR A 1 478 ? 16.569  -26.004 31.375  1.000 29.814  0 478 THR AAA C     1 ? 1 
ATOM   3473  O O     . THR A 1 478 ? 17.357  -25.744 30.440  1.000 31.134  0 478 THR AAA O     1 ? 1 
ATOM   3474  C CB    . THR A 1 478 ? 14.724  -27.671 31.033  1.000 30.581  0 478 THR AAA CB    1 ? 1 
ATOM   3475  O OG1   . THR A 1 478 ? 15.582  -28.270 30.058  1.000 30.023  0 478 THR AAA OG1   1 ? 1 
ATOM   3476  C CG2   . THR A 1 478 ? 13.259  -27.908 30.732  1.000 30.861  0 478 THR AAA CG2   1 ? 1 
ATOM   3477  N N     . LYS A 1 479 ? 16.963  -26.240 32.615  1.000 29.539  0 479 LYS AAA N     1 ? 1 
ATOM   3478  C CA    . LYS A 1 479 ? 18.391  -26.303 32.991  1.000 30.471  0 479 LYS AAA CA    1 ? 1 
ATOM   3479  C C     . LYS A 1 479 ? 19.153  -27.273 32.062  1.000 31.168  0 479 LYS AAA C     1 ? 1 
ATOM   3480  O O     . LYS A 1 479 ? 20.285  -26.959 31.713  1.000 31.205  0 479 LYS AAA O     1 ? 1 
ATOM   3481  C CB    . LYS A 1 479 ? 18.575  -26.656 34.469  1.000 30.288  0 479 LYS AAA CB    1 ? 1 
ATOM   3482  C CG    . LYS A 1 479 ? 20.024  -26.619 34.931  1.000 30.548  0 479 LYS AAA CG    1 ? 1 
ATOM   3483  C CD    . LYS A 1 479 ? 20.737  -25.353 34.546  1.000 30.909  0 479 LYS AAA CD    1 ? 1 
ATOM   3484  C CE    . LYS A 1 479 ? 21.990  -25.078 35.360  1.000 31.355  0 479 LYS AAA CE    1 ? 1 
ATOM   3485  N NZ    . LYS A 1 479 ? 22.962  -26.188 35.227  1.000 32.322  0 479 LYS AAA NZ    1 ? 1 
ATOM   3486  N N     . LYS A 1 480 ? 18.544  -28.377 31.645  1.000 32.927  0 480 LYS AAA N     1 ? 1 
ATOM   3487  C CA    . LYS A 1 480 ? 19.181  -29.409 30.777  1.000 35.023  0 480 LYS AAA CA    1 ? 1 
ATOM   3488  C C     . LYS A 1 480 ? 19.493  -28.745 29.424  1.000 34.576  0 480 LYS AAA C     1 ? 1 
ATOM   3489  O O     . LYS A 1 480 ? 20.623  -28.911 28.927  1.000 30.687  0 480 LYS AAA O     1 ? 1 
ATOM   3490  C CB    . LYS A 1 480 ? 18.300  -30.661 30.658  1.000 35.686  0 480 LYS AAA CB    1 ? 1 
ATOM   3491  C CG    . LYS A 1 480 ? 18.745  -31.671 29.619  1.000 37.700  0 480 LYS AAA CG    1 ? 1 
ATOM   3492  C CD    . LYS A 1 480 ? 18.144  -33.059 29.832  1.000 39.930  0 480 LYS AAA CD    1 ? 1 
ATOM   3493  C CE    . LYS A 1 480 ? 18.445  -34.044 28.703  1.000 43.450  0 480 LYS AAA CE    1 ? 1 
ATOM   3494  N NZ    . LYS A 1 480 ? 19.876  -34.018 28.238  1.000 43.922  0 480 LYS AAA NZ    1 ? 1 
ATOM   3495  N N     . ASP A 1 481 ? 18.525  -27.998 28.880  1.000 33.567  0 481 ASP AAA N     1 ? 1 
ATOM   3496  C CA    . ASP A 1 481 ? 18.659  -27.271 27.601  1.000 33.395  0 481 ASP AAA CA    1 ? 1 
ATOM   3497  C C     . ASP A 1 481 ? 19.879  -26.343 27.681  1.000 33.865  0 481 ASP AAA C     1 ? 1 
ATOM   3498  O O     . ASP A 1 481 ? 20.636  -26.265 26.687  1.000 32.256  0 481 ASP AAA O     1 ? 1 
ATOM   3499  C CB    . ASP A 1 481 ? 17.397  -26.474 27.277  1.000 33.599  0 481 ASP AAA CB    1 ? 1 
ATOM   3500  C CG    . ASP A 1 481 ? 16.192  -27.370 27.004  1.000 34.965  0 481 ASP AAA CG    1 ? 1 
ATOM   3501  O OD1   . ASP A 1 481 ? 16.400  -28.546 26.521  1.000 34.762  0 481 ASP AAA OD1   1 ? 1 
ATOM   3502  O OD2   . ASP A 1 481 ? 15.056  -26.932 27.321  1.000 35.065  0 481 ASP AAA OD2   1 ? 1 
ATOM   3503  N N     . PHE A 1 482 ? 20.042  -25.657 28.813  1.000 32.622  0 482 PHE AAA N     1 ? 1 
ATOM   3504  C CA    . PHE A 1 482 ? 21.145  -24.708 29.062  1.000 32.407  0 482 PHE AAA CA    1 ? 1 
ATOM   3505  C C     . PHE A 1 482 ? 22.479  -25.478 29.106  1.000 32.802  0 482 PHE AAA C     1 ? 1 
ATOM   3506  O O     . PHE A 1 482 ? 23.439  -25.004 28.501  1.000 32.476  0 482 PHE AAA O     1 ? 1 
ATOM   3507  C CB    . PHE A 1 482 ? 20.870  -23.907 30.341  1.000 32.334  0 482 PHE AAA CB    1 ? 1 
ATOM   3508  C CG    . PHE A 1 482 ? 20.054  -22.657 30.148  1.000 31.327  0 482 PHE AAA CG    1 ? 1 
ATOM   3509  C CD1   . PHE A 1 482 ? 18.680  -22.706 30.032  1.000 31.731  0 482 PHE AAA CD1   1 ? 1 
ATOM   3510  C CD2   . PHE A 1 482 ? 20.669  -21.421 30.063  1.000 32.341  0 482 PHE AAA CD2   1 ? 1 
ATOM   3511  C CE1   . PHE A 1 482 ? 17.937  -21.552 29.826  1.000 32.111  0 482 PHE AAA CE1   1 ? 1 
ATOM   3512  C CE2   . PHE A 1 482 ? 19.941  -20.263 29.847  1.000 31.581  0 482 PHE AAA CE2   1 ? 1 
ATOM   3513  C CZ    . PHE A 1 482 ? 18.566  -20.328 29.748  1.000 32.681  0 482 PHE AAA CZ    1 ? 1 
ATOM   3514  N N     . ASP A 1 483 ? 22.537  -26.632 29.766  1.000 31.651  0 483 ASP AAA N     1 ? 1 
ATOM   3515  C CA    . ASP A 1 483 ? 23.769  -27.425 29.923  1.000 32.178  0 483 ASP AAA CA    1 ? 1 
ATOM   3516  C C     . ASP A 1 483 ? 24.188  -28.038 28.590  1.000 33.115  0 483 ASP AAA C     1 ? 1 
ATOM   3517  O O     . ASP A 1 483 ? 25.405  -28.249 28.403  1.000 36.321  0 483 ASP AAA O     1 ? 1 
ATOM   3518  C CB    . ASP A 1 483 ? 23.620  -28.555 30.937  1.000 34.225  0 483 ASP AAA CB    1 ? 1 
ATOM   3519  C CG    . ASP A 1 483 ? 23.463  -28.094 32.370  1.000 35.426  0 483 ASP AAA CG    1 ? 1 
ATOM   3520  O OD1   . ASP A 1 483 ? 23.771  -26.918 32.652  1.000 35.858  0 483 ASP AAA OD1   1 ? 1 
ATOM   3521  O OD2   . ASP A 1 483 ? 23.009  -28.919 33.195  1.000 39.400  0 483 ASP AAA OD2   1 ? 1 
ATOM   3522  N N     . ASP A 1 484 ? 23.244  -28.377 27.715  1.000 34.246  0 484 ASP AAA N     1 ? 1 
ATOM   3523  C CA    . ASP A 1 484 ? 23.529  -29.068 26.428  1.000 32.664  0 484 ASP AAA CA    1 ? 1 
ATOM   3524  C C     . ASP A 1 484 ? 23.729  -28.027 25.318  1.000 30.133  0 484 ASP AAA C     1 ? 1 
ATOM   3525  O O     . ASP A 1 484 ? 24.003  -28.454 24.204  1.000 29.083  0 484 ASP AAA O     1 ? 1 
ATOM   3526  C CB    . ASP A 1 484 ? 22.440  -30.079 26.062  1.000 34.055  0 484 ASP AAA CB    1 ? 1 
ATOM   3527  C CG    . ASP A 1 484 ? 22.204  -31.201 27.068  1.000 35.770  0 484 ASP AAA CG    1 ? 1 
ATOM   3528  O OD1   . ASP A 1 484 ? 22.926  -31.284 28.063  1.000 37.973  0 484 ASP AAA OD1   1 ? 1 
ATOM   3529  O OD2   . ASP A 1 484 ? 21.249  -31.979 26.868  1.000 37.595  0 484 ASP AAA OD2   1 ? 1 
ATOM   3530  N N     . MET A 1 485 ? 23.571  -26.732 25.621  1.000 28.621  0 485 MET AAA N     1 ? 1 
ATOM   3531  C CA    . MET A 1 485 ? 23.839  -25.586 24.702  1.000 28.716  0 485 MET AAA CA    1 ? 1 
ATOM   3532  C C     . MET A 1 485 ? 25.357  -25.473 24.443  1.000 27.865  0 485 MET AAA C     1 ? 1 
ATOM   3533  O O     . MET A 1 485 ? 26.159  -25.375 25.442  1.000 27.009  0 485 MET AAA O     1 ? 1 
ATOM   3534  C CB    . MET A 1 485 ? 23.334  -24.272 25.311  1.000 28.372  0 485 MET AAA CB    1 ? 1 
ATOM   3535  C CG    . MET A 1 485 ? 23.843  -23.014 24.628  1.000 28.951  0 485 MET AAA CG    1 ? 1 
ATOM   3536  S SD    . MET A 1 485 ? 23.120  -21.555 25.386  1.000 29.444  0 485 MET AAA SD    1 ? 1 
ATOM   3537  C CE    . MET A 1 485 ? 23.835  -21.644 27.026  1.000 30.127  0 485 MET AAA CE    1 ? 1 
ATOM   3538  N N     . ILE A 1 486 ? 25.749  -25.486 23.173  1.000 26.781  0 486 ILE AAA N     1 ? 1 
ATOM   3539  C CA    . ILE A 1 486 ? 27.171  -25.268 22.808  1.000 26.607  0 486 ILE AAA CA    1 ? 1 
ATOM   3540  C C     . ILE A 1 486 ? 27.503  -23.793 22.979  1.000 26.061  0 486 ILE AAA C     1 ? 1 
ATOM   3541  O O     . ILE A 1 486 ? 26.696  -22.913 22.481  1.000 24.708  0 486 ILE AAA O     1 ? 1 
ATOM   3542  C CB    . ILE A 1 486 ? 27.518  -25.758 21.393  1.000 26.672  0 486 ILE AAA CB    1 ? 1 
ATOM   3543  C CG1   . ILE A 1 486 ? 27.082  -27.213 21.163  1.000 27.034  0 486 ILE AAA CG1   1 ? 1 
ATOM   3544  C CG2   . ILE A 1 486 ? 29.028  -25.572 21.160  1.000 26.139  0 486 ILE AAA CG2   1 ? 1 
ATOM   3545  C CD1   . ILE A 1 486 ? 27.943  -28.239 21.870  1.000 27.327  0 486 ILE AAA CD1   1 ? 1 
ATOM   3546  N N     . GLY A 1 487 ? 28.641  -23.548 23.644  1.000 25.598  0 487 GLY AAA N     1 ? 1 
ATOM   3547  C CA    . GLY A 1 487 ? 29.170  -22.196 23.910  1.000 25.057  0 487 GLY AAA CA    1 ? 1 
ATOM   3548  C C     . GLY A 1 487 ? 29.788  -21.572 22.675  1.000 23.963  0 487 GLY AAA C     1 ? 1 
ATOM   3549  O O     . GLY A 1 487 ? 30.319  -22.357 21.816  1.000 25.417  0 487 GLY AAA O     1 ? 1 
ATOM   3550  N N     . ILE A 1 488 ? 29.658  -20.250 22.565  1.000 22.497  0 488 ILE AAA N     1 ? 1 
ATOM   3551  C CA    . ILE A 1 488 ? 30.547  -19.388 21.748  1.000 22.751  0 488 ILE AAA CA    1 ? 1 
ATOM   3552  C C     . ILE A 1 488 ? 31.654  -18.886 22.674  1.000 22.421  0 488 ILE AAA C     1 ? 1 
ATOM   3553  O O     . ILE A 1 488 ? 31.318  -18.282 23.696  1.000 22.797  0 488 ILE AAA O     1 ? 1 
ATOM   3554  C CB    . ILE A 1 488 ? 29.829  -18.197 21.096  1.000 22.559  0 488 ILE AAA CB    1 ? 1 
ATOM   3555  C CG1   . ILE A 1 488 ? 28.481  -18.562 20.468  1.000 22.834  0 488 ILE AAA CG1   1 ? 1 
ATOM   3556  C CG2   . ILE A 1 488 ? 30.790  -17.515 20.127  1.000 22.198  0 488 ILE AAA CG2   1 ? 1 
ATOM   3557  C CD1   . ILE A 1 488 ? 27.727  -17.334 19.981  1.000 22.164  0 488 ILE AAA CD1   1 ? 1 
ATOM   3558  N N     . HIS A 1 489 ? 32.904  -19.145 22.319  1.000 22.247  0 489 HIS AAA N     1 ? 1 
ATOM   3559  C CA    . HIS A 1 489 ? 34.103  -18.791 23.115  1.000 22.616  0 489 HIS AAA CA    1 ? 1 
ATOM   3560  C C     . HIS A 1 489 ? 34.957  -17.822 22.311  1.000 21.751  0 489 HIS AAA C     1 ? 1 
ATOM   3561  O O     . HIS A 1 489 ? 35.088  -18.012 21.113  1.000 23.006  0 489 HIS AAA O     1 ? 1 
ATOM   3562  C CB    . HIS A 1 489 ? 34.872  -20.051 23.431  1.000 22.969  0 489 HIS AAA CB    1 ? 1 
ATOM   3563  C CG    . HIS A 1 489 ? 36.016  -19.833 24.340  1.000 24.339  0 489 HIS AAA CG    1 ? 1 
ATOM   3564  N ND1   . HIS A 1 489 ? 35.853  -19.299 25.618  1.000 25.219  0 489 HIS AAA ND1   1 ? 1 
ATOM   3565  C CD2   . HIS A 1 489 ? 37.336  -20.120 24.194  1.000 24.486  0 489 HIS AAA CD2   1 ? 1 
ATOM   3566  C CE1   . HIS A 1 489 ? 37.038  -19.283 26.219  1.000 25.503  0 489 HIS AAA CE1   1 ? 1 
ATOM   3567  N NE2   . HIS A 1 489 ? 37.959  -19.782 25.363  1.000 25.143  0 489 HIS AAA NE2   1 ? 1 
ATOM   3568  N N     . PRO A 1 490 ? 35.556  -16.776 22.907  1.000 21.795  0 490 PRO AAA N     1 ? 1 
ATOM   3569  C CA    . PRO A 1 490 ? 35.323  -16.394 24.298  1.000 22.564  0 490 PRO AAA CA    1 ? 1 
ATOM   3570  C C     . PRO A 1 490 ? 34.204  -15.366 24.410  1.000 22.875  0 490 PRO AAA C     1 ? 1 
ATOM   3571  O O     . PRO A 1 490 ? 34.333  -14.296 23.823  1.000 25.475  0 490 PRO AAA O     1 ? 1 
ATOM   3572  C CB    . PRO A 1 490 ? 36.665  -15.765 24.702  1.000 22.199  0 490 PRO AAA CB    1 ? 1 
ATOM   3573  C CG    . PRO A 1 490 ? 37.515  -15.781 23.438  1.000 21.651  0 490 PRO AAA CG    1 ? 1 
ATOM   3574  C CD    . PRO A 1 490 ? 36.551  -15.898 22.286  1.000 21.634  0 490 PRO AAA CD    1 ? 1 
ATOM   3575  N N     . THR A 1 491 ? 33.139  -15.685 25.138  1.000 22.509  0 491 THR AAA N     1 ? 1 
ATOM   3576  C CA    . THR A 1 491 ? 32.057  -14.710 25.450  1.000 21.923  0 491 THR AAA CA    1 ? 1 
ATOM   3577  C C     . THR A 1 491 ? 31.781  -14.764 26.952  1.000 22.699  0 491 THR AAA C     1 ? 1 
ATOM   3578  O O     . THR A 1 491 ? 32.258  -15.707 27.607  1.000 24.114  0 491 THR AAA O     1 ? 1 
ATOM   3579  C CB    . THR A 1 491 ? 30.795  -15.012 24.650  1.000 21.397  0 491 THR AAA CB    1 ? 1 
ATOM   3580  O OG1   . THR A 1 491 ? 30.221  -16.252 25.099  1.000 21.555  0 491 THR AAA OG1   1 ? 1 
ATOM   3581  C CG2   . THR A 1 491 ? 31.068  -15.040 23.161  1.000 21.084  0 491 THR AAA CG2   1 ? 1 
ATOM   3582  N N     . ASP A 1 492 ? 31.051  -13.798 27.465  1.000 22.309  0 492 ASP AAA N     1 ? 1 
ATOM   3583  C CA    . ASP A 1 492 ? 30.464  -13.900 28.823  1.000 22.770  0 492 ASP AAA CA    1 ? 1 
ATOM   3584  C C     . ASP A 1 492 ? 29.206  -14.785 28.758  1.000 23.658  0 492 ASP AAA C     1 ? 1 
ATOM   3585  O O     . ASP A 1 492 ? 28.940  -15.514 29.744  1.000 25.430  0 492 ASP AAA O     1 ? 1 
ATOM   3586  C CB    . ASP A 1 492 ? 30.192  -12.508 29.382  1.000 22.940  0 492 ASP AAA CB    1 ? 1 
ATOM   3587  C CG    . ASP A 1 492 ? 31.462  -11.704 29.589  1.000 23.402  0 492 ASP AAA CG    1 ? 1 
ATOM   3588  O OD1   . ASP A 1 492 ? 32.523  -12.315 29.767  1.000 24.115  0 492 ASP AAA OD1   1 ? 1 
ATOM   3589  O OD2   . ASP A 1 492 ? 31.374  -10.474 29.605  1.000 26.535  0 492 ASP AAA OD2   1 ? 1 
ATOM   3590  N N     . ALA A 1 493 ? 28.442  -14.765 27.663  1.000 21.979  0 493 ALA AAA N     1 ? 1 
ATOM   3591  C CA    . ALA A 1 493 ? 27.139  -15.438 27.615  1.000 21.584  0 493 ALA AAA CA    1 ? 1 
ATOM   3592  C C     . ALA A 1 493 ? 27.306  -16.959 27.603  1.000 21.629  0 493 ALA AAA C     1 ? 1 
ATOM   3593  O O     . ALA A 1 493 ? 26.300  -17.648 27.916  1.000 22.057  0 493 ALA AAA O     1 ? 1 
ATOM   3594  C CB    . ALA A 1 493 ? 26.385  -14.973 26.413  1.000 22.312  0 493 ALA AAA CB    1 ? 1 
ATOM   3595  N N     . GLU A 1 494 ? 28.472  -17.494 27.249  1.000 21.091  0 494 GLU AAA N     1 ? 1 
ATOM   3596  C CA    . GLU A 1 494 ? 28.707  -18.969 27.257  1.000 22.198  0 494 GLU AAA CA    1 ? 1 
ATOM   3597  C C     . GLU A 1 494 ? 28.658  -19.491 28.699  1.000 21.396  0 494 GLU AAA C     1 ? 1 
ATOM   3598  O O     . GLU A 1 494 ? 28.442  -20.689 28.916  1.000 20.251  0 494 GLU AAA O     1 ? 1 
ATOM   3599  C CB    . GLU A 1 494 ? 30.025  -19.338 26.555  1.000 24.297  0 494 GLU AAA CB    1 ? 1 
ATOM   3600  C CG    . GLU A 1 494 ? 31.279  -18.936 27.310  1.000 25.468  0 494 GLU AAA CG    1 ? 1 
ATOM   3601  C CD    . GLU A 1 494 ? 32.571  -19.421 26.681  1.000 28.153  0 494 GLU AAA CD    1 ? 1 
ATOM   3602  O OE1   . GLU A 1 494 ? 32.576  -20.569 26.286  1.000 30.782  0 494 GLU AAA OE1   1 ? 1 
ATOM   3603  O OE2   . GLU A 1 494 ? 33.569  -18.622 26.579  1.000 30.561  0 494 GLU AAA OE2   1 ? 1 
ATOM   3604  N N     . VAL A 1 495 ? 28.821  -18.627 29.691  1.000 22.012  0 495 VAL AAA N     1 ? 1 
ATOM   3605  C CA    . VAL A 1 495 ? 28.752  -19.052 31.123  1.000 22.286  0 495 VAL AAA CA    1 ? 1 
ATOM   3606  C C     . VAL A 1 495 ? 27.410  -19.760 31.356  1.000 23.050  0 495 VAL AAA C     1 ? 1 
ATOM   3607  O O     . VAL A 1 495 ? 27.432  -20.753 32.080  1.000 25.664  0 495 VAL AAA O     1 ? 1 
ATOM   3608  C CB    . VAL A 1 495 ? 28.968  -17.896 32.108  1.000 22.332  0 495 VAL AAA CB    1 ? 1 
ATOM   3609  C CG1   . VAL A 1 495 ? 27.701  -17.041 32.227  1.000 23.629  0 495 VAL AAA CG1   1 ? 1 
ATOM   3610  C CG2   . VAL A 1 495 ? 29.412  -18.415 33.470  1.000 22.882  0 495 VAL AAA CG2   1 ? 1 
ATOM   3611  N N     . PHE A 1 496 ? 26.320  -19.345 30.701  1.000 22.259  0 496 PHE AAA N     1 ? 1 
ATOM   3612  C CA    . PHE A 1 496 ? 24.977  -19.935 30.893  1.000 22.950  0 496 PHE AAA CA    1 ? 1 
ATOM   3613  C C     . PHE A 1 496 ? 24.902  -21.410 30.488  1.000 24.050  0 496 PHE AAA C     1 ? 1 
ATOM   3614  O O     . PHE A 1 496 ? 23.868  -22.010 30.783  1.000 25.506  0 496 PHE AAA O     1 ? 1 
ATOM   3615  C CB    . PHE A 1 496 ? 23.902  -19.125 30.172  1.000 22.037  0 496 PHE AAA CB    1 ? 1 
ATOM   3616  C CG    . PHE A 1 496 ? 23.591  -17.887 30.950  1.000 21.531  0 496 PHE AAA CG    1 ? 1 
ATOM   3617  C CD1   . PHE A 1 496 ? 22.867  -17.975 32.127  1.000 21.449  0 496 PHE AAA CD1   1 ? 1 
ATOM   3618  C CD2   . PHE A 1 496 ? 24.107  -16.659 30.567  1.000 21.325  0 496 PHE AAA CD2   1 ? 1 
ATOM   3619  C CE1   . PHE A 1 496 ? 22.581  -16.846 32.866  1.000 20.953  0 496 PHE AAA CE1   1 ? 1 
ATOM   3620  C CE2   . PHE A 1 496 ? 23.850  -15.534 31.334  1.000 21.210  0 496 PHE AAA CE2   1 ? 1 
ATOM   3621  C CZ    . PHE A 1 496 ? 23.082  -15.634 32.477  1.000 20.967  0 496 PHE AAA CZ    1 ? 1 
ATOM   3622  N N     . GLY A 1 497 ? 25.959  -21.977 29.933  1.000 24.957  0 497 GLY AAA N     1 ? 1 
ATOM   3623  C CA    . GLY A 1 497 ? 26.027  -23.386 29.530  1.000 26.944  0 497 GLY AAA CA    1 ? 1 
ATOM   3624  C C     . GLY A 1 497 ? 26.744  -24.272 30.520  1.000 27.510  0 497 GLY AAA C     1 ? 1 
ATOM   3625  O O     . GLY A 1 497 ? 26.772  -25.421 30.288  1.000 28.653  0 497 GLY AAA O     1 ? 1 
ATOM   3626  N N     . ILE A 1 498 ? 27.350  -23.733 31.564  1.000 30.433  0 498 ILE AAA N     1 ? 1 
ATOM   3627  C CA    . ILE A 1 498 ? 28.219  -24.486 32.514  1.000 31.176  0 498 ILE AAA CA    1 ? 1 
ATOM   3628  C C     . ILE A 1 498 ? 27.951  -23.994 33.934  1.000 30.915  0 498 ILE AAA C     1 ? 1 
ATOM   3629  O O     . ILE A 1 498 ? 28.893  -24.018 34.741  1.000 32.431  0 498 ILE AAA O     1 ? 1 
ATOM   3630  C CB    . ILE A 1 498 ? 29.706  -24.327 32.142  1.000 32.164  0 498 ILE AAA CB    1 ? 1 
ATOM   3631  C CG1   . ILE A 1 498 ? 30.116  -22.852 32.095  1.000 33.631  0 498 ILE AAA CG1   1 ? 1 
ATOM   3632  C CG2   . ILE A 1 498 ? 30.015  -25.047 30.838  1.000 32.699  0 498 ILE AAA CG2   1 ? 1 
ATOM   3633  C CD1   . ILE A 1 498 ? 31.633  -22.621 32.221  1.000 35.033  0 498 ILE AAA CD1   1 ? 1 
ATOM   3634  N N     . LEU A 1 499 ? 26.750  -23.525 34.234  1.000 30.772  0 499 LEU AAA N     1 ? 1 
ATOM   3635  C CA    . LEU A 1 499 ? 26.432  -23.136 35.631  1.000 32.797  0 499 LEU AAA CA    1 ? 1 
ATOM   3636  C C     . LEU A 1 499 ? 26.188  -24.420 36.429  1.000 35.951  0 499 LEU AAA C     1 ? 1 
ATOM   3637  O O     . LEU A 1 499 ? 25.460  -25.296 35.903  1.000 37.796  0 499 LEU AAA O     1 ? 1 
ATOM   3638  C CB    . LEU A 1 499 ? 25.216  -22.228 35.661  1.000 32.683  0 499 LEU AAA CB    1 ? 1 
ATOM   3639  C CG    . LEU A 1 499 ? 25.370  -20.854 35.011  1.000 32.165  0 499 LEU AAA CG    1 ? 1 
ATOM   3640  C CD1   . LEU A 1 499 ? 23.991  -20.232 34.835  1.000 32.054  0 499 LEU AAA CD1   1 ? 1 
ATOM   3641  C CD2   . LEU A 1 499 ? 26.268  -19.976 35.852  1.000 30.780  0 499 LEU AAA CD2   1 ? 1 
ATOM   3642  N N     . GLU A 1 500 ? 26.824  -24.574 37.598  1.000 37.459  0 500 GLU AAA N     1 ? 1 
ATOM   3643  C CA    . GLU A 1 500 ? 26.718  -25.830 38.388  1.000 39.699  0 500 GLU AAA CA    1 ? 1 
ATOM   3644  C C     . GLU A 1 500 ? 26.579  -25.572 39.887  1.000 37.587  0 500 GLU AAA C     1 ? 1 
ATOM   3645  O O     . GLU A 1 500 ? 26.056  -26.477 40.561  1.000 39.424  0 500 GLU AAA O     1 ? 1 
ATOM   3646  C CB    . GLU A 1 500 ? 27.901  -26.755 38.106  1.000 43.886  0 500 GLU AAA CB    1 ? 1 
ATOM   3647  C CG    . GLU A 1 500 ? 29.268  -26.118 38.301  1.000 47.137  0 500 GLU AAA CG    1 ? 1 
ATOM   3648  C CD    . GLU A 1 500 ? 30.394  -27.056 37.910  1.000 52.969  0 500 GLU AAA CD    1 ? 1 
ATOM   3649  O OE1   . GLU A 1 500 ? 30.110  -28.249 37.624  1.000 58.220  0 500 GLU AAA OE1   1 ? 1 
ATOM   3650  O OE2   . GLU A 1 500 ? 31.550  -26.582 37.832  1.000 61.704  0 500 GLU AAA OE2   1 ? 1 
ATOM   3651  N N     . VAL A 1 501 ? 27.018  -24.422 40.400  1.000 36.038  0 501 VAL AAA N     1 ? 1 
ATOM   3652  C CA    . VAL A 1 501 ? 26.973  -24.118 41.866  1.000 35.327  0 501 VAL AAA CA    1 ? 1 
ATOM   3653  C C     . VAL A 1 501 ? 25.566  -23.631 42.177  1.000 35.642  0 501 VAL AAA C     1 ? 1 
ATOM   3654  O O     . VAL A 1 501 ? 25.049  -22.807 41.432  1.000 34.594  0 501 VAL AAA O     1 ? 1 
ATOM   3655  C CB    . VAL A 1 501 ? 28.033  -23.093 42.273  1.000 33.937  0 501 VAL AAA CB    1 ? 1 
ATOM   3656  C CG1   . VAL A 1 501 ? 27.925  -22.715 43.748  1.000 33.704  0 501 VAL AAA CG1   1 ? 1 
ATOM   3657  C CG2   . VAL A 1 501 ? 29.443  -23.623 41.924  1.000 34.421  0 501 VAL AAA CG2   1 ? 1 
ATOM   3658  N N     . THR A 1 502 ? 24.938  -24.169 43.212  1.000 36.323  0 502 THR AAA N     1 ? 1 
ATOM   3659  C CA    . THR A 1 502 ? 23.576  -23.748 43.658  1.000 35.165  0 502 THR AAA CA    1 ? 1 
ATOM   3660  C C     . THR A 1 502 ? 23.745  -22.883 44.902  1.000 34.579  0 502 THR AAA C     1 ? 1 
ATOM   3661  O O     . THR A 1 502 ? 24.742  -23.073 45.608  1.000 36.087  0 502 THR AAA O     1 ? 1 
ATOM   3662  C CB    . THR A 1 502 ? 22.677  -24.968 43.840  1.000 34.968  0 502 THR AAA CB    1 ? 1 
ATOM   3663  O OG1   . THR A 1 502 ? 23.093  -25.619 45.039  1.000 36.177  0 502 THR AAA OG1   1 ? 1 
ATOM   3664  C CG2   . THR A 1 502 ? 22.751  -25.938 42.680  1.000 34.935  0 502 THR AAA CG2   1 ? 1 
ATOM   3665  N N     . LYS A 1 503 ? 22.879  -21.897 45.104  1.000 36.344  0 503 LYS AAA N     1 ? 1 
ATOM   3666  C CA    . LYS A 1 503 ? 22.772  -21.178 46.405  1.000 40.436  0 503 LYS AAA CA    1 ? 1 
ATOM   3667  C C     . LYS A 1 503 ? 22.659  -22.231 47.527  1.000 40.895  0 503 LYS AAA C     1 ? 1 
ATOM   3668  O O     . LYS A 1 503 ? 23.513  -22.233 48.414  1.000 41.215  0 503 LYS AAA O     1 ? 1 
ATOM   3669  C CB    . LYS A 1 503 ? 21.569  -20.233 46.420  1.000 43.669  0 503 LYS AAA CB    1 ? 1 
ATOM   3670  C CG    . LYS A 1 503 ? 21.478  -19.368 47.674  1.000 47.140  0 503 LYS AAA CG    1 ? 1 
ATOM   3671  C CD    . LYS A 1 503 ? 20.385  -18.311 47.724  1.000 49.824  0 503 LYS AAA CD    1 ? 1 
ATOM   3672  C CE    . LYS A 1 503 ? 20.932  -17.007 48.301  1.000 51.580  0 503 LYS AAA CE    1 ? 1 
ATOM   3673  N NZ    . LYS A 1 503 ? 19.959  -16.274 49.139  1.000 54.107  0 503 LYS AAA NZ    1 ? 1 
ATOM   3674  N N     . ARG A 1 504 ? 21.663  -23.121 47.434  1.000 40.613  0 504 ARG AAA N     1 ? 1 
ATOM   3675  C CA    . ARG A 1 504 ? 21.380  -24.179 48.429  1.000 42.773  0 504 ARG AAA CA    1 ? 1 
ATOM   3676  C C     . ARG A 1 504 ? 22.683  -24.904 48.824  1.000 42.971  0 504 ARG AAA C     1 ? 1 
ATOM   3677  O O     . ARG A 1 504 ? 22.896  -25.111 50.039  1.000 39.822  0 504 ARG AAA O     1 ? 1 
ATOM   3678  C CB    . ARG A 1 504 ? 20.332  -25.165 47.899  1.000 44.124  0 504 ARG AAA CB    1 ? 1 
ATOM   3679  C CG    . ARG A 1 504 ? 20.165  -26.385 48.786  1.000 45.720  0 504 ARG AAA CG    1 ? 1 
ATOM   3680  C CD    . ARG A 1 504 ? 19.012  -27.281 48.402  1.000 48.496  0 504 ARG AAA CD    1 ? 1 
ATOM   3681  N NE    . ARG A 1 504 ? 17.725  -26.601 48.526  1.000 49.553  0 504 ARG AAA NE    1 ? 1 
ATOM   3682  C CZ    . ARG A 1 504 ? 16.865  -26.439 47.530  1.000 51.120  0 504 ARG AAA CZ    1 ? 1 
ATOM   3683  N NH1   . ARG A 1 504 ? 17.123  -26.920 46.323  1.000 55.416  0 504 ARG AAA NH1   1 ? 1 
ATOM   3684  N NH2   . ARG A 1 504 ? 15.721  -25.818 47.736  1.000 49.987  0 504 ARG AAA NH2   1 ? 1 
ATOM   3685  N N     . SER A 1 505 ? 23.523  -25.282 47.856  1.000 41.068  0 505 SER AAA N     1 ? 1 
ATOM   3686  C CA    . SER A 1 505 ? 24.805  -26.005 48.111  1.000 42.203  0 505 SER AAA CA    1 ? 1 
ATOM   3687  C C     . SER A 1 505 ? 25.699  -25.217 49.088  1.000 41.519  0 505 SER AAA C     1 ? 1 
ATOM   3688  O O     . SER A 1 505 ? 26.574  -25.855 49.665  1.000 40.228  0 505 SER AAA O     1 ? 1 
ATOM   3689  C CB    . SER A 1 505 ? 25.560  -26.307 46.825  1.000 41.094  0 505 SER AAA CB    1 ? 1 
ATOM   3690  O OG    . SER A 1 505 ? 26.329  -25.179 46.412  1.000 38.965  0 505 SER AAA OG    1 ? 1 
ATOM   3691  N N     . GLY A 1 506 ? 25.523  -23.884 49.203  1.000 41.080  0 506 GLY AAA N     1 ? 1 
ATOM   3692  C CA    . GLY A 1 506 ? 26.326  -22.982 50.063  1.000 40.787  0 506 GLY AAA CA    1 ? 1 
ATOM   3693  C C     . GLY A 1 506 ? 27.800  -22.899 49.621  1.000 42.026  0 506 GLY AAA C     1 ? 1 
ATOM   3694  O O     . GLY A 1 506 ? 28.584  -22.187 50.281  1.000 36.792  0 506 GLY AAA O     1 ? 1 
ATOM   3695  N N     . GLU A 1 507 ? 28.173  -23.574 48.525  1.000 43.518  0 507 GLU AAA N     1 ? 1 
ATOM   3696  C CA    . GLU A 1 507 ? 29.550  -23.533 47.976  1.000 46.449  0 507 GLU AAA CA    1 ? 1 
ATOM   3697  C C     . GLU A 1 507 ? 29.815  -22.164 47.325  1.000 43.379  0 507 GLU AAA C     1 ? 1 
ATOM   3698  O O     . GLU A 1 507 ? 28.837  -21.401 47.045  1.000 39.375  0 507 GLU AAA O     1 ? 1 
ATOM   3699  C CB    . GLU A 1 507 ? 29.756  -24.701 47.007  1.000 51.006  0 507 GLU AAA CB    1 ? 1 
ATOM   3700  C CG    . GLU A 1 507 ? 29.942  -26.047 47.694  1.000 54.446  0 507 GLU AAA CG    1 ? 1 
ATOM   3701  C CD    . GLU A 1 507 ? 30.057  -27.212 46.718  1.000 62.049  0 507 GLU AAA CD    1 ? 1 
ATOM   3702  O OE1   . GLU A 1 507 ? 29.009  -27.580 46.149  1.000 58.947  0 507 GLU AAA OE1   1 ? 1 
ATOM   3703  O OE2   . GLU A 1 507 ? 31.214  -27.734 46.491  1.000 73.340  0 507 GLU AAA OE2   1 ? 1 
ATOM   3704  N N     . SER A 1 508 ? 31.106  -21.846 47.140  1.000 40.358  0 508 SER AAA N     1 ? 1 
ATOM   3705  C CA    . SER A 1 508 ? 31.597  -20.608 46.478  1.000 39.796  0 508 SER AAA CA    1 ? 1 
ATOM   3706  C C     . SER A 1 508 ? 31.186  -20.623 44.996  1.000 35.863  0 508 SER AAA C     1 ? 1 
ATOM   3707  O O     . SER A 1 508 ? 31.455  -21.632 44.321  1.000 35.214  0 508 SER AAA O     1 ? 1 
ATOM   3708  C CB    . SER A 1 508 ? 33.100  -20.460 46.623  1.000 41.486  0 508 SER AAA CB    1 ? 1 
ATOM   3709  O OG    . SER A 1 508 ? 33.571  -19.327 45.888  1.000 42.319  0 508 SER AAA OG    1 ? 1 
ATOM   3710  N N     . PHE A 1 509 ? 30.545  -19.565 44.523  1.000 33.572  0 509 PHE AAA N     1 ? 1 
ATOM   3711  C CA    . PHE A 1 509 ? 30.104  -19.396 43.109  1.000 34.054  0 509 PHE AAA CA    1 ? 1 
ATOM   3712  C C     . PHE A 1 509 ? 31.090  -18.457 42.391  1.000 34.421  0 509 PHE AAA C     1 ? 1 
ATOM   3713  O O     . PHE A 1 509 ? 30.919  -18.163 41.204  1.000 31.892  0 509 PHE AAA O     1 ? 1 
ATOM   3714  C CB    . PHE A 1 509 ? 28.635  -18.958 43.021  1.000 31.728  0 509 PHE AAA CB    1 ? 1 
ATOM   3715  C CG    . PHE A 1 509 ? 28.269  -17.754 43.830  1.000 31.861  0 509 PHE AAA CG    1 ? 1 
ATOM   3716  C CD1   . PHE A 1 509 ? 28.531  -16.479 43.358  1.000 31.243  0 509 PHE AAA CD1   1 ? 1 
ATOM   3717  C CD2   . PHE A 1 509 ? 27.659  -17.892 45.069  1.000 33.625  0 509 PHE AAA CD2   1 ? 1 
ATOM   3718  C CE1   . PHE A 1 509 ? 28.175  -15.361 44.095  1.000 32.206  0 509 PHE AAA CE1   1 ? 1 
ATOM   3719  C CE2   . PHE A 1 509 ? 27.308  -16.765 45.807  1.000 33.930  0 509 PHE AAA CE2   1 ? 1 
ATOM   3720  C CZ    . PHE A 1 509 ? 27.570  -15.503 45.326  1.000 32.454  0 509 PHE AAA CZ    1 ? 1 
ATOM   3721  N N     . VAL A 1 510 ? 32.118  -17.993 43.093  1.000 36.624  0 510 VAL AAA N     1 ? 1 
ATOM   3722  C CA    . VAL A 1 510 ? 33.190  -17.151 42.482  1.000 41.260  0 510 VAL AAA CA    1 ? 1 
ATOM   3723  C C     . VAL A 1 510 ? 34.099  -18.050 41.639  1.000 43.207  0 510 VAL AAA C     1 ? 1 
ATOM   3724  O O     . VAL A 1 510 ? 34.365  -19.187 42.075  1.000 46.854  0 510 VAL AAA O     1 ? 1 
ATOM   3725  C CB    . VAL A 1 510 ? 33.962  -16.405 43.586  1.000 42.305  0 510 VAL AAA CB    1 ? 1 
ATOM   3726  C CG1   . VAL A 1 510 ? 35.234  -15.755 43.090  1.000 41.692  0 510 VAL AAA CG1   1 ? 1 
ATOM   3727  C CG2   . VAL A 1 510 ? 33.063  -15.390 44.286  1.000 41.651  0 510 VAL AAA CG2   1 ? 1 
ATOM   3728  N N     . SER A 1 511 ? 34.502  -17.591 40.452  1.000 46.793  0 511 SER AAA N     1 ? 1 
ATOM   3729  C CA    . SER A 1 511 ? 35.697  -18.104 39.719  1.000 51.398  0 511 SER AAA CA    1 ? 1 
ATOM   3730  C C     . SER A 1 511 ? 36.710  -16.962 39.557  1.000 53.590  0 511 SER AAA C     1 ? 1 
ATOM   3731  O O     . SER A 1 511 ? 36.299  -15.896 39.088  1.000 50.499  0 511 SER AAA O     1 ? 1 
ATOM   3732  C CB    . SER A 1 511 ? 35.309  -18.754 38.411  1.000 49.243  0 511 SER AAA CB    1 ? 1 
ATOM   3733  O OG    . SER A 1 511 ? 34.559  -17.898 37.574  1.000 43.175  0 511 SER AAA OG    1 ? 1 
ATOM   3734  N N     . SER A 1 512 ? 37.959  -17.149 39.990  1.000 60.864  0 512 SER AAA N     1 ? 1 
ATOM   3735  C CA    . SER A 1 512 ? 39.013  -16.086 40.076  1.000 68.397  0 512 SER AAA CA    1 ? 1 
ATOM   3736  C C     . SER A 1 512 ? 39.883  -16.057 38.803  1.000 71.598  0 512 SER AAA C     1 ? 1 
ATOM   3737  O O     . SER A 1 512 ? 40.323  -14.960 38.402  1.000 69.401  0 512 SER AAA O     1 ? 1 
ATOM   3738  C CB    . SER A 1 512 ? 39.892  -16.250 41.312  1.000 75.144  0 512 SER AAA CB    1 ? 1 
ATOM   3739  O OG    . SER A 1 512 ? 39.157  -16.115 42.523  1.000 79.950  0 512 SER AAA OG    1 ? 1 
ATOM   3740  N N     . GLY A 1 513 ? 40.151  -17.224 38.206  1.000 76.846  0 513 GLY AAA N     1 ? 1 
ATOM   3741  C CA    . GLY A 1 513 ? 40.827  -17.362 36.903  1.000 82.596  0 513 GLY AAA CA    1 ? 1 
ATOM   3742  C C     . GLY A 1 513 ? 40.058  -16.644 35.803  1.000 81.924  0 513 GLY AAA C     1 ? 1 
ATOM   3743  O O     . GLY A 1 513 ? 38.812  -16.604 35.869  1.000 85.879  0 513 GLY AAA O     1 ? 1 
ATOM   3744  N N     . GLY A 1 514 ? 40.779  -16.123 34.810  1.000 75.749  0 514 GLY AAA N     1 ? 1 
ATOM   3745  C CA    . GLY A 1 514 ? 40.234  -15.269 33.739  1.000 76.922  0 514 GLY AAA CA    1 ? 1 
ATOM   3746  C C     . GLY A 1 514 ? 40.122  -15.984 32.393  1.000 74.813  0 514 GLY AAA C     1 ? 1 
ATOM   3747  O O     . GLY A 1 514 ? 40.710  -15.482 31.427  1.000 67.032  0 514 GLY AAA O     1 ? 1 
ATOM   3748  N N     . CYS A 1 515 ? 39.368  -17.095 32.316  1.000 77.433  0 515 CYS AAA N     1 ? 1 
ATOM   3749  C CA    . CYS A 1 515 ? 38.939  -17.749 31.039  1.000 79.316  0 515 CYS AAA CA    1 ? 1 
ATOM   3750  C C     . CYS A 1 515 ? 37.647  -17.088 30.524  1.000 73.751  0 515 CYS AAA C     1 ? 1 
ATOM   3751  O O     . CYS A 1 515 ? 37.098  -17.545 29.489  1.000 79.638  0 515 CYS AAA O     1 ? 1 
ATOM   3752  C CB    . CYS A 1 515 ? 38.724  -19.254 31.189  1.000 84.750  0 515 CYS AAA CB    1 ? 1 
ATOM   3753  S SG    . CYS A 1 515 ? 39.849  -20.057 32.357  1.000 93.121  0 515 CYS AAA SG    1 ? 1 
ATOM   3754  N N     . GLY A 1 516 ? 37.199  -16.014 31.188  1.000 61.748  0 516 GLY AAA N     1 ? 1 
ATOM   3755  C CA    . GLY A 1 516 ? 35.950  -15.292 30.896  1.000 56.175  0 516 GLY AAA CA    1 ? 1 
ATOM   3756  C C     . GLY A 1 516 ? 34.740  -16.088 31.346  1.000 53.149  0 516 GLY AAA C     1 ? 1 
ATOM   3757  O O     . GLY A 1 516 ? 34.771  -16.661 32.444  1.000 56.364  0 516 GLY AAA O     1 ? 1 
ATOM   3758  N N     . GLY A 1 517 ? 33.707  -16.148 30.508  1.000 57.906  0 517 GLY AAA N     1 ? 1 
ATOM   3759  C CA    . GLY A 1 517 ? 32.459  -16.898 30.771  1.000 60.243  0 517 GLY AAA CA    1 ? 1 
ATOM   3760  C C     . GLY A 1 517 ? 32.618  -18.421 30.714  1.000 62.316  0 517 GLY AAA C     1 ? 1 
ATOM   3761  O O     . GLY A 1 517 ? 31.718  -19.113 31.193  1.000 60.265  0 517 GLY AAA O     1 ? 1 
ATOM   3762  N N     . GLY A 1 518 ? 33.665  -18.953 30.087  1.000 69.576  0 518 GLY AAA N     1 ? 1 
ATOM   3763  C CA    . GLY A 1 518 ? 33.691  -20.351 29.617  1.000 73.122  0 518 GLY AAA CA    1 ? 1 
ATOM   3764  C C     . GLY A 1 518 ? 34.739  -21.170 30.339  1.000 77.503  0 518 GLY AAA C     1 ? 1 
ATOM   3765  O O     . GLY A 1 518 ? 34.928  -20.975 31.551  1.000 75.504  0 518 GLY AAA O     1 ? 1 
ATOM   3766  N N     . LYS A 1 519 ? 35.338  -22.112 29.615  1.000 82.247  0 519 LYS AAA N     1 ? 1 
ATOM   3767  C CA    . LYS A 1 519 ? 36.597  -22.798 29.985  1.000 86.474  0 519 LYS AAA CA    1 ? 1 
ATOM   3768  C C     . LYS A 1 519 ? 37.272  -23.164 28.668  1.000 80.916  0 519 LYS AAA C     1 ? 1 
ATOM   3769  O O     . LYS A 1 519 ? 36.566  -23.703 27.772  1.000 79.675  0 519 LYS AAA O     1 ? 1 
ATOM   3770  C CB    . LYS A 1 519 ? 36.368  -24.028 30.880  1.000 94.280  0 519 LYS AAA CB    1 ? 1 
ATOM   3771  C CG    . LYS A 1 519 ? 36.211  -23.745 32.375  1.000 100.428 0 519 LYS AAA CG    1 ? 1 
ATOM   3772  C CD    . LYS A 1 519 ? 37.091  -24.624 33.265  1.000 103.930 0 519 LYS AAA CD    1 ? 1 
ATOM   3773  C CE    . LYS A 1 519 ? 36.809  -24.483 34.746  1.000 104.347 0 519 LYS AAA CE    1 ? 1 
ATOM   3774  N NZ    . LYS A 1 519 ? 35.911  -25.553 35.247  1.000 102.183 0 519 LYS AAA NZ    1 ? 1 
ATOM   3775  N N     . CYS A 1 520 ? 38.551  -22.807 28.547  0.900 74.140  0 520 CYS AAA N     1 ? 1 
ATOM   3776  C CA    A CYS A 1 520 ? 39.438  -23.240 27.440  0.500 72.433  0 520 CYS AAA CA    1 ? 1 
ATOM   3777  C CA    B CYS A 1 520 ? 39.435  -23.249 27.432  0.500 69.430  0 520 CYS AAA CA    1 ? 1 
ATOM   3778  C C     . CYS A 1 520 ? 39.708  -24.748 27.594  0.900 74.267  0 520 CYS AAA C     1 ? 1 
ATOM   3779  O O     . CYS A 1 520 ? 40.176  -25.359 26.603  0.900 76.903  0 520 CYS AAA O     1 ? 1 
ATOM   3780  C CB    A CYS A 1 520 ? 40.710  -22.399 27.443  0.500 67.536  0 520 CYS AAA CB    1 ? 1 
ATOM   3781  C CB    B CYS A 1 520 ? 40.764  -22.503 27.392  0.500 60.417  0 520 CYS AAA CB    1 ? 1 
ATOM   3782  S SG    A CYS A 1 520 ? 40.517  -20.793 28.269  0.500 60.382  0 520 CYS AAA SG    1 ? 1 
ATOM   3783  S SG    B CYS A 1 520 ? 40.794  -21.028 26.345  0.500 53.842  0 520 CYS AAA SG    1 ? 1 
ATOM   3784  N N     . GLY A 1 521 ? 39.417  -25.288 28.793  1.000 77.452  0 521 GLY AAA N     1 ? 1 
ATOM   3785  C CA    . GLY A 1 521 ? 39.505  -26.722 29.139  1.000 81.300  0 521 GLY AAA CA    1 ? 1 
ATOM   3786  C C     . GLY A 1 521 ? 39.249  -26.960 30.623  1.000 85.773  0 521 GLY AAA C     1 ? 1 
ATOM   3787  O O     . GLY A 1 521 ? 38.949  -26.043 31.396  1.000 90.411  0 521 GLY AAA O     1 ? 1 
ATOM   3788  O OXT   . GLY A 1 521 ? 39.347  -28.087 31.109  1.000 80.796  0 521 GLY AAA OXT   1 ? 1 
ATOM   3789  N N     . LEU B 1 24  ? 43.674  -55.118 38.538  1.000 77.186  0 24  LEU BBB N     1 ? 2 
ATOM   3790  C CA    . LEU B 1 24  ? 43.430  -55.471 37.104  1.000 80.010  0 24  LEU BBB CA    1 ? 2 
ATOM   3791  C C     . LEU B 1 24  ? 44.636  -54.984 36.276  1.000 79.132  0 24  LEU BBB C     1 ? 2 
ATOM   3792  O O     . LEU B 1 24  ? 45.468  -54.270 36.838  1.000 82.248  0 24  LEU BBB O     1 ? 2 
ATOM   3793  C CB    . LEU B 1 24  ? 42.072  -54.885 36.661  1.000 79.231  0 24  LEU BBB CB    1 ? 2 
ATOM   3794  C CG    . LEU B 1 24  ? 41.161  -55.755 35.773  1.000 79.302  0 24  LEU BBB CG    1 ? 2 
ATOM   3795  C CD1   . LEU B 1 24  ? 41.209  -57.249 36.121  1.000 80.868  0 24  LEU BBB CD1   1 ? 2 
ATOM   3796  C CD2   . LEU B 1 24  ? 39.721  -55.262 35.841  1.000 77.991  0 24  LEU BBB CD2   1 ? 2 
ATOM   3797  N N     . THR B 1 25  ? 44.735  -55.411 35.011  1.000 77.784  0 25  THR BBB N     1 ? 2 
ATOM   3798  C CA    . THR B 1 25  ? 45.968  -55.431 34.184  1.000 76.510  0 25  THR BBB CA    1 ? 2 
ATOM   3799  C C     . THR B 1 25  ? 46.276  -54.043 33.592  1.000 71.432  0 25  THR BBB C     1 ? 2 
ATOM   3800  O O     . THR B 1 25  ? 47.070  -54.018 32.611  1.000 78.369  0 25  THR BBB O     1 ? 2 
ATOM   3801  C CB    . THR B 1 25  ? 45.845  -56.511 33.086  1.000 80.231  0 25  THR BBB CB    1 ? 2 
ATOM   3802  O OG1   . THR B 1 25  ? 44.576  -56.334 32.441  1.000 76.463  0 25  THR BBB OG1   1 ? 2 
ATOM   3803  C CG2   . THR B 1 25  ? 45.972  -57.928 33.616  1.000 79.536  0 25  THR BBB CG2   1 ? 2 
ATOM   3804  N N     . PHE B 1 26  ? 45.745  -52.941 34.146  1.000 63.062  0 26  PHE BBB N     1 ? 2 
ATOM   3805  C CA    . PHE B 1 26  ? 46.029  -51.556 33.643  1.000 59.735  0 26  PHE BBB CA    1 ? 2 
ATOM   3806  C C     . PHE B 1 26  ? 46.445  -50.608 34.775  1.000 54.833  0 26  PHE BBB C     1 ? 2 
ATOM   3807  O O     . PHE B 1 26  ? 45.665  -50.459 35.782  1.000 51.347  0 26  PHE BBB O     1 ? 2 
ATOM   3808  C CB    . PHE B 1 26  ? 44.833  -50.957 32.896  1.000 58.302  0 26  PHE BBB CB    1 ? 2 
ATOM   3809  C CG    . PHE B 1 26  ? 44.298  -51.838 31.799  1.000 57.759  0 26  PHE BBB CG    1 ? 2 
ATOM   3810  C CD1   . PHE B 1 26  ? 45.085  -52.157 30.701  1.000 54.546  0 26  PHE BBB CD1   1 ? 2 
ATOM   3811  C CD2   . PHE B 1 26  ? 43.009  -52.357 31.878  1.000 57.338  0 26  PHE BBB CD2   1 ? 2 
ATOM   3812  C CE1   . PHE B 1 26  ? 44.601  -52.978 29.701  1.000 54.586  0 26  PHE BBB CE1   1 ? 2 
ATOM   3813  C CE2   . PHE B 1 26  ? 42.518  -53.173 30.872  1.000 57.860  0 26  PHE BBB CE2   1 ? 2 
ATOM   3814  C CZ    . PHE B 1 26  ? 43.313  -53.466 29.777  1.000 57.417  0 26  PHE BBB CZ    1 ? 2 
ATOM   3815  N N     . MET B 1 27  ? 47.608  -49.966 34.602  1.000 48.484  0 27  MET BBB N     1 ? 2 
ATOM   3816  C CA    . MET B 1 27  ? 48.106  -48.950 35.560  1.000 49.891  0 27  MET BBB CA    1 ? 2 
ATOM   3817  C C     . MET B 1 27  ? 47.075  -47.822 35.700  1.000 47.924  0 27  MET BBB C     1 ? 2 
ATOM   3818  O O     . MET B 1 27  ? 46.812  -47.421 36.844  1.000 45.516  0 27  MET BBB O     1 ? 2 
ATOM   3819  C CB    . MET B 1 27  ? 49.452  -48.376 35.114  1.000 51.491  0 27  MET BBB CB    1 ? 2 
ATOM   3820  C CG    . MET B 1 27  ? 50.585  -49.397 35.210  1.000 51.288  0 27  MET BBB CG    1 ? 2 
ATOM   3821  S SD    . MET B 1 27  ? 52.068  -48.817 34.340  1.000 53.917  0 27  MET BBB SD    1 ? 2 
ATOM   3822  C CE    . MET B 1 27  ? 52.696  -47.586 35.489  1.000 53.894  0 27  MET BBB CE    1 ? 2 
ATOM   3823  N N     . TYR B 1 28  ? 46.480  -47.366 34.587  1.000 46.058  0 28  TYR BBB N     1 ? 2 
ATOM   3824  C CA    . TYR B 1 28  ? 45.520  -46.223 34.574  1.000 44.757  0 28  TYR BBB CA    1 ? 2 
ATOM   3825  C C     . TYR B 1 28  ? 44.157  -46.650 34.006  1.000 43.235  0 28  TYR BBB C     1 ? 2 
ATOM   3826  O O     . TYR B 1 28  ? 44.086  -47.614 33.228  1.000 40.486  0 28  TYR BBB O     1 ? 2 
ATOM   3827  C CB    . TYR B 1 28  ? 46.091  -45.055 33.760  1.000 43.300  0 28  TYR BBB CB    1 ? 2 
ATOM   3828  C CG    . TYR B 1 28  ? 47.314  -44.419 34.353  1.000 42.131  0 28  TYR BBB CG    1 ? 2 
ATOM   3829  C CD1   . TYR B 1 28  ? 48.580  -44.954 34.145  1.000 41.180  0 28  TYR BBB CD1   1 ? 2 
ATOM   3830  C CD2   . TYR B 1 28  ? 47.196  -43.282 35.135  1.000 42.497  0 28  TYR BBB CD2   1 ? 2 
ATOM   3831  C CE1   . TYR B 1 28  ? 49.700  -44.387 34.721  1.000 41.346  0 28  TYR BBB CE1   1 ? 2 
ATOM   3832  C CE2   . TYR B 1 28  ? 48.310  -42.699 35.711  1.000 41.794  0 28  TYR BBB CE2   1 ? 2 
ATOM   3833  C CZ    . TYR B 1 28  ? 49.560  -43.251 35.499  1.000 41.333  0 28  TYR BBB CZ    1 ? 2 
ATOM   3834  O OH    . TYR B 1 28  ? 50.651  -42.663 36.057  1.000 41.965  0 28  TYR BBB OH    1 ? 2 
ATOM   3835  N N     . ASP B 1 29  ? 43.103  -45.914 34.376  1.000 41.788  0 29  ASP BBB N     1 ? 2 
ATOM   3836  C CA    . ASP B 1 29  ? 41.754  -46.036 33.762  1.000 41.992  0 29  ASP BBB CA    1 ? 2 
ATOM   3837  C C     . ASP B 1 29  ? 41.733  -45.235 32.446  1.000 40.109  0 29  ASP BBB C     1 ? 2 
ATOM   3838  O O     . ASP B 1 29  ? 41.111  -45.720 31.473  1.000 37.831  0 29  ASP BBB O     1 ? 2 
ATOM   3839  C CB    . ASP B 1 29  ? 40.667  -45.592 34.736  1.000 42.957  0 29  ASP BBB CB    1 ? 2 
ATOM   3840  C CG    . ASP B 1 29  ? 40.547  -46.479 35.963  1.000 44.729  0 29  ASP BBB CG    1 ? 2 
ATOM   3841  O OD1   . ASP B 1 29  ? 40.061  -47.613 35.816  1.000 43.018  0 29  ASP BBB OD1   1 ? 2 
ATOM   3842  O OD2   . ASP B 1 29  ? 40.950  -46.015 37.055  1.000 44.858  0 29  ASP BBB OD2   1 ? 2 
ATOM   3843  N N     . LEU B 1 30  ? 42.424  -44.088 32.423  1.000 36.764  0 30  LEU BBB N     1 ? 2 
ATOM   3844  C CA    . LEU B 1 30  ? 42.391  -43.115 31.302  1.000 36.138  0 30  LEU BBB CA    1 ? 2 
ATOM   3845  C C     . LEU B 1 30  ? 43.723  -42.366 31.191  1.000 35.171  0 30  LEU BBB C     1 ? 2 
ATOM   3846  O O     . LEU B 1 30  ? 44.188  -41.810 32.201  1.000 33.814  0 30  LEU BBB O     1 ? 2 
ATOM   3847  C CB    . LEU B 1 30  ? 41.262  -42.102 31.510  1.000 36.750  0 30  LEU BBB CB    1 ? 2 
ATOM   3848  C CG    . LEU B 1 30  ? 41.180  -41.014 30.436  1.000 36.168  0 30  LEU BBB CG    1 ? 2 
ATOM   3849  C CD1   . LEU B 1 30  ? 40.774  -41.608 29.088  1.000 35.982  0 30  LEU BBB CD1   1 ? 2 
ATOM   3850  C CD2   . LEU B 1 30  ? 40.206  -39.937 30.844  1.000 35.862  0 30  LEU BBB CD2   1 ? 2 
ATOM   3851  N N     . VAL B 1 31  ? 44.293  -42.391 29.991  1.000 32.548  0 31  VAL BBB N     1 ? 2 
ATOM   3852  C CA    . VAL B 1 31  ? 45.491  -41.610 29.619  1.000 34.041  0 31  VAL BBB CA    1 ? 2 
ATOM   3853  C C     . VAL B 1 31  ? 45.054  -40.700 28.478  1.000 32.955  0 31  VAL BBB C     1 ? 2 
ATOM   3854  O O     . VAL B 1 31  ? 44.469  -41.198 27.503  1.000 33.226  0 31  VAL BBB O     1 ? 2 
ATOM   3855  C CB    . VAL B 1 31  ? 46.692  -42.500 29.218  1.000 33.228  0 31  VAL BBB CB    1 ? 2 
ATOM   3856  C CG1   . VAL B 1 31  ? 47.786  -41.710 28.547  1.000 32.295  0 31  VAL BBB CG1   1 ? 2 
ATOM   3857  C CG2   . VAL B 1 31  ? 47.240  -43.236 30.431  1.000 34.487  0 31  VAL BBB CG2   1 ? 2 
ATOM   3858  N N     . VAL B 1 32  ? 45.322  -39.411 28.654  1.000 30.551  0 32  VAL BBB N     1 ? 2 
ATOM   3859  C CA    . VAL B 1 32  ? 44.934  -38.341 27.702  1.000 28.515  0 32  VAL BBB CA    1 ? 2 
ATOM   3860  C C     . VAL B 1 32  ? 46.239  -37.825 27.119  1.000 27.354  0 32  VAL BBB C     1 ? 2 
ATOM   3861  O O     . VAL B 1 32  ? 47.086  -37.388 27.910  1.000 24.855  0 32  VAL BBB O     1 ? 2 
ATOM   3862  C CB    . VAL B 1 32  ? 44.112  -37.229 28.386  1.000 27.021  0 32  VAL BBB CB    1 ? 2 
ATOM   3863  C CG1   . VAL B 1 32  ? 43.760  -36.123 27.415  1.000 26.753  0 32  VAL BBB CG1   1 ? 2 
ATOM   3864  C CG2   . VAL B 1 32  ? 42.845  -37.778 28.978  1.000 26.755  0 32  VAL BBB CG2   1 ? 2 
ATOM   3865  N N     . ILE B 1 33  ? 46.375  -37.883 25.797  1.000 26.927  0 33  ILE BBB N     1 ? 2 
ATOM   3866  C CA    . ILE B 1 33  ? 47.526  -37.251 25.105  1.000 28.105  0 33  ILE BBB CA    1 ? 2 
ATOM   3867  C C     . ILE B 1 33  ? 47.065  -35.912 24.517  1.000 27.009  0 33  ILE BBB C     1 ? 2 
ATOM   3868  O O     . ILE B 1 33  ? 46.435  -35.888 23.451  1.000 29.817  0 33  ILE BBB O     1 ? 2 
ATOM   3869  C CB    . ILE B 1 33  ? 48.159  -38.189 24.068  1.000 29.525  0 33  ILE BBB CB    1 ? 2 
ATOM   3870  C CG1   . ILE B 1 33  ? 48.463  -39.560 24.678  1.000 31.087  0 33  ILE BBB CG1   1 ? 2 
ATOM   3871  C CG2   . ILE B 1 33  ? 49.396  -37.527 23.476  1.000 28.780  0 33  ILE BBB CG2   1 ? 2 
ATOM   3872  C CD1   . ILE B 1 33  ? 48.875  -40.633 23.683  1.000 31.855  0 33  ILE BBB CD1   1 ? 2 
ATOM   3873  N N     . GLY B 1 34  ? 47.444  -34.819 25.170  1.000 26.341  0 34  GLY BBB N     1 ? 2 
ATOM   3874  C CA    . GLY B 1 34  ? 47.118  -33.444 24.776  1.000 25.836  0 34  GLY BBB CA    1 ? 2 
ATOM   3875  C C     . GLY B 1 34  ? 46.398  -32.738 25.898  1.000 25.256  0 34  GLY BBB C     1 ? 2 
ATOM   3876  O O     . GLY B 1 34  ? 45.320  -33.244 26.343  1.000 26.270  0 34  GLY BBB O     1 ? 2 
ATOM   3877  N N     . GLY B 1 35  ? 46.966  -31.619 26.331  1.000 24.389  0 35  GLY BBB N     1 ? 2 
ATOM   3878  C CA    . GLY B 1 35  ? 46.438  -30.803 27.440  1.000 25.031  0 35  GLY BBB CA    1 ? 2 
ATOM   3879  C C     . GLY B 1 35  ? 45.880  -29.503 26.944  1.000 24.026  0 35  GLY BBB C     1 ? 2 
ATOM   3880  O O     . GLY B 1 35  ? 46.183  -28.480 27.522  1.000 23.943  0 35  GLY BBB O     1 ? 2 
ATOM   3881  N N     . GLY B 1 36  ? 45.106  -29.555 25.881  1.000 24.741  0 36  GLY BBB N     1 ? 2 
ATOM   3882  C CA    . GLY B 1 36  ? 44.257  -28.434 25.432  1.000 25.684  0 36  GLY BBB CA    1 ? 2 
ATOM   3883  C C     . GLY B 1 36  ? 42.805  -28.629 25.859  1.000 25.312  0 36  GLY BBB C     1 ? 2 
ATOM   3884  O O     . GLY B 1 36  ? 42.522  -29.320 26.836  1.000 23.497  0 36  GLY BBB O     1 ? 2 
ATOM   3885  N N     . SER B 1 37  ? 41.904  -28.036 25.104  1.000 27.278  0 37  SER BBB N     1 ? 2 
ATOM   3886  C CA    . SER B 1 37  ? 40.489  -27.848 25.503  1.000 29.068  0 37  SER BBB CA    1 ? 2 
ATOM   3887  C C     . SER B 1 37  ? 39.853  -29.233 25.722  1.000 29.446  0 37  SER BBB C     1 ? 2 
ATOM   3888  O O     . SER B 1 37  ? 39.210  -29.434 26.753  1.000 32.637  0 37  SER BBB O     1 ? 2 
ATOM   3889  C CB    . SER B 1 37  ? 39.754  -27.055 24.454  1.000 29.335  0 37  SER BBB CB    1 ? 2 
ATOM   3890  O OG    . SER B 1 37  ? 40.466  -25.900 24.060  1.000 30.200  0 37  SER BBB OG    1 ? 2 
ATOM   3891  N N     . GLY B 1 38  ? 40.077  -30.158 24.789  1.000 28.981  0 38  GLY BBB N     1 ? 2 
ATOM   3892  C CA    . GLY B 1 38  ? 39.488  -31.494 24.764  1.000 28.441  0 38  GLY BBB CA    1 ? 2 
ATOM   3893  C C     . GLY B 1 38  ? 40.045  -32.336 25.879  1.000 28.610  0 38  GLY BBB C     1 ? 2 
ATOM   3894  O O     . GLY B 1 38  ? 39.249  -32.864 26.656  1.000 28.004  0 38  GLY BBB O     1 ? 2 
ATOM   3895  N N     . GLY B 1 39  ? 41.371  -32.438 25.930  1.000 28.194  0 39  GLY BBB N     1 ? 2 
ATOM   3896  C CA    . GLY B 1 39  ? 42.119  -33.299 26.865  1.000 29.438  0 39  GLY BBB CA    1 ? 2 
ATOM   3897  C C     . GLY B 1 39  ? 41.895  -32.946 28.327  1.000 29.976  0 39  GLY BBB C     1 ? 2 
ATOM   3898  O O     . GLY B 1 39  ? 41.560  -33.846 29.099  1.000 29.864  0 39  GLY BBB O     1 ? 2 
ATOM   3899  N N     . MET B 1 40  ? 42.067  -31.679 28.706  1.000 31.037  0 40  MET BBB N     1 ? 2 
ATOM   3900  C CA    . MET B 1 40  ? 41.961  -31.252 30.126  1.000 32.479  0 40  MET BBB CA    1 ? 2 
ATOM   3901  C C     . MET B 1 40  ? 40.513  -31.459 30.584  1.000 30.319  0 40  MET BBB C     1 ? 2 
ATOM   3902  O O     . MET B 1 40  ? 40.313  -31.889 31.711  1.000 29.955  0 40  MET BBB O     1 ? 2 
ATOM   3903  C CB    . MET B 1 40  ? 42.411  -29.802 30.331  1.000 33.936  0 40  MET BBB CB    1 ? 2 
ATOM   3904  C CG    . MET B 1 40  ? 43.917  -29.666 30.253  1.000 36.063  0 40  MET BBB CG    1 ? 2 
ATOM   3905  S SD    . MET B 1 40  ? 44.506  -28.035 30.796  1.000 37.462  0 40  MET BBB SD    1 ? 2 
ATOM   3906  C CE    . MET B 1 40  ? 43.457  -26.948 29.841  1.000 37.473  0 40  MET BBB CE    1 ? 2 
ATOM   3907  N N     . ALA B 1 41  ? 39.549  -31.232 29.698  1.000 28.276  0 41  ALA BBB N     1 ? 2 
ATOM   3908  C CA    . ALA B 1 41  ? 38.120  -31.389 30.007  1.000 27.526  0 41  ALA BBB CA    1 ? 2 
ATOM   3909  C C     . ALA B 1 41  ? 37.813  -32.875 30.249  1.000 28.220  0 41  ALA BBB C     1 ? 2 
ATOM   3910  O O     . ALA B 1 41  ? 37.224  -33.176 31.323  1.000 28.100  0 41  ALA BBB O     1 ? 2 
ATOM   3911  C CB    . ALA B 1 41  ? 37.303  -30.802 28.892  1.000 27.555  0 41  ALA BBB CB    1 ? 2 
ATOM   3912  N N     . ALA B 1 42  ? 38.210  -33.769 29.321  1.000 27.027  0 42  ALA BBB N     1 ? 2 
ATOM   3913  C CA    . ALA B 1 42  ? 37.995  -35.219 29.456  1.000 27.893  0 42  ALA BBB CA    1 ? 2 
ATOM   3914  C C     . ALA B 1 42  ? 38.610  -35.708 30.774  1.000 29.378  0 42  ALA BBB C     1 ? 2 
ATOM   3915  O O     . ALA B 1 42  ? 37.872  -36.369 31.550  1.000 28.076  0 42  ALA BBB O     1 ? 2 
ATOM   3916  C CB    . ALA B 1 42  ? 38.554  -35.968 28.286  1.000 27.794  0 42  ALA BBB CB    1 ? 2 
ATOM   3917  N N     . ALA B 1 43  ? 39.871  -35.334 31.020  1.000 30.547  0 43  ALA BBB N     1 ? 2 
ATOM   3918  C CA    . ALA B 1 43  ? 40.753  -35.807 32.118  1.000 32.218  0 43  ALA BBB CA    1 ? 2 
ATOM   3919  C C     . ALA B 1 43  ? 40.149  -35.466 33.491  1.000 32.846  0 43  ALA BBB C     1 ? 2 
ATOM   3920  O O     . ALA B 1 43  ? 40.032  -36.377 34.327  1.000 32.541  0 43  ALA BBB O     1 ? 2 
ATOM   3921  C CB    . ALA B 1 43  ? 42.140  -35.213 31.934  1.000 30.929  0 43  ALA BBB CB    1 ? 2 
ATOM   3922  N N     . LYS B 1 44  ? 39.807  -34.192 33.718  1.000 36.114  0 44  LYS BBB N     1 ? 2 
ATOM   3923  C CA    . LYS B 1 44  ? 39.185  -33.681 34.966  1.000 36.921  0 44  LYS BBB CA    1 ? 2 
ATOM   3924  C C     . LYS B 1 44  ? 37.841  -34.374 35.208  1.000 36.385  0 44  LYS BBB C     1 ? 2 
ATOM   3925  O O     . LYS B 1 44  ? 37.533  -34.658 36.374  1.000 37.631  0 44  LYS BBB O     1 ? 2 
ATOM   3926  C CB    . LYS B 1 44  ? 38.981  -32.168 34.928  1.000 36.938  0 44  LYS BBB CB    1 ? 2 
ATOM   3927  C CG    . LYS B 1 44  ? 40.234  -31.370 35.242  1.000 41.227  0 44  LYS BBB CG    1 ? 2 
ATOM   3928  C CD    . LYS B 1 44  ? 40.000  -29.874 35.419  1.000 43.772  0 44  LYS BBB CD    1 ? 2 
ATOM   3929  C CE    . LYS B 1 44  ? 40.175  -29.057 34.155  1.000 43.709  0 44  LYS BBB CE    1 ? 2 
ATOM   3930  N NZ    . LYS B 1 44  ? 39.999  -27.619 34.510  1.000 46.929  0 44  LYS BBB NZ    1 ? 2 
ATOM   3931  N N     . GLU B 1 45  ? 37.041  -34.564 34.160  1.000 35.920  0 45  GLU BBB N     1 ? 2 
ATOM   3932  C CA    . GLU B 1 45  ? 35.692  -35.177 34.304  1.000 36.861  0 45  GLU BBB CA    1 ? 2 
ATOM   3933  C C     . GLU B 1 45  ? 35.839  -36.677 34.632  1.000 35.761  0 45  GLU BBB C     1 ? 2 
ATOM   3934  O O     . GLU B 1 45  ? 35.069  -37.178 35.456  1.000 33.058  0 45  GLU BBB O     1 ? 2 
ATOM   3935  C CB    . GLU B 1 45  ? 34.855  -34.996 33.038  1.000 37.374  0 45  GLU BBB CB    1 ? 2 
ATOM   3936  C CG    . GLU B 1 45  ? 33.399  -35.366 33.269  1.000 37.903  0 45  GLU BBB CG    1 ? 2 
ATOM   3937  C CD    . GLU B 1 45  ? 32.626  -34.280 33.989  1.000 39.377  0 45  GLU BBB CD    1 ? 2 
ATOM   3938  O OE1   . GLU B 1 45  ? 33.258  -33.252 34.365  1.000 39.900  0 45  GLU BBB OE1   1 ? 2 
ATOM   3939  O OE2   . GLU B 1 45  ? 31.372  -34.420 34.074  1.000 42.206  0 45  GLU BBB OE2   1 ? 2 
ATOM   3940  N N     . ALA B 1 46  ? 36.793  -37.376 34.002  1.000 35.788  0 46  ALA BBB N     1 ? 2 
ATOM   3941  C CA    . ALA B 1 46  ? 37.094  -38.796 34.301  1.000 35.377  0 46  ALA BBB CA    1 ? 2 
ATOM   3942  C C     . ALA B 1 46  ? 37.489  -38.904 35.772  1.000 35.625  0 46  ALA BBB C     1 ? 2 
ATOM   3943  O O     . ALA B 1 46  ? 36.893  -39.707 36.473  1.000 36.664  0 46  ALA BBB O     1 ? 2 
ATOM   3944  C CB    . ALA B 1 46  ? 38.173  -39.320 33.404  1.000 35.045  0 46  ALA BBB CB    1 ? 2 
ATOM   3945  N N     . ALA B 1 47  ? 38.453  -38.094 36.203  1.000 36.531  0 47  ALA BBB N     1 ? 2 
ATOM   3946  C CA    . ALA B 1 47  ? 39.012  -38.049 37.576  1.000 37.576  0 47  ALA BBB CA    1 ? 2 
ATOM   3947  C C     . ALA B 1 47  ? 37.902  -37.781 38.611  1.000 38.734  0 47  ALA BBB C     1 ? 2 
ATOM   3948  O O     . ALA B 1 47  ? 38.033  -38.279 39.726  1.000 40.845  0 47  ALA BBB O     1 ? 2 
ATOM   3949  C CB    . ALA B 1 47  ? 40.117  -37.010 37.650  1.000 36.335  0 47  ALA BBB CB    1 ? 2 
ATOM   3950  N N     . LYS B 1 48  ? 36.872  -37.022 38.251  1.000 41.056  0 48  LYS BBB N     1 ? 2 
ATOM   3951  C CA    . LYS B 1 48  ? 35.649  -36.747 39.077  1.000 45.846  0 48  LYS BBB CA    1 ? 2 
ATOM   3952  C C     . LYS B 1 48  ? 34.985  -38.052 39.553  1.000 46.125  0 48  LYS BBB C     1 ? 2 
ATOM   3953  O O     . LYS B 1 48  ? 34.391  -38.026 40.635  1.000 44.297  0 48  LYS BBB O     1 ? 2 
ATOM   3954  C CB    . LYS B 1 48  ? 34.597  -35.932 38.314  1.000 48.232  0 48  LYS BBB CB    1 ? 2 
ATOM   3955  C CG    . LYS B 1 48  ? 34.490  -34.467 38.723  1.000 52.582  0 48  LYS BBB CG    1 ? 2 
ATOM   3956  C CD    . LYS B 1 48  ? 33.301  -33.727 38.135  1.000 57.247  0 48  LYS BBB CD    1 ? 2 
ATOM   3957  C CE    . LYS B 1 48  ? 31.963  -34.223 38.664  1.000 63.427  0 48  LYS BBB CE    1 ? 2 
ATOM   3958  N NZ    . LYS B 1 48  ? 30.945  -33.144 38.745  1.000 64.270  0 48  LYS BBB NZ    1 ? 2 
ATOM   3959  N N     . TYR B 1 49  ? 35.079  -39.136 38.784  1.000 48.241  0 49  TYR BBB N     1 ? 2 
ATOM   3960  C CA    . TYR B 1 49  ? 34.398  -40.432 39.043  1.000 50.152  0 49  TYR BBB CA    1 ? 2 
ATOM   3961  C C     . TYR B 1 49  ? 35.342  -41.403 39.764  1.000 50.399  0 49  TYR BBB C     1 ? 2 
ATOM   3962  O O     . TYR B 1 49  ? 35.030  -42.604 39.803  1.000 54.586  0 49  TYR BBB O     1 ? 2 
ATOM   3963  C CB    . TYR B 1 49  ? 33.807  -40.991 37.742  1.000 52.148  0 49  TYR BBB CB    1 ? 2 
ATOM   3964  C CG    . TYR B 1 49  ? 32.742  -40.097 37.163  1.000 54.459  0 49  TYR BBB CG    1 ? 2 
ATOM   3965  C CD1   . TYR B 1 49  ? 31.598  -39.831 37.886  1.000 57.673  0 49  TYR BBB CD1   1 ? 2 
ATOM   3966  C CD2   . TYR B 1 49  ? 32.891  -39.467 35.930  1.000 55.415  0 49  TYR BBB CD2   1 ? 2 
ATOM   3967  C CE1   . TYR B 1 49  ? 30.636  -38.950 37.408  1.000 61.371  0 49  TYR BBB CE1   1 ? 2 
ATOM   3968  C CE2   . TYR B 1 49  ? 31.930  -38.604 35.428  1.000 55.407  0 49  TYR BBB CE2   1 ? 2 
ATOM   3969  C CZ    . TYR B 1 49  ? 30.797  -38.342 36.175  1.000 58.658  0 49  TYR BBB CZ    1 ? 2 
ATOM   3970  O OH    . TYR B 1 49  ? 29.825  -37.486 35.743  1.000 64.135  0 49  TYR BBB OH    1 ? 2 
ATOM   3971  N N     . GLY B 1 50  ? 36.412  -40.886 40.384  1.000 49.106  0 50  GLY BBB N     1 ? 2 
ATOM   3972  C CA    . GLY B 1 50  ? 37.410  -41.655 41.161  1.000 47.245  0 50  GLY BBB CA    1 ? 2 
ATOM   3973  C C     . GLY B 1 50  ? 38.329  -42.482 40.278  1.000 43.368  0 50  GLY BBB C     1 ? 2 
ATOM   3974  O O     . GLY B 1 50  ? 38.953  -43.443 40.751  1.000 42.729  0 50  GLY BBB O     1 ? 2 
ATOM   3975  N N     . LYS B 1 51  ? 38.428  -42.118 39.008  1.000 41.448  0 51  LYS BBB N     1 ? 2 
ATOM   3976  C CA    . LYS B 1 51  ? 39.279  -42.845 38.045  1.000 39.988  0 51  LYS BBB CA    1 ? 2 
ATOM   3977  C C     . LYS B 1 51  ? 40.702  -42.302 38.158  1.000 37.688  0 51  LYS BBB C     1 ? 2 
ATOM   3978  O O     . LYS B 1 51  ? 40.879  -41.144 38.524  1.000 36.497  0 51  LYS BBB O     1 ? 2 
ATOM   3979  C CB    . LYS B 1 51  ? 38.671  -42.738 36.652  1.000 44.137  0 51  LYS BBB CB    1 ? 2 
ATOM   3980  C CG    . LYS B 1 51  ? 37.244  -43.273 36.494  1.000 46.819  0 51  LYS BBB CG    1 ? 2 
ATOM   3981  C CD    . LYS B 1 51  ? 37.002  -44.562 37.231  1.000 49.720  0 51  LYS BBB CD    1 ? 2 
ATOM   3982  C CE    . LYS B 1 51  ? 35.734  -45.248 36.772  1.000 52.249  0 51  LYS BBB CE    1 ? 2 
ATOM   3983  N NZ    . LYS B 1 51  ? 35.123  -45.997 37.896  1.000 53.245  0 51  LYS BBB NZ    1 ? 2 
ATOM   3984  N N     . LYS B 1 52  ? 41.691  -43.157 37.925  1.000 37.635  0 52  LYS BBB N     1 ? 2 
ATOM   3985  C CA    . LYS B 1 52  ? 43.119  -42.784 37.859  1.000 37.199  0 52  LYS BBB CA    1 ? 2 
ATOM   3986  C C     . LYS B 1 52  ? 43.396  -42.269 36.440  1.000 35.132  0 52  LYS BBB C     1 ? 2 
ATOM   3987  O O     . LYS B 1 52  ? 43.123  -43.009 35.480  1.000 34.394  0 52  LYS BBB O     1 ? 2 
ATOM   3988  C CB    . LYS B 1 52  ? 44.019  -43.969 38.224  1.000 39.538  0 52  LYS BBB CB    1 ? 2 
ATOM   3989  C CG    . LYS B 1 52  ? 45.364  -43.557 38.805  1.000 40.999  0 52  LYS BBB CG    1 ? 2 
ATOM   3990  C CD    . LYS B 1 52  ? 46.447  -44.610 38.722  1.000 42.718  0 52  LYS BBB CD    1 ? 2 
ATOM   3991  C CE    . LYS B 1 52  ? 47.814  -43.995 38.961  1.000 42.135  0 52  LYS BBB CE    1 ? 2 
ATOM   3992  N NZ    . LYS B 1 52  ? 48.885  -44.972 38.709  1.000 42.577  0 52  LYS BBB NZ    1 ? 2 
ATOM   3993  N N     . VAL B 1 53  ? 43.892  -41.035 36.343  1.000 33.135  0 53  VAL BBB N     1 ? 2 
ATOM   3994  C CA    . VAL B 1 53  ? 43.978  -40.248 35.086  1.000 32.850  0 53  VAL BBB CA    1 ? 2 
ATOM   3995  C C     . VAL B 1 53  ? 45.378  -39.661 34.993  1.000 32.631  0 53  VAL BBB C     1 ? 2 
ATOM   3996  O O     . VAL B 1 53  ? 45.857  -39.113 36.003  1.000 32.013  0 53  VAL BBB O     1 ? 2 
ATOM   3997  C CB    . VAL B 1 53  ? 42.902  -39.153 35.002  1.000 33.261  0 53  VAL BBB CB    1 ? 2 
ATOM   3998  C CG1   . VAL B 1 53  ? 42.839  -38.545 33.606  1.000 33.589  0 53  VAL BBB CG1   1 ? 2 
ATOM   3999  C CG2   . VAL B 1 53  ? 41.522  -39.678 35.380  1.000 33.964  0 53  VAL BBB CG2   1 ? 2 
ATOM   4000  N N     . ALA B 1 54  ? 46.018  -39.829 33.831  1.000 32.035  0 54  ALA BBB N     1 ? 2 
ATOM   4001  C CA    . ALA B 1 54  ? 47.276  -39.152 33.450  1.000 31.132  0 54  ALA BBB CA    1 ? 2 
ATOM   4002  C C     . ALA B 1 54  ? 46.999  -38.326 32.204  1.000 29.629  0 54  ALA BBB C     1 ? 2 
ATOM   4003  O O     . ALA B 1 54  ? 46.286  -38.821 31.294  1.000 30.212  0 54  ALA BBB O     1 ? 2 
ATOM   4004  C CB    . ALA B 1 54  ? 48.392  -40.147 33.191  1.000 32.244  0 54  ALA BBB CB    1 ? 2 
ATOM   4005  N N     . LEU B 1 55  ? 47.584  -37.131 32.152  1.000 28.552  0 55  LEU BBB N     1 ? 2 
ATOM   4006  C CA    . LEU B 1 55  ? 47.490  -36.234 30.989  1.000 26.900  0 55  LEU BBB CA    1 ? 2 
ATOM   4007  C C     . LEU B 1 55  ? 48.899  -35.851 30.571  1.000 27.053  0 55  LEU BBB C     1 ? 2 
ATOM   4008  O O     . LEU B 1 55  ? 49.664  -35.464 31.431  1.000 28.188  0 55  LEU BBB O     1 ? 2 
ATOM   4009  C CB    . LEU B 1 55  ? 46.627  -35.012 31.318  1.000 25.520  0 55  LEU BBB CB    1 ? 2 
ATOM   4010  C CG    . LEU B 1 55  ? 46.336  -34.088 30.133  1.000 24.378  0 55  LEU BBB CG    1 ? 2 
ATOM   4011  C CD1   . LEU B 1 55  ? 44.989  -33.407 30.272  1.000 23.991  0 55  LEU BBB CD1   1 ? 2 
ATOM   4012  C CD2   . LEU B 1 55  ? 47.410  -33.032 30.009  1.000 24.207  0 55  LEU BBB CD2   1 ? 2 
ATOM   4013  N N     . PHE B 1 56  ? 49.182  -35.987 29.285  1.000 28.343  0 56  PHE BBB N     1 ? 2 
ATOM   4014  C CA    . PHE B 1 56  ? 50.411  -35.541 28.606  1.000 30.537  0 56  PHE BBB CA    1 ? 2 
ATOM   4015  C C     . PHE B 1 56  ? 50.106  -34.255 27.852  1.000 30.732  0 56  PHE BBB C     1 ? 2 
ATOM   4016  O O     . PHE B 1 56  ? 49.071  -34.185 27.131  1.000 30.635  0 56  PHE BBB O     1 ? 2 
ATOM   4017  C CB    . PHE B 1 56  ? 50.943  -36.649 27.686  1.000 31.949  0 56  PHE BBB CB    1 ? 2 
ATOM   4018  C CG    . PHE B 1 56  ? 51.426  -37.864 28.434  1.000 33.656  0 56  PHE BBB CG    1 ? 2 
ATOM   4019  C CD1   . PHE B 1 56  ? 52.720  -37.926 28.917  1.000 34.803  0 56  PHE BBB CD1   1 ? 2 
ATOM   4020  C CD2   . PHE B 1 56  ? 50.586  -38.941 28.671  1.000 35.746  0 56  PHE BBB CD2   1 ? 2 
ATOM   4021  C CE1   . PHE B 1 56  ? 53.176  -39.048 29.598  1.000 35.835  0 56  PHE BBB CE1   1 ? 2 
ATOM   4022  C CE2   . PHE B 1 56  ? 51.042  -40.062 29.352  1.000 37.108  0 56  PHE BBB CE2   1 ? 2 
ATOM   4023  C CZ    . PHE B 1 56  ? 52.330  -40.103 29.837  1.000 36.024  0 56  PHE BBB CZ    1 ? 2 
ATOM   4024  N N     . ASP B 1 57  ? 50.953  -33.246 28.058  1.000 30.281  0 57  ASP BBB N     1 ? 2 
ATOM   4025  C CA    . ASP B 1 57  ? 51.005  -32.030 27.210  1.000 29.459  0 57  ASP BBB CA    1 ? 2 
ATOM   4026  C C     . ASP B 1 57  ? 52.471  -31.634 27.073  1.000 29.032  0 57  ASP BBB C     1 ? 2 
ATOM   4027  O O     . ASP B 1 57  ? 53.117  -31.525 28.107  1.000 26.844  0 57  ASP BBB O     1 ? 2 
ATOM   4028  C CB    . ASP B 1 57  ? 50.206  -30.864 27.788  1.000 28.920  0 57  ASP BBB CB    1 ? 2 
ATOM   4029  C CG    . ASP B 1 57  ? 50.049  -29.756 26.752  1.000 30.026  0 57  ASP BBB CG    1 ? 2 
ATOM   4030  O OD1   . ASP B 1 57  ? 49.354  -30.028 25.734  1.000 28.858  0 57  ASP BBB OD1   1 ? 2 
ATOM   4031  O OD2   . ASP B 1 57  ? 50.710  -28.671 26.891  1.000 29.765  0 57  ASP BBB OD2   1 ? 2 
ATOM   4032  N N     . PHE B 1 58  ? 52.948  -31.454 25.843  1.000 28.989  0 58  PHE BBB N     1 ? 2 
ATOM   4033  C CA    . PHE B 1 58  ? 54.253  -30.838 25.529  1.000 30.448  0 58  PHE BBB CA    1 ? 2 
ATOM   4034  C C     . PHE B 1 58  ? 54.084  -29.993 24.272  1.000 30.341  0 58  PHE BBB C     1 ? 2 
ATOM   4035  O O     . PHE B 1 58  ? 53.390  -30.417 23.312  1.000 28.153  0 58  PHE BBB O     1 ? 2 
ATOM   4036  C CB    . PHE B 1 58  ? 55.338  -31.900 25.322  1.000 32.549  0 58  PHE BBB CB    1 ? 2 
ATOM   4037  C CG    . PHE B 1 58  ? 56.731  -31.371 25.037  1.000 33.472  0 58  PHE BBB CG    1 ? 2 
ATOM   4038  C CD1   . PHE B 1 58  ? 57.145  -31.141 23.730  1.000 34.046  0 58  PHE BBB CD1   1 ? 2 
ATOM   4039  C CD2   . PHE B 1 58  ? 57.630  -31.142 26.076  1.000 32.885  0 58  PHE BBB CD2   1 ? 2 
ATOM   4040  C CE1   . PHE B 1 58  ? 58.423  -30.672 23.463  1.000 34.758  0 58  PHE BBB CE1   1 ? 2 
ATOM   4041  C CE2   . PHE B 1 58  ? 58.898  -30.649 25.812  1.000 33.393  0 58  PHE BBB CE2   1 ? 2 
ATOM   4042  C CZ    . PHE B 1 58  ? 59.293  -30.413 24.510  1.000 34.801  0 58  PHE BBB CZ    1 ? 2 
ATOM   4043  N N     . VAL B 1 59  ? 54.739  -28.837 24.252  1.000 29.838  0 59  VAL BBB N     1 ? 2 
ATOM   4044  C CA    . VAL B 1 59  ? 54.588  -27.879 23.125  1.000 30.412  0 59  VAL BBB CA    1 ? 2 
ATOM   4045  C C     . VAL B 1 59  ? 55.803  -28.022 22.206  1.000 30.204  0 59  VAL BBB C     1 ? 2 
ATOM   4046  O O     . VAL B 1 59  ? 56.881  -27.559 22.622  1.000 30.436  0 59  VAL BBB O     1 ? 2 
ATOM   4047  C CB    . VAL B 1 59  ? 54.400  -26.439 23.658  1.000 29.582  0 59  VAL BBB CB    1 ? 2 
ATOM   4048  C CG1   . VAL B 1 59  ? 54.248  -25.440 22.528  1.000 29.186  0 59  VAL BBB CG1   1 ? 2 
ATOM   4049  C CG2   . VAL B 1 59  ? 53.228  -26.366 24.624  1.000 30.381  0 59  VAL BBB CG2   1 ? 2 
ATOM   4050  N N     . LYS B 1 60  ? 55.639  -28.644 21.028  1.000 30.500  0 60  LYS BBB N     1 ? 2 
ATOM   4051  C CA    . LYS B 1 60  ? 56.653  -28.570 19.931  1.000 32.370  0 60  LYS BBB CA    1 ? 2 
ATOM   4052  C C     . LYS B 1 60  ? 56.766  -27.107 19.496  1.000 31.988  0 60  LYS BBB C     1 ? 2 
ATOM   4053  O O     . LYS B 1 60  ? 55.753  -26.463 19.234  1.000 32.026  0 60  LYS BBB O     1 ? 2 
ATOM   4054  C CB    . LYS B 1 60  ? 56.331  -29.536 18.787  1.000 32.862  0 60  LYS BBB CB    1 ? 2 
ATOM   4055  C CG    . LYS B 1 60  ? 56.636  -30.993 19.158  1.000 35.376  0 60  LYS BBB CG    1 ? 2 
ATOM   4056  C CD    . LYS B 1 60  ? 56.294  -32.090 18.147  1.000 34.393  0 60  LYS BBB CD    1 ? 2 
ATOM   4057  C CE    . LYS B 1 60  ? 54.850  -32.126 17.703  1.000 34.375  0 60  LYS BBB CE    1 ? 2 
ATOM   4058  N NZ    . LYS B 1 60  ? 53.904  -32.279 18.833  1.000 35.706  0 60  LYS BBB NZ    1 ? 2 
ATOM   4059  N N     . PRO B 1 61  ? 57.976  -26.495 19.443  1.000 31.997  0 61  PRO BBB N     1 ? 2 
ATOM   4060  C CA    . PRO B 1 61  ? 58.095  -25.101 18.990  1.000 31.953  0 61  PRO BBB CA    1 ? 2 
ATOM   4061  C C     . PRO B 1 61  ? 57.562  -24.901 17.554  1.000 31.603  0 61  PRO BBB C     1 ? 2 
ATOM   4062  O O     . PRO B 1 61  ? 57.638  -25.807 16.740  1.000 32.995  0 61  PRO BBB O     1 ? 2 
ATOM   4063  C CB    . PRO B 1 61  ? 59.601  -24.771 19.070  1.000 31.594  0 61  PRO BBB CB    1 ? 2 
ATOM   4064  C CG    . PRO B 1 61  ? 60.157  -25.840 20.000  1.000 31.543  0 61  PRO BBB CG    1 ? 2 
ATOM   4065  C CD    . PRO B 1 61  ? 59.273  -27.071 19.825  1.000 31.550  0 61  PRO BBB CD    1 ? 2 
ATOM   4066  N N     . SER B 1 62  ? 57.004  -23.721 17.286  1.000 30.556  0 62  SER BBB N     1 ? 2 
ATOM   4067  C CA    . SER B 1 62  ? 56.491  -23.329 15.961  1.000 30.642  0 62  SER BBB CA    1 ? 2 
ATOM   4068  C C     . SER B 1 62  ? 57.637  -23.383 14.930  1.000 31.545  0 62  SER BBB C     1 ? 2 
ATOM   4069  O O     . SER B 1 62  ? 58.822  -23.534 15.316  1.000 30.020  0 62  SER BBB O     1 ? 2 
ATOM   4070  C CB    . SER B 1 62  ? 55.873  -21.981 16.013  1.000 30.505  0 62  SER BBB CB    1 ? 2 
ATOM   4071  O OG    . SER B 1 62  ? 56.873  -20.983 16.160  1.000 31.755  0 62  SER BBB OG    1 ? 2 
ATOM   4072  N N     . THR B 1 63  ? 57.295  -23.224 13.653  1.000 31.860  0 63  THR BBB N     1 ? 2 
ATOM   4073  C CA    . THR B 1 63  ? 58.283  -23.099 12.551  1.000 34.607  0 63  THR BBB CA    1 ? 2 
ATOM   4074  C C     . THR B 1 63  ? 59.269  -21.959 12.847  1.000 36.200  0 63  THR BBB C     1 ? 2 
ATOM   4075  O O     . THR B 1 63  ? 60.339  -21.988 12.253  1.000 36.634  0 63  THR BBB O     1 ? 2 
ATOM   4076  C CB    . THR B 1 63  ? 57.586  -22.953 11.194  1.000 34.064  0 63  THR BBB CB    1 ? 2 
ATOM   4077  O OG1   . THR B 1 63  ? 56.751  -21.796 11.247  1.000 33.660  0 63  THR BBB OG1   1 ? 2 
ATOM   4078  C CG2   . THR B 1 63  ? 56.800  -24.192 10.845  1.000 32.380  0 63  THR BBB CG2   1 ? 2 
ATOM   4079  N N     . GLN B 1 64  ? 58.944  -21.019 13.753  1.000 36.707  0 64  GLN BBB N     1 ? 2 
ATOM   4080  C CA    . GLN B 1 64  ? 59.829  -19.858 14.067  1.000 36.653  0 64  GLN BBB CA    1 ? 2 
ATOM   4081  C C     . GLN B 1 64  ? 60.362  -19.925 15.515  1.000 34.334  0 64  GLN BBB C     1 ? 2 
ATOM   4082  O O     . GLN B 1 64  ? 60.818  -18.892 16.007  1.000 36.030  0 64  GLN BBB O     1 ? 2 
ATOM   4083  C CB    . GLN B 1 64  ? 59.089  -18.552 13.749  1.000 38.016  0 64  GLN BBB CB    1 ? 2 
ATOM   4084  C CG    . GLN B 1 64  ? 58.842  -18.338 12.249  1.000 40.696  0 64  GLN BBB CG    1 ? 2 
ATOM   4085  C CD    . GLN B 1 64  ? 60.123  -18.165 11.447  1.000 42.504  0 64  GLN BBB CD    1 ? 2 
ATOM   4086  O OE1   . GLN B 1 64  ? 61.142  -17.678 11.934  1.000 42.360  0 64  GLN BBB OE1   1 ? 2 
ATOM   4087  N NE2   . GLN B 1 64  ? 60.086  -18.549 10.184  1.000 42.709  0 64  GLN BBB NE2   1 ? 2 
ATOM   4088  N N     . GLY B 1 65  ? 60.354  -21.085 16.166  1.000 31.596  0 65  GLY BBB N     1 ? 2 
ATOM   4089  C CA    . GLY B 1 65  ? 60.914  -21.267 17.520  1.000 31.540  0 65  GLY BBB CA    1 ? 2 
ATOM   4090  C C     . GLY B 1 65  ? 60.001  -20.783 18.661  1.000 33.020  0 65  GLY BBB C     1 ? 2 
ATOM   4091  O O     . GLY B 1 65  ? 60.483  -20.796 19.802  1.000 33.408  0 65  GLY BBB O     1 ? 2 
ATOM   4092  N N     . THR B 1 66  ? 58.733  -20.412 18.418  1.000 32.027  0 66  THR BBB N     1 ? 2 
ATOM   4093  C CA    . THR B 1 66  ? 57.824  -19.964 19.509  1.000 32.490  0 66  THR BBB CA    1 ? 2 
ATOM   4094  C C     . THR B 1 66  ? 57.302  -21.169 20.291  1.000 33.230  0 66  THR BBB C     1 ? 2 
ATOM   4095  O O     . THR B 1 66  ? 56.854  -22.123 19.624  1.000 33.744  0 66  THR BBB O     1 ? 2 
ATOM   4096  C CB    . THR B 1 66  ? 56.639  -19.121 19.030  1.000 31.271  0 66  THR BBB CB    1 ? 2 
ATOM   4097  O OG1   . THR B 1 66  ? 57.136  -18.157 18.122  1.000 35.147  0 66  THR BBB OG1   1 ? 2 
ATOM   4098  C CG2   . THR B 1 66  ? 55.959  -18.381 20.163  1.000 31.399  0 66  THR BBB CG2   1 ? 2 
ATOM   4099  N N     . LYS B 1 67  ? 57.315  -21.085 21.627  1.000 33.506  0 67  LYS BBB N     1 ? 2 
ATOM   4100  C CA    . LYS B 1 67  ? 56.726  -22.101 22.530  1.000 36.310  0 67  LYS BBB CA    1 ? 2 
ATOM   4101  C C     . LYS B 1 67  ? 56.047  -21.422 23.736  1.000 33.377  0 67  LYS BBB C     1 ? 2 
ATOM   4102  O O     . LYS B 1 67  ? 56.171  -20.207 23.888  1.000 30.203  0 67  LYS BBB O     1 ? 2 
ATOM   4103  C CB    . LYS B 1 67  ? 57.792  -23.105 22.980  1.000 41.242  0 67  LYS BBB CB    1 ? 2 
ATOM   4104  C CG    . LYS B 1 67  ? 58.835  -22.561 23.946  1.000 45.182  0 67  LYS BBB CG    1 ? 2 
ATOM   4105  C CD    . LYS B 1 67  ? 60.033  -23.503 24.049  1.000 51.649  0 67  LYS BBB CD    1 ? 2 
ATOM   4106  C CE    . LYS B 1 67  ? 60.659  -23.567 25.437  1.000 56.970  0 67  LYS BBB CE    1 ? 2 
ATOM   4107  N NZ    . LYS B 1 67  ? 61.091  -24.950 25.784  1.000 60.383  0 67  LYS BBB NZ    1 ? 2 
ATOM   4108  N N     . TRP B 1 68  ? 55.324  -22.219 24.540  1.000 29.875  0 68  TRP BBB N     1 ? 2 
ATOM   4109  C CA    . TRP B 1 68  ? 54.346  -21.731 25.543  1.000 27.776  0 68  TRP BBB CA    1 ? 2 
ATOM   4110  C C     . TRP B 1 68  ? 54.006  -22.854 26.538  1.000 27.326  0 68  TRP BBB C     1 ? 2 
ATOM   4111  O O     . TRP B 1 68  ? 54.451  -24.025 26.308  1.000 26.261  0 68  TRP BBB O     1 ? 2 
ATOM   4112  C CB    . TRP B 1 68  ? 53.091  -21.176 24.832  1.000 25.938  0 68  TRP BBB CB    1 ? 2 
ATOM   4113  C CG    . TRP B 1 68  ? 52.481  -22.077 23.803  1.000 24.623  0 68  TRP BBB CG    1 ? 2 
ATOM   4114  C CD1   . TRP B 1 68  ? 51.624  -23.104 24.020  1.000 24.687  0 68  TRP BBB CD1   1 ? 2 
ATOM   4115  C CD2   . TRP B 1 68  ? 52.673  -22.036 22.375  1.000 25.225  0 68  TRP BBB CD2   1 ? 2 
ATOM   4116  N NE1   . TRP B 1 68  ? 51.283  -23.709 22.846  1.000 24.831  0 68  TRP BBB NE1   1 ? 2 
ATOM   4117  C CE2   . TRP B 1 68  ? 51.881  -23.049 21.813  1.000 24.269  0 68  TRP BBB CE2   1 ? 2 
ATOM   4118  C CE3   . TRP B 1 68  ? 53.438  -21.238 21.513  1.000 26.007  0 68  TRP BBB CE3   1 ? 2 
ATOM   4119  C CZ2   . TRP B 1 68  ? 51.825  -23.289 20.449  1.000 24.660  0 68  TRP BBB CZ2   1 ? 2 
ATOM   4120  C CZ3   . TRP B 1 68  ? 53.397  -21.477 20.159  1.000 26.359  0 68  TRP BBB CZ3   1 ? 2 
ATOM   4121  C CH2   . TRP B 1 68  ? 52.594  -22.489 19.633  1.000 26.009  0 68  TRP BBB CH2   1 ? 2 
ATOM   4122  N N     . GLY B 1 69  ? 53.214  -22.511 27.564  1.000 26.401  0 69  GLY BBB N     1 ? 2 
ATOM   4123  C CA    . GLY B 1 69  ? 52.857  -23.412 28.666  1.000 26.872  0 69  GLY BBB CA    1 ? 2 
ATOM   4124  C C     . GLY B 1 69  ? 51.615  -24.223 28.373  1.000 26.764  0 69  GLY BBB C     1 ? 2 
ATOM   4125  O O     . GLY B 1 69  ? 51.216  -24.297 27.206  1.000 26.610  0 69  GLY BBB O     1 ? 2 
ATOM   4126  N N     . LEU B 1 70  ? 51.074  -24.845 29.416  1.000 26.540  0 70  LEU BBB N     1 ? 2 
ATOM   4127  C CA    . LEU B 1 70  ? 49.895  -25.738 29.405  1.000 25.751  0 70  LEU BBB CA    1 ? 2 
ATOM   4128  C C     . LEU B 1 70  ? 48.634  -24.987 28.948  1.000 25.817  0 70  LEU BBB C     1 ? 2 
ATOM   4129  O O     . LEU B 1 70  ? 48.502  -23.772 29.265  1.000 27.377  0 70  LEU BBB O     1 ? 2 
ATOM   4130  C CB    . LEU B 1 70  ? 49.703  -26.261 30.834  1.000 25.257  0 70  LEU BBB CB    1 ? 2 
ATOM   4131  C CG    . LEU B 1 70  ? 48.451  -27.116 31.064  1.000 24.443  0 70  LEU BBB CG    1 ? 2 
ATOM   4132  C CD1   . LEU B 1 70  ? 48.497  -28.415 30.305  1.000 24.039  0 70  LEU BBB CD1   1 ? 2 
ATOM   4133  C CD2   . LEU B 1 70  ? 48.312  -27.449 32.507  1.000 24.890  0 70  LEU BBB CD2   1 ? 2 
ATOM   4134  N N     . GLY B 1 71  ? 47.705  -25.697 28.314  1.000 24.157  0 71  GLY BBB N     1 ? 2 
ATOM   4135  C CA    . GLY B 1 71  ? 46.333  -25.202 28.050  1.000 23.407  0 71  GLY BBB CA    1 ? 2 
ATOM   4136  C C     . GLY B 1 71  ? 45.967  -25.304 26.580  1.000 22.244  0 71  GLY BBB C     1 ? 2 
ATOM   4137  O O     . GLY B 1 71  ? 44.765  -25.219 26.261  1.000 23.403  0 71  GLY BBB O     1 ? 2 
ATOM   4138  N N     . GLY B 1 72  ? 46.953  -25.480 25.717  1.000 21.041  0 72  GLY BBB N     1 ? 2 
ATOM   4139  C CA    . GLY B 1 72  ? 46.712  -25.838 24.322  1.000 21.759  0 72  GLY BBB CA    1 ? 2 
ATOM   4140  C C     . GLY B 1 72  ? 46.490  -24.601 23.469  1.000 21.957  0 72  GLY BBB C     1 ? 2 
ATOM   4141  O O     . GLY B 1 72  ? 46.901  -23.512 23.882  1.000 23.086  0 72  GLY BBB O     1 ? 2 
ATOM   4142  N N     . THR B 1 73  ? 45.912  -24.773 22.295  1.000 21.950  0 73  THR BBB N     1 ? 2 
ATOM   4143  C CA    . THR B 1 73  ? 45.871  -23.713 21.257  1.000 23.807  0 73  THR BBB CA    1 ? 2 
ATOM   4144  C C     . THR B 1 73  ? 44.994  -22.537 21.732  1.000 24.632  0 73  THR BBB C     1 ? 2 
ATOM   4145  O O     . THR B 1 73  ? 45.384  -21.380 21.557  1.000 23.225  0 73  THR BBB O     1 ? 2 
ATOM   4146  C CB    . THR B 1 73  ? 45.392  -24.326 19.936  1.000 23.609  0 73  THR BBB CB    1 ? 2 
ATOM   4147  O OG1   . THR B 1 73  ? 46.336  -25.336 19.593  1.000 21.873  0 73  THR BBB OG1   1 ? 2 
ATOM   4148  C CG2   . THR B 1 73  ? 45.216  -23.282 18.853  1.000 24.601  0 73  THR BBB CG2   1 ? 2 
ATOM   4149  N N     . CYS B 1 74  ? 43.830  -22.811 22.289  1.000 26.629  0 74  CYS BBB N     1 ? 2 
ATOM   4150  C CA    A CYS B 1 74  ? 42.884  -21.736 22.639  0.500 27.440  0 74  CYS BBB CA    1 ? 2 
ATOM   4151  C CA    B CYS B 1 74  ? 42.831  -21.819 22.775  0.500 29.110  0 74  CYS BBB CA    1 ? 2 
ATOM   4152  C C     . CYS B 1 74  ? 43.518  -20.797 23.683  1.000 28.158  0 74  CYS BBB C     1 ? 2 
ATOM   4153  O O     . CYS B 1 74  ? 43.407  -19.579 23.476  1.000 29.080  0 74  CYS BBB O     1 ? 2 
ATOM   4154  C CB    A CYS B 1 74  ? 41.542  -22.286 23.091  0.500 28.771  0 74  CYS BBB CB    1 ? 2 
ATOM   4155  C CB    B CYS B 1 74  ? 41.820  -22.558 23.661  0.500 33.159  0 74  CYS BBB CB    1 ? 2 
ATOM   4156  S SG    A CYS B 1 74  ? 40.340  -20.945 23.313  0.500 29.965  0 74  CYS BBB SG    1 ? 2 
ATOM   4157  S SG    B CYS B 1 74  ? 40.466  -21.608 24.415  0.500 37.136  0 74  CYS BBB SG    1 ? 2 
ATOM   4158  N N     . VAL B 1 75  ? 44.181  -21.326 24.709  1.000 25.874  0 75  VAL BBB N     1 ? 2 
ATOM   4159  C CA    . VAL B 1 75  ? 44.754  -20.552 25.837  1.000 24.092  0 75  VAL BBB CA    1 ? 2 
ATOM   4160  C C     . VAL B 1 75  ? 45.925  -19.730 25.336  1.000 22.540  0 75  VAL BBB C     1 ? 2 
ATOM   4161  O O     . VAL B 1 75  ? 46.042  -18.504 25.750  1.000 20.847  0 75  VAL BBB O     1 ? 2 
ATOM   4162  C CB    . VAL B 1 75  ? 45.190  -21.476 26.985  1.000 24.269  0 75  VAL BBB CB    1 ? 2 
ATOM   4163  C CG1   . VAL B 1 75  ? 46.056  -20.733 27.969  1.000 23.502  0 75  VAL BBB CG1   1 ? 2 
ATOM   4164  C CG2   . VAL B 1 75  ? 43.961  -22.064 27.662  1.000 24.861  0 75  VAL BBB CG2   1 ? 2 
ATOM   4165  N N     . ASN B 1 76  ? 46.798  -20.365 24.546  1.000 21.147  0 76  ASN BBB N     1 ? 2 
ATOM   4166  C CA    . ASN B 1 76  ? 48.154  -19.821 24.288  1.000 20.985  0 76  ASN BBB CA    1 ? 2 
ATOM   4167  C C     . ASN B 1 76  ? 48.213  -19.051 22.967  1.000 21.148  0 76  ASN BBB C     1 ? 2 
ATOM   4168  O O     . ASN B 1 76  ? 48.885  -18.016 22.950  1.000 20.742  0 76  ASN BBB O     1 ? 2 
ATOM   4169  C CB    . ASN B 1 76  ? 49.190  -20.944 24.372  1.000 21.400  0 76  ASN BBB CB    1 ? 2 
ATOM   4170  C CG    . ASN B 1 76  ? 49.305  -21.479 25.784  1.000 20.612  0 76  ASN BBB CG    1 ? 2 
ATOM   4171  O OD1   . ASN B 1 76  ? 49.941  -20.860 26.638  1.000 19.514  0 76  ASN BBB OD1   1 ? 2 
ATOM   4172  N ND2   . ASN B 1 76  ? 48.627  -22.593 26.031  1.000 20.790  0 76  ASN BBB ND2   1 ? 2 
ATOM   4173  N N     . VAL B 1 77  ? 47.583  -19.551 21.894  1.000 21.371  0 77  VAL BBB N     1 ? 2 
ATOM   4174  C CA    . VAL B 1 77  ? 47.865  -19.066 20.517  1.000 21.798  0 77  VAL BBB CA    1 ? 2 
ATOM   4175  C C     . VAL B 1 77  ? 46.574  -19.115 19.715  1.000 23.099  0 77  VAL BBB C     1 ? 2 
ATOM   4176  O O     . VAL B 1 77  ? 46.624  -19.291 18.487  1.000 25.166  0 77  VAL BBB O     1 ? 2 
ATOM   4177  C CB    . VAL B 1 77  ? 49.004  -19.865 19.838  1.000 21.453  0 77  VAL BBB CB    1 ? 2 
ATOM   4178  C CG1   . VAL B 1 77  ? 50.385  -19.519 20.399  1.000 21.416  0 77  VAL BBB CG1   1 ? 2 
ATOM   4179  C CG2   . VAL B 1 77  ? 48.784  -21.366 19.865  1.000 21.296  0 77  VAL BBB CG2   1 ? 2 
ATOM   4180  N N     . GLY B 1 78  ? 45.437  -18.912 20.358  1.000 24.370  0 78  GLY BBB N     1 ? 2 
ATOM   4181  C CA    . GLY B 1 78  ? 44.136  -18.952 19.667  1.000 24.140  0 78  GLY BBB CA    1 ? 2 
ATOM   4182  C C     . GLY B 1 78  ? 43.147  -18.026 20.289  1.000 23.589  0 78  GLY BBB C     1 ? 2 
ATOM   4183  O O     . GLY B 1 78  ? 43.427  -16.831 20.335  1.000 24.155  0 78  GLY BBB O     1 ? 2 
ATOM   4184  N N     . CYS B 1 79  ? 42.009  -18.555 20.715  1.000 24.317  0 79  CYS BBB N     1 ? 2 
ATOM   4185  C CA    . CYS B 1 79  ? 40.829  -17.741 21.086  1.000 25.329  0 79  CYS BBB CA    1 ? 2 
ATOM   4186  C C     . CYS B 1 79  ? 41.235  -16.680 22.094  1.000 23.929  0 79  CYS BBB C     1 ? 2 
ATOM   4187  O O     . CYS B 1 79  ? 40.819  -15.520 21.909  1.000 25.110  0 79  CYS BBB O     1 ? 2 
ATOM   4188  C CB    . CYS B 1 79  ? 39.695  -18.589 21.668  1.000 29.701  0 79  CYS BBB CB    1 ? 2 
ATOM   4189  S SG    . CYS B 1 79  ? 39.842  -20.385 21.415  1.000 32.147  0 79  CYS BBB SG    1 ? 2 
ATOM   4190  N N     . VAL B 1 80  ? 41.997  -17.043 23.131  1.000 22.831  0 80  VAL BBB N     1 ? 2 
ATOM   4191  C CA    . VAL B 1 80  ? 42.272  -16.097 24.255  1.000 22.384  0 80  VAL BBB CA    1 ? 2 
ATOM   4192  C C     . VAL B 1 80  ? 43.097  -14.906 23.768  1.000 22.675  0 80  VAL BBB C     1 ? 2 
ATOM   4193  O O     . VAL B 1 80  ? 42.638  -13.781 23.849  1.000 23.140  0 80  VAL BBB O     1 ? 2 
ATOM   4194  C CB    . VAL B 1 80  ? 42.919  -16.782 25.474  1.000 21.237  0 80  VAL BBB CB    1 ? 2 
ATOM   4195  C CG1   . VAL B 1 80  ? 43.418  -15.754 26.465  1.000 21.602  0 80  VAL BBB CG1   1 ? 2 
ATOM   4196  C CG2   . VAL B 1 80  ? 41.985  -17.738 26.154  1.000 20.664  0 80  VAL BBB CG2   1 ? 2 
ATOM   4197  N N     . PRO B 1 81  ? 44.343  -15.075 23.284  1.000 23.074  0 81  PRO BBB N     1 ? 2 
ATOM   4198  C CA    . PRO B 1 81  ? 45.119  -13.939 22.797  1.000 23.369  0 81  PRO BBB CA    1 ? 2 
ATOM   4199  C C     . PRO B 1 81  ? 44.449  -13.210 21.628  1.000 24.119  0 81  PRO BBB C     1 ? 2 
ATOM   4200  O O     . PRO B 1 81  ? 44.578  -12.011 21.583  1.000 25.097  0 81  PRO BBB O     1 ? 2 
ATOM   4201  C CB    . PRO B 1 81  ? 46.483  -14.518 22.340  1.000 23.710  0 81  PRO BBB CB    1 ? 2 
ATOM   4202  C CG    . PRO B 1 81  ? 46.284  -15.999 22.310  1.000 24.316  0 81  PRO BBB CG    1 ? 2 
ATOM   4203  C CD    . PRO B 1 81  ? 45.083  -16.328 23.191  1.000 23.259  0 81  PRO BBB CD    1 ? 2 
ATOM   4204  N N     . LYS B 1 82  ? 43.774  -13.914 20.714  1.000 25.107  0 82  LYS BBB N     1 ? 2 
ATOM   4205  C CA    . LYS B 1 82  ? 43.092  -13.264 19.556  1.000 26.826  0 82  LYS BBB CA    1 ? 2 
ATOM   4206  C C     . LYS B 1 82  ? 42.057  -12.276 20.127  1.000 26.071  0 82  LYS BBB C     1 ? 2 
ATOM   4207  O O     . LYS B 1 82  ? 42.031  -11.116 19.685  1.000 25.879  0 82  LYS BBB O     1 ? 2 
ATOM   4208  C CB    . LYS B 1 82  ? 42.463  -14.331 18.647  1.000 30.317  0 82  LYS BBB CB    1 ? 2 
ATOM   4209  C CG    . LYS B 1 82  ? 41.518  -13.827 17.549  1.000 32.648  0 82  LYS BBB CG    1 ? 2 
ATOM   4210  C CD    . LYS B 1 82  ? 40.058  -13.581 17.979  1.000 34.048  0 82  LYS BBB CD    1 ? 2 
ATOM   4211  C CE    . LYS B 1 82  ? 39.292  -14.796 18.493  1.000 34.134  0 82  LYS BBB CE    1 ? 2 
ATOM   4212  N NZ    . LYS B 1 82  ? 39.106  -15.869 17.486  1.000 35.511  0 82  LYS BBB NZ    1 ? 2 
ATOM   4213  N N     . LYS B 1 83  ? 41.286  -12.695 21.137  1.000 24.456  0 83  LYS BBB N     1 ? 2 
ATOM   4214  C CA    . LYS B 1 83  ? 40.224  -11.861 21.748  1.000 24.026  0 83  LYS BBB CA    1 ? 2 
ATOM   4215  C C     . LYS B 1 83  ? 40.845  -10.667 22.492  1.000 23.961  0 83  LYS BBB C     1 ? 2 
ATOM   4216  O O     . LYS B 1 83  ? 40.268  -9.550  22.441  1.000 23.063  0 83  LYS BBB O     1 ? 2 
ATOM   4217  C CB    . LYS B 1 83  ? 39.341  -12.724 22.637  1.000 24.199  0 83  LYS BBB CB    1 ? 2 
ATOM   4218  C CG    . LYS B 1 83  ? 38.157  -11.996 23.254  1.000 24.751  0 83  LYS BBB CG    1 ? 2 
ATOM   4219  C CD    . LYS B 1 83  ? 36.974  -11.839 22.333  1.000 25.194  0 83  LYS BBB CD    1 ? 2 
ATOM   4220  C CE    . LYS B 1 83  ? 35.921  -10.906 22.875  1.000 25.929  0 83  LYS BBB CE    1 ? 2 
ATOM   4221  N NZ    . LYS B 1 83  ? 34.695  -11.628 23.251  1.000 26.186  0 83  LYS BBB NZ    1 ? 2 
ATOM   4222  N N     . LEU B 1 84  ? 42.011  -10.830 23.127  1.000 23.437  0 84  LEU BBB N     1 ? 2 
ATOM   4223  C CA    . LEU B 1 84  ? 42.692  -9.673  23.765  1.000 23.250  0 84  LEU BBB CA    1 ? 2 
ATOM   4224  C C     . LEU B 1 84  ? 43.184  -8.705  22.672  1.000 24.229  0 84  LEU BBB C     1 ? 2 
ATOM   4225  O O     . LEU B 1 84  ? 43.016  -7.452  22.831  1.000 23.645  0 84  LEU BBB O     1 ? 2 
ATOM   4226  C CB    . LEU B 1 84  ? 43.825  -10.198 24.648  1.000 23.140  0 84  LEU BBB CB    1 ? 2 
ATOM   4227  C CG    . LEU B 1 84  ? 43.357  -11.033 25.843  1.000 22.201  0 84  LEU BBB CG    1 ? 2 
ATOM   4228  C CD1   . LEU B 1 84  ? 44.548  -11.639 26.589  1.000 21.651  0 84  LEU BBB CD1   1 ? 2 
ATOM   4229  C CD2   . LEU B 1 84  ? 42.518  -10.187 26.779  1.000 22.136  0 84  LEU BBB CD2   1 ? 2 
ATOM   4230  N N     . MET B 1 85  ? 43.722  -9.227  21.571  1.000 23.352  0 85  MET BBB N     1 ? 2 
ATOM   4231  C CA    . MET B 1 85  ? 44.158  -8.324  20.485  1.000 24.377  0 85  MET BBB CA    1 ? 2 
ATOM   4232  C C     . MET B 1 85  ? 42.932  -7.611  19.893  1.000 21.969  0 85  MET BBB C     1 ? 2 
ATOM   4233  O O     . MET B 1 85  ? 43.022  -6.413  19.646  1.000 22.278  0 85  MET BBB O     1 ? 2 
ATOM   4234  C CB    . MET B 1 85  ? 44.925  -9.062  19.390  1.000 26.730  0 85  MET BBB CB    1 ? 2 
ATOM   4235  C CG    . MET B 1 85  ? 46.113  -9.801  19.902  1.000 29.443  0 85  MET BBB CG    1 ? 2 
ATOM   4236  S SD    . MET B 1 85  ? 47.667  -8.985  19.796  1.000 33.574  0 85  MET BBB SD    1 ? 2 
ATOM   4237  C CE    . MET B 1 85  ? 47.790  -8.786  18.040  1.000 35.503  0 85  MET BBB CE    1 ? 2 
ATOM   4238  N N     . HIS B 1 86  ? 41.832  -8.307  19.674  1.000 21.053  0 86  HIS BBB N     1 ? 2 
ATOM   4239  C CA    . HIS B 1 86  ? 40.539  -7.744  19.169  1.000 20.884  0 86  HIS BBB CA    1 ? 2 
ATOM   4240  C C     . HIS B 1 86  ? 40.091  -6.603  20.086  1.000 20.316  0 86  HIS BBB C     1 ? 2 
ATOM   4241  O O     . HIS B 1 86  ? 39.761  -5.516  19.561  1.000 20.635  0 86  HIS BBB O     1 ? 2 
ATOM   4242  C CB    . HIS B 1 86  ? 39.510  -8.868  19.052  1.000 21.368  0 86  HIS BBB CB    1 ? 2 
ATOM   4243  C CG    . HIS B 1 86  ? 38.138  -8.446  18.648  1.000 22.720  0 86  HIS BBB CG    1 ? 2 
ATOM   4244  N ND1   . HIS B 1 86  ? 37.879  -7.808  17.432  1.000 22.666  0 86  HIS BBB ND1   1 ? 2 
ATOM   4245  C CD2   . HIS B 1 86  ? 36.934  -8.591  19.275  1.000 23.115  0 86  HIS BBB CD2   1 ? 2 
ATOM   4246  C CE1   . HIS B 1 86  ? 36.593  -7.607  17.316  1.000 22.758  0 86  HIS BBB CE1   1 ? 2 
ATOM   4247  N NE2   . HIS B 1 86  ? 35.983  -8.059  18.453  1.000 23.015  0 86  HIS BBB NE2   1 ? 2 
ATOM   4248  N N     . TYR B 1 87  ? 40.189  -6.804  21.402  1.000 19.597  0 87  TYR BBB N     1 ? 2 
ATOM   4249  C CA    . TYR B 1 87  ? 39.800  -5.798  22.415  1.000 19.982  0 87  TYR BBB CA    1 ? 2 
ATOM   4250  C C     . TYR B 1 87  ? 40.659  -4.544  22.234  1.000 19.368  0 87  TYR BBB C     1 ? 2 
ATOM   4251  O O     . TYR B 1 87  ? 40.118  -3.434  22.172  1.000 18.326  0 87  TYR BBB O     1 ? 2 
ATOM   4252  C CB    . TYR B 1 87  ? 39.862  -6.386  23.825  1.000 21.465  0 87  TYR BBB CB    1 ? 2 
ATOM   4253  C CG    . TYR B 1 87  ? 39.212  -5.484  24.836  1.000 25.201  0 87  TYR BBB CG    1 ? 2 
ATOM   4254  C CD1   . TYR B 1 87  ? 37.844  -5.173  24.755  1.000 28.213  0 87  TYR BBB CD1   1 ? 2 
ATOM   4255  C CD2   . TYR B 1 87  ? 39.952  -4.872  25.832  1.000 26.105  0 87  TYR BBB CD2   1 ? 2 
ATOM   4256  C CE1   . TYR B 1 87  ? 37.240  -4.316  25.668  1.000 29.484  0 87  TYR BBB CE1   1 ? 2 
ATOM   4257  C CE2   . TYR B 1 87  ? 39.361  -4.027  26.755  1.000 27.780  0 87  TYR BBB CE2   1 ? 2 
ATOM   4258  C CZ    . TYR B 1 87  ? 38.002  -3.758  26.681  1.000 29.872  0 87  TYR BBB CZ    1 ? 2 
ATOM   4259  O OH    . TYR B 1 87  ? 37.438  -2.873  27.556  1.000 32.562  0 87  TYR BBB OH    1 ? 2 
ATOM   4260  N N     . SER B 1 88  ? 41.973  -4.715  22.083  1.000 19.503  0 88  SER BBB N     1 ? 2 
ATOM   4261  C CA    . SER B 1 88  ? 42.916  -3.608  21.830  1.000 19.725  0 88  SER BBB CA    1 ? 2 
ATOM   4262  C C     . SER B 1 88  ? 42.481  -2.887  20.571  1.000 19.031  0 88  SER BBB C     1 ? 2 
ATOM   4263  O O     . SER B 1 88  ? 42.582  -1.670  20.540  1.000 19.087  0 88  SER BBB O     1 ? 2 
ATOM   4264  C CB    . SER B 1 88  ? 44.346  -4.095  21.731  1.000 20.864  0 88  SER BBB CB    1 ? 2 
ATOM   4265  O OG    . SER B 1 88  ? 45.221  -2.979  21.505  1.000 22.109  0 88  SER BBB OG    1 ? 2 
ATOM   4266  N N     . ALA B 1 89  ? 42.064  -3.631  19.556  1.000 19.121  0 89  ALA BBB N     1 ? 2 
ATOM   4267  C CA    . ALA B 1 89  ? 41.627  -3.079  18.242  1.000 19.868  0 89  ALA BBB CA    1 ? 2 
ATOM   4268  C C     . ALA B 1 89  ? 40.351  -2.244  18.428  1.000 20.491  0 89  ALA BBB C     1 ? 2 
ATOM   4269  O O     . ALA B 1 89  ? 40.327  -1.079  17.910  1.000 20.464  0 89  ALA BBB O     1 ? 2 
ATOM   4270  C CB    . ALA B 1 89  ? 41.404  -4.195  17.258  1.000 19.710  0 89  ALA BBB CB    1 ? 2 
ATOM   4271  N N     . LEU B 1 90  ? 39.370  -2.774  19.172  1.000 20.515  0 90  LEU BBB N     1 ? 2 
ATOM   4272  C CA    . LEU B 1 90  ? 38.091  -2.075  19.454  1.000 21.901  0 90  LEU BBB CA    1 ? 2 
ATOM   4273  C C     . LEU B 1 90  ? 38.420  -0.811  20.208  1.000 22.350  0 90  LEU BBB C     1 ? 2 
ATOM   4274  O O     . LEU B 1 90  ? 37.749  0.178   19.995  1.000 21.764  0 90  LEU BBB O     1 ? 2 
ATOM   4275  C CB    . LEU B 1 90  ? 37.112  -2.942  20.278  1.000 21.863  0 90  LEU BBB CB    1 ? 2 
ATOM   4276  C CG    . LEU B 1 90  ? 36.522  -4.123  19.516  1.000 21.680  0 90  LEU BBB CG    1 ? 2 
ATOM   4277  C CD1   . LEU B 1 90  ? 35.640  -4.999  20.423  1.000 21.545  0 90  LEU BBB CD1   1 ? 2 
ATOM   4278  C CD2   . LEU B 1 90  ? 35.807  -3.673  18.253  1.000 21.458  0 90  LEU BBB CD2   1 ? 2 
ATOM   4279  N N     . ILE B 1 91  ? 39.462  -0.843  21.033  1.000 24.920  0 91  ILE BBB N     1 ? 2 
ATOM   4280  C CA    . ILE B 1 91  ? 39.854  0.365   21.824  1.000 25.432  0 91  ILE BBB CA    1 ? 2 
ATOM   4281  C C     . ILE B 1 91  ? 40.406  1.392   20.842  1.000 27.040  0 91  ILE BBB C     1 ? 2 
ATOM   4282  O O     . ILE B 1 91  ? 39.911  2.544   20.888  1.000 27.005  0 91  ILE BBB O     1 ? 2 
ATOM   4283  C CB    . ILE B 1 91  ? 40.806  0.031   22.975  1.000 24.432  0 91  ILE BBB CB    1 ? 2 
ATOM   4284  C CG1   . ILE B 1 91  ? 40.043  -0.721  24.055  1.000 23.936  0 91  ILE BBB CG1   1 ? 2 
ATOM   4285  C CG2   . ILE B 1 91  ? 41.466  1.298   23.508  1.000 24.688  0 91  ILE BBB CG2   1 ? 2 
ATOM   4286  C CD1   . ILE B 1 91  ? 40.853  -1.034  25.302  1.000 24.130  0 91  ILE BBB CD1   1 ? 2 
ATOM   4287  N N     . ALA B 1 92  ? 41.355  0.992   19.988  1.000 27.511  0 92  ALA BBB N     1 ? 2 
ATOM   4288  C CA    . ALA B 1 92  ? 41.871  1.862   18.889  1.000 28.724  0 92  ALA BBB CA    1 ? 2 
ATOM   4289  C C     . ALA B 1 92  ? 40.703  2.518   18.119  1.000 29.163  0 92  ALA BBB C     1 ? 2 
ATOM   4290  O O     . ALA B 1 92  ? 40.659  3.745   17.970  1.000 28.324  0 92  ALA BBB O     1 ? 2 
ATOM   4291  C CB    . ALA B 1 92  ? 42.726  1.029   17.964  1.000 28.536  0 92  ALA BBB CB    1 ? 2 
ATOM   4292  N N     . SER B 1 93  ? 39.782  1.691   17.631  1.000 30.173  0 93  SER BBB N     1 ? 2 
ATOM   4293  C CA    . SER B 1 93  ? 38.606  2.119   16.833  1.000 31.752  0 93  SER BBB CA    1 ? 2 
ATOM   4294  C C     . SER B 1 93  ? 37.747  3.151   17.605  1.000 30.780  0 93  SER BBB C     1 ? 2 
ATOM   4295  O O     . SER B 1 93  ? 37.453  4.242   17.096  1.000 30.774  0 93  SER BBB O     1 ? 2 
ATOM   4296  C CB    . SER B 1 93  ? 37.835  0.916   16.458  1.000 32.168  0 93  SER BBB CB    1 ? 2 
ATOM   4297  O OG    . SER B 1 93  ? 36.709  1.271   15.689  1.000 36.100  0 93  SER BBB OG    1 ? 2 
ATOM   4298  N N     . SER B 1 94  ? 37.387  2.821   18.823  1.000 29.223  0 94  SER BBB N     1 ? 2 
ATOM   4299  C CA    . SER B 1 94  ? 36.599  3.689   19.729  1.000 29.790  0 94  SER BBB CA    1 ? 2 
ATOM   4300  C C     . SER B 1 94  ? 37.328  5.029   19.941  1.000 29.266  0 94  SER BBB C     1 ? 2 
ATOM   4301  O O     . SER B 1 94  ? 36.669  6.070   19.933  1.000 29.022  0 94  SER BBB O     1 ? 2 
ATOM   4302  C CB    . SER B 1 94  ? 36.346  2.933   20.999  1.000 29.975  0 94  SER BBB CB    1 ? 2 
ATOM   4303  O OG    . SER B 1 94  ? 36.307  3.809   22.103  1.000 35.781  0 94  SER BBB OG    1 ? 2 
ATOM   4304  N N     . ILE B 1 95  ? 38.649  5.011   20.106  1.000 28.883  0 95  ILE BBB N     1 ? 2 
ATOM   4305  C CA    . ILE B 1 95  ? 39.476  6.230   20.312  1.000 29.181  0 95  ILE BBB CA    1 ? 2 
ATOM   4306  C C     . ILE B 1 95  ? 39.533  7.044   19.020  1.000 28.105  0 95  ILE BBB C     1 ? 2 
ATOM   4307  O O     . ILE B 1 95  ? 39.334  8.240   19.104  1.000 26.852  0 95  ILE BBB O     1 ? 2 
ATOM   4308  C CB    . ILE B 1 95  ? 40.905  5.900   20.795  1.000 30.645  0 95  ILE BBB CB    1 ? 2 
ATOM   4309  C CG1   . ILE B 1 95  ? 40.897  5.438   22.250  1.000 28.537  0 95  ILE BBB CG1   1 ? 2 
ATOM   4310  C CG2   . ILE B 1 95  ? 41.854  7.095   20.562  1.000 31.917  0 95  ILE BBB CG2   1 ? 2 
ATOM   4311  C CD1   . ILE B 1 95  ? 42.247  5.031   22.764  1.000 29.191  0 95  ILE BBB CD1   1 ? 2 
ATOM   4312  N N     . HIS B 1 96  ? 39.809  6.425   17.882  1.000 28.742  0 96  HIS BBB N     1 ? 2 
ATOM   4313  C CA    . HIS B 1 96  ? 39.858  7.128   16.579  1.000 31.094  0 96  HIS BBB CA    1 ? 2 
ATOM   4314  C C     . HIS B 1 96  ? 38.488  7.734   16.249  1.000 31.794  0 96  HIS BBB C     1 ? 2 
ATOM   4315  O O     . HIS B 1 96  ? 38.436  8.948   15.992  1.000 30.692  0 96  HIS BBB O     1 ? 2 
ATOM   4316  C CB    . HIS B 1 96  ? 40.354  6.213   15.479  1.000 32.874  0 96  HIS BBB CB    1 ? 2 
ATOM   4317  C CG    . HIS B 1 96  ? 40.477  6.908   14.165  1.000 38.244  0 96  HIS BBB CG    1 ? 2 
ATOM   4318  N ND1   . HIS B 1 96  ? 39.622  6.641   13.093  1.000 42.492  0 96  HIS BBB ND1   1 ? 2 
ATOM   4319  C CD2   . HIS B 1 96  ? 41.344  7.852   13.736  1.000 40.616  0 96  HIS BBB CD2   1 ? 2 
ATOM   4320  C CE1   . HIS B 1 96  ? 39.960  7.387   12.067  1.000 42.935  0 96  HIS BBB CE1   1 ? 2 
ATOM   4321  N NE2   . HIS B 1 96  ? 41.026  8.132   12.443  1.000 43.003  0 96  HIS BBB NE2   1 ? 2 
ATOM   4322  N N     . HIS B 1 97  ? 37.414  6.922   16.279  1.000 32.342  0 97  HIS BBB N     1 ? 2 
ATOM   4323  C CA    . HIS B 1 97  ? 36.101  7.269   15.682  1.000 31.424  0 97  HIS BBB CA    1 ? 2 
ATOM   4324  C C     . HIS B 1 97  ? 35.183  7.973   16.679  1.000 31.731  0 97  HIS BBB C     1 ? 2 
ATOM   4325  O O     . HIS B 1 97  ? 34.426  8.813   16.236  1.000 34.396  0 97  HIS BBB O     1 ? 2 
ATOM   4326  C CB    . HIS B 1 97  ? 35.391  6.034   15.182  1.000 30.410  0 97  HIS BBB CB    1 ? 2 
ATOM   4327  C CG    . HIS B 1 97  ? 36.007  5.437   13.974  1.000 29.929  0 97  HIS BBB CG    1 ? 2 
ATOM   4328  N ND1   . HIS B 1 97  ? 36.049  6.105   12.770  1.000 29.375  0 97  HIS BBB ND1   1 ? 2 
ATOM   4329  C CD2   . HIS B 1 97  ? 36.558  4.209   13.784  1.000 29.782  0 97  HIS BBB CD2   1 ? 2 
ATOM   4330  C CE1   . HIS B 1 97  ? 36.641  5.327   11.889  1.000 30.612  0 97  HIS BBB CE1   1 ? 2 
ATOM   4331  N NE2   . HIS B 1 97  ? 36.963  4.143   12.497  1.000 30.086  0 97  HIS BBB NE2   1 ? 2 
ATOM   4332  N N     . ASP B 1 98  ? 35.204  7.594   17.952  1.000 31.010  0 98  ASP BBB N     1 ? 2 
ATOM   4333  C CA    . ASP B 1 98  ? 34.065  7.833   18.880  1.000 30.524  0 98  ASP BBB CA    1 ? 2 
ATOM   4334  C C     . ASP B 1 98  ? 34.412  8.783   20.032  1.000 29.884  0 98  ASP BBB C     1 ? 2 
ATOM   4335  O O     . ASP B 1 98  ? 33.510  9.545   20.457  1.000 27.190  0 98  ASP BBB O     1 ? 2 
ATOM   4336  C CB    . ASP B 1 98  ? 33.597  6.540   19.554  1.000 30.299  0 98  ASP BBB CB    1 ? 2 
ATOM   4337  C CG    . ASP B 1 98  ? 32.993  5.510   18.626  1.000 29.867  0 98  ASP BBB CG    1 ? 2 
ATOM   4338  O OD1   . ASP B 1 98  ? 32.792  5.815   17.445  1.000 30.081  0 98  ASP BBB OD1   1 ? 2 
ATOM   4339  O OD2   . ASP B 1 98  ? 32.765  4.405   19.116  1.000 29.627  0 98  ASP BBB OD2   1 ? 2 
ATOM   4340  N N     . ALA B 1 99  ? 35.640  8.732   20.534  1.000 30.733  0 99  ALA BBB N     1 ? 2 
ATOM   4341  C CA    . ALA B 1 99  ? 35.991  9.355   21.828  1.000 32.977  0 99  ALA BBB CA    1 ? 2 
ATOM   4342  C C     . ALA B 1 99  ? 35.685  10.854  21.782  1.000 35.578  0 99  ALA BBB C     1 ? 2 
ATOM   4343  O O     . ALA B 1 99  ? 34.994  11.356  22.687  1.000 36.902  0 99  ALA BBB O     1 ? 2 
ATOM   4344  C CB    . ALA B 1 99  ? 37.434  9.101   22.164  1.000 32.916  0 99  ALA BBB CB    1 ? 2 
ATOM   4345  N N     . GLN B 1 100 ? 36.185  11.551  20.766  1.000 37.635  0 100 GLN BBB N     1 ? 2 
ATOM   4346  C CA    . GLN B 1 100 ? 36.020  13.018  20.641  1.000 39.904  0 100 GLN BBB CA    1 ? 2 
ATOM   4347  C C     . GLN B 1 100 ? 34.519  13.338  20.548  1.000 37.336  0 100 GLN BBB C     1 ? 2 
ATOM   4348  O O     . GLN B 1 100 ? 34.055  14.257  21.269  1.000 38.456  0 100 GLN BBB O     1 ? 2 
ATOM   4349  C CB    . GLN B 1 100 ? 36.865  13.539  19.479  1.000 42.500  0 100 GLN BBB CB    1 ? 2 
ATOM   4350  C CG    . GLN B 1 100 ? 36.646  15.011  19.182  1.000 45.352  0 100 GLN BBB CG    1 ? 2 
ATOM   4351  C CD    . GLN B 1 100 ? 37.688  15.572  18.221  1.000 50.876  0 100 GLN BBB CD    1 ? 2 
ATOM   4352  O OE1   . GLN B 1 100 ? 38.482  14.838  17.585  1.000 49.903  0 100 GLN BBB OE1   1 ? 2 
ATOM   4353  N NE2   . GLN B 1 100 ? 37.720  16.905  18.134  1.000 49.520  0 100 GLN BBB NE2   1 ? 2 
ATOM   4354  N N     . MET B 1 101 ? 33.779  12.605  19.723  1.000 33.961  0 101 MET BBB N     1 ? 2 
ATOM   4355  C CA    . MET B 1 101 ? 32.325  12.841  19.511  1.000 34.243  0 101 MET BBB CA    1 ? 2 
ATOM   4356  C C     . MET B 1 101 ? 31.557  12.737  20.838  1.000 32.901  0 101 MET BBB C     1 ? 2 
ATOM   4357  O O     . MET B 1 101 ? 30.522  13.424  20.978  1.000 36.358  0 101 MET BBB O     1 ? 2 
ATOM   4358  C CB    . MET B 1 101 ? 31.737  11.834  18.509  1.000 34.751  0 101 MET BBB CB    1 ? 2 
ATOM   4359  C CG    . MET B 1 101 ? 32.074  12.118  17.054  1.000 35.763  0 101 MET BBB CG    1 ? 2 
ATOM   4360  S SD    . MET B 1 101 ? 31.406  13.765  16.557  1.000 39.863  0 101 MET BBB SD    1 ? 2 
ATOM   4361  C CE    . MET B 1 101 ? 29.637  13.465  16.545  1.000 38.228  0 101 MET BBB CE    1 ? 2 
ATOM   4362  N N     . PHE B 1 102 ? 31.991  11.867  21.741  1.000 29.327  0 102 PHE BBB N     1 ? 2 
ATOM   4363  C CA    . PHE B 1 102 ? 31.307  11.607  23.026  1.000 29.329  0 102 PHE BBB CA    1 ? 2 
ATOM   4364  C C     . PHE B 1 102 ? 31.991  12.418  24.137  1.000 28.996  0 102 PHE BBB C     1 ? 2 
ATOM   4365  O O     . PHE B 1 102 ? 31.798  12.086  25.317  1.000 27.733  0 102 PHE BBB O     1 ? 2 
ATOM   4366  C CB    . PHE B 1 102 ? 31.228  10.095  23.317  1.000 28.647  0 102 PHE BBB CB    1 ? 2 
ATOM   4367  C CG    . PHE B 1 102 ? 30.171  9.431   22.495  1.000 28.562  0 102 PHE BBB CG    1 ? 2 
ATOM   4368  C CD1   . PHE B 1 102 ? 30.403  9.066   21.186  1.000 27.918  0 102 PHE BBB CD1   1 ? 2 
ATOM   4369  C CD2   . PHE B 1 102 ? 28.898  9.261   23.015  1.000 29.525  0 102 PHE BBB CD2   1 ? 2 
ATOM   4370  C CE1   . PHE B 1 102 ? 29.373  8.578   20.403  1.000 28.675  0 102 PHE BBB CE1   1 ? 2 
ATOM   4371  C CE2   . PHE B 1 102 ? 27.884  8.720   22.228  1.000 28.692  0 102 PHE BBB CE2   1 ? 2 
ATOM   4372  C CZ    . PHE B 1 102 ? 28.127  8.379   20.937  1.000 27.472  0 102 PHE BBB CZ    1 ? 2 
ATOM   4373  N N     . GLY B 1 103 ? 32.759  13.446  23.755  1.000 30.310  0 103 GLY BBB N     1 ? 2 
ATOM   4374  C CA    . GLY B 1 103 ? 33.256  14.527  24.632  1.000 29.362  0 103 GLY BBB CA    1 ? 2 
ATOM   4375  C C     . GLY B 1 103 ? 34.647  14.260  25.155  1.000 30.097  0 103 GLY BBB C     1 ? 2 
ATOM   4376  O O     . GLY B 1 103 ? 35.126  15.040  26.023  1.000 29.455  0 103 GLY BBB O     1 ? 2 
ATOM   4377  N N     . HIS B 1 104 ? 35.283  13.177  24.714  1.000 31.190  0 104 HIS BBB N     1 ? 2 
ATOM   4378  C CA    . HIS B 1 104 ? 36.632  12.783  25.206  1.000 32.658  0 104 HIS BBB CA    1 ? 2 
ATOM   4379  C C     . HIS B 1 104 ? 37.655  13.107  24.127  1.000 34.889  0 104 HIS BBB C     1 ? 2 
ATOM   4380  O O     . HIS B 1 104 ? 37.828  12.241  23.248  1.000 34.782  0 104 HIS BBB O     1 ? 2 
ATOM   4381  C CB    . HIS B 1 104 ? 36.649  11.309  25.627  1.000 31.250  0 104 HIS BBB CB    1 ? 2 
ATOM   4382  C CG    . HIS B 1 104 ? 35.669  10.987  26.701  1.000 29.080  0 104 HIS BBB CG    1 ? 2 
ATOM   4383  N ND1   . HIS B 1 104 ? 35.936  11.230  28.035  1.000 28.518  0 104 HIS BBB ND1   1 ? 2 
ATOM   4384  C CD2   . HIS B 1 104 ? 34.434  10.437  26.630  1.000 28.729  0 104 HIS BBB CD2   1 ? 2 
ATOM   4385  C CE1   . HIS B 1 104 ? 34.912  10.832  28.762  1.000 27.903  0 104 HIS BBB CE1   1 ? 2 
ATOM   4386  N NE2   . HIS B 1 104 ? 33.948  10.355  27.917  1.000 28.058  0 104 HIS BBB NE2   1 ? 2 
ATOM   4387  N N     . LYS B 1 105 ? 38.223  14.324  24.129  1.000 39.671  0 105 LYS BBB N     1 ? 2 
ATOM   4388  C CA    . LYS B 1 105 ? 39.337  14.697  23.205  1.000 42.847  0 105 LYS BBB CA    1 ? 2 
ATOM   4389  C C     . LYS B 1 105 ? 40.602  13.945  23.655  1.000 42.033  0 105 LYS BBB C     1 ? 2 
ATOM   4390  O O     . LYS B 1 105 ? 41.061  14.139  24.796  1.000 40.624  0 105 LYS BBB O     1 ? 2 
ATOM   4391  C CB    . LYS B 1 105 ? 39.574  16.205  23.125  1.000 46.123  0 105 LYS BBB CB    1 ? 2 
ATOM   4392  C CG    . LYS B 1 105 ? 40.642  16.628  22.120  1.000 49.551  0 105 LYS BBB CG    1 ? 2 
ATOM   4393  C CD    . LYS B 1 105 ? 40.198  16.494  20.656  1.000 52.576  0 105 LYS BBB CD    1 ? 2 
ATOM   4394  C CE    . LYS B 1 105 ? 41.325  16.429  19.641  1.000 53.069  0 105 LYS BBB CE    1 ? 2 
ATOM   4395  N NZ    . LYS B 1 105 ? 42.068  17.720  19.541  1.000 52.265  0 105 LYS BBB NZ    1 ? 2 
ATOM   4396  N N     . THR B 1 106 ? 41.095  13.062  22.791  1.000 41.385  0 106 THR BBB N     1 ? 2 
ATOM   4397  C CA    . THR B 1 106 ? 42.181  12.122  23.106  1.000 42.386  0 106 THR BBB CA    1 ? 2 
ATOM   4398  C C     . THR B 1 106 ? 43.300  12.225  22.072  1.000 40.690  0 106 THR BBB C     1 ? 2 
ATOM   4399  O O     . THR B 1 106 ? 43.012  12.384  20.881  1.000 45.002  0 106 THR BBB O     1 ? 2 
ATOM   4400  C CB    . THR B 1 106 ? 41.642  10.700  23.093  1.000 41.836  0 106 THR BBB CB    1 ? 2 
ATOM   4401  O OG1   . THR B 1 106 ? 41.313  10.511  21.715  1.000 45.969  0 106 THR BBB OG1   1 ? 2 
ATOM   4402  C CG2   . THR B 1 106 ? 40.482  10.500  24.031  1.000 40.370  0 106 THR BBB CG2   1 ? 2 
ATOM   4403  N N     . SER B 1 107 ? 44.534  12.140  22.522  1.000 38.188  0 107 SER BBB N     1 ? 2 
ATOM   4404  C CA    . SER B 1 107 ? 45.672  11.773  21.638  1.000 38.445  0 107 SER BBB CA    1 ? 2 
ATOM   4405  C C     . SER B 1 107 ? 46.231  10.470  22.177  1.000 36.548  0 107 SER BBB C     1 ? 2 
ATOM   4406  O O     . SER B 1 107 ? 46.203  10.259  23.413  1.000 38.083  0 107 SER BBB O     1 ? 2 
ATOM   4407  C CB    . SER B 1 107 ? 46.728  12.855  21.505  1.000 38.824  0 107 SER BBB CB    1 ? 2 
ATOM   4408  O OG    . SER B 1 107 ? 47.182  13.281  22.767  1.000 37.416  0 107 SER BBB OG    1 ? 2 
ATOM   4409  N N     . SER B 1 108 ? 46.649  9.606   21.273  1.000 35.614  0 108 SER BBB N     1 ? 2 
ATOM   4410  C CA    . SER B 1 108 ? 46.980  8.202   21.582  1.000 34.861  0 108 SER BBB CA    1 ? 2 
ATOM   4411  C C     . SER B 1 108 ? 48.148  7.776   20.705  1.000 35.641  0 108 SER BBB C     1 ? 2 
ATOM   4412  O O     . SER B 1 108 ? 48.180  8.194   19.534  1.000 37.000  0 108 SER BBB O     1 ? 2 
ATOM   4413  C CB    . SER B 1 108 ? 45.771  7.347   21.331  1.000 34.108  0 108 SER BBB CB    1 ? 2 
ATOM   4414  O OG    . SER B 1 108 ? 45.981  6.040   21.822  1.000 33.997  0 108 SER BBB OG    1 ? 2 
ATOM   4415  N N     . SER B 1 109 ? 49.047  6.957   21.231  1.000 34.549  0 109 SER BBB N     1 ? 2 
ATOM   4416  C CA    . SER B 1 109 ? 49.981  6.174   20.387  1.000 34.465  0 109 SER BBB CA    1 ? 2 
ATOM   4417  C C     . SER B 1 109 ? 50.047  4.749   20.915  1.000 32.356  0 109 SER BBB C     1 ? 2 
ATOM   4418  O O     . SER B 1 109 ? 50.038  4.551   22.093  1.000 33.276  0 109 SER BBB O     1 ? 2 
ATOM   4419  C CB    . SER B 1 109 ? 51.365  6.791   20.232  1.000 34.861  0 109 SER BBB CB    1 ? 2 
ATOM   4420  O OG    . SER B 1 109 ? 51.857  7.255   21.449  1.000 33.870  0 109 SER BBB OG    1 ? 2 
ATOM   4421  N N     . PHE B 1 110 ? 50.123  3.828   19.989  1.000 33.146  0 110 PHE BBB N     1 ? 2 
ATOM   4422  C CA    . PHE B 1 110 ? 50.044  2.363   20.177  1.000 34.341  0 110 PHE BBB CA    1 ? 2 
ATOM   4423  C C     . PHE B 1 110 ? 51.450  1.797   20.368  1.000 33.632  0 110 PHE BBB C     1 ? 2 
ATOM   4424  O O     . PHE B 1 110 ? 52.338  2.161   19.612  1.000 35.699  0 110 PHE BBB O     1 ? 2 
ATOM   4425  C CB    . PHE B 1 110 ? 49.400  1.698   18.955  1.000 32.330  0 110 PHE BBB CB    1 ? 2 
ATOM   4426  C CG    . PHE B 1 110 ? 49.391  0.204   19.120  1.000 30.836  0 110 PHE BBB CG    1 ? 2 
ATOM   4427  C CD1   . PHE B 1 110 ? 48.713  -0.358  20.197  1.000 29.024  0 110 PHE BBB CD1   1 ? 2 
ATOM   4428  C CD2   . PHE B 1 110 ? 50.128  -0.621  18.278  1.000 28.861  0 110 PHE BBB CD2   1 ? 2 
ATOM   4429  C CE1   . PHE B 1 110 ? 48.762  -1.724  20.409  1.000 27.551  0 110 PHE BBB CE1   1 ? 2 
ATOM   4430  C CE2   . PHE B 1 110 ? 50.149  -1.982  18.486  1.000 27.806  0 110 PHE BBB CE2   1 ? 2 
ATOM   4431  C CZ    . PHE B 1 110 ? 49.479  -2.524  19.553  1.000 26.874  0 110 PHE BBB CZ    1 ? 2 
ATOM   4432  N N     . GLU B 1 111 ? 51.633  0.933   21.358  1.000 33.234  0 111 GLU BBB N     1 ? 2 
ATOM   4433  C CA    . GLU B 1 111 ? 52.957  0.356   21.695  1.000 34.713  0 111 GLU BBB CA    1 ? 2 
ATOM   4434  C C     . GLU B 1 111 ? 52.769  -1.169  21.728  1.000 32.817  0 111 GLU BBB C     1 ? 2 
ATOM   4435  O O     . GLU B 1 111 ? 52.240  -1.702  22.715  1.000 33.673  0 111 GLU BBB O     1 ? 2 
ATOM   4436  C CB    . GLU B 1 111 ? 53.485  0.968   22.994  1.000 35.798  0 111 GLU BBB CB    1 ? 2 
ATOM   4437  C CG    . GLU B 1 111 ? 53.634  2.495   22.944  1.000 39.963  0 111 GLU BBB CG    1 ? 2 
ATOM   4438  C CD    . GLU B 1 111 ? 54.664  3.106   21.972  1.000 44.253  0 111 GLU BBB CD    1 ? 2 
ATOM   4439  O OE1   . GLU B 1 111 ? 54.534  4.330   21.690  1.000 46.056  0 111 GLU BBB OE1   1 ? 2 
ATOM   4440  O OE2   . GLU B 1 111 ? 55.595  2.370   21.482  1.000 45.983  0 111 GLU BBB OE2   1 ? 2 
ATOM   4441  N N     . TRP B 1 112 ? 53.161  -1.833  20.650  1.000 30.728  0 112 TRP BBB N     1 ? 2 
ATOM   4442  C CA    . TRP B 1 112 ? 52.956  -3.280  20.417  1.000 29.154  0 112 TRP BBB CA    1 ? 2 
ATOM   4443  C C     . TRP B 1 112 ? 53.427  -4.098  21.634  1.000 28.556  0 112 TRP BBB C     1 ? 2 
ATOM   4444  O O     . TRP B 1 112 ? 52.669  -5.005  22.082  1.000 25.492  0 112 TRP BBB O     1 ? 2 
ATOM   4445  C CB    . TRP B 1 112 ? 53.631  -3.696  19.105  1.000 28.102  0 112 TRP BBB CB    1 ? 2 
ATOM   4446  C CG    . TRP B 1 112 ? 53.642  -5.179  18.863  1.000 27.636  0 112 TRP BBB CG    1 ? 2 
ATOM   4447  C CD1   . TRP B 1 112 ? 54.657  -6.034  19.177  1.000 26.696  0 112 TRP BBB CD1   1 ? 2 
ATOM   4448  C CD2   . TRP B 1 112 ? 52.602  -5.991  18.273  1.000 26.333  0 112 TRP BBB CD2   1 ? 2 
ATOM   4449  N NE1   . TRP B 1 112 ? 54.308  -7.319  18.836  1.000 26.631  0 112 TRP BBB NE1   1 ? 2 
ATOM   4450  C CE2   . TRP B 1 112 ? 53.079  -7.314  18.243  1.000 25.770  0 112 TRP BBB CE2   1 ? 2 
ATOM   4451  C CE3   . TRP B 1 112 ? 51.327  -5.732  17.751  1.000 26.230  0 112 TRP BBB CE3   1 ? 2 
ATOM   4452  C CZ2   . TRP B 1 112 ? 52.331  -8.365  17.729  1.000 25.675  0 112 TRP BBB CZ2   1 ? 2 
ATOM   4453  C CZ3   . TRP B 1 112 ? 50.602  -6.765  17.191  1.000 25.930  0 112 TRP BBB CZ3   1 ? 2 
ATOM   4454  C CH2   . TRP B 1 112 ? 51.098  -8.069  17.189  1.000 25.057  0 112 TRP BBB CH2   1 ? 2 
ATOM   4455  N N     . GLY B 1 113 ? 54.620  -3.808  22.152  1.000 28.799  0 113 GLY BBB N     1 ? 2 
ATOM   4456  C CA    . GLY B 1 113 ? 55.263  -4.613  23.225  1.000 28.830  0 113 GLY BBB CA    1 ? 2 
ATOM   4457  C C     . GLY B 1 113 ? 54.524  -4.532  24.559  1.000 28.261  0 113 GLY BBB C     1 ? 2 
ATOM   4458  O O     . GLY B 1 113 ? 54.617  -5.488  25.364  1.000 27.193  0 113 GLY BBB O     1 ? 2 
ATOM   4459  N N     . LYS B 1 114 ? 53.797  -3.441  24.804  1.000 28.138  0 114 LYS BBB N     1 ? 2 
ATOM   4460  C CA    . LYS B 1 114 ? 52.940  -3.319  26.005  1.000 28.241  0 114 LYS BBB CA    1 ? 2 
ATOM   4461  C C     . LYS B 1 114 ? 51.767  -4.322  25.927  1.000 27.641  0 114 LYS BBB C     1 ? 2 
ATOM   4462  O O     . LYS B 1 114 ? 51.492  -4.989  26.937  1.000 26.472  0 114 LYS BBB O     1 ? 2 
ATOM   4463  C CB    . LYS B 1 114 ? 52.463  -1.868  26.120  1.000 29.152  0 114 LYS BBB CB    1 ? 2 
ATOM   4464  C CG    . LYS B 1 114 ? 51.572  -1.562  27.305  1.000 29.588  0 114 LYS BBB CG    1 ? 2 
ATOM   4465  C CD    . LYS B 1 114 ? 52.138  -2.141  28.577  1.000 31.238  0 114 LYS BBB CD    1 ? 2 
ATOM   4466  C CE    . LYS B 1 114 ? 51.312  -1.801  29.786  1.000 33.540  0 114 LYS BBB CE    1 ? 2 
ATOM   4467  N NZ    . LYS B 1 114 ? 52.095  -2.088  31.013  1.000 36.157  0 114 LYS BBB NZ    1 ? 2 
ATOM   4468  N N     . LEU B 1 115 ? 51.111  -4.418  24.766  1.000 27.847  0 115 LEU BBB N     1 ? 2 
ATOM   4469  C CA    . LEU B 1 115 ? 49.946  -5.306  24.508  1.000 28.051  0 115 LEU BBB CA    1 ? 2 
ATOM   4470  C C     . LEU B 1 115 ? 50.393  -6.750  24.625  1.000 28.783  0 115 LEU BBB C     1 ? 2 
ATOM   4471  O O     . LEU B 1 115 ? 49.734  -7.546  25.344  1.000 29.313  0 115 LEU BBB O     1 ? 2 
ATOM   4472  C CB    . LEU B 1 115 ? 49.387  -5.035  23.110  1.000 28.295  0 115 LEU BBB CB    1 ? 2 
ATOM   4473  C CG    . LEU B 1 115 ? 48.308  -5.993  22.610  1.000 27.470  0 115 LEU BBB CG    1 ? 2 
ATOM   4474  C CD1   . LEU B 1 115 ? 47.084  -6.020  23.524  1.000 26.599  0 115 LEU BBB CD1   1 ? 2 
ATOM   4475  C CD2   . LEU B 1 115 ? 47.917  -5.606  21.202  1.000 27.550  0 115 LEU BBB CD2   1 ? 2 
ATOM   4476  N N     . VAL B 1 116 ? 51.512  -7.060  23.978  1.000 29.858  0 116 VAL BBB N     1 ? 2 
ATOM   4477  C CA    . VAL B 1 116 ? 52.176  -8.391  24.098  1.000 28.111  0 116 VAL BBB CA    1 ? 2 
ATOM   4478  C C     . VAL B 1 116 ? 52.363  -8.687  25.583  1.000 26.509  0 116 VAL BBB C     1 ? 2 
ATOM   4479  O O     . VAL B 1 116 ? 51.909  -9.733  26.043  1.000 24.931  0 116 VAL BBB O     1 ? 2 
ATOM   4480  C CB    . VAL B 1 116 ? 53.480  -8.435  23.292  1.000 27.109  0 116 VAL BBB CB    1 ? 2 
ATOM   4481  C CG1   . VAL B 1 116 ? 54.337  -9.625  23.684  1.000 27.137  0 116 VAL BBB CG1   1 ? 2 
ATOM   4482  C CG2   . VAL B 1 116 ? 53.165  -8.442  21.799  1.000 27.424  0 116 VAL BBB CG2   1 ? 2 
ATOM   4483  N N     . GLU B 1 117 ? 52.947  -7.765  26.316  1.000 26.985  0 117 GLU BBB N     1 ? 2 
ATOM   4484  C CA    . GLU B 1 117 ? 53.263  -7.976  27.766  1.000 28.465  0 117 GLU BBB CA    1 ? 2 
ATOM   4485  C C     . GLU B 1 117 ? 51.931  -8.281  28.523  1.000 26.149  0 117 GLU BBB C     1 ? 2 
ATOM   4486  O O     . GLU B 1 117 ? 51.892  -9.264  29.280  1.000 24.424  0 117 GLU BBB O     1 ? 2 
ATOM   4487  C CB    . GLU B 1 117 ? 54.096  -6.791  28.265  1.000 29.569  0 117 GLU BBB CB    1 ? 2 
ATOM   4488  C CG    . GLU B 1 117 ? 54.312  -6.789  29.780  1.000 33.537  0 117 GLU BBB CG    1 ? 2 
ATOM   4489  C CD    . GLU B 1 117 ? 54.913  -5.507  30.332  1.000 36.530  0 117 GLU BBB CD    1 ? 2 
ATOM   4490  O OE1   . GLU B 1 117 ? 54.193  -4.738  31.030  1.000 38.589  0 117 GLU BBB OE1   1 ? 2 
ATOM   4491  O OE2   . GLU B 1 117 ? 56.097  -5.260  30.030  1.000 40.520  0 117 GLU BBB OE2   1 ? 2 
ATOM   4492  N N     . THR B 1 118 ? 50.855  -7.532  28.277  1.000 24.036  0 118 THR BBB N     1 ? 2 
ATOM   4493  C CA    . THR B 1 118 ? 49.533  -7.798  28.901  1.000 23.801  0 118 THR BBB CA    1 ? 2 
ATOM   4494  C C     . THR B 1 118 ? 49.003  -9.194  28.493  1.000 23.570  0 118 THR BBB C     1 ? 2 
ATOM   4495  O O     . THR B 1 118 ? 48.472  -9.867  29.357  1.000 21.667  0 118 THR BBB O     1 ? 2 
ATOM   4496  C CB    . THR B 1 118 ? 48.548  -6.674  28.547  1.000 24.660  0 118 THR BBB CB    1 ? 2 
ATOM   4497  O OG1   . THR B 1 118 ? 49.014  -5.517  29.237  1.000 22.932  0 118 THR BBB OG1   1 ? 2 
ATOM   4498  C CG2   . THR B 1 118 ? 47.089  -7.007  28.887  1.000 25.000  0 118 THR BBB CG2   1 ? 2 
ATOM   4499  N N     . LEU B 1 119 ? 49.122  -9.610  27.214  1.000 23.867  0 119 LEU BBB N     1 ? 2 
ATOM   4500  C CA    . LEU B 1 119 ? 48.765  -10.993 26.759  1.000 24.387  0 119 LEU BBB CA    1 ? 2 
ATOM   4501  C C     . LEU B 1 119 ? 49.581  -12.027 27.513  1.000 24.063  0 119 LEU BBB C     1 ? 2 
ATOM   4502  O O     . LEU B 1 119 ? 48.935  -12.872 28.128  1.000 23.347  0 119 LEU BBB O     1 ? 2 
ATOM   4503  C CB    . LEU B 1 119 ? 49.030  -11.191 25.260  1.000 26.135  0 119 LEU BBB CB    1 ? 2 
ATOM   4504  C CG    . LEU B 1 119 ? 47.817  -10.928 24.378  1.000 26.667  0 119 LEU BBB CG    1 ? 2 
ATOM   4505  C CD1   . LEU B 1 119 ? 47.382  -9.467  24.508  1.000 27.486  0 119 LEU BBB CD1   1 ? 2 
ATOM   4506  C CD2   . LEU B 1 119 ? 48.121  -11.264 22.937  1.000 28.798  0 119 LEU BBB CD2   1 ? 2 
ATOM   4507  N N     . ARG B 1 120 ? 50.923  -11.943 27.433  1.000 24.724  0 120 ARG BBB N     1 ? 2 
ATOM   4508  C CA    A ARG B 1 120 ? 51.866  -12.885 28.097  0.500 25.185  0 120 ARG BBB CA    1 ? 2 
ATOM   4509  C CA    B ARG B 1 120 ? 51.859  -12.892 28.096  0.500 25.497  0 120 ARG BBB CA    1 ? 2 
ATOM   4510  C C     . ARG B 1 120 ? 51.496  -13.038 29.578  1.000 25.321  0 120 ARG BBB C     1 ? 2 
ATOM   4511  O O     . ARG B 1 120 ? 51.382  -14.161 30.022  1.000 26.078  0 120 ARG BBB O     1 ? 2 
ATOM   4512  C CB    A ARG B 1 120 ? 53.326  -12.433 27.955  0.500 26.167  0 120 ARG BBB CB    1 ? 2 
ATOM   4513  C CB    B ARG B 1 120 ? 53.320  -12.461 27.944  0.500 26.929  0 120 ARG BBB CB    1 ? 2 
ATOM   4514  C CG    A ARG B 1 120 ? 54.067  -12.999 26.751  0.500 26.823  0 120 ARG BBB CG    1 ? 2 
ATOM   4515  C CG    B ARG B 1 120 ? 53.822  -12.458 26.509  0.500 28.049  0 120 ARG BBB CG    1 ? 2 
ATOM   4516  C CD    A ARG B 1 120 ? 55.564  -12.791 26.938  0.500 27.578  0 120 ARG BBB CD    1 ? 2 
ATOM   4517  C CD    B ARG B 1 120 ? 54.731  -13.608 26.090  0.500 29.146  0 120 ARG BBB CD    1 ? 2 
ATOM   4518  N NE    A ARG B 1 120 ? 56.073  -11.589 26.290  0.500 28.295  0 120 ARG BBB NE    1 ? 2 
ATOM   4519  N NE    B ARG B 1 120 ? 55.378  -14.343 27.166  0.500 30.267  0 120 ARG BBB NE    1 ? 2 
ATOM   4520  C CZ    A ARG B 1 120 ? 56.402  -10.454 26.902  0.500 28.934  0 120 ARG BBB CZ    1 ? 2 
ATOM   4521  C CZ    B ARG B 1 120 ? 56.688  -14.441 27.305  0.500 30.882  0 120 ARG BBB CZ    1 ? 2 
ATOM   4522  N NH1   A ARG B 1 120 ? 56.274  -10.322 28.209  0.500 28.676  0 120 ARG BBB NH1   1 ? 2 
ATOM   4523  N NH1   B ARG B 1 120 ? 57.462  -13.826 26.427  0.500 32.569  0 120 ARG BBB NH1   1 ? 2 
ATOM   4524  N NH2   A ARG B 1 120 ? 56.853  -9.433  26.193  0.500 29.581  0 120 ARG BBB NH2   1 ? 2 
ATOM   4525  N NH2   B ARG B 1 120 ? 57.210  -15.146 28.295  0.500 30.231  0 120 ARG BBB NH2   1 ? 2 
ATOM   4526  N N     . ASN B 1 121 ? 51.310  -11.948 30.314  1.000 26.708  0 121 ASN BBB N     1 ? 2 
ATOM   4527  C CA    . ASN B 1 121 ? 51.001  -11.991 31.783  1.000 28.774  0 121 ASN BBB CA    1 ? 2 
ATOM   4528  C C     . ASN B 1 121 ? 49.663  -12.702 32.011  1.000 28.970  0 121 ASN BBB C     1 ? 2 
ATOM   4529  O O     . ASN B 1 121 ? 49.581  -13.541 32.905  1.000 31.729  0 121 ASN BBB O     1 ? 2 
ATOM   4530  C CB    . ASN B 1 121 ? 50.901  -10.605 32.442  1.000 30.038  0 121 ASN BBB CB    1 ? 2 
ATOM   4531  C CG    . ASN B 1 121 ? 52.206  -9.831  32.473  1.000 33.221  0 121 ASN BBB CG    1 ? 2 
ATOM   4532  O OD1   . ASN B 1 121 ? 53.272  -10.383 32.127  1.000 35.458  0 121 ASN BBB OD1   1 ? 2 
ATOM   4533  N ND2   . ASN B 1 121 ? 52.125  -8.550  32.846  1.000 32.552  0 121 ASN BBB ND2   1 ? 2 
ATOM   4534  N N     . HIS B 1 122 ? 48.640  -12.419 31.208  1.000 27.818  0 122 HIS BBB N     1 ? 2 
ATOM   4535  C CA    . HIS B 1 122 ? 47.311  -13.048 31.398  1.000 26.984  0 122 HIS BBB CA    1 ? 2 
ATOM   4536  C C     . HIS B 1 122 ? 47.397  -14.543 31.053  1.000 26.530  0 122 HIS BBB C     1 ? 2 
ATOM   4537  O O     . HIS B 1 122 ? 46.883  -15.388 31.794  1.000 25.786  0 122 HIS BBB O     1 ? 2 
ATOM   4538  C CB    . HIS B 1 122 ? 46.240  -12.250 30.638  1.000 26.313  0 122 HIS BBB CB    1 ? 2 
ATOM   4539  C CG    . HIS B 1 122 ? 44.894  -12.797 30.938  1.000 25.810  0 122 HIS BBB CG    1 ? 2 
ATOM   4540  N ND1   . HIS B 1 122 ? 44.169  -12.419 32.060  1.000 26.863  0 122 HIS BBB ND1   1 ? 2 
ATOM   4541  C CD2   . HIS B 1 122 ? 44.251  -13.843 30.390  1.000 25.902  0 122 HIS BBB CD2   1 ? 2 
ATOM   4542  C CE1   . HIS B 1 122 ? 43.087  -13.154 32.119  1.000 27.112  0 122 HIS BBB CE1   1 ? 2 
ATOM   4543  N NE2   . HIS B 1 122 ? 43.114  -14.030 31.094  1.000 27.187  0 122 HIS BBB NE2   1 ? 2 
ATOM   4544  N N     . ILE B 1 123 ? 48.079  -14.882 29.969  1.000 27.404  0 123 ILE BBB N     1 ? 2 
ATOM   4545  C CA    . ILE B 1 123 ? 48.285  -16.299 29.540  1.000 27.462  0 123 ILE BBB CA    1 ? 2 
ATOM   4546  C C     . ILE B 1 123 ? 49.123  -17.039 30.582  1.000 28.689  0 123 ILE BBB C     1 ? 2 
ATOM   4547  O O     . ILE B 1 123 ? 48.765  -18.192 30.883  1.000 28.081  0 123 ILE BBB O     1 ? 2 
ATOM   4548  C CB    . ILE B 1 123 ? 48.848  -16.336 28.116  1.000 26.133  0 123 ILE BBB CB    1 ? 2 
ATOM   4549  C CG1   . ILE B 1 123 ? 47.745  -15.889 27.138  1.000 25.933  0 123 ILE BBB CG1   1 ? 2 
ATOM   4550  C CG2   . ILE B 1 123 ? 49.374  -17.704 27.787  1.000 25.581  0 123 ILE BBB CG2   1 ? 2 
ATOM   4551  C CD1   . ILE B 1 123 ? 48.211  -15.546 25.747  1.000 24.678  0 123 ILE BBB CD1   1 ? 2 
ATOM   4552  N N     . ARG B 1 124 ? 50.160  -16.416 31.155  1.000 30.002  0 124 ARG BBB N     1 ? 2 
ATOM   4553  C CA    . ARG B 1 124 ? 50.950  -17.040 32.259  1.000 31.456  0 124 ARG BBB CA    1 ? 2 
ATOM   4554  C C     . ARG B 1 124 ? 50.000  -17.403 33.410  1.000 30.662  0 124 ARG BBB C     1 ? 2 
ATOM   4555  O O     . ARG B 1 124 ? 49.991  -18.563 33.811  1.000 33.184  0 124 ARG BBB O     1 ? 2 
ATOM   4556  C CB    . ARG B 1 124 ? 52.090  -16.120 32.711  1.000 33.062  0 124 ARG BBB CB    1 ? 2 
ATOM   4557  C CG    . ARG B 1 124 ? 53.234  -16.831 33.425  1.000 34.376  0 124 ARG BBB CG    1 ? 2 
ATOM   4558  C CD    . ARG B 1 124 ? 54.227  -15.848 34.020  1.000 34.244  0 124 ARG BBB CD    1 ? 2 
ATOM   4559  N NE    . ARG B 1 124 ? 54.832  -15.071 32.940  1.000 32.969  0 124 ARG BBB NE    1 ? 2 
ATOM   4560  C CZ    . ARG B 1 124 ? 54.735  -13.755 32.765  1.000 33.810  0 124 ARG BBB CZ    1 ? 2 
ATOM   4561  N NH1   . ARG B 1 124 ? 54.111  -12.997 33.641  1.000 34.072  0 124 ARG BBB NH1   1 ? 2 
ATOM   4562  N NH2   . ARG B 1 124 ? 55.281  -13.188 31.707  1.000 37.436  0 124 ARG BBB NH2   1 ? 2 
ATOM   4563  N N     . MET B 1 125 ? 49.168  -16.468 33.854  1.000 31.788  0 125 MET BBB N     1 ? 2 
ATOM   4564  C CA    . MET B 1 125 ? 48.176  -16.707 34.926  1.000 33.767  0 125 MET BBB CA    1 ? 2 
ATOM   4565  C C     . MET B 1 125 ? 47.340  -17.959 34.579  1.000 31.895  0 125 MET BBB C     1 ? 2 
ATOM   4566  O O     . MET B 1 125 ? 47.160  -18.812 35.469  1.000 30.783  0 125 MET BBB O     1 ? 2 
ATOM   4567  C CB    . MET B 1 125 ? 47.316  -15.458 35.130  1.000 37.904  0 125 MET BBB CB    1 ? 2 
ATOM   4568  C CG    . MET B 1 125 ? 46.256  -15.584 36.272  1.000 44.419  0 125 MET BBB CG    1 ? 2 
ATOM   4569  S SD    . MET B 1 125 ? 44.708  -16.495 35.786  1.000 49.275  0 125 MET BBB SD    1 ? 2 
ATOM   4570  C CE    . MET B 1 125 ? 44.169  -15.443 34.437  1.000 51.918  0 125 MET BBB CE    1 ? 2 
ATOM   4571  N N     . LEU B 1 126 ? 46.903  -18.100 33.318  1.000 30.257  0 126 LEU BBB N     1 ? 2 
ATOM   4572  C CA    . LEU B 1 126 ? 46.061  -19.224 32.826  1.000 28.103  0 126 LEU BBB CA    1 ? 2 
ATOM   4573  C C     . LEU B 1 126 ? 46.891  -20.509 32.760  1.000 26.806  0 126 LEU BBB C     1 ? 2 
ATOM   4574  O O     . LEU B 1 126 ? 46.367  -21.561 33.140  1.000 25.626  0 126 LEU BBB O     1 ? 2 
ATOM   4575  C CB    . LEU B 1 126 ? 45.495  -18.898 31.438  1.000 29.278  0 126 LEU BBB CB    1 ? 2 
ATOM   4576  C CG    . LEU B 1 126 ? 44.323  -17.916 31.389  1.000 29.991  0 126 LEU BBB CG    1 ? 2 
ATOM   4577  C CD1   . LEU B 1 126 ? 44.063  -17.501 29.963  1.000 30.874  0 126 LEU BBB CD1   1 ? 2 
ATOM   4578  C CD2   . LEU B 1 126 ? 43.057  -18.503 32.006  1.000 29.814  0 126 LEU BBB CD2   1 ? 2 
ATOM   4579  N N     . ASN B 1 127 ? 48.141  -20.450 32.303  1.000 25.014  0 127 ASN BBB N     1 ? 2 
ATOM   4580  C CA    . ASN B 1 127 ? 49.009  -21.662 32.356  1.000 25.428  0 127 ASN BBB CA    1 ? 2 
ATOM   4581  C C     . ASN B 1 127 ? 48.980  -22.187 33.800  1.000 27.471  0 127 ASN BBB C     1 ? 2 
ATOM   4582  O O     . ASN B 1 127 ? 48.712  -23.354 33.975  1.000 27.342  0 127 ASN BBB O     1 ? 2 
ATOM   4583  C CB    . ASN B 1 127 ? 50.463  -21.410 31.923  1.000 23.832  0 127 ASN BBB CB    1 ? 2 
ATOM   4584  C CG    . ASN B 1 127 ? 50.621  -20.900 30.505  1.000 22.956  0 127 ASN BBB CG    1 ? 2 
ATOM   4585  O OD1   . ASN B 1 127 ? 51.460  -20.022 30.282  1.000 21.903  0 127 ASN BBB OD1   1 ? 2 
ATOM   4586  N ND2   . ASN B 1 127 ? 49.817  -21.409 29.558  1.000 22.099  0 127 ASN BBB ND2   1 ? 2 
ATOM   4587  N N     . PHE B 1 128 ? 49.246  -21.331 34.786  1.000 30.349  0 128 PHE BBB N     1 ? 2 
ATOM   4588  C CA    . PHE B 1 128 ? 49.369  -21.729 36.202  1.000 33.738  0 128 PHE BBB CA    1 ? 2 
ATOM   4589  C C     . PHE B 1 128 ? 48.023  -22.241 36.728  1.000 32.777  0 128 PHE BBB C     1 ? 2 
ATOM   4590  O O     . PHE B 1 128 ? 47.937  -23.316 37.288  1.000 33.640  0 128 PHE BBB O     1 ? 2 
ATOM   4591  C CB    . PHE B 1 128 ? 49.916  -20.582 37.045  1.000 38.837  0 128 PHE BBB CB    1 ? 2 
ATOM   4592  C CG    . PHE B 1 128 ? 49.915  -21.028 38.479  1.000 48.343  0 128 PHE BBB CG    1 ? 2 
ATOM   4593  C CD1   . PHE B 1 128 ? 50.793  -22.022 38.903  1.000 53.876  0 128 PHE BBB CD1   1 ? 2 
ATOM   4594  C CD2   . PHE B 1 128 ? 48.909  -20.613 39.349  1.000 53.837  0 128 PHE BBB CD2   1 ? 2 
ATOM   4595  C CE1   . PHE B 1 128 ? 50.734  -22.510 40.202  1.000 57.826  0 128 PHE BBB CE1   1 ? 2 
ATOM   4596  C CE2   . PHE B 1 128 ? 48.846  -21.103 40.642  1.000 55.983  0 128 PHE BBB CE2   1 ? 2 
ATOM   4597  C CZ    . PHE B 1 128 ? 49.758  -22.048 41.065  1.000 58.396  0 128 PHE BBB CZ    1 ? 2 
ATOM   4598  N N     . SER B 1 129 ? 46.967  -21.502 36.454  1.000 33.411  0 129 SER BBB N     1 ? 2 
ATOM   4599  C CA    . SER B 1 129 ? 45.569  -21.833 36.805  1.000 33.095  0 129 SER BBB CA    1 ? 2 
ATOM   4600  C C     . SER B 1 129 ? 45.236  -23.254 36.323  1.000 34.138  0 129 SER BBB C     1 ? 2 
ATOM   4601  O O     . SER B 1 129 ? 44.617  -24.020 37.080  1.000 32.944  0 129 SER BBB O     1 ? 2 
ATOM   4602  C CB    . SER B 1 129 ? 44.685  -20.752 36.246  1.000 32.143  0 129 SER BBB CB    1 ? 2 
ATOM   4603  O OG    . SER B 1 129 ? 43.333  -21.080 36.361  1.000 36.947  0 129 SER BBB OG    1 ? 2 
ATOM   4604  N N     . TYR B 1 130 ? 45.642  -23.643 35.112  1.000 36.621  0 130 TYR BBB N     1 ? 2 
ATOM   4605  C CA    . TYR B 1 130 ? 45.305  -24.980 34.551  1.000 36.772  0 130 TYR BBB CA    1 ? 2 
ATOM   4606  C C     . TYR B 1 130 ? 46.201  -26.050 35.193  1.000 39.273  0 130 TYR BBB C     1 ? 2 
ATOM   4607  O O     . TYR B 1 130 ? 45.656  -27.145 35.471  1.000 37.024  0 130 TYR BBB O     1 ? 2 
ATOM   4608  C CB    . TYR B 1 130 ? 45.367  -24.971 33.025  1.000 38.037  0 130 TYR BBB CB    1 ? 2 
ATOM   4609  C CG    . TYR B 1 130 ? 44.195  -24.288 32.364  1.000 39.220  0 130 TYR BBB CG    1 ? 2 
ATOM   4610  C CD1   . TYR B 1 130 ? 42.902  -24.737 32.569  1.000 42.241  0 130 TYR BBB CD1   1 ? 2 
ATOM   4611  C CD2   . TYR B 1 130 ? 44.372  -23.216 31.499  1.000 41.017  0 130 TYR BBB CD2   1 ? 2 
ATOM   4612  C CE1   . TYR B 1 130 ? 41.813  -24.117 31.972  1.000 42.633  0 130 TYR BBB CE1   1 ? 2 
ATOM   4613  C CE2   . TYR B 1 130 ? 43.292  -22.561 30.913  1.000 40.693  0 130 TYR BBB CE2   1 ? 2 
ATOM   4614  C CZ    . TYR B 1 130 ? 42.010  -23.010 31.158  1.000 42.502  0 130 TYR BBB CZ    1 ? 2 
ATOM   4615  O OH    . TYR B 1 130 ? 40.959  -22.357 30.581  1.000 43.382  0 130 TYR BBB OH    1 ? 2 
ATOM   4616  N N     . ARG B 1 131 ? 47.504  -25.787 35.418  1.000 38.952  0 131 ARG BBB N     1 ? 2 
ATOM   4617  C CA    . ARG B 1 131 ? 48.378  -26.733 36.170  1.000 42.727  0 131 ARG BBB CA    1 ? 2 
ATOM   4618  C C     . ARG B 1 131 ? 47.696  -27.107 37.490  1.000 40.784  0 131 ARG BBB C     1 ? 2 
ATOM   4619  O O     . ARG B 1 131 ? 47.602  -28.306 37.780  1.000 40.872  0 131 ARG BBB O     1 ? 2 
ATOM   4620  C CB    . ARG B 1 131 ? 49.759  -26.163 36.518  1.000 45.582  0 131 ARG BBB CB    1 ? 2 
ATOM   4621  C CG    . ARG B 1 131 ? 50.859  -26.565 35.551  1.000 48.927  0 131 ARG BBB CG    1 ? 2 
ATOM   4622  C CD    . ARG B 1 131 ? 52.252  -26.624 36.156  1.000 53.689  0 131 ARG BBB CD    1 ? 2 
ATOM   4623  N NE    . ARG B 1 131 ? 52.707  -25.412 36.814  1.000 56.315  0 131 ARG BBB NE    1 ? 2 
ATOM   4624  C CZ    . ARG B 1 131 ? 53.014  -24.271 36.190  1.000 59.769  0 131 ARG BBB CZ    1 ? 2 
ATOM   4625  N NH1   . ARG B 1 131 ? 52.850  -24.149 34.875  1.000 60.547  0 131 ARG BBB NH1   1 ? 2 
ATOM   4626  N NH2   . ARG B 1 131 ? 53.444  -23.235 36.894  1.000 60.083  0 131 ARG BBB NH2   1 ? 2 
ATOM   4627  N N     . THR B 1 132 ? 47.270  -26.099 38.243  1.000 39.124  0 132 THR BBB N     1 ? 2 
ATOM   4628  C CA    . THR B 1 132 ? 46.646  -26.238 39.585  1.000 41.801  0 132 THR BBB CA    1 ? 2 
ATOM   4629  C C     . THR B 1 132 ? 45.325  -27.006 39.438  1.000 40.138  0 132 THR BBB C     1 ? 2 
ATOM   4630  O O     . THR B 1 132 ? 45.078  -27.925 40.257  1.000 41.566  0 132 THR BBB O     1 ? 2 
ATOM   4631  C CB    . THR B 1 132 ? 46.475  -24.860 40.258  1.000 40.424  0 132 THR BBB CB    1 ? 2 
ATOM   4632  O OG1   . THR B 1 132 ? 47.780  -24.309 40.462  1.000 38.324  0 132 THR BBB OG1   1 ? 2 
ATOM   4633  C CG2   . THR B 1 132 ? 45.766  -24.932 41.593  1.000 40.079  0 132 THR BBB CG2   1 ? 2 
ATOM   4634  N N     . GLY B 1 133 ? 44.506  -26.627 38.459  1.000 39.715  0 133 GLY BBB N     1 ? 2 
ATOM   4635  C CA    . GLY B 1 133 ? 43.174  -27.212 38.189  1.000 39.146  0 133 GLY BBB CA    1 ? 2 
ATOM   4636  C C     . GLY B 1 133 ? 43.277  -28.718 37.985  1.000 39.194  0 133 GLY BBB C     1 ? 2 
ATOM   4637  O O     . GLY B 1 133 ? 42.363  -29.466 38.443  1.000 41.502  0 133 GLY BBB O     1 ? 2 
ATOM   4638  N N     . LEU B 1 134 ? 44.356  -29.159 37.339  1.000 35.179  0 134 LEU BBB N     1 ? 2 
ATOM   4639  C CA    . LEU B 1 134 ? 44.640  -30.587 37.095  1.000 35.443  0 134 LEU BBB CA    1 ? 2 
ATOM   4640  C C     . LEU B 1 134 ? 45.070  -31.249 38.407  1.000 39.514  0 134 LEU BBB C     1 ? 2 
ATOM   4641  O O     . LEU B 1 134 ? 44.480  -32.302 38.747  1.000 38.124  0 134 LEU BBB O     1 ? 2 
ATOM   4642  C CB    . LEU B 1 134 ? 45.711  -30.734 36.010  1.000 33.553  0 134 LEU BBB CB    1 ? 2 
ATOM   4643  C CG    . LEU B 1 134 ? 45.218  -30.549 34.571  1.000 31.227  0 134 LEU BBB CG    1 ? 2 
ATOM   4644  C CD1   . LEU B 1 134 ? 46.356  -30.762 33.593  1.000 30.863  0 134 LEU BBB CD1   1 ? 2 
ATOM   4645  C CD2   . LEU B 1 134 ? 44.053  -31.465 34.259  1.000 29.819  0 134 LEU BBB CD2   1 ? 2 
ATOM   4646  N N     . ARG B 1 135 ? 46.047  -30.663 39.108  1.000 41.297  0 135 ARG BBB N     1 ? 2 
ATOM   4647  C CA    . ARG B 1 135 ? 46.577  -31.241 40.375  1.000 46.009  0 135 ARG BBB CA    1 ? 2 
ATOM   4648  C C     . ARG B 1 135 ? 45.418  -31.373 41.392  1.000 43.883  0 135 ARG BBB C     1 ? 2 
ATOM   4649  O O     . ARG B 1 135 ? 45.203  -32.477 41.909  1.000 42.867  0 135 ARG BBB O     1 ? 2 
ATOM   4650  C CB    . ARG B 1 135 ? 47.757  -30.409 40.908  1.000 48.882  0 135 ARG BBB CB    1 ? 2 
ATOM   4651  C CG    . ARG B 1 135 ? 48.697  -31.215 41.795  1.000 53.565  0 135 ARG BBB CG    1 ? 2 
ATOM   4652  C CD    . ARG B 1 135 ? 49.673  -30.386 42.627  1.000 56.171  0 135 ARG BBB CD    1 ? 2 
ATOM   4653  N NE    . ARG B 1 135 ? 48.990  -29.410 43.473  1.000 57.644  0 135 ARG BBB NE    1 ? 2 
ATOM   4654  C CZ    . ARG B 1 135 ? 48.896  -28.103 43.220  1.000 58.149  0 135 ARG BBB CZ    1 ? 2 
ATOM   4655  N NH1   . ARG B 1 135 ? 49.445  -27.585 42.130  1.000 60.129  0 135 ARG BBB NH1   1 ? 2 
ATOM   4656  N NH2   . ARG B 1 135 ? 48.244  -27.311 44.059  1.000 54.717  0 135 ARG BBB NH2   1 ? 2 
ATOM   4657  N N     . VAL B 1 136 ? 44.686  -30.285 41.641  1.000 41.920  0 136 VAL BBB N     1 ? 2 
ATOM   4658  C CA    . VAL B 1 136 ? 43.519  -30.251 42.568  1.000 41.869  0 136 VAL BBB CA    1 ? 2 
ATOM   4659  C C     . VAL B 1 136 ? 42.485  -31.280 42.072  1.000 43.581  0 136 VAL BBB C     1 ? 2 
ATOM   4660  O O     . VAL B 1 136 ? 41.928  -31.999 42.924  1.000 43.613  0 136 VAL BBB O     1 ? 2 
ATOM   4661  C CB    . VAL B 1 136 ? 42.935  -28.824 42.679  1.000 40.425  0 136 VAL BBB CB    1 ? 2 
ATOM   4662  C CG1   . VAL B 1 136 ? 41.494  -28.784 43.178  1.000 38.694  0 136 VAL BBB CG1   1 ? 2 
ATOM   4663  C CG2   . VAL B 1 136 ? 43.831  -27.932 43.527  1.000 40.282  0 136 VAL BBB CG2   1 ? 2 
ATOM   4664  N N     . GLY B 1 137 ? 42.260  -31.376 40.750  1.000 42.946  0 137 GLY BBB N     1 ? 2 
ATOM   4665  C CA    . GLY B 1 137 ? 41.253  -32.278 40.141  1.000 40.759  0 137 GLY BBB CA    1 ? 2 
ATOM   4666  C C     . GLY B 1 137 ? 41.716  -33.734 40.048  1.000 40.287  0 137 GLY BBB C     1 ? 2 
ATOM   4667  O O     . GLY B 1 137 ? 41.014  -34.538 39.419  1.000 39.196  0 137 GLY BBB O     1 ? 2 
ATOM   4668  N N     . ASN B 1 138 ? 42.879  -34.043 40.616  1.000 40.064  0 138 ASN BBB N     1 ? 2 
ATOM   4669  C CA    . ASN B 1 138 ? 43.418  -35.403 40.823  1.000 41.548  0 138 ASN BBB CA    1 ? 2 
ATOM   4670  C C     . ASN B 1 138 ? 43.807  -36.019 39.473  1.000 40.129  0 138 ASN BBB C     1 ? 2 
ATOM   4671  O O     . ASN B 1 138 ? 43.615  -37.227 39.274  1.000 38.619  0 138 ASN BBB O     1 ? 2 
ATOM   4672  C CB    . ASN B 1 138 ? 42.455  -36.284 41.638  1.000 44.614  0 138 ASN BBB CB    1 ? 2 
ATOM   4673  C CG    . ASN B 1 138 ? 43.146  -37.560 42.087  1.000 48.230  0 138 ASN BBB CG    1 ? 2 
ATOM   4674  O OD1   . ASN B 1 138 ? 44.320  -37.514 42.474  1.000 50.830  0 138 ASN BBB OD1   1 ? 2 
ATOM   4675  N ND2   . ASN B 1 138 ? 42.469  -38.703 41.997  1.000 47.821  0 138 ASN BBB ND2   1 ? 2 
ATOM   4676  N N     . VAL B 1 139 ? 44.356  -35.206 38.577  1.000 40.867  0 139 VAL BBB N     1 ? 2 
ATOM   4677  C CA    . VAL B 1 139 ? 44.933  -35.637 37.273  1.000 38.045  0 139 VAL BBB CA    1 ? 2 
ATOM   4678  C C     . VAL B 1 139 ? 46.452  -35.490 37.382  1.000 37.775  0 139 VAL BBB C     1 ? 2 
ATOM   4679  O O     . VAL B 1 139 ? 46.900  -34.427 37.788  1.000 36.924  0 139 VAL BBB O     1 ? 2 
ATOM   4680  C CB    . VAL B 1 139 ? 44.378  -34.812 36.099  1.000 37.289  0 139 VAL BBB CB    1 ? 2 
ATOM   4681  C CG1   . VAL B 1 139 ? 44.990  -35.230 34.777  1.000 37.304  0 139 VAL BBB CG1   1 ? 2 
ATOM   4682  C CG2   . VAL B 1 139 ? 42.871  -34.872 36.024  1.000 37.991  0 139 VAL BBB CG2   1 ? 2 
ATOM   4683  N N     . GLU B 1 140 ? 47.190  -36.539 37.025  1.000 39.365  0 140 GLU BBB N     1 ? 2 
ATOM   4684  C CA    . GLU B 1 140 ? 48.666  -36.540 36.904  1.000 40.814  0 140 GLU BBB CA    1 ? 2 
ATOM   4685  C C     . GLU B 1 140 ? 49.067  -35.888 35.568  1.000 38.612  0 140 GLU BBB C     1 ? 2 
ATOM   4686  O O     . GLU B 1 140 ? 48.924  -36.540 34.515  1.000 36.943  0 140 GLU BBB O     1 ? 2 
ATOM   4687  C CB    . GLU B 1 140 ? 49.211  -37.968 37.003  1.000 43.162  0 140 GLU BBB CB    1 ? 2 
ATOM   4688  C CG    . GLU B 1 140 ? 50.716  -37.996 37.228  1.000 45.759  0 140 GLU BBB CG    1 ? 2 
ATOM   4689  C CD    . GLU B 1 140 ? 51.382  -39.353 37.259  1.000 49.398  0 140 GLU BBB CD    1 ? 2 
ATOM   4690  O OE1   . GLU B 1 140 ? 50.650  -40.375 37.307  1.000 52.499  0 140 GLU BBB OE1   1 ? 2 
ATOM   4691  O OE2   . GLU B 1 140 ? 52.648  -39.385 37.196  1.000 51.832  0 140 GLU BBB OE2   1 ? 2 
ATOM   4692  N N     . TYR B 1 141 ? 49.562  -34.656 35.636  1.000 36.909  0 141 TYR BBB N     1 ? 2 
ATOM   4693  C CA    . TYR B 1 141 ? 50.063  -33.861 34.484  1.000 36.911  0 141 TYR BBB CA    1 ? 2 
ATOM   4694  C C     . TYR B 1 141 ? 51.531  -34.228 34.259  1.000 36.883  0 141 TYR BBB C     1 ? 2 
ATOM   4695  O O     . TYR B 1 141 ? 52.295  -34.131 35.197  1.000 38.650  0 141 TYR BBB O     1 ? 2 
ATOM   4696  C CB    . TYR B 1 141 ? 49.885  -32.356 34.724  1.000 34.710  0 141 TYR BBB CB    1 ? 2 
ATOM   4697  C CG    . TYR B 1 141 ? 50.661  -31.462 33.784  1.000 34.889  0 141 TYR BBB CG    1 ? 2 
ATOM   4698  C CD1   . TYR B 1 141 ? 50.589  -31.647 32.412  1.000 35.576  0 141 TYR BBB CD1   1 ? 2 
ATOM   4699  C CD2   . TYR B 1 141 ? 51.443  -30.411 34.248  1.000 34.804  0 141 TYR BBB CD2   1 ? 2 
ATOM   4700  C CE1   . TYR B 1 141 ? 51.278  -30.830 31.532  1.000 35.145  0 141 TYR BBB CE1   1 ? 2 
ATOM   4701  C CE2   . TYR B 1 141 ? 52.145  -29.588 33.384  1.000 34.023  0 141 TYR BBB CE2   1 ? 2 
ATOM   4702  C CZ    . TYR B 1 141 ? 52.054  -29.788 32.018  1.000 35.834  0 141 TYR BBB CZ    1 ? 2 
ATOM   4703  O OH    . TYR B 1 141 ? 52.772  -29.010 31.142  1.000 37.472  0 141 TYR BBB OH    1 ? 2 
ATOM   4704  N N     . ILE B 1 142 ? 51.907  -34.584 33.035  1.000 36.446  0 142 ILE BBB N     1 ? 2 
ATOM   4705  C CA    . ILE B 1 142 ? 53.316  -34.900 32.641  1.000 37.142  0 142 ILE BBB CA    1 ? 2 
ATOM   4706  C C     . ILE B 1 142 ? 53.668  -34.045 31.419  1.000 35.460  0 142 ILE BBB C     1 ? 2 
ATOM   4707  O O     . ILE B 1 142 ? 53.009  -34.216 30.387  1.000 34.202  0 142 ILE BBB O     1 ? 2 
ATOM   4708  C CB    . ILE B 1 142 ? 53.477  -36.406 32.348  1.000 37.349  0 142 ILE BBB CB    1 ? 2 
ATOM   4709  C CG1   . ILE B 1 142 ? 53.106  -37.248 33.570  1.000 39.464  0 142 ILE BBB CG1   1 ? 2 
ATOM   4710  C CG2   . ILE B 1 142 ? 54.871  -36.717 31.826  1.000 36.414  0 142 ILE BBB CG2   1 ? 2 
ATOM   4711  C CD1   . ILE B 1 142 ? 52.909  -38.707 33.278  1.000 40.125  0 142 ILE BBB CD1   1 ? 2 
ATOM   4712  N N     . ASN B 1 143 ? 54.665  -33.174 31.555  1.000 34.551  0 143 ASN BBB N     1 ? 2 
ATOM   4713  C CA    . ASN B 1 143 ? 55.137  -32.270 30.474  1.000 35.243  0 143 ASN BBB CA    1 ? 2 
ATOM   4714  C C     . ASN B 1 143 ? 56.130  -33.063 29.622  1.000 32.918  0 143 ASN BBB C     1 ? 2 
ATOM   4715  O O     . ASN B 1 143 ? 57.336  -32.823 29.775  1.000 32.726  0 143 ASN BBB O     1 ? 2 
ATOM   4716  C CB    . ASN B 1 143 ? 55.707  -30.964 31.054  1.000 36.260  0 143 ASN BBB CB    1 ? 2 
ATOM   4717  C CG    . ASN B 1 143 ? 56.058  -29.885 30.042  1.000 36.563  0 143 ASN BBB CG    1 ? 2 
ATOM   4718  O OD1   . ASN B 1 143 ? 55.540  -29.840 28.919  1.000 38.012  0 143 ASN BBB OD1   1 ? 2 
ATOM   4719  N ND2   . ASN B 1 143 ? 56.916  -28.965 30.455  1.000 36.408  0 143 ASN BBB ND2   1 ? 2 
ATOM   4720  N N     . ALA B 1 144 ? 55.635  -33.986 28.791  1.000 31.805  0 144 ALA BBB N     1 ? 2 
ATOM   4721  C CA    . ALA B 1 144 ? 56.434  -34.717 27.771  1.000 32.116  0 144 ALA BBB CA    1 ? 2 
ATOM   4722  C C     . ALA B 1 144 ? 55.568  -35.072 26.551  1.000 31.984  0 144 ALA BBB C     1 ? 2 
ATOM   4723  O O     . ALA B 1 144 ? 54.329  -35.206 26.710  1.000 31.294  0 144 ALA BBB O     1 ? 2 
ATOM   4724  C CB    . ALA B 1 144 ? 57.043  -35.947 28.380  1.000 31.903  0 144 ALA BBB CB    1 ? 2 
ATOM   4725  N N     . LEU B 1 145 ? 56.205  -35.296 25.395  1.000 31.507  0 145 LEU BBB N     1 ? 2 
ATOM   4726  C CA    . LEU B 1 145 ? 55.565  -35.939 24.217  1.000 32.573  0 145 LEU BBB CA    1 ? 2 
ATOM   4727  C C     . LEU B 1 145 ? 55.306  -37.415 24.512  1.000 34.271  0 145 LEU BBB C     1 ? 2 
ATOM   4728  O O     . LEU B 1 145 ? 56.249  -38.112 24.913  1.000 34.440  0 145 LEU BBB O     1 ? 2 
ATOM   4729  C CB    . LEU B 1 145 ? 56.423  -35.818 22.957  1.000 33.394  0 145 LEU BBB CB    1 ? 2 
ATOM   4730  C CG    . LEU B 1 145 ? 56.460  -34.420 22.336  1.000 34.555  0 145 LEU BBB CG    1 ? 2 
ATOM   4731  C CD1   . LEU B 1 145 ? 57.483  -34.357 21.211  1.000 33.171  0 145 LEU BBB CD1   1 ? 2 
ATOM   4732  C CD2   . LEU B 1 145 ? 55.052  -33.966 21.892  1.000 33.351  0 145 LEU BBB CD2   1 ? 2 
ATOM   4733  N N     . ALA B 1 146 ? 54.060  -37.856 24.274  1.000 35.571  0 146 ALA BBB N     1 ? 2 
ATOM   4734  C CA    . ALA B 1 146 ? 53.618  -39.258 24.415  1.000 35.287  0 146 ALA BBB CA    1 ? 2 
ATOM   4735  C C     . ALA B 1 146 ? 53.433  -39.822 23.017  1.000 34.400  0 146 ALA BBB C     1 ? 2 
ATOM   4736  O O     . ALA B 1 146 ? 53.119  -39.061 22.140  1.000 34.748  0 146 ALA BBB O     1 ? 2 
ATOM   4737  C CB    . ALA B 1 146 ? 52.352  -39.318 25.231  1.000 35.060  0 146 ALA BBB CB    1 ? 2 
ATOM   4738  N N     . LYS B 1 147 ? 53.657  -41.118 22.832  1.000 37.528  0 147 LYS BBB N     1 ? 2 
ATOM   4739  C CA    . LYS B 1 147 ? 53.258  -41.853 21.597  1.000 39.666  0 147 LYS BBB CA    1 ? 2 
ATOM   4740  C C     . LYS B 1 147 ? 52.600  -43.193 21.977  1.000 37.004  0 147 LYS BBB C     1 ? 2 
ATOM   4741  O O     . LYS B 1 147 ? 52.776  -43.670 23.113  1.000 33.815  0 147 LYS BBB O     1 ? 2 
ATOM   4742  C CB    . LYS B 1 147 ? 54.450  -41.981 20.640  1.000 43.824  0 147 LYS BBB CB    1 ? 2 
ATOM   4743  C CG    . LYS B 1 147 ? 55.621  -42.806 21.144  1.000 48.392  0 147 LYS BBB CG    1 ? 2 
ATOM   4744  C CD    . LYS B 1 147 ? 56.387  -43.517 20.010  1.000 53.811  0 147 LYS BBB CD    1 ? 2 
ATOM   4745  C CE    . LYS B 1 147 ? 57.587  -42.759 19.480  1.000 54.993  0 147 LYS BBB CE    1 ? 2 
ATOM   4746  N NZ    . LYS B 1 147 ? 57.921  -43.209 18.103  1.000 54.155  0 147 LYS BBB NZ    1 ? 2 
ATOM   4747  N N     . LEU B 1 148 ? 51.820  -43.761 21.064  1.000 36.782  0 148 LEU BBB N     1 ? 2 
ATOM   4748  C CA    . LEU B 1 148 ? 51.189  -45.096 21.244  1.000 38.317  0 148 LEU BBB CA    1 ? 2 
ATOM   4749  C C     . LEU B 1 148 ? 52.242  -46.191 21.000  1.000 40.426  0 148 LEU BBB C     1 ? 2 
ATOM   4750  O O     . LEU B 1 148 ? 53.036  -46.074 20.063  1.000 38.593  0 148 LEU BBB O     1 ? 2 
ATOM   4751  C CB    . LEU B 1 148 ? 49.993  -45.243 20.298  1.000 38.305  0 148 LEU BBB CB    1 ? 2 
ATOM   4752  C CG    . LEU B 1 148 ? 48.888  -44.194 20.459  1.000 36.536  0 148 LEU BBB CG    1 ? 2 
ATOM   4753  C CD1   . LEU B 1 148 ? 47.892  -44.300 19.328  1.000 36.530  0 148 LEU BBB CD1   1 ? 2 
ATOM   4754  C CD2   . LEU B 1 148 ? 48.201  -44.295 21.801  1.000 36.331  0 148 LEU BBB CD2   1 ? 2 
ATOM   4755  N N     . ILE B 1 149 ? 52.271  -47.190 21.881  1.000 43.830  0 149 ILE BBB N     1 ? 2 
ATOM   4756  C CA    . ILE B 1 149 ? 53.063  -48.440 21.746  1.000 44.387  0 149 ILE BBB CA    1 ? 2 
ATOM   4757  C C     . ILE B 1 149 ? 52.122  -49.540 21.272  1.000 43.335  0 149 ILE BBB C     1 ? 2 
ATOM   4758  O O     . ILE B 1 149 ? 52.522  -50.256 20.378  1.000 45.828  0 149 ILE BBB O     1 ? 2 
ATOM   4759  C CB    . ILE B 1 149 ? 53.802  -48.763 23.064  1.000 46.564  0 149 ILE BBB CB    1 ? 2 
ATOM   4760  C CG1   . ILE B 1 149 ? 54.993  -47.820 23.263  1.000 46.742  0 149 ILE BBB CG1   1 ? 2 
ATOM   4761  C CG2   . ILE B 1 149 ? 54.235  -50.227 23.150  1.000 48.800  0 149 ILE BBB CG2   1 ? 2 
ATOM   4762  C CD1   . ILE B 1 149 ? 56.048  -47.901 22.178  1.000 46.665  0 149 ILE BBB CD1   1 ? 2 
ATOM   4763  N N     . ASP B 1 150 ? 50.926  -49.635 21.850  1.000 44.324  0 150 ASP BBB N     1 ? 2 
ATOM   4764  C CA    . ASP B 1 150 ? 49.856  -50.598 21.463  1.000 44.079  0 150 ASP BBB CA    1 ? 2 
ATOM   4765  C C     . ASP B 1 150 ? 48.501  -50.085 21.971  1.000 42.733  0 150 ASP BBB C     1 ? 2 
ATOM   4766  O O     . ASP B 1 150 ? 48.425  -49.052 22.624  1.000 45.572  0 150 ASP BBB O     1 ? 2 
ATOM   4767  C CB    . ASP B 1 150 ? 50.249  -52.000 21.930  1.000 44.840  0 150 ASP BBB CB    1 ? 2 
ATOM   4768  C CG    . ASP B 1 150 ? 50.212  -52.231 23.433  1.000 45.883  0 150 ASP BBB CG    1 ? 2 
ATOM   4769  O OD1   . ASP B 1 150 ? 49.330  -51.653 24.104  1.000 43.330  0 150 ASP BBB OD1   1 ? 2 
ATOM   4770  O OD2   . ASP B 1 150 ? 51.080  -53.002 23.927  1.000 49.937  0 150 ASP BBB OD2   1 ? 2 
ATOM   4771  N N     . PRO B 1 151 ? 47.378  -50.774 21.699  1.000 41.579  0 151 PRO BBB N     1 ? 2 
ATOM   4772  C CA    . PRO B 1 151 ? 46.058  -50.289 22.113  1.000 41.789  0 151 PRO BBB CA    1 ? 2 
ATOM   4773  C C     . PRO B 1 151 ? 45.887  -49.914 23.594  1.000 41.890  0 151 PRO BBB C     1 ? 2 
ATOM   4774  O O     . PRO B 1 151 ? 44.860  -49.336 23.894  1.000 43.792  0 151 PRO BBB O     1 ? 2 
ATOM   4775  C CB    . PRO B 1 151 ? 45.130  -51.497 21.852  1.000 42.346  0 151 PRO BBB CB    1 ? 2 
ATOM   4776  C CG    . PRO B 1 151 ? 45.832  -52.327 20.782  1.000 42.006  0 151 PRO BBB CG    1 ? 2 
ATOM   4777  C CD    . PRO B 1 151 ? 47.308  -52.049 20.959  1.000 41.560  0 151 PRO BBB CD    1 ? 2 
ATOM   4778  N N     . HIS B 1 152 ? 46.834  -50.263 24.483  1.000 40.681  0 152 HIS BBB N     1 ? 2 
ATOM   4779  C CA    . HIS B 1 152 ? 46.717  -49.967 25.939  1.000 40.690  0 152 HIS BBB CA    1 ? 2 
ATOM   4780  C C     . HIS B 1 152 ? 47.984  -49.326 26.524  1.000 40.227  0 152 HIS BBB C     1 ? 2 
ATOM   4781  O O     . HIS B 1 152 ? 48.042  -49.221 27.753  1.000 41.885  0 152 HIS BBB O     1 ? 2 
ATOM   4782  C CB    . HIS B 1 152 ? 46.365  -51.244 26.717  1.000 40.997  0 152 HIS BBB CB    1 ? 2 
ATOM   4783  C CG    . HIS B 1 152 ? 44.991  -51.738 26.436  1.000 41.455  0 152 HIS BBB CG    1 ? 2 
ATOM   4784  N ND1   . HIS B 1 152 ? 43.868  -51.054 26.868  1.000 40.486  0 152 HIS BBB ND1   1 ? 2 
ATOM   4785  C CD2   . HIS B 1 152 ? 44.559  -52.810 25.731  1.000 42.239  0 152 HIS BBB CD2   1 ? 2 
ATOM   4786  C CE1   . HIS B 1 152 ? 42.794  -51.701 26.462  1.000 41.547  0 152 HIS BBB CE1   1 ? 2 
ATOM   4787  N NE2   . HIS B 1 152 ? 43.187  -52.787 25.770  1.000 42.807  0 152 HIS BBB NE2   1 ? 2 
ATOM   4788  N N     . SER B 1 153 ? 48.945  -48.889 25.712  1.000 39.779  0 153 SER BBB N     1 ? 2 
ATOM   4789  C CA    . SER B 1 153 ? 50.293  -48.476 26.213  1.000 39.976  0 153 SER BBB CA    1 ? 2 
ATOM   4790  C C     . SER B 1 153 ? 50.771  -47.210 25.511  1.000 39.406  0 153 SER BBB C     1 ? 2 
ATOM   4791  O O     . SER B 1 153 ? 50.629  -47.138 24.274  1.000 35.911  0 153 SER BBB O     1 ? 2 
ATOM   4792  C CB    . SER B 1 153 ? 51.307  -49.584 26.058  1.000 39.501  0 153 SER BBB CB    1 ? 2 
ATOM   4793  O OG    . SER B 1 153 ? 50.744  -50.787 26.527  1.000 40.828  0 153 SER BBB OG    1 ? 2 
ATOM   4794  N N     . VAL B 1 154 ? 51.318  -46.281 26.292  1.000 42.560  0 154 VAL BBB N     1 ? 2 
ATOM   4795  C CA    . VAL B 1 154 ? 51.851  -44.979 25.802  1.000 45.583  0 154 VAL BBB CA    1 ? 2 
ATOM   4796  C C     . VAL B 1 154 ? 53.281  -44.820 26.336  1.000 46.309  0 154 VAL BBB C     1 ? 2 
ATOM   4797  O O     . VAL B 1 154 ? 53.529  -45.236 27.478  1.000 46.900  0 154 VAL BBB O     1 ? 2 
ATOM   4798  C CB    . VAL B 1 154 ? 50.943  -43.795 26.188  1.000 48.816  0 154 VAL BBB CB    1 ? 2 
ATOM   4799  C CG1   . VAL B 1 154 ? 49.520  -43.905 25.642  1.000 49.292  0 154 VAL BBB CG1   1 ? 2 
ATOM   4800  C CG2   . VAL B 1 154 ? 50.891  -43.577 27.688  1.000 52.969  0 154 VAL BBB CG2   1 ? 2 
ATOM   4801  N N     . GLU B 1 155 ? 54.177  -44.271 25.513  1.000 46.965  0 155 GLU BBB N     1 ? 2 
ATOM   4802  C CA    . GLU B 1 155 ? 55.625  -44.092 25.808  1.000 47.495  0 155 GLU BBB CA    1 ? 2 
ATOM   4803  C C     . GLU B 1 155 ? 55.969  -42.604 25.870  1.000 46.432  0 155 GLU BBB C     1 ? 2 
ATOM   4804  O O     . GLU B 1 155 ? 55.531  -41.884 24.980  1.000 46.025  0 155 GLU BBB O     1 ? 2 
ATOM   4805  C CB    . GLU B 1 155 ? 56.454  -44.731 24.702  1.000 49.619  0 155 GLU BBB CB    1 ? 2 
ATOM   4806  C CG    . GLU B 1 155 ? 57.940  -44.781 24.997  1.000 53.413  0 155 GLU BBB CG    1 ? 2 
ATOM   4807  C CD    . GLU B 1 155 ? 58.764  -45.481 23.920  1.000 55.975  0 155 GLU BBB CD    1 ? 2 
ATOM   4808  O OE1   . GLU B 1 155 ? 58.545  -45.211 22.697  1.000 55.752  0 155 GLU BBB OE1   1 ? 2 
ATOM   4809  O OE2   . GLU B 1 155 ? 59.610  -46.318 24.299  1.000 62.395  0 155 GLU BBB OE2   1 ? 2 
ATOM   4810  N N     . TYR B 1 156 ? 56.743  -42.186 26.869  1.000 49.462  0 156 TYR BBB N     1 ? 2 
ATOM   4811  C CA    . TYR B 1 156 ? 57.323  -40.819 26.974  1.000 48.461  0 156 TYR BBB CA    1 ? 2 
ATOM   4812  C C     . TYR B 1 156 ? 58.751  -40.867 27.539  1.000 49.846  0 156 TYR BBB C     1 ? 2 
ATOM   4813  O O     . TYR B 1 156 ? 59.085  -41.784 28.315  1.000 44.737  0 156 TYR BBB O     1 ? 2 
ATOM   4814  C CB    . TYR B 1 156 ? 56.416  -39.938 27.832  1.000 46.858  0 156 TYR BBB CB    1 ? 2 
ATOM   4815  C CG    . TYR B 1 156 ? 56.376  -40.274 29.294  1.000 46.172  0 156 TYR BBB CG    1 ? 2 
ATOM   4816  C CD1   . TYR B 1 156 ? 55.612  -41.333 29.763  1.000 45.292  0 156 TYR BBB CD1   1 ? 2 
ATOM   4817  C CD2   . TYR B 1 156 ? 57.113  -39.537 30.210  1.000 45.628  0 156 TYR BBB CD2   1 ? 2 
ATOM   4818  C CE1   . TYR B 1 156 ? 55.579  -41.650 31.112  1.000 44.959  0 156 TYR BBB CE1   1 ? 2 
ATOM   4819  C CE2   . TYR B 1 156 ? 57.092  -39.835 31.562  1.000 44.742  0 156 TYR BBB CE2   1 ? 2 
ATOM   4820  C CZ    . TYR B 1 156 ? 56.320  -40.895 32.010  1.000 45.813  0 156 TYR BBB CZ    1 ? 2 
ATOM   4821  O OH    . TYR B 1 156 ? 56.288  -41.177 33.342  1.000 46.126  0 156 TYR BBB OH    1 ? 2 
ATOM   4822  N N     . GLU B 1 157 ? 59.555  -39.876 27.154  1.000 54.318  0 157 GLU BBB N     1 ? 2 
ATOM   4823  C CA    . GLU B 1 157 ? 60.907  -39.604 27.710  1.000 56.756  0 157 GLU BBB CA    1 ? 2 
ATOM   4824  C C     . GLU B 1 157 ? 60.772  -38.835 29.026  1.000 58.307  0 157 GLU BBB C     1 ? 2 
ATOM   4825  O O     . GLU B 1 157 ? 59.849  -38.009 29.149  1.000 56.979  0 157 GLU BBB O     1 ? 2 
ATOM   4826  C CB    . GLU B 1 157 ? 61.760  -38.783 26.743  1.000 59.954  0 157 GLU BBB CB    1 ? 2 
ATOM   4827  C CG    . GLU B 1 157 ? 62.633  -39.631 25.827  1.000 66.063  0 157 GLU BBB CG    1 ? 2 
ATOM   4828  C CD    . GLU B 1 157 ? 63.895  -38.945 25.334  1.000 68.726  0 157 GLU BBB CD    1 ? 2 
ATOM   4829  O OE1   . GLU B 1 157 ? 64.260  -37.882 25.899  1.000 70.862  0 157 GLU BBB OE1   1 ? 2 
ATOM   4830  O OE2   . GLU B 1 157 ? 64.505  -39.475 24.393  1.000 72.807  0 157 GLU BBB OE2   1 ? 2 
ATOM   4831  N N     . ASP B 1 158 ? 61.685  -39.110 29.956  1.000 61.504  0 158 ASP BBB N     1 ? 2 
ATOM   4832  C CA    . ASP B 1 158 ? 61.765  -38.507 31.306  1.000 62.070  0 158 ASP BBB CA    1 ? 2 
ATOM   4833  C C     . ASP B 1 158 ? 63.228  -38.616 31.779  1.000 64.682  0 158 ASP BBB C     1 ? 2 
ATOM   4834  O O     . ASP B 1 158 ? 63.646  -39.734 32.129  1.000 60.335  0 158 ASP BBB O     1 ? 2 
ATOM   4835  C CB    . ASP B 1 158 ? 60.768  -39.209 32.235  1.000 61.292  0 158 ASP BBB CB    1 ? 2 
ATOM   4836  C CG    . ASP B 1 158 ? 60.906  -38.786 33.690  1.000 59.280  0 158 ASP BBB CG    1 ? 2 
ATOM   4837  O OD1   . ASP B 1 158 ? 61.052  -37.564 33.936  1.000 58.179  0 158 ASP BBB OD1   1 ? 2 
ATOM   4838  O OD2   . ASP B 1 158 ? 60.887  -39.670 34.566  1.000 57.349  0 158 ASP BBB OD2   1 ? 2 
ATOM   4839  N N     . ASN B 1 159 ? 63.976  -37.507 31.756  1.000 66.473  0 159 ASN BBB N     1 ? 2 
ATOM   4840  C CA    . ASN B 1 159 ? 65.451  -37.481 31.929  1.000 70.229  0 159 ASN BBB CA    1 ? 2 
ATOM   4841  C C     . ASN B 1 159 ? 66.080  -38.371 30.845  1.000 70.960  0 159 ASN BBB C     1 ? 2 
ATOM   4842  O O     . ASN B 1 159 ? 66.977  -39.177 31.187  1.000 67.641  0 159 ASN BBB O     1 ? 2 
ATOM   4843  C CB    . ASN B 1 159 ? 65.869  -37.896 33.348  1.000 73.496  0 159 ASN BBB CB    1 ? 2 
ATOM   4844  C CG    . ASN B 1 159 ? 65.506  -36.864 34.405  1.000 75.249  0 159 ASN BBB CG    1 ? 2 
ATOM   4845  O OD1   . ASN B 1 159 ? 66.251  -35.905 34.640  1.000 68.074  0 159 ASN BBB OD1   1 ? 2 
ATOM   4846  N ND2   . ASN B 1 159 ? 64.363  -37.050 35.054  1.000 73.623  0 159 ASN BBB ND2   1 ? 2 
ATOM   4847  N N     . GLY B 1 160 ? 65.601  -38.261 29.596  1.000 70.900  0 160 GLY BBB N     1 ? 2 
ATOM   4848  C CA    . GLY B 1 160 ? 66.112  -39.031 28.445  1.000 73.788  0 160 GLY BBB CA    1 ? 2 
ATOM   4849  C C     . GLY B 1 160 ? 66.042  -40.533 28.673  1.000 77.411  0 160 GLY BBB C     1 ? 2 
ATOM   4850  O O     . GLY B 1 160 ? 66.937  -41.258 28.201  1.000 75.053  0 160 GLY BBB O     1 ? 2 
ATOM   4851  N N     . GLN B 1 161 ? 65.001  -40.990 29.378  1.000 81.043  0 161 GLN BBB N     1 ? 2 
ATOM   4852  C CA    . GLN B 1 161 ? 64.738  -42.425 29.660  1.000 77.638  0 161 GLN BBB CA    1 ? 2 
ATOM   4853  C C     . GLN B 1 161 ? 63.274  -42.718 29.318  1.000 72.389  0 161 GLN BBB C     1 ? 2 
ATOM   4854  O O     . GLN B 1 161 ? 62.375  -42.336 30.105  1.000 66.447  0 161 GLN BBB O     1 ? 2 
ATOM   4855  C CB    . GLN B 1 161 ? 65.071  -42.755 31.107  1.000 81.435  0 161 GLN BBB CB    1 ? 2 
ATOM   4856  C CG    . GLN B 1 161 ? 66.567  -42.754 31.375  1.000 86.881  0 161 GLN BBB CG    1 ? 2 
ATOM   4857  C CD    . GLN B 1 161 ? 66.899  -43.239 32.764  1.000 88.481  0 161 GLN BBB CD    1 ? 2 
ATOM   4858  O OE1   . GLN B 1 161 ? 66.030  -43.601 33.555  1.000 90.656  0 161 GLN BBB OE1   1 ? 2 
ATOM   4859  N NE2   . GLN B 1 161 ? 68.182  -43.246 33.082  1.000 85.650  0 161 GLN BBB NE2   1 ? 2 
ATOM   4860  N N     . LYS B 1 162 ? 63.066  -43.368 28.174  1.000 68.809  0 162 LYS BBB N     1 ? 2 
ATOM   4861  C CA    . LYS B 1 162 ? 61.767  -43.932 27.748  1.000 67.186  0 162 LYS BBB CA    1 ? 2 
ATOM   4862  C C     . LYS B 1 162 ? 61.092  -44.615 28.940  1.000 62.918  0 162 LYS BBB C     1 ? 2 
ATOM   4863  O O     . LYS B 1 162 ? 61.747  -45.413 29.629  1.000 56.983  0 162 LYS BBB O     1 ? 2 
ATOM   4864  C CB    . LYS B 1 162 ? 61.953  -44.918 26.598  1.000 69.167  0 162 LYS BBB CB    1 ? 2 
ATOM   4865  C CG    . LYS B 1 162 ? 62.493  -44.282 25.326  1.000 74.707  0 162 LYS BBB CG    1 ? 2 
ATOM   4866  C CD    . LYS B 1 162 ? 61.649  -43.154 24.788  1.000 78.023  0 162 LYS BBB CD    1 ? 2 
ATOM   4867  C CE    . LYS B 1 162 ? 61.776  -42.938 23.293  1.000 82.699  0 162 LYS BBB CE    1 ? 2 
ATOM   4868  N NZ    . LYS B 1 162 ? 60.552  -42.303 22.735  1.000 85.272  0 162 LYS BBB NZ    1 ? 2 
ATOM   4869  N N     . LYS B 1 163 ? 59.827  -44.264 29.168  1.000 58.652  0 163 LYS BBB N     1 ? 2 
ATOM   4870  C CA    . LYS B 1 163 ? 58.934  -44.926 30.140  1.000 58.842  0 163 LYS BBB CA    1 ? 2 
ATOM   4871  C C     . LYS B 1 163 ? 57.661  -45.314 29.394  1.000 57.653  0 163 LYS BBB C     1 ? 2 
ATOM   4872  O O     . LYS B 1 163 ? 57.299  -44.629 28.420  1.000 58.953  0 163 LYS BBB O     1 ? 2 
ATOM   4873  C CB    . LYS B 1 163 ? 58.631  -44.004 31.319  1.000 60.492  0 163 LYS BBB CB    1 ? 2 
ATOM   4874  C CG    . LYS B 1 163 ? 59.837  -43.723 32.192  1.000 62.614  0 163 LYS BBB CG    1 ? 2 
ATOM   4875  C CD    . LYS B 1 163 ? 59.488  -43.154 33.546  1.000 66.110  0 163 LYS BBB CD    1 ? 2 
ATOM   4876  C CE    . LYS B 1 163 ? 60.714  -43.040 34.435  1.000 69.180  0 163 LYS BBB CE    1 ? 2 
ATOM   4877  N NZ    . LYS B 1 163 ? 60.373  -42.917 35.872  1.000 72.516  0 163 LYS BBB NZ    1 ? 2 
ATOM   4878  N N     . THR B 1 164 ? 57.045  -46.409 29.821  1.000 54.969  0 164 THR BBB N     1 ? 2 
ATOM   4879  C CA    . THR B 1 164 ? 55.797  -46.941 29.242  1.000 51.536  0 164 THR BBB CA    1 ? 2 
ATOM   4880  C C     . THR B 1 164 ? 54.808  -47.063 30.393  1.000 50.496  0 164 THR BBB C     1 ? 2 
ATOM   4881  O O     . THR B 1 164 ? 55.228  -47.472 31.490  1.000 51.296  0 164 THR BBB O     1 ? 2 
ATOM   4882  C CB    . THR B 1 164 ? 56.052  -48.251 28.488  1.000 51.250  0 164 THR BBB CB    1 ? 2 
ATOM   4883  O OG1   . THR B 1 164 ? 56.975  -48.027 27.432  1.000 49.247  0 164 THR BBB OG1   1 ? 2 
ATOM   4884  C CG2   . THR B 1 164 ? 54.796  -48.843 27.898  1.000 51.994  0 164 THR BBB CG2   1 ? 2 
ATOM   4885  N N     . ILE B 1 165 ? 53.560  -46.672 30.160  1.000 47.590  0 165 ILE BBB N     1 ? 2 
ATOM   4886  C CA    . ILE B 1 165 ? 52.451  -46.827 31.144  1.000 47.165  0 165 ILE BBB CA    1 ? 2 
ATOM   4887  C C     . ILE B 1 165 ? 51.236  -47.381 30.400  1.000 45.490  0 165 ILE BBB C     1 ? 2 
ATOM   4888  O O     . ILE B 1 165 ? 51.109  -47.156 29.189  1.000 42.155  0 165 ILE BBB O     1 ? 2 
ATOM   4889  C CB    . ILE B 1 165 ? 52.154  -45.495 31.859  1.000 47.405  0 165 ILE BBB CB    1 ? 2 
ATOM   4890  C CG1   . ILE B 1 165 ? 51.622  -44.440 30.874  1.000 48.228  0 165 ILE BBB CG1   1 ? 2 
ATOM   4891  C CG2   . ILE B 1 165 ? 53.385  -45.007 32.617  1.000 46.370  0 165 ILE BBB CG2   1 ? 2 
ATOM   4892  C CD1   . ILE B 1 165 ? 50.966  -43.264 31.540  1.000 48.724  0 165 ILE BBB CD1   1 ? 2 
ATOM   4893  N N     . THR B 1 166 ? 50.359  -48.068 31.128  1.000 46.902  0 166 THR BBB N     1 ? 2 
ATOM   4894  C CA    . THR B 1 166 ? 49.233  -48.838 30.555  1.000 45.304  0 166 THR BBB CA    1 ? 2 
ATOM   4895  C C     . THR B 1 166 ? 47.930  -48.198 31.024  1.000 45.858  0 166 THR BBB C     1 ? 2 
ATOM   4896  O O     . THR B 1 166 ? 47.869  -47.728 32.201  1.000 47.638  0 166 THR BBB O     1 ? 2 
ATOM   4897  C CB    . THR B 1 166 ? 49.331  -50.313 30.944  1.000 45.616  0 166 THR BBB CB    1 ? 2 
ATOM   4898  O OG1   . THR B 1 166 ? 49.346  -50.343 32.368  1.000 47.318  0 166 THR BBB OG1   1 ? 2 
ATOM   4899  C CG2   . THR B 1 166 ? 50.555  -50.998 30.378  1.000 46.309  0 166 THR BBB CG2   1 ? 2 
ATOM   4900  N N     . SER B 1 167 ? 46.922  -48.200 30.149  1.000 43.532  0 167 SER BBB N     1 ? 2 
ATOM   4901  C CA    . SER B 1 167 ? 45.582  -47.654 30.451  1.000 41.645  0 167 SER BBB CA    1 ? 2 
ATOM   4902  C C     . SER B 1 167 ? 44.481  -48.536 29.856  1.000 42.293  0 167 SER BBB C     1 ? 2 
ATOM   4903  O O     . SER B 1 167 ? 44.696  -49.114 28.763  1.000 42.665  0 167 SER BBB O     1 ? 2 
ATOM   4904  C CB    . SER B 1 167 ? 45.488  -46.245 29.943  1.000 41.460  0 167 SER BBB CB    1 ? 2 
ATOM   4905  O OG    . SER B 1 167 ? 44.584  -45.503 30.738  1.000 42.733  0 167 SER BBB OG    1 ? 2 
ATOM   4906  N N     . ARG B 1 168 ? 43.330  -48.595 30.535  1.000 42.692  0 168 ARG BBB N     1 ? 2 
ATOM   4907  C CA    . ARG B 1 168 ? 42.081  -49.201 30.016  1.000 42.266  0 168 ARG BBB CA    1 ? 2 
ATOM   4908  C C     . ARG B 1 168 ? 41.730  -48.445 28.735  1.000 40.427  0 168 ARG BBB C     1 ? 2 
ATOM   4909  O O     . ARG B 1 168 ? 41.524  -49.087 27.679  1.000 41.836  0 168 ARG BBB O     1 ? 2 
ATOM   4910  C CB    . ARG B 1 168 ? 40.993  -49.162 31.101  1.000 45.570  0 168 ARG BBB CB    1 ? 2 
ATOM   4911  C CG    . ARG B 1 168 ? 39.751  -49.993 30.793  1.000 49.492  0 168 ARG BBB CG    1 ? 2 
ATOM   4912  C CD    . ARG B 1 168 ? 38.925  -50.232 32.017  1.000 53.769  0 168 ARG BBB CD    1 ? 2 
ATOM   4913  N NE    . ARG B 1 168 ? 37.634  -50.822 31.677  1.000 57.820  0 168 ARG BBB NE    1 ? 2 
ATOM   4914  C CZ    . ARG B 1 168 ? 36.647  -51.079 32.542  1.000 57.502  0 168 ARG BBB CZ    1 ? 2 
ATOM   4915  N NH1   . ARG B 1 168 ? 36.800  -50.812 33.830  1.000 59.825  0 168 ARG BBB NH1   1 ? 2 
ATOM   4916  N NH2   . ARG B 1 168 ? 35.520  -51.621 32.105  1.000 55.645  0 168 ARG BBB NH2   1 ? 2 
ATOM   4917  N N     . TYR B 1 169 ? 41.740  -47.114 28.814  1.000 38.364  0 169 TYR BBB N     1 ? 2 
ATOM   4918  C CA    . TYR B 1 169 ? 41.266  -46.182 27.755  1.000 37.111  0 169 TYR BBB CA    1 ? 2 
ATOM   4919  C C     . TYR B 1 169 ? 42.356  -45.144 27.449  1.000 35.611  0 169 TYR BBB C     1 ? 2 
ATOM   4920  O O     . TYR B 1 169 ? 43.074  -44.738 28.345  1.000 36.301  0 169 TYR BBB O     1 ? 2 
ATOM   4921  C CB    . TYR B 1 169 ? 39.939  -45.553 28.177  1.000 36.915  0 169 TYR BBB CB    1 ? 2 
ATOM   4922  C CG    . TYR B 1 169 ? 38.804  -46.521 28.393  1.000 37.235  0 169 TYR BBB CG    1 ? 2 
ATOM   4923  C CD1   . TYR B 1 169 ? 38.351  -47.354 27.381  1.000 37.301  0 169 TYR BBB CD1   1 ? 2 
ATOM   4924  C CD2   . TYR B 1 169 ? 38.171  -46.604 29.623  1.000 38.703  0 169 TYR BBB CD2   1 ? 2 
ATOM   4925  C CE1   . TYR B 1 169 ? 37.309  -48.239 27.601  1.000 37.121  0 169 TYR BBB CE1   1 ? 2 
ATOM   4926  C CE2   . TYR B 1 169 ? 37.115  -47.480 29.859  1.000 37.546  0 169 TYR BBB CE2   1 ? 2 
ATOM   4927  C CZ    . TYR B 1 169 ? 36.667  -48.280 28.832  1.000 36.574  0 169 TYR BBB CZ    1 ? 2 
ATOM   4928  O OH    . TYR B 1 169 ? 35.630  -49.131 29.052  1.000 35.959  0 169 TYR BBB OH    1 ? 2 
ATOM   4929  N N     . ILE B 1 170 ? 42.510  -44.794 26.177  1.000 35.316  0 170 ILE BBB N     1 ? 2 
ATOM   4930  C CA    . ILE B 1 170 ? 43.450  -43.722 25.726  1.000 34.351  0 170 ILE BBB CA    1 ? 2 
ATOM   4931  C C     . ILE B 1 170 ? 42.622  -42.726 24.923  1.000 32.748  0 170 ILE BBB C     1 ? 2 
ATOM   4932  O O     . ILE B 1 170 ? 41.816  -43.167 24.118  1.000 36.645  0 170 ILE BBB O     1 ? 2 
ATOM   4933  C CB    . ILE B 1 170 ? 44.649  -44.277 24.931  1.000 34.980  0 170 ILE BBB CB    1 ? 2 
ATOM   4934  C CG1   . ILE B 1 170 ? 45.520  -45.155 25.829  1.000 35.473  0 170 ILE BBB CG1   1 ? 2 
ATOM   4935  C CG2   . ILE B 1 170 ? 45.468  -43.149 24.328  1.000 36.442  0 170 ILE BBB CG2   1 ? 2 
ATOM   4936  C CD1   . ILE B 1 170 ? 46.506  -46.027 25.086  1.000 35.498  0 170 ILE BBB CD1   1 ? 2 
ATOM   4937  N N     . LEU B 1 171 ? 42.792  -41.443 25.195  1.000 29.122  0 171 LEU BBB N     1 ? 2 
ATOM   4938  C CA    . LEU B 1 171 ? 42.146  -40.329 24.477  1.000 27.398  0 171 LEU BBB CA    1 ? 2 
ATOM   4939  C C     . LEU B 1 171 ? 43.231  -39.512 23.784  1.000 25.614  0 171 LEU BBB C     1 ? 2 
ATOM   4940  O O     . LEU B 1 171 ? 44.110  -39.023 24.468  1.000 24.487  0 171 LEU BBB O     1 ? 2 
ATOM   4941  C CB    . LEU B 1 171 ? 41.345  -39.448 25.447  1.000 27.264  0 171 LEU BBB CB    1 ? 2 
ATOM   4942  C CG    . LEU B 1 171 ? 40.846  -38.137 24.864  1.000 26.785  0 171 LEU BBB CG    1 ? 2 
ATOM   4943  C CD1   . LEU B 1 171 ? 39.961  -38.436 23.683  1.000 27.748  0 171 LEU BBB CD1   1 ? 2 
ATOM   4944  C CD2   . LEU B 1 171 ? 40.096  -37.311 25.900  1.000 27.331  0 171 LEU BBB CD2   1 ? 2 
ATOM   4945  N N     . LEU B 1 172 ? 43.124  -39.382 22.469  1.000 25.202  0 172 LEU BBB N     1 ? 2 
ATOM   4946  C CA    . LEU B 1 172 ? 43.955  -38.496 21.634  1.000 24.925  0 172 LEU BBB CA    1 ? 2 
ATOM   4947  C C     . LEU B 1 172 ? 43.251  -37.155 21.501  1.000 24.472  0 172 LEU BBB C     1 ? 2 
ATOM   4948  O O     . LEU B 1 172 ? 42.081  -37.143 21.080  1.000 23.993  0 172 LEU BBB O     1 ? 2 
ATOM   4949  C CB    . LEU B 1 172 ? 44.135  -39.182 20.281  1.000 24.861  0 172 LEU BBB CB    1 ? 2 
ATOM   4950  C CG    . LEU B 1 172 ? 44.680  -40.608 20.355  1.000 25.462  0 172 LEU BBB CG    1 ? 2 
ATOM   4951  C CD1   . LEU B 1 172 ? 44.677  -41.257 18.972  1.000 26.096  0 172 LEU BBB CD1   1 ? 2 
ATOM   4952  C CD2   . LEU B 1 172 ? 46.083  -40.603 20.939  1.000 25.124  0 172 LEU BBB CD2   1 ? 2 
ATOM   4953  N N     . ALA B 1 173 ? 43.922  -36.074 21.892  1.000 24.953  0 173 ALA BBB N     1 ? 2 
ATOM   4954  C CA    . ALA B 1 173 ? 43.426  -34.679 21.730  1.000 24.918  0 173 ALA BBB CA    1 ? 2 
ATOM   4955  C C     . ALA B 1 173 ? 44.636  -33.757 21.576  1.000 24.978  0 173 ALA BBB C     1 ? 2 
ATOM   4956  O O     . ALA B 1 173 ? 44.791  -32.850 22.358  1.000 23.290  0 173 ALA BBB O     1 ? 2 
ATOM   4957  C CB    . ALA B 1 173 ? 42.572  -34.293 22.896  1.000 24.824  0 173 ALA BBB CB    1 ? 2 
ATOM   4958  N N     . THR B 1 174 ? 45.453  -34.024 20.553  1.000 26.501  0 174 THR BBB N     1 ? 2 
ATOM   4959  C CA    . THR B 1 174 ? 46.758  -33.366 20.279  1.000 26.398  0 174 THR BBB CA    1 ? 2 
ATOM   4960  C C     . THR B 1 174 ? 46.575  -32.084 19.458  1.000 25.845  0 174 THR BBB C     1 ? 2 
ATOM   4961  O O     . THR B 1 174 ? 47.580  -31.339 19.295  1.000 26.129  0 174 THR BBB O     1 ? 2 
ATOM   4962  C CB    . THR B 1 174 ? 47.699  -34.377 19.629  1.000 25.664  0 174 THR BBB CB    1 ? 2 
ATOM   4963  O OG1   . THR B 1 174 ? 47.035  -34.928 18.500  1.000 23.945  0 174 THR BBB OG1   1 ? 2 
ATOM   4964  C CG2   . THR B 1 174 ? 48.085  -35.474 20.600  1.000 25.971  0 174 THR BBB CG2   1 ? 2 
ATOM   4965  N N     . GLY B 1 175 ? 45.355  -31.812 18.983  1.000 25.425  0 175 GLY BBB N     1 ? 2 
ATOM   4966  C CA    . GLY B 1 175 ? 45.045  -30.583 18.217  1.000 26.069  0 175 GLY BBB CA    1 ? 2 
ATOM   4967  C C     . GLY B 1 175 ? 45.770  -30.516 16.877  1.000 26.398  0 175 GLY BBB C     1 ? 2 
ATOM   4968  O O     . GLY B 1 175 ? 46.401  -31.518 16.481  1.000 27.194  0 175 GLY BBB O     1 ? 2 
ATOM   4969  N N     . GLY B 1 176 ? 45.703  -29.376 16.206  1.000 26.367  0 176 GLY BBB N     1 ? 2 
ATOM   4970  C CA    . GLY B 1 176 ? 46.493  -29.090 14.996  1.000 26.247  0 176 GLY BBB CA    1 ? 2 
ATOM   4971  C C     . GLY B 1 176 ? 47.665  -28.140 15.285  1.000 26.663  0 176 GLY BBB C     1 ? 2 
ATOM   4972  O O     . GLY B 1 176 ? 47.922  -27.743 16.493  1.000 24.789  0 176 GLY BBB O     1 ? 2 
ATOM   4973  N N     . ARG B 1 177 ? 48.377  -27.814 14.213  1.000 27.042  0 177 ARG BBB N     1 ? 2 
ATOM   4974  C CA    . ARG B 1 177 ? 49.370  -26.715 14.110  1.000 26.581  0 177 ARG BBB CA    1 ? 2 
ATOM   4975  C C     . ARG B 1 177 ? 49.206  -26.049 12.739  1.000 25.825  0 177 ARG BBB C     1 ? 2 
ATOM   4976  O O     . ARG B 1 177 ? 48.673  -26.632 11.795  1.000 23.532  0 177 ARG BBB O     1 ? 2 
ATOM   4977  C CB    . ARG B 1 177 ? 50.764  -27.281 14.387  1.000 27.659  0 177 ARG BBB CB    1 ? 2 
ATOM   4978  C CG    . ARG B 1 177 ? 50.914  -27.849 15.804  1.000 28.674  0 177 ARG BBB CG    1 ? 2 
ATOM   4979  C CD    . ARG B 1 177 ? 50.671  -26.839 16.931  1.000 27.982  0 177 ARG BBB CD    1 ? 2 
ATOM   4980  N NE    . ARG B 1 177 ? 51.771  -25.889 16.909  1.000 27.943  0 177 ARG BBB NE    1 ? 2 
ATOM   4981  C CZ    . ARG B 1 177 ? 52.946  -26.088 17.491  1.000 28.518  0 177 ARG BBB CZ    1 ? 2 
ATOM   4982  N NH1   . ARG B 1 177 ? 53.143  -27.195 18.194  1.000 27.386  0 177 ARG BBB NH1   1 ? 2 
ATOM   4983  N NH2   . ARG B 1 177 ? 53.895  -25.167 17.380  1.000 28.467  0 177 ARG BBB NH2   1 ? 2 
ATOM   4984  N N     . PRO B 1 178 ? 49.613  -24.777 12.615  1.000 27.178  0 178 PRO BBB N     1 ? 2 
ATOM   4985  C CA    . PRO B 1 178 ? 49.438  -24.041 11.369  1.000 29.564  0 178 PRO BBB CA    1 ? 2 
ATOM   4986  C C     . PRO B 1 178 ? 50.077  -24.795 10.203  1.000 32.648  0 178 PRO BBB C     1 ? 2 
ATOM   4987  O O     . PRO B 1 178 ? 51.124  -25.388 10.384  1.000 34.074  0 178 PRO BBB O     1 ? 2 
ATOM   4988  C CB    . PRO B 1 178 ? 50.123  -22.700 11.612  1.000 29.331  0 178 PRO BBB CB    1 ? 2 
ATOM   4989  C CG    . PRO B 1 178 ? 50.141  -22.570 13.134  1.000 28.656  0 178 PRO BBB CG    1 ? 2 
ATOM   4990  C CD    . PRO B 1 178 ? 50.247  -23.977 13.671  1.000 27.683  0 178 PRO BBB CD    1 ? 2 
ATOM   4991  N N     . SER B 1 179 ? 49.430  -24.765 9.043   1.000 35.866  0 179 SER BBB N     1 ? 2 
ATOM   4992  C CA    . SER B 1 179 ? 49.960  -25.359 7.793   1.000 38.576  0 179 SER BBB CA    1 ? 2 
ATOM   4993  C C     . SER B 1 179 ? 50.528  -24.260 6.886   1.000 37.261  0 179 SER BBB C     1 ? 2 
ATOM   4994  O O     . SER B 1 179 ? 49.886  -23.214 6.685   1.000 34.106  0 179 SER BBB O     1 ? 2 
ATOM   4995  C CB    . SER B 1 179 ? 48.929  -26.181 7.099   1.000 40.912  0 179 SER BBB CB    1 ? 2 
ATOM   4996  O OG    . SER B 1 179 ? 49.541  -26.963 6.094   1.000 46.701  0 179 SER BBB OG    1 ? 2 
ATOM   4997  N N     . ILE B 1 180 ? 51.767  -24.488 6.460   1.000 39.845  0 180 ILE BBB N     1 ? 2 
ATOM   4998  C CA    . ILE B 1 180 ? 52.530  -23.617 5.530   1.000 40.470  0 180 ILE BBB CA    1 ? 2 
ATOM   4999  C C     . ILE B 1 180 ? 52.787  -24.434 4.275   1.000 40.160  0 180 ILE BBB C     1 ? 2 
ATOM   5000  O O     . ILE B 1 180 ? 53.348  -25.515 4.372   1.000 40.288  0 180 ILE BBB O     1 ? 2 
ATOM   5001  C CB    . ILE B 1 180 ? 53.842  -23.124 6.154   1.000 41.309  0 180 ILE BBB CB    1 ? 2 
ATOM   5002  C CG1   . ILE B 1 180 ? 53.617  -22.472 7.521   1.000 41.303  0 180 ILE BBB CG1   1 ? 2 
ATOM   5003  C CG2   . ILE B 1 180 ? 54.551  -22.204 5.159   1.000 41.518  0 180 ILE BBB CG2   1 ? 2 
ATOM   5004  C CD1   . ILE B 1 180 ? 54.888  -21.960 8.173   1.000 42.877  0 180 ILE BBB CD1   1 ? 2 
ATOM   5005  N N     . PRO B 1 181 ? 52.407  -23.934 3.076   1.000 42.649  0 181 PRO BBB N     1 ? 2 
ATOM   5006  C CA    . PRO B 1 181 ? 52.664  -24.656 1.823   1.000 41.948  0 181 PRO BBB CA    1 ? 2 
ATOM   5007  C C     . PRO B 1 181 ? 54.165  -24.887 1.535   1.000 43.158  0 181 PRO BBB C     1 ? 2 
ATOM   5008  O O     . PRO B 1 181 ? 54.899  -23.912 1.431   1.000 39.333  0 181 PRO BBB O     1 ? 2 
ATOM   5009  C CB    . PRO B 1 181 ? 52.042  -23.740 0.764   1.000 43.441  0 181 PRO BBB CB    1 ? 2 
ATOM   5010  C CG    . PRO B 1 181 ? 51.964  -22.359 1.403   1.000 42.412  0 181 PRO BBB CG    1 ? 2 
ATOM   5011  C CD    . PRO B 1 181 ? 51.746  -22.628 2.868   1.000 42.937  0 181 PRO BBB CD    1 ? 2 
ATOM   5012  N N     . GLU B 1 182 ? 54.574  -26.162 1.455   1.000 49.800  0 182 GLU BBB N     1 ? 2 
ATOM   5013  C CA    . GLU B 1 182 ? 55.967  -26.654 1.242   1.000 56.996  0 182 GLU BBB CA    1 ? 2 
ATOM   5014  C C     . GLU B 1 182 ? 56.389  -26.355 -0.203  1.000 58.365  0 182 GLU BBB C     1 ? 2 
ATOM   5015  O O     . GLU B 1 182 ? 57.597  -26.126 -0.425  1.000 56.125  0 182 GLU BBB O     1 ? 2 
ATOM   5016  C CB    . GLU B 1 182 ? 56.056  -28.155 1.557   1.000 61.022  0 182 GLU BBB CB    1 ? 2 
ATOM   5017  C CG    . GLU B 1 182 ? 55.904  -28.484 3.043   1.000 65.092  0 182 GLU BBB CG    1 ? 2 
ATOM   5018  C CD    . GLU B 1 182 ? 54.831  -29.516 3.419   1.000 74.003  0 182 GLU BBB CD    1 ? 2 
ATOM   5019  O OE1   . GLU B 1 182 ? 54.546  -30.397 2.570   1.000 75.191  0 182 GLU BBB OE1   1 ? 2 
ATOM   5020  O OE2   . GLU B 1 182 ? 54.243  -29.418 4.543   1.000 75.929  0 182 GLU BBB OE2   1 ? 2 
ATOM   5021  N N     . THR B 1 183 ? 55.414  -26.268 -1.117  1.000 60.891  0 183 THR BBB N     1 ? 2 
ATOM   5022  C CA    . THR B 1 183 ? 55.608  -26.035 -2.579  1.000 63.699  0 183 THR BBB CA    1 ? 2 
ATOM   5023  C C     . THR B 1 183 ? 56.042  -24.582 -2.851  1.000 61.649  0 183 THR BBB C     1 ? 2 
ATOM   5024  O O     . THR B 1 183 ? 56.851  -24.397 -3.782  1.000 57.251  0 183 THR BBB O     1 ? 2 
ATOM   5025  C CB    . THR B 1 183 ? 54.343  -26.429 -3.354  1.000 65.169  0 183 THR BBB CB    1 ? 2 
ATOM   5026  O OG1   . THR B 1 183 ? 53.269  -25.577 -2.938  1.000 68.090  0 183 THR BBB OG1   1 ? 2 
ATOM   5027  C CG2   . THR B 1 183 ? 53.974  -27.883 -3.140  1.000 65.581  0 183 THR BBB CG2   1 ? 2 
ATOM   5028  N N     . VAL B 1 184 ? 55.561  -23.598 -2.073  1.000 58.530  0 184 VAL BBB N     1 ? 2 
ATOM   5029  C CA    . VAL B 1 184 ? 55.926  -22.156 -2.248  1.000 56.980  0 184 VAL BBB CA    1 ? 2 
ATOM   5030  C C     . VAL B 1 184 ? 57.293  -21.887 -1.613  1.000 54.849  0 184 VAL BBB C     1 ? 2 
ATOM   5031  O O     . VAL B 1 184 ? 57.440  -21.943 -0.400  1.000 54.204  0 184 VAL BBB O     1 ? 2 
ATOM   5032  C CB    . VAL B 1 184 ? 54.856  -21.198 -1.695  1.000 53.760  0 184 VAL BBB CB    1 ? 2 
ATOM   5033  C CG1   . VAL B 1 184 ? 55.362  -19.769 -1.704  1.000 54.633  0 184 VAL BBB CG1   1 ? 2 
ATOM   5034  C CG2   . VAL B 1 184 ? 53.557  -21.291 -2.472  1.000 55.021  0 184 VAL BBB CG2   1 ? 2 
ATOM   5035  N N     . PRO B 1 185 ? 58.335  -21.587 -2.415  1.000 55.882  0 185 PRO BBB N     1 ? 2 
ATOM   5036  C CA    . PRO B 1 185 ? 59.686  -21.381 -1.884  1.000 54.745  0 185 PRO BBB CA    1 ? 2 
ATOM   5037  C C     . PRO B 1 185 ? 59.821  -20.139 -0.987  1.000 52.317  0 185 PRO BBB C     1 ? 2 
ATOM   5038  O O     . PRO B 1 185 ? 59.260  -19.088 -1.339  1.000 51.895  0 185 PRO BBB O     1 ? 2 
ATOM   5039  C CB    . PRO B 1 185 ? 60.568  -21.180 -3.133  1.000 55.878  0 185 PRO BBB CB    1 ? 2 
ATOM   5040  C CG    . PRO B 1 185 ? 59.716  -21.660 -4.307  1.000 57.237  0 185 PRO BBB CG    1 ? 2 
ATOM   5041  C CD    . PRO B 1 185 ? 58.275  -21.458 -3.888  1.000 58.457  0 185 PRO BBB CD    1 ? 2 
ATOM   5042  N N     . GLY B 1 186 ? 60.562  -20.290 0.117   1.000 48.203  0 186 GLY BBB N     1 ? 2 
ATOM   5043  C CA    . GLY B 1 186 ? 60.787  -19.249 1.137   1.000 50.241  0 186 GLY BBB CA    1 ? 2 
ATOM   5044  C C     . GLY B 1 186 ? 59.706  -19.189 2.236   1.000 48.509  0 186 GLY BBB C     1 ? 2 
ATOM   5045  O O     . GLY B 1 186 ? 59.979  -18.586 3.283   1.000 47.527  0 186 GLY BBB O     1 ? 2 
ATOM   5046  N N     . ALA B 1 187 ? 58.545  -19.818 2.034   1.000 47.152  0 187 ALA BBB N     1 ? 2 
ATOM   5047  C CA    . ALA B 1 187 ? 57.362  -19.763 2.922   1.000 46.197  0 187 ALA BBB CA    1 ? 2 
ATOM   5048  C C     . ALA B 1 187 ? 57.732  -20.232 4.341   1.000 45.659  0 187 ALA BBB C     1 ? 2 
ATOM   5049  O O     . ALA B 1 187 ? 57.509  -19.452 5.301   1.000 46.113  0 187 ALA BBB O     1 ? 2 
ATOM   5050  C CB    . ALA B 1 187 ? 56.228  -20.577 2.320   1.000 45.559  0 187 ALA BBB CB    1 ? 2 
ATOM   5051  N N     . ILE B 1 188 ? 58.262  -21.448 4.471   1.000 44.088  0 188 ILE BBB N     1 ? 2 
ATOM   5052  C CA    . ILE B 1 188 ? 58.590  -22.099 5.774   1.000 43.351  0 188 ILE BBB CA    1 ? 2 
ATOM   5053  C C     . ILE B 1 188 ? 59.644  -21.260 6.495   1.000 44.726  0 188 ILE BBB C     1 ? 2 
ATOM   5054  O O     . ILE B 1 188 ? 59.572  -21.130 7.727   1.000 45.022  0 188 ILE BBB O     1 ? 2 
ATOM   5055  C CB    . ILE B 1 188 ? 59.025  -23.565 5.527   1.000 44.804  0 188 ILE BBB CB    1 ? 2 
ATOM   5056  C CG1   . ILE B 1 188 ? 57.795  -24.484 5.464   1.000 43.684  0 188 ILE BBB CG1   1 ? 2 
ATOM   5057  C CG2   . ILE B 1 188 ? 60.052  -24.056 6.545   1.000 45.494  0 188 ILE BBB CG2   1 ? 2 
ATOM   5058  C CD1   . ILE B 1 188 ? 58.000  -25.797 4.755   1.000 42.859  0 188 ILE BBB CD1   1 ? 2 
ATOM   5059  N N     . GLN B 1 189 ? 60.596  -20.707 5.753   1.000 48.014  0 189 GLN BBB N     1 ? 2 
ATOM   5060  C CA    . GLN B 1 189 ? 61.791  -20.050 6.339   1.000 48.934  0 189 GLN BBB CA    1 ? 2 
ATOM   5061  C C     . GLN B 1 189 ? 61.415  -18.658 6.861   1.000 48.082  0 189 GLN BBB C     1 ? 2 
ATOM   5062  O O     . GLN B 1 189 ? 61.902  -18.299 7.954   1.000 52.583  0 189 GLN BBB O     1 ? 2 
ATOM   5063  C CB    . GLN B 1 189 ? 62.905  -19.945 5.300   1.000 51.792  0 189 GLN BBB CB    1 ? 2 
ATOM   5064  C CG    . GLN B 1 189 ? 64.287  -19.809 5.922   1.000 53.814  0 189 GLN BBB CG    1 ? 2 
ATOM   5065  C CD    . GLN B 1 189 ? 65.383  -19.558 4.907   1.000 56.031  0 189 GLN BBB CD    1 ? 2 
ATOM   5066  O OE1   . GLN B 1 189 ? 65.366  -20.025 3.768   1.000 55.959  0 189 GLN BBB OE1   1 ? 2 
ATOM   5067  N NE2   . GLN B 1 189 ? 66.347  -18.747 5.304   1.000 58.704  0 189 GLN BBB NE2   1 ? 2 
ATOM   5068  N N     . TYR B 1 190 ? 60.607  -17.892 6.118   1.000 44.022  0 190 TYR BBB N     1 ? 2 
ATOM   5069  C CA    . TYR B 1 190 ? 60.496  -16.417 6.280   1.000 43.419  0 190 TYR BBB CA    1 ? 2 
ATOM   5070  C C     . TYR B 1 190 ? 59.122  -15.993 6.828   1.000 39.019  0 190 TYR BBB C     1 ? 2 
ATOM   5071  O O     . TYR B 1 190 ? 59.036  -14.874 7.385   1.000 38.628  0 190 TYR BBB O     1 ? 2 
ATOM   5072  C CB    . TYR B 1 190 ? 60.811  -15.721 4.953   1.000 45.744  0 190 TYR BBB CB    1 ? 2 
ATOM   5073  C CG    . TYR B 1 190 ? 62.247  -15.855 4.499   1.000 50.594  0 190 TYR BBB CG    1 ? 2 
ATOM   5074  C CD1   . TYR B 1 190 ? 63.310  -15.501 5.322   1.000 51.864  0 190 TYR BBB CD1   1 ? 2 
ATOM   5075  C CD2   . TYR B 1 190 ? 62.547  -16.332 3.225   1.000 51.653  0 190 TYR BBB CD2   1 ? 2 
ATOM   5076  C CE1   . TYR B 1 190 ? 64.628  -15.624 4.893   1.000 52.705  0 190 TYR BBB CE1   1 ? 2 
ATOM   5077  C CE2   . TYR B 1 190 ? 63.855  -16.479 2.795   1.000 52.157  0 190 TYR BBB CE2   1 ? 2 
ATOM   5078  C CZ    . TYR B 1 190 ? 64.895  -16.102 3.624   1.000 52.955  0 190 TYR BBB CZ    1 ? 2 
ATOM   5079  O OH    . TYR B 1 190 ? 66.180  -16.208 3.184   1.000 59.771  0 190 TYR BBB OH    1 ? 2 
ATOM   5080  N N     . SER B 1 191 ? 58.090  -16.820 6.686   1.000 35.672  0 191 SER BBB N     1 ? 2 
ATOM   5081  C CA    . SER B 1 191 ? 56.701  -16.518 7.120   1.000 36.195  0 191 SER BBB CA    1 ? 2 
ATOM   5082  C C     . SER B 1 191 ? 56.479  -16.922 8.580   1.000 34.228  0 191 SER BBB C     1 ? 2 
ATOM   5083  O O     . SER B 1 191 ? 57.067  -17.918 9.037   1.000 35.698  0 191 SER BBB O     1 ? 2 
ATOM   5084  C CB    . SER B 1 191 ? 55.655  -17.193 6.271   1.000 37.013  0 191 SER BBB CB    1 ? 2 
ATOM   5085  O OG    . SER B 1 191 ? 56.002  -17.225 4.908   1.000 38.952  0 191 SER BBB OG    1 ? 2 
ATOM   5086  N N     . ILE B 1 192 ? 55.613  -16.184 9.261   1.000 32.746  0 192 ILE BBB N     1 ? 2 
ATOM   5087  C CA    . ILE B 1 192 ? 55.095  -16.539 10.612  1.000 31.537  0 192 ILE BBB CA    1 ? 2 
ATOM   5088  C C     . ILE B 1 192 ? 53.687  -17.140 10.452  1.000 30.013  0 192 ILE BBB C     1 ? 2 
ATOM   5089  O O     . ILE B 1 192 ? 53.172  -17.165 9.317   1.000 29.514  0 192 ILE BBB O     1 ? 2 
ATOM   5090  C CB    . ILE B 1 192 ? 55.122  -15.316 11.539  1.000 31.649  0 192 ILE BBB CB    1 ? 2 
ATOM   5091  C CG1   . ILE B 1 192 ? 54.208  -14.182 11.065  1.000 32.537  0 192 ILE BBB CG1   1 ? 2 
ATOM   5092  C CG2   . ILE B 1 192 ? 56.540  -14.836 11.769  1.000 31.231  0 192 ILE BBB CG2   1 ? 2 
ATOM   5093  C CD1   . ILE B 1 192 ? 53.947  -13.112 12.135  1.000 33.225  0 192 ILE BBB CD1   1 ? 2 
ATOM   5094  N N     . THR B 1 193 ? 53.120  -17.644 11.549  1.000 28.045  0 193 THR BBB N     1 ? 2 
ATOM   5095  C CA    . THR B 1 193 ? 51.753  -18.201 11.642  1.000 26.564  0 193 THR BBB CA    1 ? 2 
ATOM   5096  C C     . THR B 1 193 ? 51.073  -17.636 12.893  1.000 26.915  0 193 THR BBB C     1 ? 2 
ATOM   5097  O O     . THR B 1 193 ? 51.711  -16.806 13.561  1.000 26.276  0 193 THR BBB O     1 ? 2 
ATOM   5098  C CB    . THR B 1 193 ? 51.820  -19.724 11.657  1.000 26.441  0 193 THR BBB CB    1 ? 2 
ATOM   5099  O OG1   . THR B 1 193 ? 52.411  -20.155 12.877  1.000 26.095  0 193 THR BBB OG1   1 ? 2 
ATOM   5100  C CG2   . THR B 1 193 ? 52.573  -20.269 10.459  1.000 27.210  0 193 THR BBB CG2   1 ? 2 
ATOM   5101  N N     . SER B 1 194 ? 49.878  -18.117 13.234  1.000 26.409  0 194 SER BBB N     1 ? 2 
ATOM   5102  C CA    . SER B 1 194 ? 49.130  -17.747 14.457  1.000 26.367  0 194 SER BBB CA    1 ? 2 
ATOM   5103  C C     . SER B 1 194 ? 49.912  -18.185 15.699  1.000 26.377  0 194 SER BBB C     1 ? 2 
ATOM   5104  O O     . SER B 1 194 ? 49.704  -17.591 16.780  1.000 26.875  0 194 SER BBB O     1 ? 2 
ATOM   5105  C CB    . SER B 1 194 ? 47.719  -18.332 14.454  1.000 25.789  0 194 SER BBB CB    1 ? 2 
ATOM   5106  O OG    . SER B 1 194 ? 47.737  -19.714 14.131  1.000 25.838  0 194 SER BBB OG    1 ? 2 
ATOM   5107  N N     . ASP B 1 195 ? 50.781  -19.185 15.570  1.000 25.976  0 195 ASP BBB N     1 ? 2 
ATOM   5108  C CA    . ASP B 1 195 ? 51.683  -19.598 16.675  1.000 25.757  0 195 ASP BBB CA    1 ? 2 
ATOM   5109  C C     . ASP B 1 195 ? 52.656  -18.475 17.077  1.000 24.309  0 195 ASP BBB C     1 ? 2 
ATOM   5110  O O     . ASP B 1 195 ? 53.128  -18.509 18.234  1.000 22.647  0 195 ASP BBB O     1 ? 2 
ATOM   5111  C CB    . ASP B 1 195 ? 52.456  -20.859 16.285  1.000 26.739  0 195 ASP BBB CB    1 ? 2 
ATOM   5112  C CG    . ASP B 1 195 ? 51.626  -22.131 16.330  1.000 27.771  0 195 ASP BBB CG    1 ? 2 
ATOM   5113  O OD1   . ASP B 1 195 ? 50.366  -22.066 16.560  1.000 25.845  0 195 ASP BBB OD1   1 ? 2 
ATOM   5114  O OD2   . ASP B 1 195 ? 52.254  -23.197 16.165  1.000 30.088  0 195 ASP BBB OD2   1 ? 2 
ATOM   5115  N N     . ASP B 1 196 ? 52.954  -17.508 16.203  1.000 23.625  0 196 ASP BBB N     1 ? 2 
ATOM   5116  C CA    . ASP B 1 196 ? 54.000  -16.490 16.491  1.000 24.119  0 196 ASP BBB CA    1 ? 2 
ATOM   5117  C C     . ASP B 1 196 ? 53.428  -15.076 16.711  1.000 23.651  0 196 ASP BBB C     1 ? 2 
ATOM   5118  O O     . ASP B 1 196 ? 54.091  -14.255 17.468  1.000 22.983  0 196 ASP BBB O     1 ? 2 
ATOM   5119  C CB    . ASP B 1 196 ? 55.043  -16.475 15.381  1.000 24.859  0 196 ASP BBB CB    1 ? 2 
ATOM   5120  C CG    . ASP B 1 196 ? 55.485  -17.873 14.961  1.000 25.359  0 196 ASP BBB CG    1 ? 2 
ATOM   5121  O OD1   . ASP B 1 196 ? 56.073  -18.598 15.807  1.000 24.057  0 196 ASP BBB OD1   1 ? 2 
ATOM   5122  O OD2   . ASP B 1 196 ? 55.201  -18.257 13.783  1.000 26.241  0 196 ASP BBB OD2   1 ? 2 
ATOM   5123  N N     . ILE B 1 197 ? 52.281  -14.774 16.098  1.000 22.970  0 197 ILE BBB N     1 ? 2 
ATOM   5124  C CA    . ILE B 1 197 ? 51.789  -13.372 15.939  1.000 24.428  0 197 ILE BBB CA    1 ? 2 
ATOM   5125  C C     . ILE B 1 197 ? 51.506  -12.710 17.318  1.000 25.439  0 197 ILE BBB C     1 ? 2 
ATOM   5126  O O     . ILE B 1 197 ? 51.702  -11.492 17.433  1.000 25.262  0 197 ILE BBB O     1 ? 2 
ATOM   5127  C CB    . ILE B 1 197 ? 50.551  -13.313 15.033  1.000 25.072  0 197 ILE BBB CB    1 ? 2 
ATOM   5128  C CG1   . ILE B 1 197 ? 50.114  -11.856 14.780  1.000 24.935  0 197 ILE BBB CG1   1 ? 2 
ATOM   5129  C CG2   . ILE B 1 197 ? 49.405  -14.160 15.616  1.000 25.153  0 197 ILE BBB CG2   1 ? 2 
ATOM   5130  C CD1   . ILE B 1 197 ? 51.210  -10.968 14.260  1.000 24.898  0 197 ILE BBB CD1   1 ? 2 
ATOM   5131  N N     . PHE B 1 198 ? 51.088  -13.450 18.341  1.000 25.605  0 198 PHE BBB N     1 ? 2 
ATOM   5132  C CA    . PHE B 1 198 ? 50.682  -12.815 19.619  1.000 27.342  0 198 PHE BBB CA    1 ? 2 
ATOM   5133  C C     . PHE B 1 198 ? 51.901  -12.422 20.465  1.000 28.665  0 198 PHE BBB C     1 ? 2 
ATOM   5134  O O     . PHE B 1 198 ? 51.706  -11.598 21.373  1.000 28.504  0 198 PHE BBB O     1 ? 2 
ATOM   5135  C CB    . PHE B 1 198 ? 49.687  -13.704 20.365  1.000 27.903  0 198 PHE BBB CB    1 ? 2 
ATOM   5136  C CG    . PHE B 1 198 ? 48.487  -14.038 19.519  1.000 29.091  0 198 PHE BBB CG    1 ? 2 
ATOM   5137  C CD1   . PHE B 1 198 ? 47.651  -13.041 19.066  1.000 28.414  0 198 PHE BBB CD1   1 ? 2 
ATOM   5138  C CD2   . PHE B 1 198 ? 48.227  -15.332 19.110  1.000 29.621  0 198 PHE BBB CD2   1 ? 2 
ATOM   5139  C CE1   . PHE B 1 198 ? 46.580  -13.339 18.252  1.000 27.394  0 198 PHE BBB CE1   1 ? 2 
ATOM   5140  C CE2   . PHE B 1 198 ? 47.140  -15.620 18.313  1.000 28.066  0 198 PHE BBB CE2   1 ? 2 
ATOM   5141  C CZ    . PHE B 1 198 ? 46.316  -14.628 17.910  1.000 27.067  0 198 PHE BBB CZ    1 ? 2 
ATOM   5142  N N     . PHE B 1 199 ? 53.098  -12.957 20.149  1.000 31.172  0 199 PHE BBB N     1 ? 2 
ATOM   5143  C CA    . PHE B 1 199 ? 54.323  -12.876 20.996  1.000 31.017  0 199 PHE BBB CA    1 ? 2 
ATOM   5144  C C     . PHE B 1 199 ? 55.496  -12.188 20.292  1.000 30.416  0 199 PHE BBB C     1 ? 2 
ATOM   5145  O O     . PHE B 1 199 ? 56.504  -12.046 20.962  1.000 28.879  0 199 PHE BBB O     1 ? 2 
ATOM   5146  C CB    . PHE B 1 199 ? 54.711  -14.261 21.504  1.000 31.318  0 199 PHE BBB CB    1 ? 2 
ATOM   5147  C CG    . PHE B 1 199 ? 53.562  -14.920 22.214  1.000 34.195  0 199 PHE BBB CG    1 ? 2 
ATOM   5148  C CD1   . PHE B 1 199 ? 52.942  -14.295 23.303  1.000 35.860  0 199 PHE BBB CD1   1 ? 2 
ATOM   5149  C CD2   . PHE B 1 199 ? 53.055  -16.126 21.764  1.000 35.381  0 199 PHE BBB CD2   1 ? 2 
ATOM   5150  C CE1   . PHE B 1 199 ? 51.833  -14.867 23.915  1.000 36.515  0 199 PHE BBB CE1   1 ? 2 
ATOM   5151  C CE2   . PHE B 1 199 ? 51.950  -16.698 22.379  1.000 36.504  0 199 PHE BBB CE2   1 ? 2 
ATOM   5152  C CZ    . PHE B 1 199 ? 51.326  -16.058 23.433  1.000 35.208  0 199 PHE BBB CZ    1 ? 2 
ATOM   5153  N N     . LEU B 1 200 ? 55.339  -11.705 19.069  1.000 31.489  0 200 LEU BBB N     1 ? 2 
ATOM   5154  C CA    . LEU B 1 200 ? 56.449  -11.009 18.370  1.000 33.878  0 200 LEU BBB CA    1 ? 2 
ATOM   5155  C C     . LEU B 1 200 ? 57.124  -10.013 19.322  1.000 34.849  0 200 LEU BBB C     1 ? 2 
ATOM   5156  O O     . LEU B 1 200 ? 56.419  -9.135  19.869  1.000 32.715  0 200 LEU BBB O     1 ? 2 
ATOM   5157  C CB    . LEU B 1 200 ? 55.890  -10.228 17.179  1.000 34.265  0 200 LEU BBB CB    1 ? 2 
ATOM   5158  C CG    . LEU B 1 200 ? 55.444  -11.057 15.997  1.000 35.248  0 200 LEU BBB CG    1 ? 2 
ATOM   5159  C CD1   . LEU B 1 200 ? 55.072  -10.126 14.861  1.000 35.522  0 200 LEU BBB CD1   1 ? 2 
ATOM   5160  C CD2   . LEU B 1 200 ? 56.539  -12.044 15.579  1.000 35.522  0 200 LEU BBB CD2   1 ? 2 
ATOM   5161  N N     . SER B 1 201 ? 58.442  -10.127 19.475  1.000 37.560  0 201 SER BBB N     1 ? 2 
ATOM   5162  C CA    . SER B 1 201 ? 59.321  -9.172  20.201  1.000 39.486  0 201 SER BBB CA    1 ? 2 
ATOM   5163  C C     . SER B 1 201 ? 59.203  -7.777  19.584  1.000 38.438  0 201 SER BBB C     1 ? 2 
ATOM   5164  O O     . SER B 1 201 ? 59.327  -6.816  20.351  1.000 38.730  0 201 SER BBB O     1 ? 2 
ATOM   5165  C CB    . SER B 1 201 ? 60.793  -9.603  20.185  1.000 42.911  0 201 SER BBB CB    1 ? 2 
ATOM   5166  O OG    . SER B 1 201 ? 60.990  -11.009 20.320  1.000 47.174  0 201 SER BBB OG    1 ? 2 
ATOM   5167  N N     . LYS B 1 202 ? 58.988  -7.668  18.270  1.000 39.422  0 202 LYS BBB N     1 ? 2 
ATOM   5168  C CA    . LYS B 1 202 ? 58.827  -6.347  17.599  1.000 43.583  0 202 LYS BBB CA    1 ? 2 
ATOM   5169  C C     . LYS B 1 202 ? 57.479  -6.282  16.877  1.000 39.246  0 202 LYS BBB C     1 ? 2 
ATOM   5170  O O     . LYS B 1 202 ? 56.950  -7.341  16.461  1.000 38.694  0 202 LYS BBB O     1 ? 2 
ATOM   5171  C CB    . LYS B 1 202 ? 59.974  -6.066  16.616  1.000 49.018  0 202 LYS BBB CB    1 ? 2 
ATOM   5172  C CG    . LYS B 1 202 ? 61.350  -5.974  17.249  1.000 56.112  0 202 LYS BBB CG    1 ? 2 
ATOM   5173  C CD    . LYS B 1 202 ? 61.500  -4.965  18.388  1.000 59.929  0 202 LYS BBB CD    1 ? 2 
ATOM   5174  C CE    . LYS B 1 202 ? 62.841  -5.163  19.071  1.000 61.958  0 202 LYS BBB CE    1 ? 2 
ATOM   5175  N NZ    . LYS B 1 202 ? 63.039  -4.230  20.192  1.000 66.040  0 202 LYS BBB NZ    1 ? 2 
ATOM   5176  N N     . SER B 1 203 ? 56.945  -5.076  16.697  1.000 36.305  0 203 SER BBB N     1 ? 2 
ATOM   5177  C CA    . SER B 1 203 ? 55.701  -4.856  15.922  1.000 35.928  0 203 SER BBB CA    1 ? 2 
ATOM   5178  C C     . SER B 1 203 ? 55.931  -5.324  14.477  1.000 35.090  0 203 SER BBB C     1 ? 2 
ATOM   5179  O O     . SER B 1 203 ? 57.022  -5.185  13.907  1.000 35.164  0 203 SER BBB O     1 ? 2 
ATOM   5180  C CB    . SER B 1 203 ? 55.219  -3.422  16.015  1.000 35.389  0 203 SER BBB CB    1 ? 2 
ATOM   5181  O OG    . SER B 1 203 ? 55.996  -2.506  15.253  1.000 35.849  0 203 SER BBB OG    1 ? 2 
ATOM   5182  N N     . PRO B 1 204 ? 54.904  -5.924  13.845  1.000 33.537  0 204 PRO BBB N     1 ? 2 
ATOM   5183  C CA    . PRO B 1 204 ? 55.079  -6.591  12.553  1.000 33.424  0 204 PRO BBB CA    1 ? 2 
ATOM   5184  C C     . PRO B 1 204 ? 55.263  -5.654  11.337  1.000 33.708  0 204 PRO BBB C     1 ? 2 
ATOM   5185  O O     . PRO B 1 204 ? 55.598  -6.153  10.266  1.000 32.989  0 204 PRO BBB O     1 ? 2 
ATOM   5186  C CB    . PRO B 1 204 ? 53.772  -7.389  12.462  1.000 32.853  0 204 PRO BBB CB    1 ? 2 
ATOM   5187  C CG    . PRO B 1 204 ? 52.747  -6.531  13.194  1.000 33.272  0 204 PRO BBB CG    1 ? 2 
ATOM   5188  C CD    . PRO B 1 204 ? 53.531  -6.011  14.375  1.000 34.050  0 204 PRO BBB CD    1 ? 2 
ATOM   5189  N N     . GLY B 1 205 ? 55.027  -4.347  11.517  1.000 34.187  0 205 GLY BBB N     1 ? 2 
ATOM   5190  C CA    . GLY B 1 205 ? 55.006  -3.347  10.447  1.000 35.467  0 205 GLY BBB CA    1 ? 2 
ATOM   5191  C C     . GLY B 1 205 ? 54.055  -3.771  9.333   1.000 36.526  0 205 GLY BBB C     1 ? 2 
ATOM   5192  O O     . GLY B 1 205 ? 52.995  -4.447  9.628   1.000 37.577  0 205 GLY BBB O     1 ? 2 
ATOM   5193  N N     . LYS B 1 206 ? 54.414  -3.416  8.100   1.000 35.760  0 206 LYS BBB N     1 ? 2 
ATOM   5194  C CA    . LYS B 1 206 ? 53.617  -3.705  6.881   1.000 36.514  0 206 LYS BBB CA    1 ? 2 
ATOM   5195  C C     . LYS B 1 206 ? 53.446  -5.223  6.764   1.000 34.644  0 206 LYS BBB C     1 ? 2 
ATOM   5196  O O     . LYS B 1 206 ? 54.484  -5.933  6.713   1.000 35.965  0 206 LYS BBB O     1 ? 2 
ATOM   5197  C CB    . LYS B 1 206 ? 54.306  -3.091  5.656   1.000 38.879  0 206 LYS BBB CB    1 ? 2 
ATOM   5198  C CG    . LYS B 1 206 ? 53.773  -3.569  4.308   1.000 39.877  0 206 LYS BBB CG    1 ? 2 
ATOM   5199  C CD    . LYS B 1 206 ? 54.178  -2.703  3.117   1.000 40.947  0 206 LYS BBB CD    1 ? 2 
ATOM   5200  C CE    . LYS B 1 206 ? 53.368  -3.021  1.878   1.000 42.261  0 206 LYS BBB CE    1 ? 2 
ATOM   5201  N NZ    . LYS B 1 206 ? 54.053  -2.546  0.663   1.000 44.432  0 206 LYS BBB NZ    1 ? 2 
ATOM   5202  N N     . THR B 1 207 ? 52.204  -5.705  6.729   1.000 32.817  0 207 THR BBB N     1 ? 2 
ATOM   5203  C CA    . THR B 1 207 ? 51.909  -7.150  6.904   1.000 33.407  0 207 THR BBB CA    1 ? 2 
ATOM   5204  C C     . THR B 1 207 ? 51.071  -7.677  5.740   1.000 33.240  0 207 THR BBB C     1 ? 2 
ATOM   5205  O O     . THR B 1 207 ? 50.115  -7.017  5.347   1.000 34.274  0 207 THR BBB O     1 ? 2 
ATOM   5206  C CB    . THR B 1 207 ? 51.212  -7.459  8.244   1.000 31.460  0 207 THR BBB CB    1 ? 2 
ATOM   5207  O OG1   . THR B 1 207 ? 52.076  -7.034  9.305   1.000 31.566  0 207 THR BBB OG1   1 ? 2 
ATOM   5208  C CG2   . THR B 1 207 ? 50.908  -8.927  8.406   1.000 30.429  0 207 THR BBB CG2   1 ? 2 
ATOM   5209  N N     . LEU B 1 208 ? 51.447  -8.857  5.266   1.000 32.856  0 208 LEU BBB N     1 ? 2 
ATOM   5210  C CA    . LEU B 1 208 ? 50.661  -9.701  4.349   1.000 34.204  0 208 LEU BBB CA    1 ? 2 
ATOM   5211  C C     . LEU B 1 208 ? 50.103  -10.897 5.140   1.000 31.819  0 208 LEU BBB C     1 ? 2 
ATOM   5212  O O     . LEU B 1 208 ? 50.895  -11.621 5.764   1.000 30.751  0 208 LEU BBB O     1 ? 2 
ATOM   5213  C CB    . LEU B 1 208 ? 51.549  -10.173 3.190   1.000 34.340  0 208 LEU BBB CB    1 ? 2 
ATOM   5214  C CG    . LEU B 1 208 ? 50.849  -11.111 2.210   1.000 35.699  0 208 LEU BBB CG    1 ? 2 
ATOM   5215  C CD1   . LEU B 1 208 ? 49.719  -10.406 1.447   1.000 35.464  0 208 LEU BBB CD1   1 ? 2 
ATOM   5216  C CD2   . LEU B 1 208 ? 51.855  -11.694 1.225   1.000 37.709  0 208 LEU BBB CD2   1 ? 2 
ATOM   5217  N N     . VAL B 1 209 ? 48.792  -11.087 5.068   1.000 30.694  0 209 VAL BBB N     1 ? 2 
ATOM   5218  C CA    . VAL B 1 209 ? 48.080  -12.276 5.613   1.000 29.922  0 209 VAL BBB CA    1 ? 2 
ATOM   5219  C C     . VAL B 1 209 ? 47.576  -13.076 4.402   1.000 29.171  0 209 VAL BBB C     1 ? 2 
ATOM   5220  O O     . VAL B 1 209 ? 46.857  -12.486 3.558   1.000 27.541  0 209 VAL BBB O     1 ? 2 
ATOM   5221  C CB    . VAL B 1 209 ? 46.923  -11.852 6.535   1.000 30.230  0 209 VAL BBB CB    1 ? 2 
ATOM   5222  C CG1   . VAL B 1 209 ? 46.164  -13.061 7.048   1.000 31.220  0 209 VAL BBB CG1   1 ? 2 
ATOM   5223  C CG2   . VAL B 1 209 ? 47.383  -10.988 7.697   1.000 30.687  0 209 VAL BBB CG2   1 ? 2 
ATOM   5224  N N     . ILE B 1 210 ? 47.964  -14.349 4.298   1.000 28.101  0 210 ILE BBB N     1 ? 2 
ATOM   5225  C CA    . ILE B 1 210 ? 47.482  -15.256 3.209   1.000 28.765  0 210 ILE BBB CA    1 ? 2 
ATOM   5226  C C     . ILE B 1 210 ? 46.403  -16.142 3.826   1.000 28.422  0 210 ILE BBB C     1 ? 2 
ATOM   5227  O O     . ILE B 1 210 ? 46.693  -16.851 4.822   1.000 28.782  0 210 ILE BBB O     1 ? 2 
ATOM   5228  C CB    . ILE B 1 210 ? 48.631  -16.080 2.572   1.000 28.622  0 210 ILE BBB CB    1 ? 2 
ATOM   5229  C CG1   . ILE B 1 210 ? 49.788  -15.193 2.113   1.000 28.187  0 210 ILE BBB CG1   1 ? 2 
ATOM   5230  C CG2   . ILE B 1 210 ? 48.118  -16.960 1.449   1.000 29.002  0 210 ILE BBB CG2   1 ? 2 
ATOM   5231  C CD1   . ILE B 1 210 ? 51.010  -15.284 2.969   1.000 28.336  0 210 ILE BBB CD1   1 ? 2 
ATOM   5232  N N     . GLY B 1 211 ? 45.200  -16.083 3.264   1.000 28.917  0 211 GLY BBB N     1 ? 2 
ATOM   5233  C CA    . GLY B 1 211 ? 44.018  -16.784 3.810   1.000 28.681  0 211 GLY BBB CA    1 ? 2 
ATOM   5234  C C     . GLY B 1 211 ? 42.922  -15.811 4.166   1.000 28.821  0 211 GLY BBB C     1 ? 2 
ATOM   5235  O O     . GLY B 1 211 ? 43.182  -14.916 4.945   1.000 28.296  0 211 GLY BBB O     1 ? 2 
ATOM   5236  N N     . ALA B 1 212 ? 41.749  -15.973 3.565   1.000 30.748  0 212 ALA BBB N     1 ? 2 
ATOM   5237  C CA    . ALA B 1 212 ? 40.502  -15.250 3.919   1.000 32.493  0 212 ALA BBB CA    1 ? 2 
ATOM   5238  C C     . ALA B 1 212 ? 39.584  -16.176 4.723   1.000 32.643  0 212 ALA BBB C     1 ? 2 
ATOM   5239  O O     . ALA B 1 212 ? 38.356  -16.011 4.661   1.000 32.764  0 212 ALA BBB O     1 ? 2 
ATOM   5240  C CB    . ALA B 1 212 ? 39.833  -14.737 2.670   1.000 33.116  0 212 ALA BBB CB    1 ? 2 
ATOM   5241  N N     . SER B 1 213 ? 40.199  -17.153 5.409   1.000 34.111  0 213 SER BBB N     1 ? 2 
ATOM   5242  C CA    . SER B 1 213 ? 39.659  -17.973 6.536   1.000 32.811  0 213 SER BBB CA    1 ? 2 
ATOM   5243  C C     . SER B 1 213 ? 39.334  -17.038 7.722   1.000 30.958  0 213 SER BBB C     1 ? 2 
ATOM   5244  O O     . SER B 1 213 ? 39.847  -15.892 7.756   1.000 29.743  0 213 SER BBB O     1 ? 2 
ATOM   5245  C CB    . SER B 1 213 ? 40.716  -18.977 6.964   1.000 32.162  0 213 SER BBB CB    1 ? 2 
ATOM   5246  O OG    . SER B 1 213 ? 41.911  -18.259 7.338   1.000 30.534  0 213 SER BBB OG    1 ? 2 
ATOM   5247  N N     . TYR B 1 214 ? 38.633  -17.537 8.738   1.000 27.720  0 214 TYR BBB N     1 ? 2 
ATOM   5248  C CA    . TYR B 1 214 ? 38.274  -16.714 9.915   1.000 26.287  0 214 TYR BBB CA    1 ? 2 
ATOM   5249  C C     . TYR B 1 214 ? 39.562  -16.254 10.618  1.000 24.514  0 214 TYR BBB C     1 ? 2 
ATOM   5250  O O     . TYR B 1 214 ? 39.640  -15.074 11.067  1.000 24.889  0 214 TYR BBB O     1 ? 2 
ATOM   5251  C CB    . TYR B 1 214 ? 37.272  -17.447 10.801  1.000 26.664  0 214 TYR BBB CB    1 ? 2 
ATOM   5252  C CG    . TYR B 1 214 ? 37.791  -18.392 11.862  1.000 26.375  0 214 TYR BBB CG    1 ? 2 
ATOM   5253  C CD1   . TYR B 1 214 ? 38.041  -17.931 13.138  1.000 26.463  0 214 TYR BBB CD1   1 ? 2 
ATOM   5254  C CD2   . TYR B 1 214 ? 37.891  -19.752 11.650  1.000 27.566  0 214 TYR BBB CD2   1 ? 2 
ATOM   5255  C CE1   . TYR B 1 214 ? 38.415  -18.773 14.175  1.000 26.672  0 214 TYR BBB CE1   1 ? 2 
ATOM   5256  C CE2   . TYR B 1 214 ? 38.282  -20.622 12.666  1.000 29.280  0 214 TYR BBB CE2   1 ? 2 
ATOM   5257  C CZ    . TYR B 1 214 ? 38.553  -20.122 13.943  1.000 28.726  0 214 TYR BBB CZ    1 ? 2 
ATOM   5258  O OH    . TYR B 1 214 ? 38.920  -20.908 14.998  1.000 29.008  0 214 TYR BBB OH    1 ? 2 
ATOM   5259  N N     . ILE B 1 215 ? 40.580  -17.105 10.682  1.000 22.190  0 215 ILE BBB N     1 ? 2 
ATOM   5260  C CA    . ILE B 1 215 ? 41.831  -16.731 11.388  1.000 21.359  0 215 ILE BBB CA    1 ? 2 
ATOM   5261  C C     . ILE B 1 215 ? 42.469  -15.573 10.622  1.000 21.850  0 215 ILE BBB C     1 ? 2 
ATOM   5262  O O     . ILE B 1 215 ? 42.823  -14.581 11.254  1.000 21.857  0 215 ILE BBB O     1 ? 2 
ATOM   5263  C CB    . ILE B 1 215 ? 42.731  -17.963 11.555  1.000 21.516  0 215 ILE BBB CB    1 ? 2 
ATOM   5264  C CG1   . ILE B 1 215 ? 42.116  -18.995 12.518  1.000 21.386  0 215 ILE BBB CG1   1 ? 2 
ATOM   5265  C CG2   . ILE B 1 215 ? 44.166  -17.554 11.956  1.000 21.912  0 215 ILE BBB CG2   1 ? 2 
ATOM   5266  C CD1   . ILE B 1 215 ? 42.744  -20.391 12.336  1.000 21.325  0 215 ILE BBB CD1   1 ? 2 
ATOM   5267  N N     . GLY B 1 216 ? 42.613  -15.693 9.289   1.000 23.252  0 216 GLY BBB N     1 ? 2 
ATOM   5268  C CA    . GLY B 1 216 ? 43.175  -14.665 8.381   1.000 23.479  0 216 GLY BBB CA    1 ? 2 
ATOM   5269  C C     . GLY B 1 216 ? 42.464  -13.328 8.507   1.000 24.677  0 216 GLY BBB C     1 ? 2 
ATOM   5270  O O     . GLY B 1 216 ? 43.167  -12.291 8.714   1.000 26.135  0 216 GLY BBB O     1 ? 2 
ATOM   5271  N N     . LEU B 1 217 ? 41.130  -13.326 8.407   1.000 25.293  0 217 LEU BBB N     1 ? 2 
ATOM   5272  C CA    . LEU B 1 217 ? 40.341  -12.072 8.434   1.000 25.975  0 217 LEU BBB CA    1 ? 2 
ATOM   5273  C C     . LEU B 1 217 ? 40.445  -11.453 9.835   1.000 26.734  0 217 LEU BBB C     1 ? 2 
ATOM   5274  O O     . LEU B 1 217 ? 40.659  -10.214 9.902   1.000 27.340  0 217 LEU BBB O     1 ? 2 
ATOM   5275  C CB    . LEU B 1 217 ? 38.882  -12.338 8.055   1.000 26.258  0 217 LEU BBB CB    1 ? 2 
ATOM   5276  C CG    . LEU B 1 217 ? 38.578  -12.668 6.598   1.000 27.077  0 217 LEU BBB CG    1 ? 2 
ATOM   5277  C CD1   . LEU B 1 217 ? 37.074  -12.560 6.289   1.000 27.389  0 217 LEU BBB CD1   1 ? 2 
ATOM   5278  C CD2   . LEU B 1 217 ? 39.374  -11.799 5.649   1.000 28.532  0 217 LEU BBB CD2   1 ? 2 
ATOM   5279  N N     . GLU B 1 218 ? 40.267  -12.243 10.904  1.000 27.207  0 218 GLU BBB N     1 ? 2 
ATOM   5280  C CA    . GLU B 1 218 ? 40.379  -11.745 12.310  1.000 28.999  0 218 GLU BBB CA    1 ? 2 
ATOM   5281  C C     . GLU B 1 218 ? 41.754  -11.111 12.500  1.000 28.671  0 218 GLU BBB C     1 ? 2 
ATOM   5282  O O     . GLU B 1 218 ? 41.802  -9.984  13.025  1.000 28.691  0 218 GLU BBB O     1 ? 2 
ATOM   5283  C CB    . GLU B 1 218 ? 40.244  -12.843 13.360  1.000 28.759  0 218 GLU BBB CB    1 ? 2 
ATOM   5284  C CG    . GLU B 1 218 ? 38.843  -13.377 13.486  1.000 30.901  0 218 GLU BBB CG    1 ? 2 
ATOM   5285  C CD    . GLU B 1 218 ? 38.683  -14.508 14.480  1.000 32.530  0 218 GLU BBB CD    1 ? 2 
ATOM   5286  O OE1   . GLU B 1 218 ? 39.688  -15.198 14.780  1.000 35.409  0 218 GLU BBB OE1   1 ? 2 
ATOM   5287  O OE2   . GLU B 1 218 ? 37.567  -14.681 14.968  1.000 34.996  0 218 GLU BBB OE2   1 ? 2 
ATOM   5288  N N     . THR B 1 219 ? 42.806  -11.795 12.058  1.000 29.198  0 219 THR BBB N     1 ? 2 
ATOM   5289  C CA    . THR B 1 219 ? 44.206  -11.334 12.249  1.000 29.889  0 219 THR BBB CA    1 ? 2 
ATOM   5290  C C     . THR B 1 219 ? 44.427  -10.035 11.471  1.000 29.926  0 219 THR BBB C     1 ? 2 
ATOM   5291  O O     . THR B 1 219 ? 44.971  -9.064  12.066  1.000 28.400  0 219 THR BBB O     1 ? 2 
ATOM   5292  C CB    . THR B 1 219 ? 45.214  -12.401 11.809  1.000 29.757  0 219 THR BBB CB    1 ? 2 
ATOM   5293  O OG1   . THR B 1 219 ? 44.846  -13.612 12.446  1.000 29.486  0 219 THR BBB OG1   1 ? 2 
ATOM   5294  C CG2   . THR B 1 219 ? 46.631  -12.035 12.182  1.000 29.282  0 219 THR BBB CG2   1 ? 2 
ATOM   5295  N N     . ALA B 1 220 ? 44.016  -10.004 10.206  1.000 30.488  0 220 ALA BBB N     1 ? 2 
ATOM   5296  C CA    . ALA B 1 220 ? 44.195  -8.809  9.352   1.000 32.522  0 220 ALA BBB CA    1 ? 2 
ATOM   5297  C C     . ALA B 1 220 ? 43.384  -7.650  9.939   1.000 31.534  0 220 ALA BBB C     1 ? 2 
ATOM   5298  O O     . ALA B 1 220 ? 43.876  -6.499  9.957   1.000 31.482  0 220 ALA BBB O     1 ? 2 
ATOM   5299  C CB    . ALA B 1 220 ? 43.742  -9.132  7.966   1.000 34.121  0 220 ALA BBB CB    1 ? 2 
ATOM   5300  N N     . GLY B 1 221 ? 42.166  -7.961  10.399  1.000 30.166  0 221 GLY BBB N     1 ? 2 
ATOM   5301  C CA    . GLY B 1 221 ? 41.232  -6.990  10.993  1.000 29.231  0 221 GLY BBB CA    1 ? 2 
ATOM   5302  C C     . GLY B 1 221 ? 41.855  -6.303  12.195  1.000 28.586  0 221 GLY BBB C     1 ? 2 
ATOM   5303  O O     . GLY B 1 221 ? 41.793  -5.060  12.244  1.000 27.254  0 221 GLY BBB O     1 ? 2 
ATOM   5304  N N     . PHE B 1 222 ? 42.471  -7.044  13.129  1.000 27.974  0 222 PHE BBB N     1 ? 2 
ATOM   5305  C CA    . PHE B 1 222 ? 43.061  -6.378  14.322  1.000 28.834  0 222 PHE BBB CA    1 ? 2 
ATOM   5306  C C     . PHE B 1 222 ? 44.394  -5.690  13.941  1.000 28.239  0 222 PHE BBB C     1 ? 2 
ATOM   5307  O O     . PHE B 1 222 ? 44.677  -4.576  14.417  1.000 27.257  0 222 PHE BBB O     1 ? 2 
ATOM   5308  C CB    . PHE B 1 222 ? 43.006  -7.273  15.567  1.000 28.344  0 222 PHE BBB CB    1 ? 2 
ATOM   5309  C CG    . PHE B 1 222 ? 43.961  -8.424  15.636  1.000 30.185  0 222 PHE BBB CG    1 ? 2 
ATOM   5310  C CD1   . PHE B 1 222 ? 45.342  -8.228  15.651  1.000 31.280  0 222 PHE BBB CD1   1 ? 2 
ATOM   5311  C CD2   . PHE B 1 222 ? 43.474  -9.721  15.724  1.000 30.254  0 222 PHE BBB CD2   1 ? 2 
ATOM   5312  C CE1   . PHE B 1 222 ? 46.205  -9.310  15.677  1.000 31.404  0 222 PHE BBB CE1   1 ? 2 
ATOM   5313  C CE2   . PHE B 1 222 ? 44.348  -10.797 15.779  1.000 30.188  0 222 PHE BBB CE2   1 ? 2 
ATOM   5314  C CZ    . PHE B 1 222 ? 45.706  -10.591 15.751  1.000 30.807  0 222 PHE BBB CZ    1 ? 2 
ATOM   5315  N N     . LEU B 1 223 ? 45.180  -6.241  13.038  1.000 29.247  0 223 LEU BBB N     1 ? 2 
ATOM   5316  C CA    . LEU B 1 223 ? 46.441  -5.545  12.647  1.000 30.189  0 223 LEU BBB CA    1 ? 2 
ATOM   5317  C C     . LEU B 1 223 ? 46.111  -4.202  11.973  1.000 31.145  0 223 LEU BBB C     1 ? 2 
ATOM   5318  O O     . LEU B 1 223 ? 46.787  -3.192  12.281  1.000 31.630  0 223 LEU BBB O     1 ? 2 
ATOM   5319  C CB    . LEU B 1 223 ? 47.304  -6.437  11.757  1.000 29.263  0 223 LEU BBB CB    1 ? 2 
ATOM   5320  C CG    . LEU B 1 223 ? 47.899  -7.656  12.442  1.000 28.887  0 223 LEU BBB CG    1 ? 2 
ATOM   5321  C CD1   . LEU B 1 223 ? 48.727  -8.443  11.454  1.000 28.128  0 223 LEU BBB CD1   1 ? 2 
ATOM   5322  C CD2   . LEU B 1 223 ? 48.752  -7.274  13.640  1.000 30.024  0 223 LEU BBB CD2   1 ? 2 
ATOM   5323  N N     . ASN B 1 224 ? 45.082  -4.150  11.131  1.000 33.035  0 224 ASN BBB N     1 ? 2 
ATOM   5324  C CA    . ASN B 1 224 ? 44.657  -2.887  10.463  1.000 33.710  0 224 ASN BBB CA    1 ? 2 
ATOM   5325  C C     . ASN B 1 224 ? 44.134  -1.927  11.525  1.000 33.260  0 224 ASN BBB C     1 ? 2 
ATOM   5326  O O     . ASN B 1 224 ? 44.572  -0.751  11.518  1.000 33.687  0 224 ASN BBB O     1 ? 2 
ATOM   5327  C CB    . ASN B 1 224 ? 43.624  -3.122  9.357   1.000 34.278  0 224 ASN BBB CB    1 ? 2 
ATOM   5328  C CG    . ASN B 1 224 ? 43.165  -1.842  8.694   1.000 34.184  0 224 ASN BBB CG    1 ? 2 
ATOM   5329  O OD1   . ASN B 1 224 ? 43.867  -1.292  7.872   1.000 37.678  0 224 ASN BBB OD1   1 ? 2 
ATOM   5330  N ND2   . ASN B 1 224 ? 41.980  -1.360  9.013   1.000 34.918  0 224 ASN BBB ND2   1 ? 2 
ATOM   5331  N N     . GLU B 1 225 ? 43.230  -2.388  12.393  1.000 32.376  0 225 GLU BBB N     1 ? 2 
ATOM   5332  C CA    . GLU B 1 225 ? 42.630  -1.528  13.444  0.940 32.710  0 225 GLU BBB CA    1 ? 2 
ATOM   5333  C C     . GLU B 1 225 ? 43.739  -0.946  14.306  1.000 32.301  0 225 GLU BBB C     1 ? 2 
ATOM   5334  O O     . GLU B 1 225 ? 43.541  0.180   14.803  1.000 35.378  0 225 GLU BBB O     1 ? 2 
ATOM   5335  C CB    . GLU B 1 225 ? 41.611  -2.289  14.292  0.940 33.427  0 225 GLU BBB CB    1 ? 2 
ATOM   5336  C CG    . GLU B 1 225 ? 40.171  -2.032  13.875  0.940 34.740  0 225 GLU BBB CG    1 ? 2 
ATOM   5337  C CD    . GLU B 1 225 ? 39.118  -2.799  14.656  0.940 37.739  0 225 GLU BBB CD    1 ? 2 
ATOM   5338  O OE1   . GLU B 1 225 ? 39.122  -4.067  14.623  0.940 41.363  0 225 GLU BBB OE1   1 ? 2 
ATOM   5339  O OE2   . GLU B 1 225 ? 38.266  -2.141  15.304  0.940 40.276  0 225 GLU BBB OE2   1 ? 2 
ATOM   5340  N N     . LEU B 1 226 ? 44.858  -1.666  14.468  1.000 30.338  0 226 LEU BBB N     1 ? 2 
ATOM   5341  C CA    . LEU B 1 226 ? 45.957  -1.251  15.372  1.000 28.733  0 226 LEU BBB CA    1 ? 2 
ATOM   5342  C C     . LEU B 1 226 ? 46.937  -0.340  14.634  1.000 30.008  0 226 LEU BBB C     1 ? 2 
ATOM   5343  O O     . LEU B 1 226 ? 47.920  0.038   15.248  1.000 29.250  0 226 LEU BBB O     1 ? 2 
ATOM   5344  C CB    . LEU B 1 226 ? 46.667  -2.493  15.913  1.000 28.137  0 226 LEU BBB CB    1 ? 2 
ATOM   5345  C CG    . LEU B 1 226 ? 45.976  -3.272  17.032  1.000 26.195  0 226 LEU BBB CG    1 ? 2 
ATOM   5346  C CD1   . LEU B 1 226 ? 46.795  -4.497  17.391  1.000 24.453  0 226 LEU BBB CD1   1 ? 2 
ATOM   5347  C CD2   . LEU B 1 226 ? 45.732  -2.397  18.245  1.000 25.770  0 226 LEU BBB CD2   1 ? 2 
ATOM   5348  N N     . GLY B 1 227 ? 46.675  -0.032  13.359  1.000 31.189  0 227 GLY BBB N     1 ? 2 
ATOM   5349  C CA    . GLY B 1 227 ? 47.409  0.970   12.570  1.000 32.116  0 227 GLY BBB CA    1 ? 2 
ATOM   5350  C C     . GLY B 1 227 ? 48.475  0.366   11.655  1.000 32.802  0 227 GLY BBB C     1 ? 2 
ATOM   5351  O O     . GLY B 1 227 ? 49.251  1.174   11.062  1.000 33.101  0 227 GLY BBB O     1 ? 2 
ATOM   5352  N N     . PHE B 1 228 ? 48.542  -0.964  11.518  1.000 30.723  0 228 PHE BBB N     1 ? 2 
ATOM   5353  C CA    . PHE B 1 228 ? 49.526  -1.615  10.609  1.000 31.966  0 228 PHE BBB CA    1 ? 2 
ATOM   5354  C C     . PHE B 1 228 ? 48.994  -1.609  9.169   1.000 33.494  0 228 PHE BBB C     1 ? 2 
ATOM   5355  O O     . PHE B 1 228 ? 47.774  -1.778  8.982   1.000 33.378  0 228 PHE BBB O     1 ? 2 
ATOM   5356  C CB    . PHE B 1 228 ? 49.910  -3.014  11.103  1.000 31.020  0 228 PHE BBB CB    1 ? 2 
ATOM   5357  C CG    . PHE B 1 228 ? 50.577  -2.954  12.444  1.000 30.664  0 228 PHE BBB CG    1 ? 2 
ATOM   5358  C CD1   . PHE B 1 228 ? 51.825  -2.345  12.568  1.000 31.326  0 228 PHE BBB CD1   1 ? 2 
ATOM   5359  C CD2   . PHE B 1 228 ? 49.932  -3.416  13.587  1.000 29.971  0 228 PHE BBB CD2   1 ? 2 
ATOM   5360  C CE1   . PHE B 1 228 ? 52.379  -2.152  13.820  1.000 31.747  0 228 PHE BBB CE1   1 ? 2 
ATOM   5361  C CE2   . PHE B 1 228 ? 50.515  -3.259  14.832  1.000 30.154  0 228 PHE BBB CE2   1 ? 2 
ATOM   5362  C CZ    . PHE B 1 228 ? 51.734  -2.632  14.954  1.000 31.034  0 228 PHE BBB CZ    1 ? 2 
ATOM   5363  N N     . ASP B 1 229 ? 49.907  -1.406  8.200   1.000 35.103  0 229 ASP BBB N     1 ? 2 
ATOM   5364  C CA    . ASP B 1 229 ? 49.678  -1.517  6.735   1.000 34.738  0 229 ASP BBB CA    1 ? 2 
ATOM   5365  C C     . ASP B 1 229 ? 49.421  -2.989  6.434   1.000 32.475  0 229 ASP BBB C     1 ? 2 
ATOM   5366  O O     . ASP B 1 229 ? 50.354  -3.819  6.584   1.000 31.972  0 229 ASP BBB O     1 ? 2 
ATOM   5367  C CB    . ASP B 1 229 ? 50.870  -0.945  5.966   1.000 36.509  0 229 ASP BBB CB    1 ? 2 
ATOM   5368  C CG    . ASP B 1 229 ? 50.762  -0.950  4.447   1.000 38.065  0 229 ASP BBB CG    1 ? 2 
ATOM   5369  O OD1   . ASP B 1 229 ? 50.027  -1.822  3.884   1.000 40.947  0 229 ASP BBB OD1   1 ? 2 
ATOM   5370  O OD2   . ASP B 1 229 ? 51.483  -0.132  3.829   1.000 39.850  0 229 ASP BBB OD2   1 ? 2 
ATOM   5371  N N     . THR B 1 230 ? 48.179  -3.300  6.087   1.000 30.976  0 230 THR BBB N     1 ? 2 
ATOM   5372  C CA    . THR B 1 230 ? 47.684  -4.689  6.104   1.000 30.977  0 230 THR BBB CA    1 ? 2 
ATOM   5373  C C     . THR B 1 230 ? 47.113  -5.029  4.730   1.000 31.560  0 230 THR BBB C     1 ? 2 
ATOM   5374  O O     . THR B 1 230 ? 46.285  -4.235  4.203   1.000 30.721  0 230 THR BBB O     1 ? 2 
ATOM   5375  C CB    . THR B 1 230 ? 46.675  -4.873  7.236   1.000 31.240  0 230 THR BBB CB    1 ? 2 
ATOM   5376  O OG1   . THR B 1 230 ? 47.402  -4.647  8.444   1.000 33.443  0 230 THR BBB OG1   1 ? 2 
ATOM   5377  C CG2   . THR B 1 230 ? 46.037  -6.248  7.254   1.000 30.829  0 230 THR BBB CG2   1 ? 2 
ATOM   5378  N N     . THR B 1 231 ? 47.479  -6.206  4.242   1.000 31.049  0 231 THR BBB N     1 ? 2 
ATOM   5379  C CA    . THR B 1 231 ? 47.053  -6.744  2.931   1.000 31.991  0 231 THR BBB CA    1 ? 2 
ATOM   5380  C C     . THR B 1 231 ? 46.670  -8.206  3.128   1.000 30.336  0 231 THR BBB C     1 ? 2 
ATOM   5381  O O     . THR B 1 231 ? 47.411  -8.934  3.821   1.000 30.145  0 231 THR BBB O     1 ? 2 
ATOM   5382  C CB    . THR B 1 231 ? 48.167  -6.542  1.899   1.000 33.375  0 231 THR BBB CB    1 ? 2 
ATOM   5383  O OG1   . THR B 1 231 ? 48.534  -5.161  1.892   1.000 34.495  0 231 THR BBB OG1   1 ? 2 
ATOM   5384  C CG2   . THR B 1 231 ? 47.755  -6.990  0.518   1.000 33.251  0 231 THR BBB CG2   1 ? 2 
ATOM   5385  N N     . VAL B 1 232 ? 45.508  -8.600  2.608   1.000 30.613  0 232 VAL BBB N     1 ? 2 
ATOM   5386  C CA    . VAL B 1 232 ? 45.030  -10.010 2.619   1.000 29.247  0 232 VAL BBB CA    1 ? 2 
ATOM   5387  C C     . VAL B 1 232 ? 45.075  -10.533 1.186   1.000 30.248  0 232 VAL BBB C     1 ? 2 
ATOM   5388  O O     . VAL B 1 232 ? 44.386  -9.919  0.344   1.000 29.194  0 232 VAL BBB O     1 ? 2 
ATOM   5389  C CB    . VAL B 1 232 ? 43.623  -10.128 3.210   1.000 27.931  0 232 VAL BBB CB    1 ? 2 
ATOM   5390  C CG1   . VAL B 1 232 ? 43.037  -11.510 2.936   1.000 26.710  0 232 VAL BBB CG1   1 ? 2 
ATOM   5391  C CG2   . VAL B 1 232 ? 43.657  -9.816  4.709   1.000 27.644  0 232 VAL BBB CG2   1 ? 2 
ATOM   5392  N N     . ALA B 1 233 ? 45.815  -11.629 0.961   1.000 31.393  0 233 ALA BBB N     1 ? 2 
ATOM   5393  C CA    . ALA B 1 233 ? 45.803  -12.432 -0.282  1.000 32.976  0 233 ALA BBB CA    1 ? 2 
ATOM   5394  C C     . ALA B 1 233 ? 44.741  -13.522 -0.125  1.000 34.490  0 233 ALA BBB C     1 ? 2 
ATOM   5395  O O     . ALA B 1 233 ? 44.975  -14.467 0.622   1.000 36.681  0 233 ALA BBB O     1 ? 2 
ATOM   5396  C CB    . ALA B 1 233 ? 47.170  -13.014 -0.554  1.000 32.957  0 233 ALA BBB CB    1 ? 2 
ATOM   5397  N N     . MET B 1 234 ? 43.601  -13.321 -0.779  1.000 35.843  0 234 MET BBB N     1 ? 2 
ATOM   5398  C CA    . MET B 1 234 ? 42.427  -14.205 -0.805  1.000 36.187  0 234 MET BBB CA    1 ? 2 
ATOM   5399  C C     . MET B 1 234 ? 42.429  -14.960 -2.140  1.000 38.618  0 234 MET BBB C     1 ? 2 
ATOM   5400  O O     . MET B 1 234 ? 42.262  -14.294 -3.206  1.000 38.198  0 234 MET BBB O     1 ? 2 
ATOM   5401  C CB    . MET B 1 234 ? 41.197  -13.317 -0.682  1.000 36.130  0 234 MET BBB CB    1 ? 2 
ATOM   5402  C CG    . MET B 1 234 ? 39.889  -14.041 -0.891  1.000 36.973  0 234 MET BBB CG    1 ? 2 
ATOM   5403  S SD    . MET B 1 234 ? 38.499  -13.076 -0.278  1.000 40.843  0 234 MET BBB SD    1 ? 2 
ATOM   5404  C CE    . MET B 1 234 ? 38.593  -11.545 -1.209  1.000 41.510  0 234 MET BBB CE    1 ? 2 
ATOM   5405  N N     . ARG B 1 235 ? 42.689  -16.267 -2.098  1.000 39.346  0 235 ARG BBB N     1 ? 2 
ATOM   5406  C CA    . ARG B 1 235 ? 42.747  -17.130 -3.300  1.000 41.134  0 235 ARG BBB CA    1 ? 2 
ATOM   5407  C C     . ARG B 1 235 ? 41.420  -17.031 -4.078  1.000 43.213  0 235 ARG BBB C     1 ? 2 
ATOM   5408  O O     . ARG B 1 235 ? 41.471  -16.895 -5.350  1.000 40.791  0 235 ARG BBB O     1 ? 2 
ATOM   5409  C CB    . ARG B 1 235 ? 43.049  -18.581 -2.916  1.000 42.438  0 235 ARG BBB CB    1 ? 2 
ATOM   5410  C CG    . ARG B 1 235 ? 43.282  -19.493 -4.110  1.000 46.016  0 235 ARG BBB CG    1 ? 2 
ATOM   5411  C CD    . ARG B 1 235 ? 43.792  -20.864 -3.709  1.000 48.444  0 235 ARG BBB CD    1 ? 2 
ATOM   5412  N NE    . ARG B 1 235 ? 44.395  -21.531 -4.861  1.000 54.187  0 235 ARG BBB NE    1 ? 2 
ATOM   5413  C CZ    . ARG B 1 235 ? 43.707  -22.070 -5.873  1.000 56.764  0 235 ARG BBB CZ    1 ? 2 
ATOM   5414  N NH1   . ARG B 1 235 ? 42.384  -22.041 -5.890  1.000 55.051  0 235 ARG BBB NH1   1 ? 2 
ATOM   5415  N NH2   . ARG B 1 235 ? 44.342  -22.706 -6.844  1.000 59.256  0 235 ARG BBB NH2   1 ? 2 
ATOM   5416  N N     . SER B 1 236 ? 40.267  -17.085 -3.395  1.000 40.520  0 236 SER BBB N     1 ? 2 
ATOM   5417  C CA    . SER B 1 236 ? 38.950  -17.060 -4.066  1.000 40.524  0 236 SER BBB CA    1 ? 2 
ATOM   5418  C C     . SER B 1 236 ? 37.962  -16.201 -3.269  1.000 39.024  0 236 SER BBB C     1 ? 2 
ATOM   5419  O O     . SER B 1 236 ? 37.786  -15.030 -3.636  1.000 39.023  0 236 SER BBB O     1 ? 2 
ATOM   5420  C CB    . SER B 1 236 ? 38.449  -18.461 -4.306  1.000 40.665  0 236 SER BBB CB    1 ? 2 
ATOM   5421  O OG    . SER B 1 236 ? 38.487  -19.248 -3.122  1.000 41.891  0 236 SER BBB OG    1 ? 2 
ATOM   5422  N N     . ILE B 1 237 ? 37.336  -16.768 -2.240  1.000 37.473  0 237 ILE BBB N     1 ? 2 
ATOM   5423  C CA    . ILE B 1 237 ? 36.189  -16.126 -1.538  1.000 38.227  0 237 ILE BBB CA    1 ? 2 
ATOM   5424  C C     . ILE B 1 237 ? 36.489  -16.072 -0.044  1.000 38.691  0 237 ILE BBB C     1 ? 2 
ATOM   5425  O O     . ILE B 1 237 ? 37.250  -16.887 0.469   1.000 40.014  0 237 ILE BBB O     1 ? 2 
ATOM   5426  C CB    . ILE B 1 237 ? 34.876  -16.872 -1.852  1.000 37.473  0 237 ILE BBB CB    1 ? 2 
ATOM   5427  C CG1   . ILE B 1 237 ? 34.917  -18.327 -1.356  1.000 37.840  0 237 ILE BBB CG1   1 ? 2 
ATOM   5428  C CG2   . ILE B 1 237 ? 34.563  -16.768 -3.348  1.000 36.518  0 237 ILE BBB CG2   1 ? 2 
ATOM   5429  C CD1   . ILE B 1 237 ? 33.575  -19.067 -1.427  1.000 36.502  0 237 ILE BBB CD1   1 ? 2 
ATOM   5430  N N     . PRO B 1 238 ? 35.907  -15.104 0.693   1.000 39.689  0 238 PRO BBB N     1 ? 2 
ATOM   5431  C CA    . PRO B 1 238 ? 36.055  -15.024 2.143   1.000 37.878  0 238 PRO BBB CA    1 ? 2 
ATOM   5432  C C     . PRO B 1 238 ? 35.217  -16.025 2.948   1.000 37.600  0 238 PRO BBB C     1 ? 2 
ATOM   5433  O O     . PRO B 1 238 ? 34.076  -16.203 2.629   1.000 37.331  0 238 PRO BBB O     1 ? 2 
ATOM   5434  C CB    . PRO B 1 238 ? 35.623  -13.587 2.453   1.000 38.316  0 238 PRO BBB CB    1 ? 2 
ATOM   5435  C CG    . PRO B 1 238 ? 34.603  -13.265 1.385   1.000 39.557  0 238 PRO BBB CG    1 ? 2 
ATOM   5436  C CD    . PRO B 1 238 ? 35.084  -14.000 0.150   1.000 40.790  0 238 PRO BBB CD    1 ? 2 
ATOM   5437  N N     . LEU B 1 239 ? 35.803  -16.628 3.988   1.000 37.067  0 239 LEU BBB N     1 ? 2 
ATOM   5438  C CA    . LEU B 1 239 ? 35.063  -17.502 4.932   1.000 37.966  0 239 LEU BBB CA    1 ? 2 
ATOM   5439  C C     . LEU B 1 239 ? 34.269  -18.562 4.172   1.000 38.305  0 239 LEU BBB C     1 ? 2 
ATOM   5440  O O     . LEU B 1 239 ? 33.040  -18.610 4.324   1.000 37.901  0 239 LEU BBB O     1 ? 2 
ATOM   5441  C CB    . LEU B 1 239 ? 34.097  -16.617 5.726   1.000 37.678  0 239 LEU BBB CB    1 ? 2 
ATOM   5442  C CG    . LEU B 1 239 ? 34.751  -15.524 6.548   1.000 37.053  0 239 LEU BBB CG    1 ? 2 
ATOM   5443  C CD1   . LEU B 1 239 ? 33.692  -14.702 7.268   1.000 37.481  0 239 LEU BBB CD1   1 ? 2 
ATOM   5444  C CD2   . LEU B 1 239 ? 35.718  -16.123 7.530   1.000 36.459  0 239 LEU BBB CD2   1 ? 2 
ATOM   5445  N N     . ARG B 1 240 ? 34.950  -19.371 3.377   1.000 39.345  0 240 ARG BBB N     1 ? 2 
ATOM   5446  C CA    . ARG B 1 240 ? 34.320  -20.476 2.617   1.000 41.654  0 240 ARG BBB CA    1 ? 2 
ATOM   5447  C C     . ARG B 1 240 ? 33.522  -21.385 3.572   1.000 38.181  0 240 ARG BBB C     1 ? 2 
ATOM   5448  O O     . ARG B 1 240 ? 34.070  -21.814 4.571   1.000 34.787  0 240 ARG BBB O     1 ? 2 
ATOM   5449  C CB    . ARG B 1 240 ? 35.425  -21.201 1.858   1.000 45.905  0 240 ARG BBB CB    1 ? 2 
ATOM   5450  C CG    . ARG B 1 240 ? 34.961  -22.297 0.903   1.000 51.827  0 240 ARG BBB CG    1 ? 2 
ATOM   5451  C CD    . ARG B 1 240 ? 36.110  -23.261 0.636   1.000 57.677  0 240 ARG BBB CD    1 ? 2 
ATOM   5452  N NE    . ARG B 1 240 ? 37.008  -23.303 1.802   1.000 62.497  0 240 ARG BBB NE    1 ? 2 
ATOM   5453  C CZ    . ARG B 1 240 ? 36.762  -23.946 2.956   1.000 59.933  0 240 ARG BBB CZ    1 ? 2 
ATOM   5454  N NH1   . ARG B 1 240 ? 35.645  -24.631 3.127   1.000 58.329  0 240 ARG BBB NH1   1 ? 2 
ATOM   5455  N NH2   . ARG B 1 240 ? 37.651  -23.897 3.931   1.000 62.598  0 240 ARG BBB NH2   1 ? 2 
ATOM   5456  N N     . GLY B 1 241 ? 32.264  -21.672 3.218   1.000 38.305  0 241 GLY BBB N     1 ? 2 
ATOM   5457  C CA    . GLY B 1 241 ? 31.298  -22.491 3.982   1.000 37.922  0 241 GLY BBB CA    1 ? 2 
ATOM   5458  C C     . GLY B 1 241 ? 30.306  -21.602 4.731   1.000 38.581  0 241 GLY BBB C     1 ? 2 
ATOM   5459  O O     . GLY B 1 241 ? 29.211  -22.057 5.101   1.000 38.940  0 241 GLY BBB O     1 ? 2 
ATOM   5460  N N     . PHE B 1 242 ? 30.694  -20.361 5.011   1.000 36.644  0 242 PHE BBB N     1 ? 2 
ATOM   5461  C CA    . PHE B 1 242 ? 29.861  -19.394 5.750   1.000 36.738  0 242 PHE BBB CA    1 ? 2 
ATOM   5462  C C     . PHE B 1 242 ? 28.932  -18.697 4.756   1.000 36.774  0 242 PHE BBB C     1 ? 2 
ATOM   5463  O O     . PHE B 1 242 ? 29.244  -18.618 3.537   1.000 42.293  0 242 PHE BBB O     1 ? 2 
ATOM   5464  C CB    . PHE B 1 242 ? 30.724  -18.382 6.498   1.000 39.246  0 242 PHE BBB CB    1 ? 2 
ATOM   5465  C CG    . PHE B 1 242 ? 31.494  -18.906 7.694   1.000 42.504  0 242 PHE BBB CG    1 ? 2 
ATOM   5466  C CD1   . PHE B 1 242 ? 32.407  -19.949 7.577   1.000 44.405  0 242 PHE BBB CD1   1 ? 2 
ATOM   5467  C CD2   . PHE B 1 242 ? 31.432  -18.241 8.909   1.000 43.820  0 242 PHE BBB CD2   1 ? 2 
ATOM   5468  C CE1   . PHE B 1 242 ? 33.115  -20.397 8.684   1.000 45.569  0 242 PHE BBB CE1   1 ? 2 
ATOM   5469  C CE2   . PHE B 1 242 ? 32.165  -18.679 10.005  1.000 43.701  0 242 PHE BBB CE2   1 ? 2 
ATOM   5470  C CZ    . PHE B 1 242 ? 33.023  -19.742 9.886   1.000 43.908  0 242 PHE BBB CZ    1 ? 2 
ATOM   5471  N N     . ASP B 1 243 ? 27.826  -18.169 5.264   1.000 33.549  0 243 ASP BBB N     1 ? 2 
ATOM   5472  C CA    . ASP B 1 243 ? 26.839  -17.384 4.506   1.000 31.979  0 243 ASP BBB CA    1 ? 2 
ATOM   5473  C C     . ASP B 1 243 ? 27.534  -16.334 3.654   1.000 31.645  0 243 ASP BBB C     1 ? 2 
ATOM   5474  O O     . ASP B 1 243 ? 28.329  -15.588 4.216   1.000 31.635  0 243 ASP BBB O     1 ? 2 
ATOM   5475  C CB    . ASP B 1 243 ? 25.870  -16.721 5.464   1.000 31.949  0 243 ASP BBB CB    1 ? 2 
ATOM   5476  C CG    . ASP B 1 243 ? 24.784  -15.969 4.740   1.000 32.313  0 243 ASP BBB CG    1 ? 2 
ATOM   5477  O OD1   . ASP B 1 243 ? 23.891  -16.637 4.189   1.000 31.309  0 243 ASP BBB OD1   1 ? 2 
ATOM   5478  O OD2   . ASP B 1 243 ? 24.875  -14.723 4.727   1.000 32.092  0 243 ASP BBB OD2   1 ? 2 
ATOM   5479  N N     . ARG B 1 244 ? 27.237  -16.291 2.353   1.000 31.319  0 244 ARG BBB N     1 ? 2 
ATOM   5480  C CA    . ARG B 1 244 ? 27.924  -15.409 1.379   1.000 32.183  0 244 ARG BBB CA    1 ? 2 
ATOM   5481  C C     . ARG B 1 244 ? 27.605  -13.953 1.731   1.000 31.368  0 244 ARG BBB C     1 ? 2 
ATOM   5482  O O     . ARG B 1 244 ? 28.590  -13.174 1.854   1.000 30.267  0 244 ARG BBB O     1 ? 2 
ATOM   5483  C CB    . ARG B 1 244 ? 27.517  -15.686 -0.086  1.000 34.011  0 244 ARG BBB CB    1 ? 2 
ATOM   5484  C CG    . ARG B 1 244 ? 27.999  -17.017 -0.643  1.000 33.921  0 244 ARG BBB CG    1 ? 2 
ATOM   5485  C CD    . ARG B 1 244 ? 29.504  -17.077 -0.763  1.000 35.341  0 244 ARG BBB CD    1 ? 2 
ATOM   5486  N NE    . ARG B 1 244 ? 30.112  -17.505 0.493   1.000 34.274  0 244 ARG BBB NE    1 ? 2 
ATOM   5487  C CZ    . ARG B 1 244 ? 31.243  -17.052 1.005   1.000 33.671  0 244 ARG BBB CZ    1 ? 2 
ATOM   5488  N NH1   . ARG B 1 244 ? 31.959  -16.144 0.377   1.000 33.376  0 244 ARG BBB NH1   1 ? 2 
ATOM   5489  N NH2   . ARG B 1 244 ? 31.629  -17.478 2.197   1.000 35.181  0 244 ARG BBB NH2   1 ? 2 
ATOM   5490  N N     . GLN B 1 245 ? 26.319  -13.607 1.898   1.000 29.436  0 245 GLN BBB N     1 ? 2 
ATOM   5491  C CA    . GLN B 1 245 ? 25.905  -12.209 2.169   1.000 30.584  0 245 GLN BBB CA    1 ? 2 
ATOM   5492  C C     . GLN B 1 245 ? 26.693  -11.637 3.359   1.000 30.435  0 245 GLN BBB C     1 ? 2 
ATOM   5493  O O     . GLN B 1 245 ? 27.272  -10.524 3.211   1.000 30.225  0 245 GLN BBB O     1 ? 2 
ATOM   5494  C CB    . GLN B 1 245 ? 24.407  -12.119 2.459   1.000 31.278  0 245 GLN BBB CB    1 ? 2 
ATOM   5495  C CG    . GLN B 1 245 ? 23.906  -10.683 2.445   1.000 32.111  0 245 GLN BBB CG    1 ? 2 
ATOM   5496  C CD    . GLN B 1 245 ? 22.430  -10.598 2.715   1.000 32.906  0 245 GLN BBB CD    1 ? 2 
ATOM   5497  O OE1   . GLN B 1 245 ? 21.813  -11.568 3.130   1.000 32.299  0 245 GLN BBB OE1   1 ? 2 
ATOM   5498  N NE2   . GLN B 1 245 ? 21.856  -9.437  2.449   1.000 33.361  0 245 GLN BBB NE2   1 ? 2 
ATOM   5499  N N     . CYS B 1 246 ? 26.738  -12.368 4.481   1.000 29.878  0 246 CYS BBB N     1 ? 2 
ATOM   5500  C CA    . CYS B 1 246 ? 27.454  -11.952 5.713   1.000 31.092  0 246 CYS BBB CA    1 ? 2 
ATOM   5501  C C     . CYS B 1 246 ? 28.965  -11.909 5.488   1.000 30.981  0 246 CYS BBB C     1 ? 2 
ATOM   5502  O O     . CYS B 1 246 ? 29.593  -10.903 5.899   1.000 30.966  0 246 CYS BBB O     1 ? 2 
ATOM   5503  C CB    . CYS B 1 246 ? 27.165  -12.892 6.872   1.000 31.898  0 246 CYS BBB CB    1 ? 2 
ATOM   5504  S SG    . CYS B 1 246 ? 25.439  -12.816 7.412   1.000 33.669  0 246 CYS BBB SG    1 ? 2 
ATOM   5505  N N     . SER B 1 247 ? 29.537  -12.943 4.868   1.000 31.444  0 247 SER BBB N     1 ? 2 
ATOM   5506  C CA    . SER B 1 247 ? 30.991  -13.007 4.625   1.000 32.322  0 247 SER BBB CA    1 ? 2 
ATOM   5507  C C     . SER B 1 247 ? 31.405  -11.770 3.820   1.000 34.257  0 247 SER BBB C     1 ? 2 
ATOM   5508  O O     . SER B 1 247 ? 32.462  -11.197 4.109   1.000 34.905  0 247 SER BBB O     1 ? 2 
ATOM   5509  C CB    . SER B 1 247 ? 31.396  -14.303 3.984   1.000 31.723  0 247 SER BBB CB    1 ? 2 
ATOM   5510  O OG    . SER B 1 247 ? 31.038  -15.401 4.808   1.000 30.306  0 247 SER BBB OG    1 ? 2 
ATOM   5511  N N     . GLU B 1 248 ? 30.569  -11.325 2.884   1.000 36.823  0 248 GLU BBB N     1 ? 2 
ATOM   5512  C CA    . GLU B 1 248 ? 30.930  -10.233 1.929   1.000 37.117  0 248 GLU BBB CA    1 ? 2 
ATOM   5513  C C     . GLU B 1 248 ? 30.726  -8.872  2.606   1.000 35.289  0 248 GLU BBB C     1 ? 2 
ATOM   5514  O O     . GLU B 1 248 ? 31.544  -7.954  2.360   1.000 32.550  0 248 GLU BBB O     1 ? 2 
ATOM   5515  C CB    . GLU B 1 248 ? 30.122  -10.376 0.628   1.000 39.524  0 248 GLU BBB CB    1 ? 2 
ATOM   5516  C CG    . GLU B 1 248 ? 30.666  -11.482 -0.281  1.000 40.953  0 248 GLU BBB CG    1 ? 2 
ATOM   5517  C CD    . GLU B 1 248 ? 29.700  -11.961 -1.345  1.000 42.678  0 248 GLU BBB CD    1 ? 2 
ATOM   5518  O OE1   . GLU B 1 248 ? 28.757  -11.220 -1.670  1.000 43.078  0 248 GLU BBB OE1   1 ? 2 
ATOM   5519  O OE2   . GLU B 1 248 ? 29.890  -13.081 -1.839  1.000 48.128  0 248 GLU BBB OE2   1 ? 2 
ATOM   5520  N N     . LYS B 1 249 ? 29.694  -8.728  3.442   1.000 34.420  0 249 LYS BBB N     1 ? 2 
ATOM   5521  C CA    . LYS B 1 249 ? 29.568  -7.520  4.295   1.000 34.714  0 249 LYS BBB CA    1 ? 2 
ATOM   5522  C C     . LYS B 1 249 ? 30.843  -7.338  5.129   1.000 34.087  0 249 LYS BBB C     1 ? 2 
ATOM   5523  O O     . LYS B 1 249 ? 31.373  -6.207  5.148   1.000 35.674  0 249 LYS BBB O     1 ? 2 
ATOM   5524  C CB    . LYS B 1 249 ? 28.357  -7.563  5.215   1.000 34.954  0 249 LYS BBB CB    1 ? 2 
ATOM   5525  C CG    . LYS B 1 249 ? 28.205  -6.263  5.984   1.000 35.032  0 249 LYS BBB CG    1 ? 2 
ATOM   5526  C CD    . LYS B 1 249 ? 26.965  -6.149  6.795   1.000 35.675  0 249 LYS BBB CD    1 ? 2 
ATOM   5527  C CE    . LYS B 1 249 ? 26.874  -4.815  7.498   1.000 37.291  0 249 LYS BBB CE    1 ? 2 
ATOM   5528  N NZ    . LYS B 1 249 ? 27.106  -3.710  6.540   1.000 39.569  0 249 LYS BBB NZ    1 ? 2 
ATOM   5529  N N     . ILE B 1 250 ? 31.387  -8.394  5.728   1.000 32.189  0 250 ILE BBB N     1 ? 2 
ATOM   5530  C CA    . ILE B 1 250 ? 32.635  -8.239  6.529   1.000 32.752  0 250 ILE BBB CA    1 ? 2 
ATOM   5531  C C     . ILE B 1 250 ? 33.748  -7.664  5.645   1.000 33.737  0 250 ILE BBB C     1 ? 2 
ATOM   5532  O O     . ILE B 1 250 ? 34.384  -6.649  6.044   1.000 33.015  0 250 ILE BBB O     1 ? 2 
ATOM   5533  C CB    . ILE B 1 250 ? 33.031  -9.563  7.197   1.000 32.667  0 250 ILE BBB CB    1 ? 2 
ATOM   5534  C CG1   . ILE B 1 250 ? 31.998  -9.943  8.265   1.000 32.712  0 250 ILE BBB CG1   1 ? 2 
ATOM   5535  C CG2   . ILE B 1 250 ? 34.449  -9.513  7.756   1.000 31.695  0 250 ILE BBB CG2   1 ? 2 
ATOM   5536  C CD1   . ILE B 1 250 ? 31.920  -11.417 8.483   1.000 32.805  0 250 ILE BBB CD1   1 ? 2 
ATOM   5537  N N     . VAL B 1 251 ? 33.978  -8.270  4.481   1.000 33.756  0 251 VAL BBB N     1 ? 2 
ATOM   5538  C CA    . VAL B 1 251 ? 35.079  -7.857  3.567   1.000 34.109  0 251 VAL BBB CA    1 ? 2 
ATOM   5539  C C     . VAL B 1 251 ? 34.826  -6.412  3.128   1.000 34.265  0 251 VAL BBB C     1 ? 2 
ATOM   5540  O O     . VAL B 1 251 ? 35.777  -5.634  3.168   1.000 36.991  0 251 VAL BBB O     1 ? 2 
ATOM   5541  C CB    . VAL B 1 251 ? 35.207  -8.832  2.386   1.000 33.957  0 251 VAL BBB CB    1 ? 2 
ATOM   5542  C CG1   . VAL B 1 251 ? 36.077  -8.278  1.255   1.000 34.133  0 251 VAL BBB CG1   1 ? 2 
ATOM   5543  C CG2   . VAL B 1 251 ? 35.704  -10.167 2.877   1.000 32.395  0 251 VAL BBB CG2   1 ? 2 
ATOM   5544  N N     . GLU B 1 252 ? 33.589  -6.057  2.791   1.000 34.219  0 252 GLU BBB N     1 ? 2 
ATOM   5545  C CA    . GLU B 1 252 ? 33.190  -4.662  2.462   1.000 34.390  0 252 GLU BBB CA    1 ? 2 
ATOM   5546  C C     . GLU B 1 252 ? 33.603  -3.739  3.614   1.000 31.525  0 252 GLU BBB C     1 ? 2 
ATOM   5547  O O     . GLU B 1 252 ? 34.208  -2.709  3.354   1.000 30.400  0 252 GLU BBB O     1 ? 2 
ATOM   5548  C CB    . GLU B 1 252 ? 31.697  -4.635  2.125   1.000 39.017  0 252 GLU BBB CB    1 ? 2 
ATOM   5549  C CG    . GLU B 1 252 ? 31.145  -3.257  1.787   1.000 44.459  0 252 GLU BBB CG    1 ? 2 
ATOM   5550  C CD    . GLU B 1 252 ? 29.631  -3.192  1.748   1.000 47.026  0 252 GLU BBB CD    1 ? 2 
ATOM   5551  O OE1   . GLU B 1 252 ? 29.044  -3.831  0.834   1.000 51.679  0 252 GLU BBB OE1   1 ? 2 
ATOM   5552  O OE2   . GLU B 1 252 ? 29.057  -2.544  2.643   1.000 48.775  0 252 GLU BBB OE2   1 ? 2 
ATOM   5553  N N     . TYR B 1 253 ? 33.334  -4.100  4.869   1.000 30.801  0 253 TYR BBB N     1 ? 2 
ATOM   5554  C CA    . TYR B 1 253 ? 33.671  -3.253  6.042   1.000 29.738  0 253 TYR BBB CA    1 ? 2 
ATOM   5555  C C     . TYR B 1 253 ? 35.198  -3.184  6.197   1.000 29.764  0 253 TYR BBB C     1 ? 2 
ATOM   5556  O O     . TYR B 1 253 ? 35.760  -2.060  6.353   1.000 30.406  0 253 TYR BBB O     1 ? 2 
ATOM   5557  C CB    . TYR B 1 253 ? 32.963  -3.725  7.310   1.000 29.163  0 253 TYR BBB CB    1 ? 2 
ATOM   5558  C CG    . TYR B 1 253 ? 33.190  -2.827  8.496   1.000 27.682  0 253 TYR BBB CG    1 ? 2 
ATOM   5559  C CD1   . TYR B 1 253 ? 34.270  -3.007  9.347   1.000 27.751  0 253 TYR BBB CD1   1 ? 2 
ATOM   5560  C CD2   . TYR B 1 253 ? 32.359  -1.748  8.720   1.000 27.757  0 253 TYR BBB CD2   1 ? 2 
ATOM   5561  C CE1   . TYR B 1 253 ? 34.495  -2.133  10.411  1.000 28.466  0 253 TYR BBB CE1   1 ? 2 
ATOM   5562  C CE2   . TYR B 1 253 ? 32.595  -0.848  9.742   1.000 27.991  0 253 TYR BBB CE2   1 ? 2 
ATOM   5563  C CZ    . TYR B 1 253 ? 33.640  -1.056  10.614  1.000 28.351  0 253 TYR BBB CZ    1 ? 2 
ATOM   5564  O OH    . TYR B 1 253 ? 33.757  -0.159  11.648  1.000 31.547  0 253 TYR BBB OH    1 ? 2 
ATOM   5565  N N     . MET B 1 254 ? 35.881  -4.313  6.129   1.000 29.167  0 254 MET BBB N     1 ? 2 
ATOM   5566  C CA    . MET B 1 254 ? 37.352  -4.328  6.293   1.000 30.863  0 254 MET BBB CA    1 ? 2 
ATOM   5567  C C     . MET B 1 254 ? 38.026  -3.447  5.229   1.000 33.228  0 254 MET BBB C     1 ? 2 
ATOM   5568  O O     . MET B 1 254 ? 38.994  -2.733  5.588   1.000 32.619  0 254 MET BBB O     1 ? 2 
ATOM   5569  C CB    . MET B 1 254 ? 37.877  -5.759  6.203   1.000 30.725  0 254 MET BBB CB    1 ? 2 
ATOM   5570  C CG    . MET B 1 254 ? 37.344  -6.658  7.315   1.000 30.923  0 254 MET BBB CG    1 ? 2 
ATOM   5571  S SD    . MET B 1 254 ? 38.135  -8.266  7.393   1.000 31.184  0 254 MET BBB SD    1 ? 2 
ATOM   5572  C CE    . MET B 1 254 ? 39.849  -7.770  7.567   1.000 31.585  0 254 MET BBB CE    1 ? 2 
ATOM   5573  N N     . LYS B 1 255 ? 37.559  -3.514  3.970   1.000 35.037  0 255 LYS BBB N     1 ? 2 
ATOM   5574  C CA    . LYS B 1 255 ? 38.042  -2.671  2.841   1.000 36.934  0 255 LYS BBB CA    1 ? 2 
ATOM   5575  C C     . LYS B 1 255 ? 37.825  -1.191  3.166   1.000 34.590  0 255 LYS BBB C     1 ? 2 
ATOM   5576  O O     . LYS B 1 255 ? 38.764  -0.425  2.968   1.000 33.709  0 255 LYS BBB O     1 ? 2 
ATOM   5577  C CB    . LYS B 1 255 ? 37.305  -2.994  1.537   1.000 40.918  0 255 LYS BBB CB    1 ? 2 
ATOM   5578  C CG    . LYS B 1 255 ? 37.994  -4.018  0.635   1.000 46.736  0 255 LYS BBB CG    1 ? 2 
ATOM   5579  C CD    . LYS B 1 255 ? 37.134  -4.426  -0.563  1.000 52.090  0 255 LYS BBB CD    1 ? 2 
ATOM   5580  C CE    . LYS B 1 255 ? 37.810  -5.406  -1.499  1.000 55.950  0 255 LYS BBB CE    1 ? 2 
ATOM   5581  N NZ    . LYS B 1 255 ? 36.852  -6.294  -2.212  1.000 56.490  0 255 LYS BBB NZ    1 ? 2 
ATOM   5582  N N     . ALA B 1 256 ? 36.633  -0.822  3.659   1.000 33.159  0 256 ALA BBB N     1 ? 2 
ATOM   5583  C CA    . ALA B 1 256 ? 36.245  0.573   3.984   1.000 33.683  0 256 ALA BBB CA    1 ? 2 
ATOM   5584  C C     . ALA B 1 256 ? 37.065  1.114   5.149   1.000 33.534  0 256 ALA BBB C     1 ? 2 
ATOM   5585  O O     . ALA B 1 256 ? 37.088  2.345   5.287   1.000 36.026  0 256 ALA BBB O     1 ? 2 
ATOM   5586  C CB    . ALA B 1 256 ? 34.763  0.681   4.274   1.000 33.224  0 256 ALA BBB CB    1 ? 2 
ATOM   5587  N N     . THR B 1 257 ? 37.716  0.264   5.951   1.000 33.842  0 257 THR BBB N     1 ? 2 
ATOM   5588  C CA    . THR B 1 257 ? 38.511  0.719   7.125   1.000 34.069  0 257 THR BBB CA    1 ? 2 
ATOM   5589  C C     . THR B 1 257 ? 40.008  0.533   6.880   1.000 33.698  0 257 THR BBB C     1 ? 2 
ATOM   5590  O O     . THR B 1 257 ? 40.760  0.775   7.841   1.000 34.011  0 257 THR BBB O     1 ? 2 
ATOM   5591  C CB    . THR B 1 257 ? 38.101  0.021   8.439   1.000 34.480  0 257 THR BBB CB    1 ? 2 
ATOM   5592  O OG1   . THR B 1 257 ? 38.189  -1.411  8.339   1.000 34.754  0 257 THR BBB OG1   1 ? 2 
ATOM   5593  C CG2   . THR B 1 257 ? 36.716  0.480   8.860   1.000 33.886  0 257 THR BBB CG2   1 ? 2 
ATOM   5594  N N     . GLY B 1 258 ? 40.424  0.074   5.699   1.000 33.354  0 258 GLY BBB N     1 ? 2 
ATOM   5595  C CA    . GLY B 1 258 ? 41.836  0.195   5.268   1.000 34.822  0 258 GLY BBB CA    1 ? 2 
ATOM   5596  C C     . GLY B 1 258 ? 42.549  -1.124  4.995   1.000 34.136  0 258 GLY BBB C     1 ? 2 
ATOM   5597  O O     . GLY B 1 258 ? 43.728  -1.081  4.644   1.000 34.727  0 258 GLY BBB O     1 ? 2 
ATOM   5598  N N     . THR B 1 259 ? 41.893  -2.271  5.122   1.000 33.954  0 259 THR BBB N     1 ? 2 
ATOM   5599  C CA    . THR B 1 259 ? 42.522  -3.544  4.721   1.000 34.579  0 259 THR BBB CA    1 ? 2 
ATOM   5600  C C     . THR B 1 259 ? 42.477  -3.631  3.192   1.000 36.076  0 259 THR BBB C     1 ? 2 
ATOM   5601  O O     . THR B 1 259 ? 41.421  -3.383  2.582   1.000 34.864  0 259 THR BBB O     1 ? 2 
ATOM   5602  C CB    . THR B 1 259 ? 41.903  -4.721  5.466   1.000 34.738  0 259 THR BBB CB    1 ? 2 
ATOM   5603  O OG1   . THR B 1 259 ? 41.953  -4.452  6.868   1.000 36.056  0 259 THR BBB OG1   1 ? 2 
ATOM   5604  C CG2   . THR B 1 259 ? 42.629  -6.011  5.186   1.000 34.835  0 259 THR BBB CG2   1 ? 2 
ATOM   5605  N N     . LYS B 1 260 ? 43.606  -3.980  2.582   1.000 37.343  0 260 LYS BBB N     1 ? 2 
ATOM   5606  C CA    . LYS B 1 260 ? 43.719  -4.155  1.123   1.000 39.224  0 260 LYS BBB CA    1 ? 2 
ATOM   5607  C C     . LYS B 1 260 ? 43.579  -5.639  0.864   1.000 38.112  0 260 LYS BBB C     1 ? 2 
ATOM   5608  O O     . LYS B 1 260 ? 44.139  -6.404  1.630   1.000 37.947  0 260 LYS BBB O     1 ? 2 
ATOM   5609  C CB    . LYS B 1 260 ? 45.049  -3.583  0.610   1.000 42.254  0 260 LYS BBB CB    1 ? 2 
ATOM   5610  C CG    . LYS B 1 260 ? 45.129  -2.058  0.621   1.000 45.495  0 260 LYS BBB CG    1 ? 2 
ATOM   5611  C CD    . LYS B 1 260 ? 46.518  -1.496  0.441   1.000 47.997  0 260 LYS BBB CD    1 ? 2 
ATOM   5612  C CE    . LYS B 1 260 ? 47.393  -1.710  1.653   1.000 48.604  0 260 LYS BBB CE    1 ? 2 
ATOM   5613  N NZ    . LYS B 1 260 ? 48.821  -1.415  1.358   1.000 49.655  0 260 LYS BBB NZ    1 ? 2 
ATOM   5614  N N     . PHE B 1 261 ? 42.833  -5.993  -0.183  1.000 38.570  0 261 PHE BBB N     1 ? 2 
ATOM   5615  C CA    . PHE B 1 261 ? 42.546  -7.372  -0.633  1.000 38.616  0 261 PHE BBB CA    1 ? 2 
ATOM   5616  C C     . PHE B 1 261 ? 42.993  -7.571  -2.082  1.000 39.566  0 261 PHE BBB C     1 ? 2 
ATOM   5617  O O     . PHE B 1 261 ? 42.570  -6.850  -2.962  1.000 39.984  0 261 PHE BBB O     1 ? 2 
ATOM   5618  C CB    . PHE B 1 261 ? 41.049  -7.657  -0.549  1.000 38.055  0 261 PHE BBB CB    1 ? 2 
ATOM   5619  C CG    . PHE B 1 261 ? 40.557  -7.836  0.851   1.000 35.966  0 261 PHE BBB CG    1 ? 2 
ATOM   5620  C CD1   . PHE B 1 261 ? 40.233  -6.731  1.611   1.000 35.559  0 261 PHE BBB CD1   1 ? 2 
ATOM   5621  C CD2   . PHE B 1 261 ? 40.394  -9.109  1.381   1.000 35.675  0 261 PHE BBB CD2   1 ? 2 
ATOM   5622  C CE1   . PHE B 1 261 ? 39.722  -6.890  2.886   1.000 34.860  0 261 PHE BBB CE1   1 ? 2 
ATOM   5623  C CE2   . PHE B 1 261 ? 39.914  -9.269  2.668   1.000 34.894  0 261 PHE BBB CE2   1 ? 2 
ATOM   5624  C CZ    . PHE B 1 261 ? 39.566  -8.158  3.413   1.000 34.913  0 261 PHE BBB CZ    1 ? 2 
ATOM   5625  N N     . LEU B 1 262 ? 43.878  -8.546  -2.281  1.000 42.397  0 262 LEU BBB N     1 ? 2 
ATOM   5626  C CA    . LEU B 1 262 ? 44.290  -9.146  -3.569  1.000 43.441  0 262 LEU BBB CA    1 ? 2 
ATOM   5627  C C     . LEU B 1 262 ? 43.402  -10.373 -3.786  1.000 44.073  0 262 LEU BBB C     1 ? 2 
ATOM   5628  O O     . LEU B 1 262 ? 43.622  -11.394 -3.143  1.000 45.837  0 262 LEU BBB O     1 ? 2 
ATOM   5629  C CB    . LEU B 1 262 ? 45.771  -9.517  -3.487  1.000 44.937  0 262 LEU BBB CB    1 ? 2 
ATOM   5630  C CG    . LEU B 1 262 ? 46.705  -8.434  -2.942  1.000 45.210  0 262 LEU BBB CG    1 ? 2 
ATOM   5631  C CD1   . LEU B 1 262 ? 48.137  -8.913  -2.945  1.000 45.770  0 262 LEU BBB CD1   1 ? 2 
ATOM   5632  C CD2   . LEU B 1 262 ? 46.616  -7.163  -3.755  1.000 45.912  0 262 LEU BBB CD2   1 ? 2 
ATOM   5633  N N     . VAL B 1 263 ? 42.430  -10.262 -4.688  1.000 45.614  0 263 VAL BBB N     1 ? 2 
ATOM   5634  C CA    . VAL B 1 263 ? 41.374  -11.274 -4.965  1.000 45.287  0 263 VAL BBB CA    1 ? 2 
ATOM   5635  C C     . VAL B 1 263 ? 41.868  -12.191 -6.095  1.000 45.268  0 263 VAL BBB C     1 ? 2 
ATOM   5636  O O     . VAL B 1 263 ? 42.305  -11.655 -7.113  1.000 47.273  0 263 VAL BBB O     1 ? 2 
ATOM   5637  C CB    . VAL B 1 263 ? 40.065  -10.534 -5.319  1.000 45.586  0 263 VAL BBB CB    1 ? 2 
ATOM   5638  C CG1   . VAL B 1 263 ? 38.876  -11.477 -5.541  1.000 45.542  0 263 VAL BBB CG1   1 ? 2 
ATOM   5639  C CG2   . VAL B 1 263 ? 39.731  -9.465  -4.272  1.000 43.645  0 263 VAL BBB CG2   1 ? 2 
ATOM   5640  N N     . GLY B 1 264 ? 41.861  -13.513 -5.899  1.000 44.786  0 264 GLY BBB N     1 ? 2 
ATOM   5641  C CA    . GLY B 1 264 ? 42.282  -14.504 -6.909  1.000 47.303  0 264 GLY BBB CA    1 ? 2 
ATOM   5642  C C     . GLY B 1 264 ? 43.794  -14.566 -7.084  1.000 48.473  0 264 GLY BBB C     1 ? 2 
ATOM   5643  O O     . GLY B 1 264 ? 44.258  -15.021 -8.149  1.000 52.283  0 264 GLY BBB O     1 ? 2 
ATOM   5644  N N     . VAL B 1 265 ? 44.531  -14.150 -6.069  1.000 50.362  0 265 VAL BBB N     1 ? 2 
ATOM   5645  C CA    . VAL B 1 265 ? 46.011  -14.004 -6.088  1.000 52.672  0 265 VAL BBB CA    1 ? 2 
ATOM   5646  C C     . VAL B 1 265 ? 46.582  -14.666 -4.835  1.000 52.487  0 265 VAL BBB C     1 ? 2 
ATOM   5647  O O     . VAL B 1 265 ? 46.053  -14.403 -3.768  1.000 51.638  0 265 VAL BBB O     1 ? 2 
ATOM   5648  C CB    . VAL B 1 265 ? 46.406  -12.510 -6.161  1.000 55.939  0 265 VAL BBB CB    1 ? 2 
ATOM   5649  C CG1   . VAL B 1 265 ? 47.900  -12.322 -6.035  1.000 57.822  0 265 VAL BBB CG1   1 ? 2 
ATOM   5650  C CG2   . VAL B 1 265 ? 45.905  -11.824 -7.416  1.000 56.973  0 265 VAL BBB CG2   1 ? 2 
ATOM   5651  N N     . VAL B 1 266 ? 47.646  -15.452 -4.974  1.000 54.044  0 266 VAL BBB N     1 ? 2 
ATOM   5652  C CA    . VAL B 1 266 ? 48.454  -15.980 -3.837  1.000 53.745  0 266 VAL BBB CA    1 ? 2 
ATOM   5653  C C     . VAL B 1 266 ? 49.949  -15.839 -4.130  1.000 55.174  0 266 VAL BBB C     1 ? 2 
ATOM   5654  O O     . VAL B 1 266 ? 50.365  -15.728 -5.271  1.000 55.085  0 266 VAL BBB O     1 ? 2 
ATOM   5655  C CB    . VAL B 1 266 ? 48.087  -17.439 -3.515  1.000 54.276  0 266 VAL BBB CB    1 ? 2 
ATOM   5656  C CG1   . VAL B 1 266 ? 46.658  -17.533 -3.035  1.000 53.928  0 266 VAL BBB CG1   1 ? 2 
ATOM   5657  C CG2   . VAL B 1 266 ? 48.382  -18.384 -4.664  1.000 54.945  0 266 VAL BBB CG2   1 ? 2 
ATOM   5658  N N     . PRO B 1 267 ? 50.812  -15.845 -3.095  1.000 55.209  0 267 PRO BBB N     1 ? 2 
ATOM   5659  C CA    . PRO B 1 267 ? 52.250  -15.924 -3.291  1.000 54.343  0 267 PRO BBB CA    1 ? 2 
ATOM   5660  C C     . PRO B 1 267 ? 52.683  -17.197 -4.029  1.000 50.529  0 267 PRO BBB C     1 ? 2 
ATOM   5661  O O     . PRO B 1 267 ? 52.131  -18.248 -3.777  1.000 51.001  0 267 PRO BBB O     1 ? 2 
ATOM   5662  C CB    . PRO B 1 267 ? 52.846  -15.950 -1.870  1.000 53.183  0 267 PRO BBB CB    1 ? 2 
ATOM   5663  C CG    . PRO B 1 267 ? 51.756  -15.408 -0.995  1.000 53.486  0 267 PRO BBB CG    1 ? 2 
ATOM   5664  C CD    . PRO B 1 267 ? 50.457  -15.776 -1.672  1.000 53.634  0 267 PRO BBB CD    1 ? 2 
ATOM   5665  N N     . ILE B 1 268 ? 53.686  -17.044 -4.892  1.000 49.969  0 268 ILE BBB N     1 ? 2 
ATOM   5666  C CA    . ILE B 1 268 ? 54.403  -18.154 -5.595  1.000 50.914  0 268 ILE BBB CA    1 ? 2 
ATOM   5667  C C     . ILE B 1 268 ? 55.889  -18.123 -5.202  1.000 48.911  0 268 ILE BBB C     1 ? 2 
ATOM   5668  O O     . ILE B 1 268 ? 56.571  -19.137 -5.442  1.000 49.632  0 268 ILE BBB O     1 ? 2 
ATOM   5669  C CB    . ILE B 1 268 ? 54.191  -18.072 -7.125  1.000 52.121  0 268 ILE BBB CB    1 ? 2 
ATOM   5670  C CG1   . ILE B 1 268 ? 54.687  -16.741 -7.702  1.000 53.425  0 268 ILE BBB CG1   1 ? 2 
ATOM   5671  C CG2   . ILE B 1 268 ? 52.726  -18.319 -7.484  1.000 50.901  0 268 ILE BBB CG2   1 ? 2 
ATOM   5672  C CD1   . ILE B 1 268 ? 54.631  -16.651 -9.199  1.000 56.752  0 268 ILE BBB CD1   1 ? 2 
ATOM   5673  N N     . ASN B 1 269 ? 56.387  -17.029 -4.615  1.000 46.079  0 269 ASN BBB N     1 ? 2 
ATOM   5674  C CA    . ASN B 1 269 ? 57.796  -16.970 -4.133  1.000 46.872  0 269 ASN BBB CA    1 ? 2 
ATOM   5675  C C     . ASN B 1 269 ? 57.929  -15.953 -2.999  1.000 43.861  0 269 ASN BBB C     1 ? 2 
ATOM   5676  O O     . ASN B 1 269 ? 57.259  -14.895 -3.052  1.000 46.594  0 269 ASN BBB O     1 ? 2 
ATOM   5677  C CB    . ASN B 1 269 ? 58.802  -16.642 -5.243  1.000 47.918  0 269 ASN BBB CB    1 ? 2 
ATOM   5678  C CG    . ASN B 1 269 ? 60.248  -16.811 -4.808  1.000 47.782  0 269 ASN BBB CG    1 ? 2 
ATOM   5679  O OD1   . ASN B 1 269 ? 60.988  -15.841 -4.766  1.000 56.813  0 269 ASN BBB OD1   1 ? 2 
ATOM   5680  N ND2   . ASN B 1 269 ? 60.676  -18.004 -4.445  1.000 44.493  0 269 ASN BBB ND2   1 ? 2 
ATOM   5681  N N     . ILE B 1 270 ? 58.790  -16.265 -2.036  1.000 41.530  0 270 ILE BBB N     1 ? 2 
ATOM   5682  C CA    . ILE B 1 270 ? 59.034  -15.434 -0.821  1.000 41.639  0 270 ILE BBB CA    1 ? 2 
ATOM   5683  C C     . ILE B 1 270 ? 60.554  -15.362 -0.577  1.000 41.451  0 270 ILE BBB C     1 ? 2 
ATOM   5684  O O     . ILE B 1 270 ? 61.182  -16.421 -0.306  1.000 37.229  0 270 ILE BBB O     1 ? 2 
ATOM   5685  C CB    . ILE B 1 270 ? 58.216  -16.011 0.359   1.000 39.437  0 270 ILE BBB CB    1 ? 2 
ATOM   5686  C CG1   . ILE B 1 270 ? 56.715  -15.807 0.096   1.000 41.305  0 270 ILE BBB CG1   1 ? 2 
ATOM   5687  C CG2   . ILE B 1 270 ? 58.661  -15.415 1.675   1.000 39.882  0 270 ILE BBB CG2   1 ? 2 
ATOM   5688  C CD1   . ILE B 1 270 ? 55.785  -16.456 1.089   1.000 41.404  0 270 ILE BBB CD1   1 ? 2 
ATOM   5689  N N     . GLU B 1 271 ? 61.123  -14.158 -0.724  1.000 43.524  0 271 GLU BBB N     1 ? 2 
ATOM   5690  C CA    . GLU B 1 271 ? 62.594  -13.946 -0.661  1.000 51.807  0 271 GLU BBB CA    1 ? 2 
ATOM   5691  C C     . GLU B 1 271 ? 62.882  -12.852 0.363   1.000 52.185  0 271 GLU BBB C     1 ? 2 
ATOM   5692  O O     . GLU B 1 271 ? 62.059  -11.908 0.450   1.000 51.811  0 271 GLU BBB O     1 ? 2 
ATOM   5693  C CB    . GLU B 1 271 ? 63.168  -13.555 -2.024  1.000 51.715  0 271 GLU BBB CB    1 ? 2 
ATOM   5694  C CG    . GLU B 1 271 ? 63.400  -14.718 -2.970  1.000 54.196  0 271 GLU BBB CG    1 ? 2 
ATOM   5695  C CD    . GLU B 1 271 ? 63.781  -14.327 -4.405  1.000 58.802  0 271 GLU BBB CD    1 ? 2 
ATOM   5696  O OE1   . GLU B 1 271 ? 63.573  -13.153 -4.793  1.000 57.246  0 271 GLU BBB OE1   1 ? 2 
ATOM   5697  O OE2   . GLU B 1 271 ? 64.263  -15.204 -5.156  1.000 61.709  0 271 GLU BBB OE2   1 ? 2 
ATOM   5698  N N     . LYS B 1 272 ? 64.012  -12.980 1.071   1.000 53.628  0 272 LYS BBB N     1 ? 2 
ATOM   5699  C CA    . LYS B 1 272 ? 64.592  -11.870 1.879   1.000 57.375  0 272 LYS BBB CA    1 ? 2 
ATOM   5700  C C     . LYS B 1 272 ? 65.385  -10.937 0.953   1.000 55.087  0 272 LYS BBB C     1 ? 2 
ATOM   5701  O O     . LYS B 1 272 ? 66.449  -11.364 0.463   1.000 48.017  0 272 LYS BBB O     1 ? 2 
ATOM   5702  C CB    . LYS B 1 272 ? 65.463  -12.402 3.025   1.000 58.205  0 272 LYS BBB CB    1 ? 2 
ATOM   5703  C CG    . LYS B 1 272 ? 65.602  -11.411 4.174   1.000 59.455  0 272 LYS BBB CG    1 ? 2 
ATOM   5704  C CD    . LYS B 1 272 ? 64.289  -11.273 4.961   1.000 61.156  0 272 LYS BBB CD    1 ? 2 
ATOM   5705  C CE    . LYS B 1 272 ? 64.433  -10.982 6.441   1.000 63.662  0 272 LYS BBB CE    1 ? 2 
ATOM   5706  N NZ    . LYS B 1 272 ? 63.263  -11.528 7.181   1.000 64.989  0 272 LYS BBB NZ    1 ? 2 
ATOM   5707  N N     . VAL B 1 273 ? 64.870  -9.718  0.721   1.000 57.454  0 273 VAL BBB N     1 ? 2 
ATOM   5708  C CA    . VAL B 1 273 ? 65.595  -8.626  0.009   1.000 60.376  0 273 VAL BBB CA    1 ? 2 
ATOM   5709  C C     . VAL B 1 273 ? 65.963  -7.583  1.066   1.000 61.621  0 273 VAL BBB C     1 ? 2 
ATOM   5710  O O     . VAL B 1 273 ? 65.140  -6.671  1.370   1.000 57.550  0 273 VAL BBB O     1 ? 2 
ATOM   5711  C CB    . VAL B 1 273 ? 64.812  -8.039  -1.182  1.000 61.279  0 273 VAL BBB CB    1 ? 2 
ATOM   5712  C CG1   . VAL B 1 273 ? 65.465  -6.785  -1.747  1.000 60.934  0 273 VAL BBB CG1   1 ? 2 
ATOM   5713  C CG2   . VAL B 1 273 ? 64.653  -9.083  -2.282  1.000 62.250  0 273 VAL BBB CG2   1 ? 2 
ATOM   5714  N N     . ASN B 1 274 ? 67.172  -7.760  1.611   1.000 63.902  0 274 ASN BBB N     1 ? 2 
ATOM   5715  C CA    . ASN B 1 274 ? 67.747  -6.966  2.719   1.000 66.338  0 274 ASN BBB CA    1 ? 2 
ATOM   5716  C C     . ASN B 1 274 ? 66.910  -7.237  3.980   1.000 61.283  0 274 ASN BBB C     1 ? 2 
ATOM   5717  O O     . ASN B 1 274 ? 66.868  -8.424  4.415   1.000 56.592  0 274 ASN BBB O     1 ? 2 
ATOM   5718  C CB    . ASN B 1 274 ? 67.872  -5.505  2.297   1.000 70.450  0 274 ASN BBB CB    1 ? 2 
ATOM   5719  C CG    . ASN B 1 274 ? 68.836  -5.284  1.138   1.000 75.165  0 274 ASN BBB CG    1 ? 2 
ATOM   5720  O OD1   . ASN B 1 274 ? 68.443  -4.716  0.125   1.000 79.067  0 274 ASN BBB OD1   1 ? 2 
ATOM   5721  N ND2   . ASN B 1 274 ? 70.092  -5.709  1.258   1.000 73.447  0 274 ASN BBB ND2   1 ? 2 
ATOM   5722  N N     . GLU B 1 275 ? 66.240  -6.214  4.509   1.000 58.528  0 275 GLU BBB N     1 ? 2 
ATOM   5723  C CA    . GLU B 1 275 ? 65.483  -6.286  5.786   1.000 60.759  0 275 GLU BBB CA    1 ? 2 
ATOM   5724  C C     . GLU B 1 275 ? 63.999  -6.594  5.498   1.000 56.061  0 275 GLU BBB C     1 ? 2 
ATOM   5725  O O     . GLU B 1 275 ? 63.302  -6.920  6.443   1.000 49.064  0 275 GLU BBB O     1 ? 2 
ATOM   5726  C CB    . GLU B 1 275 ? 65.660  -4.989  6.590   1.000 64.406  0 275 GLU BBB CB    1 ? 2 
ATOM   5727  C CG    . GLU B 1 275 ? 65.052  -3.738  5.948   1.000 70.340  0 275 GLU BBB CG    1 ? 2 
ATOM   5728  C CD    . GLU B 1 275 ? 65.870  -3.016  4.876   1.000 75.469  0 275 GLU BBB CD    1 ? 2 
ATOM   5729  O OE1   . GLU B 1 275 ? 67.074  -3.318  4.759   1.000 78.327  0 275 GLU BBB OE1   1 ? 2 
ATOM   5730  O OE2   . GLU B 1 275 ? 65.293  -2.172  4.149   1.000 77.211  0 275 GLU BBB OE2   1 ? 2 
ATOM   5731  N N     . ASN B 1 276 ? 63.557  -6.464  4.236   1.000 52.687  0 276 ASN BBB N     1 ? 2 
ATOM   5732  C CA    . ASN B 1 276 ? 62.150  -6.669  3.838   1.000 48.232  0 276 ASN BBB CA    1 ? 2 
ATOM   5733  C C     . ASN B 1 276 ? 62.003  -8.091  3.304   1.000 45.906  0 276 ASN BBB C     1 ? 2 
ATOM   5734  O O     . ASN B 1 276 ? 63.024  -8.765  3.034   1.000 46.712  0 276 ASN BBB O     1 ? 2 
ATOM   5735  C CB    . ASN B 1 276 ? 61.685  -5.645  2.801   1.000 49.958  0 276 ASN BBB CB    1 ? 2 
ATOM   5736  C CG    . ASN B 1 276 ? 61.443  -4.263  3.376   1.000 51.568  0 276 ASN BBB CG    1 ? 2 
ATOM   5737  O OD1   . ASN B 1 276 ? 61.109  -4.087  4.545   1.000 44.721  0 276 ASN BBB OD1   1 ? 2 
ATOM   5738  N ND2   . ASN B 1 276 ? 61.593  -3.256  2.538   1.000 56.055  0 276 ASN BBB ND2   1 ? 2 
ATOM   5739  N N     . ILE B 1 277 ? 60.745  -8.512  3.144   1.000 43.209  0 277 ILE BBB N     1 ? 2 
ATOM   5740  C CA    . ILE B 1 277 ? 60.357  -9.754  2.411   1.000 41.443  0 277 ILE BBB CA    1 ? 2 
ATOM   5741  C C     . ILE B 1 277 ? 59.666  -9.354  1.094   1.000 42.039  0 277 ILE BBB C     1 ? 2 
ATOM   5742  O O     . ILE B 1 277 ? 58.549  -8.806  1.147   1.000 40.736  0 277 ILE BBB O     1 ? 2 
ATOM   5743  C CB    . ILE B 1 277 ? 59.504  -10.670 3.306   1.000 37.476  0 277 ILE BBB CB    1 ? 2 
ATOM   5744  C CG1   . ILE B 1 277 ? 60.284  -11.044 4.567   1.000 37.383  0 277 ILE BBB CG1   1 ? 2 
ATOM   5745  C CG2   . ILE B 1 277 ? 59.021  -11.882 2.529   1.000 36.597  0 277 ILE BBB CG2   1 ? 2 
ATOM   5746  C CD1   . ILE B 1 277 ? 59.475  -11.598 5.684   1.000 36.802  0 277 ILE BBB CD1   1 ? 2 
ATOM   5747  N N     . LYS B 1 278 ? 60.354  -9.598  -0.026  1.000 41.866  0 278 LYS BBB N     1 ? 2 
ATOM   5748  C CA    . LYS B 1 278 ? 59.826  -9.479  -1.407  1.000 42.440  0 278 LYS BBB CA    1 ? 2 
ATOM   5749  C C     . LYS B 1 278 ? 58.951  -10.703 -1.676  1.000 37.537  0 278 LYS BBB C     1 ? 2 
ATOM   5750  O O     . LYS B 1 278 ? 59.467  -11.825 -1.645  1.000 35.409  0 278 LYS BBB O     1 ? 2 
ATOM   5751  C CB    . LYS B 1 278 ? 60.989  -9.380  -2.407  1.000 46.904  0 278 LYS BBB CB    1 ? 2 
ATOM   5752  C CG    . LYS B 1 278 ? 60.618  -8.959  -3.824  1.000 50.151  0 278 LYS BBB CG    1 ? 2 
ATOM   5753  C CD    . LYS B 1 278 ? 61.781  -9.052  -4.805  1.000 54.056  0 278 LYS BBB CD    1 ? 2 
ATOM   5754  C CE    . LYS B 1 278 ? 61.382  -8.733  -6.233  1.000 58.403  0 278 LYS BBB CE    1 ? 2 
ATOM   5755  N NZ    . LYS B 1 278 ? 62.388  -9.182  -7.227  1.000 59.553  0 278 LYS BBB NZ    1 ? 2 
ATOM   5756  N N     . VAL B 1 279 ? 57.664  -10.484 -1.900  1.000 35.701  0 279 VAL BBB N     1 ? 2 
ATOM   5757  C CA    . VAL B 1 279 ? 56.691  -11.568 -2.211  1.000 36.011  0 279 VAL BBB CA    1 ? 2 
ATOM   5758  C C     . VAL B 1 279 ? 56.315  -11.467 -3.690  1.000 36.664  0 279 VAL BBB C     1 ? 2 
ATOM   5759  O O     . VAL B 1 279 ? 55.941  -10.377 -4.148  1.000 34.408  0 279 VAL BBB O     1 ? 2 
ATOM   5760  C CB    . VAL B 1 279 ? 55.465  -11.483 -1.282  1.000 35.710  0 279 VAL BBB CB    1 ? 2 
ATOM   5761  C CG1   . VAL B 1 279 ? 54.314  -12.362 -1.756  1.000 35.393  0 279 VAL BBB CG1   1 ? 2 
ATOM   5762  C CG2   . VAL B 1 279 ? 55.865  -11.818 0.139   1.000 34.942  0 279 VAL BBB CG2   1 ? 2 
ATOM   5763  N N     . SER B 1 280 ? 56.460  -12.566 -4.420  1.000 38.940  0 280 SER BBB N     1 ? 2 
ATOM   5764  C CA    . SER B 1 280 ? 56.061  -12.653 -5.847  1.000 39.856  0 280 SER BBB CA    1 ? 2 
ATOM   5765  C C     . SER B 1 280 ? 54.710  -13.365 -5.903  1.000 40.801  0 280 SER BBB C     1 ? 2 
ATOM   5766  O O     . SER B 1 280 ? 54.586  -14.441 -5.310  1.000 38.538  0 280 SER BBB O     1 ? 2 
ATOM   5767  C CB    . SER B 1 280 ? 57.127  -13.308 -6.672  1.000 39.869  0 280 SER BBB CB    1 ? 2 
ATOM   5768  O OG    . SER B 1 280 ? 58.224  -12.419 -6.823  1.000 38.919  0 280 SER BBB OG    1 ? 2 
ATOM   5769  N N     . PHE B 1 281 ? 53.729  -12.735 -6.535  1.000 44.462  0 281 PHE BBB N     1 ? 2 
ATOM   5770  C CA    . PHE B 1 281 ? 52.318  -13.184 -6.562  1.000 47.498  0 281 PHE BBB CA    1 ? 2 
ATOM   5771  C C     . PHE B 1 281 ? 51.995  -13.895 -7.884  1.000 52.073  0 281 PHE BBB C     1 ? 2 
ATOM   5772  O O     . PHE B 1 281 ? 52.639  -13.646 -8.912  1.000 50.995  0 281 PHE BBB O     1 ? 2 
ATOM   5773  C CB    . PHE B 1 281 ? 51.397  -11.993 -6.339  1.000 49.074  0 281 PHE BBB CB    1 ? 2 
ATOM   5774  C CG    . PHE B 1 281 ? 51.391  -11.466 -4.930  1.000 49.058  0 281 PHE BBB CG    1 ? 2 
ATOM   5775  C CD1   . PHE B 1 281 ? 50.703  -12.141 -3.925  1.000 48.211  0 281 PHE BBB CD1   1 ? 2 
ATOM   5776  C CD2   . PHE B 1 281 ? 52.099  -10.321 -4.602  1.000 50.520  0 281 PHE BBB CD2   1 ? 2 
ATOM   5777  C CE1   . PHE B 1 281 ? 50.677  -11.649 -2.629  1.000 46.909  0 281 PHE BBB CE1   1 ? 2 
ATOM   5778  C CE2   . PHE B 1 281 ? 52.078  -9.838  -3.293  1.000 52.679  0 281 PHE BBB CE2   1 ? 2 
ATOM   5779  C CZ    . PHE B 1 281 ? 51.358  -10.499 -2.312  1.000 48.305  0 281 PHE BBB CZ    1 ? 2 
ATOM   5780  N N     . SER B 1 282 ? 50.971  -14.753 -7.833  1.000 57.162  0 282 SER BBB N     1 ? 2 
ATOM   5781  C CA    . SER B 1 282 ? 50.510  -15.642 -8.937  1.000 58.593  0 282 SER BBB CA    1 ? 2 
ATOM   5782  C C     . SER B 1 282 ? 49.997  -14.812 -10.131 1.000 58.294  0 282 SER BBB C     1 ? 2 
ATOM   5783  O O     . SER B 1 282 ? 49.865  -15.399 -11.211 1.000 62.209  0 282 SER BBB O     1 ? 2 
ATOM   5784  C CB    . SER B 1 282 ? 49.460  -16.597 -8.445  1.000 56.435  0 282 SER BBB CB    1 ? 2 
ATOM   5785  O OG    . SER B 1 282 ? 48.254  -15.917 -8.193  1.000 55.610  0 282 SER BBB OG    1 ? 2 
ATOM   5786  N N     . ASP B 1 283 ? 49.714  -13.514 -9.959  1.000 57.381  0 283 ASP BBB N     1 ? 2 
ATOM   5787  C CA    . ASP B 1 283 ? 49.305  -12.613 -11.074 1.000 58.302  0 283 ASP BBB CA    1 ? 2 
ATOM   5788  C C     . ASP B 1 283 ? 50.533  -11.895 -11.679 1.000 60.833  0 283 ASP BBB C     1 ? 2 
ATOM   5789  O O     . ASP B 1 283 ? 50.329  -10.952 -12.479 1.000 59.440  0 283 ASP BBB O     1 ? 2 
ATOM   5790  C CB    . ASP B 1 283 ? 48.209  -11.632 -10.632 1.000 56.928  0 283 ASP BBB CB    1 ? 2 
ATOM   5791  C CG    . ASP B 1 283 ? 48.653  -10.531 -9.667  1.000 57.117  0 283 ASP BBB CG    1 ? 2 
ATOM   5792  O OD1   . ASP B 1 283 ? 49.783  -10.656 -9.094  1.000 57.880  0 283 ASP BBB OD1   1 ? 2 
ATOM   5793  O OD2   . ASP B 1 283 ? 47.861  -9.546  -9.487  1.000 49.933  0 283 ASP BBB OD2   1 ? 2 
ATOM   5794  N N     . GLY B 1 284 ? 51.761  -12.310 -11.325 1.000 61.746  0 284 GLY BBB N     1 ? 2 
ATOM   5795  C CA    . GLY B 1 284 ? 53.019  -11.727 -11.828 1.000 60.585  0 284 GLY BBB CA    1 ? 2 
ATOM   5796  C C     . GLY B 1 284 ? 53.386  -10.418 -11.130 1.000 60.616  0 284 GLY BBB C     1 ? 2 
ATOM   5797  O O     . GLY B 1 284 ? 54.415  -9.828  -11.514 1.000 58.283  0 284 GLY BBB O     1 ? 2 
ATOM   5798  N N     . SER B 1 285 ? 52.616  -9.968  -10.128 1.000 58.502  0 285 SER BBB N     1 ? 2 
ATOM   5799  C CA    . SER B 1 285 ? 52.931  -8.728  -9.373  1.000 57.783  0 285 SER BBB CA    1 ? 2 
ATOM   5800  C C     . SER B 1 285 ? 53.912  -9.066  -8.244  1.000 53.561  0 285 SER BBB C     1 ? 2 
ATOM   5801  O O     . SER B 1 285 ? 54.014  -10.243 -7.843  1.000 49.091  0 285 SER BBB O     1 ? 2 
ATOM   5802  C CB    . SER B 1 285 ? 51.679  -8.018  -8.878  1.000 57.126  0 285 SER BBB CB    1 ? 2 
ATOM   5803  O OG    . SER B 1 285 ? 51.096  -8.720  -7.797  1.000 58.116  0 285 SER BBB OG    1 ? 2 
ATOM   5804  N N     . VAL B 1 286 ? 54.622  -8.043  -7.771  1.000 53.061  0 286 VAL BBB N     1 ? 2 
ATOM   5805  C CA    . VAL B 1 286 ? 55.635  -8.123  -6.685  1.000 52.571  0 286 VAL BBB CA    1 ? 2 
ATOM   5806  C C     . VAL B 1 286 ? 55.291  -7.050  -5.634  1.000 51.491  0 286 VAL BBB C     1 ? 2 
ATOM   5807  O O     . VAL B 1 286 ? 54.724  -6.009  -6.016  1.000 50.734  0 286 VAL BBB O     1 ? 2 
ATOM   5808  C CB    . VAL B 1 286 ? 57.038  -7.961  -7.298  1.000 55.973  0 286 VAL BBB CB    1 ? 2 
ATOM   5809  C CG1   . VAL B 1 286 ? 58.107  -7.719  -6.256  1.000 58.178  0 286 VAL BBB CG1   1 ? 2 
ATOM   5810  C CG2   . VAL B 1 286 ? 57.418  -9.138  -8.186  1.000 55.891  0 286 VAL BBB CG2   1 ? 2 
ATOM   5811  N N     . GLU B 1 287 ? 55.549  -7.314  -4.344  1.000 49.067  0 287 GLU BBB N     1 ? 2 
ATOM   5812  C CA    . GLU B 1 287 ? 55.385  -6.297  -3.266  1.000 47.565  0 287 GLU BBB CA    1 ? 2 
ATOM   5813  C C     . GLU B 1 287 ? 56.262  -6.665  -2.065  1.000 45.635  0 287 GLU BBB C     1 ? 2 
ATOM   5814  O O     . GLU B 1 287 ? 56.421  -7.867  -1.782  1.000 41.965  0 287 GLU BBB O     1 ? 2 
ATOM   5815  C CB    . GLU B 1 287 ? 53.913  -6.155  -2.874  1.000 49.139  0 287 GLU BBB CB    1 ? 2 
ATOM   5816  C CG    . GLU B 1 287 ? 53.589  -4.852  -2.167  1.000 49.754  0 287 GLU BBB CG    1 ? 2 
ATOM   5817  C CD    . GLU B 1 287 ? 52.120  -4.641  -1.823  1.000 51.057  0 287 GLU BBB CD    1 ? 2 
ATOM   5818  O OE1   . GLU B 1 287 ? 51.312  -5.580  -2.077  1.000 53.216  0 287 GLU BBB OE1   1 ? 2 
ATOM   5819  O OE2   . GLU B 1 287 ? 51.790  -3.553  -1.250  1.000 47.337  0 287 GLU BBB OE2   1 ? 2 
ATOM   5820  N N     . GLU B 1 288 ? 56.819  -5.650  -1.403  1.000 46.056  0 288 GLU BBB N     1 ? 2 
ATOM   5821  C CA    . GLU B 1 288 ? 57.687  -5.810  -0.199  1.000 46.044  0 288 GLU BBB CA    1 ? 2 
ATOM   5822  C C     . GLU B 1 288 ? 56.826  -5.691  1.068   1.000 41.822  0 288 GLU BBB C     1 ? 2 
ATOM   5823  O O     . GLU B 1 288 ? 55.909  -4.855  1.096   1.000 40.623  0 288 GLU BBB O     1 ? 2 
ATOM   5824  C CB    . GLU B 1 288 ? 58.893  -4.864  -0.264  1.000 46.673  0 288 GLU BBB CB    1 ? 2 
ATOM   5825  C CG    . GLU B 1 288 ? 59.839  -5.256  -1.403  1.000 49.023  0 288 GLU BBB CG    1 ? 2 
ATOM   5826  C CD    . GLU B 1 288 ? 61.273  -4.750  -1.370  1.000 49.252  0 288 GLU BBB CD    1 ? 2 
ATOM   5827  O OE1   . GLU B 1 288 ? 61.750  -4.318  -0.309  1.000 46.748  0 288 GLU BBB OE1   1 ? 2 
ATOM   5828  O OE2   . GLU B 1 288 ? 61.915  -4.832  -2.424  1.000 55.194  0 288 GLU BBB OE2   1 ? 2 
ATOM   5829  N N     . PHE B 1 289 ? 57.089  -6.543  2.053   1.000 39.441  0 289 PHE BBB N     1 ? 2 
ATOM   5830  C CA    . PHE B 1 289 ? 56.456  -6.517  3.396   1.000 40.027  0 289 PHE BBB CA    1 ? 2 
ATOM   5831  C C     . PHE B 1 289 ? 57.526  -6.706  4.471   1.000 38.420  0 289 PHE BBB C     1 ? 2 
ATOM   5832  O O     . PHE B 1 289 ? 58.548  -7.307  4.167   1.000 36.758  0 289 PHE BBB O     1 ? 2 
ATOM   5833  C CB    . PHE B 1 289 ? 55.381  -7.607  3.521   1.000 39.679  0 289 PHE BBB CB    1 ? 2 
ATOM   5834  C CG    . PHE B 1 289 ? 54.340  -7.596  2.436   1.000 39.394  0 289 PHE BBB CG    1 ? 2 
ATOM   5835  C CD1   . PHE B 1 289 ? 54.555  -8.265  1.246   1.000 39.510  0 289 PHE BBB CD1   1 ? 2 
ATOM   5836  C CD2   . PHE B 1 289 ? 53.157  -6.906  2.611   1.000 40.042  0 289 PHE BBB CD2   1 ? 2 
ATOM   5837  C CE1   . PHE B 1 289 ? 53.606  -8.241  0.242   1.000 41.865  0 289 PHE BBB CE1   1 ? 2 
ATOM   5838  C CE2   . PHE B 1 289 ? 52.198  -6.896  1.612   1.000 41.533  0 289 PHE BBB CE2   1 ? 2 
ATOM   5839  C CZ    . PHE B 1 289 ? 52.424  -7.563  0.428   1.000 41.655  0 289 PHE BBB CZ    1 ? 2 
ATOM   5840  N N     . GLU B 1 290 ? 57.250  -6.241  5.690   1.000 38.800  0 290 GLU BBB N     1 ? 2 
ATOM   5841  C CA    . GLU B 1 290 ? 58.090  -6.531  6.876   1.000 38.678  0 290 GLU BBB CA    1 ? 2 
ATOM   5842  C C     . GLU B 1 290 ? 57.766  -7.924  7.430   1.000 36.573  0 290 GLU BBB C     1 ? 2 
ATOM   5843  O O     . GLU B 1 290 ? 58.694  -8.615  7.880   1.000 35.926  0 290 GLU BBB O     1 ? 2 
ATOM   5844  C CB    . GLU B 1 290 ? 57.887  -5.444  7.918   1.000 40.605  0 290 GLU BBB CB    1 ? 2 
ATOM   5845  C CG    . GLU B 1 290 ? 58.935  -5.527  9.010   1.000 44.243  0 290 GLU BBB CG    1 ? 2 
ATOM   5846  C CD    . GLU B 1 290 ? 58.989  -4.376  9.981   1.000 46.831  0 290 GLU BBB CD    1 ? 2 
ATOM   5847  O OE1   . GLU B 1 290 ? 59.318  -4.658  11.155  1.000 47.919  0 290 GLU BBB OE1   1 ? 2 
ATOM   5848  O OE2   . GLU B 1 290 ? 58.683  -3.226  9.556   1.000 50.316  0 290 GLU BBB OE2   1 ? 2 
ATOM   5849  N N     . THR B 1 291 ? 56.497  -8.340  7.369   1.000 35.492  0 291 THR BBB N     1 ? 2 
ATOM   5850  C CA    . THR B 1 291 ? 55.983  -9.584  7.985   1.000 32.733  0 291 THR BBB CA    1 ? 2 
ATOM   5851  C C     . THR B 1 291 ? 55.050  -10.278 6.991   1.000 32.475  0 291 THR BBB C     1 ? 2 
ATOM   5852  O O     . THR B 1 291 ? 54.175  -9.603  6.392   1.000 33.039  0 291 THR BBB O     1 ? 2 
ATOM   5853  C CB    . THR B 1 291 ? 55.235  -9.279  9.298   1.000 32.659  0 291 THR BBB CB    1 ? 2 
ATOM   5854  O OG1   . THR B 1 291 ? 56.085  -8.581  10.210  1.000 30.848  0 291 THR BBB OG1   1 ? 2 
ATOM   5855  C CG2   . THR B 1 291 ? 54.711  -10.521 9.987   1.000 31.336  0 291 THR BBB CG2   1 ? 2 
ATOM   5856  N N     . VAL B 1 292 ? 55.183  -11.594 6.871   1.000 30.390  0 292 VAL BBB N     1 ? 2 
ATOM   5857  C CA    . VAL B 1 292 ? 54.269  -12.439 6.076   1.000 28.770  0 292 VAL BBB CA    1 ? 2 
ATOM   5858  C C     . VAL B 1 292 ? 53.763  -13.545 6.994   1.000 28.147  0 292 VAL BBB C     1 ? 2 
ATOM   5859  O O     . VAL B 1 292 ? 54.582  -14.288 7.551   1.000 26.658  0 292 VAL BBB O     1 ? 2 
ATOM   5860  C CB    . VAL B 1 292 ? 54.955  -13.015 4.820   1.000 29.052  0 292 VAL BBB CB    1 ? 2 
ATOM   5861  C CG1   . VAL B 1 292 ? 54.054  -14.022 4.084   1.000 27.919  0 292 VAL BBB CG1   1 ? 2 
ATOM   5862  C CG2   . VAL B 1 292 ? 55.407  -11.893 3.867   1.000 29.176  0 292 VAL BBB CG2   1 ? 2 
ATOM   5863  N N     . LEU B 1 293 ? 52.439  -13.668 7.091   1.000 27.975  0 293 LEU BBB N     1 ? 2 
ATOM   5864  C CA    . LEU B 1 293 ? 51.742  -14.616 7.977   1.000 27.698  0 293 LEU BBB CA    1 ? 2 
ATOM   5865  C C     . LEU B 1 293 ? 50.872  -15.527 7.139   1.000 29.240  0 293 LEU BBB C     1 ? 2 
ATOM   5866  O O     . LEU B 1 293 ? 49.986  -14.983 6.443   1.000 31.842  0 293 LEU BBB O     1 ? 2 
ATOM   5867  C CB    . LEU B 1 293 ? 50.874  -13.827 8.959   1.000 27.250  0 293 LEU BBB CB    1 ? 2 
ATOM   5868  C CG    . LEU B 1 293 ? 50.340  -14.628 10.141  1.000 26.405  0 293 LEU BBB CG    1 ? 2 
ATOM   5869  C CD1   . LEU B 1 293 ? 50.161  -13.712 11.352  1.000 26.105  0 293 LEU BBB CD1   1 ? 2 
ATOM   5870  C CD2   . LEU B 1 293 ? 49.043  -15.322 9.771   1.000 26.639  0 293 LEU BBB CD2   1 ? 2 
ATOM   5871  N N     . TYR B 1 294 ? 51.082  -16.840 7.242   1.000 30.306  0 294 TYR BBB N     1 ? 2 
ATOM   5872  C CA    . TYR B 1 294 ? 50.235  -17.857 6.579   1.000 31.684  0 294 TYR BBB CA    1 ? 2 
ATOM   5873  C C     . TYR B 1 294 ? 49.077  -18.248 7.505   1.000 31.028  0 294 TYR BBB C     1 ? 2 
ATOM   5874  O O     . TYR B 1 294 ? 49.350  -18.861 8.565   1.000 28.275  0 294 TYR BBB O     1 ? 2 
ATOM   5875  C CB    . TYR B 1 294 ? 51.044  -19.081 6.138   1.000 32.953  0 294 TYR BBB CB    1 ? 2 
ATOM   5876  C CG    . TYR B 1 294 ? 51.549  -18.952 4.726   1.000 35.475  0 294 TYR BBB CG    1 ? 2 
ATOM   5877  C CD1   . TYR B 1 294 ? 50.723  -19.224 3.648   1.000 36.530  0 294 TYR BBB CD1   1 ? 2 
ATOM   5878  C CD2   . TYR B 1 294 ? 52.840  -18.516 4.463   1.000 37.123  0 294 TYR BBB CD2   1 ? 2 
ATOM   5879  C CE1   . TYR B 1 294 ? 51.159  -19.096 2.342   1.000 37.758  0 294 TYR BBB CE1   1 ? 2 
ATOM   5880  C CE2   . TYR B 1 294 ? 53.285  -18.340 3.168   1.000 38.591  0 294 TYR BBB CE2   1 ? 2 
ATOM   5881  C CZ    . TYR B 1 294 ? 52.457  -18.662 2.099   1.000 40.070  0 294 TYR BBB CZ    1 ? 2 
ATOM   5882  O OH    . TYR B 1 294 ? 52.924  -18.528 0.817   1.000 40.852  0 294 TYR BBB OH    1 ? 2 
ATOM   5883  N N     . ALA B 1 295 ? 47.841  -17.967 7.071   1.000 30.741  0 295 ALA BBB N     1 ? 2 
ATOM   5884  C CA    . ALA B 1 295 ? 46.608  -18.448 7.738   1.000 33.071  0 295 ALA BBB CA    1 ? 2 
ATOM   5885  C C     . ALA B 1 295 ? 45.782  -19.258 6.748   1.000 33.520  0 295 ALA BBB C     1 ? 2 
ATOM   5886  O O     . ALA B 1 295 ? 44.592  -18.976 6.533   1.000 32.638  0 295 ALA BBB O     1 ? 2 
ATOM   5887  C CB    . ALA B 1 295 ? 45.828  -17.284 8.294   1.000 33.101  0 295 ALA BBB CB    1 ? 2 
ATOM   5888  N N     . THR B 1 296 ? 46.411  -20.267 6.168   1.000 36.336  0 296 THR BBB N     1 ? 2 
ATOM   5889  C CA    . THR B 1 296 ? 45.853  -21.007 5.006   1.000 37.896  0 296 THR BBB CA    1 ? 2 
ATOM   5890  C C     . THR B 1 296 ? 45.128  -22.247 5.528   1.000 38.673  0 296 THR BBB C     1 ? 2 
ATOM   5891  O O     . THR B 1 296 ? 44.335  -22.847 4.770   1.000 42.327  0 296 THR BBB O     1 ? 2 
ATOM   5892  C CB    . THR B 1 296 ? 46.958  -21.288 3.981   1.000 38.092  0 296 THR BBB CB    1 ? 2 
ATOM   5893  O OG1   . THR B 1 296 ? 48.169  -21.652 4.663   1.000 34.708  0 296 THR BBB OG1   1 ? 2 
ATOM   5894  C CG2   . THR B 1 296 ? 47.150  -20.089 3.077   1.000 39.682  0 296 THR BBB CG2   1 ? 2 
ATOM   5895  N N     . GLY B 1 297 ? 45.439  -22.633 6.762   1.000 37.648  0 297 GLY BBB N     1 ? 2 
ATOM   5896  C CA    . GLY B 1 297 ? 44.768  -23.719 7.484   1.000 35.741  0 297 GLY BBB CA    1 ? 2 
ATOM   5897  C C     . GLY B 1 297 ? 45.691  -24.313 8.513   1.000 34.782  0 297 GLY BBB C     1 ? 2 
ATOM   5898  O O     . GLY B 1 297 ? 46.773  -23.719 8.800   1.000 35.655  0 297 GLY BBB O     1 ? 2 
ATOM   5899  N N     . ARG B 1 298 ? 45.311  -25.489 9.003   1.000 34.429  0 298 ARG BBB N     1 ? 2 
ATOM   5900  C CA    . ARG B 1 298 ? 46.027  -26.247 10.060  1.000 34.968  0 298 ARG BBB CA    1 ? 2 
ATOM   5901  C C     . ARG B 1 298 ? 45.974  -27.735 9.725   1.000 34.933  0 298 ARG BBB C     1 ? 2 
ATOM   5902  O O     . ARG B 1 298 ? 44.911  -28.178 9.270   1.000 35.251  0 298 ARG BBB O     1 ? 2 
ATOM   5903  C CB    . ARG B 1 298 ? 45.340  -25.931 11.399  1.000 34.647  0 298 ARG BBB CB    1 ? 2 
ATOM   5904  C CG    . ARG B 1 298 ? 45.520  -24.489 11.875  1.000 32.563  0 298 ARG BBB CG    1 ? 2 
ATOM   5905  C CD    . ARG B 1 298 ? 44.580  -24.054 12.981  1.000 30.391  0 298 ARG BBB CD    1 ? 2 
ATOM   5906  N NE    . ARG B 1 298 ? 44.884  -24.765 14.208  1.000 29.283  0 298 ARG BBB NE    1 ? 2 
ATOM   5907  C CZ    . ARG B 1 298 ? 45.836  -24.476 15.083  1.000 29.231  0 298 ARG BBB CZ    1 ? 2 
ATOM   5908  N NH1   . ARG B 1 298 ? 46.674  -23.461 14.892  1.000 29.970  0 298 ARG BBB NH1   1 ? 2 
ATOM   5909  N NH2   . ARG B 1 298 ? 45.929  -25.219 16.174  1.000 29.460  0 298 ARG BBB NH2   1 ? 2 
ATOM   5910  N N     . ASN B 1 299 ? 47.048  -28.477 9.992   1.000 35.079  0 299 ASN BBB N     1 ? 2 
ATOM   5911  C CA    . ASN B 1 299 ? 47.078  -29.962 9.917   1.000 35.699  0 299 ASN BBB CA    1 ? 2 
ATOM   5912  C C     . ASN B 1 299 ? 47.012  -30.550 11.318  1.000 34.340  0 299 ASN BBB C     1 ? 2 
ATOM   5913  O O     . ASN B 1 299 ? 47.623  -30.015 12.250  1.000 34.697  0 299 ASN BBB O     1 ? 2 
ATOM   5914  C CB    . ASN B 1 299 ? 48.386  -30.470 9.289   1.000 37.660  0 299 ASN BBB CB    1 ? 2 
ATOM   5915  C CG    . ASN B 1 299 ? 48.489  -30.068 7.840   1.000 38.929  0 299 ASN BBB CG    1 ? 2 
ATOM   5916  O OD1   . ASN B 1 299 ? 49.497  -29.487 7.418   1.000 40.408  0 299 ASN BBB OD1   1 ? 2 
ATOM   5917  N ND2   . ASN B 1 299 ? 47.418  -30.321 7.109   1.000 38.609  0 299 ASN BBB ND2   1 ? 2 
ATOM   5918  N N     . PRO B 1 300 ? 46.317  -31.690 11.485  1.000 31.728  0 300 PRO BBB N     1 ? 2 
ATOM   5919  C CA    . PRO B 1 300 ? 46.263  -32.381 12.777  1.000 30.974  0 300 PRO BBB CA    1 ? 2 
ATOM   5920  C C     . PRO B 1 300 ? 47.638  -32.932 13.172  1.000 32.045  0 300 PRO BBB C     1 ? 2 
ATOM   5921  O O     . PRO B 1 300 ? 48.289  -33.535 12.361  1.000 31.533  0 300 PRO BBB O     1 ? 2 
ATOM   5922  C CB    . PRO B 1 300 ? 45.268  -33.515 12.528  1.000 30.196  0 300 PRO BBB CB    1 ? 2 
ATOM   5923  C CG    . PRO B 1 300 ? 45.354  -33.740 11.039  1.000 30.662  0 300 PRO BBB CG    1 ? 2 
ATOM   5924  C CD    . PRO B 1 300 ? 45.555  -32.370 10.426  1.000 30.825  0 300 PRO BBB CD    1 ? 2 
ATOM   5925  N N     . ASP B 1 301 ? 48.058  -32.680 14.399  1.000 34.926  0 301 ASP BBB N     1 ? 2 
ATOM   5926  C CA    . ASP B 1 301 ? 49.417  -33.024 14.885  1.000 37.539  0 301 ASP BBB CA    1 ? 2 
ATOM   5927  C C     . ASP B 1 301 ? 49.382  -34.467 15.413  1.000 37.364  0 301 ASP BBB C     1 ? 2 
ATOM   5928  O O     . ASP B 1 301 ? 49.298  -34.671 16.643  1.000 37.117  0 301 ASP BBB O     1 ? 2 
ATOM   5929  C CB    . ASP B 1 301 ? 49.887  -31.997 15.904  1.000 39.887  0 301 ASP BBB CB    1 ? 2 
ATOM   5930  C CG    . ASP B 1 301 ? 51.305  -32.213 16.367  1.000 44.347  0 301 ASP BBB CG    1 ? 2 
ATOM   5931  O OD1   . ASP B 1 301 ? 52.127  -32.687 15.534  1.000 53.045  0 301 ASP BBB OD1   1 ? 2 
ATOM   5932  O OD2   . ASP B 1 301 ? 51.567  -31.900 17.539  1.000 44.223  0 301 ASP BBB OD2   1 ? 2 
ATOM   5933  N N     . VAL B 1 302 ? 49.424  -35.426 14.497  1.000 37.726  0 302 VAL BBB N     1 ? 2 
ATOM   5934  C CA    . VAL B 1 302 ? 49.220  -36.871 14.785  1.000 39.592  0 302 VAL BBB CA    1 ? 2 
ATOM   5935  C C     . VAL B 1 302 ? 50.396  -37.708 14.267  1.000 42.233  0 302 VAL BBB C     1 ? 2 
ATOM   5936  O O     . VAL B 1 302 ? 50.406  -38.928 14.564  1.000 45.752  0 302 VAL BBB O     1 ? 2 
ATOM   5937  C CB    . VAL B 1 302 ? 47.875  -37.358 14.213  1.000 37.969  0 302 VAL BBB CB    1 ? 2 
ATOM   5938  C CG1   . VAL B 1 302 ? 46.701  -36.646 14.911  1.000 37.042  0 302 VAL BBB CG1   1 ? 2 
ATOM   5939  C CG2   . VAL B 1 302 ? 47.803  -37.197 12.708  1.000 36.986  0 302 VAL BBB CG2   1 ? 2 
ATOM   5940  N N     . LYS B 1 303 ? 51.358  -37.108 13.564  1.000 43.561  0 303 LYS BBB N     1 ? 2 
ATOM   5941  C CA    . LYS B 1 303 ? 52.444  -37.875 12.897  1.000 45.282  0 303 LYS BBB CA    1 ? 2 
ATOM   5942  C C     . LYS B 1 303 ? 53.311  -38.554 13.970  1.000 43.625  0 303 LYS BBB C     1 ? 2 
ATOM   5943  O O     . LYS B 1 303 ? 53.723  -39.707 13.750  1.000 46.103  0 303 LYS BBB O     1 ? 2 
ATOM   5944  C CB    . LYS B 1 303 ? 53.240  -36.975 11.940  1.000 46.851  0 303 LYS BBB CB    1 ? 2 
ATOM   5945  C CG    . LYS B 1 303 ? 52.462  -36.443 10.742  1.000 48.821  0 303 LYS BBB CG    1 ? 2 
ATOM   5946  C CD    . LYS B 1 303 ? 53.120  -35.181 10.125  1.000 50.229  0 303 LYS BBB CD    1 ? 2 
ATOM   5947  C CE    . LYS B 1 303 ? 52.721  -34.879 8.687   1.000 51.418  0 303 LYS BBB CE    1 ? 2 
ATOM   5948  N NZ    . LYS B 1 303 ? 53.821  -34.201 7.933   1.000 49.900  0 303 LYS BBB NZ    1 ? 2 
ATOM   5949  N N     . GLY B 1 304 ? 53.523  -37.913 15.120  1.000 42.001  0 304 GLY BBB N     1 ? 2 
ATOM   5950  C CA    . GLY B 1 304 ? 54.338  -38.476 16.214  1.000 41.292  0 304 GLY BBB CA    1 ? 2 
ATOM   5951  C C     . GLY B 1 304 ? 53.602  -39.534 17.026  1.000 41.524  0 304 GLY BBB C     1 ? 2 
ATOM   5952  O O     . GLY B 1 304 ? 54.194  -40.059 17.983  1.000 40.551  0 304 GLY BBB O     1 ? 2 
ATOM   5953  N N     . LEU B 1 305 ? 52.337  -39.848 16.708  1.000 40.957  0 305 LEU BBB N     1 ? 2 
ATOM   5954  C CA    . LEU B 1 305 ? 51.484  -40.675 17.608  1.000 41.377  0 305 LEU BBB CA    1 ? 2 
ATOM   5955  C C     . LEU B 1 305 ? 51.684  -42.171 17.366  1.000 41.765  0 305 LEU BBB C     1 ? 2 
ATOM   5956  O O     . LEU B 1 305 ? 51.283  -42.958 18.223  1.000 46.333  0 305 LEU BBB O     1 ? 2 
ATOM   5957  C CB    . LEU B 1 305 ? 50.022  -40.255 17.472  1.000 38.716  0 305 LEU BBB CB    1 ? 2 
ATOM   5958  C CG    . LEU B 1 305 ? 49.673  -38.927 18.138  1.000 39.487  0 305 LEU BBB CG    1 ? 2 
ATOM   5959  C CD1   . LEU B 1 305 ? 48.206  -38.572 17.901  1.000 40.638  0 305 LEU BBB CD1   1 ? 2 
ATOM   5960  C CD2   . LEU B 1 305 ? 49.980  -38.958 19.636  1.000 38.955  0 305 LEU BBB CD2   1 ? 2 
ATOM   5961  N N     . ASN B 1 306 ? 52.252  -42.546 16.230  1.000 43.215  0 306 ASN BBB N     1 ? 2 
ATOM   5962  C CA    . ASN B 1 306 ? 52.458  -43.950 15.799  1.000 42.768  0 306 ASN BBB CA    1 ? 2 
ATOM   5963  C C     . ASN B 1 306 ? 51.093  -44.584 15.522  1.000 42.181  0 306 ASN BBB C     1 ? 2 
ATOM   5964  O O     . ASN B 1 306 ? 50.898  -45.735 15.934  1.000 40.939  0 306 ASN BBB O     1 ? 2 
ATOM   5965  C CB    . ASN B 1 306 ? 53.272  -44.700 16.850  1.000 45.040  0 306 ASN BBB CB    1 ? 2 
ATOM   5966  C CG    . ASN B 1 306 ? 53.904  -45.973 16.320  1.000 47.947  0 306 ASN BBB CG    1 ? 2 
ATOM   5967  O OD1   . ASN B 1 306 ? 54.169  -46.088 15.123  1.000 52.976  0 306 ASN BBB OD1   1 ? 2 
ATOM   5968  N ND2   . ASN B 1 306 ? 54.124  -46.947 17.192  1.000 46.134  0 306 ASN BBB ND2   1 ? 2 
ATOM   5969  N N     . LEU B 1 307 ? 50.194  -43.864 14.835  1.000 41.018  0 307 LEU BBB N     1 ? 2 
ATOM   5970  C CA    . LEU B 1 307 ? 48.798  -44.294 14.562  1.000 42.308  0 307 LEU BBB CA    1 ? 2 
ATOM   5971  C C     . LEU B 1 307 ? 48.801  -45.464 13.569  1.000 45.628  0 307 LEU BBB C     1 ? 2 
ATOM   5972  O O     . LEU B 1 307 ? 48.035  -46.411 13.804  1.000 45.132  0 307 LEU BBB O     1 ? 2 
ATOM   5973  C CB    . LEU B 1 307 ? 47.974  -43.137 13.986  1.000 42.559  0 307 LEU BBB CB    1 ? 2 
ATOM   5974  C CG    . LEU B 1 307 ? 47.741  -41.924 14.886  1.000 42.050  0 307 LEU BBB CG    1 ? 2 
ATOM   5975  C CD1   . LEU B 1 307 ? 46.858  -40.905 14.203  1.000 42.491  0 307 LEU BBB CD1   1 ? 2 
ATOM   5976  C CD2   . LEU B 1 307 ? 47.155  -42.295 16.230  1.000 42.112  0 307 LEU BBB CD2   1 ? 2 
ATOM   5977  N N     . ASN B 1 308 ? 49.597  -45.395 12.499  1.000 47.651  0 308 ASN BBB N     1 ? 2 
ATOM   5978  C CA    . ASN B 1 308 ? 49.589  -46.395 11.389  1.000 51.053  0 308 ASN BBB CA    1 ? 2 
ATOM   5979  C C     . ASN B 1 308 ? 49.856  -47.787 11.967  1.000 49.207  0 308 ASN BBB C     1 ? 2 
ATOM   5980  O O     . ASN B 1 308 ? 49.057  -48.707 11.677  1.000 49.985  0 308 ASN BBB O     1 ? 2 
ATOM   5981  C CB    . ASN B 1 308 ? 50.615  -46.082 10.297  1.000 56.799  0 308 ASN BBB CB    1 ? 2 
ATOM   5982  C CG    . ASN B 1 308 ? 50.434  -46.912 9.041   1.000 63.737  0 308 ASN BBB CG    1 ? 2 
ATOM   5983  O OD1   . ASN B 1 308 ? 49.707  -47.903 9.038   1.000 61.284  0 308 ASN BBB OD1   1 ? 2 
ATOM   5984  N ND2   . ASN B 1 308 ? 51.132  -46.545 7.975   1.000 70.922  0 308 ASN BBB ND2   1 ? 2 
ATOM   5985  N N     . ALA B 1 309 ? 50.910  -47.919 12.774  1.000 46.429  0 309 ALA BBB N     1 ? 2 
ATOM   5986  C CA    . ALA B 1 309 ? 51.374  -49.203 13.347  1.000 45.494  0 309 ALA BBB CA    1 ? 2 
ATOM   5987  C C     . ALA B 1 309 ? 50.345  -49.783 14.338  1.000 43.871  0 309 ALA BBB C     1 ? 2 
ATOM   5988  O O     . ALA B 1 309 ? 50.300  -51.015 14.475  1.000 46.569  0 309 ALA BBB O     1 ? 2 
ATOM   5989  C CB    . ALA B 1 309 ? 52.743  -49.023 13.967  1.000 45.241  0 309 ALA BBB CB    1 ? 2 
ATOM   5990  N N     . ILE B 1 310 ? 49.529  -48.962 14.990  1.000 43.240  0 310 ILE BBB N     1 ? 2 
ATOM   5991  C CA    . ILE B 1 310 ? 48.557  -49.427 16.030  1.000 44.049  0 310 ILE BBB CA    1 ? 2 
ATOM   5992  C C     . ILE B 1 310 ? 47.210  -49.787 15.389  1.000 40.125  0 310 ILE BBB C     1 ? 2 
ATOM   5993  O O     . ILE B 1 310 ? 46.483  -50.534 16.008  1.000 38.689  0 310 ILE BBB O     1 ? 2 
ATOM   5994  C CB    . ILE B 1 310 ? 48.400  -48.383 17.156  1.000 45.587  0 310 ILE BBB CB    1 ? 2 
ATOM   5995  C CG1   . ILE B 1 310 ? 49.765  -48.020 17.755  1.000 46.991  0 310 ILE BBB CG1   1 ? 2 
ATOM   5996  C CG2   . ILE B 1 310 ? 47.429  -48.868 18.220  1.000 44.740  0 310 ILE BBB CG2   1 ? 2 
ATOM   5997  C CD1   . ILE B 1 310 ? 50.714  -49.205 17.993  1.000 47.150  0 310 ILE BBB CD1   1 ? 2 
ATOM   5998  N N     . GLY B 1 311 ? 46.936  -49.290 14.187  1.000 39.638  0 311 GLY BBB N     1 ? 2 
ATOM   5999  C CA    . GLY B 1 311 ? 45.683  -49.526 13.439  1.000 40.356  0 311 GLY BBB CA    1 ? 2 
ATOM   6000  C C     . GLY B 1 311 ? 44.642  -48.439 13.678  1.000 40.397  0 311 GLY BBB C     1 ? 2 
ATOM   6001  O O     . GLY B 1 311 ? 43.452  -48.744 13.545  1.000 41.845  0 311 GLY BBB O     1 ? 2 
ATOM   6002  N N     . VAL B 1 312 ? 45.039  -47.214 14.024  1.000 38.729  0 312 VAL BBB N     1 ? 2 
ATOM   6003  C CA    . VAL B 1 312 ? 44.088  -46.072 14.144  1.000 40.480  0 312 VAL BBB CA    1 ? 2 
ATOM   6004  C C     . VAL B 1 312 ? 43.908  -45.445 12.761  1.000 41.360  0 312 VAL BBB C     1 ? 2 
ATOM   6005  O O     . VAL B 1 312 ? 44.893  -44.858 12.246  1.000 41.831  0 312 VAL BBB O     1 ? 2 
ATOM   6006  C CB    . VAL B 1 312 ? 44.532  -45.012 15.169  1.000 40.591  0 312 VAL BBB CB    1 ? 2 
ATOM   6007  C CG1   . VAL B 1 312 ? 43.670  -43.752 15.049  1.000 39.346  0 312 VAL BBB CG1   1 ? 2 
ATOM   6008  C CG2   . VAL B 1 312 ? 44.519  -45.548 16.600  1.000 39.859  0 312 VAL BBB CG2   1 ? 2 
ATOM   6009  N N     . GLU B 1 313 ? 42.692  -45.526 12.216  1.000 42.349  0 313 GLU BBB N     1 ? 2 
ATOM   6010  C CA    . GLU B 1 313 ? 42.398  -45.103 10.822  1.000 44.430  0 313 GLU BBB CA    1 ? 2 
ATOM   6011  C C     . GLU B 1 313 ? 42.417  -43.572 10.718  1.000 42.770  0 313 GLU BBB C     1 ? 2 
ATOM   6012  O O     . GLU B 1 313 ? 41.870  -42.894 11.608  1.000 40.902  0 313 GLU BBB O     1 ? 2 
ATOM   6013  C CB    . GLU B 1 313 ? 41.077  -45.719 10.341  1.000 49.321  0 313 GLU BBB CB    1 ? 2 
ATOM   6014  C CG    . GLU B 1 313 ? 41.172  -47.241 10.168  1.000 56.900  0 313 GLU BBB CG    1 ? 2 
ATOM   6015  C CD    . GLU B 1 313 ? 40.052  -47.925 9.402   1.000 65.838  0 313 GLU BBB CD    1 ? 2 
ATOM   6016  O OE1   . GLU B 1 313 ? 40.387  -48.715 8.476   1.000 66.263  0 313 GLU BBB OE1   1 ? 2 
ATOM   6017  O OE2   . GLU B 1 313 ? 38.843  -47.676 9.742   1.000 76.703  0 313 GLU BBB OE2   1 ? 2 
ATOM   6018  N N     . VAL B 1 314 ? 42.980  -43.053 9.628   1.000 40.785  0 314 VAL BBB N     1 ? 2 
ATOM   6019  C CA    . VAL B 1 314 ? 43.000  -41.591 9.321   1.000 40.414  0 314 VAL BBB CA    1 ? 2 
ATOM   6020  C C     . VAL B 1 314 ? 42.354  -41.347 7.951   1.000 41.633  0 314 VAL BBB C     1 ? 2 
ATOM   6021  O O     . VAL B 1 314 ? 42.413  -42.242 7.098   1.000 39.983  0 314 VAL BBB O     1 ? 2 
ATOM   6022  C CB    . VAL B 1 314 ? 44.437  -41.028 9.406   1.000 39.504  0 314 VAL BBB CB    1 ? 2 
ATOM   6023  C CG1   . VAL B 1 314 ? 45.050  -41.245 10.795  1.000 37.265  0 314 VAL BBB CG1   1 ? 2 
ATOM   6024  C CG2   . VAL B 1 314 ? 45.350  -41.572 8.317   1.000 39.038  0 314 VAL BBB CG2   1 ? 2 
ATOM   6025  N N     . SER B 1 315 ? 41.734  -40.179 7.769   1.000 42.691  0 315 SER BBB N     1 ? 2 
ATOM   6026  C CA    . SER B 1 315 ? 41.109  -39.743 6.492   1.000 43.063  0 315 SER BBB CA    1 ? 2 
ATOM   6027  C C     . SER B 1 315 ? 42.205  -39.239 5.545   1.000 42.702  0 315 SER BBB C     1 ? 2 
ATOM   6028  O O     . SER B 1 315 ? 43.389  -39.246 5.923   1.000 40.963  0 315 SER BBB O     1 ? 2 
ATOM   6029  C CB    . SER B 1 315 ? 40.063  -38.676 6.727   1.000 42.772  0 315 SER BBB CB    1 ? 2 
ATOM   6030  O OG    . SER B 1 315 ? 40.705  -37.437 7.036   1.000 45.190  0 315 SER BBB OG    1 ? 2 
ATOM   6031  N N     . ASP B 1 316 ? 41.805  -38.808 4.356   1.000 44.975  0 316 ASP BBB N     1 ? 2 
ATOM   6032  C CA    . ASP B 1 316 ? 42.708  -38.302 3.287   1.000 48.643  0 316 ASP BBB CA    1 ? 2 
ATOM   6033  C C     . ASP B 1 316 ? 43.375  -37.011 3.786   1.000 50.237  0 316 ASP BBB C     1 ? 2 
ATOM   6034  O O     . ASP B 1 316 ? 44.507  -36.750 3.371   1.000 45.068  0 316 ASP BBB O     1 ? 2 
ATOM   6035  C CB    . ASP B 1 316 ? 41.951  -38.071 1.967   1.000 48.267  0 316 ASP BBB CB    1 ? 2 
ATOM   6036  C CG    . ASP B 1 316 ? 40.971  -39.167 1.555   1.000 46.505  0 316 ASP BBB CG    1 ? 2 
ATOM   6037  O OD1   . ASP B 1 316 ? 41.449  -40.293 1.386   1.000 43.785  0 316 ASP BBB OD1   1 ? 2 
ATOM   6038  O OD2   . ASP B 1 316 ? 39.714  -38.870 1.405   1.000 44.941  0 316 ASP BBB OD2   1 ? 2 
ATOM   6039  N N     . SER B 1 317 ? 42.711  -36.261 4.684   1.000 52.658  0 317 SER BBB N     1 ? 2 
ATOM   6040  C CA    . SER B 1 317 ? 43.229  -34.988 5.263   1.000 51.898  0 317 SER BBB CA    1 ? 2 
ATOM   6041  C C     . SER B 1 317 ? 44.226  -35.245 6.408   1.000 48.061  0 317 SER BBB C     1 ? 2 
ATOM   6042  O O     . SER B 1 317 ? 44.831  -34.255 6.876   1.000 41.822  0 317 SER BBB O     1 ? 2 
ATOM   6043  C CB    . SER B 1 317 ? 42.096  -34.104 5.723   1.000 52.982  0 317 SER BBB CB    1 ? 2 
ATOM   6044  O OG    . SER B 1 317 ? 41.412  -34.710 6.801   1.000 56.157  0 317 SER BBB OG    1 ? 2 
ATOM   6045  N N     . GLY B 1 318 ? 44.396  -36.504 6.838   1.000 45.893  0 318 GLY BBB N     1 ? 2 
ATOM   6046  C CA    . GLY B 1 318 ? 45.238  -36.876 7.995   1.000 43.912  0 318 GLY BBB CA    1 ? 2 
ATOM   6047  C C     . GLY B 1 318 ? 44.460  -36.863 9.312   1.000 41.412  0 318 GLY BBB C     1 ? 2 
ATOM   6048  O O     . GLY B 1 318 ? 45.061  -37.180 10.361  1.000 44.304  0 318 GLY BBB O     1 ? 2 
ATOM   6049  N N     . LYS B 1 319 ? 43.183  -36.493 9.307   1.000 36.710  0 319 LYS BBB N     1 ? 2 
ATOM   6050  C CA    . LYS B 1 319 ? 42.371  -36.438 10.544  1.000 37.061  0 319 LYS BBB CA    1 ? 2 
ATOM   6051  C C     . LYS B 1 319 ? 41.954  -37.864 10.954  1.000 38.031  0 319 LYS BBB C     1 ? 2 
ATOM   6052  O O     . LYS B 1 319 ? 41.766  -38.722 10.058  1.000 40.835  0 319 LYS BBB O     1 ? 2 
ATOM   6053  C CB    . LYS B 1 319 ? 41.173  -35.518 10.337  1.000 37.218  0 319 LYS BBB CB    1 ? 2 
ATOM   6054  C CG    . LYS B 1 319 ? 41.473  -34.027 10.409  1.000 37.884  0 319 LYS BBB CG    1 ? 2 
ATOM   6055  C CD    . LYS B 1 319 ? 40.268  -33.167 10.655  1.000 34.969  0 319 LYS BBB CD    1 ? 2 
ATOM   6056  C CE    . LYS B 1 319 ? 40.602  -31.697 10.811  1.000 34.282  0 319 LYS BBB CE    1 ? 2 
ATOM   6057  N NZ    . LYS B 1 319 ? 39.395  -30.878 11.152  1.000 34.408  0 319 LYS BBB NZ    1 ? 2 
ATOM   6058  N N     . ILE B 1 320 ? 41.850  -38.128 12.254  1.000 34.570  0 320 ILE BBB N     1 ? 2 
ATOM   6059  C CA    . ILE B 1 320 ? 41.406  -39.444 12.795  1.000 33.316  0 320 ILE BBB CA    1 ? 2 
ATOM   6060  C C     . ILE B 1 320 ? 39.912  -39.639 12.501  1.000 32.924  0 320 ILE BBB C     1 ? 2 
ATOM   6061  O O     . ILE B 1 320 ? 39.122  -38.683 12.729  1.000 32.706  0 320 ILE BBB O     1 ? 2 
ATOM   6062  C CB    . ILE B 1 320 ? 41.664  -39.511 14.304  1.000 33.701  0 320 ILE BBB CB    1 ? 2 
ATOM   6063  C CG1   . ILE B 1 320 ? 43.154  -39.332 14.604  1.000 33.754  0 320 ILE BBB CG1   1 ? 2 
ATOM   6064  C CG2   . ILE B 1 320 ? 41.083  -40.794 14.893  1.000 33.444  0 320 ILE BBB CG2   1 ? 2 
ATOM   6065  C CD1   . ILE B 1 320 ? 43.480  -39.365 16.070  1.000 34.307  0 320 ILE BBB CD1   1 ? 2 
ATOM   6066  N N     . ILE B 1 321 ? 39.549  -40.832 12.029  1.000 31.671  0 321 ILE BBB N     1 ? 2 
ATOM   6067  C CA    . ILE B 1 321 ? 38.141  -41.237 11.814  1.000 32.824  0 321 ILE BBB CA    1 ? 2 
ATOM   6068  C C     . ILE B 1 321 ? 37.593  -41.696 13.166  1.000 31.375  0 321 ILE BBB C     1 ? 2 
ATOM   6069  O O     . ILE B 1 321 ? 38.124  -42.661 13.714  1.000 30.234  0 321 ILE BBB O     1 ? 2 
ATOM   6070  C CB    . ILE B 1 321 ? 38.024  -42.293 10.688  1.000 34.491  0 321 ILE BBB CB    1 ? 2 
ATOM   6071  C CG1   . ILE B 1 321 ? 38.386  -41.699 9.323   1.000 35.343  0 321 ILE BBB CG1   1 ? 2 
ATOM   6072  C CG2   . ILE B 1 321 ? 36.639  -42.918 10.643  1.000 34.055  0 321 ILE BBB CG2   1 ? 2 
ATOM   6073  C CD1   . ILE B 1 321 ? 38.723  -42.757 8.272   1.000 35.909  0 321 ILE BBB CD1   1 ? 2 
ATOM   6074  N N     . ALA B 1 322 ? 36.642  -40.937 13.717  1.000 30.852  0 322 ALA BBB N     1 ? 2 
ATOM   6075  C CA    . ALA B 1 322 ? 36.013  -41.178 15.035  1.000 31.582  0 322 ALA BBB CA    1 ? 2 
ATOM   6076  C C     . ALA B 1 322 ? 34.710  -40.375 15.110  1.000 31.920  0 322 ALA BBB C     1 ? 2 
ATOM   6077  O O     . ALA B 1 322 ? 34.555  -39.478 15.943  1.000 28.847  0 322 ALA BBB O     1 ? 2 
ATOM   6078  C CB    . ALA B 1 322 ? 36.983  -40.804 16.130  1.000 30.594  0 322 ALA BBB CB    1 ? 2 
ATOM   6079  N N     . PRO B 1 323 ? 33.716  -40.687 14.242  1.000 34.465  0 323 PRO BBB N     1 ? 2 
ATOM   6080  C CA    . PRO B 1 323 ? 32.477  -39.909 14.182  1.000 35.151  0 323 PRO BBB CA    1 ? 2 
ATOM   6081  C C     . PRO B 1 323 ? 31.727  -39.926 15.519  1.000 33.779  0 323 PRO BBB C     1 ? 2 
ATOM   6082  O O     . PRO B 1 323 ? 30.978  -39.018 15.730  1.000 32.675  0 323 PRO BBB O     1 ? 2 
ATOM   6083  C CB    . PRO B 1 323 ? 31.650  -40.546 13.041  1.000 35.856  0 323 PRO BBB CB    1 ? 2 
ATOM   6084  C CG    . PRO B 1 323 ? 32.276  -41.908 12.805  1.000 35.740  0 323 PRO BBB CG    1 ? 2 
ATOM   6085  C CD    . PRO B 1 323 ? 33.714  -41.803 13.283  1.000 35.214  0 323 PRO BBB CD    1 ? 2 
ATOM   6086  N N     . LYS B 1 324 ? 31.992  -40.927 16.363  1.000 35.519  0 324 LYS BBB N     1 ? 2 
ATOM   6087  C CA    . LYS B 1 324 ? 31.416  -41.046 17.732  1.000 37.843  0 324 LYS BBB CA    1 ? 2 
ATOM   6088  C C     . LYS B 1 324 ? 32.510  -40.999 18.797  1.000 33.148  0 324 LYS BBB C     1 ? 2 
ATOM   6089  O O     . LYS B 1 324 ? 32.286  -41.557 19.859  1.000 30.816  0 324 LYS BBB O     1 ? 2 
ATOM   6090  C CB    . LYS B 1 324 ? 30.609  -42.352 17.853  1.000 42.838  0 324 LYS BBB CB    1 ? 2 
ATOM   6091  C CG    . LYS B 1 324 ? 29.322  -42.392 17.037  1.000 47.682  0 324 LYS BBB CG    1 ? 2 
ATOM   6092  C CD    . LYS B 1 324 ? 28.279  -41.400 17.509  1.000 52.190  0 324 LYS BBB CD    1 ? 2 
ATOM   6093  C CE    . LYS B 1 324 ? 26.851  -41.898 17.415  1.000 56.421  0 324 LYS BBB CE    1 ? 2 
ATOM   6094  N NZ    . LYS B 1 324 ? 25.965  -40.998 18.191  1.000 58.491  0 324 LYS BBB NZ    1 ? 2 
ATOM   6095  N N     . ASP B 1 325 ? 33.659  -40.383 18.497  1.000 33.110  0 325 ASP BBB N     1 ? 2 
ATOM   6096  C CA    . ASP B 1 325 ? 34.833  -40.271 19.411  1.000 31.748  0 325 ASP BBB CA    1 ? 2 
ATOM   6097  C C     . ASP B 1 325 ? 35.643  -41.589 19.430  1.000 33.261  0 325 ASP BBB C     1 ? 2 
ATOM   6098  O O     . ASP B 1 325 ? 36.844  -41.521 19.742  1.000 38.977  0 325 ASP BBB O     1 ? 2 
ATOM   6099  C CB    . ASP B 1 325 ? 34.419  -39.803 20.807  1.000 30.292  0 325 ASP BBB CB    1 ? 2 
ATOM   6100  C CG    . ASP B 1 325 ? 33.533  -38.542 20.836  1.000 30.346  0 325 ASP BBB CG    1 ? 2 
ATOM   6101  O OD1   . ASP B 1 325 ? 33.542  -37.715 19.886  1.000 32.146  0 325 ASP BBB OD1   1 ? 2 
ATOM   6102  O OD2   . ASP B 1 325 ? 32.831  -38.376 21.818  1.000 29.985  0 325 ASP BBB OD2   1 ? 2 
ATOM   6103  N N     . ALA B 1 326 ? 35.049  -42.727 19.091  1.000 33.506  0 326 ALA BBB N     1 ? 2 
ATOM   6104  C CA    . ALA B 1 326 ? 35.698  -44.058 19.063  1.000 34.621  0 326 ALA BBB CA    1 ? 2 
ATOM   6105  C C     . ALA B 1 326 ? 36.424  -44.235 17.722  1.000 34.649  0 326 ALA BBB C     1 ? 2 
ATOM   6106  O O     . ALA B 1 326 ? 35.778  -44.157 16.650  1.000 32.420  0 326 ALA BBB O     1 ? 2 
ATOM   6107  C CB    . ALA B 1 326 ? 34.684  -45.167 19.307  1.000 34.201  0 326 ALA BBB CB    1 ? 2 
ATOM   6108  N N     . THR B 1 327 ? 37.745  -44.444 17.779  1.000 35.523  0 327 THR BBB N     1 ? 2 
ATOM   6109  C CA    . THR B 1 327 ? 38.582  -44.775 16.598  1.000 34.580  0 327 THR BBB CA    1 ? 2 
ATOM   6110  C C     . THR B 1 327 ? 38.328  -46.222 16.159  1.000 35.026  0 327 THR BBB C     1 ? 2 
ATOM   6111  O O     . THR B 1 327 ? 37.532  -46.915 16.775  1.000 35.000  0 327 THR BBB O     1 ? 2 
ATOM   6112  C CB    . THR B 1 327 ? 40.075  -44.582 16.894  1.000 36.240  0 327 THR BBB CB    1 ? 2 
ATOM   6113  O OG1   . THR B 1 327 ? 40.522  -45.649 17.747  1.000 34.665  0 327 THR BBB OG1   1 ? 2 
ATOM   6114  C CG2   . THR B 1 327 ? 40.394  -43.219 17.478  1.000 36.141  0 327 THR BBB CG2   1 ? 2 
ATOM   6115  N N     . SER B 1 328 ? 39.027  -46.651 15.121  1.000 38.059  0 328 SER BBB N     1 ? 2 
ATOM   6116  C CA    . SER B 1 328 ? 39.054  -48.047 14.606  1.000 39.563  0 328 SER BBB CA    1 ? 2 
ATOM   6117  C C     . SER B 1 328 ? 39.663  -49.000 15.652  1.000 39.322  0 328 SER BBB C     1 ? 2 
ATOM   6118  O O     . SER B 1 328 ? 39.419  -50.214 15.528  1.000 43.405  0 328 SER BBB O     1 ? 2 
ATOM   6119  C CB    . SER B 1 328 ? 39.801  -48.113 13.290  1.000 38.263  0 328 SER BBB CB    1 ? 2 
ATOM   6120  O OG    . SER B 1 328 ? 41.070  -47.491 13.418  1.000 38.468  0 328 SER BBB OG    1 ? 2 
ATOM   6121  N N     . VAL B 1 329 ? 40.398  -48.485 16.640  1.000 36.809  0 329 VAL BBB N     1 ? 2 
ATOM   6122  C CA    . VAL B 1 329 ? 40.927  -49.269 17.805  1.000 37.050  0 329 VAL BBB CA    1 ? 2 
ATOM   6123  C C     . VAL B 1 329 ? 40.062  -48.987 19.040  1.000 36.601  0 329 VAL BBB C     1 ? 2 
ATOM   6124  O O     . VAL B 1 329 ? 40.008  -47.868 19.533  1.000 38.698  0 329 VAL BBB O     1 ? 2 
ATOM   6125  C CB    . VAL B 1 329 ? 42.425  -48.982 18.029  1.000 35.373  0 329 VAL BBB CB    1 ? 2 
ATOM   6126  C CG1   . VAL B 1 329 ? 42.940  -49.612 19.305  1.000 35.007  0 329 VAL BBB CG1   1 ? 2 
ATOM   6127  C CG2   . VAL B 1 329 ? 43.241  -49.475 16.837  1.000 35.191  0 329 VAL BBB CG2   1 ? 2 
ATOM   6128  N N     . PRO B 1 330 ? 39.342  -49.990 19.577  1.000 37.185  0 330 PRO BBB N     1 ? 2 
ATOM   6129  C CA    . PRO B 1 330 ? 38.219  -49.710 20.484  1.000 37.791  0 330 PRO BBB CA    1 ? 2 
ATOM   6130  C C     . PRO B 1 330 ? 38.551  -49.214 21.902  1.000 36.490  0 330 PRO BBB C     1 ? 2 
ATOM   6131  O O     . PRO B 1 330 ? 37.629  -48.765 22.581  1.000 34.962  0 330 PRO BBB O     1 ? 2 
ATOM   6132  C CB    . PRO B 1 330 ? 37.462  -51.043 20.557  1.000 39.087  0 330 PRO BBB CB    1 ? 2 
ATOM   6133  C CG    . PRO B 1 330 ? 38.472  -52.120 20.121  1.000 39.979  0 330 PRO BBB CG    1 ? 2 
ATOM   6134  C CD    . PRO B 1 330 ? 39.547  -51.420 19.317  1.000 37.959  0 330 PRO BBB CD    1 ? 2 
ATOM   6135  N N     . SER B 1 331 ? 39.831  -49.256 22.292  1.000 34.190  0 331 SER BBB N     1 ? 2 
ATOM   6136  C CA    . SER B 1 331 ? 40.362  -48.741 23.580  1.000 32.747  0 331 SER BBB CA    1 ? 2 
ATOM   6137  C C     . SER B 1 331 ? 40.843  -47.301 23.390  1.000 31.921  0 331 SER BBB C     1 ? 2 
ATOM   6138  O O     . SER B 1 331 ? 41.303  -46.660 24.387  1.000 30.760  0 331 SER BBB O     1 ? 2 
ATOM   6139  C CB    . SER B 1 331 ? 41.506  -49.620 24.049  1.000 33.816  0 331 SER BBB CB    1 ? 2 
ATOM   6140  O OG    . SER B 1 331 ? 42.566  -49.668 23.093  1.000 32.423  0 331 SER BBB OG    1 ? 2 
ATOM   6141  N N     . ILE B 1 332 ? 40.824  -46.809 22.143  1.000 30.454  0 332 ILE BBB N     1 ? 2 
ATOM   6142  C CA    . ILE B 1 332 ? 41.429  -45.493 21.794  1.000 28.897  0 332 ILE BBB CA    1 ? 2 
ATOM   6143  C C     . ILE B 1 332 ? 40.344  -44.570 21.241  1.000 27.949  0 332 ILE BBB C     1 ? 2 
ATOM   6144  O O     . ILE B 1 332 ? 39.709  -44.887 20.233  1.000 27.399  0 332 ILE BBB O     1 ? 2 
ATOM   6145  C CB    . ILE B 1 332 ? 42.611  -45.646 20.827  1.000 28.773  0 332 ILE BBB CB    1 ? 2 
ATOM   6146  C CG1   . ILE B 1 332 ? 43.754  -46.421 21.493  1.000 29.284  0 332 ILE BBB CG1   1 ? 2 
ATOM   6147  C CG2   . ILE B 1 332 ? 43.053  -44.282 20.335  1.000 27.907  0 332 ILE BBB CG2   1 ? 2 
ATOM   6148  C CD1   . ILE B 1 332 ? 44.991  -46.555 20.638  1.000 30.037  0 332 ILE BBB CD1   1 ? 2 
ATOM   6149  N N     . PHE B 1 333 ? 40.198  -43.429 21.899  1.000 27.343  0 333 PHE BBB N     1 ? 2 
ATOM   6150  C CA    . PHE B 1 333 ? 39.184  -42.390 21.616  1.000 27.865  0 333 PHE BBB CA    1 ? 2 
ATOM   6151  C C     . PHE B 1 333 ? 39.938  -41.160 21.123  1.000 27.991  0 333 PHE BBB C     1 ? 2 
ATOM   6152  O O     . PHE B 1 333 ? 41.162  -41.090 21.259  1.000 26.428  0 333 PHE BBB O     1 ? 2 
ATOM   6153  C CB    . PHE B 1 333 ? 38.317  -42.170 22.856  1.000 27.181  0 333 PHE BBB CB    1 ? 2 
ATOM   6154  C CG    . PHE B 1 333 ? 37.523  -43.396 23.225  1.000 27.252  0 333 PHE BBB CG    1 ? 2 
ATOM   6155  C CD1   . PHE B 1 333 ? 38.070  -44.396 24.014  1.000 27.373  0 333 PHE BBB CD1   1 ? 2 
ATOM   6156  C CD2   . PHE B 1 333 ? 36.247  -43.591 22.712  1.000 27.178  0 333 PHE BBB CD2   1 ? 2 
ATOM   6157  C CE1   . PHE B 1 333 ? 37.352  -45.555 24.279  1.000 28.062  0 333 PHE BBB CE1   1 ? 2 
ATOM   6158  C CE2   . PHE B 1 333 ? 35.520  -44.725 23.032  1.000 27.631  0 333 PHE BBB CE2   1 ? 2 
ATOM   6159  C CZ    . PHE B 1 333 ? 36.075  -45.719 23.795  1.000 27.262  0 333 PHE BBB CZ    1 ? 2 
ATOM   6160  N N     . ALA B 1 334 ? 39.201  -40.221 20.546  1.000 29.630  0 334 ALA BBB N     1 ? 2 
ATOM   6161  C CA    . ALA B 1 334 ? 39.752  -38.951 20.035  1.000 27.885  0 334 ALA BBB CA    1 ? 2 
ATOM   6162  C C     . ALA B 1 334 ? 38.671  -37.880 20.121  1.000 27.873  0 334 ALA BBB C     1 ? 2 
ATOM   6163  O O     . ALA B 1 334 ? 37.452  -38.229 19.963  1.000 28.488  0 334 ALA BBB O     1 ? 2 
ATOM   6164  C CB    . ALA B 1 334 ? 40.244  -39.159 18.631  1.000 28.463  0 334 ALA BBB CB    1 ? 2 
ATOM   6165  N N     . VAL B 1 335 ? 39.080  -36.643 20.416  1.000 26.116  0 335 VAL BBB N     1 ? 2 
ATOM   6166  C CA    . VAL B 1 335 ? 38.181  -35.450 20.393  1.000 26.014  0 335 VAL BBB CA    1 ? 2 
ATOM   6167  C C     . VAL B 1 335 ? 38.981  -34.262 19.884  1.000 24.680  0 335 VAL BBB C     1 ? 2 
ATOM   6168  O O     . VAL B 1 335 ? 40.200  -34.389 19.736  1.000 23.644  0 335 VAL BBB O     1 ? 2 
ATOM   6169  C CB    . VAL B 1 335 ? 37.573  -35.137 21.772  1.000 26.982  0 335 VAL BBB CB    1 ? 2 
ATOM   6170  C CG1   . VAL B 1 335 ? 36.730  -36.289 22.279  1.000 28.949  0 335 VAL BBB CG1   1 ? 2 
ATOM   6171  C CG2   . VAL B 1 335 ? 38.655  -34.750 22.778  1.000 26.963  0 335 VAL BBB CG2   1 ? 2 
ATOM   6172  N N     . GLY B 1 336 ? 38.270  -33.173 19.634  1.000 25.044  0 336 GLY BBB N     1 ? 2 
ATOM   6173  C CA    . GLY B 1 336 ? 38.820  -31.864 19.227  1.000 25.396  0 336 GLY BBB CA    1 ? 2 
ATOM   6174  C C     . GLY B 1 336 ? 39.199  -31.797 17.761  1.000 25.763  0 336 GLY BBB C     1 ? 2 
ATOM   6175  O O     . GLY B 1 336 ? 38.704  -32.609 16.967  1.000 25.533  0 336 GLY BBB O     1 ? 2 
ATOM   6176  N N     . ASP B 1 337 ? 40.124  -30.891 17.441  1.000 27.746  0 337 ASP BBB N     1 ? 2 
ATOM   6177  C CA    . ASP B 1 337 ? 40.502  -30.468 16.063  1.000 28.390  0 337 ASP BBB CA    1 ? 2 
ATOM   6178  C C     . ASP B 1 337 ? 41.024  -31.652 15.228  1.000 29.132  0 337 ASP BBB C     1 ? 2 
ATOM   6179  O O     . ASP B 1 337 ? 40.991  -31.527 13.967  1.000 29.830  0 337 ASP BBB O     1 ? 2 
ATOM   6180  C CB    . ASP B 1 337 ? 41.582  -29.386 16.088  1.000 28.374  0 337 ASP BBB CB    1 ? 2 
ATOM   6181  C CG    . ASP B 1 337 ? 41.137  -28.010 16.522  1.000 29.455  0 337 ASP BBB CG    1 ? 2 
ATOM   6182  O OD1   . ASP B 1 337 ? 39.960  -27.847 16.869  1.000 31.665  0 337 ASP BBB OD1   1 ? 2 
ATOM   6183  O OD2   . ASP B 1 337 ? 41.997  -27.092 16.534  1.000 34.135  0 337 ASP BBB OD2   1 ? 2 
ATOM   6184  N N     . ILE B 1 338 ? 41.541  -32.728 15.845  1.000 28.671  0 338 ILE BBB N     1 ? 2 
ATOM   6185  C CA    . ILE B 1 338 ? 42.150  -33.863 15.087  1.000 29.347  0 338 ILE BBB CA    1 ? 2 
ATOM   6186  C C     . ILE B 1 338 ? 41.075  -34.792 14.503  1.000 30.914  0 338 ILE BBB C     1 ? 2 
ATOM   6187  O O     . ILE B 1 338 ? 41.439  -35.683 13.703  1.000 35.747  0 338 ILE BBB O     1 ? 2 
ATOM   6188  C CB    . ILE B 1 338 ? 43.143  -34.661 15.944  1.000 28.981  0 338 ILE BBB CB    1 ? 2 
ATOM   6189  C CG1   . ILE B 1 338 ? 42.467  -35.444 17.064  1.000 26.796  0 338 ILE BBB CG1   1 ? 2 
ATOM   6190  C CG2   . ILE B 1 338 ? 44.256  -33.750 16.422  1.000 29.634  0 338 ILE BBB CG2   1 ? 2 
ATOM   6191  C CD1   . ILE B 1 338 ? 43.426  -36.173 17.976  1.000 26.562  0 338 ILE BBB CD1   1 ? 2 
ATOM   6192  N N     . VAL B 1 339 ? 39.811  -34.654 14.892  1.000 30.606  0 339 VAL BBB N     1 ? 2 
ATOM   6193  C CA    . VAL B 1 339 ? 38.759  -35.619 14.467  1.000 30.859  0 339 VAL BBB CA    1 ? 2 
ATOM   6194  C C     . VAL B 1 339 ? 38.091  -35.086 13.200  1.000 31.644  0 339 VAL BBB C     1 ? 2 
ATOM   6195  O O     . VAL B 1 339 ? 37.658  -33.912 13.182  1.000 30.780  0 339 VAL BBB O     1 ? 2 
ATOM   6196  C CB    . VAL B 1 339 ? 37.749  -35.906 15.588  1.000 29.293  0 339 VAL BBB CB    1 ? 2 
ATOM   6197  C CG1   . VAL B 1 339 ? 36.653  -36.850 15.117  1.000 28.602  0 339 VAL BBB CG1   1 ? 2 
ATOM   6198  C CG2   . VAL B 1 339 ? 38.443  -36.482 16.809  1.000 28.622  0 339 VAL BBB CG2   1 ? 2 
ATOM   6199  N N     . GLU B 1 340 ? 37.993  -35.944 12.191  1.000 32.753  0 340 GLU BBB N     1 ? 2 
ATOM   6200  C CA    . GLU B 1 340 ? 37.333  -35.592 10.917  1.000 34.908  0 340 GLU BBB CA    1 ? 2 
ATOM   6201  C C     . GLU B 1 340 ? 35.823  -35.381 11.135  1.000 33.635  0 340 GLU BBB C     1 ? 2 
ATOM   6202  O O     . GLU B 1 340 ? 35.188  -36.191 11.853  1.000 31.907  0 340 GLU BBB O     1 ? 2 
ATOM   6203  C CB    . GLU B 1 340 ? 37.582  -36.665 9.862   1.000 38.805  0 340 GLU BBB CB    1 ? 2 
ATOM   6204  C CG    . GLU B 1 340 ? 36.620  -36.545 8.695   1.000 45.362  0 340 GLU BBB CG    1 ? 2 
ATOM   6205  C CD    . GLU B 1 340 ? 37.216  -36.823 7.337   1.000 51.499  0 340 GLU BBB CD    1 ? 2 
ATOM   6206  O OE1   . GLU B 1 340 ? 36.816  -37.834 6.725   1.000 55.835  0 340 GLU BBB OE1   1 ? 2 
ATOM   6207  O OE2   . GLU B 1 340 ? 38.078  -36.012 6.901   1.000 59.302  0 340 GLU BBB OE2   1 ? 2 
ATOM   6208  N N     . GLY B 1 341 ? 35.278  -34.358 10.473  1.000 32.789  0 341 GLY BBB N     1 ? 2 
ATOM   6209  C CA    . GLY B 1 341 ? 33.829  -34.135 10.305  1.000 31.638  0 341 GLY BBB CA    1 ? 2 
ATOM   6210  C C     . GLY B 1 341 ? 33.207  -33.383 11.457  1.000 30.570  0 341 GLY BBB C     1 ? 2 
ATOM   6211  O O     . GLY B 1 341 ? 32.001  -33.458 11.627  1.000 30.423  0 341 GLY BBB O     1 ? 2 
ATOM   6212  N N     . ARG B 1 342 ? 33.998  -32.675 12.258  1.000 31.630  0 342 ARG BBB N     1 ? 2 
ATOM   6213  C CA    . ARG B 1 342 ? 33.429  -31.790 13.324  1.000 29.313  0 342 ARG BBB CA    1 ? 2 
ATOM   6214  C C     . ARG B 1 342 ? 34.145  -30.445 13.308  1.000 28.743  0 342 ARG BBB C     1 ? 2 
ATOM   6215  O O     . ARG B 1 342 ? 35.331  -30.342 12.966  1.000 27.612  0 342 ARG BBB O     1 ? 2 
ATOM   6216  C CB    . ARG B 1 342 ? 33.527  -32.461 14.704  1.000 29.786  0 342 ARG BBB CB    1 ? 2 
ATOM   6217  C CG    . ARG B 1 342 ? 34.944  -32.652 15.232  1.000 29.438  0 342 ARG BBB CG    1 ? 2 
ATOM   6218  C CD    . ARG B 1 342 ? 34.941  -33.315 16.591  1.000 28.736  0 342 ARG BBB CD    1 ? 2 
ATOM   6219  N NE    . ARG B 1 342 ? 34.490  -34.687 16.546  1.000 28.137  0 342 ARG BBB NE    1 ? 2 
ATOM   6220  C CZ    . ARG B 1 342 ? 34.341  -35.492 17.583  1.000 27.910  0 342 ARG BBB CZ    1 ? 2 
ATOM   6221  N NH1   . ARG B 1 342 ? 34.614  -35.068 18.808  1.000 27.127  0 342 ARG BBB NH1   1 ? 2 
ATOM   6222  N NH2   . ARG B 1 342 ? 33.878  -36.725 17.373  1.000 29.360  0 342 ARG BBB NH2   1 ? 2 
ATOM   6223  N N     . PRO B 1 343 ? 33.441  -29.366 13.702  1.000 28.408  0 343 PRO BBB N     1 ? 2 
ATOM   6224  C CA    . PRO B 1 343 ? 34.015  -28.026 13.695  1.000 29.146  0 343 PRO BBB CA    1 ? 2 
ATOM   6225  C C     . PRO B 1 343 ? 35.217  -27.944 14.654  1.000 29.888  0 343 PRO BBB C     1 ? 2 
ATOM   6226  O O     . PRO B 1 343 ? 35.187  -28.555 15.714  1.000 27.720  0 343 PRO BBB O     1 ? 2 
ATOM   6227  C CB    . PRO B 1 343 ? 32.879  -27.100 14.166  1.000 29.231  0 343 PRO BBB CB    1 ? 2 
ATOM   6228  C CG    . PRO B 1 343 ? 31.620  -27.938 14.000  1.000 29.121  0 343 PRO BBB CG    1 ? 2 
ATOM   6229  C CD    . PRO B 1 343 ? 32.051  -29.379 14.173  1.000 29.017  0 343 PRO BBB CD    1 ? 2 
ATOM   6230  N N     . GLU B 1 344 ? 36.242  -27.200 14.240  1.000 30.187  0 344 GLU BBB N     1 ? 2 
ATOM   6231  C CA    . GLU B 1 344 ? 37.467  -26.988 15.041  1.000 30.445  0 344 GLU BBB CA    1 ? 2 
ATOM   6232  C C     . GLU B 1 344 ? 37.215  -25.805 15.983  1.000 28.451  0 344 GLU BBB C     1 ? 2 
ATOM   6233  O O     . GLU B 1 344 ? 37.835  -24.765 15.762  1.000 30.034  0 344 GLU BBB O     1 ? 2 
ATOM   6234  C CB    . GLU B 1 344 ? 38.671  -26.711 14.129  1.000 33.669  0 344 GLU BBB CB    1 ? 2 
ATOM   6235  C CG    . GLU B 1 344 ? 39.046  -27.848 13.209  1.000 37.490  0 344 GLU BBB CG    1 ? 2 
ATOM   6236  C CD    . GLU B 1 344 ? 40.205  -27.608 12.243  1.000 43.982  0 344 GLU BBB CD    1 ? 2 
ATOM   6237  O OE1   . GLU B 1 344 ? 41.039  -26.688 12.489  1.000 48.317  0 344 GLU BBB OE1   1 ? 2 
ATOM   6238  O OE2   . GLU B 1 344 ? 40.308  -28.381 11.242  1.000 48.186  0 344 GLU BBB OE2   1 ? 2 
ATOM   6239  N N     . LEU B 1 345 ? 36.355  -25.977 16.986  1.000 25.315  0 345 LEU BBB N     1 ? 2 
ATOM   6240  C CA    . LEU B 1 345 ? 35.998  -24.939 17.987  1.000 23.230  0 345 LEU BBB CA    1 ? 2 
ATOM   6241  C C     . LEU B 1 345 ? 36.262  -25.442 19.412  1.000 21.323  0 345 LEU BBB C     1 ? 2 
ATOM   6242  O O     . LEU B 1 345 ? 36.161  -26.646 19.640  1.000 21.297  0 345 LEU BBB O     1 ? 2 
ATOM   6243  C CB    . LEU B 1 345 ? 34.509  -24.587 17.802  1.000 22.986  0 345 LEU BBB CB    1 ? 2 
ATOM   6244  C CG    . LEU B 1 345 ? 34.157  -23.935 16.470  1.000 22.535  0 345 LEU BBB CG    1 ? 2 
ATOM   6245  C CD1   . LEU B 1 345 ? 32.634  -23.826 16.292  1.000 22.852  0 345 LEU BBB CD1   1 ? 2 
ATOM   6246  C CD2   . LEU B 1 345 ? 34.834  -22.575 16.345  1.000 22.721  0 345 LEU BBB CD2   1 ? 2 
ATOM   6247  N N     . THR B 1 346 ? 36.564  -24.544 20.344  1.000 20.745  0 346 THR BBB N     1 ? 2 
ATOM   6248  C CA    . THR B 1 346 ? 36.971  -24.915 21.720  1.000 20.967  0 346 THR BBB CA    1 ? 2 
ATOM   6249  C C     . THR B 1 346 ? 35.812  -25.559 22.459  1.000 21.043  0 346 THR BBB C     1 ? 2 
ATOM   6250  O O     . THR B 1 346 ? 35.968  -26.656 22.998  1.000 19.715  0 346 THR BBB O     1 ? 2 
ATOM   6251  C CB    . THR B 1 346 ? 37.591  -23.726 22.452  1.000 23.016  0 346 THR BBB CB    1 ? 2 
ATOM   6252  O OG1   . THR B 1 346 ? 38.986  -23.766 22.139  1.000 25.020  0 346 THR BBB OG1   1 ? 2 
ATOM   6253  C CG2   . THR B 1 346 ? 37.457  -23.782 23.957  1.000 23.235  0 346 THR BBB CG2   1 ? 2 
ATOM   6254  N N     . PRO B 1 347 ? 34.607  -24.928 22.521  1.000 21.062  0 347 PRO BBB N     1 ? 2 
ATOM   6255  C CA    . PRO B 1 347 ? 33.453  -25.534 23.206  1.000 21.807  0 347 PRO BBB CA    1 ? 2 
ATOM   6256  C C     . PRO B 1 347 ? 33.087  -26.940 22.726  1.000 21.783  0 347 PRO BBB C     1 ? 2 
ATOM   6257  O O     . PRO B 1 347 ? 32.672  -27.707 23.478  1.000 23.028  0 347 PRO BBB O     1 ? 2 
ATOM   6258  C CB    . PRO B 1 347 ? 32.312  -24.515 22.984  1.000 22.465  0 347 PRO BBB CB    1 ? 2 
ATOM   6259  C CG    . PRO B 1 347 ? 33.056  -23.186 22.788  1.000 22.128  0 347 PRO BBB CG    1 ? 2 
ATOM   6260  C CD    . PRO B 1 347 ? 34.290  -23.606 21.994  1.000 21.518  0 347 PRO BBB CD    1 ? 2 
ATOM   6261  N N     . VAL B 1 348 ? 33.292  -27.251 21.455  1.000 22.666  0 348 VAL BBB N     1 ? 2 
ATOM   6262  C CA    . VAL B 1 348 ? 33.048  -28.598 20.863  1.000 22.236  0 348 VAL BBB CA    1 ? 2 
ATOM   6263  C C     . VAL B 1 348 ? 34.085  -29.569 21.405  1.000 22.651  0 348 VAL BBB C     1 ? 2 
ATOM   6264  O O     . VAL B 1 348 ? 33.702  -30.664 21.754  1.000 24.150  0 348 VAL BBB O     1 ? 2 
ATOM   6265  C CB    . VAL B 1 348 ? 33.086  -28.518 19.332  1.000 23.355  0 348 VAL BBB CB    1 ? 2 
ATOM   6266  C CG1   . VAL B 1 348 ? 32.901  -29.883 18.672  1.000 22.785  0 348 VAL BBB CG1   1 ? 2 
ATOM   6267  C CG2   . VAL B 1 348 ? 32.051  -27.495 18.847  1.000 23.642  0 348 VAL BBB CG2   1 ? 2 
ATOM   6268  N N     . ALA B 1 349 ? 35.360  -29.180 21.461  1.000 21.957  0 349 ALA BBB N     1 ? 2 
ATOM   6269  C CA    . ALA B 1 349 ? 36.435  -29.993 22.074  1.000 21.951  0 349 ALA BBB CA    1 ? 2 
ATOM   6270  C C     . ALA B 1 349 ? 36.085  -30.317 23.545  1.000 21.427  0 349 ALA BBB C     1 ? 2 
ATOM   6271  O O     . ALA B 1 349 ? 36.046  -31.489 23.912  1.000 21.824  0 349 ALA BBB O     1 ? 2 
ATOM   6272  C CB    . ALA B 1 349 ? 37.744  -29.241 21.941  1.000 21.637  0 349 ALA BBB CB    1 ? 2 
ATOM   6273  N N     . VAL B 1 350 ? 35.832  -29.292 24.353  1.000 21.456  0 350 VAL BBB N     1 ? 2 
ATOM   6274  C CA    . VAL B 1 350 ? 35.471  -29.376 25.809  1.000 21.495  0 350 VAL BBB CA    1 ? 2 
ATOM   6275  C C     . VAL B 1 350 ? 34.273  -30.308 26.005  1.000 22.634  0 350 VAL BBB C     1 ? 2 
ATOM   6276  O O     . VAL B 1 350 ? 34.398  -31.282 26.771  1.000 22.929  0 350 VAL BBB O     1 ? 2 
ATOM   6277  C CB    . VAL B 1 350 ? 35.192  -27.976 26.395  1.000 20.798  0 350 VAL BBB CB    1 ? 2 
ATOM   6278  C CG1   . VAL B 1 350 ? 34.577  -28.032 27.783  1.000 21.326  0 350 VAL BBB CG1   1 ? 2 
ATOM   6279  C CG2   . VAL B 1 350 ? 36.436  -27.105 26.428  1.000 20.389  0 350 VAL BBB CG2   1 ? 2 
ATOM   6280  N N     . LYS B 1 351 ? 33.140  -30.032 25.350  1.000 23.861  0 351 LYS BBB N     1 ? 2 
ATOM   6281  C CA    . LYS B 1 351 ? 31.908  -30.793 25.641  1.000 25.355  0 351 LYS BBB CA    1 ? 2 
ATOM   6282  C C     . LYS B 1 351 ? 32.116  -32.240 25.169  1.000 27.029  0 351 LYS BBB C     1 ? 2 
ATOM   6283  O O     . LYS B 1 351 ? 31.624  -33.160 25.816  1.000 28.864  0 351 LYS BBB O     1 ? 2 
ATOM   6284  C CB    . LYS B 1 351 ? 30.655  -30.160 25.029  1.000 25.173  0 351 LYS BBB CB    1 ? 2 
ATOM   6285  C CG    . LYS B 1 351 ? 29.391  -30.883 25.450  1.000 26.469  0 351 LYS BBB CG    1 ? 2 
ATOM   6286  C CD    . LYS B 1 351 ? 28.087  -30.172 25.118  1.000 28.592  0 351 LYS BBB CD    1 ? 2 
ATOM   6287  C CE    . LYS B 1 351 ? 27.790  -28.910 25.937  1.000 29.356  0 351 LYS BBB CE    1 ? 2 
ATOM   6288  N NZ    . LYS B 1 351 ? 27.568  -29.155 27.391  1.000 29.393  0 351 LYS BBB NZ    1 ? 2 
ATOM   6289  N N     . ALA B 1 352 ? 32.781  -32.470 24.055  1.000 28.391  0 352 ALA BBB N     1 ? 2 
ATOM   6290  C CA    . ALA B 1 352 ? 33.046  -33.852 23.582  1.000 30.511  0 352 ALA BBB CA    1 ? 2 
ATOM   6291  C C     . ALA B 1 352 ? 33.903  -34.574 24.629  1.000 29.900  0 352 ALA BBB C     1 ? 2 
ATOM   6292  O O     . ALA B 1 352 ? 33.611  -35.745 24.896  1.000 30.481  0 352 ALA BBB O     1 ? 2 
ATOM   6293  C CB    . ALA B 1 352 ? 33.730  -33.875 22.221  1.000 31.701  0 352 ALA BBB CB    1 ? 2 
ATOM   6294  N N     . GLY B 1 353 ? 34.882  -33.884 25.215  1.000 28.029  0 353 GLY BBB N     1 ? 2 
ATOM   6295  C CA    . GLY B 1 353 ? 35.737  -34.472 26.259  1.000 28.336  0 353 GLY BBB CA    1 ? 2 
ATOM   6296  C C     . GLY B 1 353 ? 34.941  -34.858 27.505  1.000 27.486  0 353 GLY BBB C     1 ? 2 
ATOM   6297  O O     . GLY B 1 353 ? 35.120  -35.959 28.029  1.000 25.767  0 353 GLY BBB O     1 ? 2 
ATOM   6298  N N     . ILE B 1 354 ? 34.076  -33.961 27.961  1.000 28.305  0 354 ILE BBB N     1 ? 2 
ATOM   6299  C CA    . ILE B 1 354 ? 33.206  -34.174 29.150  1.000 28.608  0 354 ILE BBB CA    1 ? 2 
ATOM   6300  C C     . ILE B 1 354 ? 32.212  -35.318 28.855  1.000 28.486  0 354 ILE BBB C     1 ? 2 
ATOM   6301  O O     . ILE B 1 354 ? 32.093  -36.215 29.716  1.000 30.134  0 354 ILE BBB O     1 ? 2 
ATOM   6302  C CB    . ILE B 1 354 ? 32.494  -32.872 29.577  1.000 28.443  0 354 ILE BBB CB    1 ? 2 
ATOM   6303  C CG1   . ILE B 1 354 ? 33.501  -31.809 30.040  1.000 29.131  0 354 ILE BBB CG1   1 ? 2 
ATOM   6304  C CG2   . ILE B 1 354 ? 31.462  -33.187 30.666  1.000 29.168  0 354 ILE BBB CG2   1 ? 2 
ATOM   6305  C CD1   . ILE B 1 354 ? 32.876  -30.410 30.331  1.000 27.161  0 354 ILE BBB CD1   1 ? 2 
ATOM   6306  N N     . LEU B 1 355 ? 31.510  -35.290 27.707  1.000 26.674  0 355 LEU BBB N     1 ? 2 
ATOM   6307  C CA    . LEU B 1 355 ? 30.477  -36.306 27.404  1.000 26.522  0 355 LEU BBB CA    1 ? 2 
ATOM   6308  C C     . LEU B 1 355 ? 31.160  -37.677 27.232  1.000 27.464  0 355 LEU BBB C     1 ? 2 
ATOM   6309  O O     . LEU B 1 355 ? 30.584  -38.683 27.719  1.000 27.280  0 355 LEU BBB O     1 ? 2 
ATOM   6310  C CB    . LEU B 1 355 ? 29.688  -35.882 26.172  1.000 26.073  0 355 LEU BBB CB    1 ? 2 
ATOM   6311  C CG    . LEU B 1 355 ? 28.772  -34.658 26.327  1.000 26.555  0 355 LEU BBB CG    1 ? 2 
ATOM   6312  C CD1   . LEU B 1 355 ? 27.916  -34.530 25.080  1.000 27.011  0 355 LEU BBB CD1   1 ? 2 
ATOM   6313  C CD2   . LEU B 1 355 ? 27.879  -34.721 27.554  1.000 25.439  0 355 LEU BBB CD2   1 ? 2 
ATOM   6314  N N     . LEU B 1 356 ? 32.344  -37.725 26.608  1.000 27.439  0 356 LEU BBB N     1 ? 2 
ATOM   6315  C CA    . LEU B 1 356 ? 33.122  -38.982 26.455  1.000 29.648  0 356 LEU BBB CA    1 ? 2 
ATOM   6316  C C     . LEU B 1 356 ? 33.410  -39.539 27.853  1.000 29.944  0 356 LEU BBB C     1 ? 2 
ATOM   6317  O O     . LEU B 1 356 ? 33.006  -40.683 28.119  1.000 29.905  0 356 LEU BBB O     1 ? 2 
ATOM   6318  C CB    . LEU B 1 356 ? 34.417  -38.727 25.676  1.000 30.296  0 356 LEU BBB CB    1 ? 2 
ATOM   6319  C CG    . LEU B 1 356 ? 35.424  -39.880 25.629  1.000 31.551  0 356 LEU BBB CG    1 ? 2 
ATOM   6320  C CD1   . LEU B 1 356 ? 34.872  -41.111 24.917  1.000 32.788  0 356 LEU BBB CD1   1 ? 2 
ATOM   6321  C CD2   . LEU B 1 356 ? 36.715  -39.452 24.969  1.000 31.606  0 356 LEU BBB CD2   1 ? 2 
ATOM   6322  N N     . ALA B 1 357 ? 34.075  -38.765 28.711  1.000 30.235  0 357 ALA BBB N     1 ? 2 
ATOM   6323  C CA    . ALA B 1 357 ? 34.331  -39.111 30.134  1.000 30.900  0 357 ALA BBB CA    1 ? 2 
ATOM   6324  C C     . ALA B 1 357 ? 33.067  -39.723 30.773  1.000 31.818  0 357 ALA BBB C     1 ? 2 
ATOM   6325  O O     . ALA B 1 357 ? 33.167  -40.809 31.371  1.000 30.940  0 357 ALA BBB O     1 ? 2 
ATOM   6326  C CB    . ALA B 1 357 ? 34.811  -37.899 30.900  1.000 29.975  0 357 ALA BBB CB    1 ? 2 
ATOM   6327  N N     . ARG B 1 358 ? 31.912  -39.088 30.625  1.000 33.336  0 358 ARG BBB N     1 ? 2 
ATOM   6328  C CA    . ARG B 1 358 ? 30.638  -39.579 31.236  1.000 37.452  0 358 ARG BBB CA    1 ? 2 
ATOM   6329  C C     . ARG B 1 358 ? 30.188  -40.907 30.616  1.000 36.897  0 358 ARG BBB C     1 ? 2 
ATOM   6330  O O     . ARG B 1 358 ? 29.744  -41.770 31.364  1.000 39.312  0 358 ARG BBB O     1 ? 2 
ATOM   6331  C CB    . ARG B 1 358 ? 29.525  -38.534 31.098  1.000 40.265  0 358 ARG BBB CB    1 ? 2 
ATOM   6332  C CG    . ARG B 1 358 ? 29.710  -37.339 32.019  1.000 41.679  0 358 ARG BBB CG    1 ? 2 
ATOM   6333  C CD    . ARG B 1 358 ? 28.677  -36.249 31.822  1.000 42.531  0 358 ARG BBB CD    1 ? 2 
ATOM   6334  N NE    . ARG B 1 358 ? 29.065  -35.065 32.591  1.000 42.597  0 358 ARG BBB NE    1 ? 2 
ATOM   6335  C CZ    . ARG B 1 358 ? 28.527  -33.867 32.414  1.000 44.287  0 358 ARG BBB CZ    1 ? 2 
ATOM   6336  N NH1   . ARG B 1 358 ? 27.575  -33.703 31.506  1.000 47.009  0 358 ARG BBB NH1   1 ? 2 
ATOM   6337  N NH2   . ARG B 1 358 ? 28.942  -32.839 33.131  1.000 44.401  0 358 ARG BBB NH2   1 ? 2 
ATOM   6338  N N     . ARG B 1 359 ? 30.248  -41.044 29.289  1.000 37.534  0 359 ARG BBB N     1 ? 2 
ATOM   6339  C CA    . ARG B 1 359 ? 29.831  -42.284 28.584  1.000 37.816  0 359 ARG BBB CA    1 ? 2 
ATOM   6340  C C     . ARG B 1 359 ? 30.711  -43.459 29.046  1.000 40.276  0 359 ARG BBB C     1 ? 2 
ATOM   6341  O O     . ARG B 1 359 ? 30.183  -44.586 29.189  1.000 43.145  0 359 ARG BBB O     1 ? 2 
ATOM   6342  C CB    . ARG B 1 359 ? 29.883  -42.109 27.064  1.000 35.139  0 359 ARG BBB CB    1 ? 2 
ATOM   6343  C CG    . ARG B 1 359 ? 28.827  -41.171 26.497  1.000 32.685  0 359 ARG BBB CG    1 ? 2 
ATOM   6344  C CD    . ARG B 1 359 ? 28.554  -41.375 25.023  1.000 31.321  0 359 ARG BBB CD    1 ? 2 
ATOM   6345  N NE    . ARG B 1 359 ? 29.773  -41.333 24.245  1.000 29.876  0 359 ARG BBB NE    1 ? 2 
ATOM   6346  C CZ    . ARG B 1 359 ? 30.410  -40.235 23.887  1.000 28.227  0 359 ARG BBB CZ    1 ? 2 
ATOM   6347  N NH1   . ARG B 1 359 ? 29.942  -39.047 24.227  1.000 27.615  0 359 ARG BBB NH1   1 ? 2 
ATOM   6348  N NH2   . ARG B 1 359 ? 31.549  -40.345 23.219  1.000 27.863  0 359 ARG BBB NH2   1 ? 2 
ATOM   6349  N N     . LEU B 1 360 ? 32.012  -43.217 29.239  1.000 41.622  0 360 LEU BBB N     1 ? 2 
ATOM   6350  C CA    . LEU B 1 360 ? 33.010  -44.255 29.620  1.000 40.036  0 360 LEU BBB CA    1 ? 2 
ATOM   6351  C C     . LEU B 1 360 ? 32.779  -44.710 31.066  1.000 41.263  0 360 LEU BBB C     1 ? 2 
ATOM   6352  O O     . LEU B 1 360 ? 32.942  -45.924 31.305  1.000 40.652  0 360 LEU BBB O     1 ? 2 
ATOM   6353  C CB    . LEU B 1 360 ? 34.427  -43.692 29.460  1.000 40.587  0 360 LEU BBB CB    1 ? 2 
ATOM   6354  C CG    . LEU B 1 360 ? 34.950  -43.542 28.029  1.000 41.406  0 360 LEU BBB CG    1 ? 2 
ATOM   6355  C CD1   . LEU B 1 360 ? 36.356  -42.955 28.024  1.000 39.974  0 360 LEU BBB CD1   1 ? 2 
ATOM   6356  C CD2   . LEU B 1 360 ? 34.976  -44.905 27.353  1.000 41.870  0 360 LEU BBB CD2   1 ? 2 
ATOM   6357  N N     . PHE B 1 361 ? 32.391  -43.796 31.973  1.000 40.627  0 361 PHE BBB N     1 ? 2 
ATOM   6358  C CA    . PHE B 1 361 ? 32.548  -43.993 33.437  1.000 41.980  0 361 PHE BBB CA    1 ? 2 
ATOM   6359  C C     . PHE B 1 361 ? 31.270  -43.728 34.243  1.000 44.343  0 361 PHE BBB C     1 ? 2 
ATOM   6360  O O     . PHE B 1 361 ? 31.316  -44.112 35.424  1.000 45.644  0 361 PHE BBB O     1 ? 2 
ATOM   6361  C CB    . PHE B 1 361 ? 33.695  -43.135 33.966  1.000 42.461  0 361 PHE BBB CB    1 ? 2 
ATOM   6362  C CG    . PHE B 1 361 ? 35.044  -43.453 33.374  1.000 42.093  0 361 PHE BBB CG    1 ? 2 
ATOM   6363  C CD1   . PHE B 1 361 ? 35.573  -44.720 33.484  1.000 42.903  0 361 PHE BBB CD1   1 ? 2 
ATOM   6364  C CD2   . PHE B 1 361 ? 35.794  -42.483 32.718  1.000 42.234  0 361 PHE BBB CD2   1 ? 2 
ATOM   6365  C CE1   . PHE B 1 361 ? 36.847  -45.006 32.992  1.000 43.263  0 361 PHE BBB CE1   1 ? 2 
ATOM   6366  C CE2   . PHE B 1 361 ? 37.034  -42.784 32.169  1.000 42.002  0 361 PHE BBB CE2   1 ? 2 
ATOM   6367  C CZ    . PHE B 1 361 ? 37.574  -44.045 32.325  1.000 42.730  0 361 PHE BBB CZ    1 ? 2 
ATOM   6368  N N     . ALA B 1 362 ? 30.207  -43.142 33.663  1.000 44.411  0 362 ALA BBB N     1 ? 2 
ATOM   6369  C CA    . ALA B 1 362 ? 28.971  -42.755 34.374  1.000 43.114  0 362 ALA BBB CA    1 ? 2 
ATOM   6370  C C     . ALA B 1 362 ? 27.724  -43.209 33.598  1.000 44.147  0 362 ALA BBB C     1 ? 2 
ATOM   6371  O O     . ALA B 1 362 ? 26.648  -42.663 33.842  1.000 44.430  0 362 ALA BBB O     1 ? 2 
ATOM   6372  C CB    . ALA B 1 362 ? 28.986  -41.263 34.620  1.000 41.618  0 362 ALA BBB CB    1 ? 2 
ATOM   6373  N N     . GLY B 1 363 ? 27.855  -44.166 32.689  1.000 45.616  0 363 GLY BBB N     1 ? 2 
ATOM   6374  C CA    . GLY B 1 363 ? 26.708  -44.796 32.012  1.000 47.394  0 363 GLY BBB CA    1 ? 2 
ATOM   6375  C C     . GLY B 1 363 ? 25.876  -43.825 31.194  1.000 48.043  0 363 GLY BBB C     1 ? 2 
ATOM   6376  O O     . GLY B 1 363 ? 24.691  -44.151 30.933  1.000 51.254  0 363 GLY BBB O     1 ? 2 
ATOM   6377  N N     . SER B 1 364 ? 26.451  -42.690 30.783  1.000 46.597  0 364 SER BBB N     1 ? 2 
ATOM   6378  C CA    . SER B 1 364 ? 25.810  -41.693 29.888  1.000 46.972  0 364 SER BBB CA    1 ? 2 
ATOM   6379  C C     . SER B 1 364 ? 25.825  -42.236 28.451  1.000 46.912  0 364 SER BBB C     1 ? 2 
ATOM   6380  O O     . SER B 1 364 ? 26.687  -43.083 28.139  1.000 46.090  0 364 SER BBB O     1 ? 2 
ATOM   6381  C CB    . SER B 1 364 ? 26.482  -40.324 30.012  1.000 47.801  0 364 SER BBB CB    1 ? 2 
ATOM   6382  O OG    . SER B 1 364 ? 26.116  -39.446 28.950  1.000 47.545  0 364 SER BBB OG    1 ? 2 
ATOM   6383  N N     . ASN B 1 365 ? 24.877  -41.819 27.616  1.000 48.861  0 365 ASN BBB N     1 ? 2 
ATOM   6384  C CA    . ASN B 1 365 ? 24.900  -42.108 26.164  1.000 55.294  0 365 ASN BBB CA    1 ? 2 
ATOM   6385  C C     . ASN B 1 365 ? 24.637  -40.807 25.390  1.000 57.591  0 365 ASN BBB C     1 ? 2 
ATOM   6386  O O     . ASN B 1 365 ? 24.125  -40.867 24.247  1.000 56.523  0 365 ASN BBB O     1 ? 2 
ATOM   6387  C CB    . ASN B 1 365 ? 23.932  -43.234 25.792  1.000 61.055  0 365 ASN BBB CB    1 ? 2 
ATOM   6388  C CG    . ASN B 1 365 ? 22.472  -42.928 26.067  1.000 69.005  0 365 ASN BBB CG    1 ? 2 
ATOM   6389  O OD1   . ASN B 1 365 ? 22.068  -41.774 26.245  1.000 73.028  0 365 ASN BBB OD1   1 ? 2 
ATOM   6390  N ND2   . ASN B 1 365 ? 21.658  -43.969 26.099  1.000 74.754  0 365 ASN BBB ND2   1 ? 2 
ATOM   6391  N N     . GLU B 1 366 ? 25.018  -39.663 25.971  1.000 56.161  0 366 GLU BBB N     1 ? 2 
ATOM   6392  C CA    . GLU B 1 366 ? 24.753  -38.315 25.405  1.000 52.946  0 366 GLU BBB CA    1 ? 2 
ATOM   6393  C C     . GLU B 1 366 ? 25.951  -37.929 24.549  1.000 47.145  0 366 GLU BBB C     1 ? 2 
ATOM   6394  O O     . GLU B 1 366 ? 27.104  -38.072 25.012  1.000 41.989  0 366 GLU BBB O     1 ? 2 
ATOM   6395  C CB    . GLU B 1 366 ? 24.442  -37.277 26.493  1.000 57.014  0 366 GLU BBB CB    1 ? 2 
ATOM   6396  C CG    . GLU B 1 366 ? 23.072  -37.490 27.163  1.000 61.801  0 366 GLU BBB CG    1 ? 2 
ATOM   6397  C CD    . GLU B 1 366 ? 22.089  -36.331 27.305  1.000 67.226  0 366 GLU BBB CD    1 ? 2 
ATOM   6398  O OE1   . GLU B 1 366 ? 22.318  -35.441 28.170  1.000 70.099  0 366 GLU BBB OE1   1 ? 2 
ATOM   6399  O OE2   . GLU B 1 366 ? 21.081  -36.329 26.541  1.000 68.444  0 366 GLU BBB OE2   1 ? 2 
ATOM   6400  N N     . PHE B 1 367 ? 25.645  -37.520 23.314  1.000 42.191  0 367 PHE BBB N     1 ? 2 
ATOM   6401  C CA    . PHE B 1 367 ? 26.577  -36.947 22.324  1.000 40.543  0 367 PHE BBB CA    1 ? 2 
ATOM   6402  C C     . PHE B 1 367 ? 26.172  -35.487 22.082  1.000 39.429  0 367 PHE BBB C     1 ? 2 
ATOM   6403  O O     . PHE B 1 367 ? 25.037  -35.099 22.407  1.000 38.424  0 367 PHE BBB O     1 ? 2 
ATOM   6404  C CB    . PHE B 1 367 ? 26.572  -37.793 21.044  1.000 39.607  0 367 PHE BBB CB    1 ? 2 
ATOM   6405  C CG    . PHE B 1 367 ? 27.184  -39.159 21.199  1.000 39.456  0 367 PHE BBB CG    1 ? 2 
ATOM   6406  C CD1   . PHE B 1 367 ? 26.424  -40.203 21.716  1.000 38.211  0 367 PHE BBB CD1   1 ? 2 
ATOM   6407  C CD2   . PHE B 1 367 ? 28.518  -39.405 20.841  1.000 38.710  0 367 PHE BBB CD2   1 ? 2 
ATOM   6408  C CE1   . PHE B 1 367 ? 26.975  -41.467 21.881  1.000 38.513  0 367 PHE BBB CE1   1 ? 2 
ATOM   6409  C CE2   . PHE B 1 367 ? 29.072  -40.676 21.004  1.000 39.025  0 367 PHE BBB CE2   1 ? 2 
ATOM   6410  C CZ    . PHE B 1 367 ? 28.302  -41.702 21.537  1.000 39.508  0 367 PHE BBB CZ    1 ? 2 
ATOM   6411  N N     . ILE B 1 368 ? 27.089  -34.686 21.520  1.000 38.424  0 368 ILE BBB N     1 ? 2 
ATOM   6412  C CA    . ILE B 1 368 ? 26.750  -33.336 20.978  1.000 36.335  0 368 ILE BBB CA    1 ? 2 
ATOM   6413  C C     . ILE B 1 368 ? 25.758  -33.504 19.821  1.000 36.304  0 368 ILE BBB C     1 ? 2 
ATOM   6414  O O     . ILE B 1 368 ? 25.867  -34.509 19.051  1.000 38.116  0 368 ILE BBB O     1 ? 2 
ATOM   6415  C CB    . ILE B 1 368 ? 28.017  -32.591 20.526  1.000 35.080  0 368 ILE BBB CB    1 ? 2 
ATOM   6416  C CG1   . ILE B 1 368 ? 28.898  -32.201 21.712  1.000 34.377  0 368 ILE BBB CG1   1 ? 2 
ATOM   6417  C CG2   . ILE B 1 368 ? 27.657  -31.380 19.689  1.000 34.769  0 368 ILE BBB CG2   1 ? 2 
ATOM   6418  C CD1   . ILE B 1 368 ? 30.345  -31.949 21.343  1.000 32.940  0 368 ILE BBB CD1   1 ? 2 
ATOM   6419  N N     . ASP B 1 369 ? 24.837  -32.545 19.698  1.000 35.058  0 369 ASP BBB N     1 ? 2 
ATOM   6420  C CA    . ASP B 1 369 ? 23.951  -32.365 18.522  1.000 35.560  0 369 ASP BBB CA    1 ? 2 
ATOM   6421  C C     . ASP B 1 369 ? 24.682  -31.388 17.598  1.000 36.821  0 369 ASP BBB C     1 ? 2 
ATOM   6422  O O     . ASP B 1 369 ? 24.678  -30.161 17.882  1.000 38.124  0 369 ASP BBB O     1 ? 2 
ATOM   6423  C CB    . ASP B 1 369 ? 22.551  -31.945 18.978  1.000 35.088  0 369 ASP BBB CB    1 ? 2 
ATOM   6424  C CG    . ASP B 1 369 ? 21.527  -31.713 17.877  1.000 34.928  0 369 ASP BBB CG    1 ? 2 
ATOM   6425  O OD1   . ASP B 1 369 ? 21.914  -31.803 16.679  1.000 33.401  0 369 ASP BBB OD1   1 ? 2 
ATOM   6426  O OD2   . ASP B 1 369 ? 20.355  -31.433 18.243  1.000 34.045  0 369 ASP BBB OD2   1 ? 2 
ATOM   6427  N N     . TYR B 1 370 ? 25.323  -31.906 16.554  1.000 37.683  0 370 TYR BBB N     1 ? 2 
ATOM   6428  C CA    . TYR B 1 370 ? 26.222  -31.122 15.676  1.000 40.212  0 370 TYR BBB CA    1 ? 2 
ATOM   6429  C C     . TYR B 1 370 ? 25.401  -30.232 14.738  1.000 39.751  0 370 TYR BBB C     1 ? 2 
ATOM   6430  O O     . TYR B 1 370 ? 26.016  -29.454 13.997  1.000 44.021  0 370 TYR BBB O     1 ? 2 
ATOM   6431  C CB    . TYR B 1 370 ? 27.209  -32.022 14.923  1.000 41.728  0 370 TYR BBB CB    1 ? 2 
ATOM   6432  C CG    . TYR B 1 370 ? 28.322  -32.543 15.796  1.000 44.672  0 370 TYR BBB CG    1 ? 2 
ATOM   6433  C CD1   . TYR B 1 370 ? 29.372  -31.724 16.182  1.000 44.044  0 370 TYR BBB CD1   1 ? 2 
ATOM   6434  C CD2   . TYR B 1 370 ? 28.331  -33.857 16.256  1.000 47.156  0 370 TYR BBB CD2   1 ? 2 
ATOM   6435  C CE1   . TYR B 1 370 ? 30.397  -32.192 16.992  1.000 44.100  0 370 TYR BBB CE1   1 ? 2 
ATOM   6436  C CE2   . TYR B 1 370 ? 29.349  -34.336 17.076  1.000 46.395  0 370 TYR BBB CE2   1 ? 2 
ATOM   6437  C CZ    . TYR B 1 370 ? 30.383  -33.495 17.464  1.000 46.296  0 370 TYR BBB CZ    1 ? 2 
ATOM   6438  O OH    . TYR B 1 370 ? 31.405  -33.969 18.253  1.000 43.347  0 370 TYR BBB OH    1 ? 2 
ATOM   6439  N N     . ASP B 1 371 ? 24.075  -30.297 14.792  1.000 39.968  0 371 ASP BBB N     1 ? 2 
ATOM   6440  C CA    . ASP B 1 371 ? 23.180  -29.422 13.984  1.000 41.507  0 371 ASP BBB CA    1 ? 2 
ATOM   6441  C C     . ASP B 1 371 ? 23.149  -28.004 14.566  1.000 40.332  0 371 ASP BBB C     1 ? 2 
ATOM   6442  O O     . ASP B 1 371 ? 22.743  -27.095 13.830  1.000 40.237  0 371 ASP BBB O     1 ? 2 
ATOM   6443  C CB    . ASP B 1 371 ? 21.750  -29.977 13.902  1.000 41.682  0 371 ASP BBB CB    1 ? 2 
ATOM   6444  C CG    . ASP B 1 371 ? 21.622  -31.276 13.128  1.000 41.500  0 371 ASP BBB CG    1 ? 2 
ATOM   6445  O OD1   . ASP B 1 371 ? 22.422  -31.461 12.158  1.000 42.582  0 371 ASP BBB OD1   1 ? 2 
ATOM   6446  O OD2   . ASP B 1 371 ? 20.730  -32.084 13.501  1.000 39.829  0 371 ASP BBB OD2   1 ? 2 
ATOM   6447  N N     . PHE B 1 372 ? 23.516  -27.823 15.839  1.000 37.698  0 372 PHE BBB N     1 ? 2 
ATOM   6448  C CA    . PHE B 1 372 ? 23.368  -26.534 16.561  1.000 37.220  0 372 PHE BBB CA    1 ? 2 
ATOM   6449  C C     . PHE B 1 372 ? 24.683  -26.203 17.262  1.000 34.437  0 372 PHE BBB C     1 ? 2 
ATOM   6450  O O     . PHE B 1 372 ? 24.774  -26.212 18.508  1.000 35.847  0 372 PHE BBB O     1 ? 2 
ATOM   6451  C CB    . PHE B 1 372 ? 22.170  -26.583 17.509  1.000 38.411  0 372 PHE BBB CB    1 ? 2 
ATOM   6452  C CG    . PHE B 1 372 ? 20.862  -26.826 16.801  1.000 39.140  0 372 PHE BBB CG    1 ? 2 
ATOM   6453  C CD1   . PHE B 1 372 ? 20.274  -25.795 16.078  1.000 40.561  0 372 PHE BBB CD1   1 ? 2 
ATOM   6454  C CD2   . PHE B 1 372 ? 20.242  -28.070 16.816  1.000 39.700  0 372 PHE BBB CD2   1 ? 2 
ATOM   6455  C CE1   . PHE B 1 372 ? 19.100  -26.003 15.373  1.000 40.590  0 372 PHE BBB CE1   1 ? 2 
ATOM   6456  C CE2   . PHE B 1 372 ? 19.064  -28.265 16.115  1.000 41.107  0 372 PHE BBB CE2   1 ? 2 
ATOM   6457  C CZ    . PHE B 1 372 ? 18.506  -27.234 15.392  1.000 40.970  0 372 PHE BBB CZ    1 ? 2 
ATOM   6458  N N     . VAL B 1 373 ? 25.693  -25.912 16.448  1.000 31.897  0 373 VAL BBB N     1 ? 2 
ATOM   6459  C CA    . VAL B 1 373 ? 27.036  -25.460 16.914  1.000 28.313  0 373 VAL BBB CA    1 ? 2 
ATOM   6460  C C     . VAL B 1 373 ? 27.182  -24.009 16.484  1.000 26.248  0 373 VAL BBB C     1 ? 2 
ATOM   6461  O O     . VAL B 1 373 ? 27.431  -23.740 15.322  1.000 25.635  0 373 VAL BBB O     1 ? 2 
ATOM   6462  C CB    . VAL B 1 373 ? 28.170  -26.346 16.365  1.000 27.250  0 373 VAL BBB CB    1 ? 2 
ATOM   6463  C CG1   . VAL B 1 373 ? 29.527  -25.805 16.781  1.000 26.725  0 373 VAL BBB CG1   1 ? 2 
ATOM   6464  C CG2   . VAL B 1 373 ? 28.030  -27.783 16.832  1.000 27.457  0 373 VAL BBB CG2   1 ? 2 
ATOM   6465  N N     . PRO B 1 374 ? 27.027  -23.031 17.397  1.000 25.375  0 374 PRO BBB N     1 ? 2 
ATOM   6466  C CA    . PRO B 1 374 ? 27.166  -21.626 17.021  1.000 25.605  0 374 PRO BBB CA    1 ? 2 
ATOM   6467  C C     . PRO B 1 374 ? 28.649  -21.271 16.976  1.000 26.860  0 374 PRO BBB C     1 ? 2 
ATOM   6468  O O     . PRO B 1 374 ? 29.488  -21.985 17.542  1.000 25.769  0 374 PRO BBB O     1 ? 2 
ATOM   6469  C CB    . PRO B 1 374 ? 26.474  -20.870 18.162  1.000 25.298  0 374 PRO BBB CB    1 ? 2 
ATOM   6470  C CG    . PRO B 1 374 ? 26.675  -21.795 19.374  1.000 24.435  0 374 PRO BBB CG    1 ? 2 
ATOM   6471  C CD    . PRO B 1 374 ? 26.718  -23.211 18.829  1.000 24.590  0 374 PRO BBB CD    1 ? 2 
ATOM   6472  N N     . THR B 1 375 ? 28.955  -20.179 16.292  1.000 29.207  0 375 THR BBB N     1 ? 2 
ATOM   6473  C CA    . THR B 1 375 ? 30.339  -19.710 16.090  1.000 29.865  0 375 THR BBB CA    1 ? 2 
ATOM   6474  C C     . THR B 1 375 ? 30.242  -18.201 15.974  1.000 29.392  0 375 THR BBB C     1 ? 2 
ATOM   6475  O O     . THR B 1 375 ? 29.194  -17.725 15.537  1.000 32.206  0 375 THR BBB O     1 ? 2 
ATOM   6476  C CB    . THR B 1 375 ? 31.002  -20.414 14.903  1.000 31.605  0 375 THR BBB CB    1 ? 2 
ATOM   6477  O OG1   . THR B 1 375 ? 32.261  -19.794 14.665  1.000 37.304  0 375 THR BBB OG1   1 ? 2 
ATOM   6478  C CG2   . THR B 1 375 ? 30.196  -20.325 13.634  1.000 33.466  0 375 THR BBB CG2   1 ? 2 
ATOM   6479  N N     . THR B 1 376 ? 31.260  -17.492 16.430  1.000 27.925  0 376 THR BBB N     1 ? 2 
ATOM   6480  C CA    . THR B 1 376 ? 31.442  -16.063 16.127  1.000 26.826  0 376 THR BBB CA    1 ? 2 
ATOM   6481  C C     . THR B 1 376 ? 32.846  -15.840 15.564  1.000 26.190  0 376 THR BBB C     1 ? 2 
ATOM   6482  O O     . THR B 1 376 ? 33.797  -16.388 16.103  1.000 24.314  0 376 THR BBB O     1 ? 2 
ATOM   6483  C CB    . THR B 1 376 ? 31.208  -15.166 17.338  1.000 26.575  0 376 THR BBB CB    1 ? 2 
ATOM   6484  O OG1   . THR B 1 376 ? 29.830  -15.158 17.659  1.000 25.765  0 376 THR BBB OG1   1 ? 2 
ATOM   6485  C CG2   . THR B 1 376 ? 31.620  -13.739 17.053  1.000 28.354  0 376 THR BBB CG2   1 ? 2 
ATOM   6486  N N     . VAL B 1 377 ? 32.914  -15.040 14.496  1.000 26.575  0 377 VAL BBB N     1 ? 2 
ATOM   6487  C CA    . VAL B 1 377 ? 34.175  -14.576 13.869  1.000 25.867  0 377 VAL BBB CA    1 ? 2 
ATOM   6488  C C     . VAL B 1 377 ? 34.423  -13.177 14.421  1.000 25.536  0 377 VAL BBB C     1 ? 2 
ATOM   6489  O O     . VAL B 1 377 ? 33.507  -12.339 14.288  1.000 26.002  0 377 VAL BBB O     1 ? 2 
ATOM   6490  C CB    . VAL B 1 377 ? 34.041  -14.601 12.348  1.000 27.353  0 377 VAL BBB CB    1 ? 2 
ATOM   6491  C CG1   . VAL B 1 377 ? 35.242  -13.949 11.662  1.000 28.524  0 377 VAL BBB CG1   1 ? 2 
ATOM   6492  C CG2   . VAL B 1 377 ? 33.784  -16.017 11.857  1.000 27.929  0 377 VAL BBB CG2   1 ? 2 
ATOM   6493  N N     . PHE B 1 378 ? 35.567  -12.952 15.080  1.000 24.005  0 378 PHE BBB N     1 ? 2 
ATOM   6494  C CA    . PHE B 1 378 ? 35.847  -11.666 15.761  1.000 23.930  0 378 PHE BBB CA    1 ? 2 
ATOM   6495  C C     . PHE B 1 378 ? 36.579  -10.715 14.810  1.000 24.048  0 378 PHE BBB C     1 ? 2 
ATOM   6496  O O     . PHE B 1 378 ? 37.676  -10.231 15.138  1.000 24.924  0 378 PHE BBB O     1 ? 2 
ATOM   6497  C CB    . PHE B 1 378 ? 36.551  -11.912 17.085  1.000 22.892  0 378 PHE BBB CB    1 ? 2 
ATOM   6498  C CG    . PHE B 1 378 ? 35.666  -12.619 18.072  1.000 22.444  0 378 PHE BBB CG    1 ? 2 
ATOM   6499  C CD1   . PHE B 1 378 ? 34.776  -11.907 18.865  1.000 22.230  0 378 PHE BBB CD1   1 ? 2 
ATOM   6500  C CD2   . PHE B 1 378 ? 35.685  -14.006 18.166  1.000 23.131  0 378 PHE BBB CD2   1 ? 2 
ATOM   6501  C CE1   . PHE B 1 378 ? 33.967  -12.556 19.783  1.000 22.466  0 378 PHE BBB CE1   1 ? 2 
ATOM   6502  C CE2   . PHE B 1 378 ? 34.854  -14.662 19.076  1.000 22.268  0 378 PHE BBB CE2   1 ? 2 
ATOM   6503  C CZ    . PHE B 1 378 ? 33.997  -13.938 19.867  1.000 22.181  0 378 PHE BBB CZ    1 ? 2 
ATOM   6504  N N     . THR B 1 379 ? 35.920  -10.390 13.707  1.000 24.195  0 379 THR BBB N     1 ? 2 
ATOM   6505  C CA    . THR B 1 379 ? 36.384  -9.381  12.737  1.000 25.962  0 379 THR BBB CA    1 ? 2 
ATOM   6506  C C     . THR B 1 379 ? 35.996  -8.003  13.272  1.000 27.009  0 379 THR BBB C     1 ? 2 
ATOM   6507  O O     . THR B 1 379 ? 35.197  -7.910  14.195  1.000 26.612  0 379 THR BBB O     1 ? 2 
ATOM   6508  C CB    . THR B 1 379 ? 35.870  -9.736  11.339  1.000 26.134  0 379 THR BBB CB    1 ? 2 
ATOM   6509  O OG1   . THR B 1 379 ? 34.577  -10.319 11.476  1.000 25.711  0 379 THR BBB OG1   1 ? 2 
ATOM   6510  C CG2   . THR B 1 379 ? 36.770  -10.730 10.655  1.000 25.999  0 379 THR BBB CG2   1 ? 2 
ATOM   6511  N N     . PRO B 1 380 ? 36.564  -6.905  12.727  1.000 27.826  0 380 PRO BBB N     1 ? 2 
ATOM   6512  C CA    . PRO B 1 380 ? 36.320  -5.551  13.229  1.000 28.432  0 380 PRO BBB CA    1 ? 2 
ATOM   6513  C C     . PRO B 1 380 ? 34.832  -5.236  13.451  1.000 29.323  0 380 PRO BBB C     1 ? 2 
ATOM   6514  O O     . PRO B 1 380 ? 34.544  -4.578  14.393  1.000 32.143  0 380 PRO BBB O     1 ? 2 
ATOM   6515  C CB    . PRO B 1 380 ? 36.945  -4.655  12.150  1.000 28.648  0 380 PRO BBB CB    1 ? 2 
ATOM   6516  C CG    . PRO B 1 380 ? 38.090  -5.505  11.654  1.000 28.969  0 380 PRO BBB CG    1 ? 2 
ATOM   6517  C CD    . PRO B 1 380 ? 37.517  -6.912  11.608  1.000 28.719  0 380 PRO BBB CD    1 ? 2 
ATOM   6518  N N     . ILE B 1 381 ? 33.942  -5.724  12.600  1.000 29.428  0 381 ILE BBB N     1 ? 2 
ATOM   6519  C CA    . ILE B 1 381 ? 32.534  -6.037  12.970  1.000 28.393  0 381 ILE BBB CA    1 ? 2 
ATOM   6520  C C     . ILE B 1 381 ? 32.489  -7.565  13.007  1.000 26.738  0 381 ILE BBB C     1 ? 2 
ATOM   6521  O O     . ILE B 1 381 ? 33.042  -8.205  12.088  1.000 26.650  0 381 ILE BBB O     1 ? 2 
ATOM   6522  C CB    . ILE B 1 381 ? 31.478  -5.456  11.993  1.000 30.970  0 381 ILE BBB CB    1 ? 2 
ATOM   6523  C CG1   . ILE B 1 381 ? 31.764  -5.840  10.545  1.000 31.260  0 381 ILE BBB CG1   1 ? 2 
ATOM   6524  C CG2   . ILE B 1 381 ? 31.337  -3.950  12.114  1.000 33.269  0 381 ILE BBB CG2   1 ? 2 
ATOM   6525  C CD1   . ILE B 1 381 ? 30.774  -5.282  9.556   1.000 32.549  0 381 ILE BBB CD1   1 ? 2 
ATOM   6526  N N     . GLU B 1 382 ? 31.876  -8.112  14.042  1.000 24.592  0 382 GLU BBB N     1 ? 2 
ATOM   6527  C CA    . GLU B 1 382 ? 31.883  -9.553  14.363  1.000 23.804  0 382 GLU BBB CA    1 ? 2 
ATOM   6528  C C     . GLU B 1 382 ? 30.752  -10.211 13.594  1.000 23.654  0 382 GLU BBB C     1 ? 2 
ATOM   6529  O O     . GLU B 1 382 ? 29.804  -9.499  13.197  1.000 24.748  0 382 GLU BBB O     1 ? 2 
ATOM   6530  C CB    . GLU B 1 382 ? 31.714  -9.759  15.874  1.000 23.155  0 382 GLU BBB CB    1 ? 2 
ATOM   6531  C CG    . GLU B 1 382 ? 32.617  -8.844  16.690  1.000 23.740  0 382 GLU BBB CG    1 ? 2 
ATOM   6532  C CD    . GLU B 1 382 ? 32.566  -9.018  18.186  1.000 24.197  0 382 GLU BBB CD    1 ? 2 
ATOM   6533  O OE1   . GLU B 1 382 ? 31.559  -9.617  18.724  1.000 24.786  0 382 GLU BBB OE1   1 ? 2 
ATOM   6534  O OE2   . GLU B 1 382 ? 33.541  -8.583  18.800  1.000 25.492  0 382 GLU BBB OE2   1 ? 2 
ATOM   6535  N N     . TYR B 1 383 ? 30.807  -11.525 13.448  1.000 23.146  0 383 TYR BBB N     1 ? 2 
ATOM   6536  C CA    . TYR B 1 383 ? 29.750  -12.291 12.743  1.000 22.714  0 383 TYR BBB CA    1 ? 2 
ATOM   6537  C C     . TYR B 1 383 ? 29.468  -13.545 13.550  1.000 21.519  0 383 TYR BBB C     1 ? 2 
ATOM   6538  O O     . TYR B 1 383 ? 30.363  -14.383 13.737  1.000 20.872  0 383 TYR BBB O     1 ? 2 
ATOM   6539  C CB    . TYR B 1 383 ? 30.174  -12.573 11.299  1.000 23.895  0 383 TYR BBB CB    1 ? 2 
ATOM   6540  C CG    . TYR B 1 383 ? 29.312  -13.592 10.595  1.000 24.733  0 383 TYR BBB CG    1 ? 2 
ATOM   6541  C CD1   . TYR B 1 383 ? 27.932  -13.543 10.727  1.000 24.168  0 383 TYR BBB CD1   1 ? 2 
ATOM   6542  C CD2   . TYR B 1 383 ? 29.854  -14.586 9.806   1.000 25.629  0 383 TYR BBB CD2   1 ? 2 
ATOM   6543  C CE1   . TYR B 1 383 ? 27.129  -14.487 10.137  1.000 23.946  0 383 TYR BBB CE1   1 ? 2 
ATOM   6544  C CE2   . TYR B 1 383 ? 29.046  -15.537 9.194   1.000 26.124  0 383 TYR BBB CE2   1 ? 2 
ATOM   6545  C CZ    . TYR B 1 383 ? 27.674  -15.491 9.383   1.000 24.371  0 383 TYR BBB CZ    1 ? 2 
ATOM   6546  O OH    . TYR B 1 383 ? 26.850  -16.395 8.789   1.000 24.643  0 383 TYR BBB OH    1 ? 2 
ATOM   6547  N N     . GLY B 1 384 ? 28.259  -13.634 14.048  1.000 21.195  0 384 GLY BBB N     1 ? 2 
ATOM   6548  C CA    . GLY B 1 384 ? 27.798  -14.769 14.832  1.000 22.262  0 384 GLY BBB CA    1 ? 2 
ATOM   6549  C C     . GLY B 1 384 ? 26.686  -15.460 14.070  1.000 24.265  0 384 GLY BBB C     1 ? 2 
ATOM   6550  O O     . GLY B 1 384 ? 25.825  -14.726 13.459  1.000 24.792  0 384 GLY BBB O     1 ? 2 
ATOM   6551  N N     . HIS B 1 385 ? 26.683  -16.798 14.080  1.000 23.563  0 385 HIS BBB N     1 ? 2 
ATOM   6552  C CA    . HIS B 1 385 ? 25.606  -17.561 13.409  1.000 24.899  0 385 HIS BBB CA    1 ? 2 
ATOM   6553  C C     . HIS B 1 385 ? 25.436  -18.906 14.092  1.000 24.663  0 385 HIS BBB C     1 ? 2 
ATOM   6554  O O     . HIS B 1 385 ? 26.381  -19.354 14.755  1.000 25.155  0 385 HIS BBB O     1 ? 2 
ATOM   6555  C CB    . HIS B 1 385 ? 25.862  -17.701 11.902  1.000 24.341  0 385 HIS BBB CB    1 ? 2 
ATOM   6556  C CG    . HIS B 1 385 ? 26.684  -18.888 11.519  1.000 24.950  0 385 HIS BBB CG    1 ? 2 
ATOM   6557  N ND1   . HIS B 1 385 ? 26.130  -20.074 11.085  1.000 25.621  0 385 HIS BBB ND1   1 ? 2 
ATOM   6558  C CD2   . HIS B 1 385 ? 28.029  -19.059 11.472  1.000 24.228  0 385 HIS BBB CD2   1 ? 2 
ATOM   6559  C CE1   . HIS B 1 385 ? 27.103  -20.912 10.787  1.000 25.407  0 385 HIS BBB CE1   1 ? 2 
ATOM   6560  N NE2   . HIS B 1 385 ? 28.282  -20.317 11.062  1.000 23.929  0 385 HIS BBB NE2   1 ? 2 
ATOM   6561  N N     . VAL B 1 386 ? 24.264  -19.489 13.913  1.000 25.091  0 386 VAL BBB N     1 ? 2 
ATOM   6562  C CA    . VAL B 1 386 ? 24.000  -20.930 14.148  1.000 26.066  0 386 VAL BBB CA    1 ? 2 
ATOM   6563  C C     . VAL B 1 386 ? 23.062  -21.420 13.042  1.000 27.550  0 386 VAL BBB C     1 ? 2 
ATOM   6564  O O     . VAL B 1 386 ? 22.228  -20.605 12.524  1.000 28.599  0 386 VAL BBB O     1 ? 2 
ATOM   6565  C CB    . VAL B 1 386 ? 23.397  -21.185 15.528  1.000 25.427  0 386 VAL BBB CB    1 ? 2 
ATOM   6566  C CG1   . VAL B 1 386 ? 21.969  -20.626 15.628  1.000 25.987  0 386 VAL BBB CG1   1 ? 2 
ATOM   6567  C CG2   . VAL B 1 386 ? 23.448  -22.654 15.883  1.000 25.072  0 386 VAL BBB CG2   1 ? 2 
ATOM   6568  N N     . GLY B 1 387 ? 23.219  -22.690 12.702  1.000 28.397  0 387 GLY BBB N     1 ? 2 
ATOM   6569  C CA    . GLY B 1 387 ? 22.422  -23.363 11.674  1.000 30.046  0 387 GLY BBB CA    1 ? 2 
ATOM   6570  C C     . GLY B 1 387 ? 22.896  -23.000 10.298  1.000 30.682  0 387 GLY BBB C     1 ? 2 
ATOM   6571  O O     . GLY B 1 387 ? 24.117  -22.778 10.140  1.000 30.071  0 387 GLY BBB O     1 ? 2 
ATOM   6572  N N     . LEU B 1 388 ? 21.962  -22.924 9.346   1.000 32.508  0 388 LEU BBB N     1 ? 2 
ATOM   6573  C CA    . LEU B 1 388 ? 22.274  -22.957 7.894   1.000 34.094  0 388 LEU BBB CA    1 ? 2 
ATOM   6574  C C     . LEU B 1 388 ? 22.411  -21.535 7.367   1.000 35.473  0 388 LEU BBB C     1 ? 2 
ATOM   6575  O O     . LEU B 1 388 ? 21.615  -20.652 7.779   1.000 37.449  0 388 LEU BBB O     1 ? 2 
ATOM   6576  C CB    . LEU B 1 388 ? 21.176  -23.728 7.151   1.000 35.217  0 388 LEU BBB CB    1 ? 2 
ATOM   6577  C CG    . LEU B 1 388 ? 20.850  -25.119 7.724   1.000 35.048  0 388 LEU BBB CG    1 ? 2 
ATOM   6578  C CD1   . LEU B 1 388 ? 19.612  -25.735 7.068   1.000 34.458  0 388 LEU BBB CD1   1 ? 2 
ATOM   6579  C CD2   . LEU B 1 388 ? 22.061  -26.043 7.626   1.000 34.488  0 388 LEU BBB CD2   1 ? 2 
ATOM   6580  N N     . SER B 1 389 ? 23.396  -21.335 6.495   1.000 36.640  0 389 SER BBB N     1 ? 2 
ATOM   6581  C CA    . SER B 1 389 ? 23.490  -20.165 5.586   1.000 38.775  0 389 SER BBB CA    1 ? 2 
ATOM   6582  C C     . SER B 1 389 ? 22.248  -20.147 4.689   1.000 39.793  0 389 SER BBB C     1 ? 2 
ATOM   6583  O O     . SER B 1 389 ? 21.553  -21.197 4.614   1.000 38.408  0 389 SER BBB O     1 ? 2 
ATOM   6584  C CB    . SER B 1 389 ? 24.742  -20.229 4.784   1.000 38.424  0 389 SER BBB CB    1 ? 2 
ATOM   6585  O OG    . SER B 1 389 ? 24.794  -21.450 4.080   1.000 41.589  0 389 SER BBB OG    1 ? 2 
ATOM   6586  N N     . SER B 1 390 ? 21.959  -19.007 4.059   1.000 40.932  0 390 SER BBB N     1 ? 2 
ATOM   6587  C CA    . SER B 1 390 ? 21.009  -18.912 2.915   1.000 43.024  0 390 SER BBB CA    1 ? 2 
ATOM   6588  C C     . SER B 1 390 ? 21.306  -20.037 1.909   1.000 42.009  0 390 SER BBB C     1 ? 2 
ATOM   6589  O O     . SER B 1 390 ? 20.369  -20.765 1.560   1.000 40.488  0 390 SER BBB O     1 ? 2 
ATOM   6590  C CB    . SER B 1 390 ? 21.065  -17.525 2.278   1.000 45.356  0 390 SER BBB CB    1 ? 2 
ATOM   6591  O OG    . SER B 1 390 ? 20.772  -16.507 3.238   1.000 45.399  0 390 SER BBB OG    1 ? 2 
ATOM   6592  N N     . GLU B 1 391 ? 22.587  -20.221 1.544   1.000 41.670  0 391 GLU BBB N     1 ? 2 
ATOM   6593  C CA    . GLU B 1 391 ? 23.034  -21.199 0.512   1.000 42.632  0 391 GLU BBB CA    1 ? 2 
ATOM   6594  C C     . GLU B 1 391 ? 22.682  -22.625 0.965   1.000 41.002  0 391 GLU BBB C     1 ? 2 
ATOM   6595  O O     . GLU B 1 391 ? 22.022  -23.349 0.165   1.000 45.168  0 391 GLU BBB O     1 ? 2 
ATOM   6596  C CB    . GLU B 1 391 ? 24.532  -21.048 0.188   1.000 43.059  0 391 GLU BBB CB    1 ? 2 
ATOM   6597  C CG    . GLU B 1 391 ? 24.898  -19.766 -0.564  1.000 42.710  0 391 GLU BBB CG    1 ? 2 
ATOM   6598  C CD    . GLU B 1 391 ? 24.845  -18.481 0.264   1.000 45.010  0 391 GLU BBB CD    1 ? 2 
ATOM   6599  O OE1   . GLU B 1 391 ? 25.285  -18.492 1.428   1.000 42.844  0 391 GLU BBB OE1   1 ? 2 
ATOM   6600  O OE2   . GLU B 1 391 ? 24.335  -17.458 -0.249  1.000 48.539  0 391 GLU BBB OE2   1 ? 2 
ATOM   6601  N N     . ALA B 1 392 ? 23.087  -23.041 2.166   1.000 37.344  0 392 ALA BBB N     1 ? 2 
ATOM   6602  C CA    . ALA B 1 392 ? 22.814  -24.408 2.672   1.000 37.861  0 392 ALA BBB CA    1 ? 2 
ATOM   6603  C C     . ALA B 1 392 ? 21.292  -24.606 2.849   1.000 39.362  0 392 ALA BBB C     1 ? 2 
ATOM   6604  O O     . ALA B 1 392 ? 20.814  -25.754 2.718   1.000 40.605  0 392 ALA BBB O     1 ? 2 
ATOM   6605  C CB    . ALA B 1 392 ? 23.570  -24.675 3.958   1.000 36.833  0 392 ALA BBB CB    1 ? 2 
ATOM   6606  N N     . ALA B 1 393 ? 20.539  -23.534 3.131   1.000 39.327  0 393 ALA BBB N     1 ? 2 
ATOM   6607  C CA    . ALA B 1 393 ? 19.076  -23.593 3.356   1.000 39.163  0 393 ALA BBB CA    1 ? 2 
ATOM   6608  C C     . ALA B 1 393 ? 18.359  -23.802 2.019   1.000 38.273  0 393 ALA BBB C     1 ? 2 
ATOM   6609  O O     . ALA B 1 393 ? 17.514  -24.693 1.934   1.000 34.555  0 393 ALA BBB O     1 ? 2 
ATOM   6610  C CB    . ALA B 1 393 ? 18.600  -22.350 4.054   1.000 38.975  0 393 ALA BBB CB    1 ? 2 
ATOM   6611  N N     . ILE B 1 394 ? 18.745  -23.021 1.011   1.000 42.065  0 394 ILE BBB N     1 ? 2 
ATOM   6612  C CA    . ILE B 1 394 ? 18.217  -23.115 -0.383  1.000 45.092  0 394 ILE BBB CA    1 ? 2 
ATOM   6613  C C     . ILE B 1 394 ? 18.530  -24.514 -0.945  1.000 48.361  0 394 ILE BBB C     1 ? 2 
ATOM   6614  O O     . ILE B 1 394 ? 17.571  -25.177 -1.401  1.000 47.900  0 394 ILE BBB O     1 ? 2 
ATOM   6615  C CB    . ILE B 1 394 ? 18.731  -21.937 -1.238  1.000 45.633  0 394 ILE BBB CB    1 ? 2 
ATOM   6616  C CG1   . ILE B 1 394 ? 17.983  -20.651 -0.848  1.000 44.748  0 394 ILE BBB CG1   1 ? 2 
ATOM   6617  C CG2   . ILE B 1 394 ? 18.596  -22.236 -2.731  1.000 47.635  0 394 ILE BBB CG2   1 ? 2 
ATOM   6618  C CD1   . ILE B 1 394 ? 18.499  -19.372 -1.481  1.000 44.566  0 394 ILE BBB CD1   1 ? 2 
ATOM   6619  N N     . ALA B 1 395 ? 19.781  -24.988 -0.817  1.000 50.654  0 395 ALA BBB N     1 ? 2 
ATOM   6620  C CA    . ALA B 1 395 ? 20.235  -26.321 -1.284  1.000 52.071  0 395 ALA BBB CA    1 ? 2 
ATOM   6621  C C     . ALA B 1 395 ? 19.380  -27.430 -0.650  1.000 52.408  0 395 ALA BBB C     1 ? 2 
ATOM   6622  O O     . ALA B 1 395 ? 19.058  -28.387 -1.375  1.000 53.797  0 395 ALA BBB O     1 ? 2 
ATOM   6623  C CB    . ALA B 1 395 ? 21.716  -26.533 -0.984  1.000 51.821  0 395 ALA BBB CB    1 ? 2 
ATOM   6624  N N     . LYS B 1 396 ? 19.065  -27.347 0.652   1.000 51.093  0 396 LYS BBB N     1 ? 2 
ATOM   6625  C CA    . LYS B 1 396 ? 18.462  -28.477 1.407   1.000 51.344  0 396 LYS BBB CA    1 ? 2 
ATOM   6626  C C     . LYS B 1 396 ? 16.941  -28.517 1.206   1.000 52.390  0 396 LYS BBB C     1 ? 2 
ATOM   6627  O O     . LYS B 1 396 ? 16.413  -29.629 1.077   1.000 53.991  0 396 LYS BBB O     1 ? 2 
ATOM   6628  C CB    . LYS B 1 396 ? 18.823  -28.392 2.888   1.000 50.651  0 396 LYS BBB CB    1 ? 2 
ATOM   6629  C CG    . LYS B 1 396 ? 18.314  -29.528 3.758   1.000 52.071  0 396 LYS BBB CG    1 ? 2 
ATOM   6630  C CD    . LYS B 1 396 ? 18.558  -29.273 5.229   1.000 52.441  0 396 LYS BBB CD    1 ? 2 
ATOM   6631  C CE    . LYS B 1 396 ? 17.827  -30.243 6.133   1.000 52.842  0 396 LYS BBB CE    1 ? 2 
ATOM   6632  N NZ    . LYS B 1 396 ? 18.491  -31.563 6.119   1.000 53.517  0 396 LYS BBB NZ    1 ? 2 
ATOM   6633  N N     . TYR B 1 397 ? 16.255  -27.370 1.219   1.000 52.994  0 397 TYR BBB N     1 ? 2 
ATOM   6634  C CA    . TYR B 1 397 ? 14.762  -27.274 1.281   1.000 52.175  0 397 TYR BBB CA    1 ? 2 
ATOM   6635  C C     . TYR B 1 397 ? 14.171  -26.767 -0.047  1.000 52.693  0 397 TYR BBB C     1 ? 2 
ATOM   6636  O O     . TYR B 1 397 ? 12.937  -26.864 -0.199  1.000 51.988  0 397 TYR BBB O     1 ? 2 
ATOM   6637  C CB    . TYR B 1 397 ? 14.327  -26.373 2.448   1.000 49.667  0 397 TYR BBB CB    1 ? 2 
ATOM   6638  C CG    . TYR B 1 397 ? 14.613  -26.955 3.808   1.000 47.929  0 397 TYR BBB CG    1 ? 2 
ATOM   6639  C CD1   . TYR B 1 397 ? 13.865  -27.998 4.317   1.000 47.258  0 397 TYR BBB CD1   1 ? 2 
ATOM   6640  C CD2   . TYR B 1 397 ? 15.646  -26.470 4.584   1.000 46.960  0 397 TYR BBB CD2   1 ? 2 
ATOM   6641  C CE1   . TYR B 1 397 ? 14.125  -28.537 5.566   1.000 47.415  0 397 TYR BBB CE1   1 ? 2 
ATOM   6642  C CE2   . TYR B 1 397 ? 15.928  -27.005 5.833   1.000 46.818  0 397 TYR BBB CE2   1 ? 2 
ATOM   6643  C CZ    . TYR B 1 397 ? 15.155  -28.034 6.342   1.000 47.167  0 397 TYR BBB CZ    1 ? 2 
ATOM   6644  O OH    . TYR B 1 397 ? 15.453  -28.594 7.562   1.000 43.765  0 397 TYR BBB OH    1 ? 2 
ATOM   6645  N N     . GLY B 1 398 ? 15.004  -26.229 -0.947  1.000 52.987  0 398 GLY BBB N     1 ? 2 
ATOM   6646  C CA    . GLY B 1 398 ? 14.581  -25.580 -2.199  1.000 54.339  0 398 GLY BBB CA    1 ? 2 
ATOM   6647  C C     . GLY B 1 398 ? 14.277  -24.100 -2.010  1.000 56.451  0 398 GLY BBB C     1 ? 2 
ATOM   6648  O O     . GLY B 1 398 ? 13.727  -23.740 -0.955  1.000 56.946  0 398 GLY BBB O     1 ? 2 
ATOM   6649  N N     . GLU B 1 399 ? 14.590  -23.287 -3.028  1.000 61.310  0 399 GLU BBB N     1 ? 2 
ATOM   6650  C CA    . GLU B 1 399 ? 14.448  -21.809 -3.072  1.000 63.586  0 399 GLU BBB CA    1 ? 2 
ATOM   6651  C C     . GLU B 1 399 ? 13.050  -21.382 -2.615  1.000 63.914  0 399 GLU BBB C     1 ? 2 
ATOM   6652  O O     . GLU B 1 399 ? 12.941  -20.318 -1.984  1.000 65.110  0 399 GLU BBB O     1 ? 2 
ATOM   6653  C CB    . GLU B 1 399 ? 14.717  -21.334 -4.503  1.000 70.123  0 399 GLU BBB CB    1 ? 2 
ATOM   6654  C CG    . GLU B 1 399 ? 14.629  -19.827 -4.692  1.000 76.924  0 399 GLU BBB CG    1 ? 2 
ATOM   6655  C CD    . GLU B 1 399 ? 15.822  -19.054 -4.152  1.000 81.301  0 399 GLU BBB CD    1 ? 2 
ATOM   6656  O OE1   . GLU B 1 399 ? 16.960  -19.443 -4.490  1.000 85.859  0 399 GLU BBB OE1   1 ? 2 
ATOM   6657  O OE2   . GLU B 1 399 ? 15.615  -18.071 -3.391  1.000 83.987  0 399 GLU BBB OE2   1 ? 2 
ATOM   6658  N N     . ASP B 1 400 ? 12.013  -22.154 -2.941  1.000 63.452  0 400 ASP BBB N     1 ? 2 
ATOM   6659  C CA    . ASP B 1 400 ? 10.600  -21.719 -2.783  1.000 66.055  0 400 ASP BBB CA    1 ? 2 
ATOM   6660  C C     . ASP B 1 400 ? 10.094  -22.004 -1.371  1.000 59.128  0 400 ASP BBB C     1 ? 2 
ATOM   6661  O O     . ASP B 1 400 ? 9.074   -21.410 -0.997  1.000 55.506  0 400 ASP BBB O     1 ? 2 
ATOM   6662  C CB    . ASP B 1 400 ? 9.682   -22.407 -3.794  1.000 72.424  0 400 ASP BBB CB    1 ? 2 
ATOM   6663  C CG    . ASP B 1 400 ? 9.549   -21.621 -5.083  1.000 78.829  0 400 ASP BBB CG    1 ? 2 
ATOM   6664  O OD1   . ASP B 1 400 ? 10.450  -20.810 -5.392  1.000 82.731  0 400 ASP BBB OD1   1 ? 2 
ATOM   6665  O OD2   . ASP B 1 400 ? 8.542   -21.814 -5.766  1.000 87.433  0 400 ASP BBB OD2   1 ? 2 
ATOM   6666  N N     . ASP B 1 401 ? 10.743  -22.909 -0.644  1.000 56.603  0 401 ASP BBB N     1 ? 2 
ATOM   6667  C CA    . ASP B 1 401 ? 10.356  -23.245 0.748   1.000 56.818  0 401 ASP BBB CA    1 ? 2 
ATOM   6668  C C     . ASP B 1 401 ? 11.203  -22.400 1.729   1.000 54.740  0 401 ASP BBB C     1 ? 2 
ATOM   6669  O O     . ASP B 1 401 ? 11.116  -22.661 2.944   1.000 58.316  0 401 ASP BBB O     1 ? 2 
ATOM   6670  C CB    . ASP B 1 401 ? 10.460  -24.758 0.939   1.000 56.823  0 401 ASP BBB CB    1 ? 2 
ATOM   6671  C CG    . ASP B 1 401 ? 9.614   -25.332 2.053   1.000 58.770  0 401 ASP BBB CG    1 ? 2 
ATOM   6672  O OD1   . ASP B 1 401 ? 8.644   -24.668 2.469   1.000 59.557  0 401 ASP BBB OD1   1 ? 2 
ATOM   6673  O OD2   . ASP B 1 401 ? 9.937   -26.454 2.492   1.000 59.602  0 401 ASP BBB OD2   1 ? 2 
ATOM   6674  N N     . ILE B 1 402 ? 11.963  -21.415 1.232   1.000 51.224  0 402 ILE BBB N     1 ? 2 
ATOM   6675  C CA    . ILE B 1 402 ? 12.894  -20.563 2.039   1.000 49.193  0 402 ILE BBB CA    1 ? 2 
ATOM   6676  C C     . ILE B 1 402 ? 12.440  -19.099 2.015   1.000 47.862  0 402 ILE BBB C     1 ? 2 
ATOM   6677  O O     . ILE B 1 402 ? 12.296  -18.527 0.934   1.000 45.950  0 402 ILE BBB O     1 ? 2 
ATOM   6678  C CB    . ILE B 1 402 ? 14.356  -20.691 1.551   1.000 46.833  0 402 ILE BBB CB    1 ? 2 
ATOM   6679  C CG1   . ILE B 1 402 ? 14.948  -22.062 1.879   1.000 46.562  0 402 ILE BBB CG1   1 ? 2 
ATOM   6680  C CG2   . ILE B 1 402 ? 15.222  -19.560 2.084   1.000 46.956  0 402 ILE BBB CG2   1 ? 2 
ATOM   6681  C CD1   . ILE B 1 402 ? 14.726  -22.506 3.295   1.000 45.404  0 402 ILE BBB CD1   1 ? 2 
ATOM   6682  N N     . GLU B 1 403 ? 12.313  -18.501 3.200   1.000 48.709  0 403 GLU BBB N     1 ? 2 
ATOM   6683  C CA    . GLU B 1 403 ? 12.201  -17.034 3.357   1.000 48.808  0 403 GLU BBB CA    1 ? 2 
ATOM   6684  C C     . GLU B 1 403 ? 13.417  -16.538 4.127   1.000 47.148  0 403 GLU BBB C     1 ? 2 
ATOM   6685  O O     . GLU B 1 403 ? 13.809  -17.176 5.111   1.000 45.608  0 403 GLU BBB O     1 ? 2 
ATOM   6686  C CB    . GLU B 1 403 ? 10.878  -16.652 4.042   1.000 51.650  0 403 GLU BBB CB    1 ? 2 
ATOM   6687  C CG    . GLU B 1 403 ? 10.318  -15.305 3.570   1.000 53.238  0 403 GLU BBB CG    1 ? 2 
ATOM   6688  C CD    . GLU B 1 403 ? 9.769   -15.298 2.155   1.000 53.711  0 403 GLU BBB CD    1 ? 2 
ATOM   6689  O OE1   . GLU B 1 403 ? 8.818   -16.059 1.907   1.000 57.212  0 403 GLU BBB OE1   1 ? 2 
ATOM   6690  O OE2   . GLU B 1 403 ? 10.301  -14.540 1.312   1.000 51.537  0 403 GLU BBB OE2   1 ? 2 
ATOM   6691  N N     . GLU B 1 404 ? 13.997  -15.435 3.661   1.000 47.531  0 404 GLU BBB N     1 ? 2 
ATOM   6692  C CA    . GLU B 1 404 ? 15.073  -14.690 4.346   1.000 45.769  0 404 GLU BBB CA    1 ? 2 
ATOM   6693  C C     . GLU B 1 404 ? 14.499  -13.331 4.755   1.000 44.844  0 404 GLU BBB C     1 ? 2 
ATOM   6694  O O     . GLU B 1 404 ? 14.125  -12.522 3.884   1.000 45.784  0 404 GLU BBB O     1 ? 2 
ATOM   6695  C CB    . GLU B 1 404 ? 16.297  -14.570 3.453   1.000 46.679  0 404 GLU BBB CB    1 ? 2 
ATOM   6696  C CG    . GLU B 1 404 ? 16.771  -15.913 2.934   1.000 49.387  0 404 GLU BBB CG    1 ? 2 
ATOM   6697  C CD    . GLU B 1 404 ? 17.848  -15.816 1.871   1.000 52.655  0 404 GLU BBB CD    1 ? 2 
ATOM   6698  O OE1   . GLU B 1 404 ? 18.746  -14.945 2.018   1.000 49.826  0 404 GLU BBB OE1   1 ? 2 
ATOM   6699  O OE2   . GLU B 1 404 ? 17.772  -16.604 0.889   1.000 60.609  0 404 GLU BBB OE2   1 ? 2 
ATOM   6700  N N     . TYR B 1 405 ? 14.392  -13.121 6.070   1.000 41.830  0 405 TYR BBB N     1 ? 2 
ATOM   6701  C CA    . TYR B 1 405 ? 14.024  -11.833 6.682   1.000 38.984  0 405 TYR BBB CA    1 ? 2 
ATOM   6702  C C     . TYR B 1 405 ? 15.320  -11.185 7.151   1.000 37.797  0 405 TYR BBB C     1 ? 2 
ATOM   6703  O O     . TYR B 1 405 ? 16.149  -11.880 7.752   1.000 36.943  0 405 TYR BBB O     1 ? 2 
ATOM   6704  C CB    . TYR B 1 405 ? 13.052  -12.073 7.826   1.000 39.223  0 405 TYR BBB CB    1 ? 2 
ATOM   6705  C CG    . TYR B 1 405 ? 11.682  -12.576 7.431   1.000 39.786  0 405 TYR BBB CG    1 ? 2 
ATOM   6706  C CD1   . TYR B 1 405 ? 10.631  -11.700 7.223   1.000 39.631  0 405 TYR BBB CD1   1 ? 2 
ATOM   6707  C CD2   . TYR B 1 405 ? 11.412  -13.934 7.365   1.000 40.403  0 405 TYR BBB CD2   1 ? 2 
ATOM   6708  C CE1   . TYR B 1 405 ? 9.351   -12.151 6.955   1.000 41.403  0 405 TYR BBB CE1   1 ? 2 
ATOM   6709  C CE2   . TYR B 1 405 ? 10.136  -14.406 7.104   1.000 40.927  0 405 TYR BBB CE2   1 ? 2 
ATOM   6710  C CZ    . TYR B 1 405 ? 9.102   -13.511 6.856   1.000 41.599  0 405 TYR BBB CZ    1 ? 2 
ATOM   6711  O OH    . TYR B 1 405 ? 7.841   -13.962 6.551   1.000 38.672  0 405 TYR BBB OH    1 ? 2 
ATOM   6712  N N     . LEU B 1 406 ? 15.514  -9.899  6.866   1.000 36.446  0 406 LEU BBB N     1 ? 2 
ATOM   6713  C CA    . LEU B 1 406 ? 16.794  -9.245  7.174   1.000 36.062  0 406 LEU BBB CA    1 ? 2 
ATOM   6714  C C     . LEU B 1 406 ? 16.621  -7.737  7.313   1.000 35.304  0 406 LEU BBB C     1 ? 2 
ATOM   6715  O O     . LEU B 1 406 ? 15.579  -7.179  6.920   1.000 35.221  0 406 LEU BBB O     1 ? 2 
ATOM   6716  C CB    . LEU B 1 406 ? 17.852  -9.653  6.144   1.000 37.847  0 406 LEU BBB CB    1 ? 2 
ATOM   6717  C CG    . LEU B 1 406 ? 17.796  -9.059  4.740   1.000 40.182  0 406 LEU BBB CG    1 ? 2 
ATOM   6718  C CD1   . LEU B 1 406 ? 19.051  -9.459  3.974   1.000 40.723  0 406 LEU BBB CD1   1 ? 2 
ATOM   6719  C CD2   . LEU B 1 406 ? 16.561  -9.527  3.960   1.000 41.802  0 406 LEU BBB CD2   1 ? 2 
ATOM   6720  N N     . SER B 1 407 ? 17.592  -7.142  7.982   1.000 34.204  0 407 SER BBB N     1 ? 2 
ATOM   6721  C CA    . SER B 1 407 ? 17.664  -5.697  8.267   1.000 34.735  0 407 SER BBB CA    1 ? 2 
ATOM   6722  C C     . SER B 1 407 ? 19.151  -5.323  8.403   1.000 35.809  0 407 SER BBB C     1 ? 2 
ATOM   6723  O O     . SER B 1 407 ? 19.908  -6.072  9.039   1.000 34.803  0 407 SER BBB O     1 ? 2 
ATOM   6724  C CB    . SER B 1 407 ? 16.867  -5.370  9.525   1.000 33.547  0 407 SER BBB CB    1 ? 2 
ATOM   6725  O OG    . SER B 1 407 ? 16.962  -3.992  9.792   1.000 33.454  0 407 SER BBB OG    1 ? 2 
ATOM   6726  N N     . GLU B 1 408 ? 19.569  -4.252  7.739   1.000 36.937  0 408 GLU BBB N     1 ? 2 
ATOM   6727  C CA    . GLU B 1 408 ? 20.941  -3.698  7.803   1.000 35.865  0 408 GLU BBB CA    1 ? 2 
ATOM   6728  C C     . GLU B 1 408 ? 20.784  -2.323  8.423   1.000 35.300  0 408 GLU BBB C     1 ? 2 
ATOM   6729  O O     . GLU B 1 408 ? 19.972  -1.534  7.901   1.000 37.483  0 408 GLU BBB O     1 ? 2 
ATOM   6730  C CB    . GLU B 1 408 ? 21.582  -3.590  6.422   1.000 36.230  0 408 GLU BBB CB    1 ? 2 
ATOM   6731  C CG    . GLU B 1 408 ? 23.062  -3.286  6.446   1.000 36.792  0 408 GLU BBB CG    1 ? 2 
ATOM   6732  C CD    . GLU B 1 408 ? 23.727  -3.272  5.078   1.000 39.227  0 408 GLU BBB CD    1 ? 2 
ATOM   6733  O OE1   . GLU B 1 408 ? 23.009  -3.183  4.057   1.000 42.047  0 408 GLU BBB OE1   1 ? 2 
ATOM   6734  O OE2   . GLU B 1 408 ? 24.965  -3.350  5.030   1.000 41.027  0 408 GLU BBB OE2   1 ? 2 
ATOM   6735  N N     . PHE B 1 409 ? 21.514  -2.051  9.490   1.000 34.260  0 409 PHE BBB N     1 ? 2 
ATOM   6736  C CA    . PHE B 1 409 ? 21.327  -0.811  10.282  1.000 32.943  0 409 PHE BBB CA    1 ? 2 
ATOM   6737  C C     . PHE B 1 409 ? 22.590  -0.519  11.063  1.000 32.154  0 409 PHE BBB C     1 ? 2 
ATOM   6738  O O     . PHE B 1 409 ? 23.528  -1.314  11.078  1.000 32.624  0 409 PHE BBB O     1 ? 2 
ATOM   6739  C CB    . PHE B 1 409 ? 20.178  -0.982  11.266  1.000 31.317  0 409 PHE BBB CB    1 ? 2 
ATOM   6740  C CG    . PHE B 1 409 ? 20.406  -2.125  12.222  1.000 29.982  0 409 PHE BBB CG    1 ? 2 
ATOM   6741  C CD1   . PHE B 1 409 ? 20.226  -3.433  11.810  1.000 28.679  0 409 PHE BBB CD1   1 ? 2 
ATOM   6742  C CD2   . PHE B 1 409 ? 20.817  -1.895  13.522  1.000 28.193  0 409 PHE BBB CD2   1 ? 2 
ATOM   6743  C CE1   . PHE B 1 409 ? 20.395  -4.486  12.684  1.000 27.506  0 409 PHE BBB CE1   1 ? 2 
ATOM   6744  C CE2   . PHE B 1 409 ? 21.021  -2.957  14.393  1.000 27.199  0 409 PHE BBB CE2   1 ? 2 
ATOM   6745  C CZ    . PHE B 1 409 ? 20.806  -4.243  13.977  1.000 27.815  0 409 PHE BBB CZ    1 ? 2 
ATOM   6746  N N     . SER B 1 410 ? 22.568  0.610   11.736  1.000 34.365  0 410 SER BBB N     1 ? 2 
ATOM   6747  C CA    . SER B 1 410 ? 23.683  1.058   12.598  1.000 34.565  0 410 SER BBB CA    1 ? 2 
ATOM   6748  C C     . SER B 1 410 ? 23.266  0.929   14.058  1.000 33.312  0 410 SER BBB C     1 ? 2 
ATOM   6749  O O     . SER B 1 410 ? 22.112  1.223   14.366  1.000 34.586  0 410 SER BBB O     1 ? 2 
ATOM   6750  C CB    . SER B 1 410 ? 24.060  2.435   12.254  1.000 35.499  0 410 SER BBB CB    1 ? 2 
ATOM   6751  O OG    . SER B 1 410 ? 24.983  2.895   13.203  1.000 37.946  0 410 SER BBB OG    1 ? 2 
ATOM   6752  N N     . THR B 1 411 ? 24.159  0.439   14.903  1.000 33.218  0 411 THR BBB N     1 ? 2 
ATOM   6753  C CA    . THR B 1 411 ? 24.102  0.631   16.371  1.000 32.500  0 411 THR BBB CA    1 ? 2 
ATOM   6754  C C     . THR B 1 411 ? 23.788  2.107   16.614  1.000 33.252  0 411 THR BBB C     1 ? 2 
ATOM   6755  O O     . THR B 1 411 ? 24.322  2.947   15.857  1.000 31.471  0 411 THR BBB O     1 ? 2 
ATOM   6756  C CB    . THR B 1 411 ? 25.417  0.216   17.035  1.000 33.115  0 411 THR BBB CB    1 ? 2 
ATOM   6757  O OG1   . THR B 1 411 ? 25.653  -1.139  16.657  1.000 32.982  0 411 THR BBB OG1   1 ? 2 
ATOM   6758  C CG2   . THR B 1 411 ? 25.412  0.302   18.547  1.000 32.562  0 411 THR BBB CG2   1 ? 2 
ATOM   6759  N N     . LEU B 1 412 ? 22.918  2.391   17.594  1.000 32.641  0 412 LEU BBB N     1 ? 2 
ATOM   6760  C CA    . LEU B 1 412 ? 22.549  3.753   18.035  1.000 32.226  0 412 LEU BBB CA    1 ? 2 
ATOM   6761  C C     . LEU B 1 412 ? 23.797  4.608   18.308  1.000 30.586  0 412 LEU BBB C     1 ? 2 
ATOM   6762  O O     . LEU B 1 412 ? 23.918  5.711   17.763  1.000 26.426  0 412 LEU BBB O     1 ? 2 
ATOM   6763  C CB    . LEU B 1 412 ? 21.717  3.595   19.303  1.000 34.457  0 412 LEU BBB CB    1 ? 2 
ATOM   6764  C CG    . LEU B 1 412 ? 21.285  4.900   19.968  1.000 35.619  0 412 LEU BBB CG    1 ? 2 
ATOM   6765  C CD1   . LEU B 1 412 ? 20.576  5.804   18.981  1.000 36.246  0 412 LEU BBB CD1   1 ? 2 
ATOM   6766  C CD2   . LEU B 1 412 ? 20.403  4.626   21.169  1.000 37.233  0 412 LEU BBB CD2   1 ? 2 
ATOM   6767  N N     . GLU B 1 413 ? 24.689  4.114   19.157  1.000 30.518  0 413 GLU BBB N     1 ? 2 
ATOM   6768  C CA    . GLU B 1 413 ? 25.885  4.855   19.643  1.000 31.222  0 413 GLU BBB CA    1 ? 2 
ATOM   6769  C C     . GLU B 1 413 ? 26.807  5.145   18.452  1.000 30.156  0 413 GLU BBB C     1 ? 2 
ATOM   6770  O O     . GLU B 1 413 ? 27.328  6.270   18.344  1.000 30.742  0 413 GLU BBB O     1 ? 2 
ATOM   6771  C CB    . GLU B 1 413 ? 26.624  4.043   20.698  1.000 31.816  0 413 GLU BBB CB    1 ? 2 
ATOM   6772  C CG    . GLU B 1 413 ? 25.761  3.630   21.854  1.000 33.027  0 413 GLU BBB CG    1 ? 2 
ATOM   6773  C CD    . GLU B 1 413 ? 25.116  2.252   21.796  1.000 33.760  0 413 GLU BBB CD    1 ? 2 
ATOM   6774  O OE1   . GLU B 1 413 ? 24.433  1.966   20.788  1.000 34.785  0 413 GLU BBB OE1   1 ? 2 
ATOM   6775  O OE2   . GLU B 1 413 ? 25.231  1.511   22.822  1.000 34.188  0 413 GLU BBB OE2   1 ? 2 
ATOM   6776  N N     . ILE B 1 414 ? 27.016  4.145   17.611  1.000 29.228  0 414 ILE BBB N     1 ? 2 
ATOM   6777  C CA    . ILE B 1 414 ? 27.831  4.307   16.376  1.000 30.113  0 414 ILE BBB CA    1 ? 2 
ATOM   6778  C C     . ILE B 1 414 ? 27.135  5.294   15.442  1.000 29.627  0 414 ILE BBB C     1 ? 2 
ATOM   6779  O O     . ILE B 1 414 ? 27.817  6.143   14.884  1.000 31.824  0 414 ILE BBB O     1 ? 2 
ATOM   6780  C CB    . ILE B 1 414 ? 28.086  2.948   15.694  1.000 30.843  0 414 ILE BBB CB    1 ? 2 
ATOM   6781  C CG1   . ILE B 1 414 ? 28.544  1.905   16.710  1.000 30.151  0 414 ILE BBB CG1   1 ? 2 
ATOM   6782  C CG2   . ILE B 1 414 ? 29.047  3.093   14.510  1.000 31.493  0 414 ILE BBB CG2   1 ? 2 
ATOM   6783  C CD1   . ILE B 1 414 ? 29.880  2.176   17.273  1.000 30.699  0 414 ILE BBB CD1   1 ? 2 
ATOM   6784  N N     . ALA B 1 415 ? 25.825  5.209   15.268  1.000 28.287  0 415 ALA BBB N     1 ? 2 
ATOM   6785  C CA    . ALA B 1 415 ? 25.080  6.130   14.384  1.000 27.799  0 415 ALA BBB CA    1 ? 2 
ATOM   6786  C C     . ALA B 1 415 ? 25.385  7.556   14.813  1.000 28.250  0 415 ALA BBB C     1 ? 2 
ATOM   6787  O O     . ALA B 1 415 ? 25.683  8.338   13.934  1.000 30.885  0 415 ALA BBB O     1 ? 2 
ATOM   6788  C CB    . ALA B 1 415 ? 23.601  5.838   14.368  1.000 27.927  0 415 ALA BBB CB    1 ? 2 
ATOM   6789  N N     . ALA B 1 416 ? 25.351  7.865   16.107  1.000 27.429  0 416 ALA BBB N     1 ? 2 
ATOM   6790  C CA    . ALA B 1 416 ? 25.549  9.224   16.652  1.000 27.558  0 416 ALA BBB CA    1 ? 2 
ATOM   6791  C C     . ALA B 1 416 ? 27.028  9.667   16.518  1.000 28.242  0 416 ALA BBB C     1 ? 2 
ATOM   6792  O O     . ALA B 1 416 ? 27.309  10.887  16.519  1.000 26.561  0 416 ALA BBB O     1 ? 2 
ATOM   6793  C CB    . ALA B 1 416 ? 25.072  9.242   18.099  1.000 27.227  0 416 ALA BBB CB    1 ? 2 
ATOM   6794  N N     . ALA B 1 417 ? 27.961  8.724   16.407  1.000 29.547  0 417 ALA BBB N     1 ? 2 
ATOM   6795  C CA    . ALA B 1 417 ? 29.414  8.997   16.254  1.000 31.321  0 417 ALA BBB CA    1 ? 2 
ATOM   6796  C C     . ALA B 1 417 ? 29.732  9.517   14.836  1.000 32.053  0 417 ALA BBB C     1 ? 2 
ATOM   6797  O O     . ALA B 1 417 ? 30.703  10.246  14.704  1.000 33.309  0 417 ALA BBB O     1 ? 2 
ATOM   6798  C CB    . ALA B 1 417 ? 30.243  7.768   16.584  1.000 29.827  0 417 ALA BBB CB    1 ? 2 
ATOM   6799  N N     . HIS B 1 418 ? 28.955  9.141   13.822  1.000 35.425  0 418 HIS BBB N     1 ? 2 
ATOM   6800  C CA    . HIS B 1 418 ? 29.201  9.497   12.391  1.000 37.956  0 418 HIS BBB CA    1 ? 2 
ATOM   6801  C C     . HIS B 1 418 ? 30.618  9.044   11.998  1.000 37.804  0 418 HIS BBB C     1 ? 2 
ATOM   6802  O O     . HIS B 1 418 ? 31.444  9.897   11.619  1.000 39.826  0 418 HIS BBB O     1 ? 2 
ATOM   6803  C CB    . HIS B 1 418 ? 28.994  11.009  12.149  1.000 38.744  0 418 HIS BBB CB    1 ? 2 
ATOM   6804  C CG    . HIS B 1 418 ? 27.572  11.454  12.243  1.000 41.164  0 418 HIS BBB CG    1 ? 2 
ATOM   6805  N ND1   . HIS B 1 418 ? 26.665  11.281  11.195  1.000 45.024  0 418 HIS BBB ND1   1 ? 2 
ATOM   6806  C CD2   . HIS B 1 418 ? 26.875  12.038  13.242  1.000 40.533  0 418 HIS BBB CD2   1 ? 2 
ATOM   6807  C CE1   . HIS B 1 418 ? 25.482  11.725  11.565  1.000 42.539  0 418 HIS BBB CE1   1 ? 2 
ATOM   6808  N NE2   . HIS B 1 418 ? 25.585  12.194  12.799  1.000 40.505  0 418 HIS BBB NE2   1 ? 2 
ATOM   6809  N N     . ARG B 1 419 ? 30.895  7.756   12.122  1.000 38.036  0 419 ARG BBB N     1 ? 2 
ATOM   6810  C CA    . ARG B 1 419 ? 32.177  7.115   11.701  1.000 39.090  0 419 ARG BBB CA    1 ? 2 
ATOM   6811  C C     . ARG B 1 419 ? 32.418  7.338   10.189  1.000 42.303  0 419 ARG BBB C     1 ? 2 
ATOM   6812  O O     . ARG B 1 419 ? 31.504  7.033   9.370   1.000 41.640  0 419 ARG BBB O     1 ? 2 
ATOM   6813  C CB    . ARG B 1 419 ? 32.157  5.621   12.031  1.000 37.719  0 419 ARG BBB CB    1 ? 2 
ATOM   6814  C CG    . ARG B 1 419 ? 32.134  5.280   13.523  1.000 35.369  0 419 ARG BBB CG    1 ? 2 
ATOM   6815  C CD    . ARG B 1 419 ? 32.629  3.873   13.828  1.000 33.231  0 419 ARG BBB CD    1 ? 2 
ATOM   6816  N NE    . ARG B 1 419 ? 32.931  3.739   15.242  1.000 33.193  0 419 ARG BBB NE    1 ? 2 
ATOM   6817  C CZ    . ARG B 1 419 ? 33.371  2.633   15.840  1.000 32.806  0 419 ARG BBB CZ    1 ? 2 
ATOM   6818  N NH1   . ARG B 1 419 ? 33.548  1.511   15.165  1.000 31.202  0 419 ARG BBB NH1   1 ? 2 
ATOM   6819  N NH2   . ARG B 1 419 ? 33.645  2.652   17.134  1.000 33.000  0 419 ARG BBB NH2   1 ? 2 
ATOM   6820  N N     . GLU B 1 420 ? 33.618  7.838   9.841   1.000 44.151  0 420 GLU BBB N     1 ? 2 
ATOM   6821  C CA    . GLU B 1 420 ? 34.032  8.216   8.457   1.000 45.802  0 420 GLU BBB CA    1 ? 2 
ATOM   6822  C C     . GLU B 1 420 ? 35.141  7.285   7.960   1.000 43.417  0 420 GLU BBB C     1 ? 2 
ATOM   6823  O O     . GLU B 1 420 ? 36.028  6.885   8.796   1.000 37.778  0 420 GLU BBB O     1 ? 2 
ATOM   6824  C CB    . GLU B 1 420 ? 34.505  9.673   8.409   1.000 50.474  0 420 GLU BBB CB    1 ? 2 
ATOM   6825  C CG    . GLU B 1 420 ? 33.371  10.656  8.681   1.000 55.073  0 420 GLU BBB CG    1 ? 2 
ATOM   6826  C CD    . GLU B 1 420 ? 33.615  12.128  8.360   1.000 59.141  0 420 GLU BBB CD    1 ? 2 
ATOM   6827  O OE1   . GLU B 1 420 ? 34.204  12.434  7.278   1.000 58.907  0 420 GLU BBB OE1   1 ? 2 
ATOM   6828  O OE2   . GLU B 1 420 ? 33.209  12.984  9.196   1.000 57.716  0 420 GLU BBB OE2   1 ? 2 
ATOM   6829  N N     . LYS B 1 421 ? 35.079  6.970   6.660   1.000 43.485  0 421 LYS BBB N     1 ? 2 
ATOM   6830  C CA    . LYS B 1 421 ? 36.166  6.327   5.876   1.000 45.885  0 421 LYS BBB CA    1 ? 2 
ATOM   6831  C C     . LYS B 1 421 ? 37.475  7.092   6.065   1.000 43.198  0 421 LYS BBB C     1 ? 2 
ATOM   6832  O O     . LYS B 1 421 ? 37.461  8.312   6.194   1.000 37.167  0 421 LYS BBB O     1 ? 2 
ATOM   6833  C CB    . LYS B 1 421 ? 35.820  6.359   4.380   1.000 48.298  0 421 LYS BBB CB    1 ? 2 
ATOM   6834  C CG    . LYS B 1 421 ? 34.901  5.256   3.894   1.000 51.200  0 421 LYS BBB CG    1 ? 2 
ATOM   6835  C CD    . LYS B 1 421 ? 34.983  5.089   2.379   1.000 55.157  0 421 LYS BBB CD    1 ? 2 
ATOM   6836  C CE    . LYS B 1 421 ? 34.522  3.739   1.865   1.000 59.505  0 421 LYS BBB CE    1 ? 2 
ATOM   6837  N NZ    . LYS B 1 421 ? 33.134  3.784   1.325   1.000 63.371  0 421 LYS BBB NZ    1 ? 2 
ATOM   6838  N N     . PRO B 1 422 ? 38.639  6.409   6.054   1.000 44.529  0 422 PRO BBB N     1 ? 2 
ATOM   6839  C CA    . PRO B 1 422 ? 39.931  7.083   5.897   1.000 47.780  0 422 PRO BBB CA    1 ? 2 
ATOM   6840  C C     . PRO B 1 422 ? 39.918  7.830   4.556   1.000 52.895  0 422 PRO BBB C     1 ? 2 
ATOM   6841  O O     . PRO B 1 422 ? 39.299  7.325   3.618   1.000 54.320  0 422 PRO BBB O     1 ? 2 
ATOM   6842  C CB    . PRO B 1 422 ? 40.986  5.970   5.892   1.000 46.379  0 422 PRO BBB CB    1 ? 2 
ATOM   6843  C CG    . PRO B 1 422 ? 40.266  4.759   6.467   1.000 47.291  0 422 PRO BBB CG    1 ? 2 
ATOM   6844  C CD    . PRO B 1 422 ? 38.793  4.957   6.154   1.000 45.564  0 422 PRO BBB CD    1 ? 2 
ATOM   6845  N N     . GLU B 1 423 ? 40.550  9.007   4.468   1.000 57.424  0 423 GLU BBB N     1 ? 2 
ATOM   6846  C CA    . GLU B 1 423 ? 40.305  9.910   3.308   1.000 61.154  0 423 GLU BBB CA    1 ? 2 
ATOM   6847  C C     . GLU B 1 423 ? 41.015  9.341   2.063   1.000 61.352  0 423 GLU BBB C     1 ? 2 
ATOM   6848  O O     . GLU B 1 423 ? 40.581  9.704   0.962   1.000 62.041  0 423 GLU BBB O     1 ? 2 
ATOM   6849  C CB    . GLU B 1 423 ? 40.522  11.370  3.701   1.000 66.365  0 423 GLU BBB CB    1 ? 2 
ATOM   6850  C CG    . GLU B 1 423 ? 41.871  11.971  3.370   1.000 71.212  0 423 GLU BBB CG    1 ? 2 
ATOM   6851  C CD    . GLU B 1 423 ? 42.074  13.313  4.061   1.000 75.175  0 423 GLU BBB CD    1 ? 2 
ATOM   6852  O OE1   . GLU B 1 423 ? 43.218  13.824  4.037   1.000 75.822  0 423 GLU BBB OE1   1 ? 2 
ATOM   6853  O OE2   . GLU B 1 423 ? 41.081  13.839  4.634   1.000 74.471  0 423 GLU BBB OE2   1 ? 2 
ATOM   6854  N N     . HIS B 1 424 ? 41.932  8.373   2.198   1.000 62.372  0 424 HIS BBB N     1 ? 2 
ATOM   6855  C CA    . HIS B 1 424 ? 42.577  7.712   1.021   1.000 64.537  0 424 HIS BBB CA    1 ? 2 
ATOM   6856  C C     . HIS B 1 424 ? 41.616  6.739   0.310   1.000 63.167  0 424 HIS BBB C     1 ? 2 
ATOM   6857  O O     . HIS B 1 424 ? 41.993  6.289   -0.781  1.000 62.860  0 424 HIS BBB O     1 ? 2 
ATOM   6858  C CB    . HIS B 1 424 ? 43.923  7.049   1.375   1.000 62.884  0 424 HIS BBB CB    1 ? 2 
ATOM   6859  C CG    . HIS B 1 424 ? 43.857  5.928   2.359   1.000 64.473  0 424 HIS BBB CG    1 ? 2 
ATOM   6860  N ND1   . HIS B 1 424 ? 43.554  4.625   1.993   1.000 64.429  0 424 HIS BBB ND1   1 ? 2 
ATOM   6861  C CD2   . HIS B 1 424 ? 44.118  5.892   3.686   1.000 65.746  0 424 HIS BBB CD2   1 ? 2 
ATOM   6862  C CE1   . HIS B 1 424 ? 43.602  3.849   3.056   1.000 63.323  0 424 HIS BBB CE1   1 ? 2 
ATOM   6863  N NE2   . HIS B 1 424 ? 43.956  4.595   4.104   1.000 63.352  0 424 HIS BBB NE2   1 ? 2 
ATOM   6864  N N     . LEU B 1 425 ? 40.426  6.440   0.860   1.000 60.741  0 425 LEU BBB N     1 ? 2 
ATOM   6865  C CA    . LEU B 1 425 ? 39.462  5.474   0.254   1.000 58.512  0 425 LEU BBB CA    1 ? 2 
ATOM   6866  C C     . LEU B 1 425 ? 38.192  6.175   -0.222  1.000 59.377  0 425 LEU BBB C     1 ? 2 
ATOM   6867  O O     . LEU B 1 425 ? 37.273  5.455   -0.701  1.000 64.270  0 425 LEU BBB O     1 ? 2 
ATOM   6868  C CB    . LEU B 1 425 ? 39.111  4.400   1.283   1.000 57.809  0 425 LEU BBB CB    1 ? 2 
ATOM   6869  C CG    . LEU B 1 425 ? 40.227  3.415   1.585   1.000 56.777  0 425 LEU BBB CG    1 ? 2 
ATOM   6870  C CD1   . LEU B 1 425 ? 39.953  2.684   2.883   1.000 55.316  0 425 LEU BBB CD1   1 ? 2 
ATOM   6871  C CD2   . LEU B 1 425 ? 40.398  2.449   0.418   1.000 58.822  0 425 LEU BBB CD2   1 ? 2 
ATOM   6872  N N     . ARG B 1 426 ? 38.147  7.506   -0.120  1.000 57.382  0 426 ARG BBB N     1 ? 2 
ATOM   6873  C CA    . ARG B 1 426 ? 36.975  8.319   -0.536  1.000 56.076  0 426 ARG BBB CA    1 ? 2 
ATOM   6874  C C     . ARG B 1 426 ? 36.892  8.350   -2.074  1.000 57.315  0 426 ARG BBB C     1 ? 2 
ATOM   6875  O O     . ARG B 1 426 ? 37.937  8.561   -2.699  1.000 53.485  0 426 ARG BBB O     1 ? 2 
ATOM   6876  C CB    . ARG B 1 426 ? 37.115  9.726   0.040   1.000 54.605  0 426 ARG BBB CB    1 ? 2 
ATOM   6877  C CG    . ARG B 1 426 ? 36.932  9.818   1.547   1.000 52.515  0 426 ARG BBB CG    1 ? 2 
ATOM   6878  C CD    . ARG B 1 426 ? 35.519  9.658   1.966   1.000 50.806  0 426 ARG BBB CD    1 ? 2 
ATOM   6879  N NE    . ARG B 1 426 ? 34.678  10.639  1.280   1.000 50.939  0 426 ARG BBB NE    1 ? 2 
ATOM   6880  C CZ    . ARG B 1 426 ? 34.414  11.875  1.702   1.000 48.462  0 426 ARG BBB CZ    1 ? 2 
ATOM   6881  N NH1   . ARG B 1 426 ? 34.925  12.324  2.831   1.000 48.676  0 426 ARG BBB NH1   1 ? 2 
ATOM   6882  N NH2   . ARG B 1 426 ? 33.603  12.653  1.011   1.000 46.356  0 426 ARG BBB NH2   1 ? 2 
ATOM   6883  N N     . GLU B 1 427 ? 35.692  8.146   -2.637  1.000 60.368  0 427 GLU BBB N     1 ? 2 
ATOM   6884  C CA    . GLU B 1 427 ? 35.408  8.085   -4.100  1.000 63.084  0 427 GLU BBB CA    1 ? 2 
ATOM   6885  C C     . GLU B 1 427 ? 34.650  9.335   -4.579  1.000 60.205  0 427 GLU BBB C     1 ? 2 
ATOM   6886  O O     . GLU B 1 427 ? 34.697  9.600   -5.781  1.000 63.498  0 427 GLU BBB O     1 ? 2 
ATOM   6887  C CB    . GLU B 1 427 ? 34.604  6.821   -4.445  1.000 69.197  0 427 GLU BBB CB    1 ? 2 
ATOM   6888  C CG    . GLU B 1 427 ? 35.409  5.719   -5.146  1.000 74.250  0 427 GLU BBB CG    1 ? 2 
ATOM   6889  C CD    . GLU B 1 427 ? 34.671  4.399   -5.370  1.000 77.417  0 427 GLU BBB CD    1 ? 2 
ATOM   6890  O OE1   . GLU B 1 427 ? 34.425  4.009   -6.568  1.000 75.530  0 427 GLU BBB OE1   1 ? 2 
ATOM   6891  O OE2   . GLU B 1 427 ? 34.352  3.745   -4.345  1.000 77.252  0 427 GLU BBB OE2   1 ? 2 
ATOM   6892  N N     . ASN B 1 428 ? 34.005  10.089  -3.694  1.000 57.090  0 428 ASN BBB N     1 ? 2 
ATOM   6893  C CA    . ASN B 1 428 ? 33.250  11.319  -4.055  1.000 56.959  0 428 ASN BBB CA    1 ? 2 
ATOM   6894  C C     . ASN B 1 428 ? 32.929  12.120  -2.782  1.000 56.841  0 428 ASN BBB C     1 ? 2 
ATOM   6895  O O     . ASN B 1 428 ? 33.589  11.891  -1.763  1.000 52.860  0 428 ASN BBB O     1 ? 2 
ATOM   6896  C CB    . ASN B 1 428 ? 31.992  10.994  -4.863  1.000 56.576  0 428 ASN BBB CB    1 ? 2 
ATOM   6897  C CG    . ASN B 1 428 ? 31.118  9.945   -4.213  1.000 56.797  0 428 ASN BBB CG    1 ? 2 
ATOM   6898  O OD1   . ASN B 1 428 ? 30.705  10.071  -3.053  1.000 52.457  0 428 ASN BBB OD1   1 ? 2 
ATOM   6899  N ND2   . ASN B 1 428 ? 30.828  8.905   -4.983  1.000 57.870  0 428 ASN BBB ND2   1 ? 2 
ATOM   6900  N N     . GLU B 1 429 ? 31.954  13.031  -2.867  1.000 58.362  0 429 GLU BBB N     1 ? 2 
ATOM   6901  C CA    . GLU B 1 429 ? 31.552  13.947  -1.771  1.000 60.315  0 429 GLU BBB CA    1 ? 2 
ATOM   6902  C C     . GLU B 1 429 ? 30.389  13.360  -0.945  1.000 58.911  0 429 GLU BBB C     1 ? 2 
ATOM   6903  O O     . GLU B 1 429 ? 29.966  14.057  -0.001  1.000 61.408  0 429 GLU BBB O     1 ? 2 
ATOM   6904  C CB    . GLU B 1 429 ? 31.174  15.320  -2.337  1.000 59.599  0 429 GLU BBB CB    1 ? 2 
ATOM   6905  C CG    . GLU B 1 429 ? 32.213  15.895  -3.278  1.000 63.602  0 429 GLU BBB CG    1 ? 2 
ATOM   6906  C CD    . GLU B 1 429 ? 33.661  15.699  -2.836  1.000 63.297  0 429 GLU BBB CD    1 ? 2 
ATOM   6907  O OE1   . GLU B 1 429 ? 33.967  16.040  -1.638  1.000 55.549  0 429 GLU BBB OE1   1 ? 2 
ATOM   6908  O OE2   . GLU B 1 429 ? 34.467  15.159  -3.688  1.000 58.795  0 429 GLU BBB OE2   1 ? 2 
ATOM   6909  N N     . MET B 1 430 ? 29.893  12.161  -1.274  1.000 56.781  0 430 MET BBB N     1 ? 2 
ATOM   6910  C CA    . MET B 1 430 ? 28.802  11.487  -0.516  1.000 56.700  0 430 MET BBB CA    1 ? 2 
ATOM   6911  C C     . MET B 1 430 ? 29.192  10.044  -0.149  1.000 55.132  0 430 MET BBB C     1 ? 2 
ATOM   6912  O O     . MET B 1 430 ? 28.303  9.286   0.308   1.000 57.282  0 430 MET BBB O     1 ? 2 
ATOM   6913  C CB    . MET B 1 430 ? 27.464  11.520  -1.263  1.000 57.502  0 430 MET BBB CB    1 ? 2 
ATOM   6914  C CG    . MET B 1 430 ? 27.493  10.797  -2.574  1.000 59.586  0 430 MET BBB CG    1 ? 2 
ATOM   6915  S SD    . MET B 1 430 ? 26.144  11.318  -3.638  1.000 59.933  0 430 MET BBB SD    1 ? 2 
ATOM   6916  C CE    . MET B 1 430 ? 27.061  11.404  -5.178  1.000 67.276  0 430 MET BBB CE    1 ? 2 
ATOM   6917  N N     . ASP B 1 431 ? 30.482  9.707   -0.233  1.000 52.786  0 431 ASP BBB N     1 ? 2 
ATOM   6918  C CA    . ASP B 1 431 ? 31.060  8.387   0.156   1.000 52.206  0 431 ASP BBB CA    1 ? 2 
ATOM   6919  C C     . ASP B 1 431 ? 31.787  8.492   1.521   1.000 47.256  0 431 ASP BBB C     1 ? 2 
ATOM   6920  O O     . ASP B 1 431 ? 32.720  7.722   1.775   1.000 46.590  0 431 ASP BBB O     1 ? 2 
ATOM   6921  C CB    . ASP B 1 431 ? 31.952  7.932   -0.999  1.000 56.218  0 431 ASP BBB CB    1 ? 2 
ATOM   6922  C CG    . ASP B 1 431 ? 32.885  6.775   -0.695  1.000 60.087  0 431 ASP BBB CG    1 ? 2 
ATOM   6923  O OD1   . ASP B 1 431 ? 32.415  5.789   -0.059  1.000 61.944  0 431 ASP BBB OD1   1 ? 2 
ATOM   6924  O OD2   . ASP B 1 431 ? 34.076  6.871   -1.088  1.000 62.071  0 431 ASP BBB OD2   1 ? 2 
ATOM   6925  N N     . PHE B 1 432 ? 31.395  9.422   2.373   1.000 45.184  0 432 PHE BBB N     1 ? 2 
ATOM   6926  C CA    . PHE B 1 432 ? 32.144  9.838   3.592   1.000 46.410  0 432 PHE BBB CA    1 ? 2 
ATOM   6927  C C     . PHE B 1 432 ? 32.019  8.749   4.689   1.000 45.075  0 432 PHE BBB C     1 ? 2 
ATOM   6928  O O     . PHE B 1 432 ? 33.008  8.491   5.397   1.000 42.775  0 432 PHE BBB O     1 ? 2 
ATOM   6929  C CB    . PHE B 1 432 ? 31.676  11.219  4.074   1.000 46.448  0 432 PHE BBB CB    1 ? 2 
ATOM   6930  C CG    . PHE B 1 432 ? 30.183  11.414  4.159   1.000 47.845  0 432 PHE BBB CG    1 ? 2 
ATOM   6931  C CD1   . PHE B 1 432 ? 29.454  11.029  5.286   1.000 47.871  0 432 PHE BBB CD1   1 ? 2 
ATOM   6932  C CD2   . PHE B 1 432 ? 29.504  12.017  3.101   1.000 49.388  0 432 PHE BBB CD2   1 ? 2 
ATOM   6933  C CE1   . PHE B 1 432 ? 28.078  11.220  5.335   1.000 50.279  0 432 PHE BBB CE1   1 ? 2 
ATOM   6934  C CE2   . PHE B 1 432 ? 28.126  12.217  3.165   1.000 52.145  0 432 PHE BBB CE2   1 ? 2 
ATOM   6935  C CZ    . PHE B 1 432 ? 27.413  11.824  4.282   1.000 51.262  0 432 PHE BBB CZ    1 ? 2 
ATOM   6936  N N     . ALA B 1 433 ? 30.835  8.136   4.817   1.000 44.702  0 433 ALA BBB N     1 ? 2 
ATOM   6937  C CA    . ALA B 1 433 ? 30.440  7.196   5.897   1.000 43.921  0 433 ALA BBB CA    1 ? 2 
ATOM   6938  C C     . ALA B 1 433 ? 31.093  5.824   5.708   1.000 42.525  0 433 ALA BBB C     1 ? 2 
ATOM   6939  O O     . ALA B 1 433 ? 31.191  5.379   4.579   1.000 41.737  0 433 ALA BBB O     1 ? 2 
ATOM   6940  C CB    . ALA B 1 433 ? 28.933  7.049   5.913   1.000 44.169  0 433 ALA BBB CB    1 ? 2 
ATOM   6941  N N     . LEU B 1 434 ? 31.452  5.164   6.806   1.000 42.132  0 434 LEU BBB N     1 ? 2 
ATOM   6942  C CA    . LEU B 1 434 ? 31.615  3.684   6.867   1.000 39.842  0 434 LEU BBB CA    1 ? 2 
ATOM   6943  C C     . LEU B 1 434 ? 30.285  3.006   6.524   1.000 36.003  0 434 LEU BBB C     1 ? 2 
ATOM   6944  O O     . LEU B 1 434 ? 29.221  3.568   6.734   1.000 37.230  0 434 LEU BBB O     1 ? 2 
ATOM   6945  C CB    . LEU B 1 434 ? 32.018  3.295   8.293   1.000 41.012  0 434 LEU BBB CB    1 ? 2 
ATOM   6946  C CG    . LEU B 1 434 ? 33.386  3.763   8.771   1.000 41.875  0 434 LEU BBB CG    1 ? 2 
ATOM   6947  C CD1   . LEU B 1 434 ? 33.767  3.100   10.093  1.000 41.042  0 434 LEU BBB CD1   1 ? 2 
ATOM   6948  C CD2   . LEU B 1 434 ? 34.419  3.454   7.720   1.000 43.910  0 434 LEU BBB CD2   1 ? 2 
ATOM   6949  N N     . PRO B 1 435 ? 30.284  1.772   6.010   1.000 32.363  0 435 PRO BBB N     1 ? 2 
ATOM   6950  C CA    . PRO B 1 435 ? 29.074  0.973   5.939   1.000 32.130  0 435 PRO BBB CA    1 ? 2 
ATOM   6951  C C     . PRO B 1 435 ? 28.353  0.887   7.291   1.000 32.032  0 435 PRO BBB C     1 ? 2 
ATOM   6952  O O     . PRO B 1 435 ? 28.968  0.939   8.346   1.000 32.264  0 435 PRO BBB O     1 ? 2 
ATOM   6953  C CB    . PRO B 1 435 ? 29.574  -0.427  5.523   1.000 31.408  0 435 PRO BBB CB    1 ? 2 
ATOM   6954  C CG    . PRO B 1 435 ? 30.846  -0.131  4.782   1.000 31.876  0 435 PRO BBB CG    1 ? 2 
ATOM   6955  C CD    . PRO B 1 435 ? 31.448  1.046   5.506   1.000 32.568  0 435 PRO BBB CD    1 ? 2 
ATOM   6956  N N     . LEU B 1 436 ? 27.043  0.722   7.235   1.000 31.851  0 436 LEU BBB N     1 ? 2 
ATOM   6957  C CA    . LEU B 1 436 ? 26.227  0.363   8.420   1.000 30.941  0 436 LEU BBB CA    1 ? 2 
ATOM   6958  C C     . LEU B 1 436 ? 26.905  -0.828  9.112   1.000 29.805  0 436 LEU BBB C     1 ? 2 
ATOM   6959  O O     . LEU B 1 436 ? 27.356  -1.742  8.401   1.000 29.786  0 436 LEU BBB O     1 ? 2 
ATOM   6960  C CB    . LEU B 1 436 ? 24.816  0.027   7.923   1.000 31.857  0 436 LEU BBB CB    1 ? 2 
ATOM   6961  C CG    . LEU B 1 436 ? 24.082  1.163   7.208   1.000 32.465  0 436 LEU BBB CG    1 ? 2 
ATOM   6962  C CD1   . LEU B 1 436 ? 22.868  0.639   6.488   1.000 33.056  0 436 LEU BBB CD1   1 ? 2 
ATOM   6963  C CD2   . LEU B 1 436 ? 23.689  2.265   8.172   1.000 32.626  0 436 LEU BBB CD2   1 ? 2 
ATOM   6964  N N     . ASN B 1 437 ? 27.031  -0.809  10.430  1.000 29.795  0 437 ASN BBB N     1 ? 2 
ATOM   6965  C CA    . ASN B 1 437 ? 27.888  -1.787  11.152  1.000 29.178  0 437 ASN BBB CA    1 ? 2 
ATOM   6966  C C     . ASN B 1 437 ? 27.144  -3.114  11.363  1.000 28.264  0 437 ASN BBB C     1 ? 2 
ATOM   6967  O O     . ASN B 1 437 ? 27.849  -4.083  11.577  1.000 29.483  0 437 ASN BBB O     1 ? 2 
ATOM   6968  C CB    . ASN B 1 437 ? 28.458  -1.212  12.455  1.000 29.157  0 437 ASN BBB CB    1 ? 2 
ATOM   6969  C CG    . ASN B 1 437 ? 27.415  -0.941  13.523  1.000 29.746  0 437 ASN BBB CG    1 ? 2 
ATOM   6970  O OD1   . ASN B 1 437 ? 26.261  -0.620  13.247  1.000 28.749  0 437 ASN BBB OD1   1 ? 2 
ATOM   6971  N ND2   . ASN B 1 437 ? 27.812  -1.088  14.769  1.000 30.803  0 437 ASN BBB ND2   1 ? 2 
ATOM   6972  N N     . CYS B 1 438 ? 25.812  -3.174  11.264  1.000 26.952  0 438 CYS BBB N     1 ? 2 
ATOM   6973  C CA    . CYS B 1 438 ? 25.004  -4.358  11.631  1.000 27.120  0 438 CYS BBB CA    1 ? 2 
ATOM   6974  C C     . CYS B 1 438 ? 24.212  -4.928  10.454  1.000 29.539  0 438 CYS BBB C     1 ? 2 
ATOM   6975  O O     . CYS B 1 438 ? 23.715  -4.158  9.605   1.000 28.435  0 438 CYS BBB O     1 ? 2 
ATOM   6976  C CB    . CYS B 1 438 ? 23.985  -4.068  12.732  1.000 27.429  0 438 CYS BBB CB    1 ? 2 
ATOM   6977  S SG    . CYS B 1 438 ? 24.761  -3.513  14.280  1.000 26.858  0 438 CYS BBB SG    1 ? 2 
ATOM   6978  N N     . LEU B 1 439 ? 24.059  -6.259  10.483  1.000 30.683  0 439 LEU BBB N     1 ? 2 
ATOM   6979  C CA    . LEU B 1 439 ? 23.172  -7.024  9.591   1.000 31.443  0 439 LEU BBB CA    1 ? 2 
ATOM   6980  C C     . LEU B 1 439 ? 22.574  -8.193  10.369  1.000 29.803  0 439 LEU BBB C     1 ? 2 
ATOM   6981  O O     . LEU B 1 439 ? 23.333  -9.062  10.786  1.000 26.755  0 439 LEU BBB O     1 ? 2 
ATOM   6982  C CB    . LEU B 1 439 ? 23.949  -7.554  8.381   1.000 33.278  0 439 LEU BBB CB    1 ? 2 
ATOM   6983  C CG    . LEU B 1 439 ? 23.093  -8.393  7.434   1.000 34.808  0 439 LEU BBB CG    1 ? 2 
ATOM   6984  C CD1   . LEU B 1 439 ? 22.075  -7.514  6.751   1.000 37.742  0 439 LEU BBB CD1   1 ? 2 
ATOM   6985  C CD2   . LEU B 1 439 ? 23.945  -9.110  6.411   1.000 36.321  0 439 LEU BBB CD2   1 ? 2 
ATOM   6986  N N     . ALA B 1 440 ? 21.244  -8.220  10.445  1.000 29.882  0 440 ALA BBB N     1 ? 2 
ATOM   6987  C CA    . ALA B 1 440 ? 20.446  -9.286  11.066  1.000 29.198  0 440 ALA BBB CA    1 ? 2 
ATOM   6988  C C     . ALA B 1 440 ? 19.719  -10.070 9.974   1.000 30.290  0 440 ALA BBB C     1 ? 2 
ATOM   6989  O O     . ALA B 1 440 ? 19.111  -9.433  9.088   1.000 30.315  0 440 ALA BBB O     1 ? 2 
ATOM   6990  C CB    . ALA B 1 440 ? 19.508  -8.648  12.038  1.000 29.240  0 440 ALA BBB CB    1 ? 2 
ATOM   6991  N N     . LYS B 1 441 ? 19.799  -11.405 10.026  1.000 31.309  0 441 LYS BBB N     1 ? 2 
ATOM   6992  C CA    . LYS B 1 441 ? 19.097  -12.291 9.075   1.000 31.094  0 441 LYS BBB CA    1 ? 2 
ATOM   6993  C C     . LYS B 1 441 ? 18.619  -13.583 9.736   1.000 29.961  0 441 LYS BBB C     1 ? 2 
ATOM   6994  O O     . LYS B 1 441 ? 19.429  -14.279 10.361  1.000 30.466  0 441 LYS BBB O     1 ? 2 
ATOM   6995  C CB    . LYS B 1 441 ? 20.024  -12.638 7.927   1.000 33.480  0 441 LYS BBB CB    1 ? 2 
ATOM   6996  C CG    . LYS B 1 441 ? 19.409  -13.592 6.913   1.000 34.765  0 441 LYS BBB CG    1 ? 2 
ATOM   6997  C CD    . LYS B 1 441 ? 20.054  -13.469 5.578   1.000 35.934  0 441 LYS BBB CD    1 ? 2 
ATOM   6998  C CE    . LYS B 1 441 ? 21.452  -14.054 5.559   1.000 36.300  0 441 LYS BBB CE    1 ? 2 
ATOM   6999  N NZ    . LYS B 1 441 ? 22.036  -13.975 4.204   1.000 36.319  0 441 LYS BBB NZ    1 ? 2 
ATOM   7000  N N     . LEU B 1 442 ? 17.328  -13.872 9.570   1.000 30.040  0 442 LEU BBB N     1 ? 2 
ATOM   7001  C CA    . LEU B 1 442 ? 16.698  -15.191 9.834   1.000 29.883  0 442 LEU BBB CA    1 ? 2 
ATOM   7002  C C     . LEU B 1 442 ? 16.412  -15.920 8.513   1.000 32.166  0 442 LEU BBB C     1 ? 2 
ATOM   7003  O O     . LEU B 1 442 ? 15.859  -15.316 7.587   1.000 30.440  0 442 LEU BBB O     1 ? 2 
ATOM   7004  C CB    . LEU B 1 442 ? 15.414  -15.013 10.625  1.000 28.405  0 442 LEU BBB CB    1 ? 2 
ATOM   7005  C CG    . LEU B 1 442 ? 15.586  -14.356 11.993  1.000 28.475  0 442 LEU BBB CG    1 ? 2 
ATOM   7006  C CD1   . LEU B 1 442 ? 14.228  -14.075 12.610  1.000 28.012  0 442 LEU BBB CD1   1 ? 2 
ATOM   7007  C CD2   . LEU B 1 442 ? 16.440  -15.213 12.918  1.000 27.462  0 442 LEU BBB CD2   1 ? 2 
ATOM   7008  N N     . VAL B 1 443 ? 16.772  -17.194 8.473   1.000 34.136  0 443 VAL BBB N     1 ? 2 
ATOM   7009  C CA    . VAL B 1 443 ? 16.455  -18.112 7.360   1.000 37.668  0 443 VAL BBB CA    1 ? 2 
ATOM   7010  C C     . VAL B 1 443 ? 15.440  -19.116 7.898   1.000 38.302  0 443 VAL BBB C     1 ? 2 
ATOM   7011  O O     . VAL B 1 443 ? 15.760  -19.801 8.924   1.000 40.408  0 443 VAL BBB O     1 ? 2 
ATOM   7012  C CB    . VAL B 1 443 ? 17.753  -18.760 6.855   1.000 41.200  0 443 VAL BBB CB    1 ? 2 
ATOM   7013  C CG1   . VAL B 1 443 ? 17.508  -19.638 5.640   1.000 43.194  0 443 VAL BBB CG1   1 ? 2 
ATOM   7014  C CG2   . VAL B 1 443 ? 18.799  -17.688 6.536   1.000 41.707  0 443 VAL BBB CG2   1 ? 2 
ATOM   7015  N N     . VAL B 1 444 ? 14.236  -19.126 7.310   1.000 38.392  0 444 VAL BBB N     1 ? 2 
ATOM   7016  C CA    . VAL B 1 444 ? 13.061  -19.896 7.820   1.000 38.168  0 444 VAL BBB CA    1 ? 2 
ATOM   7017  C C     . VAL B 1 444 ? 12.509  -20.802 6.714   1.000 40.461  0 444 VAL BBB C     1 ? 2 
ATOM   7018  O O     . VAL B 1 444 ? 12.587  -20.429 5.500   1.000 38.917  0 444 VAL BBB O     1 ? 2 
ATOM   7019  C CB    . VAL B 1 444 ? 11.986  -18.954 8.384   1.000 39.296  0 444 VAL BBB CB    1 ? 2 
ATOM   7020  C CG1   . VAL B 1 444 ? 12.608  -17.960 9.354   1.000 38.017  0 444 VAL BBB CG1   1 ? 2 
ATOM   7021  C CG2   . VAL B 1 444 ? 11.188  -18.226 7.301   1.000 39.280  0 444 VAL BBB CG2   1 ? 2 
ATOM   7022  N N     . VAL B 1 445 ? 11.964  -21.954 7.120   1.000 43.720  0 445 VAL BBB N     1 ? 2 
ATOM   7023  C CA    . VAL B 1 445 ? 11.273  -22.915 6.207   1.000 47.300  0 445 VAL BBB CA    1 ? 2 
ATOM   7024  C C     . VAL B 1 445 ? 9.754   -22.679 6.296   1.000 47.344  0 445 VAL BBB C     1 ? 2 
ATOM   7025  O O     . VAL B 1 445 ? 9.155   -22.863 7.384   1.000 42.133  0 445 VAL BBB O     1 ? 2 
ATOM   7026  C CB    . VAL B 1 445 ? 11.652  -24.366 6.544   1.000 47.967  0 445 VAL BBB CB    1 ? 2 
ATOM   7027  C CG1   . VAL B 1 445 ? 10.976  -25.344 5.611   1.000 48.834  0 445 VAL BBB CG1   1 ? 2 
ATOM   7028  C CG2   . VAL B 1 445 ? 13.153  -24.583 6.535   1.000 47.650  0 445 VAL BBB CG2   1 ? 2 
ATOM   7029  N N     . LYS B 1 446 ? 9.159   -22.292 5.177   1.000 53.134  0 446 LYS BBB N     1 ? 2 
ATOM   7030  C CA    . LYS B 1 446 ? 7.711   -21.960 5.065   1.000 58.223  0 446 LYS BBB CA    1 ? 2 
ATOM   7031  C C     . LYS B 1 446 ? 6.849   -23.177 5.421   1.000 56.593  0 446 LYS BBB C     1 ? 2 
ATOM   7032  O O     . LYS B 1 446 ? 5.906   -23.000 6.183   1.000 60.013  0 446 LYS BBB O     1 ? 2 
ATOM   7033  C CB    . LYS B 1 446 ? 7.415   -21.442 3.659   1.000 58.712  0 446 LYS BBB CB    1 ? 2 
ATOM   7034  C CG    . LYS B 1 446 ? 8.197   -20.190 3.329   1.000 61.251  0 446 LYS BBB CG    1 ? 2 
ATOM   7035  C CD    . LYS B 1 446 ? 7.358   -19.143 2.667   1.000 65.016  0 446 LYS BBB CD    1 ? 2 
ATOM   7036  C CE    . LYS B 1 446 ? 7.333   -19.319 1.165   1.000 66.376  0 446 LYS BBB CE    1 ? 2 
ATOM   7037  N NZ    . LYS B 1 446 ? 6.753   -18.122 0.513   1.000 68.799  0 446 LYS BBB NZ    1 ? 2 
ATOM   7038  N N     . SER B 1 447 ? 7.204   -24.369 4.944   1.000 58.012  0 447 SER BBB N     1 ? 2 
ATOM   7039  C CA    . SER B 1 447 ? 6.392   -25.604 5.115   1.000 58.293  0 447 SER BBB CA    1 ? 2 
ATOM   7040  C C     . SER B 1 447 ? 6.441   -26.093 6.569   1.000 58.040  0 447 SER BBB C     1 ? 2 
ATOM   7041  O O     . SER B 1 447 ? 5.876   -27.161 6.832   1.000 59.128  0 447 SER BBB O     1 ? 2 
ATOM   7042  C CB    . SER B 1 447 ? 6.831   -26.677 4.152   1.000 56.537  0 447 SER BBB CB    1 ? 2 
ATOM   7043  O OG    . SER B 1 447 ? 8.192   -27.013 4.361   1.000 52.774  0 447 SER BBB OG    1 ? 2 
ATOM   7044  N N     . GLN B 1 448 ? 7.094   -25.367 7.483   1.000 57.862  0 448 GLN BBB N     1 ? 2 
ATOM   7045  C CA    . GLN B 1 448 ? 7.132   -25.736 8.926   1.000 56.630  0 448 GLN BBB CA    1 ? 2 
ATOM   7046  C C     . GLN B 1 448 ? 6.740   -24.526 9.780   1.000 55.446  0 448 GLN BBB C     1 ? 2 
ATOM   7047  O O     . GLN B 1 448 ? 7.301   -24.368 10.892  1.000 55.041  0 448 GLN BBB O     1 ? 2 
ATOM   7048  C CB    . GLN B 1 448 ? 8.500   -26.286 9.323   1.000 55.774  0 448 GLN BBB CB    1 ? 2 
ATOM   7049  C CG    . GLN B 1 448 ? 8.987   -27.413 8.429   1.000 57.242  0 448 GLN BBB CG    1 ? 2 
ATOM   7050  C CD    . GLN B 1 448 ? 10.361  -27.881 8.834   1.000 57.924  0 448 GLN BBB CD    1 ? 2 
ATOM   7051  O OE1   . GLN B 1 448 ? 11.148  -27.146 9.433   1.000 62.519  0 448 GLN BBB OE1   1 ? 2 
ATOM   7052  N NE2   . GLN B 1 448 ? 10.657  -29.134 8.546   1.000 56.662  0 448 GLN BBB NE2   1 ? 2 
ATOM   7053  N N     . GLY B 1 449 ? 5.762   -23.749 9.306   1.000 53.939  0 449 GLY BBB N     1 ? 2 
ATOM   7054  C CA    . GLY B 1 449 ? 5.266   -22.537 9.988   1.000 53.605  0 449 GLY BBB CA    1 ? 2 
ATOM   7055  C C     . GLY B 1 449 ? 6.383   -21.525 10.189  1.000 50.838  0 449 GLY BBB C     1 ? 2 
ATOM   7056  O O     . GLY B 1 449 ? 6.426   -20.950 11.256  1.000 49.902  0 449 GLY BBB O     1 ? 2 
ATOM   7057  N N     . GLU B 1 450 ? 7.251   -21.356 9.184   1.000 47.946  0 450 GLU BBB N     1 ? 2 
ATOM   7058  C CA    . GLU B 1 450 ? 8.449   -20.475 9.181   1.000 47.031  0 450 GLU BBB CA    1 ? 2 
ATOM   7059  C C     . GLU B 1 450 ? 9.392   -20.842 10.338  1.000 45.119  0 450 GLU BBB C     1 ? 2 
ATOM   7060  O O     . GLU B 1 450 ? 9.813   -19.910 11.038  1.000 46.937  0 450 GLU BBB O     1 ? 2 
ATOM   7061  C CB    . GLU B 1 450 ? 8.015   -19.006 9.223   1.000 45.893  0 450 GLU BBB CB    1 ? 2 
ATOM   7062  C CG    . GLU B 1 450 ? 7.308   -18.558 7.969   1.000 46.042  0 450 GLU BBB CG    1 ? 2 
ATOM   7063  C CD    . GLU B 1 450 ? 7.261   -17.061 7.753   1.000 45.865  0 450 GLU BBB CD    1 ? 2 
ATOM   7064  O OE1   . GLU B 1 450 ? 6.800   -16.334 8.642   1.000 47.128  0 450 GLU BBB OE1   1 ? 2 
ATOM   7065  O OE2   . GLU B 1 450 ? 7.695   -16.631 6.692   1.000 48.377  0 450 GLU BBB OE2   1 ? 2 
ATOM   7066  N N     . LYS B 1 451 ? 9.727   -22.122 10.541  1.000 42.266  0 451 LYS BBB N     1 ? 2 
ATOM   7067  C CA    . LYS B 1 451 ? 10.724  -22.539 11.554  1.000 42.367  0 451 LYS BBB CA    1 ? 2 
ATOM   7068  C C     . LYS B 1 451 ? 12.074  -21.873 11.236  1.000 39.612  0 451 LYS BBB C     1 ? 2 
ATOM   7069  O O     . LYS B 1 451 ? 12.453  -21.830 10.048  1.000 37.754  0 451 LYS BBB O     1 ? 2 
ATOM   7070  C CB    . LYS B 1 451 ? 10.923  -24.053 11.591  1.000 45.870  0 451 LYS BBB CB    1 ? 2 
ATOM   7071  C CG    . LYS B 1 451 ? 11.745  -24.574 12.772  1.000 47.752  0 451 LYS BBB CG    1 ? 2 
ATOM   7072  C CD    . LYS B 1 451 ? 11.838  -26.079 12.857  1.000 49.727  0 451 LYS BBB CD    1 ? 2 
ATOM   7073  C CE    . LYS B 1 451 ? 11.370  -26.638 14.190  1.000 52.312  0 451 LYS BBB CE    1 ? 2 
ATOM   7074  N NZ    . LYS B 1 451 ? 11.006  -28.069 14.084  1.000 53.607  0 451 LYS BBB NZ    1 ? 2 
ATOM   7075  N N     . VAL B 1 452 ? 12.781  -21.367 12.251  1.000 36.212  0 452 VAL BBB N     1 ? 2 
ATOM   7076  C CA    . VAL B 1 452 ? 14.125  -20.754 12.040  1.000 35.744  0 452 VAL BBB CA    1 ? 2 
ATOM   7077  C C     . VAL B 1 452 ? 15.156  -21.884 11.929  1.000 36.187  0 452 VAL BBB C     1 ? 2 
ATOM   7078  O O     . VAL B 1 452 ? 15.292  -22.679 12.887  1.000 37.084  0 452 VAL BBB O     1 ? 2 
ATOM   7079  C CB    . VAL B 1 452 ? 14.472  -19.748 13.146  1.000 34.849  0 452 VAL BBB CB    1 ? 2 
ATOM   7080  C CG1   . VAL B 1 452 ? 15.856  -19.130 12.937  1.000 33.926  0 452 VAL BBB CG1   1 ? 2 
ATOM   7081  C CG2   . VAL B 1 452 ? 13.384  -18.670 13.236  1.000 35.083  0 452 VAL BBB CG2   1 ? 2 
ATOM   7082  N N     . VAL B 1 453 ? 15.822  -21.993 10.777  1.000 35.742  0 453 VAL BBB N     1 ? 2 
ATOM   7083  C CA    . VAL B 1 453 ? 16.862  -23.042 10.558  1.000 35.832  0 453 VAL BBB CA    1 ? 2 
ATOM   7084  C C     . VAL B 1 453 ? 18.228  -22.365 10.448  1.000 34.529  0 453 VAL BBB C     1 ? 2 
ATOM   7085  O O     . VAL B 1 453 ? 19.221  -23.109 10.554  1.000 32.145  0 453 VAL BBB O     1 ? 2 
ATOM   7086  C CB    . VAL B 1 453 ? 16.555  -23.923 9.330   1.000 36.625  0 453 VAL BBB CB    1 ? 2 
ATOM   7087  C CG1   . VAL B 1 453 ? 15.297  -24.760 9.541   1.000 36.753  0 453 VAL BBB CG1   1 ? 2 
ATOM   7088  C CG2   . VAL B 1 453 ? 16.493  -23.103 8.044   1.000 36.405  0 453 VAL BBB CG2   1 ? 2 
ATOM   7089  N N     . GLY B 1 454 ? 18.251  -21.027 10.267  1.000 34.752  0 454 GLY BBB N     1 ? 2 
ATOM   7090  C CA    . GLY B 1 454 ? 19.487  -20.220 10.188  1.000 34.141  0 454 GLY BBB CA    1 ? 2 
ATOM   7091  C C     . GLY B 1 454 ? 19.323  -18.860 10.844  1.000 32.691  0 454 GLY BBB C     1 ? 2 
ATOM   7092  O O     . GLY B 1 454 ? 18.353  -18.160 10.502  1.000 35.010  0 454 GLY BBB O     1 ? 2 
ATOM   7093  N N     . PHE B 1 455 ? 20.204  -18.541 11.803  1.000 29.812  0 455 PHE BBB N     1 ? 2 
ATOM   7094  C CA    . PHE B 1 455 ? 20.304  -17.230 12.488  1.000 28.302  0 455 PHE BBB CA    1 ? 2 
ATOM   7095  C C     . PHE B 1 455 ? 21.701  -16.641 12.247  1.000 27.260  0 455 PHE BBB C     1 ? 2 
ATOM   7096  O O     . PHE B 1 455 ? 22.684  -17.356 12.433  1.000 27.084  0 455 PHE BBB O     1 ? 2 
ATOM   7097  C CB    . PHE B 1 455 ? 20.008  -17.414 13.975  1.000 27.773  0 455 PHE BBB CB    1 ? 2 
ATOM   7098  C CG    . PHE B 1 455 ? 20.307  -16.199 14.818  1.000 26.746  0 455 PHE BBB CG    1 ? 2 
ATOM   7099  C CD1   . PHE B 1 455 ? 21.617  -15.861 15.124  1.000 25.947  0 455 PHE BBB CD1   1 ? 2 
ATOM   7100  C CD2   . PHE B 1 455 ? 19.293  -15.400 15.314  1.000 26.149  0 455 PHE BBB CD2   1 ? 2 
ATOM   7101  C CE1   . PHE B 1 455 ? 21.903  -14.751 15.900  1.000 24.462  0 455 PHE BBB CE1   1 ? 2 
ATOM   7102  C CE2   . PHE B 1 455 ? 19.579  -14.287 16.085  1.000 25.675  0 455 PHE BBB CE2   1 ? 2 
ATOM   7103  C CZ    . PHE B 1 455 ? 20.891  -13.967 16.379  1.000 24.959  0 455 PHE BBB CZ    1 ? 2 
ATOM   7104  N N     . HIS B 1 456 ? 21.766  -15.360 11.875  1.000 27.228  0 456 HIS BBB N     1 ? 2 
ATOM   7105  C CA    . HIS B 1 456 ? 22.990  -14.667 11.392  1.000 27.692  0 456 HIS BBB CA    1 ? 2 
ATOM   7106  C C     . HIS B 1 456 ? 23.005  -13.240 11.907  1.000 27.031  0 456 HIS BBB C     1 ? 2 
ATOM   7107  O O     . HIS B 1 456 ? 22.020  -12.536 11.686  1.000 28.984  0 456 HIS BBB O     1 ? 2 
ATOM   7108  C CB    . HIS B 1 456 ? 23.037  -14.667 9.848   1.000 28.677  0 456 HIS BBB CB    1 ? 2 
ATOM   7109  C CG    . HIS B 1 456 ? 23.069  -16.038 9.285   1.000 28.440  0 456 HIS BBB CG    1 ? 2 
ATOM   7110  N ND1   . HIS B 1 456 ? 24.257  -16.695 9.038   1.000 28.201  0 456 HIS BBB ND1   1 ? 2 
ATOM   7111  C CD2   . HIS B 1 456 ? 22.082  -16.912 9.008   1.000 29.037  0 456 HIS BBB CD2   1 ? 2 
ATOM   7112  C CE1   . HIS B 1 456 ? 23.998  -17.913 8.583   1.000 29.219  0 456 HIS BBB CE1   1 ? 2 
ATOM   7113  N NE2   . HIS B 1 456 ? 22.667  -18.075 8.565   1.000 29.384  0 456 HIS BBB NE2   1 ? 2 
ATOM   7114  N N     . PHE B 1 457 ? 24.082  -12.809 12.535  1.000 26.181  0 457 PHE BBB N     1 ? 2 
ATOM   7115  C CA    . PHE B 1 457 ? 24.190  -11.421 13.024  1.000 24.964  0 457 PHE BBB CA    1 ? 2 
ATOM   7116  C C     . PHE B 1 457 ? 25.619  -10.928 12.834  1.000 24.869  0 457 PHE BBB C     1 ? 2 
ATOM   7117  O O     . PHE B 1 457 ? 26.533  -11.523 13.380  1.000 24.910  0 457 PHE BBB O     1 ? 2 
ATOM   7118  C CB    . PHE B 1 457 ? 23.772  -11.280 14.484  1.000 24.365  0 457 PHE BBB CB    1 ? 2 
ATOM   7119  C CG    . PHE B 1 457 ? 23.875  -9.852  14.939  1.000 24.819  0 457 PHE BBB CG    1 ? 2 
ATOM   7120  C CD1   . PHE B 1 457 ? 22.884  -8.943  14.608  1.000 25.279  0 457 PHE BBB CD1   1 ? 2 
ATOM   7121  C CD2   . PHE B 1 457 ? 24.994  -9.386  15.614  1.000 24.465  0 457 PHE BBB CD2   1 ? 2 
ATOM   7122  C CE1   . PHE B 1 457 ? 22.999  -7.609  14.969  1.000 25.133  0 457 PHE BBB CE1   1 ? 2 
ATOM   7123  C CE2   . PHE B 1 457 ? 25.101  -8.055  15.975  1.000 24.292  0 457 PHE BBB CE2   1 ? 2 
ATOM   7124  C CZ    . PHE B 1 457 ? 24.100  -7.169  15.654  1.000 24.098  0 457 PHE BBB CZ    1 ? 2 
ATOM   7125  N N     . VAL B 1 458 ? 25.769  -9.895  12.026  1.000 24.834  0 458 VAL BBB N     1 ? 2 
ATOM   7126  C CA    . VAL B 1 458 ? 27.014  -9.127  11.828  1.000 25.285  0 458 VAL BBB CA    1 ? 2 
ATOM   7127  C C     . VAL B 1 458 ? 26.857  -7.837  12.624  1.000 25.565  0 458 VAL BBB C     1 ? 2 
ATOM   7128  O O     . VAL B 1 458 ? 25.808  -7.205  12.452  1.000 27.031  0 458 VAL BBB O     1 ? 2 
ATOM   7129  C CB    . VAL B 1 458 ? 27.263  -8.850  10.332  1.000 25.542  0 458 VAL BBB CB    1 ? 2 
ATOM   7130  C CG1   . VAL B 1 458 ? 28.518  -8.029  10.107  1.000 25.543  0 458 VAL BBB CG1   1 ? 2 
ATOM   7131  C CG2   . VAL B 1 458 ? 27.316  -10.139 9.526   1.000 25.501  0 458 VAL BBB CG2   1 ? 2 
ATOM   7132  N N     . GLY B 1 459 ? 27.874  -7.460  13.411  1.000 24.189  0 459 GLY BBB N     1 ? 2 
ATOM   7133  C CA    . GLY B 1 459 ? 27.831  -6.238  14.235  1.000 23.935  0 459 GLY BBB CA    1 ? 2 
ATOM   7134  C C     . GLY B 1 459 ? 28.635  -6.381  15.531  1.000 23.215  0 459 GLY BBB C     1 ? 2 
ATOM   7135  O O     . GLY B 1 459 ? 29.321  -7.375  15.730  1.000 22.911  0 459 GLY BBB O     1 ? 2 
ATOM   7136  N N     . PRO B 1 460 ? 28.585  -5.392  16.438  1.000 22.820  0 460 PRO BBB N     1 ? 2 
ATOM   7137  C CA    . PRO B 1 460 ? 29.273  -5.471  17.725  1.000 23.463  0 460 PRO BBB CA    1 ? 2 
ATOM   7138  C C     . PRO B 1 460 ? 28.738  -6.586  18.613  1.000 23.769  0 460 PRO BBB C     1 ? 2 
ATOM   7139  O O     . PRO B 1 460 ? 27.575  -6.876  18.522  1.000 26.587  0 460 PRO BBB O     1 ? 2 
ATOM   7140  C CB    . PRO B 1 460 ? 29.031  -4.119  18.402  1.000 22.639  0 460 PRO BBB CB    1 ? 2 
ATOM   7141  C CG    . PRO B 1 460 ? 28.566  -3.215  17.284  1.000 23.447  0 460 PRO BBB CG    1 ? 2 
ATOM   7142  C CD    . PRO B 1 460 ? 27.877  -4.115  16.272  1.000 23.680  0 460 PRO BBB CD    1 ? 2 
ATOM   7143  N N     . ASN B 1 461 ? 29.591  -7.175  19.451  1.000 24.622  0 461 ASN BBB N     1 ? 2 
ATOM   7144  C CA    . ASN B 1 461 ? 29.120  -8.141  20.469  1.000 24.533  0 461 ASN BBB CA    1 ? 2 
ATOM   7145  C C     . ASN B 1 461 ? 28.257  -9.230  19.791  1.000 25.178  0 461 ASN BBB C     1 ? 2 
ATOM   7146  O O     . ASN B 1 461 ? 27.197  -9.606  20.357  1.000 26.738  0 461 ASN BBB O     1 ? 2 
ATOM   7147  C CB    . ASN B 1 461 ? 28.329  -7.386  21.525  1.000 25.320  0 461 ASN BBB CB    1 ? 2 
ATOM   7148  C CG    . ASN B 1 461 ? 29.021  -6.108  21.933  1.000 26.136  0 461 ASN BBB CG    1 ? 2 
ATOM   7149  O OD1   . ASN B 1 461 ? 30.160  -6.147  22.361  1.000 28.271  0 461 ASN BBB OD1   1 ? 2 
ATOM   7150  N ND2   . ASN B 1 461 ? 28.365  -4.977  21.782  1.000 26.372  0 461 ASN BBB ND2   1 ? 2 
ATOM   7151  N N     . ALA B 1 462 ? 28.694  -9.763  18.657  1.000 24.035  0 462 ALA BBB N     1 ? 2 
ATOM   7152  C CA    . ALA B 1 462 ? 27.858  -10.708 17.889  1.000 24.255  0 462 ALA BBB CA    1 ? 2 
ATOM   7153  C C     . ALA B 1 462 ? 27.776  -12.049 18.611  1.000 23.248  0 462 ALA BBB C     1 ? 2 
ATOM   7154  O O     . ALA B 1 462 ? 26.755  -12.718 18.512  1.000 23.010  0 462 ALA BBB O     1 ? 2 
ATOM   7155  C CB    . ALA B 1 462 ? 28.373  -10.868 16.465  1.000 24.559  0 462 ALA BBB CB    1 ? 2 
ATOM   7156  N N     . GLY B 1 463 ? 28.856  -12.477 19.226  1.000 23.828  0 463 GLY BBB N     1 ? 2 
ATOM   7157  C CA    . GLY B 1 463 ? 28.869  -13.687 20.077  1.000 24.866  0 463 GLY BBB CA    1 ? 2 
ATOM   7158  C C     . GLY B 1 463 ? 27.937  -13.539 21.271  1.000 25.111  0 463 GLY BBB C     1 ? 2 
ATOM   7159  O O     . GLY B 1 463 ? 27.157  -14.454 21.552  1.000 24.618  0 463 GLY BBB O     1 ? 2 
ATOM   7160  N N     . GLU B 1 464 ? 27.965  -12.390 21.921  1.000 26.645  0 464 GLU BBB N     1 ? 2 
ATOM   7161  C CA    . GLU B 1 464 ? 27.100  -12.126 23.099  1.000 27.381  0 464 GLU BBB CA    1 ? 2 
ATOM   7162  C C     . GLU B 1 464 ? 25.637  -12.202 22.623  1.000 28.533  0 464 GLU BBB C     1 ? 2 
ATOM   7163  O O     . GLU B 1 464 ? 24.778  -12.716 23.364  1.000 28.586  0 464 GLU BBB O     1 ? 2 
ATOM   7164  C CB    . GLU B 1 464 ? 27.481  -10.798 23.756  1.000 28.155  0 464 GLU BBB CB    1 ? 2 
ATOM   7165  C CG    . GLU B 1 464 ? 28.966  -10.679 24.141  1.000 28.987  0 464 GLU BBB CG    1 ? 2 
ATOM   7166  C CD    . GLU B 1 464 ? 29.552  -11.613 25.186  1.000 29.927  0 464 GLU BBB CD    1 ? 2 
ATOM   7167  O OE1   . GLU B 1 464 ? 28.789  -12.339 25.834  1.000 30.231  0 464 GLU BBB OE1   1 ? 2 
ATOM   7168  O OE2   . GLU B 1 464 ? 30.817  -11.561 25.389  1.000 33.705  0 464 GLU BBB OE2   1 ? 2 
ATOM   7169  N N     . ILE B 1 465 ? 25.344  -11.754 21.406  1.000 28.561  0 465 ILE BBB N     1 ? 2 
ATOM   7170  C CA    . ILE B 1 465 ? 23.947  -11.705 20.883  1.000 26.796  0 465 ILE BBB CA    1 ? 2 
ATOM   7171  C C     . ILE B 1 465 ? 23.534  -13.108 20.465  1.000 25.733  0 465 ILE BBB C     1 ? 2 
ATOM   7172  O O     . ILE B 1 465 ? 22.376  -13.478 20.693  1.000 27.633  0 465 ILE BBB O     1 ? 2 
ATOM   7173  C CB    . ILE B 1 465 ? 23.814  -10.667 19.757  1.000 26.709  0 465 ILE BBB CB    1 ? 2 
ATOM   7174  C CG1   . ILE B 1 465 ? 23.911  -9.257  20.345  1.000 27.491  0 465 ILE BBB CG1   1 ? 2 
ATOM   7175  C CG2   . ILE B 1 465 ? 22.518  -10.860 19.001  1.000 26.299  0 465 ILE BBB CG2   1 ? 2 
ATOM   7176  C CD1   . ILE B 1 465 ? 24.125  -8.146  19.335  1.000 29.360  0 465 ILE BBB CD1   1 ? 2 
ATOM   7177  N N     . THR B 1 466 ? 24.449  -13.889 19.924  1.000 23.636  0 466 THR BBB N     1 ? 2 
ATOM   7178  C CA    . THR B 1 466 ? 24.069  -15.135 19.229  1.000 23.244  0 466 THR BBB CA    1 ? 2 
ATOM   7179  C C     . THR B 1 466 ? 23.867  -16.265 20.221  1.000 23.205  0 466 THR BBB C     1 ? 2 
ATOM   7180  O O     . THR B 1 466 ? 23.106  -17.176 19.899  1.000 23.424  0 466 THR BBB O     1 ? 2 
ATOM   7181  C CB    . THR B 1 466 ? 25.129  -15.515 18.198  1.000 23.088  0 466 THR BBB CB    1 ? 2 
ATOM   7182  O OG1   . THR B 1 466 ? 25.097  -14.549 17.141  1.000 22.466  0 466 THR BBB OG1   1 ? 2 
ATOM   7183  C CG2   . THR B 1 466 ? 24.929  -16.896 17.627  1.000 22.756  0 466 THR BBB CG2   1 ? 2 
ATOM   7184  N N     . GLN B 1 467 ? 24.600  -16.258 21.334  1.000 23.065  0 467 GLN BBB N     1 ? 2 
ATOM   7185  C CA    . GLN B 1 467 ? 24.567  -17.359 22.323  1.000 23.106  0 467 GLN BBB CA    1 ? 2 
ATOM   7186  C C     . GLN B 1 467 ? 23.117  -17.709 22.637  1.000 24.923  0 467 GLN BBB C     1 ? 2 
ATOM   7187  O O     . GLN B 1 467 ? 22.708  -18.872 22.382  1.000 28.014  0 467 GLN BBB O     1 ? 2 
ATOM   7188  C CB    . GLN B 1 467 ? 25.274  -16.978 23.615  1.000 23.042  0 467 GLN BBB CB    1 ? 2 
ATOM   7189  C CG    . GLN B 1 467 ? 25.483  -18.159 24.563  1.000 22.987  0 467 GLN BBB CG    1 ? 2 
ATOM   7190  C CD    . GLN B 1 467 ? 26.364  -19.241 23.980  1.000 23.850  0 467 GLN BBB CD    1 ? 2 
ATOM   7191  O OE1   . GLN B 1 467 ? 27.598  -19.142 23.974  1.000 22.135  0 467 GLN BBB OE1   1 ? 2 
ATOM   7192  N NE2   . GLN B 1 467 ? 25.733  -20.284 23.440  1.000 23.861  0 467 GLN BBB NE2   1 ? 2 
ATOM   7193  N N     . GLY B 1 468 ? 22.336  -16.737 23.082  1.000 23.770  0 468 GLY BBB N     1 ? 2 
ATOM   7194  C CA    . GLY B 1 468 ? 20.963  -16.990 23.542  1.000 23.386  0 468 GLY BBB CA    1 ? 2 
ATOM   7195  C C     . GLY B 1 468 ? 20.075  -17.412 22.421  1.000 23.162  0 468 GLY BBB C     1 ? 2 
ATOM   7196  O O     . GLY B 1 468 ? 19.239  -18.325 22.606  1.000 25.801  0 468 GLY BBB O     1 ? 2 
ATOM   7197  N N     . PHE B 1 469 ? 20.164  -16.712 21.308  1.000 23.319  0 469 PHE BBB N     1 ? 2 
ATOM   7198  C CA    . PHE B 1 469 ? 19.341  -16.988 20.122  1.000 23.548  0 469 PHE BBB CA    1 ? 2 
ATOM   7199  C C     . PHE B 1 469 ? 19.619  -18.397 19.647  1.000 24.712  0 469 PHE BBB C     1 ? 2 
ATOM   7200  O O     . PHE B 1 469 ? 18.661  -19.087 19.289  1.000 27.228  0 469 PHE BBB O     1 ? 2 
ATOM   7201  C CB    . PHE B 1 469 ? 19.585  -15.935 19.058  1.000 22.804  0 469 PHE BBB CB    1 ? 2 
ATOM   7202  C CG    . PHE B 1 469 ? 18.789  -14.685 19.293  1.000 21.695  0 469 PHE BBB CG    1 ? 2 
ATOM   7203  C CD1   . PHE B 1 469 ? 17.399  -14.751 19.283  1.000 21.325  0 469 PHE BBB CD1   1 ? 2 
ATOM   7204  C CD2   . PHE B 1 469 ? 19.411  -13.461 19.473  1.000 20.423  0 469 PHE BBB CD2   1 ? 2 
ATOM   7205  C CE1   . PHE B 1 469 ? 16.651  -13.606 19.479  1.000 20.884  0 469 PHE BBB CE1   1 ? 2 
ATOM   7206  C CE2   . PHE B 1 469 ? 18.660  -12.322 19.671  1.000 20.318  0 469 PHE BBB CE2   1 ? 2 
ATOM   7207  C CZ    . PHE B 1 469 ? 17.278  -12.396 19.652  1.000 20.736  0 469 PHE BBB CZ    1 ? 2 
ATOM   7208  N N     . SER B 1 470 ? 20.875  -18.819 19.688  1.000 25.134  0 470 SER BBB N     1 ? 2 
ATOM   7209  C CA    . SER B 1 470 ? 21.262  -20.201 19.297  1.000 25.530  0 470 SER BBB CA    1 ? 2 
ATOM   7210  C C     . SER B 1 470 ? 20.473  -21.227 20.128  1.000 26.521  0 470 SER BBB C     1 ? 2 
ATOM   7211  O O     . SER B 1 470 ? 20.004  -22.187 19.523  1.000 28.928  0 470 SER BBB O     1 ? 2 
ATOM   7212  C CB    . SER B 1 470 ? 22.781  -20.430 19.373  1.000 24.095  0 470 SER BBB CB    1 ? 2 
ATOM   7213  O OG    . SER B 1 470 ? 23.206  -20.636 20.701  1.000 23.451  0 470 SER BBB OG    1 ? 2 
ATOM   7214  N N     . LEU B 1 471 ? 20.348  -21.047 21.443  1.000 26.672  0 471 LEU BBB N     1 ? 2 
ATOM   7215  C CA    . LEU B 1 471 ? 19.503  -21.922 22.297  1.000 29.030  0 471 LEU BBB CA    1 ? 2 
ATOM   7216  C C     . LEU B 1 471 ? 18.045  -21.900 21.810  1.000 29.945  0 471 LEU BBB C     1 ? 2 
ATOM   7217  O O     . LEU B 1 471 ? 17.447  -22.982 21.708  1.000 29.316  0 471 LEU BBB O     1 ? 2 
ATOM   7218  C CB    . LEU B 1 471 ? 19.539  -21.474 23.760  1.000 28.891  0 471 LEU BBB CB    1 ? 2 
ATOM   7219  C CG    . LEU B 1 471 ? 18.677  -22.323 24.700  1.000 29.829  0 471 LEU BBB CG    1 ? 2 
ATOM   7220  C CD1   . LEU B 1 471 ? 18.965  -23.799 24.535  1.000 31.685  0 471 LEU BBB CD1   1 ? 2 
ATOM   7221  C CD2   . LEU B 1 471 ? 18.913  -21.959 26.155  1.000 29.705  0 471 LEU BBB CD2   1 ? 2 
ATOM   7222  N N     . ALA B 1 472 ? 17.481  -20.711 21.601  1.000 31.485  0 472 ALA BBB N     1 ? 2 
ATOM   7223  C CA    . ALA B 1 472 ? 16.073  -20.530 21.163  1.000 31.617  0 472 ALA BBB CA    1 ? 2 
ATOM   7224  C C     . ALA B 1 472 ? 15.900  -21.249 19.821  1.000 31.432  0 472 ALA BBB C     1 ? 2 
ATOM   7225  O O     . ALA B 1 472 ? 14.881  -21.929 19.607  1.000 30.198  0 472 ALA BBB O     1 ? 2 
ATOM   7226  C CB    . ALA B 1 472 ? 15.732  -19.074 21.051  1.000 30.357  0 472 ALA BBB CB    1 ? 2 
ATOM   7227  N N     . VAL B 1 473 ? 16.873  -21.123 18.941  1.000 31.518  0 473 VAL BBB N     1 ? 2 
ATOM   7228  C CA    . VAL B 1 473 ? 16.753  -21.722 17.580  1.000 33.673  0 473 VAL BBB CA    1 ? 2 
ATOM   7229  C C     . VAL B 1 473 ? 16.794  -23.244 17.759  1.000 36.193  0 473 VAL BBB C     1 ? 2 
ATOM   7230  O O     . VAL B 1 473 ? 15.988  -23.929 17.108  1.000 41.636  0 473 VAL BBB O     1 ? 2 
ATOM   7231  C CB    . VAL B 1 473 ? 17.818  -21.197 16.597  1.000 31.894  0 473 VAL BBB CB    1 ? 2 
ATOM   7232  C CG1   . VAL B 1 473 ? 17.901  -22.042 15.332  1.000 33.365  0 473 VAL BBB CG1   1 ? 2 
ATOM   7233  C CG2   . VAL B 1 473 ? 17.558  -19.744 16.232  1.000 31.160  0 473 VAL BBB CG2   1 ? 2 
ATOM   7234  N N     . LYS B 1 474 ? 17.631  -23.744 18.669  1.000 37.077  0 474 LYS BBB N     1 ? 2 
ATOM   7235  C CA    . LYS B 1 474 ? 17.759  -25.204 18.942  1.000 37.909  0 474 LYS BBB CA    1 ? 2 
ATOM   7236  C C     . LYS B 1 474 ? 16.435  -25.760 19.500  1.000 35.683  0 474 LYS BBB C     1 ? 2 
ATOM   7237  O O     . LYS B 1 474 ? 16.082  -26.910 19.132  1.000 34.203  0 474 LYS BBB O     1 ? 2 
ATOM   7238  C CB    . LYS B 1 474 ? 18.938  -25.449 19.887  1.000 37.717  0 474 LYS BBB CB    1 ? 2 
ATOM   7239  C CG    . LYS B 1 474 ? 19.192  -26.910 20.205  1.000 39.339  0 474 LYS BBB CG    1 ? 2 
ATOM   7240  C CD    . LYS B 1 474 ? 20.327  -27.140 21.131  1.000 40.224  0 474 LYS BBB CD    1 ? 2 
ATOM   7241  C CE    . LYS B 1 474 ? 20.712  -28.599 21.221  1.000 41.017  0 474 LYS BBB CE    1 ? 2 
ATOM   7242  N NZ    . LYS B 1 474 ? 21.695  -28.803 22.318  1.000 40.167  0 474 LYS BBB NZ    1 ? 2 
ATOM   7243  N N     . LEU B 1 475 ? 15.708  -24.958 20.287  1.000 34.707  0 475 LEU BBB N     1 ? 2 
ATOM   7244  C CA    . LEU B 1 475 ? 14.402  -25.343 20.895  1.000 35.209  0 475 LEU BBB CA    1 ? 2 
ATOM   7245  C C     . LEU B 1 475 ? 13.244  -25.272 19.891  1.000 33.959  0 475 LEU BBB C     1 ? 2 
ATOM   7246  O O     . LEU B 1 475 ? 12.148  -25.688 20.277  1.000 33.763  0 475 LEU BBB O     1 ? 2 
ATOM   7247  C CB    . LEU B 1 475 ? 14.132  -24.484 22.146  1.000 34.936  0 475 LEU BBB CB    1 ? 2 
ATOM   7248  C CG    . LEU B 1 475 ? 14.997  -24.832 23.365  1.000 34.145  0 475 LEU BBB CG    1 ? 2 
ATOM   7249  C CD1   . LEU B 1 475 ? 14.789  -23.892 24.540  1.000 32.635  0 475 LEU BBB CD1   1 ? 2 
ATOM   7250  C CD2   . LEU B 1 475 ? 14.736  -26.263 23.815  1.000 34.785  0 475 LEU BBB CD2   1 ? 2 
ATOM   7251  N N     . GLY B 1 476 ? 13.467  -24.776 18.671  1.000 34.898  0 476 GLY BBB N     1 ? 2 
ATOM   7252  C CA    . GLY B 1 476 ? 12.473  -24.812 17.574  1.000 33.762  0 476 GLY BBB CA    1 ? 2 
ATOM   7253  C C     . GLY B 1 476 ? 11.684  -23.522 17.428  1.000 34.294  0 476 GLY BBB C     1 ? 2 
ATOM   7254  O O     . GLY B 1 476 ? 10.467  -23.571 17.129  1.000 37.053  0 476 GLY BBB O     1 ? 2 
ATOM   7255  N N     . ALA B 1 477 ? 12.334  -22.387 17.635  1.000 33.210  0 477 ALA BBB N     1 ? 2 
ATOM   7256  C CA    . ALA B 1 477 ? 11.740  -21.033 17.491  1.000 33.474  0 477 ALA BBB CA    1 ? 2 
ATOM   7257  C C     . ALA B 1 477 ? 11.256  -20.819 16.043  1.000 33.297  0 477 ALA BBB C     1 ? 2 
ATOM   7258  O O     . ALA B 1 477 ? 11.981  -21.159 15.117  1.000 33.291  0 477 ALA BBB O     1 ? 2 
ATOM   7259  C CB    . ALA B 1 477 ? 12.773  -19.998 17.883  1.000 32.587  0 477 ALA BBB CB    1 ? 2 
ATOM   7260  N N     . THR B 1 478 ? 10.074  -20.253 15.856  1.000 34.051  0 478 THR BBB N     1 ? 2 
ATOM   7261  C CA    . THR B 1 478 ? 9.492   -19.885 14.535  1.000 34.584  0 478 THR BBB CA    1 ? 2 
ATOM   7262  C C     . THR B 1 478 ? 9.621   -18.370 14.311  1.000 34.100  0 478 THR BBB C     1 ? 2 
ATOM   7263  O O     . THR B 1 478 ? 9.818   -17.616 15.284  1.000 30.684  0 478 THR BBB O     1 ? 2 
ATOM   7264  C CB    . THR B 1 478 ? 8.015   -20.292 14.446  1.000 36.170  0 478 THR BBB CB    1 ? 2 
ATOM   7265  O OG1   . THR B 1 478 ? 7.329   -19.501 15.411  1.000 36.287  0 478 THR BBB OG1   1 ? 2 
ATOM   7266  C CG2   . THR B 1 478 ? 7.755   -21.757 14.735  1.000 37.284  0 478 THR BBB CG2   1 ? 2 
ATOM   7267  N N     . LYS B 1 479 ? 9.415   -17.922 13.075  1.000 34.577  0 479 LYS BBB N     1 ? 2 
ATOM   7268  C CA    . LYS B 1 479 ? 9.359   -16.470 12.800  1.000 35.815  0 479 LYS BBB CA    1 ? 2 
ATOM   7269  C C     . LYS B 1 479 ? 8.273   -15.818 13.664  1.000 34.220  0 479 LYS BBB C     1 ? 2 
ATOM   7270  O O     . LYS B 1 479 ? 8.508   -14.681 14.100  1.000 33.437  0 479 LYS BBB O     1 ? 2 
ATOM   7271  C CB    . LYS B 1 479 ? 9.195   -16.186 11.308  1.000 37.775  0 479 LYS BBB CB    1 ? 2 
ATOM   7272  C CG    . LYS B 1 479 ? 9.191   -14.700 10.957  1.000 38.955  0 479 LYS BBB CG    1 ? 2 
ATOM   7273  C CD    . LYS B 1 479 ? 10.373  -13.945 11.515  1.000 38.994  0 479 LYS BBB CD    1 ? 2 
ATOM   7274  C CE    . LYS B 1 479 ? 10.639  -12.642 10.783  1.000 40.164  0 479 LYS BBB CE    1 ? 2 
ATOM   7275  N NZ    . LYS B 1 479 ? 9.457   -11.745 10.846  1.000 41.545  0 479 LYS BBB NZ    1 ? 2 
ATOM   7276  N N     . LYS B 1 480 ? 7.161   -16.499 13.945  1.000 35.853  0 480 LYS BBB N     1 ? 2 
ATOM   7277  C CA    . LYS B 1 480 ? 6.053   -15.956 14.790  1.000 37.994  0 480 LYS BBB CA    1 ? 2 
ATOM   7278  C C     . LYS B 1 480 ? 6.614   -15.700 16.204  1.000 36.941  0 480 LYS BBB C     1 ? 2 
ATOM   7279  O O     . LYS B 1 480 ? 6.388   -14.604 16.763  1.000 35.951  0 480 LYS BBB O     1 ? 2 
ATOM   7280  C CB    . LYS B 1 480 ? 4.805   -16.861 14.776  1.000 38.494  0 480 LYS BBB CB    1 ? 2 
ATOM   7281  C CG    . LYS B 1 480 ? 3.715   -16.476 15.769  1.000 39.049  0 480 LYS BBB CG    1 ? 2 
ATOM   7282  C CD    . LYS B 1 480 ? 2.302   -16.850 15.342  1.000 42.754  0 480 LYS BBB CD    1 ? 2 
ATOM   7283  C CE    . LYS B 1 480 ? 1.247   -16.840 16.449  1.000 43.341  0 480 LYS BBB CE    1 ? 2 
ATOM   7284  N NZ    . LYS B 1 480 ? 1.237   -15.587 17.262  1.000 41.802  0 480 LYS BBB NZ    1 ? 2 
ATOM   7285  N N     . ASP B 1 481 ? 7.347   -16.667 16.748  1.000 37.596  0 481 ASP BBB N     1 ? 2 
ATOM   7286  C CA    . ASP B 1 481 ? 8.018   -16.556 18.077  1.000 37.194  0 481 ASP BBB CA    1 ? 2 
ATOM   7287  C C     . ASP B 1 481 ? 8.899   -15.311 18.129  1.000 35.234  0 481 ASP BBB C     1 ? 2 
ATOM   7288  O O     . ASP B 1 481 ? 8.870   -14.604 19.167  1.000 34.017  0 481 ASP BBB O     1 ? 2 
ATOM   7289  C CB    . ASP B 1 481 ? 8.860   -17.788 18.377  1.000 37.909  0 481 ASP BBB CB    1 ? 2 
ATOM   7290  C CG    . ASP B 1 481 ? 8.014   -19.035 18.537  1.000 39.737  0 481 ASP BBB CG    1 ? 2 
ATOM   7291  O OD1   . ASP B 1 481 ? 6.845   -18.894 18.983  1.000 40.630  0 481 ASP BBB OD1   1 ? 2 
ATOM   7292  O OD2   . ASP B 1 481 ? 8.531   -20.132 18.221  1.000 43.478  0 481 ASP BBB OD2   1 ? 2 
ATOM   7293  N N     . PHE B 1 482 ? 9.644   -15.054 17.050  1.000 34.016  0 482 PHE BBB N     1 ? 2 
ATOM   7294  C CA    . PHE B 1 482 ? 10.552  -13.885 16.945  1.000 34.175  0 482 PHE BBB CA    1 ? 2 
ATOM   7295  C C     . PHE B 1 482 ? 9.726   -12.586 16.909  1.000 36.101  0 482 PHE BBB C     1 ? 2 
ATOM   7296  O O     . PHE B 1 482 ? 10.096  -11.634 17.611  1.000 36.345  0 482 PHE BBB O     1 ? 2 
ATOM   7297  C CB    . PHE B 1 482 ? 11.479  -14.049 15.752  1.000 32.929  0 482 PHE BBB CB    1 ? 2 
ATOM   7298  C CG    . PHE B 1 482 ? 12.755  -14.802 16.039  1.000 31.488  0 482 PHE BBB CG    1 ? 2 
ATOM   7299  C CD1   . PHE B 1 482 ? 12.780  -16.185 16.070  1.000 32.418  0 482 PHE BBB CD1   1 ? 2 
ATOM   7300  C CD2   . PHE B 1 482 ? 13.952  -14.138 16.194  1.000 29.801  0 482 PHE BBB CD2   1 ? 2 
ATOM   7301  C CE1   . PHE B 1 482 ? 13.966  -16.876 16.255  1.000 30.683  0 482 PHE BBB CE1   1 ? 2 
ATOM   7302  C CE2   . PHE B 1 482 ? 15.134  -14.828 16.418  1.000 29.067  0 482 PHE BBB CE2   1 ? 2 
ATOM   7303  C CZ    . PHE B 1 482 ? 15.138  -16.197 16.439  1.000 29.439  0 482 PHE BBB CZ    1 ? 2 
ATOM   7304  N N     . ASP B 1 483 ? 8.604   -12.558 16.173  1.000 36.792  0 483 ASP BBB N     1 ? 2 
ATOM   7305  C CA    . ASP B 1 483 ? 7.741   -11.349 16.038  1.000 35.622  0 483 ASP BBB CA    1 ? 2 
ATOM   7306  C C     . ASP B 1 483 ? 7.040   -11.042 17.359  1.000 35.096  0 483 ASP BBB C     1 ? 2 
ATOM   7307  O O     . ASP B 1 483 ? 6.761   -9.857  17.565  1.000 38.971  0 483 ASP BBB O     1 ? 2 
ATOM   7308  C CB    . ASP B 1 483 ? 6.677   -11.515 14.953  1.000 36.333  0 483 ASP BBB CB    1 ? 2 
ATOM   7309  C CG    . ASP B 1 483 ? 7.249   -11.522 13.538  1.000 36.412  0 483 ASP BBB CG    1 ? 2 
ATOM   7310  O OD1   . ASP B 1 483 ? 8.437   -11.103 13.384  1.000 36.751  0 483 ASP BBB OD1   1 ? 2 
ATOM   7311  O OD2   . ASP B 1 483 ? 6.520   -11.963 12.575  1.000 35.881  0 483 ASP BBB OD2   1 ? 2 
ATOM   7312  N N     . ASP B 1 484 ? 6.722   -12.048 18.176  1.000 32.937  0 484 ASP BBB N     1 ? 2 
ATOM   7313  C CA    . ASP B 1 484 ? 5.959   -11.856 19.435  1.000 33.795  0 484 ASP BBB CA    1 ? 2 
ATOM   7314  C C     . ASP B 1 484 ? 6.914   -11.614 20.620  1.000 32.840  0 484 ASP BBB C     1 ? 2 
ATOM   7315  O O     . ASP B 1 484 ? 6.393   -11.328 21.736  1.000 31.187  0 484 ASP BBB O     1 ? 2 
ATOM   7316  C CB    . ASP B 1 484 ? 5.039   -13.041 19.726  1.000 35.604  0 484 ASP BBB CB    1 ? 2 
ATOM   7317  C CG    . ASP B 1 484 ? 3.983   -13.334 18.672  1.000 37.429  0 484 ASP BBB CG    1 ? 2 
ATOM   7318  O OD1   . ASP B 1 484 ? 3.846   -12.509 17.715  1.000 37.480  0 484 ASP BBB OD1   1 ? 2 
ATOM   7319  O OD2   . ASP B 1 484 ? 3.347   -14.432 18.792  1.000 39.251  0 484 ASP BBB OD2   1 ? 2 
ATOM   7320  N N     . MET B 1 485 ? 8.232   -11.695 20.376  1.000 32.664  0 485 MET BBB N     1 ? 2 
ATOM   7321  C CA    . MET B 1 485 ? 9.305   -11.477 21.386  1.000 30.103  0 485 MET BBB CA    1 ? 2 
ATOM   7322  C C     . MET B 1 485 ? 9.377   -9.985  21.760  1.000 27.972  0 485 MET BBB C     1 ? 2 
ATOM   7323  O O     . MET B 1 485 ? 9.467   -9.119  20.881  1.000 26.680  0 485 MET BBB O     1 ? 2 
ATOM   7324  C CB    . MET B 1 485 ? 10.659  -11.932 20.815  1.000 30.014  0 485 MET BBB CB    1 ? 2 
ATOM   7325  C CG    . MET B 1 485 ? 11.858  -11.533 21.624  1.000 30.190  0 485 MET BBB CG    1 ? 2 
ATOM   7326  S SD    . MET B 1 485 ? 13.487  -11.977 20.928  1.000 29.444  0 485 MET BBB SD    1 ? 2 
ATOM   7327  C CE    . MET B 1 485 ? 13.368  -11.309 19.290  1.000 29.346  0 485 MET BBB CE    1 ? 2 
ATOM   7328  N N     . ILE B 1 486 ? 9.344   -9.680  23.051  1.000 28.362  0 486 ILE BBB N     1 ? 2 
ATOM   7329  C CA    . ILE B 1 486 ? 9.524   -8.270  23.519  1.000 27.909  0 486 ILE BBB CA    1 ? 2 
ATOM   7330  C C     . ILE B 1 486 ? 11.023  -7.949  23.456  1.000 28.662  0 486 ILE BBB C     1 ? 2 
ATOM   7331  O O     . ILE B 1 486 ? 11.862  -8.786  23.895  1.000 26.537  0 486 ILE BBB O     1 ? 2 
ATOM   7332  C CB    . ILE B 1 486 ? 8.967   -8.042  24.925  1.000 28.640  0 486 ILE BBB CB    1 ? 2 
ATOM   7333  C CG1   . ILE B 1 486 ? 7.523   -8.564  25.081  1.000 29.485  0 486 ILE BBB CG1   1 ? 2 
ATOM   7334  C CG2   . ILE B 1 486 ? 9.140   -6.573  25.299  1.000 26.765  0 486 ILE BBB CG2   1 ? 2 
ATOM   7335  C CD1   . ILE B 1 486 ? 6.491   -7.640  24.453  1.000 29.671  0 486 ILE BBB CD1   1 ? 2 
ATOM   7336  N N     . GLY B 1 487 ? 11.329  -6.792  22.875  1.000 28.383  0 487 GLY BBB N     1 ? 2 
ATOM   7337  C CA    . GLY B 1 487 ? 12.690  -6.275  22.716  1.000 27.160  0 487 GLY BBB CA    1 ? 2 
ATOM   7338  C C     . GLY B 1 487 ? 13.165  -5.595  23.992  1.000 27.013  0 487 GLY BBB C     1 ? 2 
ATOM   7339  O O     . GLY B 1 487 ? 12.311  -5.117  24.819  1.000 26.097  0 487 GLY BBB O     1 ? 2 
ATOM   7340  N N     . ILE B 1 488 ? 14.474  -5.623  24.180  1.000 25.579  0 488 ILE BBB N     1 ? 2 
ATOM   7341  C CA    . ILE B 1 488 ? 15.241  -4.752  25.117  1.000 26.093  0 488 ILE BBB CA    1 ? 2 
ATOM   7342  C C     . ILE B 1 488 ? 15.740  -3.555  24.313  1.000 27.317  0 488 ILE BBB C     1 ? 2 
ATOM   7343  O O     . ILE B 1 488 ? 16.405  -3.781  23.292  1.000 27.144  0 488 ILE BBB O     1 ? 2 
ATOM   7344  C CB    . ILE B 1 488 ? 16.417  -5.495  25.769  1.000 24.423  0 488 ILE BBB CB    1 ? 2 
ATOM   7345  C CG1   . ILE B 1 488 ? 15.991  -6.837  26.372  1.000 23.734  0 488 ILE BBB CG1   1 ? 2 
ATOM   7346  C CG2   . ILE B 1 488 ? 17.069  -4.581  26.798  1.000 25.173  0 488 ILE BBB CG2   1 ? 2 
ATOM   7347  C CD1   . ILE B 1 488 ? 17.117  -7.638  26.942  1.000 23.158  0 488 ILE BBB CD1   1 ? 2 
ATOM   7348  N N     . HIS B 1 489 ? 15.407  -2.351  24.749  1.000 27.723  0 489 HIS BBB N     1 ? 2 
ATOM   7349  C CA    . HIS B 1 489 ? 15.738  -1.096  24.034  1.000 29.441  0 489 HIS BBB CA    1 ? 2 
ATOM   7350  C C     . HIS B 1 489 ? 16.594  -0.242  24.953  1.000 28.750  0 489 HIS BBB C     1 ? 2 
ATOM   7351  O O     . HIS B 1 489 ? 16.310  -0.177  26.143  1.000 29.391  0 489 HIS BBB O     1 ? 2 
ATOM   7352  C CB    . HIS B 1 489 ? 14.448  -0.353  23.680  1.000 31.941  0 489 HIS BBB CB    1 ? 2 
ATOM   7353  C CG    . HIS B 1 489 ? 14.672  0.869   22.871  1.000 35.343  0 489 HIS BBB CG    1 ? 2 
ATOM   7354  N ND1   . HIS B 1 489 ? 15.305  0.830   21.635  1.000 38.379  0 489 HIS BBB ND1   1 ? 2 
ATOM   7355  C CD2   . HIS B 1 489 ? 14.296  2.145   23.088  1.000 37.093  0 489 HIS BBB CD2   1 ? 2 
ATOM   7356  C CE1   . HIS B 1 489 ? 15.330  2.050   21.139  1.000 41.360  0 489 HIS BBB CE1   1 ? 2 
ATOM   7357  N NE2   . HIS B 1 489 ? 14.715  2.873   22.013  1.000 40.159  0 489 HIS BBB NE2   1 ? 2 
ATOM   7358  N N     . PRO B 1 490 ? 17.642  0.443   24.457  1.000 26.732  0 490 PRO BBB N     1 ? 2 
ATOM   7359  C CA    . PRO B 1 490 ? 18.149  0.287   23.099  1.000 26.600  0 490 PRO BBB CA    1 ? 2 
ATOM   7360  C C     . PRO B 1 490 ? 19.238  -0.790  23.019  1.000 25.717  0 490 PRO BBB C     1 ? 2 
ATOM   7361  O O     . PRO B 1 490 ? 20.173  -0.739  23.832  1.000 25.812  0 490 PRO BBB O     1 ? 2 
ATOM   7362  C CB    . PRO B 1 490 ? 18.780  1.639   22.790  1.000 27.021  0 490 PRO BBB CB    1 ? 2 
ATOM   7363  C CG    . PRO B 1 490 ? 18.581  2.450   24.063  1.000 27.460  0 490 PRO BBB CG    1 ? 2 
ATOM   7364  C CD    . PRO B 1 490 ? 18.401  1.447   25.187  1.000 26.885  0 490 PRO BBB CD    1 ? 2 
ATOM   7365  N N     . THR B 1 491 ? 19.026  -1.791  22.163  1.000 24.289  0 491 THR BBB N     1 ? 2 
ATOM   7366  C CA    . THR B 1 491 ? 20.026  -2.820  21.836  1.000 24.610  0 491 THR BBB CA    1 ? 2 
ATOM   7367  C C     . THR B 1 491 ? 20.058  -2.996  20.325  1.000 24.805  0 491 THR BBB C     1 ? 2 
ATOM   7368  O O     . THR B 1 491 ? 19.150  -2.502  19.644  1.000 24.719  0 491 THR BBB O     1 ? 2 
ATOM   7369  C CB    . THR B 1 491 ? 19.741  -4.167  22.523  1.000 24.410  0 491 THR BBB CB    1 ? 2 
ATOM   7370  O OG1   . THR B 1 491 ? 18.545  -4.744  22.025  1.000 24.285  0 491 THR BBB OG1   1 ? 2 
ATOM   7371  C CG2   . THR B 1 491 ? 19.627  -4.046  24.024  1.000 23.913  0 491 THR BBB CG2   1 ? 2 
ATOM   7372  N N     . ASP B 1 492 ? 21.076  -3.698  19.826  1.000 23.965  0 492 ASP BBB N     1 ? 2 
ATOM   7373  C CA    . ASP B 1 492 ? 21.076  -4.230  18.450  1.000 23.775  0 492 ASP BBB CA    1 ? 2 
ATOM   7374  C C     . ASP B 1 492 ? 20.192  -5.489  18.397  1.000 22.952  0 492 ASP BBB C     1 ? 2 
ATOM   7375  O O     . ASP B 1 492 ? 19.539  -5.706  17.369  1.000 24.425  0 492 ASP BBB O     1 ? 2 
ATOM   7376  C CB    . ASP B 1 492 ? 22.510  -4.425  17.973  1.000 23.875  0 492 ASP BBB CB    1 ? 2 
ATOM   7377  C CG    . ASP B 1 492 ? 23.261  -3.103  17.863  1.000 25.192  0 492 ASP BBB CG    1 ? 2 
ATOM   7378  O OD1   . ASP B 1 492 ? 22.601  -2.035  17.687  1.000 25.361  0 492 ASP BBB OD1   1 ? 2 
ATOM   7379  O OD2   . ASP B 1 492 ? 24.523  -3.130  17.889  1.000 26.413  0 492 ASP BBB OD2   1 ? 2 
ATOM   7380  N N     . ALA B 1 493 ? 20.148  -6.301  19.435  1.000 21.695  0 493 ALA BBB N     1 ? 2 
ATOM   7381  C CA    . ALA B 1 493 ? 19.538  -7.644  19.387  1.000 21.765  0 493 ALA BBB CA    1 ? 2 
ATOM   7382  C C     . ALA B 1 493 ? 18.008  -7.533  19.339  1.000 23.334  0 493 ALA BBB C     1 ? 2 
ATOM   7383  O O     . ALA B 1 493 ? 17.371  -8.538  18.907  1.000 22.572  0 493 ALA BBB O     1 ? 2 
ATOM   7384  C CB    . ALA B 1 493 ? 19.967  -8.458  20.575  1.000 21.310  0 493 ALA BBB CB    1 ? 2 
ATOM   7385  N N     . GLU B 1 494 ? 17.417  -6.394  19.739  1.000 24.131  0 494 GLU BBB N     1 ? 2 
ATOM   7386  C CA    . GLU B 1 494 ? 15.948  -6.187  19.623  1.000 26.091  0 494 GLU BBB CA    1 ? 2 
ATOM   7387  C C     . GLU B 1 494 ? 15.513  -6.188  18.141  1.000 26.514  0 494 GLU BBB C     1 ? 2 
ATOM   7388  O O     . GLU B 1 494 ? 14.322  -6.446  17.853  1.000 25.643  0 494 GLU BBB O     1 ? 2 
ATOM   7389  C CB    . GLU B 1 494 ? 15.531  -4.902  20.334  1.000 27.702  0 494 GLU BBB CB    1 ? 2 
ATOM   7390  C CG    . GLU B 1 494 ? 15.968  -3.614  19.682  1.000 29.294  0 494 GLU BBB CG    1 ? 2 
ATOM   7391  C CD    . GLU B 1 494 ? 15.392  -2.377  20.356  1.000 32.180  0 494 GLU BBB CD    1 ? 2 
ATOM   7392  O OE1   . GLU B 1 494 ? 14.164  -2.419  20.688  1.000 34.347  0 494 GLU BBB OE1   1 ? 2 
ATOM   7393  O OE2   . GLU B 1 494 ? 16.160  -1.357  20.563  1.000 32.934  0 494 GLU BBB OE2   1 ? 2 
ATOM   7394  N N     . VAL B 1 495 ? 16.443  -5.941  17.207  1.000 26.762  0 495 VAL BBB N     1 ? 2 
ATOM   7395  C CA    . VAL B 1 495 ? 16.100  -5.958  15.756  1.000 26.641  0 495 VAL BBB CA    1 ? 2 
ATOM   7396  C C     . VAL B 1 495 ? 15.433  -7.296  15.409  1.000 26.707  0 495 VAL BBB C     1 ? 2 
ATOM   7397  O O     . VAL B 1 495 ? 14.473  -7.268  14.608  1.000 28.020  0 495 VAL BBB O     1 ? 2 
ATOM   7398  C CB    . VAL B 1 495 ? 17.316  -5.679  14.861  1.000 26.115  0 495 VAL BBB CB    1 ? 2 
ATOM   7399  C CG1   . VAL B 1 495 ? 18.199  -6.896  14.709  1.000 25.900  0 495 VAL BBB CG1   1 ? 2 
ATOM   7400  C CG2   . VAL B 1 495 ? 16.866  -5.155  13.501  1.000 26.854  0 495 VAL BBB CG2   1 ? 2 
ATOM   7401  N N     . PHE B 1 496 ? 15.840  -8.407  16.042  1.000 26.189  0 496 PHE BBB N     1 ? 2 
ATOM   7402  C CA    . PHE B 1 496 ? 15.314  -9.762  15.722  1.000 27.130  0 496 PHE BBB CA    1 ? 2 
ATOM   7403  C C     . PHE B 1 496 ? 13.811  -9.899  16.005  1.000 29.232  0 496 PHE BBB C     1 ? 2 
ATOM   7404  O O     . PHE B 1 496 ? 13.257  -10.937 15.605  1.000 32.314  0 496 PHE BBB O     1 ? 2 
ATOM   7405  C CB    . PHE B 1 496 ? 16.125  -10.839 16.409  1.000 25.003  0 496 PHE BBB CB    1 ? 2 
ATOM   7406  C CG    . PHE B 1 496 ? 17.412  -11.065 15.683  1.000 25.341  0 496 PHE BBB CG    1 ? 2 
ATOM   7407  C CD1   . PHE B 1 496 ? 17.415  -11.727 14.459  1.000 25.454  0 496 PHE BBB CD1   1 ? 2 
ATOM   7408  C CD2   . PHE B 1 496 ? 18.599  -10.539 16.161  1.000 24.083  0 496 PHE BBB CD2   1 ? 2 
ATOM   7409  C CE1   . PHE B 1 496 ? 18.599  -11.921 13.762  1.000 26.065  0 496 PHE BBB CE1   1 ? 2 
ATOM   7410  C CE2   . PHE B 1 496 ? 19.780  -10.705 15.444  1.000 25.124  0 496 PHE BBB CE2   1 ? 2 
ATOM   7411  C CZ    . PHE B 1 496 ? 19.785  -11.413 14.254  1.000 25.764  0 496 PHE BBB CZ    1 ? 2 
ATOM   7412  N N     . GLY B 1 497 ? 13.167  -8.891  16.579  1.000 29.483  0 497 GLY BBB N     1 ? 2 
ATOM   7413  C CA    . GLY B 1 497 ? 11.727  -8.952  16.883  1.000 30.067  0 497 GLY BBB CA    1 ? 2 
ATOM   7414  C C     . GLY B 1 497 ? 10.879  -8.158  15.915  1.000 31.109  0 497 GLY BBB C     1 ? 2 
ATOM   7415  O O     . GLY B 1 497 ? 9.682   -8.213  16.051  1.000 30.044  0 497 GLY BBB O     1 ? 2 
ATOM   7416  N N     . ILE B 1 498 ? 11.482  -7.448  14.959  1.000 32.541  0 498 ILE BBB N     1 ? 2 
ATOM   7417  C CA    . ILE B 1 498 ? 10.741  -6.575  14.009  1.000 32.398  0 498 ILE BBB CA    1 ? 2 
ATOM   7418  C C     . ILE B 1 498 ? 11.311  -6.735  12.600  1.000 32.614  0 498 ILE BBB C     1 ? 2 
ATOM   7419  O O     . ILE B 1 498 ? 11.300  -5.749  11.849  1.000 31.626  0 498 ILE BBB O     1 ? 2 
ATOM   7420  C CB    . ILE B 1 498 ? 10.823  -5.115  14.487  1.000 33.122  0 498 ILE BBB CB    1 ? 2 
ATOM   7421  C CG1   . ILE B 1 498 ? 12.288  -4.660  14.632  1.000 33.676  0 498 ILE BBB CG1   1 ? 2 
ATOM   7422  C CG2   . ILE B 1 498 ? 9.996   -4.923  15.749  1.000 32.250  0 498 ILE BBB CG2   1 ? 2 
ATOM   7423  C CD1   . ILE B 1 498 ? 12.469  -3.148  14.641  1.000 34.001  0 498 ILE BBB CD1   1 ? 2 
ATOM   7424  N N     . LEU B 1 499 ? 11.851  -7.899  12.254  1.000 32.806  0 499 LEU BBB N     1 ? 2 
ATOM   7425  C CA    . LEU B 1 499 ? 12.327  -8.144  10.878  1.000 34.425  0 499 LEU BBB CA    1 ? 2 
ATOM   7426  C C     . LEU B 1 499 ? 11.089  -8.377  10.006  1.000 38.994  0 499 LEU BBB C     1 ? 2 
ATOM   7427  O O     . LEU B 1 499 ? 10.203  -9.149  10.440  1.000 40.958  0 499 LEU BBB O     1 ? 2 
ATOM   7428  C CB    . LEU B 1 499 ? 13.248  -9.359  10.866  1.000 33.330  0 499 LEU BBB CB    1 ? 2 
ATOM   7429  C CG    . LEU B 1 499 ? 14.604  -9.202  11.553  1.000 32.065  0 499 LEU BBB CG    1 ? 2 
ATOM   7430  C CD1   . LEU B 1 499 ? 15.229  -10.562 11.713  1.000 31.849  0 499 LEU BBB CD1   1 ? 2 
ATOM   7431  C CD2   . LEU B 1 499 ? 15.534  -8.283  10.788  1.000 31.919  0 499 LEU BBB CD2   1 ? 2 
ATOM   7432  N N     . GLU B 1 500 ? 10.978  -7.708  8.859   1.000 42.954  0 500 GLU BBB N     1 ? 2 
ATOM   7433  C CA    . GLU B 1 500 ? 9.761   -7.801  7.995   1.000 45.406  0 500 GLU BBB CA    1 ? 2 
ATOM   7434  C C     . GLU B 1 500 ? 10.124  -7.839  6.504   1.000 44.445  0 500 GLU BBB C     1 ? 2 
ATOM   7435  O O     . GLU B 1 500 ? 9.315   -8.377  5.753   1.000 48.493  0 500 GLU BBB O     1 ? 2 
ATOM   7436  C CB    . GLU B 1 500 ? 8.748   -6.687  8.298   1.000 47.049  0 500 GLU BBB CB    1 ? 2 
ATOM   7437  C CG    . GLU B 1 500 ? 9.315   -5.296  8.246   1.000 48.670  0 500 GLU BBB CG    1 ? 2 
ATOM   7438  C CD    . GLU B 1 500 ? 8.345   -4.219  8.711   1.000 54.631  0 500 GLU BBB CD    1 ? 2 
ATOM   7439  O OE1   . GLU B 1 500 ? 7.382   -4.541  9.473   1.000 55.565  0 500 GLU BBB OE1   1 ? 2 
ATOM   7440  O OE2   . GLU B 1 500 ? 8.557   -3.047  8.325   1.000 56.650  0 500 GLU BBB OE2   1 ? 2 
ATOM   7441  N N     . VAL B 1 501 ? 11.266  -7.302  6.093   1.000 41.931  0 501 VAL BBB N     1 ? 2 
ATOM   7442  C CA    . VAL B 1 501 ? 11.681  -7.254  4.663   1.000 42.663  0 501 VAL BBB CA    1 ? 2 
ATOM   7443  C C     . VAL B 1 501 ? 12.250  -8.626  4.286   1.000 43.488  0 501 VAL BBB C     1 ? 2 
ATOM   7444  O O     . VAL B 1 501 ? 13.047  -9.142  5.065   1.000 43.332  0 501 VAL BBB O     1 ? 2 
ATOM   7445  C CB    . VAL B 1 501 ? 12.684  -6.120  4.399   1.000 40.841  0 501 VAL BBB CB    1 ? 2 
ATOM   7446  C CG1   . VAL B 1 501 ? 13.158  -6.130  2.950   1.000 41.877  0 501 VAL BBB CG1   1 ? 2 
ATOM   7447  C CG2   . VAL B 1 501 ? 12.074  -4.776  4.764   1.000 40.387  0 501 VAL BBB CG2   1 ? 2 
ATOM   7448  N N     . THR B 1 502 ? 11.821  -9.198  3.167   1.000 43.872  0 502 THR BBB N     1 ? 2 
ATOM   7449  C CA    . THR B 1 502 ? 12.308  -10.510 2.681   1.000 45.557  0 502 THR BBB CA    1 ? 2 
ATOM   7450  C C     . THR B 1 502 ? 13.241  -10.253 1.494   1.000 47.034  0 502 THR BBB C     1 ? 2 
ATOM   7451  O O     . THR B 1 502 ? 13.063  -9.225  0.818   1.000 46.789  0 502 THR BBB O     1 ? 2 
ATOM   7452  C CB    . THR B 1 502 ? 11.136  -11.445 2.340   1.000 45.441  0 502 THR BBB CB    1 ? 2 
ATOM   7453  O OG1   . THR B 1 502 ? 10.564  -10.998 1.106   1.000 46.071  0 502 THR BBB OG1   1 ? 2 
ATOM   7454  C CG2   . THR B 1 502 ? 10.094  -11.500 3.440   1.000 44.897  0 502 THR BBB CG2   1 ? 2 
ATOM   7455  N N     . LYS B 1 503 ? 14.234  -11.118 1.292   1.000 50.128  0 503 LYS BBB N     1 ? 2 
ATOM   7456  C CA    . LYS B 1 503 ? 15.084  -11.079 0.081   1.000 54.245  0 503 LYS BBB CA    1 ? 2 
ATOM   7457  C C     . LYS B 1 503 ? 14.156  -11.169 -1.135  1.000 55.880  0 503 LYS BBB C     1 ? 2 
ATOM   7458  O O     . LYS B 1 503 ? 14.194  -10.258 -1.974  1.000 52.126  0 503 LYS BBB O     1 ? 2 
ATOM   7459  C CB    . LYS B 1 503 ? 16.104  -12.218 0.089   1.000 56.949  0 503 LYS BBB CB    1 ? 2 
ATOM   7460  C CG    . LYS B 1 503 ? 17.124  -12.138 -1.026  1.000 60.315  0 503 LYS BBB CG    1 ? 2 
ATOM   7461  C CD    . LYS B 1 503 ? 17.958  -13.399 -1.177  1.000 64.130  0 503 LYS BBB CD    1 ? 2 
ATOM   7462  C CE    . LYS B 1 503 ? 18.669  -13.466 -2.516  1.000 65.978  0 503 LYS BBB CE    1 ? 2 
ATOM   7463  N NZ    . LYS B 1 503 ? 19.717  -12.421 -2.627  1.000 65.534  0 503 LYS BBB NZ    1 ? 2 
ATOM   7464  N N     . ARG B 1 504 ? 13.299  -12.198 -1.167  1.000 58.228  0 504 ARG BBB N     1 ? 2 
ATOM   7465  C CA    . ARG B 1 504 ? 12.322  -12.463 -2.255  1.000 60.511  0 504 ARG BBB CA    1 ? 2 
ATOM   7466  C C     . ARG B 1 504 ? 11.593  -11.170 -2.633  1.000 61.297  0 504 ARG BBB C     1 ? 2 
ATOM   7467  O O     . ARG B 1 504 ? 11.489  -10.907 -3.846  1.000 60.744  0 504 ARG BBB O     1 ? 2 
ATOM   7468  C CB    . ARG B 1 504 ? 11.319  -13.551 -1.852  1.000 63.605  0 504 ARG BBB CB    1 ? 2 
ATOM   7469  C CG    . ARG B 1 504 ? 10.101  -13.664 -2.767  1.000 63.882  0 504 ARG BBB CG    1 ? 2 
ATOM   7470  C CD    . ARG B 1 504 ? 9.252   -14.909 -2.561  1.000 63.286  0 504 ARG BBB CD    1 ? 2 
ATOM   7471  N NE    . ARG B 1 504 ? 10.017  -16.141 -2.723  1.000 64.076  0 504 ARG BBB NE    1 ? 2 
ATOM   7472  C CZ    . ARG B 1 504 ? 10.187  -17.065 -1.786  1.000 62.972  0 504 ARG BBB CZ    1 ? 2 
ATOM   7473  N NH1   . ARG B 1 504 ? 9.626   -16.927 -0.598  1.000 65.583  0 504 ARG BBB NH1   1 ? 2 
ATOM   7474  N NH2   . ARG B 1 504 ? 10.917  -18.135 -2.031  1.000 63.101  0 504 ARG BBB NH2   1 ? 2 
ATOM   7475  N N     . SER B 1 505 ? 11.098  -10.396 -1.657  1.000 61.639  0 505 SER BBB N     1 ? 2 
ATOM   7476  C CA    . SER B 1 505 ? 10.338  -9.139  -1.909  1.000 61.320  0 505 SER BBB CA    1 ? 2 
ATOM   7477  C C     . SER B 1 505 ? 11.164  -8.167  -2.773  1.000 60.139  0 505 SER BBB C     1 ? 2 
ATOM   7478  O O     . SER B 1 505 ? 10.540  -7.299  -3.395  1.000 59.078  0 505 SER BBB O     1 ? 2 
ATOM   7479  C CB    . SER B 1 505 ? 9.902   -8.466  -0.627  1.000 62.687  0 505 SER BBB CB    1 ? 2 
ATOM   7480  O OG    . SER B 1 505 ? 10.944  -7.678  -0.068  1.000 61.130  0 505 SER BBB OG    1 ? 2 
ATOM   7481  N N     . GLY B 1 506 ? 12.504  -8.276  -2.770  1.000 56.606  0 506 GLY BBB N     1 ? 2 
ATOM   7482  C CA    . GLY B 1 506 ? 13.435  -7.382  -3.490  1.000 55.496  0 506 GLY BBB CA    1 ? 2 
ATOM   7483  C C     . GLY B 1 506 ? 13.445  -5.956  -2.960  1.000 54.119  0 506 GLY BBB C     1 ? 2 
ATOM   7484  O O     . GLY B 1 506 ? 14.293  -5.166  -3.435  1.000 53.154  0 506 GLY BBB O     1 ? 2 
ATOM   7485  N N     . GLU B 1 507 ? 12.594  -5.630  -1.983  1.000 53.735  0 507 GLU BBB N     1 ? 2 
ATOM   7486  C CA    . GLU B 1 507 ? 12.532  -4.298  -1.329  1.000 54.402  0 507 GLU BBB CA    1 ? 2 
ATOM   7487  C C     . GLU B 1 507 ? 13.797  -4.047  -0.483  1.000 48.778  0 507 GLU BBB C     1 ? 2 
ATOM   7488  O O     . GLU B 1 507 ? 14.559  -5.007  -0.203  1.000 47.978  0 507 GLU BBB O     1 ? 2 
ATOM   7489  C CB    . GLU B 1 507 ? 11.247  -4.195  -0.505  1.000 58.486  0 507 GLU BBB CB    1 ? 2 
ATOM   7490  C CG    . GLU B 1 507 ? 9.977   -4.071  -1.344  1.000 62.310  0 507 GLU BBB CG    1 ? 2 
ATOM   7491  C CD    . GLU B 1 507 ? 8.681   -4.083  -0.545  1.000 68.203  0 507 GLU BBB CD    1 ? 2 
ATOM   7492  O OE1   . GLU B 1 507 ? 8.374   -5.128  0.078   1.000 74.570  0 507 GLU BBB OE1   1 ? 2 
ATOM   7493  O OE2   . GLU B 1 507 ? 7.995   -3.039  -0.502  1.000 69.954  0 507 GLU BBB OE2   1 ? 2 
ATOM   7494  N N     . SER B 1 508 ? 14.068  -2.775  -0.190  1.000 46.123  0 508 SER BBB N     1 ? 2 
ATOM   7495  C CA    . SER B 1 508 ? 15.280  -2.291  0.533   1.000 47.399  0 508 SER BBB CA    1 ? 2 
ATOM   7496  C C     . SER B 1 508 ? 15.250  -2.796  1.990   1.000 44.342  0 508 SER BBB C     1 ? 2 
ATOM   7497  O O     . SER B 1 508 ? 14.214  -2.596  2.660   1.000 41.136  0 508 SER BBB O     1 ? 2 
ATOM   7498  C CB    . SER B 1 508 ? 15.395  -0.783  0.476   1.000 47.498  0 508 SER BBB CB    1 ? 2 
ATOM   7499  O OG    . SER B 1 508 ? 16.473  -0.326  1.284   1.000 47.427  0 508 SER BBB OG    1 ? 2 
ATOM   7500  N N     . PHE B 1 509 ? 16.321  -3.461  2.440   1.000 43.469  0 509 PHE BBB N     1 ? 2 
ATOM   7501  C CA    . PHE B 1 509 ? 16.457  -3.972  3.837   1.000 43.515  0 509 PHE BBB CA    1 ? 2 
ATOM   7502  C C     . PHE B 1 509 ? 17.322  -3.002  4.660   1.000 43.682  0 509 PHE BBB C     1 ? 2 
ATOM   7503  O O     . PHE B 1 509 ? 17.533  -3.224  5.859   1.000 42.270  0 509 PHE BBB O     1 ? 2 
ATOM   7504  C CB    . PHE B 1 509 ? 16.942  -5.418  3.854   1.000 41.878  0 509 PHE BBB CB    1 ? 2 
ATOM   7505  C CG    . PHE B 1 509 ? 18.216  -5.678  3.078   1.000 43.997  0 509 PHE BBB CG    1 ? 2 
ATOM   7506  C CD1   . PHE B 1 509 ? 19.457  -5.394  3.631   1.000 42.334  0 509 PHE BBB CD1   1 ? 2 
ATOM   7507  C CD2   . PHE B 1 509 ? 18.173  -6.221  1.799   1.000 43.296  0 509 PHE BBB CD2   1 ? 2 
ATOM   7508  C CE1   . PHE B 1 509 ? 20.621  -5.587  2.905   1.000 41.971  0 509 PHE BBB CE1   1 ? 2 
ATOM   7509  C CE2   . PHE B 1 509 ? 19.337  -6.467  1.099   1.000 43.337  0 509 PHE BBB CE2   1 ? 2 
ATOM   7510  C CZ    . PHE B 1 509 ? 20.559  -6.152  1.652   1.000 42.876  0 509 PHE BBB CZ    1 ? 2 
ATOM   7511  N N     . VAL B 1 510 ? 17.765  -1.907  4.045   1.000 47.893  0 510 VAL BBB N     1 ? 2 
ATOM   7512  C CA    . VAL B 1 510 ? 18.512  -0.826  4.742   1.000 53.211  0 510 VAL BBB CA    1 ? 2 
ATOM   7513  C C     . VAL B 1 510 ? 17.514  -0.018  5.573   1.000 58.923  0 510 VAL BBB C     1 ? 2 
ATOM   7514  O O     . VAL B 1 510 ? 16.374  0.197   5.102   1.000 61.357  0 510 VAL BBB O     1 ? 2 
ATOM   7515  C CB    . VAL B 1 510 ? 19.282  0.045   3.736   1.000 53.820  0 510 VAL BBB CB    1 ? 2 
ATOM   7516  C CG1   . VAL B 1 510 ? 19.848  1.298   4.396   1.000 56.796  0 510 VAL BBB CG1   1 ? 2 
ATOM   7517  C CG2   . VAL B 1 510 ? 20.380  -0.750  3.051   1.000 53.366  0 510 VAL BBB CG2   1 ? 2 
ATOM   7518  N N     . SER B 1 511 ? 17.904  0.354   6.795   1.000 63.941  0 511 SER BBB N     1 ? 2 
ATOM   7519  C CA    . SER B 1 511 ? 17.213  1.391   7.608   1.000 68.636  0 511 SER BBB CA    1 ? 2 
ATOM   7520  C C     . SER B 1 511 ? 18.228  2.501   7.887   1.000 70.640  0 511 SER BBB C     1 ? 2 
ATOM   7521  O O     . SER B 1 511 ? 19.322  2.183   8.408   1.000 69.247  0 511 SER BBB O     1 ? 2 
ATOM   7522  C CB    . SER B 1 511 ? 16.610  0.804   8.851   1.000 69.270  0 511 SER BBB CB    1 ? 2 
ATOM   7523  O OG    . SER B 1 511 ? 15.724  -0.257  8.502   1.000 69.504  0 511 SER BBB OG    1 ? 2 
ATOM   7524  N N     . SER B 1 512 ? 17.894  3.731   7.479   1.000 76.424  0 512 SER BBB N     1 ? 2 
ATOM   7525  C CA    . SER B 1 512 ? 18.795  4.919   7.510   1.000 84.367  0 512 SER BBB CA    1 ? 2 
ATOM   7526  C C     . SER B 1 512 ? 18.609  5.712   8.815   1.000 85.821  0 512 SER BBB C     1 ? 2 
ATOM   7527  O O     . SER B 1 512 ? 19.615  6.259   9.302   1.000 83.378  0 512 SER BBB O     1 ? 2 
ATOM   7528  C CB    . SER B 1 512 ? 18.599  5.803   6.286   1.000 85.417  0 512 SER BBB CB    1 ? 2 
ATOM   7529  O OG    . SER B 1 512 ? 19.033  5.149   5.093   1.000 81.063  0 512 SER BBB OG    1 ? 2 
ATOM   7530  N N     . GLY B 1 513 ? 17.382  5.783   9.351   1.000 90.458  0 513 GLY BBB N     1 ? 2 
ATOM   7531  C CA    . GLY B 1 513 ? 17.090  6.348   10.689  1.000 94.401  0 513 GLY BBB CA    1 ? 2 
ATOM   7532  C C     . GLY B 1 513 ? 17.853  5.612   11.784  1.000 94.345  0 513 GLY BBB C     1 ? 2 
ATOM   7533  O O     . GLY B 1 513 ? 18.011  4.388   11.647  1.000 100.029 0 513 GLY BBB O     1 ? 2 
ATOM   7534  N N     . GLY B 1 514 ? 18.312  6.317   12.826  1.000 87.649  0 514 GLY BBB N     1 ? 2 
ATOM   7535  C CA    . GLY B 1 514 ? 19.273  5.792   13.819  1.000 81.345  0 514 GLY BBB CA    1 ? 2 
ATOM   7536  C C     . GLY B 1 514 ? 18.643  5.546   15.180  1.000 76.983  0 514 GLY BBB C     1 ? 2 
ATOM   7537  O O     . GLY B 1 514 ? 19.150  6.122   16.165  1.000 67.333  0 514 GLY BBB O     1 ? 2 
ATOM   7538  N N     . CYS B 1 515 ? 17.600  4.704   15.245  1.000 79.130  0 515 CYS BBB N     1 ? 2 
ATOM   7539  C CA    . CYS B 1 515 ? 16.969  4.204   16.506  1.000 78.107  0 515 CYS BBB CA    1 ? 2 
ATOM   7540  C C     . CYS B 1 515 ? 17.732  2.954   17.001  1.000 72.119  0 515 CYS BBB C     1 ? 2 
ATOM   7541  O O     . CYS B 1 515 ? 17.302  2.332   18.007  1.000 68.323  0 515 CYS BBB O     1 ? 2 
ATOM   7542  C CB    . CYS B 1 515 ? 15.479  3.880   16.320  1.000 83.140  0 515 CYS BBB CB    1 ? 2 
ATOM   7543  S SG    . CYS B 1 515 ? 14.638  4.723   14.941  1.000 84.468  0 515 CYS BBB SG    1 ? 2 
ATOM   7544  N N     . GLY B 1 516 ? 18.841  2.601   16.336  1.000 67.204  0 516 GLY BBB N     1 ? 2 
ATOM   7545  C CA    . GLY B 1 516 ? 19.585  1.349   16.573  1.000 64.628  0 516 GLY BBB CA    1 ? 2 
ATOM   7546  C C     . GLY B 1 516 ? 18.869  0.142   16.010  1.000 61.112  0 516 GLY BBB C     1 ? 2 
ATOM   7547  O O     . GLY B 1 516 ? 18.372  0.230   14.888  1.000 66.243  0 516 GLY BBB O     1 ? 2 
ATOM   7548  N N     . GLY B 1 517 ? 18.777  -0.942  16.786  1.000 60.884  0 517 GLY BBB N     1 ? 2 
ATOM   7549  C CA    . GLY B 1 517 ? 18.094  -2.199  16.413  1.000 61.214  0 517 GLY BBB CA    1 ? 2 
ATOM   7550  C C     . GLY B 1 517 ? 16.586  -2.024  16.192  1.000 62.972  0 517 GLY BBB C     1 ? 2 
ATOM   7551  O O     . GLY B 1 517 ? 15.933  -2.993  15.800  1.000 59.398  0 517 GLY BBB O     1 ? 2 
ATOM   7552  N N     . GLY B 1 518 ? 16.091  -0.778  16.371  1.000 63.856  0 518 GLY BBB N     1 ? 2 
ATOM   7553  C CA    . GLY B 1 518 ? 14.886  -0.210  15.719  1.000 62.623  0 518 GLY BBB CA    1 ? 2 
ATOM   7554  C C     . GLY B 1 518 ? 13.867  0.246   16.749  1.000 58.969  0 518 GLY BBB C     1 ? 2 
ATOM   7555  O O     . GLY B 1 518 ? 14.058  -0.167  17.874  1.000 51.690  0 518 GLY BBB O     1 ? 2 
ATOM   7556  N N     . LEU C 1 24  ? 15.922  -6.551  87.598  1.000 91.841  0 24  LEU CCC N     1 ? 3 
ATOM   7557  C CA    . LEU C 1 24  ? 15.762  -5.362  86.679  1.000 90.711  0 24  LEU CCC CA    1 ? 3 
ATOM   7558  C C     . LEU C 1 24  ? 16.157  -5.857  85.281  1.000 91.219  0 24  LEU CCC C     1 ? 3 
ATOM   7559  O O     . LEU C 1 24  ? 16.953  -6.829  85.212  1.000 86.584  0 24  LEU CCC O     1 ? 3 
ATOM   7560  C CB    . LEU C 1 24  ? 16.639  -4.197  87.168  1.000 88.571  0 24  LEU CCC CB    1 ? 3 
ATOM   7561  C CG    . LEU C 1 24  ? 16.007  -2.800  87.249  1.000 87.576  0 24  LEU CCC CG    1 ? 3 
ATOM   7562  C CD1   . LEU C 1 24  ? 14.710  -2.780  88.052  1.000 86.434  0 24  LEU CCC CD1   1 ? 3 
ATOM   7563  C CD2   . LEU C 1 24  ? 16.995  -1.804  87.850  1.000 84.976  0 24  LEU CCC CD2   1 ? 3 
ATOM   7564  N N     . THR C 1 25  ? 15.629  -5.249  84.215  1.000 93.522  0 25  THR CCC N     1 ? 3 
ATOM   7565  C CA    . THR C 1 25  ? 15.625  -5.861  82.854  1.000 91.616  0 25  THR CCC CA    1 ? 3 
ATOM   7566  C C     . THR C 1 25  ? 17.034  -6.320  82.461  1.000 87.853  0 25  THR CCC C     1 ? 3 
ATOM   7567  O O     . THR C 1 25  ? 17.069  -7.138  81.522  1.000 90.306  0 25  THR CCC O     1 ? 3 
ATOM   7568  C CB    . THR C 1 25  ? 15.054  -4.946  81.766  1.000 91.227  0 25  THR CCC CB    1 ? 3 
ATOM   7569  O OG1   . THR C 1 25  ? 13.910  -4.279  82.304  1.000 94.396  0 25  THR CCC OG1   1 ? 3 
ATOM   7570  C CG2   . THR C 1 25  ? 14.625  -5.680  80.508  1.000 89.068  0 25  THR CCC CG2   1 ? 3 
ATOM   7571  N N     . PHE C 1 26  ? 18.129  -5.801  83.064  1.000 80.607  0 26  PHE CCC N     1 ? 3 
ATOM   7572  C CA    . PHE C 1 26  ? 19.521  -6.058  82.575  1.000 72.082  0 26  PHE CCC CA    1 ? 3 
ATOM   7573  C C     . PHE C 1 26  ? 20.463  -6.474  83.714  1.000 66.157  0 26  PHE CCC C     1 ? 3 
ATOM   7574  O O     . PHE C 1 26  ? 20.680  -5.708  84.668  1.000 63.039  0 26  PHE CCC O     1 ? 3 
ATOM   7575  C CB    . PHE C 1 26  ? 20.113  -4.867  81.816  1.000 68.488  0 26  PHE CCC CB    1 ? 3 
ATOM   7576  C CG    . PHE C 1 26  ? 19.215  -4.292  80.756  1.000 67.240  0 26  PHE CCC CG    1 ? 3 
ATOM   7577  C CD1   . PHE C 1 26  ? 18.823  -5.042  79.657  1.000 65.576  0 26  PHE CCC CD1   1 ? 3 
ATOM   7578  C CD2   . PHE C 1 26  ? 18.742  -2.994  80.873  1.000 68.996  0 26  PHE CCC CD2   1 ? 3 
ATOM   7579  C CE1   . PHE C 1 26  ? 17.951  -4.509  78.716  1.000 66.172  0 26  PHE CCC CE1   1 ? 3 
ATOM   7580  C CE2   . PHE C 1 26  ? 17.895  -2.453  79.910  1.000 67.772  0 26  PHE CCC CE2   1 ? 3 
ATOM   7581  C CZ    . PHE C 1 26  ? 17.509  -3.210  78.824  1.000 66.192  0 26  PHE CCC CZ    1 ? 3 
ATOM   7582  N N     . MET C 1 27  ? 21.064  -7.658  83.558  1.000 62.132  0 27  MET CCC N     1 ? 3 
ATOM   7583  C CA    . MET C 1 27  ? 22.102  -8.190  84.475  1.000 59.935  0 27  MET CCC CA    1 ? 3 
ATOM   7584  C C     . MET C 1 27  ? 23.265  -7.196  84.542  1.000 57.088  0 27  MET CCC C     1 ? 3 
ATOM   7585  O O     . MET C 1 27  ? 23.734  -6.921  85.661  1.000 58.347  0 27  MET CCC O     1 ? 3 
ATOM   7586  C CB    . MET C 1 27  ? 22.615  -9.554  84.007  1.000 61.329  0 27  MET CCC CB    1 ? 3 
ATOM   7587  C CG    . MET C 1 27  ? 21.592  -10.679 84.120  1.000 63.897  0 27  MET CCC CG    1 ? 3 
ATOM   7588  S SD    . MET C 1 27  ? 22.046  -12.217 83.224  1.000 61.219  0 27  MET CCC SD    1 ? 3 
ATOM   7589  C CE    . MET C 1 27  ? 23.387  -12.817 84.257  1.000 60.956  0 27  MET CCC CE    1 ? 3 
ATOM   7590  N N     . TYR C 1 28  ? 23.698  -6.641  83.402  1.000 53.395  0 28  TYR CCC N     1 ? 3 
ATOM   7591  C CA    . TYR C 1 28  ? 24.891  -5.750  83.312  1.000 50.132  0 28  TYR CCC CA    1 ? 3 
ATOM   7592  C C     . TYR C 1 28  ? 24.505  -4.371  82.757  1.000 47.666  0 28  TYR CCC C     1 ? 3 
ATOM   7593  O O     . TYR C 1 28  ? 23.509  -4.258  82.038  1.000 48.541  0 28  TYR CCC O     1 ? 3 
ATOM   7594  C CB    . TYR C 1 28  ? 25.996  -6.390  82.464  1.000 47.181  0 28  TYR CCC CB    1 ? 3 
ATOM   7595  C CG    . TYR C 1 28  ? 26.581  -7.647  83.054  1.000 46.566  0 28  TYR CCC CG    1 ? 3 
ATOM   7596  C CD1   . TYR C 1 28  ? 25.984  -8.880  82.847  1.000 46.373  0 28  TYR CCC CD1   1 ? 3 
ATOM   7597  C CD2   . TYR C 1 28  ? 27.729  -7.606  83.824  1.000 47.782  0 28  TYR CCC CD2   1 ? 3 
ATOM   7598  C CE1   . TYR C 1 28  ? 26.504  -10.037 83.398  1.000 46.477  0 28  TYR CCC CE1   1 ? 3 
ATOM   7599  C CE2   . TYR C 1 28  ? 28.274  -8.749  84.382  1.000 47.817  0 28  TYR CCC CE2   1 ? 3 
ATOM   7600  C CZ    . TYR C 1 28  ? 27.643  -9.965  84.184  1.000 48.453  0 28  TYR CCC CZ    1 ? 3 
ATOM   7601  O OH    . TYR C 1 28  ? 28.194  -11.085 84.742  1.000 47.114  0 28  TYR CCC OH    1 ? 3 
ATOM   7602  N N     . ASP C 1 29  ? 25.307  -3.358  83.084  1.000 46.586  0 29  ASP CCC N     1 ? 3 
ATOM   7603  C CA    . ASP C 1 29  ? 25.250  -1.995  82.498  1.000 45.752  0 29  ASP CCC CA    1 ? 3 
ATOM   7604  C C     . ASP C 1 29  ? 25.968  -2.019  81.139  1.000 42.634  0 29  ASP CCC C     1 ? 3 
ATOM   7605  O O     . ASP C 1 29  ? 25.467  -1.381  80.179  1.000 40.063  0 29  ASP CCC O     1 ? 3 
ATOM   7606  C CB    . ASP C 1 29  ? 25.841  -0.955  83.469  1.000 46.744  0 29  ASP CCC CB    1 ? 3 
ATOM   7607  C CG    . ASP C 1 29  ? 25.018  -0.788  84.739  1.000 48.211  0 29  ASP CCC CG    1 ? 3 
ATOM   7608  O OD1   . ASP C 1 29  ? 23.893  -0.239  84.642  1.000 45.599  0 29  ASP CCC OD1   1 ? 3 
ATOM   7609  O OD2   . ASP C 1 29  ? 25.498  -1.236  85.809  1.000 49.222  0 29  ASP CCC OD2   1 ? 3 
ATOM   7610  N N     . LEU C 1 30  ? 27.077  -2.758  81.069  1.000 42.058  0 30  LEU CCC N     1 ? 3 
ATOM   7611  C CA    . LEU C 1 30  ? 28.002  -2.804  79.907  1.000 40.522  0 30  LEU CCC CA    1 ? 3 
ATOM   7612  C C     . LEU C 1 30  ? 28.659  -4.182  79.782  1.000 37.374  0 30  LEU CCC C     1 ? 3 
ATOM   7613  O O     . LEU C 1 30  ? 29.244  -4.666  80.773  1.000 34.675  0 30  LEU CCC O     1 ? 3 
ATOM   7614  C CB    . LEU C 1 30  ? 29.076  -1.728  80.068  1.000 42.779  0 30  LEU CCC CB    1 ? 3 
ATOM   7615  C CG    . LEU C 1 30  ? 30.171  -1.745  79.002  1.000 40.336  0 30  LEU CCC CG    1 ? 3 
ATOM   7616  C CD1   . LEU C 1 30  ? 29.611  -1.326  77.657  1.000 41.794  0 30  LEU CCC CD1   1 ? 3 
ATOM   7617  C CD2   . LEU C 1 30  ? 31.300  -0.844  79.426  1.000 40.215  0 30  LEU CCC CD2   1 ? 3 
ATOM   7618  N N     . VAL C 1 31  ? 28.553  -4.752  78.582  1.000 35.734  0 31  VAL CCC N     1 ? 3 
ATOM   7619  C CA    . VAL C 1 31  ? 29.255  -5.994  78.181  1.000 35.253  0 31  VAL CCC CA    1 ? 3 
ATOM   7620  C C     . VAL C 1 31  ? 30.129  -5.621  77.002  1.000 34.140  0 31  VAL CCC C     1 ? 3 
ATOM   7621  O O     . VAL C 1 31  ? 29.623  -5.031  76.031  1.000 32.412  0 31  VAL CCC O     1 ? 3 
ATOM   7622  C CB    . VAL C 1 31  ? 28.310  -7.159  77.858  1.000 36.867  0 31  VAL CCC CB    1 ? 3 
ATOM   7623  C CG1   . VAL C 1 31  ? 29.053  -8.310  77.238  1.000 36.901  0 31  VAL CCC CG1   1 ? 3 
ATOM   7624  C CG2   . VAL C 1 31  ? 27.579  -7.647  79.091  1.000 39.587  0 31  VAL CCC CG2   1 ? 3 
ATOM   7625  N N     . VAL C 1 32  ? 31.416  -5.920  77.137  1.000 35.664  0 32  VAL CCC N     1 ? 3 
ATOM   7626  C CA    . VAL C 1 32  ? 32.465  -5.609  76.147  1.000 34.818  0 32  VAL CCC CA    1 ? 3 
ATOM   7627  C C     . VAL C 1 32  ? 32.883  -6.942  75.540  1.000 36.550  0 32  VAL CCC C     1 ? 3 
ATOM   7628  O O     . VAL C 1 32  ? 33.282  -7.837  76.317  1.000 38.055  0 32  VAL CCC O     1 ? 3 
ATOM   7629  C CB    . VAL C 1 32  ? 33.651  -4.880  76.799  1.000 35.927  0 32  VAL CCC CB    1 ? 3 
ATOM   7630  C CG1   . VAL C 1 32  ? 34.761  -4.590  75.782  1.000 35.913  0 32  VAL CCC CG1   1 ? 3 
ATOM   7631  C CG2   . VAL C 1 32  ? 33.208  -3.585  77.441  1.000 35.534  0 32  VAL CCC CG2   1 ? 3 
ATOM   7632  N N     . ILE C 1 33  ? 32.769  -7.075  74.218  1.000 35.592  0 33  ILE CCC N     1 ? 3 
ATOM   7633  C CA    . ILE C 1 33  ? 33.330  -8.253  73.508  1.000 36.857  0 33  ILE CCC CA    1 ? 3 
ATOM   7634  C C     . ILE C 1 33  ? 34.687  -7.867  72.885  1.000 35.427  0 33  ILE CCC C     1 ? 3 
ATOM   7635  O O     . ILE C 1 33  ? 34.721  -7.229  71.822  1.000 33.559  0 33  ILE CCC O     1 ? 3 
ATOM   7636  C CB    . ILE C 1 33  ? 32.320  -8.810  72.493  1.000 36.677  0 33  ILE CCC CB    1 ? 3 
ATOM   7637  C CG1   . ILE C 1 33  ? 30.969  -9.085  73.164  1.000 37.971  0 33  ILE CCC CG1   1 ? 3 
ATOM   7638  C CG2   . ILE C 1 33  ? 32.898  -10.051 71.848  1.000 36.766  0 33  ILE CCC CG2   1 ? 3 
ATOM   7639  C CD1   . ILE C 1 33  ? 29.827  -9.422  72.223  1.000 38.420  0 33  ILE CCC CD1   1 ? 3 
ATOM   7640  N N     . GLY C 1 34  ? 35.769  -8.290  73.523  1.000 34.944  0 34  GLY CCC N     1 ? 3 
ATOM   7641  C CA    . GLY C 1 34  ? 37.147  -8.055  73.052  1.000 34.271  0 34  GLY CCC CA    1 ? 3 
ATOM   7642  C C     . GLY C 1 34  ? 37.953  -7.393  74.142  1.000 34.788  0 34  GLY CCC C     1 ? 3 
ATOM   7643  O O     . GLY C 1 34  ? 37.535  -6.289  74.609  1.000 35.691  0 34  GLY CCC O     1 ? 3 
ATOM   7644  N N     . GLY C 1 35  ? 39.044  -8.039  74.553  1.000 34.888  0 35  GLY CCC N     1 ? 3 
ATOM   7645  C CA    . GLY C 1 35  ? 39.928  -7.562  75.622  1.000 33.898  0 35  GLY CCC CA    1 ? 3 
ATOM   7646  C C     . GLY C 1 35  ? 41.241  -7.065  75.063  1.000 35.647  0 35  GLY CCC C     1 ? 3 
ATOM   7647  O O     . GLY C 1 35  ? 42.268  -7.423  75.631  1.000 33.642  0 35  GLY CCC O     1 ? 3 
ATOM   7648  N N     . GLY C 1 36  ? 41.197  -6.265  73.992  1.000 36.896  0 36  GLY CCC N     1 ? 3 
ATOM   7649  C CA    . GLY C 1 36  ? 42.353  -5.480  73.528  1.000 35.530  0 36  GLY CCC CA    1 ? 3 
ATOM   7650  C C     . GLY C 1 36  ? 42.276  -4.019  73.938  1.000 36.820  0 36  GLY CCC C     1 ? 3 
ATOM   7651  O O     . GLY C 1 36  ? 41.623  -3.698  74.951  1.000 36.910  0 36  GLY CCC O     1 ? 3 
ATOM   7652  N N     . SER C 1 37  ? 42.885  -3.140  73.147  1.000 38.468  0 37  SER CCC N     1 ? 3 
ATOM   7653  C CA    . SER C 1 37  ? 43.150  -1.736  73.551  1.000 38.584  0 37  SER CCC CA    1 ? 3 
ATOM   7654  C C     . SER C 1 37  ? 41.812  -1.031  73.802  1.000 38.086  0 37  SER CCC C     1 ? 3 
ATOM   7655  O O     . SER C 1 37  ? 41.677  -0.369  74.843  1.000 39.164  0 37  SER CCC O     1 ? 3 
ATOM   7656  C CB    . SER C 1 37  ? 43.960  -1.020  72.520  1.000 39.465  0 37  SER CCC CB    1 ? 3 
ATOM   7657  O OG    . SER C 1 37  ? 45.145  -1.736  72.244  1.000 40.075  0 37  SER CCC OG    1 ? 3 
ATOM   7658  N N     . GLY C 1 38  ? 40.857  -1.190  72.881  1.000 37.482  0 38  GLY CCC N     1 ? 3 
ATOM   7659  C CA    . GLY C 1 38  ? 39.546  -0.513  72.918  1.000 35.857  0 38  GLY CCC CA    1 ? 3 
ATOM   7660  C C     . GLY C 1 38  ? 38.708  -1.059  74.056  1.000 35.847  0 38  GLY CCC C     1 ? 3 
ATOM   7661  O O     . GLY C 1 38  ? 38.232  -0.251  74.853  1.000 37.292  0 38  GLY CCC O     1 ? 3 
ATOM   7662  N N     . GLY C 1 39  ? 38.556  -2.383  74.126  1.000 36.953  0 39  GLY CCC N     1 ? 3 
ATOM   7663  C CA    . GLY C 1 39  ? 37.658  -3.079  75.076  1.000 38.503  0 39  GLY CCC CA    1 ? 3 
ATOM   7664  C C     . GLY C 1 39  ? 38.064  -2.883  76.535  1.000 38.159  0 39  GLY CCC C     1 ? 3 
ATOM   7665  O O     . GLY C 1 39  ? 37.214  -2.498  77.336  1.000 35.633  0 39  GLY CCC O     1 ? 3 
ATOM   7666  N N     . MET C 1 40  ? 39.328  -3.139  76.872  1.000 38.729  0 40  MET CCC N     1 ? 3 
ATOM   7667  C CA    . MET C 1 40  ? 39.798  -3.042  78.275  1.000 39.920  0 40  MET CCC CA    1 ? 3 
ATOM   7668  C C     . MET C 1 40  ? 39.725  -1.579  78.714  1.000 39.763  0 40  MET CCC C     1 ? 3 
ATOM   7669  O O     . MET C 1 40  ? 39.362  -1.352  79.887  1.000 39.952  0 40  MET CCC O     1 ? 3 
ATOM   7670  C CB    . MET C 1 40  ? 41.215  -3.578  78.428  1.000 40.929  0 40  MET CCC CB    1 ? 3 
ATOM   7671  C CG    . MET C 1 40  ? 41.248  -5.088  78.379  1.000 42.988  0 40  MET CCC CG    1 ? 3 
ATOM   7672  S SD    . MET C 1 40  ? 42.803  -5.738  78.944  1.000 48.410  0 40  MET CCC SD    1 ? 3 
ATOM   7673  C CE    . MET C 1 40  ? 43.953  -4.805  77.927  1.000 47.242  0 40  MET CCC CE    1 ? 3 
ATOM   7674  N N     . ALA C 1 41  ? 39.975  -0.625  77.809  1.000 36.098  0 41  ALA CCC N     1 ? 3 
ATOM   7675  C CA    . ALA C 1 41  ? 39.902  0.813   78.134  1.000 34.864  0 41  ALA CCC CA    1 ? 3 
ATOM   7676  C C     . ALA C 1 41  ? 38.435  1.188   78.442  1.000 34.425  0 41  ALA CCC C     1 ? 3 
ATOM   7677  O O     . ALA C 1 41  ? 38.197  1.790   79.485  1.000 33.343  0 41  ALA CCC O     1 ? 3 
ATOM   7678  C CB    . ALA C 1 41  ? 40.467  1.630   76.996  1.000 34.717  0 41  ALA CCC CB    1 ? 3 
ATOM   7679  N N     . ALA C 1 42  ? 37.489  0.851   77.558  1.000 34.485  0 42  ALA CCC N     1 ? 3 
ATOM   7680  C CA    . ALA C 1 42  ? 36.053  1.138   77.763  1.000 37.595  0 42  ALA CCC CA    1 ? 3 
ATOM   7681  C C     . ALA C 1 42  ? 35.595  0.525   79.105  1.000 40.078  0 42  ALA CCC C     1 ? 3 
ATOM   7682  O O     . ALA C 1 42  ? 35.018  1.271   79.906  1.000 39.737  0 42  ALA CCC O     1 ? 3 
ATOM   7683  C CB    . ALA C 1 42  ? 35.238  0.617   76.616  1.000 37.929  0 42  ALA CCC CB    1 ? 3 
ATOM   7684  N N     . ALA C 1 43  ? 35.915  -0.756  79.336  1.000 41.946  0 43  ALA CCC N     1 ? 3 
ATOM   7685  C CA    . ALA C 1 43  ? 35.458  -1.613  80.454  1.000 44.537  0 43  ALA CCC CA    1 ? 3 
ATOM   7686  C C     . ALA C 1 43  ? 35.904  -1.040  81.821  1.000 47.949  0 43  ALA CCC C     1 ? 3 
ATOM   7687  O O     . ALA C 1 43  ? 35.034  -0.871  82.709  1.000 45.340  0 43  ALA CCC O     1 ? 3 
ATOM   7688  C CB    . ALA C 1 43  ? 35.974  -3.019  80.237  1.000 44.121  0 43  ALA CCC CB    1 ? 3 
ATOM   7689  N N     . LYS C 1 44  ? 37.206  -0.765  81.991  1.000 49.157  0 44  LYS CCC N     1 ? 3 
ATOM   7690  C CA    . LYS C 1 44  ? 37.792  -0.179  83.235  1.000 47.803  0 44  LYS CCC CA    1 ? 3 
ATOM   7691  C C     . LYS C 1 44  ? 37.222  1.221   83.471  1.000 46.908  0 44  LYS CCC C     1 ? 3 
ATOM   7692  O O     . LYS C 1 44  ? 37.011  1.556   84.637  1.000 49.550  0 44  LYS CCC O     1 ? 3 
ATOM   7693  C CB    . LYS C 1 44  ? 39.318  -0.088  83.182  1.000 47.986  0 44  LYS CCC CB    1 ? 3 
ATOM   7694  C CG    . LYS C 1 44  ? 40.046  -1.403  83.445  1.000 49.756  0 44  LYS CCC CG    1 ? 3 
ATOM   7695  C CD    . LYS C 1 44  ? 41.555  -1.321  83.561  1.000 50.643  0 44  LYS CCC CD    1 ? 3 
ATOM   7696  C CE    . LYS C 1 44  ? 42.254  -1.491  82.222  1.000 51.655  0 44  LYS CCC CE    1 ? 3 
ATOM   7697  N NZ    . LYS C 1 44  ? 43.723  -1.362  82.343  1.000 52.680  0 44  LYS CCC NZ    1 ? 3 
ATOM   7698  N N     . GLU C 1 45  ? 37.011  2.021   82.428  1.000 45.639  0 45  GLU CCC N     1 ? 3 
ATOM   7699  C CA    . GLU C 1 45  ? 36.459  3.398   82.582  1.000 46.619  0 45  GLU CCC CA    1 ? 3 
ATOM   7700  C C     . GLU C 1 45  ? 34.976  3.325   82.989  1.000 44.767  0 45  GLU CCC C     1 ? 3 
ATOM   7701  O O     . GLU C 1 45  ? 34.570  4.120   83.839  1.000 44.735  0 45  GLU CCC O     1 ? 3 
ATOM   7702  C CB    . GLU C 1 45  ? 36.618  4.233   81.310  1.000 45.994  0 45  GLU CCC CB    1 ? 3 
ATOM   7703  C CG    . GLU C 1 45  ? 36.326  5.704   81.551  1.000 47.646  0 45  GLU CCC CG    1 ? 3 
ATOM   7704  C CD    . GLU C 1 45  ? 37.461  6.453   82.230  1.000 51.046  0 45  GLU CCC CD    1 ? 3 
ATOM   7705  O OE1   . GLU C 1 45  ? 38.426  5.787   82.702  1.000 50.829  0 45  GLU CCC OE1   1 ? 3 
ATOM   7706  O OE2   . GLU C 1 45  ? 37.392  7.704   82.271  1.000 53.204  0 45  GLU CCC OE2   1 ? 3 
ATOM   7707  N N     . ALA C 1 46  ? 34.204  2.405   82.417  1.000 41.919  0 46  ALA CCC N     1 ? 3 
ATOM   7708  C CA    . ALA C 1 46  ? 32.796  2.175   82.793  1.000 44.852  0 46  ALA CCC CA    1 ? 3 
ATOM   7709  C C     . ALA C 1 46  ? 32.738  1.792   84.274  1.000 46.482  0 46  ALA CCC C     1 ? 3 
ATOM   7710  O O     . ALA C 1 46  ? 32.002  2.445   85.015  1.000 46.725  0 46  ALA CCC O     1 ? 3 
ATOM   7711  C CB    . ALA C 1 46  ? 32.178  1.122   81.927  1.000 43.288  0 46  ALA CCC CB    1 ? 3 
ATOM   7712  N N     . ALA C 1 47  ? 33.528  0.795   84.668  1.000 48.414  0 47  ALA CCC N     1 ? 3 
ATOM   7713  C CA    . ALA C 1 47  ? 33.592  0.224   86.030  1.000 49.830  0 47  ALA CCC CA    1 ? 3 
ATOM   7714  C C     . ALA C 1 47  ? 33.992  1.304   87.047  1.000 53.706  0 47  ALA CCC C     1 ? 3 
ATOM   7715  O O     . ALA C 1 47  ? 33.546  1.200   88.201  1.000 53.339  0 47  ALA CCC O     1 ? 3 
ATOM   7716  C CB    . ALA C 1 47  ? 34.576  -0.927  86.047  1.000 50.729  0 47  ALA CCC CB    1 ? 3 
ATOM   7717  N N     . LYS C 1 48  ? 34.793  2.299   86.641  1.000 55.882  0 48  LYS CCC N     1 ? 3 
ATOM   7718  C CA    . LYS C 1 48  ? 35.182  3.496   87.447  1.000 58.533  0 48  LYS CCC CA    1 ? 3 
ATOM   7719  C C     . LYS C 1 48  ? 33.942  4.202   88.016  1.000 58.702  0 48  LYS CCC C     1 ? 3 
ATOM   7720  O O     . LYS C 1 48  ? 34.066  4.796   89.104  1.000 58.918  0 48  LYS CCC O     1 ? 3 
ATOM   7721  C CB    . LYS C 1 48  ? 35.961  4.532   86.616  1.000 60.262  0 48  LYS CCC CB    1 ? 3 
ATOM   7722  C CG    . LYS C 1 48  ? 37.454  4.647   86.886  1.000 62.659  0 48  LYS CCC CG    1 ? 3 
ATOM   7723  C CD    . LYS C 1 48  ? 38.073  6.009   86.518  1.000 65.298  0 48  LYS CCC CD    1 ? 3 
ATOM   7724  C CE    . LYS C 1 48  ? 37.513  7.178   87.322  1.000 69.546  0 48  LYS CCC CE    1 ? 3 
ATOM   7725  N NZ    . LYS C 1 48  ? 38.557  8.107   87.839  1.000 70.830  0 48  LYS CCC NZ    1 ? 3 
ATOM   7726  N N     . TYR C 1 49  ? 32.813  4.189   87.294  1.000 57.781  0 49  TYR CCC N     1 ? 3 
ATOM   7727  C CA    . TYR C 1 49  ? 31.591  4.962   87.634  1.000 62.611  0 49  TYR CCC CA    1 ? 3 
ATOM   7728  C C     . TYR C 1 49  ? 30.581  4.063   88.370  1.000 65.591  0 49  TYR CCC C     1 ? 3 
ATOM   7729  O O     . TYR C 1 49  ? 29.375  4.424   88.415  1.000 66.305  0 49  TYR CCC O     1 ? 3 
ATOM   7730  C CB    . TYR C 1 49  ? 31.039  5.637   86.377  1.000 62.834  0 49  TYR CCC CB    1 ? 3 
ATOM   7731  C CG    . TYR C 1 49  ? 31.993  6.645   85.791  1.000 63.856  0 49  TYR CCC CG    1 ? 3 
ATOM   7732  C CD1   . TYR C 1 49  ? 32.387  7.753   86.524  1.000 62.819  0 49  TYR CCC CD1   1 ? 3 
ATOM   7733  C CD2   . TYR C 1 49  ? 32.554  6.466   84.528  1.000 64.256  0 49  TYR CCC CD2   1 ? 3 
ATOM   7734  C CE1   . TYR C 1 49  ? 33.286  8.675   86.012  1.000 64.188  0 49  TYR CCC CE1   1 ? 3 
ATOM   7735  C CE2   . TYR C 1 49  ? 33.461  7.373   84.005  1.000 60.779  0 49  TYR CCC CE2   1 ? 3 
ATOM   7736  C CZ    . TYR C 1 49  ? 33.825  8.484   84.748  1.000 64.101  0 49  TYR CCC CZ    1 ? 3 
ATOM   7737  O OH    . TYR C 1 49  ? 34.695  9.399   84.232  1.000 63.706  0 49  TYR CCC OH    1 ? 3 
ATOM   7738  N N     . GLY C 1 50  ? 31.062  2.961   88.969  1.000 65.518  0 50  GLY CCC N     1 ? 3 
ATOM   7739  C CA    . GLY C 1 50  ? 30.273  2.017   89.792  1.000 63.686  0 50  GLY CCC CA    1 ? 3 
ATOM   7740  C C     . GLY C 1 50  ? 29.374  1.128   88.947  1.000 60.753  0 50  GLY CCC C     1 ? 3 
ATOM   7741  O O     . GLY C 1 50  ? 28.424  0.540   89.495  1.000 60.752  0 50  GLY CCC O     1 ? 3 
ATOM   7742  N N     . LYS C 1 51  ? 29.656  1.015   87.653  1.000 55.791  0 51  LYS CCC N     1 ? 3 
ATOM   7743  C CA    . LYS C 1 51  ? 28.822  0.209   86.737  1.000 54.936  0 51  LYS CCC CA    1 ? 3 
ATOM   7744  C C     . LYS C 1 51  ? 29.272  -1.250  86.823  1.000 52.791  0 51  LYS CCC C     1 ? 3 
ATOM   7745  O O     . LYS C 1 51  ? 30.457  -1.507  87.124  1.000 53.496  0 51  LYS CCC O     1 ? 3 
ATOM   7746  C CB    . LYS C 1 51  ? 28.906  0.792   85.324  1.000 56.014  0 51  LYS CCC CB    1 ? 3 
ATOM   7747  C CG    . LYS C 1 51  ? 28.382  2.215   85.206  1.000 56.854  0 51  LYS CCC CG    1 ? 3 
ATOM   7748  C CD    . LYS C 1 51  ? 27.143  2.514   86.028  1.000 57.029  0 51  LYS CCC CD    1 ? 3 
ATOM   7749  C CE    . LYS C 1 51  ? 26.469  3.780   85.558  1.000 59.092  0 51  LYS CCC CE    1 ? 3 
ATOM   7750  N NZ    . LYS C 1 51  ? 25.933  4.620   86.645  1.000 60.077  0 51  LYS CCC NZ    1 ? 3 
ATOM   7751  N N     . LYS C 1 52  ? 28.339  -2.160  86.597  1.000 54.796  0 52  LYS CCC N     1 ? 3 
ATOM   7752  C CA    . LYS C 1 52  ? 28.613  -3.609  86.480  1.000 55.889  0 52  LYS CCC CA    1 ? 3 
ATOM   7753  C C     . LYS C 1 52  ? 29.029  -3.884  85.036  1.000 52.368  0 52  LYS CCC C     1 ? 3 
ATOM   7754  O O     . LYS C 1 52  ? 28.253  -3.554  84.106  1.000 49.310  0 52  LYS CCC O     1 ? 3 
ATOM   7755  C CB    . LYS C 1 52  ? 27.396  -4.442  86.885  1.000 63.102  0 52  LYS CCC CB    1 ? 3 
ATOM   7756  C CG    . LYS C 1 52  ? 27.763  -5.790  87.489  1.000 69.215  0 52  LYS CCC CG    1 ? 3 
ATOM   7757  C CD    . LYS C 1 52  ? 26.625  -6.794  87.489  1.000 72.227  0 52  LYS CCC CD    1 ? 3 
ATOM   7758  C CE    . LYS C 1 52  ? 27.125  -8.209  87.677  1.000 72.799  0 52  LYS CCC CE    1 ? 3 
ATOM   7759  N NZ    . LYS C 1 52  ? 26.051  -9.201  87.434  1.000 73.555  0 52  LYS CCC NZ    1 ? 3 
ATOM   7760  N N     . VAL C 1 53  ? 30.221  -4.462  84.868  1.000 48.040  0 53  VAL CCC N     1 ? 3 
ATOM   7761  C CA    . VAL C 1 53  ? 30.921  -4.597  83.566  1.000 45.186  0 53  VAL CCC CA    1 ? 3 
ATOM   7762  C C     . VAL C 1 53  ? 31.403  -6.040  83.447  1.000 43.814  0 53  VAL CCC C     1 ? 3 
ATOM   7763  O O     . VAL C 1 53  ? 31.979  -6.554  84.407  1.000 42.298  0 53  VAL CCC O     1 ? 3 
ATOM   7764  C CB    . VAL C 1 53  ? 32.097  -3.603  83.461  1.000 46.792  0 53  VAL CCC CB    1 ? 3 
ATOM   7765  C CG1   . VAL C 1 53  ? 32.708  -3.592  82.056  1.000 47.672  0 53  VAL CCC CG1   1 ? 3 
ATOM   7766  C CG2   . VAL C 1 53  ? 31.717  -2.193  83.906  1.000 46.105  0 53  VAL CCC CG2   1 ? 3 
ATOM   7767  N N     . ALA C 1 54  ? 31.132  -6.669  82.304  1.000 44.438  0 54  ALA CCC N     1 ? 3 
ATOM   7768  C CA    . ALA C 1 54  ? 31.708  -7.970  81.878  1.000 43.469  0 54  ALA CCC CA    1 ? 3 
ATOM   7769  C C     . ALA C 1 54  ? 32.497  -7.755  80.593  1.000 39.857  0 54  ALA CCC C     1 ? 3 
ATOM   7770  O O     . ALA C 1 54  ? 32.038  -6.981  79.743  1.000 38.584  0 54  ALA CCC O     1 ? 3 
ATOM   7771  C CB    . ALA C 1 54  ? 30.650  -9.024  81.674  1.000 44.644  0 54  ALA CCC CB    1 ? 3 
ATOM   7772  N N     . LEU C 1 55  ? 33.645  -8.408  80.490  1.000 37.662  0 55  LEU CCC N     1 ? 3 
ATOM   7773  C CA    . LEU C 1 55  ? 34.538  -8.327  79.309  1.000 38.600  0 55  LEU CCC CA    1 ? 3 
ATOM   7774  C C     . LEU C 1 55  ? 34.835  -9.753  78.866  1.000 37.749  0 55  LEU CCC C     1 ? 3 
ATOM   7775  O O     . LEU C 1 55  ? 35.186  -10.569 79.720  1.000 38.779  0 55  LEU CCC O     1 ? 3 
ATOM   7776  C CB    . LEU C 1 55  ? 35.813  -7.534  79.622  1.000 38.919  0 55  LEU CCC CB    1 ? 3 
ATOM   7777  C CG    . LEU C 1 55  ? 36.734  -7.305  78.420  1.000 39.868  0 55  LEU CCC CG    1 ? 3 
ATOM   7778  C CD1   . LEU C 1 55  ? 37.482  -5.974  78.512  1.000 41.377  0 55  LEU CCC CD1   1 ? 3 
ATOM   7779  C CD2   . LEU C 1 55  ? 37.736  -8.446  78.280  1.000 39.409  0 55  LEU CCC CD2   1 ? 3 
ATOM   7780  N N     . PHE C 1 56  ? 34.645  -10.012 77.578  1.000 36.508  0 56  PHE CCC N     1 ? 3 
ATOM   7781  C CA    . PHE C 1 56  ? 35.011  -11.266 76.894  1.000 38.055  0 56  PHE CCC CA    1 ? 3 
ATOM   7782  C C     . PHE C 1 56  ? 36.304  -11.027 76.113  1.000 39.007  0 56  PHE CCC C     1 ? 3 
ATOM   7783  O O     . PHE C 1 56  ? 36.413  -10.005 75.412  1.000 42.180  0 56  PHE CCC O     1 ? 3 
ATOM   7784  C CB    . PHE C 1 56  ? 33.873  -11.745 76.000  1.000 37.923  0 56  PHE CCC CB    1 ? 3 
ATOM   7785  C CG    . PHE C 1 56  ? 32.648  -12.173 76.767  1.000 39.949  0 56  PHE CCC CG    1 ? 3 
ATOM   7786  C CD1   . PHE C 1 56  ? 32.534  -13.464 77.270  1.000 41.737  0 56  PHE CCC CD1   1 ? 3 
ATOM   7787  C CD2   . PHE C 1 56  ? 31.608  -11.286 76.990  1.000 40.176  0 56  PHE CCC CD2   1 ? 3 
ATOM   7788  C CE1   . PHE C 1 56  ? 31.409  -13.867 77.973  1.000 43.474  0 56  PHE CCC CE1   1 ? 3 
ATOM   7789  C CE2   . PHE C 1 56  ? 30.478  -11.690 77.682  1.000 41.897  0 56  PHE CCC CE2   1 ? 3 
ATOM   7790  C CZ    . PHE C 1 56  ? 30.376  -12.977 78.173  1.000 43.241  0 56  PHE CCC CZ    1 ? 3 
ATOM   7791  N N     . ASP C 1 57  ? 37.262  -11.926 76.287  1.000 39.291  0 57  ASP CCC N     1 ? 3 
ATOM   7792  C CA    . ASP C 1 57  ? 38.433  -12.068 75.401  1.000 40.463  0 57  ASP CCC CA    1 ? 3 
ATOM   7793  C C     . ASP C 1 57  ? 38.747  -13.551 75.278  1.000 40.454  0 57  ASP CCC C     1 ? 3 
ATOM   7794  O O     . ASP C 1 57  ? 38.859  -14.206 76.307  1.000 41.375  0 57  ASP CCC O     1 ? 3 
ATOM   7795  C CB    . ASP C 1 57  ? 39.680  -11.341 75.924  1.000 41.551  0 57  ASP CCC CB    1 ? 3 
ATOM   7796  C CG    . ASP C 1 57  ? 40.748  -11.231 74.857  1.000 39.315  0 57  ASP CCC CG    1 ? 3 
ATOM   7797  O OD1   . ASP C 1 57  ? 40.482  -10.522 73.876  1.000 38.561  0 57  ASP CCC OD1   1 ? 3 
ATOM   7798  O OD2   . ASP C 1 57  ? 41.764  -11.938 74.976  1.000 39.275  0 57  ASP CCC OD2   1 ? 3 
ATOM   7799  N N     . PHE C 1 58  ? 38.850  -14.045 74.050  1.000 40.681  0 58  PHE CCC N     1 ? 3 
ATOM   7800  C CA    . PHE C 1 58  ? 39.418  -15.380 73.731  1.000 42.954  0 58  PHE CCC CA    1 ? 3 
ATOM   7801  C C     . PHE C 1 58  ? 40.239  -15.235 72.458  1.000 39.377  0 58  PHE CCC C     1 ? 3 
ATOM   7802  O O     . PHE C 1 58  ? 39.804  -14.568 71.532  1.000 40.316  0 58  PHE CCC O     1 ? 3 
ATOM   7803  C CB    . PHE C 1 58  ? 38.314  -16.445 73.593  1.000 46.263  0 58  PHE CCC CB    1 ? 3 
ATOM   7804  C CG    . PHE C 1 58  ? 38.812  -17.847 73.320  1.000 46.410  0 58  PHE CCC CG    1 ? 3 
ATOM   7805  C CD1   . PHE C 1 58  ? 38.994  -18.291 72.022  1.000 47.949  0 58  PHE CCC CD1   1 ? 3 
ATOM   7806  C CD2   . PHE C 1 58  ? 39.102  -18.719 74.358  1.000 47.326  0 58  PHE CCC CD2   1 ? 3 
ATOM   7807  C CE1   . PHE C 1 58  ? 39.448  -19.582 71.774  1.000 50.739  0 58  PHE CCC CE1   1 ? 3 
ATOM   7808  C CE2   . PHE C 1 58  ? 39.593  -19.990 74.119  1.000 50.015  0 58  PHE CCC CE2   1 ? 3 
ATOM   7809  C CZ    . PHE C 1 58  ? 39.753  -20.426 72.822  1.000 51.433  0 58  PHE CCC CZ    1 ? 3 
ATOM   7810  N N     . VAL C 1 59  ? 41.382  -15.890 72.407  1.000 40.077  0 59  VAL CCC N     1 ? 3 
ATOM   7811  C CA    . VAL C 1 59  ? 42.306  -15.790 71.250  1.000 37.912  0 59  VAL CCC CA    1 ? 3 
ATOM   7812  C C     . VAL C 1 59  ? 42.104  -17.018 70.370  1.000 38.617  0 59  VAL CCC C     1 ? 3 
ATOM   7813  O O     . VAL C 1 59  ? 42.539  -18.106 70.775  1.000 36.583  0 59  VAL CCC O     1 ? 3 
ATOM   7814  C CB    . VAL C 1 59  ? 43.764  -15.615 71.704  1.000 37.722  0 59  VAL CCC CB    1 ? 3 
ATOM   7815  C CG1   . VAL C 1 59  ? 44.717  -15.496 70.534  1.000 37.442  0 59  VAL CCC CG1   1 ? 3 
ATOM   7816  C CG2   . VAL C 1 59  ? 43.913  -14.397 72.589  1.000 38.223  0 59  VAL CCC CG2   1 ? 3 
ATOM   7817  N N     . LYS C 1 60  ? 41.457  -16.821 69.206  1.000 40.000  0 60  LYS CCC N     1 ? 3 
ATOM   7818  C CA    . LYS C 1 60  ? 41.436  -17.827 68.115  1.000 40.745  0 60  LYS CCC CA    1 ? 3 
ATOM   7819  C C     . LYS C 1 60  ? 42.875  -18.002 67.618  1.000 41.513  0 60  LYS CCC C     1 ? 3 
ATOM   7820  O O     . LYS C 1 60  ? 43.553  -17.014 67.327  1.000 44.007  0 60  LYS CCC O     1 ? 3 
ATOM   7821  C CB    . LYS C 1 60  ? 40.420  -17.396 67.051  1.000 39.560  0 60  LYS CCC CB    1 ? 3 
ATOM   7822  C CG    . LYS C 1 60  ? 38.975  -17.534 67.499  1.000 40.082  0 60  LYS CCC CG    1 ? 3 
ATOM   7823  C CD    . LYS C 1 60  ? 37.941  -17.308 66.429  1.000 39.775  0 60  LYS CCC CD    1 ? 3 
ATOM   7824  C CE    . LYS C 1 60  ? 37.899  -15.876 65.943  1.000 39.682  0 60  LYS CCC CE    1 ? 3 
ATOM   7825  N NZ    . LYS C 1 60  ? 37.535  -14.933 67.035  1.000 39.874  0 60  LYS CCC NZ    1 ? 3 
ATOM   7826  N N     . PRO C 1 61  ? 43.416  -19.239 67.525  1.000 41.015  0 61  PRO CCC N     1 ? 3 
ATOM   7827  C CA    . PRO C 1 61  ? 44.796  -19.421 67.041  1.000 40.869  0 61  PRO CCC CA    1 ? 3 
ATOM   7828  C C     . PRO C 1 61  ? 44.988  -18.892 65.602  1.000 40.998  0 61  PRO CCC C     1 ? 3 
ATOM   7829  O O     . PRO C 1 61  ? 44.023  -18.931 64.781  1.000 43.757  0 61  PRO CCC O     1 ? 3 
ATOM   7830  C CB    . PRO C 1 61  ? 45.056  -20.939 67.108  1.000 39.983  0 61  PRO CCC CB    1 ? 3 
ATOM   7831  C CG    . PRO C 1 61  ? 43.883  -21.516 67.942  1.000 41.521  0 61  PRO CCC CG    1 ? 3 
ATOM   7832  C CD    . PRO C 1 61  ? 42.758  -20.506 67.883  1.000 40.444  0 61  PRO CCC CD    1 ? 3 
ATOM   7833  N N     . SER C 1 62  ? 46.194  -18.407 65.303  1.000 38.080  0 62  SER CCC N     1 ? 3 
ATOM   7834  C CA    . SER C 1 62  ? 46.574  -17.917 63.950  1.000 38.335  0 62  SER CCC CA    1 ? 3 
ATOM   7835  C C     . SER C 1 62  ? 46.444  -19.050 62.928  1.000 38.494  0 62  SER CCC C     1 ? 3 
ATOM   7836  O O     . SER C 1 62  ? 46.250  -20.219 63.333  1.000 38.076  0 62  SER CCC O     1 ? 3 
ATOM   7837  C CB    . SER C 1 62  ? 47.979  -17.362 63.965  1.000 36.945  0 62  SER CCC CB    1 ? 3 
ATOM   7838  O OG    . SER C 1 62  ? 48.932  -18.410 64.088  1.000 35.015  0 62  SER CCC OG    1 ? 3 
ATOM   7839  N N     . THR C 1 63  ? 46.605  -18.734 61.649  1.000 41.273  0 63  THR CCC N     1 ? 3 
ATOM   7840  C CA    . THR C 1 63  ? 46.658  -19.749 60.563  1.000 43.873  0 63  THR CCC CA    1 ? 3 
ATOM   7841  C C     . THR C 1 63  ? 47.768  -20.779 60.840  1.000 44.801  0 63  THR CCC C     1 ? 3 
ATOM   7842  O O     . THR C 1 63  ? 47.694  -21.869 60.263  1.000 44.084  0 63  THR CCC O     1 ? 3 
ATOM   7843  C CB    . THR C 1 63  ? 46.807  -19.099 59.183  1.000 45.126  0 63  THR CCC CB    1 ? 3 
ATOM   7844  O OG1   . THR C 1 63  ? 48.007  -18.324 59.178  1.000 45.136  0 63  THR CCC OG1   1 ? 3 
ATOM   7845  C CG2   . THR C 1 63  ? 45.588  -18.279 58.825  1.000 45.069  0 63  THR CCC CG2   1 ? 3 
ATOM   7846  N N     . GLN C 1 64  ? 48.740  -20.484 61.709  1.000 45.519  0 64  GLN CCC N     1 ? 3 
ATOM   7847  C CA    . GLN C 1 64  ? 49.864  -21.421 62.004  1.000 46.761  0 64  GLN CCC CA    1 ? 3 
ATOM   7848  C C     . GLN C 1 64  ? 49.802  -21.944 63.452  1.000 45.832  0 64  GLN CCC C     1 ? 3 
ATOM   7849  O O     . GLN C 1 64  ? 50.785  -22.512 63.890  1.000 44.842  0 64  GLN CCC O     1 ? 3 
ATOM   7850  C CB    . GLN C 1 64  ? 51.199  -20.758 61.645  1.000 47.557  0 64  GLN CCC CB    1 ? 3 
ATOM   7851  C CG    . GLN C 1 64  ? 51.380  -20.520 60.141  1.000 47.947  0 64  GLN CCC CG    1 ? 3 
ATOM   7852  C CD    . GLN C 1 64  ? 51.497  -21.801 59.358  1.000 48.860  0 64  GLN CCC CD    1 ? 3 
ATOM   7853  O OE1   . GLN C 1 64  ? 51.951  -22.815 59.874  1.000 54.446  0 64  GLN CCC OE1   1 ? 3 
ATOM   7854  N NE2   . GLN C 1 64  ? 51.111  -21.769 58.095  1.000 51.352  0 64  GLN CCC NE2   1 ? 3 
ATOM   7855  N N     . GLY C 1 65  ? 48.653  -21.847 64.133  1.000 45.861  0 65  GLY CCC N     1 ? 3 
ATOM   7856  C CA    . GLY C 1 65  ? 48.441  -22.415 65.475  1.000 45.891  0 65  GLY CCC CA    1 ? 3 
ATOM   7857  C C     . GLY C 1 65  ? 49.016  -21.552 66.599  1.000 46.809  0 65  GLY CCC C     1 ? 3 
ATOM   7858  O O     . GLY C 1 65  ? 49.019  -22.033 67.745  1.000 48.700  0 65  GLY CCC O     1 ? 3 
ATOM   7859  N N     . THR C 1 66  ? 49.468  -20.317 66.345  1.000 46.400  0 66  THR CCC N     1 ? 3 
ATOM   7860  C CA    . THR C 1 66  ? 50.000  -19.433 67.416  1.000 44.841  0 66  THR CCC CA    1 ? 3 
ATOM   7861  C C     . THR C 1 66  ? 48.828  -18.831 68.202  1.000 44.693  0 66  THR CCC C     1 ? 3 
ATOM   7862  O O     . THR C 1 66  ? 47.895  -18.342 67.557  1.000 45.966  0 66  THR CCC O     1 ? 3 
ATOM   7863  C CB    . THR C 1 66  ? 50.905  -18.316 66.880  1.000 43.253  0 66  THR CCC CB    1 ? 3 
ATOM   7864  O OG1   . THR C 1 66  ? 51.806  -18.874 65.930  1.000 40.828  0 66  THR CCC OG1   1 ? 3 
ATOM   7865  C CG2   . THR C 1 66  ? 51.663  -17.609 67.980  1.000 43.015  0 66  THR CCC CG2   1 ? 3 
ATOM   7866  N N     . LYS C 1 67  ? 48.902  -18.842 69.539  1.000 44.746  0 67  LYS CCC N     1 ? 3 
ATOM   7867  C CA    . LYS C 1 67  ? 47.920  -18.180 70.438  1.000 44.565  0 67  LYS CCC CA    1 ? 3 
ATOM   7868  C C     . LYS C 1 67  ? 48.648  -17.533 71.621  1.000 42.886  0 67  LYS CCC C     1 ? 3 
ATOM   7869  O O     . LYS C 1 67  ? 49.874  -17.758 71.770  1.000 42.775  0 67  LYS CCC O     1 ? 3 
ATOM   7870  C CB    . LYS C 1 67  ? 46.854  -19.170 70.902  1.000 48.157  0 67  LYS CCC CB    1 ? 3 
ATOM   7871  C CG    . LYS C 1 67  ? 47.307  -20.225 71.902  1.000 49.916  0 67  LYS CCC CG    1 ? 3 
ATOM   7872  C CD    . LYS C 1 67  ? 46.309  -21.380 72.005  1.000 52.414  0 67  LYS CCC CD    1 ? 3 
ATOM   7873  C CE    . LYS C 1 67  ? 46.028  -21.836 73.431  1.000 54.751  0 67  LYS CCC CE    1 ? 3 
ATOM   7874  N NZ    . LYS C 1 67  ? 45.676  -23.272 73.468  1.000 56.048  0 67  LYS CCC NZ    1 ? 3 
ATOM   7875  N N     . TRP C 1 68  ? 47.927  -16.736 72.416  1.000 38.889  0 68  TRP CCC N     1 ? 3 
ATOM   7876  C CA    . TRP C 1 68  ? 48.508  -15.790 73.405  1.000 38.140  0 68  TRP CCC CA    1 ? 3 
ATOM   7877  C C     . TRP C 1 68  ? 47.431  -15.377 74.418  1.000 40.757  0 68  TRP CCC C     1 ? 3 
ATOM   7878  O O     . TRP C 1 68  ? 46.222  -15.747 74.239  1.000 42.350  0 68  TRP CCC O     1 ? 3 
ATOM   7879  C CB    . TRP C 1 68  ? 49.123  -14.582 72.677  1.000 35.586  0 68  TRP CCC CB    1 ? 3 
ATOM   7880  C CG    . TRP C 1 68  ? 48.218  -13.917 71.670  1.000 34.992  0 68  TRP CCC CG    1 ? 3 
ATOM   7881  C CD1   . TRP C 1 68  ? 47.245  -12.979 71.918  1.000 32.151  0 68  TRP CCC CD1   1 ? 3 
ATOM   7882  C CD2   . TRP C 1 68  ? 48.196  -14.131 70.237  1.000 31.746  0 68  TRP CCC CD2   1 ? 3 
ATOM   7883  N NE1   . TRP C 1 68  ? 46.653  -12.590 70.742  1.000 31.169  0 68  TRP CCC NE1   1 ? 3 
ATOM   7884  C CE2   . TRP C 1 68  ? 47.192  -13.295 69.708  1.000 30.217  0 68  TRP CCC CE2   1 ? 3 
ATOM   7885  C CE3   . TRP C 1 68  ? 48.919  -14.951 69.365  1.000 32.208  0 68  TRP CCC CE3   1 ? 3 
ATOM   7886  C CZ2   . TRP C 1 68  ? 46.899  -13.248 68.346  1.000 31.068  0 68  TRP CCC CZ2   1 ? 3 
ATOM   7887  C CZ3   . TRP C 1 68  ? 48.629  -14.921 68.014  1.000 31.169  0 68  TRP CCC CZ3   1 ? 3 
ATOM   7888  C CH2   . TRP C 1 68  ? 47.637  -14.075 67.518  1.000 30.993  0 68  TRP CCC CH2   1 ? 3 
ATOM   7889  N N     . GLY C 1 69  ? 47.840  -14.631 75.442  1.000 39.470  0 69  GLY CCC N     1 ? 3 
ATOM   7890  C CA    . GLY C 1 69  ? 46.982  -14.251 76.579  1.000 38.327  0 69  GLY CCC CA    1 ? 3 
ATOM   7891  C C     . GLY C 1 69  ? 46.244  -12.961 76.331  1.000 35.840  0 69  GLY CCC C     1 ? 3 
ATOM   7892  O O     . GLY C 1 69  ? 46.144  -12.536 75.175  1.000 36.296  0 69  GLY CCC O     1 ? 3 
ATOM   7893  N N     . LEU C 1 70  ? 45.719  -12.398 77.407  1.000 35.251  0 70  LEU CCC N     1 ? 3 
ATOM   7894  C CA    . LEU C 1 70  ? 44.867  -11.190 77.428  1.000 36.942  0 70  LEU CCC CA    1 ? 3 
ATOM   7895  C C     . LEU C 1 70  ? 45.682  -9.966  76.996  1.000 37.453  0 70  LEU CCC C     1 ? 3 
ATOM   7896  O O     . LEU C 1 70  ? 46.892  -9.899  77.280  1.000 34.165  0 70  LEU CCC O     1 ? 3 
ATOM   7897  C CB    . LEU C 1 70  ? 44.354  -11.018 78.853  1.000 38.659  0 70  LEU CCC CB    1 ? 3 
ATOM   7898  C CG    . LEU C 1 70  ? 43.573  -9.740  79.123  1.000 42.477  0 70  LEU CCC CG    1 ? 3 
ATOM   7899  C CD1   . LEU C 1 70  ? 42.241  -9.726  78.377  1.000 42.609  0 70  LEU CCC CD1   1 ? 3 
ATOM   7900  C CD2   . LEU C 1 70  ? 43.321  -9.614  80.608  1.000 43.870  0 70  LEU CCC CD2   1 ? 3 
ATOM   7901  N N     . GLY C 1 71  ? 45.004  -8.995  76.378  1.000 38.303  0 71  GLY CCC N     1 ? 3 
ATOM   7902  C CA    . GLY C 1 71  ? 45.571  -7.679  76.051  1.000 38.562  0 71  GLY CCC CA    1 ? 3 
ATOM   7903  C C     . GLY C 1 71  ? 45.411  -7.343  74.584  1.000 38.313  0 71  GLY CCC C     1 ? 3 
ATOM   7904  O O     . GLY C 1 71  ? 45.539  -6.162  74.247  1.000 40.008  0 71  GLY CCC O     1 ? 3 
ATOM   7905  N N     . GLY C 1 72  ? 45.143  -8.349  73.753  1.000 36.867  0 72  GLY CCC N     1 ? 3 
ATOM   7906  C CA    . GLY C 1 72  ? 44.737  -8.153  72.354  1.000 37.171  0 72  GLY CCC CA    1 ? 3 
ATOM   7907  C C     . GLY C 1 72  ? 45.935  -7.978  71.446  1.000 36.239  0 72  GLY CCC C     1 ? 3 
ATOM   7908  O O     . GLY C 1 72  ? 47.056  -8.353  71.863  1.000 36.890  0 72  GLY CCC O     1 ? 3 
ATOM   7909  N N     . THR C 1 73  ? 45.720  -7.397  70.272  1.000 33.666  0 73  THR CCC N     1 ? 3 
ATOM   7910  C CA    . THR C 1 73  ? 46.731  -7.315  69.211  1.000 33.410  0 73  THR CCC CA    1 ? 3 
ATOM   7911  C C     . THR C 1 73  ? 47.951  -6.481  69.667  1.000 33.054  0 73  THR CCC C     1 ? 3 
ATOM   7912  O O     . THR C 1 73  ? 49.096  -6.927  69.448  1.000 29.818  0 73  THR CCC O     1 ? 3 
ATOM   7913  C CB    . THR C 1 73  ? 46.064  -6.810  67.917  1.000 34.503  0 73  THR CCC CB    1 ? 3 
ATOM   7914  O OG1   . THR C 1 73  ? 45.142  -7.837  67.534  1.000 33.514  0 73  THR CCC OG1   1 ? 3 
ATOM   7915  C CG2   . THR C 1 73  ? 47.048  -6.491  66.801  1.000 33.919  0 73  THR CCC CG2   1 ? 3 
ATOM   7916  N N     . CYS C 1 74  ? 47.752  -5.315  70.260  1.000 33.404  0 74  CYS CCC N     1 ? 3 
ATOM   7917  C CA    A CYS C 1 74  ? 48.883  -4.394  70.522  0.500 34.852  0 74  CYS CCC CA    1 ? 3 
ATOM   7918  C CA    B CYS C 1 74  ? 48.879  -4.395  70.523  0.500 34.733  0 74  CYS CCC CA    1 ? 3 
ATOM   7919  C C     . CYS C 1 74  ? 49.852  -5.035  71.530  1.000 36.187  0 74  CYS CCC C     1 ? 3 
ATOM   7920  O O     . CYS C 1 74  ? 51.099  -4.958  71.288  1.000 32.277  0 74  CYS CCC O     1 ? 3 
ATOM   7921  C CB    A CYS C 1 74  ? 48.408  -3.022  70.976  0.500 36.382  0 74  CYS CCC CB    1 ? 3 
ATOM   7922  C CB    B CYS C 1 74  ? 48.370  -3.037  70.979  0.500 36.112  0 74  CYS CCC CB    1 ? 3 
ATOM   7923  S SG    A CYS C 1 74  ? 49.780  -1.856  71.194  0.500 40.255  0 74  CYS CCC SG    1 ? 3 
ATOM   7924  S SG    B CYS C 1 74  ? 49.693  -1.820  71.206  0.500 39.634  0 74  CYS CCC SG    1 ? 3 
ATOM   7925  N N     . VAL C 1 75  ? 49.322  -5.668  72.598  1.000 36.988  0 75  VAL CCC N     1 ? 3 
ATOM   7926  C CA    . VAL C 1 75  ? 50.159  -6.262  73.678  1.000 36.484  0 75  VAL CCC CA    1 ? 3 
ATOM   7927  C C     . VAL C 1 75  ? 50.930  -7.472  73.142  1.000 34.330  0 75  VAL CCC C     1 ? 3 
ATOM   7928  O O     . VAL C 1 75  ? 52.124  -7.647  73.503  1.000 37.423  0 75  VAL CCC O     1 ? 3 
ATOM   7929  C CB    . VAL C 1 75  ? 49.282  -6.671  74.881  1.000 40.236  0 75  VAL CCC CB    1 ? 3 
ATOM   7930  C CG1   . VAL C 1 75  ? 50.034  -7.599  75.834  1.000 39.455  0 75  VAL CCC CG1   1 ? 3 
ATOM   7931  C CG2   . VAL C 1 75  ? 48.750  -5.459  75.637  1.000 41.705  0 75  VAL CCC CG2   1 ? 3 
ATOM   7932  N N     . ASN C 1 76  ? 50.254  -8.329  72.382  1.000 31.328  0 76  ASN CCC N     1 ? 3 
ATOM   7933  C CA    . ASN C 1 76  ? 50.723  -9.709  72.105  1.000 30.571  0 76  ASN CCC CA    1 ? 3 
ATOM   7934  C C     . ASN C 1 76  ? 51.414  -9.813  70.733  1.000 28.567  0 76  ASN CCC C     1 ? 3 
ATOM   7935  O O     . ASN C 1 76  ? 52.396  -10.552 70.645  1.000 28.551  0 76  ASN CCC O     1 ? 3 
ATOM   7936  C CB    . ASN C 1 76  ? 49.573  -10.702 72.244  1.000 30.820  0 76  ASN CCC CB    1 ? 3 
ATOM   7937  C CG    . ASN C 1 76  ? 49.081  -10.790 73.672  1.000 33.053  0 76  ASN CCC CG    1 ? 3 
ATOM   7938  O OD1   . ASN C 1 76  ? 49.662  -11.487 74.488  1.000 32.245  0 76  ASN CCC OD1   1 ? 3 
ATOM   7939  N ND2   . ASN C 1 76  ? 48.017  -10.061 73.989  1.000 34.376  0 76  ASN CCC ND2   1 ? 3 
ATOM   7940  N N     . VAL C 1 77  ? 50.904  -9.157  69.695  1.000 26.708  0 77  VAL CCC N     1 ? 3 
ATOM   7941  C CA    . VAL C 1 77  ? 51.287  -9.462  68.285  1.000 26.198  0 77  VAL CCC CA    1 ? 3 
ATOM   7942  C C     . VAL C 1 77  ? 51.267  -8.164  67.489  1.000 25.519  0 77  VAL CCC C     1 ? 3 
ATOM   7943  O O     . VAL C 1 77  ? 51.204  -8.263  66.325  1.000 25.976  0 77  VAL CCC O     1 ? 3 
ATOM   7944  C CB    . VAL C 1 77  ? 50.417  -10.554 67.629  1.000 25.883  0 77  VAL CCC CB    1 ? 3 
ATOM   7945  C CG1   . VAL C 1 77  ? 50.695  -11.940 68.158  1.000 27.152  0 77  VAL CCC CG1   1 ? 3 
ATOM   7946  C CG2   . VAL C 1 77  ? 48.938  -10.283 67.760  1.000 25.747  0 77  VAL CCC CG2   1 ? 3 
ATOM   7947  N N     . GLY C 1 78  ? 51.480  -7.020  68.127  1.000 26.861  0 78  GLY CCC N     1 ? 3 
ATOM   7948  C CA    . GLY C 1 78  ? 51.453  -5.711  67.459  1.000 27.932  0 78  GLY CCC CA    1 ? 3 
ATOM   7949  C C     . GLY C 1 78  ? 52.531  -4.782  68.010  1.000 29.725  0 78  GLY CCC C     1 ? 3 
ATOM   7950  O O     . GLY C 1 78  ? 53.751  -5.147  67.978  1.000 29.201  0 78  GLY CCC O     1 ? 3 
ATOM   7951  N N     . CYS C 1 79  ? 52.090  -3.630  68.522  1.000 30.412  0 79  CYS CCC N     1 ? 3 
ATOM   7952  C CA    . CYS C 1 79  ? 52.952  -2.490  68.860  1.000 30.884  0 79  CYS CCC CA    1 ? 3 
ATOM   7953  C C     . CYS C 1 79  ? 54.078  -2.979  69.758  1.000 30.059  0 79  CYS CCC C     1 ? 3 
ATOM   7954  O O     . CYS C 1 79  ? 55.243  -2.611  69.515  1.000 30.168  0 79  CYS CCC O     1 ? 3 
ATOM   7955  C CB    . CYS C 1 79  ? 52.179  -1.369  69.552  1.000 34.629  0 79  CYS CCC CB    1 ? 3 
ATOM   7956  S SG    . CYS C 1 79  ? 50.376  -1.387  69.290  1.000 33.788  0 79  CYS CCC SG    1 ? 3 
ATOM   7957  N N     . VAL C 1 80  ? 53.751  -3.766  70.778  1.000 29.075  0 80  VAL CCC N     1 ? 3 
ATOM   7958  C CA    . VAL C 1 80  ? 54.729  -4.071  71.862  1.000 28.274  0 80  VAL CCC CA    1 ? 3 
ATOM   7959  C C     . VAL C 1 80  ? 55.859  -4.936  71.315  1.000 28.228  0 80  VAL CCC C     1 ? 3 
ATOM   7960  O O     . VAL C 1 80  ? 57.016  -4.520  71.356  1.000 26.498  0 80  VAL CCC O     1 ? 3 
ATOM   7961  C CB    . VAL C 1 80  ? 54.071  -4.686  73.099  1.000 27.822  0 80  VAL CCC CB    1 ? 3 
ATOM   7962  C CG1   . VAL C 1 80  ? 55.116  -5.260  74.036  1.000 28.139  0 80  VAL CCC CG1   1 ? 3 
ATOM   7963  C CG2   . VAL C 1 80  ? 53.200  -3.650  73.794  1.000 28.212  0 80  VAL CCC CG2   1 ? 3 
ATOM   7964  N N     . PRO C 1 81  ? 55.592  -6.167  70.818  1.000 28.629  0 81  PRO CCC N     1 ? 3 
ATOM   7965  C CA    . PRO C 1 81  ? 56.665  -6.989  70.277  1.000 29.384  0 81  PRO CCC CA    1 ? 3 
ATOM   7966  C C     . PRO C 1 81  ? 57.396  -6.335  69.092  1.000 29.465  0 81  PRO CCC C     1 ? 3 
ATOM   7967  O O     . PRO C 1 81  ? 58.607  -6.484  69.024  1.000 30.043  0 81  PRO CCC O     1 ? 3 
ATOM   7968  C CB    . PRO C 1 81  ? 56.005  -8.303  69.844  1.000 29.966  0 81  PRO CCC CB    1 ? 3 
ATOM   7969  C CG    . PRO C 1 81  ? 54.519  -8.036  69.866  1.000 29.270  0 81  PRO CCC CG    1 ? 3 
ATOM   7970  C CD    . PRO C 1 81  ? 54.290  -6.838  70.775  1.000 28.817  0 81  PRO CCC CD    1 ? 3 
ATOM   7971  N N     . LYS C 1 82  ? 56.686  -5.623  68.222  1.000 28.678  0 82  LYS CCC N     1 ? 3 
ATOM   7972  C CA    . LYS C 1 82  ? 57.306  -4.954  67.050  1.000 29.476  0 82  LYS CCC CA    1 ? 3 
ATOM   7973  C C     . LYS C 1 82  ? 58.353  -3.962  67.576  1.000 29.625  0 82  LYS CCC C     1 ? 3 
ATOM   7974  O O     . LYS C 1 82  ? 59.499  -3.961  67.078  1.000 29.474  0 82  LYS CCC O     1 ? 3 
ATOM   7975  C CB    . LYS C 1 82  ? 56.216  -4.282  66.205  1.000 31.997  0 82  LYS CCC CB    1 ? 3 
ATOM   7976  C CG    . LYS C 1 82  ? 56.704  -3.353  65.095  1.000 33.751  0 82  LYS CCC CG    1 ? 3 
ATOM   7977  C CD    . LYS C 1 82  ? 57.008  -1.903  65.509  1.000 33.837  0 82  LYS CCC CD    1 ? 3 
ATOM   7978  C CE    . LYS C 1 82  ? 55.791  -1.127  66.021  1.000 34.132  0 82  LYS CCC CE    1 ? 3 
ATOM   7979  N NZ    . LYS C 1 82  ? 54.711  -0.913  65.017  1.000 33.225  0 82  LYS CCC NZ    1 ? 3 
ATOM   7980  N N     . LYS C 1 83  ? 58.007  -3.185  68.604  1.000 29.310  0 83  LYS CCC N     1 ? 3 
ATOM   7981  C CA    . LYS C 1 83  ? 58.898  -2.138  69.164  1.000 29.294  0 83  LYS CCC CA    1 ? 3 
ATOM   7982  C C     . LYS C 1 83  ? 60.115  -2.787  69.852  1.000 29.764  0 83  LYS CCC C     1 ? 3 
ATOM   7983  O O     . LYS C 1 83  ? 61.242  -2.236  69.727  1.000 28.858  0 83  LYS CCC O     1 ? 3 
ATOM   7984  C CB    . LYS C 1 83  ? 58.093  -1.228  70.082  1.000 30.652  0 83  LYS CCC CB    1 ? 3 
ATOM   7985  C CG    . LYS C 1 83  ? 58.870  -0.040  70.637  1.000 30.738  0 83  LYS CCC CG    1 ? 3 
ATOM   7986  C CD    . LYS C 1 83  ? 58.963  1.120   69.684  1.000 30.372  0 83  LYS CCC CD    1 ? 3 
ATOM   7987  C CE    . LYS C 1 83  ? 59.928  2.192   70.149  1.000 30.417  0 83  LYS CCC CE    1 ? 3 
ATOM   7988  N NZ    . LYS C 1 83  ? 59.241  3.443   70.533  1.000 29.145  0 83  LYS CCC NZ    1 ? 3 
ATOM   7989  N N     . LEU C 1 84  ? 59.946  -3.940  70.502  1.000 30.068  0 84  LEU CCC N     1 ? 3 
ATOM   7990  C CA    . LEU C 1 84  ? 61.115  -4.662  71.103  1.000 29.601  0 84  LEU CCC CA    1 ? 3 
ATOM   7991  C C     . LEU C 1 84  ? 61.996  -5.215  69.970  1.000 30.265  0 84  LEU CCC C     1 ? 3 
ATOM   7992  O O     . LEU C 1 84  ? 63.229  -5.114  70.067  1.000 30.926  0 84  LEU CCC O     1 ? 3 
ATOM   7993  C CB    . LEU C 1 84  ? 60.602  -5.776  72.020  1.000 29.531  0 84  LEU CCC CB    1 ? 3 
ATOM   7994  C CG    . LEU C 1 84  ? 59.776  -5.288  73.213  1.000 30.001  0 84  LEU CCC CG    1 ? 3 
ATOM   7995  C CD1   . LEU C 1 84  ? 59.249  -6.454  74.044  1.000 30.778  0 84  LEU CCC CD1   1 ? 3 
ATOM   7996  C CD2   . LEU C 1 84  ? 60.553  -4.345  74.115  1.000 30.354  0 84  LEU CCC CD2   1 ? 3 
ATOM   7997  N N     . MET C 1 85  ? 61.404  -5.748  68.897  1.000 31.170  0 85  MET CCC N     1 ? 3 
ATOM   7998  C CA    . MET C 1 85  ? 62.218  -6.225  67.752  1.000 34.242  0 85  MET CCC CA    1 ? 3 
ATOM   7999  C C     . MET C 1 85  ? 62.992  -5.038  67.146  1.000 33.583  0 85  MET CCC C     1 ? 3 
ATOM   8000  O O     . MET C 1 85  ? 64.179  -5.184  66.852  1.000 34.636  0 85  MET CCC O     1 ? 3 
ATOM   8001  C CB    . MET C 1 85  ? 61.352  -6.893  66.685  1.000 36.961  0 85  MET CCC CB    1 ? 3 
ATOM   8002  C CG    . MET C 1 85  ? 60.671  -8.139  67.205  1.000 39.799  0 85  MET CCC CG    1 ? 3 
ATOM   8003  S SD    . MET C 1 85  ? 61.539  -9.583  66.502  1.000 48.218  0 85  MET CCC SD    1 ? 3 
ATOM   8004  C CE    . MET C 1 85  ? 60.956  -10.904 67.565  1.000 49.676  0 85  MET CCC CE    1 ? 3 
ATOM   8005  N N     . HIS C 1 86  ? 62.340  -3.896  66.969  1.000 32.966  0 86  HIS CCC N     1 ? 3 
ATOM   8006  C CA    . HIS C 1 86  ? 62.930  -2.659  66.407  1.000 32.386  0 86  HIS CCC CA    1 ? 3 
ATOM   8007  C C     . HIS C 1 86  ? 64.130  -2.268  67.269  1.000 31.292  0 86  HIS CCC C     1 ? 3 
ATOM   8008  O O     . HIS C 1 86  ? 65.201  -1.983  66.691  1.000 27.171  0 86  HIS CCC O     1 ? 3 
ATOM   8009  C CB    . HIS C 1 86  ? 61.829  -1.574  66.346  1.000 32.566  0 86  HIS CCC CB    1 ? 3 
ATOM   8010  C CG    . HIS C 1 86  ? 62.277  -0.229  65.898  1.000 33.075  0 86  HIS CCC CG    1 ? 3 
ATOM   8011  N ND1   . HIS C 1 86  ? 62.829  -0.026  64.639  1.000 32.306  0 86  HIS CCC ND1   1 ? 3 
ATOM   8012  C CD2   . HIS C 1 86  ? 62.210  0.984   66.502  1.000 31.872  0 86  HIS CCC CD2   1 ? 3 
ATOM   8013  C CE1   . HIS C 1 86  ? 63.100  1.272   64.494  1.000 32.567  0 86  HIS CCC CE1   1 ? 3 
ATOM   8014  N NE2   . HIS C 1 86  ? 62.726  1.915   65.629  1.000 30.678  0 86  HIS CCC NE2   1 ? 3 
ATOM   8015  N N     . TYR C 1 87  ? 63.965  -2.341  68.599  1.000 29.146  0 87  TYR CCC N     1 ? 3 
ATOM   8016  C CA    . TYR C 1 87  ? 65.017  -1.980  69.570  1.000 29.341  0 87  TYR CCC CA    1 ? 3 
ATOM   8017  C C     . TYR C 1 87  ? 66.223  -2.890  69.369  1.000 28.808  0 87  TYR CCC C     1 ? 3 
ATOM   8018  O O     . TYR C 1 87  ? 67.336  -2.386  69.261  1.000 27.470  0 87  TYR CCC O     1 ? 3 
ATOM   8019  C CB    . TYR C 1 87  ? 64.461  -2.013  70.991  1.000 32.651  0 87  TYR CCC CB    1 ? 3 
ATOM   8020  C CG    . TYR C 1 87  ? 65.384  -1.386  71.989  1.000 35.742  0 87  TYR CCC CG    1 ? 3 
ATOM   8021  C CD1   . TYR C 1 87  ? 65.696  -0.037  71.916  1.000 39.604  0 87  TYR CCC CD1   1 ? 3 
ATOM   8022  C CD2   . TYR C 1 87  ? 66.001  -2.148  72.962  1.000 37.696  0 87  TYR CCC CD2   1 ? 3 
ATOM   8023  C CE1   . TYR C 1 87  ? 66.582  0.554   72.818  1.000 42.882  0 87  TYR CCC CE1   1 ? 3 
ATOM   8024  C CE2   . TYR C 1 87  ? 66.880  -1.577  73.867  1.000 41.562  0 87  TYR CCC CE2   1 ? 3 
ATOM   8025  C CZ    . TYR C 1 87  ? 67.185  -0.232  73.789  1.000 42.594  0 87  TYR CCC CZ    1 ? 3 
ATOM   8026  O OH    . TYR C 1 87  ? 68.056  0.282   74.695  1.000 50.964  0 87  TYR CCC OH    1 ? 3 
ATOM   8027  N N     . SER C 1 88  ? 66.002  -4.203  69.268  1.000 29.075  0 88  SER CCC N     1 ? 3 
ATOM   8028  C CA    . SER C 1 88  ? 67.057  -5.187  68.946  1.000 28.376  0 88  SER CCC CA    1 ? 3 
ATOM   8029  C C     . SER C 1 88  ? 67.763  -4.775  67.657  1.000 28.149  0 88  SER CCC C     1 ? 3 
ATOM   8030  O O     . SER C 1 88  ? 68.987  -4.895  67.617  1.000 27.248  0 88  SER CCC O     1 ? 3 
ATOM   8031  C CB    . SER C 1 88  ? 66.525  -6.598  68.827  1.000 29.014  0 88  SER CCC CB    1 ? 3 
ATOM   8032  O OG    . SER C 1 88  ? 67.589  -7.527  68.625  1.000 27.496  0 88  SER CCC OG    1 ? 3 
ATOM   8033  N N     . ALA C 1 89  ? 66.997  -4.333  66.651  1.000 27.678  0 89  ALA CCC N     1 ? 3 
ATOM   8034  C CA    . ALA C 1 89  ? 67.523  -3.907  65.334  1.000 27.545  0 89  ALA CCC CA    1 ? 3 
ATOM   8035  C C     . ALA C 1 89  ? 68.431  -2.672  65.504  1.000 28.597  0 89  ALA CCC C     1 ? 3 
ATOM   8036  O O     . ALA C 1 89  ? 69.582  -2.679  64.949  1.000 30.981  0 89  ALA CCC O     1 ? 3 
ATOM   8037  C CB    . ALA C 1 89  ? 66.393  -3.660  64.367  1.000 25.788  0 89  ALA CCC CB    1 ? 3 
ATOM   8038  N N     . LEU C 1 90  ? 67.949  -1.672  66.242  1.000 28.160  0 90  LEU CCC N     1 ? 3 
ATOM   8039  C CA    . LEU C 1 90  ? 68.677  -0.409  66.503  1.000 29.957  0 90  LEU CCC CA    1 ? 3 
ATOM   8040  C C     . LEU C 1 90  ? 69.977  -0.775  67.208  1.000 30.531  0 90  LEU CCC C     1 ? 3 
ATOM   8041  O O     . LEU C 1 90  ? 71.018  -0.131  66.909  1.000 31.666  0 90  LEU CCC O     1 ? 3 
ATOM   8042  C CB    . LEU C 1 90  ? 67.856  0.580   67.344  1.000 29.637  0 90  LEU CCC CB    1 ? 3 
ATOM   8043  C CG    . LEU C 1 90  ? 66.665  1.205   66.602  1.000 31.568  0 90  LEU CCC CG    1 ? 3 
ATOM   8044  C CD1   . LEU C 1 90  ? 65.857  2.154   67.490  1.000 30.992  0 90  LEU CCC CD1   1 ? 3 
ATOM   8045  C CD2   . LEU C 1 90  ? 67.100  1.933   65.321  1.000 32.607  0 90  LEU CCC CD2   1 ? 3 
ATOM   8046  N N     . ILE C 1 91  ? 69.924  -1.799  68.056  1.000 28.655  0 91  ILE CCC N     1 ? 3 
ATOM   8047  C CA    . ILE C 1 91  ? 71.137  -2.229  68.800  1.000 28.520  0 91  ILE CCC CA    1 ? 3 
ATOM   8048  C C     . ILE C 1 91  ? 72.129  -2.824  67.795  1.000 29.671  0 91  ILE CCC C     1 ? 3 
ATOM   8049  O O     . ILE C 1 91  ? 73.302  -2.400  67.811  1.000 29.132  0 91  ILE CCC O     1 ? 3 
ATOM   8050  C CB    . ILE C 1 91  ? 70.778  -3.176  69.964  1.000 27.913  0 91  ILE CCC CB    1 ? 3 
ATOM   8051  C CG1   . ILE C 1 91  ? 70.075  -2.386  71.076  1.000 27.102  0 91  ILE CCC CG1   1 ? 3 
ATOM   8052  C CG2   . ILE C 1 91  ? 72.011  -3.923  70.453  1.000 27.206  0 91  ILE CCC CG2   1 ? 3 
ATOM   8053  C CD1   . ILE C 1 91  ? 69.782  -3.159  72.318  1.000 27.855  0 91  ILE CCC CD1   1 ? 3 
ATOM   8054  N N     . ALA C 1 92  ? 71.680  -3.765  66.963  1.000 29.115  0 92  ALA CCC N     1 ? 3 
ATOM   8055  C CA    . ALA C 1 92  ? 72.494  -4.344  65.869  1.000 31.455  0 92  ALA CCC CA    1 ? 3 
ATOM   8056  C C     . ALA C 1 92  ? 73.184  -3.225  65.067  1.000 30.650  0 92  ALA CCC C     1 ? 3 
ATOM   8057  O O     . ALA C 1 92  ? 74.419  -3.252  64.903  1.000 29.297  0 92  ALA CCC O     1 ? 3 
ATOM   8058  C CB    . ALA C 1 92  ? 71.606  -5.171  64.963  1.000 33.067  0 92  ALA CCC CB    1 ? 3 
ATOM   8059  N N     . SER C 1 93  ? 72.395  -2.270  64.583  1.000 30.594  0 93  SER CCC N     1 ? 3 
ATOM   8060  C CA    . SER C 1 93  ? 72.874  -1.132  63.762  1.000 30.416  0 93  SER CCC CA    1 ? 3 
ATOM   8061  C C     . SER C 1 93  ? 73.949  -0.333  64.496  1.000 29.541  0 93  SER CCC C     1 ? 3 
ATOM   8062  O O     . SER C 1 93  ? 75.025  -0.100  63.946  1.000 29.751  0 93  SER CCC O     1 ? 3 
ATOM   8063  C CB    . SER C 1 93  ? 71.740  -0.274  63.361  1.000 30.735  0 93  SER CCC CB    1 ? 3 
ATOM   8064  O OG    . SER C 1 93  ? 71.217  -0.817  62.171  1.000 35.677  0 93  SER CCC OG    1 ? 3 
ATOM   8065  N N     A SER C 1 94  ? 73.663  0.069   65.729  0.500 29.521  0 94  SER CCC N     1 ? 3 
ATOM   8066  N N     B SER C 1 94  ? 73.664  0.075   65.730  0.500 29.092  0 94  SER CCC N     1 ? 3 
ATOM   8067  C CA    A SER C 1 94  ? 74.587  0.821   66.605  0.500 28.891  0 94  SER CCC CA    1 ? 3 
ATOM   8068  C CA    B SER C 1 94  ? 74.586  0.829   66.612  0.500 28.228  0 94  SER CCC CA    1 ? 3 
ATOM   8069  C C     A SER C 1 94  ? 75.905  0.045   66.761  0.500 29.841  0 94  SER CCC C     1 ? 3 
ATOM   8070  C C     B SER C 1 94  ? 75.904  0.045   66.759  0.500 29.448  0 94  SER CCC C     1 ? 3 
ATOM   8071  O O     A SER C 1 94  ? 76.978  0.666   66.686  0.500 29.910  0 94  SER CCC O     1 ? 3 
ATOM   8072  O O     B SER C 1 94  ? 76.983  0.655   66.663  0.500 29.509  0 94  SER CCC O     1 ? 3 
ATOM   8073  C CB    A SER C 1 94  ? 73.905  1.099   67.920  0.500 28.961  0 94  SER CCC CB    1 ? 3 
ATOM   8074  C CB    B SER C 1 94  ? 73.903  1.115   67.939  0.500 27.853  0 94  SER CCC CB    1 ? 3 
ATOM   8075  O OG    A SER C 1 94  ? 74.841  1.125   68.992  0.500 29.285  0 94  SER CCC OG    1 ? 3 
ATOM   8076  O OG    B SER C 1 94  ? 73.666  2.512   68.139  0.500 26.893  0 94  SER CCC OG    1 ? 3 
ATOM   8077  N N     . ILE C 1 95  ? 75.831  -1.273  66.950  1.000 30.365  0 95  ILE CCC N     1 ? 3 
ATOM   8078  C CA    . ILE C 1 95  ? 77.029  -2.142  67.134  1.000 32.642  0 95  ILE CCC CA    1 ? 3 
ATOM   8079  C C     . ILE C 1 95  ? 77.801  -2.258  65.817  1.000 33.269  0 95  ILE CCC C     1 ? 3 
ATOM   8080  O O     . ILE C 1 95  ? 79.003  -2.113  65.860  1.000 34.807  0 95  ILE CCC O     1 ? 3 
ATOM   8081  C CB    . ILE C 1 95  ? 76.661  -3.536  67.663  1.000 33.749  0 95  ILE CCC CB    1 ? 3 
ATOM   8082  C CG1   . ILE C 1 95  ? 76.186  -3.490  69.110  1.000 34.373  0 95  ILE CCC CG1   1 ? 3 
ATOM   8083  C CG2   . ILE C 1 95  ? 77.844  -4.478  67.509  1.000 34.316  0 95  ILE CCC CG2   1 ? 3 
ATOM   8084  C CD1   . ILE C 1 95  ? 75.693  -4.823  69.634  1.000 35.071  0 95  ILE CCC CD1   1 ? 3 
ATOM   8085  N N     . HIS C 1 96  ? 77.137  -2.538  64.704  1.000 32.859  0 96  HIS CCC N     1 ? 3 
ATOM   8086  C CA    . HIS C 1 96  ? 77.786  -2.609  63.372  1.000 33.144  0 96  HIS CCC CA    1 ? 3 
ATOM   8087  C C     . HIS C 1 96  ? 78.399  -1.257  62.982  1.000 31.807  0 96  HIS CCC C     1 ? 3 
ATOM   8088  O O     . HIS C 1 96  ? 79.578  -1.224  62.654  1.000 36.417  0 96  HIS CCC O     1 ? 3 
ATOM   8089  C CB    . HIS C 1 96  ? 76.806  -3.117  62.320  1.000 34.097  0 96  HIS CCC CB    1 ? 3 
ATOM   8090  C CG    . HIS C 1 96  ? 77.422  -3.259  60.969  1.000 37.292  0 96  HIS CCC CG    1 ? 3 
ATOM   8091  N ND1   . HIS C 1 96  ? 77.107  -2.403  59.903  1.000 39.149  0 96  HIS CCC ND1   1 ? 3 
ATOM   8092  C CD2   . HIS C 1 96  ? 78.329  -4.153  60.506  1.000 38.762  0 96  HIS CCC CD2   1 ? 3 
ATOM   8093  C CE1   . HIS C 1 96  ? 77.797  -2.777  58.842  1.000 40.295  0 96  HIS CCC CE1   1 ? 3 
ATOM   8094  N NE2   . HIS C 1 96  ? 78.551  -3.858  59.190  1.000 41.412  0 96  HIS CCC NE2   1 ? 3 
ATOM   8095  N N     . HIS C 1 97  ? 77.644  -0.169  63.022  1.000 31.748  0 97  HIS CCC N     1 ? 3 
ATOM   8096  C CA    . HIS C 1 97  ? 77.999  1.135   62.379  1.000 30.116  0 97  HIS CCC CA    1 ? 3 
ATOM   8097  C C     . HIS C 1 97  ? 78.760  2.064   63.314  1.000 27.890  0 97  HIS CCC C     1 ? 3 
ATOM   8098  O O     . HIS C 1 97  ? 79.524  2.832   62.790  1.000 28.806  0 97  HIS CCC O     1 ? 3 
ATOM   8099  C CB    . HIS C 1 97  ? 76.748  1.898   61.935  1.000 29.918  0 97  HIS CCC CB    1 ? 3 
ATOM   8100  C CG    . HIS C 1 97  ? 76.082  1.303   60.765  1.000 30.916  0 97  HIS CCC CG    1 ? 3 
ATOM   8101  N ND1   . HIS C 1 97  ? 76.718  1.199   59.550  1.000 30.890  0 97  HIS CCC ND1   1 ? 3 
ATOM   8102  C CD2   . HIS C 1 97  ? 74.850  0.768   60.619  1.000 30.711  0 97  HIS CCC CD2   1 ? 3 
ATOM   8103  C CE1   . HIS C 1 97  ? 75.906  0.618   58.693  1.000 30.108  0 97  HIS CCC CE1   1 ? 3 
ATOM   8104  N NE2   . HIS C 1 97  ? 74.745  0.364   59.320  1.000 31.483  0 97  HIS CCC NE2   1 ? 3 
ATOM   8105  N N     . ASP C 1 98  ? 78.452  2.063   64.616  1.000 25.599  0 98  ASP CCC N     1 ? 3 
ATOM   8106  C CA    . ASP C 1 98  ? 78.751  3.204   65.515  1.000 24.632  0 98  ASP CCC CA    1 ? 3 
ATOM   8107  C C     . ASP C 1 98  ? 79.763  2.810   66.592  1.000 23.401  0 98  ASP CCC C     1 ? 3 
ATOM   8108  O O     . ASP C 1 98  ? 80.569  3.671   66.972  1.000 23.123  0 98  ASP CCC O     1 ? 3 
ATOM   8109  C CB    . ASP C 1 98  ? 77.503  3.735   66.238  1.000 24.573  0 98  ASP CCC CB    1 ? 3 
ATOM   8110  C CG    . ASP C 1 98  ? 76.423  4.330   65.348  1.000 25.423  0 98  ASP CCC CG    1 ? 3 
ATOM   8111  O OD1   . ASP C 1 98  ? 76.661  4.491   64.145  1.000 24.099  0 98  ASP CCC OD1   1 ? 3 
ATOM   8112  O OD2   . ASP C 1 98  ? 75.313  4.623   65.875  1.000 25.967  0 98  ASP CCC OD2   1 ? 3 
ATOM   8113  N N     . ALA C 1 99  ? 79.695  1.603   67.125  1.000 23.123  0 99  ALA CCC N     1 ? 3 
ATOM   8114  C CA    . ALA C 1 99  ? 80.373  1.248   68.394  1.000 23.760  0 99  ALA CCC CA    1 ? 3 
ATOM   8115  C C     . ALA C 1 99  ? 81.879  1.487   68.245  1.000 25.635  0 99  ALA CCC C     1 ? 3 
ATOM   8116  O O     . ALA C 1 99  ? 82.435  2.157   69.109  1.000 25.824  0 99  ALA CCC O     1 ? 3 
ATOM   8117  C CB    . ALA C 1 99  ? 80.059  -0.161  68.816  1.000 22.915  0 99  ALA CCC CB    1 ? 3 
ATOM   8118  N N     . GLN C 1 100 ? 82.521  0.971   67.199  1.000 28.244  0 100 GLN CCC N     1 ? 3 
ATOM   8119  C CA    . GLN C 1 100 ? 83.999  1.100   67.060  1.000 29.863  0 100 GLN CCC CA    1 ? 3 
ATOM   8120  C C     . GLN C 1 100 ? 84.360  2.587   66.924  1.000 30.876  0 100 GLN CCC C     1 ? 3 
ATOM   8121  O O     . GLN C 1 100 ? 85.281  3.044   67.639  1.000 30.595  0 100 GLN CCC O     1 ? 3 
ATOM   8122  C CB    . GLN C 1 100 ? 84.559  0.259   65.917  1.000 30.969  0 100 GLN CCC CB    1 ? 3 
ATOM   8123  C CG    . GLN C 1 100 ? 86.087  0.275   65.939  1.000 33.634  0 100 GLN CCC CG    1 ? 3 
ATOM   8124  C CD    . GLN C 1 100 ? 86.735  -0.728  65.013  1.000 34.537  0 100 GLN CCC CD    1 ? 3 
ATOM   8125  O OE1   . GLN C 1 100 ? 86.086  -1.464  64.275  1.000 34.802  0 100 GLN CCC OE1   1 ? 3 
ATOM   8126  N NE2   . GLN C 1 100 ? 88.047  -0.796  65.075  1.000 35.796  0 100 GLN CCC NE2   1 ? 3 
ATOM   8127  N N     . MET C 1 101 ? 83.598  3.347   66.137  1.000 31.674  0 101 MET CCC N     1 ? 3 
ATOM   8128  C CA    . MET C 1 101 ? 83.854  4.794   65.896  1.000 31.777  0 101 MET CCC CA    1 ? 3 
ATOM   8129  C C     . MET C 1 101 ? 83.779  5.571   67.217  1.000 30.424  0 101 MET CCC C     1 ? 3 
ATOM   8130  O O     . MET C 1 101 ? 84.485  6.595   67.339  1.000 31.613  0 101 MET CCC O     1 ? 3 
ATOM   8131  C CB    . MET C 1 101 ? 82.837  5.382   64.912  1.000 32.915  0 101 MET CCC CB    1 ? 3 
ATOM   8132  C CG    . MET C 1 101 ? 83.023  4.944   63.466  1.000 33.759  0 101 MET CCC CG    1 ? 3 
ATOM   8133  S SD    . MET C 1 101 ? 84.599  5.520   62.751  1.000 38.303  0 101 MET CCC SD    1 ? 3 
ATOM   8134  C CE    . MET C 1 101 ? 84.444  7.302   62.717  1.000 34.917  0 101 MET CCC CE    1 ? 3 
ATOM   8135  N N     . PHE C 1 102 ? 82.932  5.142   68.153  1.000 28.521  0 102 PHE CCC N     1 ? 3 
ATOM   8136  C CA    . PHE C 1 102 ? 82.724  5.830   69.451  1.000 27.966  0 102 PHE CCC CA    1 ? 3 
ATOM   8137  C C     . PHE C 1 102 ? 83.569  5.158   70.530  1.000 28.901  0 102 PHE CCC C     1 ? 3 
ATOM   8138  O O     . PHE C 1 102 ? 83.350  5.427   71.722  1.000 29.177  0 102 PHE CCC O     1 ? 3 
ATOM   8139  C CB    . PHE C 1 102 ? 81.227  5.956   69.796  1.000 26.803  0 102 PHE CCC CB    1 ? 3 
ATOM   8140  C CG    . PHE C 1 102 ? 80.563  7.031   68.981  1.000 25.607  0 102 PHE CCC CG    1 ? 3 
ATOM   8141  C CD1   . PHE C 1 102 ? 80.119  6.767   67.698  1.000 25.384  0 102 PHE CCC CD1   1 ? 3 
ATOM   8142  C CD2   . PHE C 1 102 ? 80.483  8.325   69.449  1.000 24.707  0 102 PHE CCC CD2   1 ? 3 
ATOM   8143  C CE1   . PHE C 1 102 ? 79.542  7.761   66.929  1.000 24.941  0 102 PHE CCC CE1   1 ? 3 
ATOM   8144  C CE2   . PHE C 1 102 ? 79.934  9.330   68.675  1.000 24.646  0 102 PHE CCC CE2   1 ? 3 
ATOM   8145  C CZ    . PHE C 1 102 ? 79.486  9.047   67.405  1.000 25.573  0 102 PHE CCC CZ    1 ? 3 
ATOM   8146  N N     . GLY C 1 103 ? 84.556  4.357   70.120  1.000 31.772  0 103 GLY CCC N     1 ? 3 
ATOM   8147  C CA    . GLY C 1 103 ? 85.651  3.856   70.984  1.000 32.049  0 103 GLY CCC CA    1 ? 3 
ATOM   8148  C C     . GLY C 1 103 ? 85.373  2.466   71.528  1.000 32.563  0 103 GLY CCC C     1 ? 3 
ATOM   8149  O O     . GLY C 1 103 ? 86.196  1.971   72.316  1.000 36.278  0 103 GLY CCC O     1 ? 3 
ATOM   8150  N N     . HIS C 1 104 ? 84.258  1.859   71.149  1.000 31.053  0 104 HIS CCC N     1 ? 3 
ATOM   8151  C CA    . HIS C 1 104 ? 83.820  0.540   71.675  1.000 30.944  0 104 HIS CCC CA    1 ? 3 
ATOM   8152  C C     . HIS C 1 104 ? 84.082  -0.523  70.590  1.000 32.020  0 104 HIS CCC C     1 ? 3 
ATOM   8153  O O     . HIS C 1 104 ? 83.247  -0.688  69.709  1.000 30.478  0 104 HIS CCC O     1 ? 3 
ATOM   8154  C CB    . HIS C 1 104 ? 82.349  0.606   72.106  1.000 29.134  0 104 HIS CCC CB    1 ? 3 
ATOM   8155  C CG    . HIS C 1 104 ? 82.060  1.628   73.139  1.000 27.701  0 104 HIS CCC CG    1 ? 3 
ATOM   8156  N ND1   . HIS C 1 104 ? 82.293  1.407   74.490  1.000 27.155  0 104 HIS CCC ND1   1 ? 3 
ATOM   8157  C CD2   . HIS C 1 104 ? 81.568  2.875   73.040  1.000 27.672  0 104 HIS CCC CD2   1 ? 3 
ATOM   8158  C CE1   . HIS C 1 104 ? 81.967  2.482   75.153  1.000 26.734  0 104 HIS CCC CE1   1 ? 3 
ATOM   8159  N NE2   . HIS C 1 104 ? 81.507  3.399   74.296  1.000 25.968  0 104 HIS CCC NE2   1 ? 3 
ATOM   8160  N N     . LYS C 1 105 ? 85.255  -1.148  70.631  1.000 34.516  0 105 LYS CCC N     1 ? 3 
ATOM   8161  C CA    . LYS C 1 105 ? 85.611  -2.331  69.816  1.000 38.357  0 105 LYS CCC CA    1 ? 3 
ATOM   8162  C C     . LYS C 1 105 ? 84.825  -3.531  70.369  1.000 38.427  0 105 LYS CCC C     1 ? 3 
ATOM   8163  O O     . LYS C 1 105 ? 85.007  -3.893  71.555  1.000 36.649  0 105 LYS CCC O     1 ? 3 
ATOM   8164  C CB    . LYS C 1 105 ? 87.126  -2.580  69.822  1.000 39.569  0 105 LYS CCC CB    1 ? 3 
ATOM   8165  C CG    . LYS C 1 105 ? 87.553  -3.711  68.897  1.000 43.637  0 105 LYS CCC CG    1 ? 3 
ATOM   8166  C CD    . LYS C 1 105 ? 87.460  -3.337  67.426  1.000 46.774  0 105 LYS CCC CD    1 ? 3 
ATOM   8167  C CE    . LYS C 1 105 ? 87.056  -4.446  66.474  1.000 49.695  0 105 LYS CCC CE    1 ? 3 
ATOM   8168  N NZ    . LYS C 1 105 ? 88.071  -5.517  66.371  1.000 48.427  0 105 LYS CCC NZ    1 ? 3 
ATOM   8169  N N     . THR C 1 106 ? 83.956  -4.104  69.549  1.000 37.934  0 106 THR CCC N     1 ? 3 
ATOM   8170  C CA    . THR C 1 106 ? 82.989  -5.141  69.966  1.000 42.026  0 106 THR CCC CA    1 ? 3 
ATOM   8171  C C     . THR C 1 106 ? 83.045  -6.315  68.982  1.000 44.780  0 106 THR CCC C     1 ? 3 
ATOM   8172  O O     . THR C 1 106 ? 83.276  -6.072  67.782  1.000 51.245  0 106 THR CCC O     1 ? 3 
ATOM   8173  C CB    . THR C 1 106 ? 81.559  -4.585  69.958  1.000 41.687  0 106 THR CCC CB    1 ? 3 
ATOM   8174  O OG1   . THR C 1 106 ? 81.262  -4.446  68.566  1.000 45.210  0 106 THR CCC OG1   1 ? 3 
ATOM   8175  C CG2   . THR C 1 106 ? 81.405  -3.264  70.677  1.000 40.224  0 106 THR CCC CG2   1 ? 3 
ATOM   8176  N N     . SER C 1 107 ? 82.772  -7.535  69.429  1.000 43.214  0 107 SER CCC N     1 ? 3 
ATOM   8177  C CA    . SER C 1 107 ? 82.241  -8.587  68.530  1.000 43.998  0 107 SER CCC CA    1 ? 3 
ATOM   8178  C C     . SER C 1 107 ? 80.852  -8.958  69.040  1.000 39.849  0 107 SER CCC C     1 ? 3 
ATOM   8179  O O     . SER C 1 107 ? 80.645  -8.917  70.243  1.000 37.746  0 107 SER CCC O     1 ? 3 
ATOM   8180  C CB    . SER C 1 107 ? 83.183  -9.783  68.393  1.000 44.551  0 107 SER CCC CB    1 ? 3 
ATOM   8181  O OG    . SER C 1 107 ? 83.493  -10.309 69.666  1.000 44.502  0 107 SER CCC OG    1 ? 3 
ATOM   8182  N N     . SER C 1 108 ? 79.964  -9.327  68.132  1.000 39.260  0 108 SER CCC N     1 ? 3 
ATOM   8183  C CA    . SER C 1 108 ? 78.561  -9.638  68.431  1.000 40.091  0 108 SER CCC CA    1 ? 3 
ATOM   8184  C C     . SER C 1 108 ? 78.098  -10.755 67.507  1.000 41.679  0 108 SER CCC C     1 ? 3 
ATOM   8185  O O     . SER C 1 108 ? 78.491  -10.739 66.341  1.000 41.332  0 108 SER CCC O     1 ? 3 
ATOM   8186  C CB    . SER C 1 108 ? 77.720  -8.408  68.270  1.000 40.801  0 108 SER CCC CB    1 ? 3 
ATOM   8187  O OG    . SER C 1 108 ? 76.399  -8.632  68.722  1.000 42.282  0 108 SER CCC OG    1 ? 3 
ATOM   8188  N N     . SER C 1 109 ? 77.244  -11.655 68.007  1.000 42.261  0 109 SER CCC N     1 ? 3 
ATOM   8189  C CA    . SER C 1 109 ? 76.417  -12.541 67.159  1.000 42.941  0 109 SER CCC CA    1 ? 3 
ATOM   8190  C C     . SER C 1 109 ? 74.988  -12.554 67.694  1.000 41.397  0 109 SER CCC C     1 ? 3 
ATOM   8191  O O     . SER C 1 109 ? 74.790  -12.439 68.918  1.000 39.857  0 109 SER CCC O     1 ? 3 
ATOM   8192  C CB    . SER C 1 109 ? 76.995  -13.927 67.053  1.000 46.369  0 109 SER CCC CB    1 ? 3 
ATOM   8193  O OG    . SER C 1 109 ? 77.368  -14.446 68.328  1.000 48.883  0 109 SER CCC OG    1 ? 3 
ATOM   8194  N N     . PHE C 1 110 ? 74.038  -12.666 66.781  1.000 40.935  0 110 PHE CCC N     1 ? 3 
ATOM   8195  C CA    . PHE C 1 110 ? 72.592  -12.587 67.066  1.000 40.809  0 110 PHE CCC CA    1 ? 3 
ATOM   8196  C C     . PHE C 1 110 ? 72.018  -13.992 67.239  1.000 41.283  0 110 PHE CCC C     1 ? 3 
ATOM   8197  O O     . PHE C 1 110 ? 72.274  -14.817 66.377  1.000 41.860  0 110 PHE CCC O     1 ? 3 
ATOM   8198  C CB    . PHE C 1 110 ? 71.858  -11.880 65.938  1.000 40.038  0 110 PHE CCC CB    1 ? 3 
ATOM   8199  C CG    . PHE C 1 110 ? 70.382  -11.838 66.209  1.000 41.035  0 110 PHE CCC CG    1 ? 3 
ATOM   8200  C CD1   . PHE C 1 110 ? 69.895  -11.229 67.358  1.000 42.056  0 110 PHE CCC CD1   1 ? 3 
ATOM   8201  C CD2   . PHE C 1 110 ? 69.498  -12.471 65.361  1.000 39.263  0 110 PHE CCC CD2   1 ? 3 
ATOM   8202  C CE1   . PHE C 1 110 ? 68.531  -11.166 67.584  1.000 41.686  0 110 PHE CCC CE1   1 ? 3 
ATOM   8203  C CE2   . PHE C 1 110 ? 68.145  -12.423 65.601  1.000 39.056  0 110 PHE CCC CE2   1 ? 3 
ATOM   8204  C CZ    . PHE C 1 110 ? 67.660  -11.763 66.703  1.000 40.114  0 110 PHE CCC CZ    1 ? 3 
ATOM   8205  N N     . GLU C 1 111 ? 71.232  -14.217 68.289  1.000 41.611  0 111 GLU CCC N     1 ? 3 
ATOM   8206  C CA    . GLU C 1 111 ? 70.518  -15.490 68.507  1.000 44.193  0 111 GLU CCC CA    1 ? 3 
ATOM   8207  C C     . GLU C 1 111 ? 69.044  -15.164 68.715  1.000 40.706  0 111 GLU CCC C     1 ? 3 
ATOM   8208  O O     . GLU C 1 111 ? 68.642  -14.662 69.783  1.000 38.523  0 111 GLU CCC O     1 ? 3 
ATOM   8209  C CB    . GLU C 1 111 ? 71.161  -16.334 69.602  1.000 49.552  0 111 GLU CCC CB    1 ? 3 
ATOM   8210  C CG    . GLU C 1 111 ? 72.584  -16.768 69.215  1.000 56.368  0 111 GLU CCC CG    1 ? 3 
ATOM   8211  C CD    . GLU C 1 111 ? 72.768  -17.732 68.030  1.000 61.981  0 111 GLU CCC CD    1 ? 3 
ATOM   8212  O OE1   . GLU C 1 111 ? 73.959  -17.910 67.600  1.000 61.173  0 111 GLU CCC OE1   1 ? 3 
ATOM   8213  O OE2   . GLU C 1 111 ? 71.738  -18.347 67.537  1.000 61.783  0 111 GLU CCC OE2   1 ? 3 
ATOM   8214  N N     . TRP C 1 112 ? 68.291  -15.497 67.675  1.000 39.062  0 112 TRP CCC N     1 ? 3 
ATOM   8215  C CA    . TRP C 1 112 ? 66.848  -15.213 67.511  1.000 37.437  0 112 TRP CCC CA    1 ? 3 
ATOM   8216  C C     . TRP C 1 112 ? 66.075  -15.650 68.757  1.000 36.557  0 112 TRP CCC C     1 ? 3 
ATOM   8217  O O     . TRP C 1 112 ? 65.243  -14.841 69.240  1.000 34.323  0 112 TRP CCC O     1 ? 3 
ATOM   8218  C CB    . TRP C 1 112 ? 66.346  -15.873 66.214  1.000 37.440  0 112 TRP CCC CB    1 ? 3 
ATOM   8219  C CG    . TRP C 1 112 ? 64.858  -15.834 66.044  1.000 37.190  0 112 TRP CCC CG    1 ? 3 
ATOM   8220  C CD1   . TRP C 1 112 ? 63.964  -16.805 66.406  1.000 36.828  0 112 TRP CCC CD1   1 ? 3 
ATOM   8221  C CD2   . TRP C 1 112 ? 64.078  -14.752 65.491  1.000 35.023  0 112 TRP CCC CD2   1 ? 3 
ATOM   8222  N NE1   . TRP C 1 112 ? 62.693  -16.393 66.114  1.000 37.639  0 112 TRP CCC NE1   1 ? 3 
ATOM   8223  C CE2   . TRP C 1 112 ? 62.731  -15.149 65.542  1.000 35.160  0 112 TRP CCC CE2   1 ? 3 
ATOM   8224  C CE3   . TRP C 1 112 ? 64.370  -13.490 64.962  1.000 34.000  0 112 TRP CCC CE3   1 ? 3 
ATOM   8225  C CZ2   . TRP C 1 112 ? 61.704  -14.329 65.092  1.000 33.715  0 112 TRP CCC CZ2   1 ? 3 
ATOM   8226  C CZ3   . TRP C 1 112 ? 63.353  -12.684 64.524  1.000 31.660  0 112 TRP CCC CZ3   1 ? 3 
ATOM   8227  C CH2   . TRP C 1 112 ? 62.041  -13.101 64.592  1.000 32.701  0 112 TRP CCC CH2   1 ? 3 
ATOM   8228  N N     . GLY C 1 113 ? 66.306  -16.867 69.254  1.000 36.875  0 113 GLY CCC N     1 ? 3 
ATOM   8229  C CA    . GLY C 1 113 ? 65.502  -17.471 70.343  1.000 38.830  0 113 GLY CCC CA    1 ? 3 
ATOM   8230  C C     . GLY C 1 113 ? 65.651  -16.727 71.669  1.000 38.967  0 113 GLY CCC C     1 ? 3 
ATOM   8231  O O     . GLY C 1 113 ? 64.739  -16.784 72.507  1.000 38.938  0 113 GLY CCC O     1 ? 3 
ATOM   8232  N N     . LYS C 1 114 ? 66.773  -16.042 71.870  1.000 38.775  0 114 LYS CCC N     1 ? 3 
ATOM   8233  C CA    . LYS C 1 114 ? 66.997  -15.232 73.085  1.000 38.287  0 114 LYS CCC CA    1 ? 3 
ATOM   8234  C C     . LYS C 1 114 ? 66.097  -13.995 73.041  1.000 35.814  0 114 LYS CCC C     1 ? 3 
ATOM   8235  O O     . LYS C 1 114 ? 65.484  -13.672 74.083  1.000 37.984  0 114 LYS CCC O     1 ? 3 
ATOM   8236  C CB    . LYS C 1 114 ? 68.486  -14.923 73.195  1.000 39.689  0 114 LYS CCC CB    1 ? 3 
ATOM   8237  C CG    . LYS C 1 114 ? 68.865  -14.076 74.393  1.000 40.682  0 114 LYS CCC CG    1 ? 3 
ATOM   8238  C CD    . LYS C 1 114 ? 68.282  -14.547 75.672  1.000 42.333  0 114 LYS CCC CD    1 ? 3 
ATOM   8239  C CE    . LYS C 1 114 ? 68.869  -13.766 76.828  1.000 44.494  0 114 LYS CCC CE    1 ? 3 
ATOM   8240  N NZ    . LYS C 1 114 ? 68.306  -14.212 78.122  1.000 46.773  0 114 LYS CCC NZ    1 ? 3 
ATOM   8241  N N     . LEU C 1 115 ? 66.022  -13.321 71.892  1.000 33.362  0 115 LEU CCC N     1 ? 3 
ATOM   8242  C CA    . LEU C 1 115 ? 65.175  -12.115 71.666  1.000 31.839  0 115 LEU CCC CA    1 ? 3 
ATOM   8243  C C     . LEU C 1 115 ? 63.696  -12.497 71.861  1.000 31.147  0 115 LEU CCC C     1 ? 3 
ATOM   8244  O O     . LEU C 1 115 ? 62.974  -11.817 72.602  1.000 32.500  0 115 LEU CCC O     1 ? 3 
ATOM   8245  C CB    . LEU C 1 115 ? 65.408  -11.559 70.253  1.000 29.746  0 115 LEU CCC CB    1 ? 3 
ATOM   8246  C CG    . LEU C 1 115 ? 64.458  -10.437 69.827  1.000 28.051  0 115 LEU CCC CG    1 ? 3 
ATOM   8247  C CD1   . LEU C 1 115 ? 64.562  -9.216  70.737  1.000 27.930  0 115 LEU CCC CD1   1 ? 3 
ATOM   8248  C CD2   . LEU C 1 115 ? 64.675  -10.012 68.395  1.000 28.776  0 115 LEU CCC CD2   1 ? 3 
ATOM   8249  N N     . VAL C 1 116 ? 63.286  -13.568 71.212  1.000 31.725  0 116 VAL CCC N     1 ? 3 
ATOM   8250  C CA    . VAL C 1 116 ? 61.944  -14.171 71.366  1.000 33.404  0 116 VAL CCC CA    1 ? 3 
ATOM   8251  C C     . VAL C 1 116 ? 61.685  -14.375 72.856  1.000 35.361  0 116 VAL CCC C     1 ? 3 
ATOM   8252  O O     . VAL C 1 116 ? 60.678  -13.867 73.346  1.000 37.606  0 116 VAL CCC O     1 ? 3 
ATOM   8253  C CB    . VAL C 1 116 ? 61.832  -15.460 70.542  1.000 33.640  0 116 VAL CCC CB    1 ? 3 
ATOM   8254  C CG1   . VAL C 1 116 ? 60.650  -16.325 70.965  1.000 35.825  0 116 VAL CCC CG1   1 ? 3 
ATOM   8255  C CG2   . VAL C 1 116 ? 61.714  -15.117 69.069  1.000 33.163  0 116 VAL CCC CG2   1 ? 3 
ATOM   8256  N N     . GLU C 1 117 ? 62.615  -14.994 73.568  1.000 37.890  0 117 GLU CCC N     1 ? 3 
ATOM   8257  C CA    . GLU C 1 117 ? 62.452  -15.291 75.015  1.000 39.061  0 117 GLU CCC CA    1 ? 3 
ATOM   8258  C C     . GLU C 1 117 ? 62.234  -13.971 75.780  1.000 38.507  0 117 GLU CCC C     1 ? 3 
ATOM   8259  O O     . GLU C 1 117 ? 61.266  -13.897 76.589  1.000 39.910  0 117 GLU CCC O     1 ? 3 
ATOM   8260  C CB    . GLU C 1 117 ? 63.621  -16.172 75.475  1.000 40.491  0 117 GLU CCC CB    1 ? 3 
ATOM   8261  C CG    . GLU C 1 117 ? 63.640  -16.484 76.965  1.000 42.726  0 117 GLU CCC CG    1 ? 3 
ATOM   8262  C CD    . GLU C 1 117 ? 65.055  -16.755 77.495  1.000 47.007  0 117 GLU CCC CD    1 ? 3 
ATOM   8263  O OE1   . GLU C 1 117 ? 65.500  -15.990 78.378  1.000 48.639  0 117 GLU CCC OE1   1 ? 3 
ATOM   8264  O OE2   . GLU C 1 117 ? 65.758  -17.694 76.997  1.000 48.947  0 117 GLU CCC OE2   1 ? 3 
ATOM   8265  N N     . THR C 1 118 ? 63.020  -12.927 75.506  1.000 36.555  0 118 THR CCC N     1 ? 3 
ATOM   8266  C CA    . THR C 1 118 ? 62.851  -11.591 76.151  1.000 35.119  0 118 THR CCC CA    1 ? 3 
ATOM   8267  C C     . THR C 1 118 ? 61.465  -10.995 75.827  1.000 33.858  0 118 THR CCC C     1 ? 3 
ATOM   8268  O O     . THR C 1 118 ? 60.847  -10.445 76.758  1.000 32.650  0 118 THR CCC O     1 ? 3 
ATOM   8269  C CB    . THR C 1 118 ? 64.003  -10.665 75.756  1.000 35.975  0 118 THR CCC CB    1 ? 3 
ATOM   8270  O OG1   . THR C 1 118 ? 65.162  -11.174 76.403  1.000 37.458  0 118 THR CCC OG1   1 ? 3 
ATOM   8271  C CG2   . THR C 1 118 ? 63.807  -9.225  76.154  1.000 36.133  0 118 THR CCC CG2   1 ? 3 
ATOM   8272  N N     . LEU C 1 119 ? 60.990  -11.104 74.579  1.000 32.973  0 119 LEU CCC N     1 ? 3 
ATOM   8273  C CA    . LEU C 1 119 ? 59.624  -10.674 74.168  1.000 33.906  0 119 LEU CCC CA    1 ? 3 
ATOM   8274  C C     . LEU C 1 119 ? 58.563  -11.426 74.978  1.000 33.955  0 119 LEU CCC C     1 ? 3 
ATOM   8275  O O     . LEU C 1 119 ? 57.747  -10.749 75.636  1.000 29.146  0 119 LEU CCC O     1 ? 3 
ATOM   8276  C CB    . LEU C 1 119 ? 59.376  -10.927 72.674  1.000 33.420  0 119 LEU CCC CB    1 ? 3 
ATOM   8277  C CG    . LEU C 1 119 ? 59.660  -9.738  71.775  1.000 34.122  0 119 LEU CCC CG    1 ? 3 
ATOM   8278  C CD1   . LEU C 1 119 ? 61.123  -9.387  71.835  1.000 35.476  0 119 LEU CCC CD1   1 ? 3 
ATOM   8279  C CD2   . LEU C 1 119 ? 59.252  -10.021 70.342  1.000 34.466  0 119 LEU CCC CD2   1 ? 3 
ATOM   8280  N N     . ARG C 1 120 ? 58.589  -12.765 74.879  1.000 36.996  0 120 ARG CCC N     1 ? 3 
ATOM   8281  C CA    . ARG C 1 120 ? 57.608  -13.679 75.522  1.000 39.773  0 120 ARG CCC CA    1 ? 3 
ATOM   8282  C C     . ARG C 1 120 ? 57.499  -13.332 77.010  1.000 39.828  0 120 ARG CCC C     1 ? 3 
ATOM   8283  O O     . ARG C 1 120 ? 56.380  -13.188 77.483  1.000 39.302  0 120 ARG CCC O     1 ? 3 
ATOM   8284  C CB    . ARG C 1 120 ? 57.977  -15.152 75.339  1.000 44.021  0 120 ARG CCC CB    1 ? 3 
ATOM   8285  C CG    . ARG C 1 120 ? 57.299  -15.837 74.159  1.000 50.025  0 120 ARG CCC CG    1 ? 3 
ATOM   8286  C CD    . ARG C 1 120 ? 57.352  -17.368 74.161  1.000 59.386  0 120 ARG CCC CD    1 ? 3 
ATOM   8287  N NE    . ARG C 1 120 ? 58.579  -17.954 73.563  1.000 64.779  0 120 ARG CCC NE    1 ? 3 
ATOM   8288  C CZ    . ARG C 1 120 ? 59.719  -18.281 74.208  1.000 66.387  0 120 ARG CCC CZ    1 ? 3 
ATOM   8289  N NH1   . ARG C 1 120 ? 59.867  -18.097 75.512  1.000 68.609  0 120 ARG CCC NH1   1 ? 3 
ATOM   8290  N NH2   . ARG C 1 120 ? 60.724  -18.796 73.523  1.000 69.048  0 120 ARG CCC NH2   1 ? 3 
ATOM   8291  N N     . ASN C 1 121 ? 58.625  -13.196 77.720  1.000 40.410  0 121 ASN CCC N     1 ? 3 
ATOM   8292  C CA    . ASN C 1 121 ? 58.631  -12.946 79.188  1.000 40.344  0 121 ASN CCC CA    1 ? 3 
ATOM   8293  C C     . ASN C 1 121 ? 57.966  -11.606 79.470  1.000 38.804  0 121 ASN CCC C     1 ? 3 
ATOM   8294  O O     . ASN C 1 121 ? 57.150  -11.538 80.385  1.000 37.536  0 121 ASN CCC O     1 ? 3 
ATOM   8295  C CB    . ASN C 1 121 ? 60.030  -12.966 79.814  1.000 43.018  0 121 ASN CCC CB    1 ? 3 
ATOM   8296  C CG    . ASN C 1 121 ? 60.704  -14.328 79.764  1.000 46.023  0 121 ASN CCC CG    1 ? 3 
ATOM   8297  O OD1   . ASN C 1 121 ? 60.099  -15.333 79.380  1.000 47.752  0 121 ASN CCC OD1   1 ? 3 
ATOM   8298  N ND2   . ASN C 1 121 ? 61.973  -14.372 80.137  1.000 49.688  0 121 ASN CCC ND2   1 ? 3 
ATOM   8299  N N     . HIS C 1 122 ? 58.280  -10.569 78.699  1.000 37.254  0 122 HIS CCC N     1 ? 3 
ATOM   8300  C CA    . HIS C 1 122 ? 57.712  -9.221  78.948  1.000 37.106  0 122 HIS CCC CA    1 ? 3 
ATOM   8301  C C     . HIS C 1 122 ? 56.191  -9.234  78.646  1.000 37.275  0 122 HIS CCC C     1 ? 3 
ATOM   8302  O O     . HIS C 1 122 ? 55.407  -8.698  79.431  1.000 35.807  0 122 HIS CCC O     1 ? 3 
ATOM   8303  C CB    . HIS C 1 122 ? 58.523  -8.181  78.187  1.000 35.738  0 122 HIS CCC CB    1 ? 3 
ATOM   8304  C CG    . HIS C 1 122 ? 58.086  -6.814  78.524  1.000 33.535  0 122 HIS CCC CG    1 ? 3 
ATOM   8305  N ND1   . HIS C 1 122 ? 57.193  -6.133  77.730  1.000 33.681  0 122 HIS CCC ND1   1 ? 3 
ATOM   8306  C CD2   . HIS C 1 122 ? 58.387  -6.025  79.569  1.000 32.967  0 122 HIS CCC CD2   1 ? 3 
ATOM   8307  C CE1   . HIS C 1 122 ? 56.992  -4.936  78.253  1.000 34.073  0 122 HIS CCC CE1   1 ? 3 
ATOM   8308  N NE2   . HIS C 1 122 ? 57.712  -4.847  79.398  1.000 33.011  0 122 HIS CCC NE2   1 ? 3 
ATOM   8309  N N     . ILE C 1 123 ? 55.787  -9.878  77.560  1.000 36.140  0 123 ILE CCC N     1 ? 3 
ATOM   8310  C CA    . ILE C 1 123 ? 54.365  -9.995  77.168  1.000 36.899  0 123 ILE CCC CA    1 ? 3 
ATOM   8311  C C     . ILE C 1 123 ? 53.613  -10.835 78.227  1.000 40.761  0 123 ILE CCC C     1 ? 3 
ATOM   8312  O O     . ILE C 1 123 ? 52.485  -10.449 78.572  1.000 39.749  0 123 ILE CCC O     1 ? 3 
ATOM   8313  C CB    . ILE C 1 123 ? 54.261  -10.539 75.732  1.000 34.285  0 123 ILE CCC CB    1 ? 3 
ATOM   8314  C CG1   . ILE C 1 123 ? 54.726  -9.465  74.752  1.000 33.817  0 123 ILE CCC CG1   1 ? 3 
ATOM   8315  C CG2   . ILE C 1 123 ? 52.856  -11.047 75.445  1.000 34.769  0 123 ILE CCC CG2   1 ? 3 
ATOM   8316  C CD1   . ILE C 1 123 ? 54.979  -9.952  73.345  1.000 34.650  0 123 ILE CCC CD1   1 ? 3 
ATOM   8317  N N     . ARG C 1 124 ? 54.203  -11.922 78.737  1.000 41.147  0 124 ARG CCC N     1 ? 3 
ATOM   8318  C CA    . ARG C 1 124 ? 53.576  -12.724 79.812  1.000 44.447  0 124 ARG CCC CA    1 ? 3 
ATOM   8319  C C     . ARG C 1 124 ? 53.300  -11.803 81.023  1.000 46.376  0 124 ARG CCC C     1 ? 3 
ATOM   8320  O O     . ARG C 1 124 ? 52.150  -11.752 81.499  1.000 41.167  0 124 ARG CCC O     1 ? 3 
ATOM   8321  C CB    . ARG C 1 124 ? 54.441  -13.929 80.168  1.000 46.622  0 124 ARG CCC CB    1 ? 3 
ATOM   8322  C CG    . ARG C 1 124 ? 53.676  -15.078 80.803  1.000 51.550  0 124 ARG CCC CG    1 ? 3 
ATOM   8323  C CD    . ARG C 1 124 ? 54.536  -16.329 81.015  1.000 54.959  0 124 ARG CCC CD    1 ? 3 
ATOM   8324  N NE    . ARG C 1 124 ? 55.273  -16.771 79.827  1.000 56.986  0 124 ARG CCC NE    1 ? 3 
ATOM   8325  C CZ    . ARG C 1 124 ? 56.603  -16.685 79.659  1.000 58.524  0 124 ARG CCC CZ    1 ? 3 
ATOM   8326  N NH1   . ARG C 1 124 ? 57.390  -16.184 80.603  1.000 59.406  0 124 ARG CCC NH1   1 ? 3 
ATOM   8327  N NH2   . ARG C 1 124 ? 57.149  -17.101 78.529  1.000 58.082  0 124 ARG CCC NH2   1 ? 3 
ATOM   8328  N N     . MET C 1 125 ? 54.302  -11.041 81.468  1.000 46.816  0 125 MET CCC N     1 ? 3 
ATOM   8329  C CA    . MET C 1 125 ? 54.144  -10.074 82.578  1.000 48.028  0 125 MET CCC CA    1 ? 3 
ATOM   8330  C C     . MET C 1 125 ? 52.935  -9.159  82.299  1.000 46.138  0 125 MET CCC C     1 ? 3 
ATOM   8331  O O     . MET C 1 125 ? 52.144  -8.927  83.233  1.000 46.748  0 125 MET CCC O     1 ? 3 
ATOM   8332  C CB    . MET C 1 125 ? 55.446  -9.276  82.766  1.000 53.211  0 125 MET CCC CB    1 ? 3 
ATOM   8333  C CG    . MET C 1 125 ? 55.464  -8.323  83.962  1.000 55.352  0 125 MET CCC CG    1 ? 3 
ATOM   8334  S SD    . MET C 1 125 ? 54.673  -6.715  83.631  1.000 69.772  0 125 MET CCC SD    1 ? 3 
ATOM   8335  C CE    . MET C 1 125 ? 55.567  -6.104  82.197  1.000 65.031  0 125 MET CCC CE    1 ? 3 
ATOM   8336  N N     . LEU C 1 126 ? 52.766  -8.684  81.052  1.000 44.134  0 126 LEU CCC N     1 ? 3 
ATOM   8337  C CA    . LEU C 1 126 ? 51.669  -7.762  80.614  1.000 40.710  0 126 LEU CCC CA    1 ? 3 
ATOM   8338  C C     . LEU C 1 126 ? 50.332  -8.514  80.592  1.000 37.471  0 126 LEU CCC C     1 ? 3 
ATOM   8339  O O     . LEU C 1 126 ? 49.335  -7.946  80.996  1.000 35.728  0 126 LEU CCC O     1 ? 3 
ATOM   8340  C CB    . LEU C 1 126 ? 51.973  -7.173  79.229  1.000 39.728  0 126 LEU CCC CB    1 ? 3 
ATOM   8341  C CG    . LEU C 1 126 ? 53.027  -6.064  79.144  1.000 38.742  0 126 LEU CCC CG    1 ? 3 
ATOM   8342  C CD1   . LEU C 1 126 ? 53.365  -5.776  77.699  1.000 39.007  0 126 LEU CCC CD1   1 ? 3 
ATOM   8343  C CD2   . LEU C 1 126 ? 52.569  -4.786  79.789  1.000 38.522  0 126 LEU CCC CD2   1 ? 3 
ATOM   8344  N N     . ASN C 1 127 ? 50.302  -9.755  80.141  1.000 36.973  0 127 ASN CCC N     1 ? 3 
ATOM   8345  C CA    . ASN C 1 127 ? 49.067  -10.578 80.235  1.000 37.365  0 127 ASN CCC CA    1 ? 3 
ATOM   8346  C C     . ASN C 1 127 ? 48.601  -10.545 81.688  1.000 38.834  0 127 ASN CCC C     1 ? 3 
ATOM   8347  O O     . ASN C 1 127 ? 47.445  -10.233 81.921  1.000 40.443  0 127 ASN CCC O     1 ? 3 
ATOM   8348  C CB    . ASN C 1 127 ? 49.246  -12.032 79.764  1.000 37.111  0 127 ASN CCC CB    1 ? 3 
ATOM   8349  C CG    . ASN C 1 127 ? 49.696  -12.187 78.326  1.000 35.721  0 127 ASN CCC CG    1 ? 3 
ATOM   8350  O OD1   . ASN C 1 127 ? 50.496  -13.061 78.032  1.000 35.198  0 127 ASN CCC OD1   1 ? 3 
ATOM   8351  N ND2   . ASN C 1 127 ? 49.204  -11.341 77.432  1.000 34.754  0 127 ASN CCC ND2   1 ? 3 
ATOM   8352  N N     . PHE C 1 128 ? 49.479  -10.866 82.634  1.000 39.043  0 128 PHE CCC N     1 ? 3 
ATOM   8353  C CA    . PHE C 1 128 ? 49.142  -10.980 84.084  1.000 40.296  0 128 PHE CCC CA    1 ? 3 
ATOM   8354  C C     . PHE C 1 128 ? 48.713  -9.606  84.611  1.000 40.358  0 128 PHE CCC C     1 ? 3 
ATOM   8355  O O     . PHE C 1 128 ? 47.634  -9.492  85.223  1.000 40.505  0 128 PHE CCC O     1 ? 3 
ATOM   8356  C CB    . PHE C 1 128 ? 50.310  -11.585 84.868  1.000 37.951  0 128 PHE CCC CB    1 ? 3 
ATOM   8357  C CG    . PHE C 1 128 ? 50.277  -13.088 84.863  1.000 38.033  0 128 PHE CCC CG    1 ? 3 
ATOM   8358  C CD1   . PHE C 1 128 ? 49.259  -13.751 85.532  1.000 37.730  0 128 PHE CCC CD1   1 ? 3 
ATOM   8359  C CD2   . PHE C 1 128 ? 51.197  -13.837 84.143  1.000 37.661  0 128 PHE CCC CD2   1 ? 3 
ATOM   8360  C CE1   . PHE C 1 128 ? 49.205  -15.141 85.529  1.000 38.564  0 128 PHE CCC CE1   1 ? 3 
ATOM   8361  C CE2   . PHE C 1 128 ? 51.122  -15.219 84.115  1.000 38.561  0 128 PHE CCC CE2   1 ? 3 
ATOM   8362  C CZ    . PHE C 1 128 ? 50.120  -15.870 84.805  1.000 38.895  0 128 PHE CCC CZ    1 ? 3 
ATOM   8363  N N     . SER C 1 129 ? 49.501  -8.588  84.309  1.000 38.465  0 129 SER CCC N     1 ? 3 
ATOM   8364  C CA    . SER C 1 129 ? 49.233  -7.192  84.690  1.000 40.359  0 129 SER CCC CA    1 ? 3 
ATOM   8365  C C     . SER C 1 129 ? 47.802  -6.791  84.253  1.000 41.788  0 129 SER CCC C     1 ? 3 
ATOM   8366  O O     . SER C 1 129 ? 47.093  -6.135  85.031  1.000 38.516  0 129 SER CCC O     1 ? 3 
ATOM   8367  C CB    . SER C 1 129 ? 50.317  -6.323  84.102  1.000 43.446  0 129 SER CCC CB    1 ? 3 
ATOM   8368  O OG    . SER C 1 129 ? 49.994  -4.933  84.182  1.000 46.814  0 129 SER CCC OG    1 ? 3 
ATOM   8369  N N     . TYR C 1 130 ? 47.352  -7.176  83.058  1.000 41.906  0 130 TYR CCC N     1 ? 3 
ATOM   8370  C CA    . TYR C 1 130 ? 46.013  -6.788  82.542  1.000 44.740  0 130 TYR CCC CA    1 ? 3 
ATOM   8371  C C     . TYR C 1 130 ? 44.916  -7.612  83.238  1.000 45.290  0 130 TYR CCC C     1 ? 3 
ATOM   8372  O O     . TYR C 1 130 ? 43.886  -7.026  83.562  1.000 45.038  0 130 TYR CCC O     1 ? 3 
ATOM   8373  C CB    . TYR C 1 130 ? 45.977  -6.836  81.009  1.000 45.185  0 130 TYR CCC CB    1 ? 3 
ATOM   8374  C CG    . TYR C 1 130 ? 46.654  -5.644  80.362  1.000 46.568  0 130 TYR CCC CG    1 ? 3 
ATOM   8375  C CD1   . TYR C 1 130 ? 46.218  -4.355  80.635  1.000 49.623  0 130 TYR CCC CD1   1 ? 3 
ATOM   8376  C CD2   . TYR C 1 130 ? 47.736  -5.783  79.499  1.000 47.545  0 130 TYR CCC CD2   1 ? 3 
ATOM   8377  C CE1   . TYR C 1 130 ? 46.808  -3.247  80.046  1.000 49.573  0 130 TYR CCC CE1   1 ? 3 
ATOM   8378  C CE2   . TYR C 1 130 ? 48.353  -4.689  78.907  1.000 46.515  0 130 TYR CCC CE2   1 ? 3 
ATOM   8379  C CZ    . TYR C 1 130 ? 47.874  -3.415  79.175  1.000 48.866  0 130 TYR CCC CZ    1 ? 3 
ATOM   8380  O OH    . TYR C 1 130 ? 48.414  -2.270  78.668  1.000 47.413  0 130 TYR CCC OH    1 ? 3 
ATOM   8381  N N     . ARG C 1 131 ? 45.113  -8.913  83.461  1.000 46.028  0 131 ARG CCC N     1 ? 3 
ATOM   8382  C CA    . ARG C 1 131 ? 44.146  -9.742  84.232  1.000 47.419  0 131 ARG CCC CA    1 ? 3 
ATOM   8383  C C     . ARG C 1 131 ? 43.879  -9.068  85.571  1.000 46.820  0 131 ARG CCC C     1 ? 3 
ATOM   8384  O O     . ARG C 1 131 ? 42.708  -8.913  85.909  1.000 49.386  0 131 ARG CCC O     1 ? 3 
ATOM   8385  C CB    . ARG C 1 131 ? 44.657  -11.153 84.529  1.000 52.800  0 131 ARG CCC CB    1 ? 3 
ATOM   8386  C CG    . ARG C 1 131 ? 44.162  -12.228 83.579  1.000 56.560  0 131 ARG CCC CG    1 ? 3 
ATOM   8387  C CD    . ARG C 1 131 ? 45.075  -13.439 83.631  1.000 60.852  0 131 ARG CCC CD    1 ? 3 
ATOM   8388  N NE    . ARG C 1 131 ? 44.937  -14.147 84.899  1.000 63.388  0 131 ARG CCC NE    1 ? 3 
ATOM   8389  C CZ    . ARG C 1 131 ? 45.423  -15.362 85.139  1.000 64.637  0 131 ARG CCC CZ    1 ? 3 
ATOM   8390  N NH1   . ARG C 1 131 ? 46.089  -16.012 84.198  1.000 66.788  0 131 ARG CCC NH1   1 ? 3 
ATOM   8391  N NH2   . ARG C 1 131 ? 45.220  -15.938 86.312  1.000 64.046  0 131 ARG CCC NH2   1 ? 3 
ATOM   8392  N N     . THR C 1 132 ? 44.934  -8.703  86.292  1.000 46.771  0 132 THR CCC N     1 ? 3 
ATOM   8393  C CA    . THR C 1 132 ? 44.884  -8.067  87.634  1.000 48.748  0 132 THR CCC CA    1 ? 3 
ATOM   8394  C C     . THR C 1 132 ? 44.181  -6.718  87.508  1.000 49.088  0 132 THR CCC C     1 ? 3 
ATOM   8395  O O     . THR C 1 132 ? 43.311  -6.433  88.367  1.000 53.204  0 132 THR CCC O     1 ? 3 
ATOM   8396  C CB    . THR C 1 132 ? 46.295  -7.950  88.242  1.000 50.367  0 132 THR CCC CB    1 ? 3 
ATOM   8397  O OG1   . THR C 1 132 ? 46.774  -9.276  88.455  1.000 49.825  0 132 THR CCC OG1   1 ? 3 
ATOM   8398  C CG2   . THR C 1 132 ? 46.356  -7.189  89.546  1.000 50.418  0 132 THR CCC CG2   1 ? 3 
ATOM   8399  N N     . GLY C 1 133 ? 44.553  -5.917  86.504  1.000 45.624  0 133 GLY CCC N     1 ? 3 
ATOM   8400  C CA    . GLY C 1 133 ? 44.043  -4.550  86.288  1.000 46.330  0 133 GLY CCC CA    1 ? 3 
ATOM   8401  C C     . GLY C 1 133 ? 42.535  -4.570  86.134  1.000 49.525  0 133 GLY CCC C     1 ? 3 
ATOM   8402  O O     . GLY C 1 133 ? 41.871  -3.627  86.638  1.000 50.094  0 133 GLY CCC O     1 ? 3 
ATOM   8403  N N     . LEU C 1 134 ? 42.012  -5.619  85.490  1.000 48.989  0 134 LEU CCC N     1 ? 3 
ATOM   8404  C CA    . LEU C 1 134 ? 40.557  -5.844  85.295  1.000 49.853  0 134 LEU CCC CA    1 ? 3 
ATOM   8405  C C     . LEU C 1 134 ? 39.933  -6.242  86.639  1.000 50.396  0 134 LEU CCC C     1 ? 3 
ATOM   8406  O O     . LEU C 1 134 ? 38.968  -5.603  87.041  1.000 45.090  0 134 LEU CCC O     1 ? 3 
ATOM   8407  C CB    . LEU C 1 134 ? 40.339  -6.916  84.223  1.000 48.690  0 134 LEU CCC CB    1 ? 3 
ATOM   8408  C CG    . LEU C 1 134 ? 40.537  -6.454  82.774  1.000 50.515  0 134 LEU CCC CG    1 ? 3 
ATOM   8409  C CD1   . LEU C 1 134 ? 40.162  -7.537  81.783  1.000 50.271  0 134 LEU CCC CD1   1 ? 3 
ATOM   8410  C CD2   . LEU C 1 134 ? 39.736  -5.204  82.453  1.000 51.839  0 134 LEU CCC CD2   1 ? 3 
ATOM   8411  N N     . ARG C 1 135 ? 40.478  -7.252  87.316  1.000 53.420  0 135 ARG CCC N     1 ? 3 
ATOM   8412  C CA    . ARG C 1 135 ? 39.930  -7.761  88.603  1.000 57.061  0 135 ARG CCC CA    1 ? 3 
ATOM   8413  C C     . ARG C 1 135 ? 39.918  -6.617  89.631  1.000 57.798  0 135 ARG CCC C     1 ? 3 
ATOM   8414  O O     . ARG C 1 135 ? 38.841  -6.340  90.174  1.000 62.873  0 135 ARG CCC O     1 ? 3 
ATOM   8415  C CB    . ARG C 1 135 ? 40.718  -8.995  89.056  1.000 60.308  0 135 ARG CCC CB    1 ? 3 
ATOM   8416  C CG    . ARG C 1 135 ? 39.994  -9.891  90.053  1.000 64.296  0 135 ARG CCC CG    1 ? 3 
ATOM   8417  C CD    . ARG C 1 135 ? 40.777  -11.132 90.452  1.000 66.141  0 135 ARG CCC CD    1 ? 3 
ATOM   8418  N NE    . ARG C 1 135 ? 42.116  -10.819 90.960  1.000 69.879  0 135 ARG CCC NE    1 ? 3 
ATOM   8419  C CZ    . ARG C 1 135 ? 43.261  -10.951 90.266  1.000 70.217  0 135 ARG CCC CZ    1 ? 3 
ATOM   8420  N NH1   . ARG C 1 135 ? 43.249  -11.418 89.024  1.000 68.005  0 135 ARG CCC NH1   1 ? 3 
ATOM   8421  N NH2   . ARG C 1 135 ? 44.418  -10.616 90.822  1.000 65.364  0 135 ARG CCC NH2   1 ? 3 
ATOM   8422  N N     . VAL C 1 136 ? 41.055  -5.948  89.847  1.000 58.306  0 136 VAL CCC N     1 ? 3 
ATOM   8423  C CA    . VAL C 1 136 ? 41.204  -4.783  90.774  1.000 57.078  0 136 VAL CCC CA    1 ? 3 
ATOM   8424  C C     . VAL C 1 136 ? 40.221  -3.700  90.330  1.000 55.032  0 136 VAL CCC C     1 ? 3 
ATOM   8425  O O     . VAL C 1 136 ? 39.577  -3.111  91.214  1.000 54.179  0 136 VAL CCC O     1 ? 3 
ATOM   8426  C CB    . VAL C 1 136 ? 42.664  -4.267  90.811  1.000 59.996  0 136 VAL CCC CB    1 ? 3 
ATOM   8427  C CG1   . VAL C 1 136 ? 42.797  -2.831  91.308  1.000 58.465  0 136 VAL CCC CG1   1 ? 3 
ATOM   8428  C CG2   . VAL C 1 136 ? 43.552  -5.190  91.635  1.000 61.439  0 136 VAL CCC CG2   1 ? 3 
ATOM   8429  N N     . GLY C 1 137 ? 40.086  -3.470  89.015  1.000 54.707  0 137 GLY CCC N     1 ? 3 
ATOM   8430  C CA    . GLY C 1 137 ? 39.249  -2.394  88.438  1.000 53.238  0 137 GLY CCC CA    1 ? 3 
ATOM   8431  C C     . GLY C 1 137 ? 37.775  -2.756  88.394  1.000 51.093  0 137 GLY CCC C     1 ? 3 
ATOM   8432  O O     . GLY C 1 137 ? 37.009  -1.975  87.804  1.000 56.103  0 137 GLY CCC O     1 ? 3 
ATOM   8433  N N     . ASN C 1 138 ? 37.401  -3.908  88.962  1.000 48.284  0 138 ASN CCC N     1 ? 3 
ATOM   8434  C CA    . ASN C 1 138 ? 36.008  -4.351  89.198  1.000 48.036  0 138 ASN CCC CA    1 ? 3 
ATOM   8435  C C     . ASN C 1 138 ? 35.330  -4.658  87.856  1.000 44.357  0 138 ASN CCC C     1 ? 3 
ATOM   8436  O O     . ASN C 1 138 ? 34.153  -4.372  87.688  1.000 41.902  0 138 ASN CCC O     1 ? 3 
ATOM   8437  C CB    . ASN C 1 138 ? 35.249  -3.340  90.065  1.000 49.930  0 138 ASN CCC CB    1 ? 3 
ATOM   8438  C CG    . ASN C 1 138 ? 33.897  -3.862  90.504  1.000 50.508  0 138 ASN CCC CG    1 ? 3 
ATOM   8439  O OD1   . ASN C 1 138 ? 33.786  -5.034  90.858  1.000 50.001  0 138 ASN CCC OD1   1 ? 3 
ATOM   8440  N ND2   . ASN C 1 138 ? 32.877  -3.016  90.446  1.000 49.583  0 138 ASN CCC ND2   1 ? 3 
ATOM   8441  N N     . VAL C 1 139 ? 36.073  -5.273  86.947  1.000 42.959  0 139 VAL CCC N     1 ? 3 
ATOM   8442  C CA    . VAL C 1 139 ? 35.577  -5.807  85.651  1.000 43.013  0 139 VAL CCC CA    1 ? 3 
ATOM   8443  C C     . VAL C 1 139 ? 35.587  -7.330  85.762  1.000 43.579  0 139 VAL CCC C     1 ? 3 
ATOM   8444  O O     . VAL C 1 139 ? 36.603  -7.878  86.196  1.000 41.263  0 139 VAL CCC O     1 ? 3 
ATOM   8445  C CB    . VAL C 1 139 ? 36.447  -5.323  84.471  1.000 42.436  0 139 VAL CCC CB    1 ? 3 
ATOM   8446  C CG1   . VAL C 1 139 ? 35.957  -5.896  83.143  1.000 42.827  0 139 VAL CCC CG1   1 ? 3 
ATOM   8447  C CG2   . VAL C 1 139 ? 36.520  -3.798  84.390  1.000 42.804  0 139 VAL CCC CG2   1 ? 3 
ATOM   8448  N N     . GLU C 1 140 ? 34.490  -7.979  85.376  1.000 45.006  0 140 GLU CCC N     1 ? 3 
ATOM   8449  C CA    . GLU C 1 140 ? 34.400  -9.457  85.226  1.000 45.373  0 140 GLU CCC CA    1 ? 3 
ATOM   8450  C C     . GLU C 1 140 ? 34.970  -9.865  83.862  1.000 41.574  0 140 GLU CCC C     1 ? 3 
ATOM   8451  O O     . GLU C 1 140 ? 34.292  -9.694  82.866  1.000 38.069  0 140 GLU CCC O     1 ? 3 
ATOM   8452  C CB    . GLU C 1 140 ? 32.965  -9.959  85.408  1.000 46.971  0 140 GLU CCC CB    1 ? 3 
ATOM   8453  C CG    . GLU C 1 140 ? 32.922  -11.458 85.653  1.000 49.499  0 140 GLU CCC CG    1 ? 3 
ATOM   8454  C CD    . GLU C 1 140 ? 31.571  -12.128 85.500  1.000 53.720  0 140 GLU CCC CD    1 ? 3 
ATOM   8455  O OE1   . GLU C 1 140 ? 30.722  -11.576 84.761  1.000 56.064  0 140 GLU CCC OE1   1 ? 3 
ATOM   8456  O OE2   . GLU C 1 140 ? 31.386  -13.218 86.101  1.000 56.230  0 140 GLU CCC OE2   1 ? 3 
ATOM   8457  N N     . TYR C 1 141 ? 36.186  -10.406 83.863  1.000 40.739  0 141 TYR CCC N     1 ? 3 
ATOM   8458  C CA    . TYR C 1 141 ? 36.880  -11.009 82.708  1.000 40.784  0 141 TYR CCC CA    1 ? 3 
ATOM   8459  C C     . TYR C 1 141 ? 36.416  -12.461 82.528  1.000 40.483  0 141 TYR CCC C     1 ? 3 
ATOM   8460  O O     . TYR C 1 141 ? 36.513  -13.224 83.452  1.000 39.915  0 141 TYR CCC O     1 ? 3 
ATOM   8461  C CB    . TYR C 1 141 ? 38.395  -10.937 82.929  1.000 41.214  0 141 TYR CCC CB    1 ? 3 
ATOM   8462  C CG    . TYR C 1 141 ? 39.211  -11.735 81.939  1.000 41.341  0 141 TYR CCC CG    1 ? 3 
ATOM   8463  C CD1   . TYR C 1 141 ? 38.962  -11.658 80.580  1.000 40.957  0 141 TYR CCC CD1   1 ? 3 
ATOM   8464  C CD2   . TYR C 1 141 ? 40.251  -12.549 82.361  1.000 42.612  0 141 TYR CCC CD2   1 ? 3 
ATOM   8465  C CE1   . TYR C 1 141 ? 39.710  -12.377 79.662  1.000 41.795  0 141 TYR CCC CE1   1 ? 3 
ATOM   8466  C CE2   . TYR C 1 141 ? 41.017  -13.270 81.451  1.000 43.338  0 141 TYR CCC CE2   1 ? 3 
ATOM   8467  C CZ    . TYR C 1 141 ? 40.723  -13.206 80.097  1.000 41.764  0 141 TYR CCC CZ    1 ? 3 
ATOM   8468  O OH    . TYR C 1 141 ? 41.444  -13.905 79.190  1.000 39.944  0 141 TYR CCC OH    1 ? 3 
ATOM   8469  N N     . ILE C 1 142 ? 35.999  -12.833 81.326  1.000 42.638  0 142 ILE CCC N     1 ? 3 
ATOM   8470  C CA    . ILE C 1 142 ? 35.615  -14.229 80.945  1.000 43.141  0 142 ILE CCC CA    1 ? 3 
ATOM   8471  C C     . ILE C 1 142 ? 36.410  -14.618 79.694  1.000 42.015  0 142 ILE CCC C     1 ? 3 
ATOM   8472  O O     . ILE C 1 142 ? 36.217  -13.945 78.647  1.000 42.453  0 142 ILE CCC O     1 ? 3 
ATOM   8473  C CB    . ILE C 1 142 ? 34.097  -14.315 80.688  1.000 43.829  0 142 ILE CCC CB    1 ? 3 
ATOM   8474  C CG1   . ILE C 1 142 ? 33.297  -13.894 81.929  1.000 45.577  0 142 ILE CCC CG1   1 ? 3 
ATOM   8475  C CG2   . ILE C 1 142 ? 33.698  -15.693 80.168  1.000 42.913  0 142 ILE CCC CG2   1 ? 3 
ATOM   8476  C CD1   . ILE C 1 142 ? 31.824  -13.670 81.636  1.000 45.514  0 142 ILE CCC CD1   1 ? 3 
ATOM   8477  N N     . ASN C 1 143 ? 37.248  -15.652 79.806  1.000 39.320  0 143 ASN CCC N     1 ? 3 
ATOM   8478  C CA    . ASN C 1 143 ? 38.095  -16.184 78.712  1.000 38.817  0 143 ASN CCC CA    1 ? 3 
ATOM   8479  C C     . ASN C 1 143 ? 37.247  -17.128 77.862  1.000 39.109  0 143 ASN CCC C     1 ? 3 
ATOM   8480  O O     . ASN C 1 143 ? 37.456  -18.336 77.940  1.000 40.756  0 143 ASN CCC O     1 ? 3 
ATOM   8481  C CB    . ASN C 1 143 ? 39.373  -16.837 79.276  1.000 38.418  0 143 ASN CCC CB    1 ? 3 
ATOM   8482  C CG    . ASN C 1 143 ? 40.443  -17.192 78.253  1.000 38.721  0 143 ASN CCC CG    1 ? 3 
ATOM   8483  O OD1   . ASN C 1 143 ? 40.497  -16.660 77.128  1.000 39.192  0 143 ASN CCC OD1   1 ? 3 
ATOM   8484  N ND2   . ASN C 1 143 ? 41.327  -18.086 78.660  1.000 38.597  0 143 ASN CCC ND2   1 ? 3 
ATOM   8485  N N     . ALA C 1 144 ? 36.313  -16.594 77.077  1.000 40.217  0 144 ALA CCC N     1 ? 3 
ATOM   8486  C CA    . ALA C 1 144 ? 35.480  -17.353 76.094  1.000 39.114  0 144 ALA CCC CA    1 ? 3 
ATOM   8487  C C     . ALA C 1 144 ? 35.112  -16.488 74.886  1.000 36.862  0 144 ALA CCC C     1 ? 3 
ATOM   8488  O O     . ALA C 1 144 ? 35.082  -15.257 75.019  1.000 35.925  0 144 ALA CCC O     1 ? 3 
ATOM   8489  C CB    . ALA C 1 144 ? 34.243  -17.907 76.759  1.000 37.716  0 144 ALA CCC CB    1 ? 3 
ATOM   8490  N N     . LEU C 1 145 ? 34.807  -17.132 73.763  1.000 38.880  0 145 LEU CCC N     1 ? 3 
ATOM   8491  C CA    . LEU C 1 145 ? 34.196  -16.479 72.573  1.000 41.940  0 145 LEU CCC CA    1 ? 3 
ATOM   8492  C C     . LEU C 1 145 ? 32.747  -16.115 72.862  1.000 44.941  0 145 LEU CCC C     1 ? 3 
ATOM   8493  O O     . LEU C 1 145 ? 31.996  -17.008 73.297  1.000 47.626  0 145 LEU CCC O     1 ? 3 
ATOM   8494  C CB    . LEU C 1 145 ? 34.277  -17.389 71.347  1.000 43.255  0 145 LEU CCC CB    1 ? 3 
ATOM   8495  C CG    . LEU C 1 145 ? 35.673  -17.509 70.728  1.000 44.543  0 145 LEU CCC CG    1 ? 3 
ATOM   8496  C CD1   . LEU C 1 145 ? 35.688  -18.540 69.595  1.000 44.310  0 145 LEU CCC CD1   1 ? 3 
ATOM   8497  C CD2   . LEU C 1 145 ? 36.171  -16.134 70.231  1.000 44.113  0 145 LEU CCC CD2   1 ? 3 
ATOM   8498  N N     . ALA C 1 146 ? 32.383  -14.855 72.609  1.000 46.717  0 146 ALA CCC N     1 ? 3 
ATOM   8499  C CA    . ALA C 1 146 ? 31.027  -14.303 72.800  1.000 48.327  0 146 ALA CCC CA    1 ? 3 
ATOM   8500  C C     . ALA C 1 146 ? 30.379  -14.080 71.436  1.000 47.052  0 146 ALA CCC C     1 ? 3 
ATOM   8501  O O     . ALA C 1 146 ? 31.114  -13.834 70.496  1.000 43.759  0 146 ALA CCC O     1 ? 3 
ATOM   8502  C CB    . ALA C 1 146 ? 31.124  -13.014 73.573  1.000 50.157  0 146 ALA CCC CB    1 ? 3 
ATOM   8503  N N     . LYS C 1 147 ? 29.056  -14.197 71.346  1.000 51.534  0 147 LYS CCC N     1 ? 3 
ATOM   8504  C CA    . LYS C 1 147 ? 28.271  -13.768 70.150  1.000 53.236  0 147 LYS CCC CA    1 ? 3 
ATOM   8505  C C     . LYS C 1 147 ? 27.000  -13.010 70.590  1.000 49.078  0 147 LYS CCC C     1 ? 3 
ATOM   8506  O O     . LYS C 1 147 ? 26.557  -13.166 71.749  1.000 45.714  0 147 LYS CCC O     1 ? 3 
ATOM   8507  C CB    . LYS C 1 147 ? 27.995  -14.958 69.225  1.000 54.053  0 147 LYS CCC CB    1 ? 3 
ATOM   8508  C CG    . LYS C 1 147 ? 27.093  -16.040 69.795  1.000 57.823  0 147 LYS CCC CG    1 ? 3 
ATOM   8509  C CD    . LYS C 1 147 ? 26.659  -17.069 68.762  1.000 59.532  0 147 LYS CCC CD    1 ? 3 
ATOM   8510  C CE    . LYS C 1 147 ? 27.578  -18.277 68.668  1.000 60.683  0 147 LYS CCC CE    1 ? 3 
ATOM   8511  N NZ    . LYS C 1 147 ? 27.593  -18.869 67.304  1.000 62.383  0 147 LYS CCC NZ    1 ? 3 
ATOM   8512  N N     . LEU C 1 148 ? 26.455  -12.184 69.702  1.000 46.621  0 148 LEU CCC N     1 ? 3 
ATOM   8513  C CA    . LEU C 1 148 ? 25.185  -11.457 69.943  1.000 50.661  0 148 LEU CCC CA    1 ? 3 
ATOM   8514  C C     . LEU C 1 148 ? 23.999  -12.415 69.758  1.000 48.096  0 148 LEU CCC C     1 ? 3 
ATOM   8515  O O     . LEU C 1 148 ? 24.019  -13.216 68.811  1.000 43.748  0 148 LEU CCC O     1 ? 3 
ATOM   8516  C CB    . LEU C 1 148 ? 25.097  -10.267 68.983  1.000 50.415  0 148 LEU CCC CB    1 ? 3 
ATOM   8517  C CG    . LEU C 1 148 ? 26.173  -9.204  69.142  1.000 49.136  0 148 LEU CCC CG    1 ? 3 
ATOM   8518  C CD1   . LEU C 1 148 ? 26.083  -8.187  68.005  1.000 48.294  0 148 LEU CCC CD1   1 ? 3 
ATOM   8519  C CD2   . LEU C 1 148 ? 26.053  -8.523  70.501  1.000 47.378  0 148 LEU CCC CD2   1 ? 3 
ATOM   8520  N N     . ILE C 1 149 ? 23.044  -12.362 70.682  1.000 51.117  0 149 ILE CCC N     1 ? 3 
ATOM   8521  C CA    . ILE C 1 149 ? 21.746  -13.093 70.583  1.000 55.264  0 149 ILE CCC CA    1 ? 3 
ATOM   8522  C C     . ILE C 1 149 ? 20.689  -12.078 70.151  1.000 57.438  0 149 ILE CCC C     1 ? 3 
ATOM   8523  O O     . ILE C 1 149 ? 19.924  -12.409 69.242  1.000 60.266  0 149 ILE CCC O     1 ? 3 
ATOM   8524  C CB    . ILE C 1 149 ? 21.407  -13.815 71.901  1.000 59.683  0 149 ILE CCC CB    1 ? 3 
ATOM   8525  C CG1   . ILE C 1 149 ? 22.316  -15.032 72.114  1.000 60.813  0 149 ILE CCC CG1   1 ? 3 
ATOM   8526  C CG2   . ILE C 1 149 ? 19.928  -14.197 71.975  1.000 61.448  0 149 ILE CCC CG2   1 ? 3 
ATOM   8527  C CD1   . ILE C 1 149 ? 22.192  -16.102 71.038  1.000 62.461  0 149 ILE CCC CD1   1 ? 3 
ATOM   8528  N N     . ASP C 1 150 ? 20.693  -10.882 70.754  1.000 58.225  0 150 ASP CCC N     1 ? 3 
ATOM   8529  C CA    . ASP C 1 150 ? 19.773  -9.760  70.431  1.000 56.100  0 150 ASP CCC CA    1 ? 3 
ATOM   8530  C C     . ASP C 1 150 ? 20.389  -8.452  70.946  1.000 49.563  0 150 ASP CCC C     1 ? 3 
ATOM   8531  O O     . ASP C 1 150 ? 21.440  -8.447  71.564  1.000 43.191  0 150 ASP CCC O     1 ? 3 
ATOM   8532  C CB    . ASP C 1 150 ? 18.371  -10.092 70.959  1.000 57.666  0 150 ASP CCC CB    1 ? 3 
ATOM   8533  C CG    . ASP C 1 150 ? 18.215  -10.065 72.479  1.000 64.947  0 150 ASP CCC CG    1 ? 3 
ATOM   8534  O OD1   . ASP C 1 150 ? 18.855  -9.214  73.133  1.000 72.114  0 150 ASP CCC OD1   1 ? 3 
ATOM   8535  O OD2   . ASP C 1 150 ? 17.424  -10.878 73.000  1.000 63.863  0 150 ASP CCC OD2   1 ? 3 
ATOM   8536  N N     . PRO C 1 151 ? 19.755  -7.284  70.712  1.000 48.976  0 151 PRO CCC N     1 ? 3 
ATOM   8537  C CA    . PRO C 1 151 ? 20.347  -6.007  71.104  1.000 47.071  0 151 PRO CCC CA    1 ? 3 
ATOM   8538  C C     . PRO C 1 151 ? 20.812  -5.873  72.566  1.000 49.102  0 151 PRO CCC C     1 ? 3 
ATOM   8539  O O     . PRO C 1 151 ? 21.467  -4.886  72.856  1.000 47.164  0 151 PRO CCC O     1 ? 3 
ATOM   8540  C CB    . PRO C 1 151 ? 19.202  -4.993  70.860  1.000 47.038  0 151 PRO CCC CB    1 ? 3 
ATOM   8541  C CG    . PRO C 1 151 ? 18.327  -5.626  69.806  1.000 46.126  0 151 PRO CCC CG    1 ? 3 
ATOM   8542  C CD    . PRO C 1 151 ? 18.442  -7.118  70.045  1.000 47.936  0 151 PRO CCC CD    1 ? 3 
ATOM   8543  N N     . HIS C 1 152 ? 20.430  -6.793  73.465  1.000 49.734  0 152 HIS CCC N     1 ? 3 
ATOM   8544  C CA    . HIS C 1 152 ? 20.769  -6.711  74.917  1.000 47.584  0 152 HIS CCC CA    1 ? 3 
ATOM   8545  C C     . HIS C 1 152 ? 21.308  -8.032  75.476  1.000 45.475  0 152 HIS CCC C     1 ? 3 
ATOM   8546  O O     . HIS C 1 152 ? 21.448  -8.098  76.689  1.000 44.964  0 152 HIS CCC O     1 ? 3 
ATOM   8547  C CB    . HIS C 1 152 ? 19.551  -6.271  75.734  1.000 50.301  0 152 HIS CCC CB    1 ? 3 
ATOM   8548  C CG    . HIS C 1 152 ? 19.110  -4.878  75.442  1.000 50.376  0 152 HIS CCC CG    1 ? 3 
ATOM   8549  N ND1   . HIS C 1 152 ? 19.849  -3.785  75.852  1.000 48.163  0 152 HIS CCC ND1   1 ? 3 
ATOM   8550  C CD2   . HIS C 1 152 ? 18.042  -4.399  74.760  1.000 49.962  0 152 HIS CCC CD2   1 ? 3 
ATOM   8551  C CE1   . HIS C 1 152 ? 19.237  -2.687  75.462  1.000 48.083  0 152 HIS CCC CE1   1 ? 3 
ATOM   8552  N NE2   . HIS C 1 152 ? 18.129  -3.038  74.795  1.000 49.375  0 152 HIS CCC NE2   1 ? 3 
ATOM   8553  N N     . SER C 1 153 ? 21.641  -9.028  74.650  1.000 46.568  0 153 SER CCC N     1 ? 3 
ATOM   8554  C CA    . SER C 1 153 ? 22.034  -10.384 75.120  1.000 47.305  0 153 SER CCC CA    1 ? 3 
ATOM   8555  C C     . SER C 1 153 ? 23.239  -10.905 74.340  1.000 47.789  0 153 SER CCC C     1 ? 3 
ATOM   8556  O O     . SER C 1 153 ? 23.270  -10.753 73.088  1.000 45.023  0 153 SER CCC O     1 ? 3 
ATOM   8557  C CB    . SER C 1 153 ? 20.886  -11.333 75.009  1.000 47.327  0 153 SER CCC CB    1 ? 3 
ATOM   8558  O OG    . SER C 1 153 ? 19.724  -10.742 75.564  1.000 51.296  0 153 SER CCC OG    1 ? 3 
ATOM   8559  N N     . VAL C 1 154 ? 24.174  -11.527 75.062  1.000 52.891  0 154 VAL CCC N     1 ? 3 
ATOM   8560  C CA    . VAL C 1 154 ? 25.403  -12.147 74.486  1.000 54.849  0 154 VAL CCC CA    1 ? 3 
ATOM   8561  C C     . VAL C 1 154 ? 25.500  -13.582 75.017  1.000 53.495  0 154 VAL CCC C     1 ? 3 
ATOM   8562  O O     . VAL C 1 154 ? 25.091  -13.800 76.170  1.000 49.825  0 154 VAL CCC O     1 ? 3 
ATOM   8563  C CB    . VAL C 1 154 ? 26.643  -11.301 74.821  1.000 57.164  0 154 VAL CCC CB    1 ? 3 
ATOM   8564  C CG1   . VAL C 1 154 ? 27.017  -11.434 76.269  1.000 60.852  0 154 VAL CCC CG1   1 ? 3 
ATOM   8565  C CG2   . VAL C 1 154 ? 27.839  -11.662 73.967  1.000 60.782  0 154 VAL CCC CG2   1 ? 3 
ATOM   8566  N N     . GLU C 1 155 ? 25.978  -14.512 74.182  1.000 55.292  0 155 GLU CCC N     1 ? 3 
ATOM   8567  C CA    . GLU C 1 155 ? 26.084  -15.965 74.480  1.000 58.628  0 155 GLU CCC CA    1 ? 3 
ATOM   8568  C C     . GLU C 1 155 ? 27.558  -16.383 74.485  1.000 57.685  0 155 GLU CCC C     1 ? 3 
ATOM   8569  O O     . GLU C 1 155 ? 28.285  -15.981 73.559  1.000 53.702  0 155 GLU CCC O     1 ? 3 
ATOM   8570  C CB    . GLU C 1 155 ? 25.343  -16.774 73.418  1.000 63.666  0 155 GLU CCC CB    1 ? 3 
ATOM   8571  C CG    . GLU C 1 155 ? 25.293  -18.277 73.686  1.000 70.835  0 155 GLU CCC CG    1 ? 3 
ATOM   8572  C CD    . GLU C 1 155 ? 24.427  -19.060 72.710  1.000 80.665  0 155 GLU CCC CD    1 ? 3 
ATOM   8573  O OE1   . GLU C 1 155 ? 24.624  -18.878 71.485  1.000 88.361  0 155 GLU CCC OE1   1 ? 3 
ATOM   8574  O OE2   . GLU C 1 155 ? 23.520  -19.813 73.172  1.000 87.053  0 155 GLU CCC OE2   1 ? 3 
ATOM   8575  N N     . TYR C 1 156 ? 27.961  -17.208 75.455  1.000 57.145  0 156 TYR CCC N     1 ? 3 
ATOM   8576  C CA    . TYR C 1 156 ? 29.298  -17.862 75.485  1.000 59.280  0 156 TYR CCC CA    1 ? 3 
ATOM   8577  C C     . TYR C 1 156 ? 29.201  -19.292 76.026  1.000 59.806  0 156 TYR CCC C     1 ? 3 
ATOM   8578  O O     . TYR C 1 156 ? 28.282  -19.587 76.827  1.000 62.667  0 156 TYR CCC O     1 ? 3 
ATOM   8579  C CB    . TYR C 1 156 ? 30.280  -17.032 76.313  1.000 56.335  0 156 TYR CCC CB    1 ? 3 
ATOM   8580  C CG    . TYR C 1 156 ? 29.999  -16.998 77.790  1.000 54.161  0 156 TYR CCC CG    1 ? 3 
ATOM   8581  C CD1   . TYR C 1 156 ? 29.016  -16.177 78.309  1.000 55.089  0 156 TYR CCC CD1   1 ? 3 
ATOM   8582  C CD2   . TYR C 1 156 ? 30.715  -17.787 78.667  1.000 53.928  0 156 TYR CCC CD2   1 ? 3 
ATOM   8583  C CE1   . TYR C 1 156 ? 28.756  -16.131 79.671  1.000 56.651  0 156 TYR CCC CE1   1 ? 3 
ATOM   8584  C CE2   . TYR C 1 156 ? 30.467  -17.772 80.028  1.000 56.720  0 156 TYR CCC CE2   1 ? 3 
ATOM   8585  C CZ    . TYR C 1 156 ? 29.478  -16.942 80.529  1.000 57.294  0 156 TYR CCC CZ    1 ? 3 
ATOM   8586  O OH    . TYR C 1 156 ? 29.243  -16.908 81.864  1.000 60.242  0 156 TYR CCC OH    1 ? 3 
ATOM   8587  N N     . GLU C 1 157 ? 30.140  -20.148 75.603  1.000 59.425  0 157 GLU CCC N     1 ? 3 
ATOM   8588  C CA    . GLU C 1 157 ? 30.295  -21.521 76.140  1.000 61.902  0 157 GLU CCC CA    1 ? 3 
ATOM   8589  C C     . GLU C 1 157 ? 31.164  -21.457 77.397  1.000 65.557  0 157 GLU CCC C     1 ? 3 
ATOM   8590  O O     . GLU C 1 157 ? 32.051  -20.584 77.497  1.000 65.888  0 157 GLU CCC O     1 ? 3 
ATOM   8591  C CB    . GLU C 1 157 ? 30.821  -22.483 75.084  1.000 64.930  0 157 GLU CCC CB    1 ? 3 
ATOM   8592  C CG    . GLU C 1 157 ? 32.318  -22.687 75.086  1.000 68.822  0 157 GLU CCC CG    1 ? 3 
ATOM   8593  C CD    . GLU C 1 157 ? 32.760  -23.974 74.407  1.000 73.752  0 157 GLU CCC CD    1 ? 3 
ATOM   8594  O OE1   . GLU C 1 157 ? 31.898  -24.875 74.201  1.000 77.129  0 157 GLU CCC OE1   1 ? 3 
ATOM   8595  O OE2   . GLU C 1 157 ? 33.966  -24.076 74.086  1.000 73.429  0 157 GLU CCC OE2   1 ? 3 
ATOM   8596  N N     . ASP C 1 158 ? 30.887  -22.361 78.330  1.000 67.359  0 158 ASP CCC N     1 ? 3 
ATOM   8597  C CA    . ASP C 1 158 ? 31.556  -22.487 79.651  1.000 69.258  0 158 ASP CCC CA    1 ? 3 
ATOM   8598  C C     . ASP C 1 158 ? 31.418  -23.942 80.106  1.000 71.485  0 158 ASP CCC C     1 ? 3 
ATOM   8599  O O     . ASP C 1 158 ? 30.312  -24.328 80.494  1.000 76.268  0 158 ASP CCC O     1 ? 3 
ATOM   8600  C CB    . ASP C 1 158 ? 30.952  -21.476 80.617  1.000 68.774  0 158 ASP CCC CB    1 ? 3 
ATOM   8601  C CG    . ASP C 1 158 ? 31.376  -21.651 82.058  1.000 71.215  0 158 ASP CCC CG    1 ? 3 
ATOM   8602  O OD1   . ASP C 1 158 ? 32.588  -21.851 82.301  1.000 68.495  0 158 ASP CCC OD1   1 ? 3 
ATOM   8603  O OD2   . ASP C 1 158 ? 30.474  -21.560 82.919  1.000 75.023  0 158 ASP CCC OD2   1 ? 3 
ATOM   8604  N N     . ASN C 1 159 ? 32.496  -24.723 80.004  1.000 75.373  0 159 ASN CCC N     1 ? 3 
ATOM   8605  C CA    . ASN C 1 159 ? 32.481  -26.207 80.137  1.000 77.114  0 159 ASN CCC CA    1 ? 3 
ATOM   8606  C C     . ASN C 1 159 ? 31.509  -26.782 79.099  1.000 79.445  0 159 ASN CCC C     1 ? 3 
ATOM   8607  O O     . ASN C 1 159 ? 30.696  -27.652 79.466  1.000 76.636  0 159 ASN CCC O     1 ? 3 
ATOM   8608  C CB    . ASN C 1 159 ? 32.143  -26.645 81.568  1.000 80.241  0 159 ASN CCC CB    1 ? 3 
ATOM   8609  C CG    . ASN C 1 159 ? 33.257  -26.335 82.557  1.000 84.471  0 159 ASN CCC CG    1 ? 3 
ATOM   8610  O OD1   . ASN C 1 159 ? 34.204  -27.116 82.714  1.000 84.065  0 159 ASN CCC OD1   1 ? 3 
ATOM   8611  N ND2   . ASN C 1 159 ? 33.162  -25.195 83.231  1.000 81.947  0 159 ASN CCC ND2   1 ? 3 
ATOM   8612  N N     . GLY C 1 160 ? 31.580  -26.295 77.851  1.000 80.217  0 160 GLY CCC N     1 ? 3 
ATOM   8613  C CA    . GLY C 1 160 ? 30.724  -26.747 76.735  1.000 80.659  0 160 GLY CCC CA    1 ? 3 
ATOM   8614  C C     . GLY C 1 160 ? 29.239  -26.601 77.043  1.000 83.272  0 160 GLY CCC C     1 ? 3 
ATOM   8615  O O     . GLY C 1 160 ? 28.451  -27.467 76.612  1.000 83.781  0 160 GLY CCC O     1 ? 3 
ATOM   8616  N N     . GLN C 1 161 ? 28.866  -25.547 77.771  1.000 83.192  0 161 GLN CCC N     1 ? 3 
ATOM   8617  C CA    . GLN C 1 161 ? 27.464  -25.225 78.131  1.000 84.135  0 161 GLN CCC CA    1 ? 3 
ATOM   8618  C C     . GLN C 1 161 ? 27.188  -23.748 77.841  1.000 82.958  0 161 GLN CCC C     1 ? 3 
ATOM   8619  O O     . GLN C 1 161 ? 27.643  -22.879 78.618  1.000 83.290  0 161 GLN CCC O     1 ? 3 
ATOM   8620  C CB    . GLN C 1 161 ? 27.207  -25.563 79.602  1.000 87.961  0 161 GLN CCC CB    1 ? 3 
ATOM   8621  C CG    . GLN C 1 161 ? 27.189  -27.058 79.886  1.000 90.588  0 161 GLN CCC CG    1 ? 3 
ATOM   8622  C CD    . GLN C 1 161 ? 26.185  -27.428 80.948  1.000 91.688  0 161 GLN CCC CD    1 ? 3 
ATOM   8623  O OE1   . GLN C 1 161 ? 25.216  -26.707 81.169  1.000 92.336  0 161 GLN CCC OE1   1 ? 3 
ATOM   8624  N NE2   . GLN C 1 161 ? 26.402  -28.563 81.593  1.000 92.771  0 161 GLN CCC NE2   1 ? 3 
ATOM   8625  N N     . LYS C 1 162 ? 26.464  -23.499 76.752  1.000 82.896  0 162 LYS CCC N     1 ? 3 
ATOM   8626  C CA    . LYS C 1 162 ? 25.939  -22.169 76.356  1.000 81.711  0 162 LYS CCC CA    1 ? 3 
ATOM   8627  C C     . LYS C 1 162 ? 25.386  -21.448 77.585  1.000 80.084  0 162 LYS CCC C     1 ? 3 
ATOM   8628  O O     . LYS C 1 162 ? 24.589  -22.056 78.320  1.000 82.069  0 162 LYS CCC O     1 ? 3 
ATOM   8629  C CB    . LYS C 1 162 ? 24.822  -22.319 75.323  1.000 85.614  0 162 LYS CCC CB    1 ? 3 
ATOM   8630  C CG    . LYS C 1 162 ? 25.248  -22.952 74.004  1.000 91.216  0 162 LYS CCC CG    1 ? 3 
ATOM   8631  C CD    . LYS C 1 162 ? 26.389  -22.228 73.310  1.000 92.544  0 162 LYS CCC CD    1 ? 3 
ATOM   8632  C CE    . LYS C 1 162 ? 26.386  -22.445 71.812  1.000 94.566  0 162 LYS CCC CE    1 ? 3 
ATOM   8633  N NZ    . LYS C 1 162 ? 27.096  -21.344 71.125  1.000 98.581  0 162 LYS CCC NZ    1 ? 3 
ATOM   8634  N N     . LYS C 1 163 ? 25.816  -20.205 77.793  1.000 76.252  0 163 LYS CCC N     1 ? 3 
ATOM   8635  C CA    . LYS C 1 163 ? 25.238  -19.273 78.790  1.000 73.645  0 163 LYS CCC CA    1 ? 3 
ATOM   8636  C C     . LYS C 1 163 ? 24.886  -17.969 78.078  1.000 72.061  0 163 LYS CCC C     1 ? 3 
ATOM   8637  O O     . LYS C 1 163 ? 25.556  -17.635 77.091  1.000 69.404  0 163 LYS CCC O     1 ? 3 
ATOM   8638  C CB    . LYS C 1 163 ? 26.219  -19.027 79.935  1.000 75.086  0 163 LYS CCC CB    1 ? 3 
ATOM   8639  C CG    . LYS C 1 163 ? 26.545  -20.251 80.772  1.000 76.546  0 163 LYS CCC CG    1 ? 3 
ATOM   8640  C CD    . LYS C 1 163 ? 27.018  -19.903 82.161  1.000 77.672  0 163 LYS CCC CD    1 ? 3 
ATOM   8641  C CE    . LYS C 1 163 ? 27.123  -21.112 83.066  1.000 79.296  0 163 LYS CCC CE    1 ? 3 
ATOM   8642  N NZ    . LYS C 1 163 ? 27.415  -20.722 84.463  1.000 77.638  0 163 LYS CCC NZ    1 ? 3 
ATOM   8643  N N     . THR C 1 164 ? 23.860  -17.274 78.565  1.000 68.024  0 164 THR CCC N     1 ? 3 
ATOM   8644  C CA    . THR C 1 164 ? 23.392  -15.973 78.041  1.000 64.795  0 164 THR CCC CA    1 ? 3 
ATOM   8645  C C     . THR C 1 164 ? 23.422  -14.982 79.202  1.000 59.214  0 164 THR CCC C     1 ? 3 
ATOM   8646  O O     . THR C 1 164 ? 23.079  -15.375 80.304  1.000 62.596  0 164 THR CCC O     1 ? 3 
ATOM   8647  C CB    . THR C 1 164 ? 22.030  -16.128 77.348  1.000 66.680  0 164 THR CCC CB    1 ? 3 
ATOM   8648  O OG1   . THR C 1 164 ? 22.229  -16.920 76.176  1.000 67.403  0 164 THR CCC OG1   1 ? 3 
ATOM   8649  C CG2   . THR C 1 164 ? 21.417  -14.821 76.901  1.000 67.340  0 164 THR CCC CG2   1 ? 3 
ATOM   8650  N N     . ILE C 1 165 ? 23.879  -13.763 78.955  1.000 54.460  0 165 ILE CCC N     1 ? 3 
ATOM   8651  C CA    . ILE C 1 165 ? 23.864  -12.654 79.945  1.000 51.666  0 165 ILE CCC CA    1 ? 3 
ATOM   8652  C C     . ILE C 1 165 ? 23.345  -11.387 79.256  1.000 49.387  0 165 ILE CCC C     1 ? 3 
ATOM   8653  O O     . ILE C 1 165 ? 23.519  -11.253 78.008  1.000 50.735  0 165 ILE CCC O     1 ? 3 
ATOM   8654  C CB    . ILE C 1 165 ? 25.265  -12.462 80.566  1.000 53.961  0 165 ILE CCC CB    1 ? 3 
ATOM   8655  C CG1   . ILE C 1 165 ? 26.290  -11.988 79.534  1.000 50.114  0 165 ILE CCC CG1   1 ? 3 
ATOM   8656  C CG2   . ILE C 1 165 ? 25.741  -13.736 81.273  1.000 53.590  0 165 ILE CCC CG2   1 ? 3 
ATOM   8657  C CD1   . ILE C 1 165 ? 27.492  -11.359 80.165  1.000 50.154  0 165 ILE CCC CD1   1 ? 3 
ATOM   8658  N N     . THR C 1 166 ? 22.748  -10.476 80.023  1.000 44.394  0 166 THR CCC N     1 ? 3 
ATOM   8659  C CA    . THR C 1 166 ? 21.967  -9.337  79.471  1.000 42.544  0 166 THR CCC CA    1 ? 3 
ATOM   8660  C C     . THR C 1 166 ? 22.638  -8.039  79.888  1.000 41.662  0 166 THR CCC C     1 ? 3 
ATOM   8661  O O     . THR C 1 166 ? 23.165  -7.999  81.035  1.000 41.921  0 166 THR CCC O     1 ? 3 
ATOM   8662  C CB    . THR C 1 166 ? 20.493  -9.394  79.928  1.000 42.747  0 166 THR CCC CB    1 ? 3 
ATOM   8663  O OG1   . THR C 1 166 ? 20.521  -9.401  81.350  1.000 42.819  0 166 THR CCC OG1   1 ? 3 
ATOM   8664  C CG2   . THR C 1 166 ? 19.752  -10.610 79.413  1.000 42.426  0 166 THR CCC CG2   1 ? 3 
ATOM   8665  N N     . SER C 1 167 ? 22.604  -7.029  79.019  1.000 41.643  0 167 SER CCC N     1 ? 3 
ATOM   8666  C CA    . SER C 1 167 ? 23.267  -5.718  79.249  1.000 42.417  0 167 SER CCC CA    1 ? 3 
ATOM   8667  C C     . SER C 1 167 ? 22.440  -4.553  78.701  1.000 42.872  0 167 SER CCC C     1 ? 3 
ATOM   8668  O O     . SER C 1 167 ? 21.817  -4.717  77.641  1.000 43.896  0 167 SER CCC O     1 ? 3 
ATOM   8669  C CB    . SER C 1 167 ? 24.663  -5.715  78.669  1.000 39.132  0 167 SER CCC CB    1 ? 3 
ATOM   8670  O OG    . SER C 1 167 ? 25.484  -4.848  79.445  1.000 36.804  0 167 SER CCC OG    1 ? 3 
ATOM   8671  N N     . ARG C 1 168 ? 22.449  -3.417  79.409  1.000 44.635  0 168 ARG CCC N     1 ? 3 
ATOM   8672  C CA    . ARG C 1 168 ? 21.879  -2.122  78.933  1.000 47.863  0 168 ARG CCC CA    1 ? 3 
ATOM   8673  C C     . ARG C 1 168 ? 22.596  -1.764  77.611  1.000 42.898  0 168 ARG CCC C     1 ? 3 
ATOM   8674  O O     . ARG C 1 168 ? 21.905  -1.490  76.617  1.000 43.032  0 168 ARG CCC O     1 ? 3 
ATOM   8675  C CB    . ARG C 1 168 ? 21.993  -1.085  80.066  1.000 52.972  0 168 ARG CCC CB    1 ? 3 
ATOM   8676  C CG    . ARG C 1 168 ? 21.383  0.293   79.837  1.000 58.853  0 168 ARG CCC CG    1 ? 3 
ATOM   8677  C CD    . ARG C 1 168 ? 19.999  0.287   79.190  1.000 68.629  0 168 ARG CCC CD    1 ? 3 
ATOM   8678  N NE    . ARG C 1 168 ? 19.660  1.577   78.580  1.000 77.665  0 168 ARG CCC NE    1 ? 3 
ATOM   8679  C CZ    . ARG C 1 168 ? 18.900  1.752   77.490  1.000 83.334  0 168 ARG CCC CZ    1 ? 3 
ATOM   8680  N NH1   . ARG C 1 168 ? 18.376  0.711   76.856  1.000 83.413  0 168 ARG CCC NH1   1 ? 3 
ATOM   8681  N NH2   . ARG C 1 168 ? 18.686  2.979   77.037  1.000 85.950  0 168 ARG CCC NH2   1 ? 3 
ATOM   8682  N N     . TYR C 1 169 ? 23.920  -1.892  77.593  1.000 41.093  0 169 TYR CCC N     1 ? 3 
ATOM   8683  C CA    . TYR C 1 169 ? 24.816  -1.495  76.480  1.000 41.610  0 169 TYR CCC CA    1 ? 3 
ATOM   8684  C C     . TYR C 1 169 ? 25.763  -2.650  76.132  1.000 40.459  0 169 TYR CCC C     1 ? 3 
ATOM   8685  O O     . TYR C 1 169 ? 26.217  -3.371  77.036  1.000 42.371  0 169 TYR CCC O     1 ? 3 
ATOM   8686  C CB    . TYR C 1 169 ? 25.584  -0.215  76.843  1.000 41.722  0 169 TYR CCC CB    1 ? 3 
ATOM   8687  C CG    . TYR C 1 169 ? 24.718  0.995   77.080  1.000 43.784  0 169 TYR CCC CG    1 ? 3 
ATOM   8688  C CD1   . TYR C 1 169 ? 23.878  1.497   76.091  1.000 43.221  0 169 TYR CCC CD1   1 ? 3 
ATOM   8689  C CD2   . TYR C 1 169 ? 24.726  1.637   78.308  1.000 45.893  0 169 TYR CCC CD2   1 ? 3 
ATOM   8690  C CE1   . TYR C 1 169 ? 23.076  2.607   76.316  1.000 44.171  0 169 TYR CCC CE1   1 ? 3 
ATOM   8691  C CE2   . TYR C 1 169 ? 23.917  2.735   78.557  1.000 46.619  0 169 TYR CCC CE2   1 ? 3 
ATOM   8692  C CZ    . TYR C 1 169 ? 23.095  3.221   77.557  1.000 46.370  0 169 TYR CCC CZ    1 ? 3 
ATOM   8693  O OH    . TYR C 1 169 ? 22.351  4.322   77.846  1.000 47.368  0 169 TYR CCC OH    1 ? 3 
ATOM   8694  N N     . ILE C 1 170 ? 26.030  -2.854  74.841  1.000 38.143  0 170 ILE CCC N     1 ? 3 
ATOM   8695  C CA    . ILE C 1 170 ? 27.049  -3.833  74.366  1.000 38.494  0 170 ILE CCC CA    1 ? 3 
ATOM   8696  C C     . ILE C 1 170 ? 28.074  -3.078  73.516  1.000 37.415  0 170 ILE CCC C     1 ? 3 
ATOM   8697  O O     . ILE C 1 170 ? 27.660  -2.224  72.721  1.000 38.231  0 170 ILE CCC O     1 ? 3 
ATOM   8698  C CB    . ILE C 1 170 ? 26.406  -5.018  73.626  1.000 38.645  0 170 ILE CCC CB    1 ? 3 
ATOM   8699  C CG1   . ILE C 1 170 ? 25.482  -5.791  74.572  1.000 39.084  0 170 ILE CCC CG1   1 ? 3 
ATOM   8700  C CG2   . ILE C 1 170 ? 27.479  -5.922  73.022  1.000 38.156  0 170 ILE CCC CG2   1 ? 3 
ATOM   8701  C CD1   . ILE C 1 170 ? 24.639  -6.834  73.896  1.000 38.934  0 170 ILE CCC CD1   1 ? 3 
ATOM   8702  N N     . LEU C 1 171 ? 29.361  -3.318  73.763  1.000 36.148  0 171 LEU CCC N     1 ? 3 
ATOM   8703  C CA    . LEU C 1 171 ? 30.482  -2.695  73.010  1.000 34.749  0 171 LEU CCC CA    1 ? 3 
ATOM   8704  C C     . LEU C 1 171 ? 31.224  -3.809  72.289  1.000 33.612  0 171 LEU CCC C     1 ? 3 
ATOM   8705  O O     . LEU C 1 171 ? 31.691  -4.752  72.966  1.000 33.844  0 171 LEU CCC O     1 ? 3 
ATOM   8706  C CB    . LEU C 1 171 ? 31.437  -1.967  73.958  1.000 35.541  0 171 LEU CCC CB    1 ? 3 
ATOM   8707  C CG    . LEU C 1 171 ? 32.761  -1.525  73.316  1.000 35.161  0 171 LEU CCC CG    1 ? 3 
ATOM   8708  C CD1   . LEU C 1 171 ? 32.471  -0.591  72.148  1.000 35.613  0 171 LEU CCC CD1   1 ? 3 
ATOM   8709  C CD2   . LEU C 1 171 ? 33.711  -0.875  74.309  1.000 34.423  0 171 LEU CCC CD2   1 ? 3 
ATOM   8710  N N     . LEU C 1 172 ? 31.330  -3.702  70.966  1.000 31.826  0 172 LEU CCC N     1 ? 3 
ATOM   8711  C CA    . LEU C 1 172 ? 32.128  -4.638  70.140  1.000 30.517  0 172 LEU CCC CA    1 ? 3 
ATOM   8712  C C     . LEU C 1 172 ? 33.492  -3.986  69.935  1.000 31.979  0 172 LEU CCC C     1 ? 3 
ATOM   8713  O O     . LEU C 1 172 ? 33.538  -2.804  69.502  1.000 30.393  0 172 LEU CCC O     1 ? 3 
ATOM   8714  C CB    . LEU C 1 172 ? 31.407  -4.867  68.806  1.000 30.919  0 172 LEU CCC CB    1 ? 3 
ATOM   8715  C CG    . LEU C 1 172 ? 29.895  -5.123  68.886  1.000 29.367  0 172 LEU CCC CG    1 ? 3 
ATOM   8716  C CD1   . LEU C 1 172 ? 29.330  -5.236  67.508  1.000 28.690  0 172 LEU CCC CD1   1 ? 3 
ATOM   8717  C CD2   . LEU C 1 172 ? 29.540  -6.376  69.697  1.000 29.935  0 172 LEU CCC CD2   1 ? 3 
ATOM   8718  N N     . ALA C 1 173 ? 34.560  -4.720  70.260  1.000 34.001  0 173 ALA CCC N     1 ? 3 
ATOM   8719  C CA    . ALA C 1 173 ? 35.963  -4.309  70.023  1.000 33.909  0 173 ALA CCC CA    1 ? 3 
ATOM   8720  C C     . ALA C 1 173 ? 36.827  -5.547  69.826  1.000 32.617  0 173 ALA CCC C     1 ? 3 
ATOM   8721  O O     . ALA C 1 173 ? 37.753  -5.744  70.587  1.000 32.196  0 173 ALA CCC O     1 ? 3 
ATOM   8722  C CB    . ALA C 1 173 ? 36.469  -3.474  71.167  1.000 36.244  0 173 ALA CCC CB    1 ? 3 
ATOM   8723  N N     . THR C 1 174 ? 36.482  -6.342  68.818  1.000 34.179  0 174 THR CCC N     1 ? 3 
ATOM   8724  C CA    . THR C 1 174 ? 37.062  -7.683  68.535  1.000 34.127  0 174 THR CCC CA    1 ? 3 
ATOM   8725  C C     . THR C 1 174 ? 38.329  -7.580  67.667  1.000 32.364  0 174 THR CCC C     1 ? 3 
ATOM   8726  O O     . THR C 1 174 ? 38.981  -8.614  67.483  1.000 30.911  0 174 THR CCC O     1 ? 3 
ATOM   8727  C CB    . THR C 1 174 ? 35.983  -8.571  67.908  1.000 34.524  0 174 THR CCC CB    1 ? 3 
ATOM   8728  O OG1   . THR C 1 174 ? 35.440  -7.877  66.775  1.000 32.594  0 174 THR CCC OG1   1 ? 3 
ATOM   8729  C CG2   . THR C 1 174 ? 34.914  -8.913  68.932  1.000 35.707  0 174 THR CCC CG2   1 ? 3 
ATOM   8730  N N     . GLY C 1 175 ? 38.650  -6.384  67.170  1.000 32.074  0 175 GLY CCC N     1 ? 3 
ATOM   8731  C CA    . GLY C 1 175 ? 39.853  -6.113  66.354  1.000 33.414  0 175 GLY CCC CA    1 ? 3 
ATOM   8732  C C     . GLY C 1 175 ? 39.834  -6.847  65.021  1.000 34.537  0 175 GLY CCC C     1 ? 3 
ATOM   8733  O O     . GLY C 1 175 ? 38.783  -7.424  64.659  1.000 37.833  0 175 GLY CCC O     1 ? 3 
ATOM   8734  N N     . GLY C 1 176 ? 40.963  -6.860  64.320  1.000 35.348  0 176 GLY CCC N     1 ? 3 
ATOM   8735  C CA    . GLY C 1 176 ? 41.151  -7.671  63.107  1.000 35.695  0 176 GLY CCC CA    1 ? 3 
ATOM   8736  C C     . GLY C 1 176 ? 42.066  -8.860  63.331  1.000 36.533  0 176 GLY CCC C     1 ? 3 
ATOM   8737  O O     . GLY C 1 176 ? 42.474  -9.113  64.482  1.000 43.781  0 176 GLY CCC O     1 ? 3 
ATOM   8738  N N     . ARG C 1 177 ? 42.340  -9.581  62.247  1.000 34.874  0 177 ARG CCC N     1 ? 3 
ATOM   8739  C CA    . ARG C 1 177 ? 43.385  -10.625 62.129  1.000 34.784  0 177 ARG CCC CA    1 ? 3 
ATOM   8740  C C     . ARG C 1 177 ? 44.045  -10.482 60.755  1.000 35.280  0 177 ARG CCC C     1 ? 3 
ATOM   8741  O O     . ARG C 1 177 ? 43.446  -9.938  59.817  1.000 34.786  0 177 ARG CCC O     1 ? 3 
ATOM   8742  C CB    . ARG C 1 177 ? 42.787  -12.007 62.422  1.000 34.260  0 177 ARG CCC CB    1 ? 3 
ATOM   8743  C CG    . ARG C 1 177 ? 42.245  -12.127 63.847  1.000 36.414  0 177 ARG CCC CG    1 ? 3 
ATOM   8744  C CD    . ARG C 1 177 ? 43.314  -11.936 64.932  1.000 36.304  0 177 ARG CCC CD    1 ? 3 
ATOM   8745  N NE    . ARG C 1 177 ? 44.223  -13.085 64.893  1.000 37.376  0 177 ARG CCC NE    1 ? 3 
ATOM   8746  C CZ    . ARG C 1 177 ? 43.991  -14.261 65.473  1.000 36.784  0 177 ARG CCC CZ    1 ? 3 
ATOM   8747  N NH1   . ARG C 1 177 ? 42.895  -14.439 66.186  1.000 36.309  0 177 ARG CCC NH1   1 ? 3 
ATOM   8748  N NH2   . ARG C 1 177 ? 44.865  -15.239 65.356  1.000 35.850  0 177 ARG CCC NH2   1 ? 3 
ATOM   8749  N N     . PRO C 1 178 ? 45.296  -10.953 60.603  1.000 33.611  0 178 PRO CCC N     1 ? 3 
ATOM   8750  C CA    . PRO C 1 178 ? 45.990  -10.870 59.328  1.000 35.122  0 178 PRO CCC CA    1 ? 3 
ATOM   8751  C C     . PRO C 1 178 ? 45.162  -11.516 58.216  1.000 37.992  0 178 PRO CCC C     1 ? 3 
ATOM   8752  O O     . PRO C 1 178 ? 44.485  -12.510 58.471  1.000 39.378  0 178 PRO CCC O     1 ? 3 
ATOM   8753  C CB    . PRO C 1 178 ? 47.294  -11.652 59.550  1.000 34.388  0 178 PRO CCC CB    1 ? 3 
ATOM   8754  C CG    . PRO C 1 178 ? 47.490  -11.620 61.050  1.000 33.641  0 178 PRO CCC CG    1 ? 3 
ATOM   8755  C CD    . PRO C 1 178 ? 46.100  -11.601 61.649  1.000 33.524  0 178 PRO CCC CD    1 ? 3 
ATOM   8756  N N     . SER C 1 179 ? 45.202  -10.930 57.025  1.000 41.558  0 179 SER CCC N     1 ? 3 
ATOM   8757  C CA    . SER C 1 179 ? 44.533  -11.513 55.830  1.000 44.545  0 179 SER CCC CA    1 ? 3 
ATOM   8758  C C     . SER C 1 179 ? 45.586  -12.117 54.900  1.000 45.459  0 179 SER CCC C     1 ? 3 
ATOM   8759  O O     . SER C 1 179 ? 46.604  -11.448 54.600  1.000 41.447  0 179 SER CCC O     1 ? 3 
ATOM   8760  C CB    . SER C 1 179 ? 43.672  -10.517 55.119  1.000 45.773  0 179 SER CCC CB    1 ? 3 
ATOM   8761  O OG    . SER C 1 179 ? 42.796  -11.211 54.251  1.000 47.927  0 179 SER CCC OG    1 ? 3 
ATOM   8762  N N     . ILE C 1 180 ? 45.352  -13.364 54.510  1.000 47.419  0 180 ILE CCC N     1 ? 3 
ATOM   8763  C CA    . ILE C 1 180 ? 46.154  -14.126 53.517  1.000 51.785  0 180 ILE CCC CA    1 ? 3 
ATOM   8764  C C     . ILE C 1 180 ? 45.262  -14.409 52.307  1.000 52.251  0 180 ILE CCC C     1 ? 3 
ATOM   8765  O O     . ILE C 1 180 ? 44.161  -14.938 52.466  1.000 54.732  0 180 ILE CCC O     1 ? 3 
ATOM   8766  C CB    . ILE C 1 180 ? 46.660  -15.439 54.136  1.000 54.591  0 180 ILE CCC CB    1 ? 3 
ATOM   8767  C CG1   . ILE C 1 180 ? 47.493  -15.190 55.388  1.000 56.149  0 180 ILE CCC CG1   1 ? 3 
ATOM   8768  C CG2   . ILE C 1 180 ? 47.423  -16.275 53.119  1.000 56.070  0 180 ILE CCC CG2   1 ? 3 
ATOM   8769  C CD1   . ILE C 1 180 ? 47.883  -16.478 56.112  1.000 58.029  0 180 ILE CCC CD1   1 ? 3 
ATOM   8770  N N     . PRO C 1 181 ? 45.711  -14.085 51.076  1.000 50.620  0 181 PRO CCC N     1 ? 3 
ATOM   8771  C CA    . PRO C 1 181 ? 44.939  -14.364 49.864  1.000 52.949  0 181 PRO CCC CA    1 ? 3 
ATOM   8772  C C     . PRO C 1 181 ? 44.626  -15.857 49.644  1.000 53.679  0 181 PRO CCC C     1 ? 3 
ATOM   8773  O O     . PRO C 1 181 ? 45.567  -16.631 49.503  1.000 51.071  0 181 PRO CCC O     1 ? 3 
ATOM   8774  C CB    . PRO C 1 181 ? 45.801  -13.813 48.715  1.000 52.274  0 181 PRO CCC CB    1 ? 3 
ATOM   8775  C CG    . PRO C 1 181 ? 47.178  -13.689 49.308  1.000 52.202  0 181 PRO CCC CG    1 ? 3 
ATOM   8776  C CD    . PRO C 1 181 ? 46.992  -13.438 50.787  1.000 50.445  0 181 PRO CCC CD    1 ? 3 
ATOM   8777  N N     . GLU C 1 182 ? 43.322  -16.195 49.614  1.000 56.235  0 182 GLU CCC N     1 ? 3 
ATOM   8778  C CA    . GLU C 1 182 ? 42.756  -17.565 49.429  1.000 62.015  0 182 GLU CCC CA    1 ? 3 
ATOM   8779  C C     . GLU C 1 182 ? 42.985  -18.014 47.978  1.000 61.396  0 182 GLU CCC C     1 ? 3 
ATOM   8780  O O     . GLU C 1 182 ? 43.122  -19.231 47.751  1.000 61.683  0 182 GLU CCC O     1 ? 3 
ATOM   8781  C CB    . GLU C 1 182 ? 41.272  -17.601 49.808  1.000 65.244  0 182 GLU CCC CB    1 ? 3 
ATOM   8782  C CG    . GLU C 1 182 ? 41.032  -17.435 51.307  1.000 67.355  0 182 GLU CCC CG    1 ? 3 
ATOM   8783  C CD    . GLU C 1 182 ? 39.668  -17.896 51.819  1.000 70.948  0 182 GLU CCC CD    1 ? 3 
ATOM   8784  O OE1   . GLU C 1 182 ? 38.723  -18.101 50.980  1.000 64.150  0 182 GLU CCC OE1   1 ? 3 
ATOM   8785  O OE2   . GLU C 1 182 ? 39.527  -18.051 53.071  1.000 65.399  0 182 GLU CCC OE2   1 ? 3 
ATOM   8786  N N     . THR C 1 183 ? 43.099  -17.051 47.057  1.000 60.914  0 183 THR CCC N     1 ? 3 
ATOM   8787  C CA    . THR C 1 183 ? 43.274  -17.246 45.592  1.000 61.887  0 183 THR CCC CA    1 ? 3 
ATOM   8788  C C     . THR C 1 183 ? 44.679  -17.803 45.282  1.000 62.201  0 183 THR CCC C     1 ? 3 
ATOM   8789  O O     . THR C 1 183 ? 44.797  -18.601 44.345  1.000 61.685  0 183 THR CCC O     1 ? 3 
ATOM   8790  C CB    . THR C 1 183 ? 42.972  -15.930 44.854  1.000 61.642  0 183 THR CCC CB    1 ? 3 
ATOM   8791  O OG1   . THR C 1 183 ? 43.921  -14.940 45.250  1.000 62.672  0 183 THR CCC OG1   1 ? 3 
ATOM   8792  C CG2   . THR C 1 183 ? 41.575  -15.418 45.126  1.000 62.343  0 183 THR CCC CG2   1 ? 3 
ATOM   8793  N N     . VAL C 1 184 ? 45.718  -17.388 46.018  1.000 61.587  0 184 VAL CCC N     1 ? 3 
ATOM   8794  C CA    . VAL C 1 184 ? 47.135  -17.792 45.759  1.000 59.452  0 184 VAL CCC CA    1 ? 3 
ATOM   8795  C C     . VAL C 1 184 ? 47.388  -19.157 46.390  1.000 58.363  0 184 VAL CCC C     1 ? 3 
ATOM   8796  O O     . VAL C 1 184 ? 47.378  -19.291 47.607  1.000 53.966  0 184 VAL CCC O     1 ? 3 
ATOM   8797  C CB    . VAL C 1 184 ? 48.149  -16.750 46.256  1.000 58.166  0 184 VAL CCC CB    1 ? 3 
ATOM   8798  C CG1   . VAL C 1 184 ? 49.565  -17.317 46.204  1.000 60.012  0 184 VAL CCC CG1   1 ? 3 
ATOM   8799  C CG2   . VAL C 1 184 ? 48.036  -15.451 45.461  1.000 56.686  0 184 VAL CCC CG2   1 ? 3 
ATOM   8800  N N     . PRO C 1 185 ? 47.627  -20.211 45.573  1.000 60.104  0 185 PRO CCC N     1 ? 3 
ATOM   8801  C CA    . PRO C 1 185 ? 47.855  -21.560 46.097  1.000 57.248  0 185 PRO CCC CA    1 ? 3 
ATOM   8802  C C     . PRO C 1 185 ? 49.111  -21.715 46.957  1.000 53.571  0 185 PRO CCC C     1 ? 3 
ATOM   8803  O O     . PRO C 1 185 ? 50.131  -21.214 46.561  1.000 50.901  0 185 PRO CCC O     1 ? 3 
ATOM   8804  C CB    . PRO C 1 185 ? 48.016  -22.428 44.836  1.000 61.611  0 185 PRO CCC CB    1 ? 3 
ATOM   8805  C CG    . PRO C 1 185 ? 47.375  -21.605 43.731  1.000 62.672  0 185 PRO CCC CG    1 ? 3 
ATOM   8806  C CD    . PRO C 1 185 ? 47.665  -20.167 44.099  1.000 61.160  0 185 PRO CCC CD    1 ? 3 
ATOM   8807  N N     . GLY C 1 186 ? 48.986  -22.434 48.079  1.000 52.049  0 186 GLY CCC N     1 ? 3 
ATOM   8808  C CA    . GLY C 1 186 ? 50.042  -22.669 49.090  1.000 52.259  0 186 GLY CCC CA    1 ? 3 
ATOM   8809  C C     . GLY C 1 186 ? 50.142  -21.588 50.176  1.000 48.661  0 186 GLY CCC C     1 ? 3 
ATOM   8810  O O     . GLY C 1 186 ? 50.780  -21.864 51.196  1.000 45.792  0 186 GLY CCC O     1 ? 3 
ATOM   8811  N N     . ALA C 1 187 ? 49.537  -20.413 49.977  1.000 48.063  0 187 ALA CCC N     1 ? 3 
ATOM   8812  C CA    . ALA C 1 187 ? 49.672  -19.214 50.843  1.000 51.417  0 187 ALA CCC CA    1 ? 3 
ATOM   8813  C C     . ALA C 1 187 ? 49.251  -19.535 52.291  1.000 54.889  0 187 ALA CCC C     1 ? 3 
ATOM   8814  O O     . ALA C 1 187 ? 50.065  -19.326 53.212  1.000 55.617  0 187 ALA CCC O     1 ? 3 
ATOM   8815  C CB    . ALA C 1 187 ? 48.871  -18.065 50.266  1.000 51.288  0 187 ALA CCC CB    1 ? 3 
ATOM   8816  N N     . ILE C 1 188 ? 48.027  -20.032 52.485  1.000 53.158  0 188 ILE CCC N     1 ? 3 
ATOM   8817  C CA    . ILE C 1 188 ? 47.420  -20.320 53.817  1.000 49.989  0 188 ILE CCC CA    1 ? 3 
ATOM   8818  C C     . ILE C 1 188 ? 48.258  -21.390 54.516  1.000 49.939  0 188 ILE CCC C     1 ? 3 
ATOM   8819  O O     . ILE C 1 188 ? 48.444  -21.301 55.736  1.000 52.804  0 188 ILE CCC O     1 ? 3 
ATOM   8820  C CB    . ILE C 1 188 ? 45.932  -20.721 53.636  1.000 50.172  0 188 ILE CCC CB    1 ? 3 
ATOM   8821  C CG1   . ILE C 1 188 ? 45.033  -19.483 53.511  1.000 47.718  0 188 ILE CCC CG1   1 ? 3 
ATOM   8822  C CG2   . ILE C 1 188 ? 45.445  -21.645 54.742  1.000 50.514  0 188 ILE CCC CG2   1 ? 3 
ATOM   8823  C CD1   . ILE C 1 188 ? 43.740  -19.726 52.771  1.000 47.264  0 188 ILE CCC CD1   1 ? 3 
ATOM   8824  N N     . GLN C 1 189 ? 48.764  -22.361 53.771  1.000 52.507  0 189 GLN CCC N     1 ? 3 
ATOM   8825  C CA    . GLN C 1 189 ? 49.428  -23.558 54.351  1.000 56.226  0 189 GLN CCC CA    1 ? 3 
ATOM   8826  C C     . GLN C 1 189 ? 50.848  -23.210 54.810  1.000 57.823  0 189 GLN CCC C     1 ? 3 
ATOM   8827  O O     . GLN C 1 189 ? 51.251  -23.681 55.909  1.000 60.289  0 189 GLN CCC O     1 ? 3 
ATOM   8828  C CB    . GLN C 1 189 ? 49.467  -24.708 53.344  1.000 59.505  0 189 GLN CCC CB    1 ? 3 
ATOM   8829  C CG    . GLN C 1 189 ? 49.583  -26.070 54.013  1.000 62.902  0 189 GLN CCC CG    1 ? 3 
ATOM   8830  C CD    . GLN C 1 189 ? 49.904  -27.199 53.056  1.000 65.741  0 189 GLN CCC CD    1 ? 3 
ATOM   8831  O OE1   . GLN C 1 189 ? 49.390  -27.259 51.935  1.000 64.984  0 189 GLN CCC OE1   1 ? 3 
ATOM   8832  N NE2   . GLN C 1 189 ? 50.758  -28.108 53.506  1.000 63.859  0 189 GLN CCC NE2   1 ? 3 
ATOM   8833  N N     . TYR C 1 190 ? 51.588  -22.429 54.015  1.000 53.821  0 190 TYR CCC N     1 ? 3 
ATOM   8834  C CA    . TYR C 1 190 ? 53.070  -22.334 54.116  1.000 54.046  0 190 TYR CCC CA    1 ? 3 
ATOM   8835  C C     . TYR C 1 190 ? 53.540  -20.970 54.646  1.000 47.920  0 190 TYR CCC C     1 ? 3 
ATOM   8836  O O     . TYR C 1 190 ? 54.658  -20.909 55.143  1.000 43.856  0 190 TYR CCC O     1 ? 3 
ATOM   8837  C CB    . TYR C 1 190 ? 53.694  -22.676 52.760  1.000 58.516  0 190 TYR CCC CB    1 ? 3 
ATOM   8838  C CG    . TYR C 1 190 ? 53.542  -24.124 52.352  1.000 64.265  0 190 TYR CCC CG    1 ? 3 
ATOM   8839  C CD1   . TYR C 1 190 ? 53.954  -25.150 53.187  1.000 66.063  0 190 TYR CCC CD1   1 ? 3 
ATOM   8840  C CD2   . TYR C 1 190 ? 52.992  -24.470 51.127  1.000 68.908  0 190 TYR CCC CD2   1 ? 3 
ATOM   8841  C CE1   . TYR C 1 190 ? 53.849  -26.477 52.807  1.000 70.820  0 190 TYR CCC CE1   1 ? 3 
ATOM   8842  C CE2   . TYR C 1 190 ? 52.872  -25.794 50.732  1.000 73.318  0 190 TYR CCC CE2   1 ? 3 
ATOM   8843  C CZ    . TYR C 1 190 ? 53.299  -26.804 51.578  1.000 75.036  0 190 TYR CCC CZ    1 ? 3 
ATOM   8844  O OH    . TYR C 1 190 ? 53.170  -28.112 51.201  1.000 78.452  0 190 TYR CCC OH    1 ? 3 
ATOM   8845  N N     . SER C 1 191 ? 52.728  -19.919 54.523  1.000 45.145  0 191 SER CCC N     1 ? 3 
ATOM   8846  C CA    . SER C 1 191 ? 53.094  -18.524 54.882  1.000 44.914  0 191 SER CCC CA    1 ? 3 
ATOM   8847  C C     . SER C 1 191 ? 52.724  -18.236 56.344  1.000 42.927  0 191 SER CCC C     1 ? 3 
ATOM   8848  O O     . SER C 1 191 ? 51.724  -18.785 56.859  1.000 43.518  0 191 SER CCC O     1 ? 3 
ATOM   8849  C CB    . SER C 1 191 ? 52.470  -17.513 53.967  1.000 43.317  0 191 SER CCC CB    1 ? 3 
ATOM   8850  O OG    . SER C 1 191 ? 51.142  -17.330 54.344  1.000 49.646  0 191 SER CCC OG    1 ? 3 
ATOM   8851  N N     . ILE C 1 192 ? 53.500  -17.363 56.975  1.000 40.351  0 192 ILE CCC N     1 ? 3 
ATOM   8852  C CA    . ILE C 1 192 ? 53.225  -16.835 58.344  1.000 39.055  0 192 ILE CCC CA    1 ? 3 
ATOM   8853  C C     . ILE C 1 192 ? 52.693  -15.408 58.203  1.000 37.000  0 192 ILE CCC C     1 ? 3 
ATOM   8854  O O     . ILE C 1 192 ? 52.658  -14.900 57.067  1.000 37.329  0 192 ILE CCC O     1 ? 3 
ATOM   8855  C CB    . ILE C 1 192 ? 54.490  -16.910 59.238  1.000 38.666  0 192 ILE CCC CB    1 ? 3 
ATOM   8856  C CG1   . ILE C 1 192 ? 55.642  -16.056 58.704  1.000 39.079  0 192 ILE CCC CG1   1 ? 3 
ATOM   8857  C CG2   . ILE C 1 192 ? 54.930  -18.350 59.429  1.000 39.170  0 192 ILE CCC CG2   1 ? 3 
ATOM   8858  C CD1   . ILE C 1 192 ? 56.722  -15.828 59.725  1.000 38.697  0 192 ILE CCC CD1   1 ? 3 
ATOM   8859  N N     . THR C 1 193 ? 52.276  -14.813 59.320  1.000 35.325  0 193 THR CCC N     1 ? 3 
ATOM   8860  C CA    . THR C 1 193 ? 51.768  -13.428 59.425  1.000 34.424  0 193 THR CCC CA    1 ? 3 
ATOM   8861  C C     . THR C 1 193 ? 52.400  -12.788 60.655  1.000 35.247  0 193 THR CCC C     1 ? 3 
ATOM   8862  O O     . THR C 1 193 ? 53.175  -13.465 61.312  1.000 34.689  0 193 THR CCC O     1 ? 3 
ATOM   8863  C CB    . THR C 1 193 ? 50.234  -13.421 59.507  1.000 34.007  0 193 THR CCC CB    1 ? 3 
ATOM   8864  O OG1   . THR C 1 193 ? 49.806  -13.997 60.744  1.000 30.070  0 193 THR CCC OG1   1 ? 3 
ATOM   8865  C CG2   . THR C 1 193 ? 49.618  -14.174 58.357  1.000 34.817  0 193 THR CCC CG2   1 ? 3 
ATOM   8866  N N     . SER C 1 194 ? 52.007  -11.555 60.982  1.000 36.179  0 194 SER CCC N     1 ? 3 
ATOM   8867  C CA    . SER C 1 194 ? 52.415  -10.809 62.203  1.000 34.333  0 194 SER CCC CA    1 ? 3 
ATOM   8868  C C     . SER C 1 194 ? 51.985  -11.573 63.464  1.000 35.467  0 194 SER CCC C     1 ? 3 
ATOM   8869  O O     . SER C 1 194 ? 52.610  -11.394 64.494  1.000 37.633  0 194 SER CCC O     1 ? 3 
ATOM   8870  C CB    . SER C 1 194 ? 51.876  -9.394  62.191  1.000 33.127  0 194 SER CCC CB    1 ? 3 
ATOM   8871  O OG    . SER C 1 194 ? 50.494  -9.365  61.864  1.000 32.712  0 194 SER CCC OG    1 ? 3 
ATOM   8872  N N     . ASP C 1 195 ? 50.949  -12.399 63.386  1.000 37.172  0 195 ASP CCC N     1 ? 3 
ATOM   8873  C CA    . ASP C 1 195 ? 50.525  -13.275 64.507  1.000 36.797  0 195 ASP CCC CA    1 ? 3 
ATOM   8874  C C     . ASP C 1 195 ? 51.623  -14.290 64.890  1.000 36.804  0 195 ASP CCC C     1 ? 3 
ATOM   8875  O O     . ASP C 1 195 ? 51.597  -14.776 66.049  1.000 37.579  0 195 ASP CCC O     1 ? 3 
ATOM   8876  C CB    . ASP C 1 195 ? 49.223  -14.003 64.148  1.000 36.274  0 195 ASP CCC CB    1 ? 3 
ATOM   8877  C CG    . ASP C 1 195 ? 47.978  -13.134 64.224  1.000 35.982  0 195 ASP CCC CG    1 ? 3 
ATOM   8878  O OD1   . ASP C 1 195 ? 48.108  -11.910 64.453  1.000 35.199  0 195 ASP CCC OD1   1 ? 3 
ATOM   8879  O OD2   . ASP C 1 195 ? 46.882  -13.701 64.077  1.000 36.937  0 195 ASP CCC OD2   1 ? 3 
ATOM   8880  N N     . ASP C 1 196 ? 52.552  -14.629 63.997  1.000 35.244  0 196 ASP CCC N     1 ? 3 
ATOM   8881  C CA    . ASP C 1 196 ? 53.518  -15.737 64.260  1.000 35.041  0 196 ASP CCC CA    1 ? 3 
ATOM   8882  C C     . ASP C 1 196 ? 54.959  -15.241 64.374  1.000 36.359  0 196 ASP CCC C     1 ? 3 
ATOM   8883  O O     . ASP C 1 196 ? 55.748  -15.929 65.069  1.000 38.453  0 196 ASP CCC O     1 ? 3 
ATOM   8884  C CB    . ASP C 1 196 ? 53.454  -16.779 63.146  1.000 34.037  0 196 ASP CCC CB    1 ? 3 
ATOM   8885  C CG    . ASP C 1 196 ? 52.042  -17.163 62.778  1.000 32.361  0 196 ASP CCC CG    1 ? 3 
ATOM   8886  O OD1   . ASP C 1 196 ? 51.363  -17.751 63.651  1.000 31.132  0 196 ASP CCC OD1   1 ? 3 
ATOM   8887  O OD2   . ASP C 1 196 ? 51.660  -16.867 61.622  1.000 32.277  0 196 ASP CCC OD2   1 ? 3 
ATOM   8888  N N     . ILE C 1 197 ? 55.294  -14.112 63.723  1.000 35.166  0 197 ILE CCC N     1 ? 3 
ATOM   8889  C CA    . ILE C 1 197 ? 56.710  -13.682 63.502  1.000 33.156  0 197 ILE CCC CA    1 ? 3 
ATOM   8890  C C     . ILE C 1 197 ? 57.408  -13.415 64.840  1.000 33.481  0 197 ILE CCC C     1 ? 3 
ATOM   8891  O O     . ILE C 1 197 ? 58.620  -13.635 64.923  1.000 36.353  0 197 ILE CCC O     1 ? 3 
ATOM   8892  C CB    . ILE C 1 197 ? 56.778  -12.456 62.576  1.000 32.093  0 197 ILE CCC CB    1 ? 3 
ATOM   8893  C CG1   . ILE C 1 197 ? 58.224  -12.085 62.261  1.000 32.755  0 197 ILE CCC CG1   1 ? 3 
ATOM   8894  C CG2   . ILE C 1 197 ? 56.001  -11.254 63.140  1.000 32.007  0 197 ILE CCC CG2   1 ? 3 
ATOM   8895  C CD1   . ILE C 1 197 ? 59.042  -13.228 61.733  1.000 34.911  0 197 ILE CCC CD1   1 ? 3 
ATOM   8896  N N     . PHE C 1 198 ? 56.713  -12.943 65.869  1.000 33.608  0 198 PHE CCC N     1 ? 3 
ATOM   8897  C CA    . PHE C 1 198 ? 57.370  -12.533 67.132  1.000 34.394  0 198 PHE CCC CA    1 ? 3 
ATOM   8898  C C     . PHE C 1 198 ? 57.748  -13.745 67.989  1.000 35.846  0 198 PHE CCC C     1 ? 3 
ATOM   8899  O O     . PHE C 1 198 ? 58.575  -13.551 68.912  1.000 34.942  0 198 PHE CCC O     1 ? 3 
ATOM   8900  C CB    . PHE C 1 198 ? 56.516  -11.499 67.856  1.000 32.138  0 198 PHE CCC CB    1 ? 3 
ATOM   8901  C CG    . PHE C 1 198 ? 56.254  -10.299 66.991  1.000 31.805  0 198 PHE CCC CG    1 ? 3 
ATOM   8902  C CD1   . PHE C 1 198 ? 57.300  -9.516  66.509  1.000 31.984  0 198 PHE CCC CD1   1 ? 3 
ATOM   8903  C CD2   . PHE C 1 198 ? 54.958  -9.952  66.641  1.000 31.692  0 198 PHE CCC CD2   1 ? 3 
ATOM   8904  C CE1   . PHE C 1 198 ? 57.045  -8.425  65.693  1.000 31.010  0 198 PHE CCC CE1   1 ? 3 
ATOM   8905  C CE2   . PHE C 1 198 ? 54.700  -8.841  65.852  1.000 29.809  0 198 PHE CCC CE2   1 ? 3 
ATOM   8906  C CZ    . PHE C 1 198 ? 55.741  -8.087  65.380  1.000 30.704  0 198 PHE CCC CZ    1 ? 3 
ATOM   8907  N N     . PHE C 1 199 ? 57.193  -14.927 67.698  1.000 40.041  0 199 PHE CCC N     1 ? 3 
ATOM   8908  C CA    . PHE C 1 199 ? 57.262  -16.140 68.561  1.000 42.384  0 199 PHE CCC CA    1 ? 3 
ATOM   8909  C C     . PHE C 1 199 ? 57.818  -17.349 67.808  1.000 42.589  0 199 PHE CCC C     1 ? 3 
ATOM   8910  O O     . PHE C 1 199 ? 57.792  -18.444 68.374  1.000 43.749  0 199 PHE CCC O     1 ? 3 
ATOM   8911  C CB    . PHE C 1 199 ? 55.871  -16.472 69.110  1.000 43.417  0 199 PHE CCC CB    1 ? 3 
ATOM   8912  C CG    . PHE C 1 199 ? 55.236  -15.303 69.810  1.000 45.070  0 199 PHE CCC CG    1 ? 3 
ATOM   8913  C CD1   . PHE C 1 199 ? 55.882  -14.681 70.862  1.000 47.504  0 199 PHE CCC CD1   1 ? 3 
ATOM   8914  C CD2   . PHE C 1 199 ? 54.032  -14.783 69.381  1.000 45.652  0 199 PHE CCC CD2   1 ? 3 
ATOM   8915  C CE1   . PHE C 1 199 ? 55.318  -13.586 71.497  1.000 47.607  0 199 PHE CCC CE1   1 ? 3 
ATOM   8916  C CE2   . PHE C 1 199 ? 53.463  -13.700 70.020  1.000 45.319  0 199 PHE CCC CE2   1 ? 3 
ATOM   8917  C CZ    . PHE C 1 199 ? 54.102  -13.116 71.088  1.000 47.874  0 199 PHE CCC CZ    1 ? 3 
ATOM   8918  N N     . LEU C 1 200 ? 58.293  -17.196 66.571  1.000 42.871  0 200 LEU CCC N     1 ? 3 
ATOM   8919  C CA    . LEU C 1 200 ? 58.917  -18.327 65.844  1.000 42.285  0 200 LEU CCC CA    1 ? 3 
ATOM   8920  C C     . LEU C 1 200 ? 59.894  -19.053 66.763  1.000 41.458  0 200 LEU CCC C     1 ? 3 
ATOM   8921  O O     . LEU C 1 200 ? 60.778  -18.399 67.291  1.000 37.570  0 200 LEU CCC O     1 ? 3 
ATOM   8922  C CB    . LEU C 1 200 ? 59.672  -17.785 64.637  1.000 41.560  0 200 LEU CCC CB    1 ? 3 
ATOM   8923  C CG    . LEU C 1 200 ? 58.838  -17.396 63.441  1.000 40.854  0 200 LEU CCC CG    1 ? 3 
ATOM   8924  C CD1   . LEU C 1 200 ? 59.747  -17.125 62.246  1.000 40.062  0 200 LEU CCC CD1   1 ? 3 
ATOM   8925  C CD2   . LEU C 1 200 ? 57.856  -18.507 63.120  1.000 42.972  0 200 LEU CCC CD2   1 ? 3 
ATOM   8926  N N     . SER C 1 201 ? 59.732  -20.369 66.910  1.000 44.961  0 201 SER CCC N     1 ? 3 
ATOM   8927  C CA    A SER C 1 201 ? 60.670  -21.247 67.660  0.500 46.873  0 201 SER CCC CA    1 ? 3 
ATOM   8928  C CA    B SER C 1 201 ? 60.670  -21.236 67.664  0.500 48.143  0 201 SER CCC CA    1 ? 3 
ATOM   8929  C C     . SER C 1 201 ? 62.046  -21.234 66.975  1.000 50.039  0 201 SER CCC C     1 ? 3 
ATOM   8930  O O     . SER C 1 201 ? 63.055  -21.362 67.680  1.000 49.800  0 201 SER CCC O     1 ? 3 
ATOM   8931  C CB    A SER C 1 201 ? 60.127  -22.640 67.793  0.500 46.227  0 201 SER CCC CB    1 ? 3 
ATOM   8932  C CB    B SER C 1 201 ? 60.117  -22.619 67.813  0.500 48.847  0 201 SER CCC CB    1 ? 3 
ATOM   8933  O OG    A SER C 1 201 ? 59.796  -23.184 66.523  0.500 45.167  0 201 SER CCC OG    1 ? 3 
ATOM   8934  O OG    B SER C 1 201 ? 58.937  -22.599 68.600  0.500 50.941  0 201 SER CCC OG    1 ? 3 
ATOM   8935  N N     . LYS C 1 202 ? 62.069  -21.063 65.652  1.000 51.370  0 202 LYS CCC N     1 ? 3 
ATOM   8936  C CA    . LYS C 1 202 ? 63.303  -21.041 64.843  1.000 54.469  0 202 LYS CCC CA    1 ? 3 
ATOM   8937  C C     . LYS C 1 202 ? 63.439  -19.676 64.155  1.000 51.483  0 202 LYS CCC C     1 ? 3 
ATOM   8938  O O     . LYS C 1 202 ? 62.424  -19.078 63.810  1.000 52.605  0 202 LYS CCC O     1 ? 3 
ATOM   8939  C CB    . LYS C 1 202 ? 63.264  -22.177 63.821  1.000 62.814  0 202 LYS CCC CB    1 ? 3 
ATOM   8940  C CG    . LYS C 1 202 ? 64.606  -22.408 63.149  1.000 73.084  0 202 LYS CCC CG    1 ? 3 
ATOM   8941  C CD    . LYS C 1 202 ? 64.611  -23.369 62.002  1.000 80.945  0 202 LYS CCC CD    1 ? 3 
ATOM   8942  C CE    . LYS C 1 202 ? 66.010  -23.533 61.434  1.000 87.701  0 202 LYS CCC CE    1 ? 3 
ATOM   8943  N NZ    . LYS C 1 202 ? 66.473  -22.321 60.707  1.000 88.417  0 202 LYS CCC NZ    1 ? 3 
ATOM   8944  N N     . SER C 1 203 ? 64.664  -19.222 63.926  1.000 46.346  0 203 SER CCC N     1 ? 3 
ATOM   8945  C CA    . SER C 1 203 ? 64.938  -17.985 63.159  1.000 45.179  0 203 SER CCC CA    1 ? 3 
ATOM   8946  C C     . SER C 1 203 ? 64.377  -18.155 61.751  1.000 45.484  0 203 SER CCC C     1 ? 3 
ATOM   8947  O O     . SER C 1 203 ? 64.387  -19.241 61.174  1.000 49.990  0 203 SER CCC O     1 ? 3 
ATOM   8948  C CB    . SER C 1 203 ? 66.415  -17.604 63.174  1.000 43.529  0 203 SER CCC CB    1 ? 3 
ATOM   8949  O OG    . SER C 1 203 ? 67.179  -18.563 62.459  1.000 40.728  0 203 SER CCC OG    1 ? 3 
ATOM   8950  N N     . PRO C 1 204 ? 63.858  -17.070 61.149  1.000 43.944  0 204 PRO CCC N     1 ? 3 
ATOM   8951  C CA    . PRO C 1 204 ? 63.207  -17.163 59.843  1.000 42.514  0 204 PRO CCC CA    1 ? 3 
ATOM   8952  C C     . PRO C 1 204 ? 64.125  -17.371 58.624  1.000 41.248  0 204 PRO CCC C     1 ? 3 
ATOM   8953  O O     . PRO C 1 204 ? 63.609  -17.693 57.561  1.000 40.025  0 204 PRO CCC O     1 ? 3 
ATOM   8954  C CB    . PRO C 1 204 ? 62.483  -15.809 59.778  1.000 43.645  0 204 PRO CCC CB    1 ? 3 
ATOM   8955  C CG    . PRO C 1 204 ? 63.370  -14.866 60.546  1.000 42.985  0 204 PRO CCC CG    1 ? 3 
ATOM   8956  C CD    . PRO C 1 204 ? 63.885  -15.699 61.693  1.000 43.331  0 204 PRO CCC CD    1 ? 3 
ATOM   8957  N N     . GLY C 1 205 ? 65.434  -17.196 58.799  1.000 41.399  0 205 GLY CCC N     1 ? 3 
ATOM   8958  C CA    . GLY C 1 205 ? 66.440  -17.193 57.711  1.000 42.624  0 205 GLY CCC CA    1 ? 3 
ATOM   8959  C C     . GLY C 1 205 ? 66.047  -16.247 56.578  1.000 40.738  0 205 GLY CCC C     1 ? 3 
ATOM   8960  O O     . GLY C 1 205 ? 65.410  -15.174 56.873  1.000 37.514  0 205 GLY CCC O     1 ? 3 
ATOM   8961  N N     . LYS C 1 206 ? 66.346  -16.647 55.338  1.000 38.300  0 206 LYS CCC N     1 ? 3 
ATOM   8962  C CA    . LYS C 1 206 ? 66.010  -15.886 54.113  1.000 39.040  0 206 LYS CCC CA    1 ? 3 
ATOM   8963  C C     . LYS C 1 206 ? 64.488  -15.659 54.064  1.000 37.831  0 206 LYS CCC C     1 ? 3 
ATOM   8964  O O     . LYS C 1 206 ? 63.743  -16.654 54.050  1.000 38.291  0 206 LYS CCC O     1 ? 3 
ATOM   8965  C CB    . LYS C 1 206 ? 66.531  -16.624 52.879  1.000 40.316  0 206 LYS CCC CB    1 ? 3 
ATOM   8966  C CG    . LYS C 1 206 ? 66.034  -16.084 51.543  1.000 42.339  0 206 LYS CCC CG    1 ? 3 
ATOM   8967  C CD    . LYS C 1 206 ? 66.856  -16.558 50.324  1.000 44.073  0 206 LYS CCC CD    1 ? 3 
ATOM   8968  C CE    . LYS C 1 206 ? 66.517  -15.766 49.083  1.000 44.665  0 206 LYS CCC CE    1 ? 3 
ATOM   8969  N NZ    . LYS C 1 206 ? 66.882  -16.516 47.860  1.000 46.294  0 206 LYS CCC NZ    1 ? 3 
ATOM   8970  N N     . THR C 1 207 ? 64.031  -14.406 54.020  1.000 35.643  0 207 THR CCC N     1 ? 3 
ATOM   8971  C CA    . THR C 1 207 ? 62.599  -14.073 54.220  1.000 35.035  0 207 THR CCC CA    1 ? 3 
ATOM   8972  C C     . THR C 1 207 ? 62.056  -13.221 53.081  1.000 34.663  0 207 THR CCC C     1 ? 3 
ATOM   8973  O O     . THR C 1 207 ? 62.754  -12.290 52.658  1.000 35.824  0 207 THR CCC O     1 ? 3 
ATOM   8974  C CB    . THR C 1 207 ? 62.358  -13.342 55.546  1.000 34.117  0 207 THR CCC CB    1 ? 3 
ATOM   8975  O OG1   . THR C 1 207 ? 62.891  -14.129 56.619  1.000 33.551  0 207 THR CCC OG1   1 ? 3 
ATOM   8976  C CG2   . THR C 1 207 ? 60.885  -13.049 55.762  1.000 33.699  0 207 THR CCC CG2   1 ? 3 
ATOM   8977  N N     . LEU C 1 208 ? 60.843  -13.546 52.634  1.000 33.808  0 208 LEU CCC N     1 ? 3 
ATOM   8978  C CA    . LEU C 1 208 ? 60.019  -12.723 51.722  1.000 34.525  0 208 LEU CCC CA    1 ? 3 
ATOM   8979  C C     . LEU C 1 208 ? 58.853  -12.139 52.523  1.000 33.225  0 208 LEU CCC C     1 ? 3 
ATOM   8980  O O     . LEU C 1 208 ? 58.121  -12.916 53.178  1.000 31.927  0 208 LEU CCC O     1 ? 3 
ATOM   8981  C CB    . LEU C 1 208 ? 59.478  -13.590 50.574  1.000 36.026  0 208 LEU CCC CB    1 ? 3 
ATOM   8982  C CG    . LEU C 1 208 ? 58.493  -12.898 49.623  1.000 35.831  0 208 LEU CCC CG    1 ? 3 
ATOM   8983  C CD1   . LEU C 1 208 ? 59.196  -11.808 48.821  1.000 36.615  0 208 LEU CCC CD1   1 ? 3 
ATOM   8984  C CD2   . LEU C 1 208 ? 57.816  -13.879 48.711  1.000 35.699  0 208 LEU CCC CD2   1 ? 3 
ATOM   8985  N N     . VAL C 1 209 ? 58.691  -10.820 52.443  1.000 33.161  0 209 VAL CCC N     1 ? 3 
ATOM   8986  C CA    . VAL C 1 209 ? 57.566  -10.071 53.060  1.000 32.210  0 209 VAL CCC CA    1 ? 3 
ATOM   8987  C C     . VAL C 1 209 ? 56.731  -9.531  51.895  1.000 32.773  0 209 VAL CCC C     1 ? 3 
ATOM   8988  O O     . VAL C 1 209 ? 57.302  -8.842  51.041  1.000 32.416  0 209 VAL CCC O     1 ? 3 
ATOM   8989  C CB    . VAL C 1 209 ? 58.072  -8.952  53.986  1.000 31.867  0 209 VAL CCC CB    1 ? 3 
ATOM   8990  C CG1   . VAL C 1 209 ? 56.937  -8.103  54.512  1.000 33.248  0 209 VAL CCC CG1   1 ? 3 
ATOM   8991  C CG2   . VAL C 1 209 ? 58.872  -9.482  55.148  1.000 31.901  0 209 VAL CCC CG2   1 ? 3 
ATOM   8992  N N     . ILE C 1 210 ? 55.447  -9.887  51.845  1.000 33.643  0 210 ILE CCC N     1 ? 3 
ATOM   8993  C CA    . ILE C 1 210 ? 54.494  -9.404  50.806  1.000 33.884  0 210 ILE CCC CA    1 ? 3 
ATOM   8994  C C     . ILE C 1 210 ? 53.676  -8.279  51.444  1.000 32.042  0 210 ILE CCC C     1 ? 3 
ATOM   8995  O O     . ILE C 1 210 ? 53.002  -8.528  52.457  1.000 32.575  0 210 ILE CCC O     1 ? 3 
ATOM   8996  C CB    . ILE C 1 210 ? 53.607  -10.541 50.242  1.000 35.283  0 210 ILE CCC CB    1 ? 3 
ATOM   8997  C CG1   . ILE C 1 210 ? 54.441  -11.737 49.757  1.000 35.643  0 210 ILE CCC CG1   1 ? 3 
ATOM   8998  C CG2   . ILE C 1 210 ? 52.707  -10.016 49.119  1.000 34.821  0 210 ILE CCC CG2   1 ? 3 
ATOM   8999  C CD1   . ILE C 1 210 ? 54.332  -12.940 50.639  1.000 34.693  0 210 ILE CCC CD1   1 ? 3 
ATOM   9000  N N     . GLY C 1 211 ? 53.745  -7.085  50.862  1.000 30.624  0 211 GLY CCC N     1 ? 3 
ATOM   9001  C CA    . GLY C 1 211 ? 53.102  -5.878  51.386  1.000 30.385  0 211 GLY CCC CA    1 ? 3 
ATOM   9002  C C     . GLY C 1 211 ? 54.149  -4.826  51.704  1.000 31.909  0 211 GLY CCC C     1 ? 3 
ATOM   9003  O O     . GLY C 1 211 ? 55.040  -5.094  52.538  1.000 32.061  0 211 GLY CCC O     1 ? 3 
ATOM   9004  N N     . ALA C 1 212 ? 54.034  -3.656  51.090  1.000 32.294  0 212 ALA CCC N     1 ? 3 
ATOM   9005  C CA    . ALA C 1 212 ? 54.819  -2.451  51.425  1.000 33.394  0 212 ALA CCC CA    1 ? 3 
ATOM   9006  C C     . ALA C 1 212 ? 53.939  -1.489  52.259  1.000 32.389  0 212 ALA CCC C     1 ? 3 
ATOM   9007  O O     . ALA C 1 212 ? 54.206  -0.265  52.226  1.000 31.721  0 212 ALA CCC O     1 ? 3 
ATOM   9008  C CB    . ALA C 1 212 ? 55.321  -1.839  50.142  1.000 32.555  0 212 ALA CCC CB    1 ? 3 
ATOM   9009  N N     . SER C 1 213 ? 52.922  -2.043  52.933  1.000 32.081  0 213 SER CCC N     1 ? 3 
ATOM   9010  C CA    . SER C 1 213 ? 52.231  -1.496  54.136  1.000 33.492  0 213 SER CCC CA    1 ? 3 
ATOM   9011  C C     . SER C 1 213 ? 53.226  -1.215  55.278  1.000 31.668  0 213 SER CCC C     1 ? 3 
ATOM   9012  O O     . SER C 1 213 ? 54.348  -1.786  55.266  1.000 31.906  0 213 SER CCC O     1 ? 3 
ATOM   9013  C CB    . SER C 1 213 ? 51.200  -2.499  54.630  1.000 35.239  0 213 SER CCC CB    1 ? 3 
ATOM   9014  O OG    . SER C 1 213 ? 51.865  -3.711  55.009  1.000 34.031  0 213 SER CCC OG    1 ? 3 
ATOM   9015  N N     . TYR C 1 214 ? 52.826  -0.439  56.282  1.000 29.962  0 214 TYR CCC N     1 ? 3 
ATOM   9016  C CA    . TYR C 1 214 ? 53.707  -0.115  57.434  1.000 30.117  0 214 TYR CCC CA    1 ? 3 
ATOM   9017  C C     . TYR C 1 214 ? 54.140  -1.404  58.146  1.000 28.987  0 214 TYR CCC C     1 ? 3 
ATOM   9018  O O     . TYR C 1 214 ? 55.324  -1.520  58.557  1.000 28.914  0 214 TYR CCC O     1 ? 3 
ATOM   9019  C CB    . TYR C 1 214 ? 53.036  0.932   58.326  1.000 32.420  0 214 TYR CCC CB    1 ? 3 
ATOM   9020  C CG    . TYR C 1 214 ? 52.124  0.464   59.443  1.000 32.566  0 214 TYR CCC CG    1 ? 3 
ATOM   9021  C CD1   . TYR C 1 214 ? 52.644  0.214   60.718  1.000 32.634  0 214 TYR CCC CD1   1 ? 3 
ATOM   9022  C CD2   . TYR C 1 214 ? 50.748  0.418   59.280  1.000 31.560  0 214 TYR CCC CD2   1 ? 3 
ATOM   9023  C CE1   . TYR C 1 214 ? 51.825  -0.123  61.783  1.000 32.817  0 214 TYR CCC CE1   1 ? 3 
ATOM   9024  C CE2   . TYR C 1 214 ? 49.915  0.080   60.334  1.000 33.574  0 214 TYR CCC CE2   1 ? 3 
ATOM   9025  C CZ    . TYR C 1 214 ? 50.457  -0.194  61.587  1.000 34.914  0 214 TYR CCC CZ    1 ? 3 
ATOM   9026  O OH    . TYR C 1 214 ? 49.653  -0.529  62.640  1.000 40.850  0 214 TYR CCC OH    1 ? 3 
ATOM   9027  N N     . ILE C 1 215 ? 53.246  -2.388  58.259  1.000 27.490  0 215 ILE CCC N     1 ? 3 
ATOM   9028  C CA    . ILE C 1 215 ? 53.592  -3.646  58.984  1.000 27.006  0 215 ILE CCC CA    1 ? 3 
ATOM   9029  C C     . ILE C 1 215 ? 54.704  -4.349  58.184  1.000 27.764  0 215 ILE CCC C     1 ? 3 
ATOM   9030  O O     . ILE C 1 215 ? 55.713  -4.744  58.773  1.000 27.528  0 215 ILE CCC O     1 ? 3 
ATOM   9031  C CB    . ILE C 1 215 ? 52.340  -4.506  59.240  1.000 26.177  0 215 ILE CCC CB    1 ? 3 
ATOM   9032  C CG1   . ILE C 1 215 ? 51.371  -3.797  60.199  1.000 26.309  0 215 ILE CCC CG1   1 ? 3 
ATOM   9033  C CG2   . ILE C 1 215 ? 52.729  -5.850  59.804  1.000 25.485  0 215 ILE CCC CG2   1 ? 3 
ATOM   9034  C CD1   . ILE C 1 215 ? 49.907  -4.264  60.074  1.000 26.005  0 215 ILE CCC CD1   1 ? 3 
ATOM   9035  N N     . GLY C 1 216 ? 54.526  -4.480  56.866  1.000 27.432  0 216 GLY CCC N     1 ? 3 
ATOM   9036  C CA    . GLY C 1 216 ? 55.494  -5.093  55.945  1.000 27.828  0 216 GLY CCC CA    1 ? 3 
ATOM   9037  C C     . GLY C 1 216 ? 56.866  -4.428  55.996  1.000 28.562  0 216 GLY CCC C     1 ? 3 
ATOM   9038  O O     . GLY C 1 216 ? 57.898  -5.154  56.139  1.000 28.170  0 216 GLY CCC O     1 ? 3 
ATOM   9039  N N     . LEU C 1 217 ? 56.912  -3.101  55.875  1.000 27.912  0 217 LEU CCC N     1 ? 3 
ATOM   9040  C CA    . LEU C 1 217 ? 58.187  -2.360  55.827  1.000 27.732  0 217 LEU CCC CA    1 ? 3 
ATOM   9041  C C     . LEU C 1 217 ? 58.874  -2.475  57.191  1.000 27.739  0 217 LEU CCC C     1 ? 3 
ATOM   9042  O O     . LEU C 1 217 ? 60.106  -2.743  57.192  1.000 25.221  0 217 LEU CCC O     1 ? 3 
ATOM   9043  C CB    . LEU C 1 217 ? 57.947  -0.901  55.427  1.000 28.431  0 217 LEU CCC CB    1 ? 3 
ATOM   9044  C CG    . LEU C 1 217 ? 57.633  -0.647  53.953  1.000 29.169  0 217 LEU CCC CG    1 ? 3 
ATOM   9045  C CD1   . LEU C 1 217 ? 57.837  0.818   53.592  1.000 29.766  0 217 LEU CCC CD1   1 ? 3 
ATOM   9046  C CD2   . LEU C 1 217 ? 58.486  -1.504  53.047  1.000 31.185  0 217 LEU CCC CD2   1 ? 3 
ATOM   9047  N N     . GLU C 1 218 ? 58.135  -2.256  58.287  1.000 28.682  0 218 GLU CCC N     1 ? 3 
ATOM   9048  C CA    . GLU C 1 218 ? 58.683  -2.381  59.670  1.000 29.430  0 218 GLU CCC CA    1 ? 3 
ATOM   9049  C C     . GLU C 1 218 ? 59.281  -3.778  59.835  1.000 28.155  0 218 GLU CCC C     1 ? 3 
ATOM   9050  O O     . GLU C 1 218 ? 60.411  -3.872  60.317  1.000 26.231  0 218 GLU CCC O     1 ? 3 
ATOM   9051  C CB    . GLU C 1 218 ? 57.630  -2.194  60.763  1.000 30.400  0 218 GLU CCC CB    1 ? 3 
ATOM   9052  C CG    . GLU C 1 218 ? 57.144  -0.773  60.901  1.000 32.464  0 218 GLU CCC CG    1 ? 3 
ATOM   9053  C CD    . GLU C 1 218 ? 56.083  -0.606  61.983  1.000 34.634  0 218 GLU CCC CD    1 ? 3 
ATOM   9054  O OE1   . GLU C 1 218 ? 55.358  -1.601  62.308  1.000 35.382  0 218 GLU CCC OE1   1 ? 3 
ATOM   9055  O OE2   . GLU C 1 218 ? 55.936  0.554   62.450  1.000 38.299  0 218 GLU CCC OE2   1 ? 3 
ATOM   9056  N N     . THR C 1 219 ? 58.537  -4.807  59.440  1.000 27.874  0 219 THR CCC N     1 ? 3 
ATOM   9057  C CA    . THR C 1 219 ? 58.954  -6.221  59.611  1.000 29.712  0 219 THR CCC CA    1 ? 3 
ATOM   9058  C C     . THR C 1 219 ? 60.220  -6.496  58.791  1.000 28.885  0 219 THR CCC C     1 ? 3 
ATOM   9059  O O     . THR C 1 219 ? 61.180  -7.075  59.334  1.000 28.974  0 219 THR CCC O     1 ? 3 
ATOM   9060  C CB    . THR C 1 219 ? 57.808  -7.166  59.250  1.000 30.925  0 219 THR CCC CB    1 ? 3 
ATOM   9061  O OG1   . THR C 1 219 ? 56.667  -6.742  60.016  1.000 30.600  0 219 THR CCC OG1   1 ? 3 
ATOM   9062  C CG2   . THR C 1 219 ? 58.162  -8.616  59.529  1.000 31.220  0 219 THR CCC CG2   1 ? 3 
ATOM   9063  N N     . ALA C 1 220 ? 60.222  -6.096  57.528  1.000 29.476  0 220 ALA CCC N     1 ? 3 
ATOM   9064  C CA    . ALA C 1 220 ? 61.367  -6.315  56.619  1.000 29.804  0 220 ALA CCC CA    1 ? 3 
ATOM   9065  C C     . ALA C 1 220 ? 62.579  -5.540  57.159  1.000 30.431  0 220 ALA CCC C     1 ? 3 
ATOM   9066  O O     . ALA C 1 220 ? 63.705  -6.072  57.155  1.000 30.007  0 220 ALA CCC O     1 ? 3 
ATOM   9067  C CB    . ALA C 1 220 ? 60.996  -5.878  55.232  1.000 28.823  0 220 ALA CCC CB    1 ? 3 
ATOM   9068  N N     . GLY C 1 221 ? 62.327  -4.315  57.605  1.000 30.622  0 221 GLY CCC N     1 ? 3 
ATOM   9069  C CA    . GLY C 1 221 ? 63.339  -3.418  58.182  1.000 31.922  0 221 GLY CCC CA    1 ? 3 
ATOM   9070  C C     . GLY C 1 221 ? 64.052  -4.041  59.364  1.000 31.979  0 221 GLY CCC C     1 ? 3 
ATOM   9071  O O     . GLY C 1 221 ? 65.325  -4.012  59.363  1.000 38.970  0 221 GLY CCC O     1 ? 3 
ATOM   9072  N N     . PHE C 1 222 ? 63.337  -4.626  60.321  1.000 29.222  0 222 PHE CCC N     1 ? 3 
ATOM   9073  C CA    . PHE C 1 222 ? 64.031  -5.225  61.491  1.000 30.084  0 222 PHE CCC CA    1 ? 3 
ATOM   9074  C C     . PHE C 1 222 ? 64.660  -6.574  61.092  1.000 31.141  0 222 PHE CCC C     1 ? 3 
ATOM   9075  O O     . PHE C 1 222 ? 65.793  -6.889  61.555  1.000 30.473  0 222 PHE CCC O     1 ? 3 
ATOM   9076  C CB    . PHE C 1 222 ? 63.190  -5.160  62.776  1.000 29.881  0 222 PHE CCC CB    1 ? 3 
ATOM   9077  C CG    . PHE C 1 222 ? 61.991  -6.075  62.861  1.000 28.810  0 222 PHE CCC CG    1 ? 3 
ATOM   9078  C CD1   . PHE C 1 222 ? 62.146  -7.442  62.899  1.000 28.992  0 222 PHE CCC CD1   1 ? 3 
ATOM   9079  C CD2   . PHE C 1 222 ? 60.721  -5.551  62.986  1.000 28.004  0 222 PHE CCC CD2   1 ? 3 
ATOM   9080  C CE1   . PHE C 1 222 ? 61.054  -8.282  62.986  1.000 29.494  0 222 PHE CCC CE1   1 ? 3 
ATOM   9081  C CE2   . PHE C 1 222 ? 59.627  -6.390  63.100  1.000 29.866  0 222 PHE CCC CE2   1 ? 3 
ATOM   9082  C CZ    . PHE C 1 222 ? 59.786  -7.760  63.074  1.000 29.744  0 222 PHE CCC CZ    1 ? 3 
ATOM   9083  N N     . LEU C 1 223 ? 64.039  -7.358  60.210  1.000 31.507  0 223 LEU CCC N     1 ? 3 
ATOM   9084  C CA    . LEU C 1 223 ? 64.677  -8.656  59.829  1.000 31.964  0 223 LEU CCC CA    1 ? 3 
ATOM   9085  C C     . LEU C 1 223 ? 66.005  -8.388  59.104  1.000 32.348  0 223 LEU CCC C     1 ? 3 
ATOM   9086  O O     . LEU C 1 223 ? 66.996  -9.099  59.370  1.000 34.651  0 223 LEU CCC O     1 ? 3 
ATOM   9087  C CB    . LEU C 1 223 ? 63.724  -9.504  58.990  1.000 31.283  0 223 LEU CCC CB    1 ? 3 
ATOM   9088  C CG    . LEU C 1 223 ? 62.532  -10.061 59.740  1.000 30.825  0 223 LEU CCC CG    1 ? 3 
ATOM   9089  C CD1   . LEU C 1 223 ? 61.653  -10.864 58.799  1.000 31.871  0 223 LEU CCC CD1   1 ? 3 
ATOM   9090  C CD2   . LEU C 1 223 ? 62.959  -10.913 60.918  1.000 29.973  0 223 LEU CCC CD2   1 ? 3 
ATOM   9091  N N     . ASN C 1 224 ? 66.049  -7.377  58.242  1.000 32.858  0 224 ASN CCC N     1 ? 3 
ATOM   9092  C CA    . ASN C 1 224 ? 67.302  -6.987  57.531  1.000 32.948  0 224 ASN CCC CA    1 ? 3 
ATOM   9093  C C     . ASN C 1 224 ? 68.329  -6.473  58.544  1.000 31.995  0 224 ASN CCC C     1 ? 3 
ATOM   9094  O O     . ASN C 1 224 ? 69.455  -6.943  58.506  1.000 35.226  0 224 ASN CCC O     1 ? 3 
ATOM   9095  C CB    . ASN C 1 224 ? 67.042  -5.940  56.446  1.000 32.231  0 224 ASN CCC CB    1 ? 3 
ATOM   9096  C CG    . ASN C 1 224 ? 68.288  -5.581  55.690  1.000 32.121  0 224 ASN CCC CG    1 ? 3 
ATOM   9097  O OD1   . ASN C 1 224 ? 68.719  -6.339  54.832  1.000 35.789  0 224 ASN CCC OD1   1 ? 3 
ATOM   9098  N ND2   . ASN C 1 224 ? 68.851  -4.420  55.975  1.000 31.457  0 224 ASN CCC ND2   1 ? 3 
ATOM   9099  N N     . GLU C 1 225 ? 67.950  -5.555  59.424  1.000 32.217  0 225 GLU CCC N     1 ? 3 
ATOM   9100  C CA    . GLU C 1 225 ? 68.872  -4.987  60.443  0.940 32.578  0 225 GLU CCC CA    1 ? 3 
ATOM   9101  C C     . GLU C 1 225 ? 69.452  -6.118  61.286  1.000 31.591  0 225 GLU CCC C     1 ? 3 
ATOM   9102  O O     . GLU C 1 225 ? 70.641  -5.965  61.715  1.000 33.846  0 225 GLU CCC O     1 ? 3 
ATOM   9103  C CB    . GLU C 1 225 ? 68.198  -3.944  61.338  0.940 33.746  0 225 GLU CCC CB    1 ? 3 
ATOM   9104  C CG    . GLU C 1 225 ? 68.491  -2.519  60.908  0.940 35.831  0 225 GLU CCC CG    1 ? 3 
ATOM   9105  C CD    . GLU C 1 225 ? 67.826  -1.427  61.735  0.940 38.073  0 225 GLU CCC CD    1 ? 3 
ATOM   9106  O OE1   . GLU C 1 225 ? 66.540  -1.338  61.738  0.940 37.046  0 225 GLU CCC OE1   1 ? 3 
ATOM   9107  O OE2   . GLU C 1 225 ? 68.594  -0.640  62.353  0.940 38.801  0 225 GLU CCC OE2   1 ? 3 
ATOM   9108  N N     . LEU C 1 226 ? 68.695  -7.199  61.485  1.000 29.605  0 226 LEU CCC N     1 ? 3 
ATOM   9109  C CA    . LEU C 1 226 ? 69.096  -8.311  62.373  1.000 29.892  0 226 LEU CCC CA    1 ? 3 
ATOM   9110  C C     . LEU C 1 226 ? 69.927  -9.334  61.601  1.000 32.423  0 226 LEU CCC C     1 ? 3 
ATOM   9111  O O     . LEU C 1 226 ? 70.278  -10.368 62.209  1.000 34.450  0 226 LEU CCC O     1 ? 3 
ATOM   9112  C CB    . LEU C 1 226 ? 67.850  -8.960  62.994  1.000 28.701  0 226 LEU CCC CB    1 ? 3 
ATOM   9113  C CG    . LEU C 1 226 ? 67.229  -8.189  64.158  1.000 27.391  0 226 LEU CCC CG    1 ? 3 
ATOM   9114  C CD1   . LEU C 1 226 ? 65.960  -8.863  64.623  1.000 28.468  0 226 LEU CCC CD1   1 ? 3 
ATOM   9115  C CD2   . LEU C 1 226 ? 68.168  -8.071  65.322  1.000 27.335  0 226 LEU CCC CD2   1 ? 3 
ATOM   9116  N N     . GLY C 1 227 ? 70.174  -9.086  60.313  1.000 35.479  0 227 GLY CCC N     1 ? 3 
ATOM   9117  C CA    . GLY C 1 227 ? 71.149  -9.831  59.485  1.000 35.953  0 227 GLY CCC CA    1 ? 3 
ATOM   9118  C C     . GLY C 1 227 ? 70.497  -10.855 58.568  1.000 36.801  0 227 GLY CCC C     1 ? 3 
ATOM   9119  O O     . GLY C 1 227 ? 71.257  -11.552 57.894  1.000 35.647  0 227 GLY CCC O     1 ? 3 
ATOM   9120  N N     . PHE C 1 228 ? 69.153  -10.936 58.515  1.000 38.914  0 228 PHE CCC N     1 ? 3 
ATOM   9121  C CA    . PHE C 1 228 ? 68.439  -11.912 57.652  1.000 39.665  0 228 PHE CCC CA    1 ? 3 
ATOM   9122  C C     . PHE C 1 228 ? 68.365  -11.403 56.202  1.000 39.077  0 228 PHE CCC C     1 ? 3 
ATOM   9123  O O     . PHE C 1 228 ? 68.238  -10.189 56.001  1.000 39.476  0 228 PHE CCC O     1 ? 3 
ATOM   9124  C CB    . PHE C 1 228 ? 67.076  -12.233 58.243  1.000 40.655  0 228 PHE CCC CB    1 ? 3 
ATOM   9125  C CG    . PHE C 1 228 ? 67.171  -12.880 59.598  1.000 43.207  0 228 PHE CCC CG    1 ? 3 
ATOM   9126  C CD1   . PHE C 1 228 ? 67.693  -14.150 59.737  1.000 44.599  0 228 PHE CCC CD1   1 ? 3 
ATOM   9127  C CD2   . PHE C 1 228 ? 66.744  -12.216 60.735  1.000 43.934  0 228 PHE CCC CD2   1 ? 3 
ATOM   9128  C CE1   . PHE C 1 228 ? 67.774  -14.750 60.986  1.000 46.223  0 228 PHE CCC CE1   1 ? 3 
ATOM   9129  C CE2   . PHE C 1 228 ? 66.832  -12.812 61.983  1.000 44.561  0 228 PHE CCC CE2   1 ? 3 
ATOM   9130  C CZ    . PHE C 1 228 ? 67.361  -14.074 62.113  1.000 44.443  0 228 PHE CCC CZ    1 ? 3 
ATOM   9131  N N     . ASP C 1 229 ? 68.469  -12.325 55.234  1.000 39.337  0 229 ASP CCC N     1 ? 3 
ATOM   9132  C CA    . ASP C 1 229 ? 68.316  -12.080 53.770  1.000 39.282  0 229 ASP CCC CA    1 ? 3 
ATOM   9133  C C     . ASP C 1 229 ? 66.847  -11.766 53.518  1.000 38.412  0 229 ASP CCC C     1 ? 3 
ATOM   9134  O O     . ASP C 1 229 ? 65.982  -12.656 53.714  1.000 37.169  0 229 ASP CCC O     1 ? 3 
ATOM   9135  C CB    . ASP C 1 229 ? 68.801  -13.283 52.957  1.000 42.646  0 229 ASP CCC CB    1 ? 3 
ATOM   9136  C CG    . ASP C 1 229 ? 68.745  -13.158 51.439  1.000 44.932  0 229 ASP CCC CG    1 ? 3 
ATOM   9137  O OD1   . ASP C 1 229 ? 67.924  -12.368 50.915  1.000 46.989  0 229 ASP CCC OD1   1 ? 3 
ATOM   9138  O OD2   . ASP C 1 229 ? 69.505  -13.883 50.788  1.000 47.289  0 229 ASP CCC OD2   1 ? 3 
ATOM   9139  N N     . THR C 1 230 ? 66.571  -10.519 53.167  1.000 36.851  0 230 THR CCC N     1 ? 3 
ATOM   9140  C CA    . THR C 1 230 ? 65.219  -9.957  53.248  1.000 36.108  0 230 THR CCC CA    1 ? 3 
ATOM   9141  C C     . THR C 1 230 ? 64.806  -9.390  51.896  1.000 34.925  0 230 THR CCC C     1 ? 3 
ATOM   9142  O O     . THR C 1 230 ? 65.574  -8.577  51.338  1.000 34.635  0 230 THR CCC O     1 ? 3 
ATOM   9143  C CB    . THR C 1 230 ? 65.140  -8.943  54.399  1.000 35.343  0 230 THR CCC CB    1 ? 3 
ATOM   9144  O OG1   . THR C 1 230 ? 65.391  -9.685  55.597  1.000 34.939  0 230 THR CCC OG1   1 ? 3 
ATOM   9145  C CG2   . THR C 1 230 ? 63.776  -8.288  54.496  1.000 34.707  0 230 THR CCC CG2   1 ? 3 
ATOM   9146  N N     . THR C 1 231 ? 63.572  -9.704  51.481  1.000 33.614  0 231 THR CCC N     1 ? 3 
ATOM   9147  C CA    . THR C 1 231 ? 62.999  -9.266  50.188  1.000 34.160  0 231 THR CCC CA    1 ? 3 
ATOM   9148  C C     . THR C 1 231 ? 61.571  -8.797  50.448  1.000 34.438  0 231 THR CCC C     1 ? 3 
ATOM   9149  O O     . THR C 1 231 ? 60.842  -9.500  51.175  1.000 36.093  0 231 THR CCC O     1 ? 3 
ATOM   9150  C CB    . THR C 1 231 ? 63.135  -10.398 49.161  1.000 34.256  0 231 THR CCC CB    1 ? 3 
ATOM   9151  O OG1   . THR C 1 231 ? 64.527  -10.772 49.075  1.000 35.797  0 231 THR CCC OG1   1 ? 3 
ATOM   9152  C CG2   . THR C 1 231 ? 62.618  -10.024 47.795  1.000 33.983  0 231 THR CCC CG2   1 ? 3 
ATOM   9153  N N     . VAL C 1 232 ? 61.202  -7.634  49.917  1.000 33.485  0 232 VAL CCC N     1 ? 3 
ATOM   9154  C CA    . VAL C 1 232 ? 59.813  -7.117  49.965  1.000 34.533  0 232 VAL CCC CA    1 ? 3 
ATOM   9155  C C     . VAL C 1 232 ? 59.218  -7.194  48.551  1.000 36.953  0 232 VAL CCC C     1 ? 3 
ATOM   9156  O O     . VAL C 1 232 ? 59.841  -6.589  47.652  1.000 35.311  0 232 VAL CCC O     1 ? 3 
ATOM   9157  C CB    . VAL C 1 232 ? 59.777  -5.680  50.508  1.000 33.638  0 232 VAL CCC CB    1 ? 3 
ATOM   9158  C CG1   . VAL C 1 232 ? 58.399  -5.048  50.289  1.000 35.342  0 232 VAL CCC CG1   1 ? 3 
ATOM   9159  C CG2   . VAL C 1 232 ? 60.141  -5.645  51.979  1.000 32.246  0 232 VAL CCC CG2   1 ? 3 
ATOM   9160  N N     . ALA C 1 233 ? 58.076  -7.885  48.397  1.000 37.713  0 233 ALA CCC N     1 ? 3 
ATOM   9161  C CA    . ALA C 1 233 ? 57.207  -7.891  47.192  1.000 40.257  0 233 ALA CCC CA    1 ? 3 
ATOM   9162  C C     . ALA C 1 233 ? 56.184  -6.775  47.346  1.000 41.231  0 233 ALA CCC C     1 ? 3 
ATOM   9163  O O     . ALA C 1 233 ? 55.267  -6.915  48.174  1.000 43.490  0 233 ALA CCC O     1 ? 3 
ATOM   9164  C CB    . ALA C 1 233 ? 56.499  -9.216  47.002  1.000 41.429  0 233 ALA CCC CB    1 ? 3 
ATOM   9165  N N     . MET C 1 234 ? 56.401  -5.688  46.619  1.000 42.438  0 234 MET CCC N     1 ? 3 
ATOM   9166  C CA    . MET C 1 234 ? 55.615  -4.441  46.645  1.000 41.970  0 234 MET CCC CA    1 ? 3 
ATOM   9167  C C     . MET C 1 234 ? 54.790  -4.426  45.351  1.000 41.606  0 234 MET CCC C     1 ? 3 
ATOM   9168  O O     . MET C 1 234 ? 55.381  -4.359  44.246  1.000 38.839  0 234 MET CCC O     1 ? 3 
ATOM   9169  C CB    . MET C 1 234 ? 56.579  -3.256  46.703  1.000 44.254  0 234 MET CCC CB    1 ? 3 
ATOM   9170  C CG    . MET C 1 234 ? 55.918  -1.918  46.537  1.000 45.755  0 234 MET CCC CG    1 ? 3 
ATOM   9171  S SD    . MET C 1 234 ? 56.913  -0.561  47.195  1.000 50.319  0 234 MET CCC SD    1 ? 3 
ATOM   9172  C CE    . MET C 1 234 ? 58.380  -0.621  46.173  1.000 52.000  0 234 MET CCC CE    1 ? 3 
ATOM   9173  N N     . ARG C 1 235 ? 53.470  -4.590  45.467  1.000 40.645  0 235 ARG CCC N     1 ? 3 
ATOM   9174  C CA    . ARG C 1 235 ? 52.555  -4.592  44.299  1.000 40.626  0 235 ARG CCC CA    1 ? 3 
ATOM   9175  C C     . ARG C 1 235 ? 52.701  -3.263  43.522  1.000 40.603  0 235 ARG CCC C     1 ? 3 
ATOM   9176  O O     . ARG C 1 235 ? 52.743  -3.304  42.270  1.000 41.526  0 235 ARG CCC O     1 ? 3 
ATOM   9177  C CB    . ARG C 1 235 ? 51.124  -4.842  44.751  1.000 41.093  0 235 ARG CCC CB    1 ? 3 
ATOM   9178  C CG    . ARG C 1 235 ? 50.171  -5.000  43.584  1.000 43.134  0 235 ARG CCC CG    1 ? 3 
ATOM   9179  C CD    . ARG C 1 235 ? 48.730  -5.336  43.945  1.000 43.698  0 235 ARG CCC CD    1 ? 3 
ATOM   9180  N NE    . ARG C 1 235 ? 48.123  -5.849  42.730  1.000 45.590  0 235 ARG CCC NE    1 ? 3 
ATOM   9181  C CZ    . ARG C 1 235 ? 47.752  -5.100  41.694  1.000 47.616  0 235 ARG CCC CZ    1 ? 3 
ATOM   9182  N NH1   . ARG C 1 235 ? 47.871  -3.780  41.736  1.000 47.107  0 235 ARG CCC NH1   1 ? 3 
ATOM   9183  N NH2   . ARG C 1 235 ? 47.202  -5.670  40.635  1.000 51.439  0 235 ARG CCC NH2   1 ? 3 
ATOM   9184  N N     . SER C 1 236 ? 52.788  -2.109  44.189  1.000 38.374  0 236 SER CCC N     1 ? 3 
ATOM   9185  C CA    . SER C 1 236 ? 52.879  -0.799  43.490  1.000 37.967  0 236 SER CCC CA    1 ? 3 
ATOM   9186  C C     . SER C 1 236 ? 53.799  0.147   44.243  1.000 37.577  0 236 SER CCC C     1 ? 3 
ATOM   9187  O O     . SER C 1 236 ? 54.975  0.249   43.868  1.000 37.932  0 236 SER CCC O     1 ? 3 
ATOM   9188  C CB    . SER C 1 236 ? 51.497  -0.178  43.248  1.000 38.326  0 236 SER CCC CB    1 ? 3 
ATOM   9189  O OG    . SER C 1 236 ? 50.728  -0.196  44.426  1.000 33.858  0 236 SER CCC OG    1 ? 3 
ATOM   9190  N N     . ILE C 1 237 ? 53.281  0.797   45.288  1.000 37.487  0 237 ILE CCC N     1 ? 3 
ATOM   9191  C CA    . ILE C 1 237 ? 53.984  1.915   45.982  1.000 35.119  0 237 ILE CCC CA    1 ? 3 
ATOM   9192  C C     . ILE C 1 237 ? 54.056  1.602   47.469  1.000 34.951  0 237 ILE CCC C     1 ? 3 
ATOM   9193  O O     . ILE C 1 237 ? 53.220  0.866   47.992  1.000 35.185  0 237 ILE CCC O     1 ? 3 
ATOM   9194  C CB    . ILE C 1 237 ? 53.280  3.251   45.683  1.000 33.784  0 237 ILE CCC CB    1 ? 3 
ATOM   9195  C CG1   . ILE C 1 237 ? 51.830  3.248   46.212  1.000 32.301  0 237 ILE CCC CG1   1 ? 3 
ATOM   9196  C CG2   . ILE C 1 237 ? 53.381  3.589   44.185  1.000 32.575  0 237 ILE CCC CG2   1 ? 3 
ATOM   9197  C CD1   . ILE C 1 237 ? 51.139  4.608   46.174  1.000 31.270  0 237 ILE CCC CD1   1 ? 3 
ATOM   9198  N N     . PRO C 1 238 ? 55.075  2.141   48.169  1.000 34.162  0 238 PRO CCC N     1 ? 3 
ATOM   9199  C CA    . PRO C 1 238 ? 55.212  1.977   49.620  1.000 34.312  0 238 PRO CCC CA    1 ? 3 
ATOM   9200  C C     . PRO C 1 238 ? 54.296  2.866   50.460  1.000 32.795  0 238 PRO CCC C     1 ? 3 
ATOM   9201  O O     . PRO C 1 238 ? 54.140  4.021   50.141  1.000 32.364  0 238 PRO CCC O     1 ? 3 
ATOM   9202  C CB    . PRO C 1 238 ? 56.682  2.399   49.889  1.000 34.101  0 238 PRO CCC CB    1 ? 3 
ATOM   9203  C CG    . PRO C 1 238 ? 56.993  3.367   48.764  1.000 34.324  0 238 PRO CCC CG    1 ? 3 
ATOM   9204  C CD    . PRO C 1 238 ? 56.190  2.903   47.577  1.000 35.516  0 238 PRO CCC CD    1 ? 3 
ATOM   9205  N N     . LEU C 1 239 ? 53.734  2.317   51.531  1.000 32.455  0 239 LEU CCC N     1 ? 3 
ATOM   9206  C CA    . LEU C 1 239 ? 52.919  3.096   52.508  1.000 31.942  0 239 LEU CCC CA    1 ? 3 
ATOM   9207  C C     . LEU C 1 239 ? 51.845  3.890   51.766  1.000 32.918  0 239 LEU CCC C     1 ? 3 
ATOM   9208  O O     . LEU C 1 239 ? 51.816  5.127   51.869  1.000 31.848  0 239 LEU CCC O     1 ? 3 
ATOM   9209  C CB    . LEU C 1 239 ? 53.854  4.030   53.266  1.000 31.587  0 239 LEU CCC CB    1 ? 3 
ATOM   9210  C CG    . LEU C 1 239 ? 54.995  3.331   54.002  1.000 31.470  0 239 LEU CCC CG    1 ? 3 
ATOM   9211  C CD1   . LEU C 1 239 ? 55.922  4.339   54.655  1.000 30.915  0 239 LEU CCC CD1   1 ? 3 
ATOM   9212  C CD2   . LEU C 1 239 ? 54.424  2.361   55.033  1.000 31.874  0 239 LEU CCC CD2   1 ? 3 
ATOM   9213  N N     . ARG C 1 240 ? 51.008  3.184   51.016  1.000 34.905  0 240 ARG CCC N     1 ? 3 
ATOM   9214  C CA    A ARG C 1 240 ? 49.861  3.778   50.285  0.500 35.146  0 240 ARG CCC CA    1 ? 3 
ATOM   9215  C CA    B ARG C 1 240 ? 49.832  3.745   50.294  0.500 35.352  0 240 ARG CCC CA    1 ? 3 
ATOM   9216  C C     . ARG C 1 240 ? 49.015  4.639   51.240  1.000 33.960  0 240 ARG CCC C     1 ? 3 
ATOM   9217  O O     . ARG C 1 240 ? 48.639  4.147   52.291  1.000 35.404  0 240 ARG CCC O     1 ? 3 
ATOM   9218  C CB    A ARG C 1 240 ? 49.050  2.650   49.646  0.500 35.088  0 240 ARG CCC CB    1 ? 3 
ATOM   9219  C CB    B ARG C 1 240 ? 49.014  2.562   49.752  0.500 35.512  0 240 ARG CCC CB    1 ? 3 
ATOM   9220  C CG    A ARG C 1 240 ? 48.064  3.143   48.605  0.500 35.198  0 240 ARG CCC CG    1 ? 3 
ATOM   9221  C CG    B ARG C 1 240 ? 47.825  2.917   48.870  0.500 35.961  0 240 ARG CCC CG    1 ? 3 
ATOM   9222  C CD    A ARG C 1 240 ? 47.366  2.032   47.844  0.500 34.010  0 240 ARG CCC CD    1 ? 3 
ATOM   9223  C CD    B ARG C 1 240 ? 46.475  2.509   49.458  0.500 34.319  0 240 ARG CCC CD    1 ? 3 
ATOM   9224  N NE    A ARG C 1 240 ? 48.098  1.606   46.654  0.500 32.711  0 240 ARG CCC NE    1 ? 3 
ATOM   9225  N NE    B ARG C 1 240 ? 46.091  3.370   50.565  0.500 32.913  0 240 ARG CCC NE    1 ? 3 
ATOM   9226  C CZ    A ARG C 1 240 ? 48.137  2.284   45.516  0.500 31.921  0 240 ARG CCC CZ    1 ? 3 
ATOM   9227  C CZ    B ARG C 1 240 ? 45.801  2.937   51.779  0.500 31.241  0 240 ARG CCC CZ    1 ? 3 
ATOM   9228  N NH1   A ARG C 1 240 ? 47.562  3.468   45.400  0.500 31.436  0 240 ARG CCC NH1   1 ? 3 
ATOM   9229  N NH1   B ARG C 1 240 ? 45.497  3.805   52.720  0.500 30.158  0 240 ARG CCC NH1   1 ? 3 
ATOM   9230  N NH2   A ARG C 1 240 ? 48.837  1.810   44.508  0.500 32.903  0 240 ARG CCC NH2   1 ? 3 
ATOM   9231  N NH2   B ARG C 1 240 ? 45.810  1.644   52.042  0.500 31.115  0 240 ARG CCC NH2   1 ? 3 
ATOM   9232  N N     . GLY C 1 241 ? 48.744  5.885   50.835  1.000 34.186  0 241 GLY CCC N     1 ? 3 
ATOM   9233  C CA    . GLY C 1 241 ? 47.991  6.914   51.562  1.000 33.491  0 241 GLY CCC CA    1 ? 3 
ATOM   9234  C C     . GLY C 1 241 ? 48.899  7.899   52.264  1.000 35.201  0 241 GLY CCC C     1 ? 3 
ATOM   9235  O O     . GLY C 1 241 ? 48.442  8.993   52.563  1.000 40.002  0 241 GLY CCC O     1 ? 3 
ATOM   9236  N N     . PHE C 1 242 ? 50.131  7.513   52.566  1.000 35.012  0 242 PHE CCC N     1 ? 3 
ATOM   9237  C CA    . PHE C 1 242 ? 51.142  8.363   53.265  1.000 33.007  0 242 PHE CCC CA    1 ? 3 
ATOM   9238  C C     . PHE C 1 242 ? 51.848  9.263   52.242  1.000 31.910  0 242 PHE CCC C     1 ? 3 
ATOM   9239  O O     . PHE C 1 242 ? 51.884  8.937   51.031  1.000 30.334  0 242 PHE CCC O     1 ? 3 
ATOM   9240  C CB    . PHE C 1 242 ? 52.174  7.491   53.986  1.000 32.420  0 242 PHE CCC CB    1 ? 3 
ATOM   9241  C CG    . PHE C 1 242 ? 51.688  6.760   55.219  1.000 33.530  0 242 PHE CCC CG    1 ? 3 
ATOM   9242  C CD1   . PHE C 1 242 ? 50.638  5.852   55.150  1.000 31.760  0 242 PHE CCC CD1   1 ? 3 
ATOM   9243  C CD2   . PHE C 1 242 ? 52.307  6.974   56.457  1.000 31.792  0 242 PHE CCC CD2   1 ? 3 
ATOM   9244  C CE1   . PHE C 1 242 ? 50.206  5.200   56.297  1.000 34.089  0 242 PHE CCC CE1   1 ? 3 
ATOM   9245  C CE2   . PHE C 1 242 ? 51.885  6.295   57.586  1.000 31.563  0 242 PHE CCC CE2   1 ? 3 
ATOM   9246  C CZ    . PHE C 1 242 ? 50.844  5.403   57.512  1.000 31.973  0 242 PHE CCC CZ    1 ? 3 
ATOM   9247  N N     . ASP C 1 243 ? 52.436  10.350  52.725  1.000 30.388  0 243 ASP CCC N     1 ? 3 
ATOM   9248  C CA    . ASP C 1 243 ? 53.218  11.317  51.908  1.000 30.270  0 243 ASP CCC CA    1 ? 3 
ATOM   9249  C C     . ASP C 1 243 ? 54.214  10.587  51.017  1.000 29.816  0 243 ASP CCC C     1 ? 3 
ATOM   9250  O O     . ASP C 1 243 ? 54.962  9.754   51.570  1.000 31.257  0 243 ASP CCC O     1 ? 3 
ATOM   9251  C CB    . ASP C 1 243 ? 53.975  12.262  52.813  1.000 30.568  0 243 ASP CCC CB    1 ? 3 
ATOM   9252  C CG    . ASP C 1 243 ? 54.740  13.310  52.069  1.000 32.259  0 243 ASP CCC CG    1 ? 3 
ATOM   9253  O OD1   . ASP C 1 243 ? 54.086  14.236  51.588  1.000 32.747  0 243 ASP CCC OD1   1 ? 3 
ATOM   9254  O OD2   . ASP C 1 243 ? 55.992  13.170  51.964  1.000 35.460  0 243 ASP CCC OD2   1 ? 3 
ATOM   9255  N N     . ARG C 1 244 ? 54.225  10.901  49.711  1.000 28.827  0 244 ARG CCC N     1 ? 3 
ATOM   9256  C CA    . ARG C 1 244 ? 55.037  10.156  48.716  1.000 30.792  0 244 ARG CCC CA    1 ? 3 
ATOM   9257  C C     . ARG C 1 244 ? 56.519  10.358  49.008  1.000 29.099  0 244 ARG CCC C     1 ? 3 
ATOM   9258  O O     . ARG C 1 244 ? 57.231  9.354   49.120  1.000 29.397  0 244 ARG CCC O     1 ? 3 
ATOM   9259  C CB    . ARG C 1 244 ? 54.710  10.543  47.262  1.000 33.815  0 244 ARG CCC CB    1 ? 3 
ATOM   9260  C CG    . ARG C 1 244 ? 53.326  10.105  46.798  1.000 36.138  0 244 ARG CCC CG    1 ? 3 
ATOM   9261  C CD    . ARG C 1 244 ? 53.222  8.581   46.717  1.000 37.768  0 244 ARG CCC CD    1 ? 3 
ATOM   9262  N NE    . ARG C 1 244 ? 52.847  8.009   48.000  1.000 37.090  0 244 ARG CCC NE    1 ? 3 
ATOM   9263  C CZ    . ARG C 1 244 ? 53.290  6.870   48.510  1.000 36.912  0 244 ARG CCC CZ    1 ? 3 
ATOM   9264  N NH1   . ARG C 1 244 ? 54.165  6.122   47.867  1.000 37.250  0 244 ARG CCC NH1   1 ? 3 
ATOM   9265  N NH2   . ARG C 1 244 ? 52.858  6.474   49.698  1.000 38.139  0 244 ARG CCC NH2   1 ? 3 
ATOM   9266  N N     . GLN C 1 245 ? 56.945  11.607  49.139  1.000 29.520  0 245 GLN CCC N     1 ? 3 
ATOM   9267  C CA    . GLN C 1 245 ? 58.359  12.006  49.323  1.000 29.698  0 245 GLN CCC CA    1 ? 3 
ATOM   9268  C C     . GLN C 1 245 ? 58.940  11.227  50.517  1.000 31.508  0 245 GLN CCC C     1 ? 3 
ATOM   9269  O O     . GLN C 1 245 ? 60.031  10.614  50.341  1.000 32.010  0 245 GLN CCC O     1 ? 3 
ATOM   9270  C CB    . GLN C 1 245 ? 58.476  13.511  49.559  1.000 29.962  0 245 GLN CCC CB    1 ? 3 
ATOM   9271  C CG    . GLN C 1 245 ? 59.921  13.985  49.479  1.000 30.966  0 245 GLN CCC CG    1 ? 3 
ATOM   9272  C CD    . GLN C 1 245 ? 60.049  15.466  49.721  1.000 31.906  0 245 GLN CCC CD    1 ? 3 
ATOM   9273  O OE1   . GLN C 1 245 ? 59.130  16.120  50.194  1.000 34.207  0 245 GLN CCC OE1   1 ? 3 
ATOM   9274  N NE2   . GLN C 1 245 ? 61.194  16.020  49.406  1.000 33.654  0 245 GLN CCC NE2   1 ? 3 
ATOM   9275  N N     . CYS C 1 246 ? 58.252  11.232  51.668  1.000 29.601  0 246 CYS CCC N     1 ? 3 
ATOM   9276  C CA    . CYS C 1 246 ? 58.688  10.521  52.893  1.000 30.943  0 246 CYS CCC CA    1 ? 3 
ATOM   9277  C C     . CYS C 1 246 ? 58.674  9.009   52.688  1.000 31.753  0 246 CYS CCC C     1 ? 3 
ATOM   9278  O O     . CYS C 1 246 ? 59.679  8.333   53.072  1.000 36.727  0 246 CYS CCC O     1 ? 3 
ATOM   9279  C CB    . CYS C 1 246 ? 57.822  10.838  54.099  1.000 31.290  0 246 CYS CCC CB    1 ? 3 
ATOM   9280  S SG    . CYS C 1 246 ? 57.981  12.559  54.596  1.000 34.948  0 246 CYS CCC SG    1 ? 3 
ATOM   9281  N N     . SER C 1 247 ? 57.598  8.466   52.139  1.000 31.307  0 247 SER CCC N     1 ? 3 
ATOM   9282  C CA    . SER C 1 247 ? 57.497  6.996   51.930  1.000 30.926  0 247 SER CCC CA    1 ? 3 
ATOM   9283  C C     . SER C 1 247 ? 58.675  6.535   51.048  1.000 31.363  0 247 SER CCC C     1 ? 3 
ATOM   9284  O O     . SER C 1 247 ? 59.228  5.467   51.314  1.000 31.482  0 247 SER CCC O     1 ? 3 
ATOM   9285  C CB    . SER C 1 247 ? 56.137  6.627   51.381  1.000 30.169  0 247 SER CCC CB    1 ? 3 
ATOM   9286  O OG    . SER C 1 247 ? 55.085  7.052   52.244  1.000 26.880  0 247 SER CCC OG    1 ? 3 
ATOM   9287  N N     . GLU C 1 248 ? 59.114  7.356   50.094  1.000 32.870  0 248 GLU CCC N     1 ? 3 
ATOM   9288  C CA    . GLU C 1 248 ? 60.161  6.962   49.115  1.000 36.335  0 248 GLU CCC CA    1 ? 3 
ATOM   9289  C C     . GLU C 1 248 ? 61.563  7.111   49.737  1.000 34.810  0 248 GLU CCC C     1 ? 3 
ATOM   9290  O O     . GLU C 1 248 ? 62.433  6.260   49.475  1.000 32.555  0 248 GLU CCC O     1 ? 3 
ATOM   9291  C CB    . GLU C 1 248 ? 60.017  7.765   47.821  1.000 39.885  0 248 GLU CCC CB    1 ? 3 
ATOM   9292  C CG    . GLU C 1 248 ? 58.857  7.305   46.924  1.000 42.159  0 248 GLU CCC CG    1 ? 3 
ATOM   9293  C CD    . GLU C 1 248 ? 58.498  8.366   45.888  1.000 43.745  0 248 GLU CCC CD    1 ? 3 
ATOM   9294  O OE1   . GLU C 1 248 ? 59.357  9.273   45.652  1.000 46.599  0 248 GLU CCC OE1   1 ? 3 
ATOM   9295  O OE2   . GLU C 1 248 ? 57.358  8.336   45.363  1.000 44.675  0 248 GLU CCC OE2   1 ? 3 
ATOM   9296  N N     . LYS C 1 249 ? 61.765  8.135   50.563  1.000 34.835  0 249 LYS CCC N     1 ? 3 
ATOM   9297  C CA    . LYS C 1 249 ? 62.995  8.232   51.386  1.000 34.960  0 249 LYS CCC CA    1 ? 3 
ATOM   9298  C C     . LYS C 1 249 ? 63.181  6.939   52.198  1.000 32.528  0 249 LYS CCC C     1 ? 3 
ATOM   9299  O O     . LYS C 1 249 ? 64.299  6.375   52.185  1.000 32.010  0 249 LYS CCC O     1 ? 3 
ATOM   9300  C CB    . LYS C 1 249 ? 62.997  9.420   52.346  1.000 35.874  0 249 LYS CCC CB    1 ? 3 
ATOM   9301  C CG    . LYS C 1 249 ? 64.369  9.557   52.993  1.000 36.412  0 249 LYS CCC CG    1 ? 3 
ATOM   9302  C CD    . LYS C 1 249 ? 64.578  10.789  53.809  1.000 35.943  0 249 LYS CCC CD    1 ? 3 
ATOM   9303  C CE    . LYS C 1 249 ? 65.975  10.838  54.405  1.000 35.867  0 249 LYS CCC CE    1 ? 3 
ATOM   9304  N NZ    . LYS C 1 249 ? 67.009  10.568  53.384  1.000 36.188  0 249 LYS CCC NZ    1 ? 3 
ATOM   9305  N N     . ILE C 1 250 ? 62.123  6.426   52.824  1.000 30.173  0 250 ILE CCC N     1 ? 3 
ATOM   9306  C CA    . ILE C 1 250 ? 62.264  5.192   53.642  1.000 27.984  0 250 ILE CCC CA    1 ? 3 
ATOM   9307  C C     . ILE C 1 250 ? 62.782  4.051   52.773  1.000 28.473  0 250 ILE CCC C     1 ? 3 
ATOM   9308  O O     . ILE C 1 250 ? 63.812  3.407   53.170  1.000 26.204  0 250 ILE CCC O     1 ? 3 
ATOM   9309  C CB    . ILE C 1 250 ? 60.970  4.866   54.390  1.000 26.596  0 250 ILE CCC CB    1 ? 3 
ATOM   9310  C CG1   . ILE C 1 250 ? 60.695  5.939   55.449  1.000 25.672  0 250 ILE CCC CG1   1 ? 3 
ATOM   9311  C CG2   . ILE C 1 250 ? 61.053  3.486   55.037  1.000 25.704  0 250 ILE CCC CG2   1 ? 3 
ATOM   9312  C CD1   . ILE C 1 250 ? 59.235  6.078   55.733  1.000 25.743  0 250 ILE CCC CD1   1 ? 3 
ATOM   9313  N N     . VAL C 1 251 ? 62.122  3.831   51.627  1.000 29.108  0 251 VAL CCC N     1 ? 3 
ATOM   9314  C CA    . VAL C 1 251 ? 62.477  2.726   50.704  1.000 30.127  0 251 VAL CCC CA    1 ? 3 
ATOM   9315  C C     . VAL C 1 251 ? 63.917  2.930   50.224  1.000 31.361  0 251 VAL CCC C     1 ? 3 
ATOM   9316  O O     . VAL C 1 251 ? 64.667  1.954   50.220  1.000 30.710  0 251 VAL CCC O     1 ? 3 
ATOM   9317  C CB    . VAL C 1 251 ? 61.469  2.619   49.551  1.000 31.182  0 251 VAL CCC CB    1 ? 3 
ATOM   9318  C CG1   . VAL C 1 251 ? 61.973  1.733   48.397  1.000 31.002  0 251 VAL CCC CG1   1 ? 3 
ATOM   9319  C CG2   . VAL C 1 251 ? 60.128  2.128   50.085  1.000 30.840  0 251 VAL CCC CG2   1 ? 3 
ATOM   9320  N N     . GLU C 1 252 ? 64.296  4.156   49.863  1.000 33.725  0 252 GLU CCC N     1 ? 3 
ATOM   9321  C CA    . GLU C 1 252 ? 65.674  4.507   49.454  1.000 35.667  0 252 GLU CCC CA    1 ? 3 
ATOM   9322  C C     . GLU C 1 252 ? 66.638  4.053   50.567  1.000 35.307  0 252 GLU CCC C     1 ? 3 
ATOM   9323  O O     . GLU C 1 252 ? 67.645  3.351   50.228  1.000 31.759  0 252 GLU CCC O     1 ? 3 
ATOM   9324  C CB    . GLU C 1 252 ? 65.746  5.999   49.127  1.000 40.376  0 252 GLU CCC CB    1 ? 3 
ATOM   9325  C CG    . GLU C 1 252 ? 67.144  6.468   48.696  1.000 46.039  0 252 GLU CCC CG    1 ? 3 
ATOM   9326  C CD    . GLU C 1 252 ? 67.596  7.875   49.071  1.000 47.513  0 252 GLU CCC CD    1 ? 3 
ATOM   9327  O OE1   . GLU C 1 252 ? 68.108  8.577   48.196  1.000 52.267  0 252 GLU CCC OE1   1 ? 3 
ATOM   9328  O OE2   . GLU C 1 252 ? 67.468  8.253   50.239  1.000 55.692  0 252 GLU CCC OE2   1 ? 3 
ATOM   9329  N N     . TYR C 1 253 ? 66.337  4.355   51.849  1.000 33.251  0 253 TYR CCC N     1 ? 3 
ATOM   9330  C CA    . TYR C 1 253 ? 67.236  3.973   52.971  1.000 31.923  0 253 TYR CCC CA    1 ? 3 
ATOM   9331  C C     . TYR C 1 253 ? 67.246  2.446   53.129  1.000 31.509  0 253 TYR CCC C     1 ? 3 
ATOM   9332  O O     . TYR C 1 253 ? 68.329  1.836   53.239  1.000 32.369  0 253 TYR CCC O     1 ? 3 
ATOM   9333  C CB    . TYR C 1 253 ? 66.865  4.714   54.259  1.000 31.420  0 253 TYR CCC CB    1 ? 3 
ATOM   9334  C CG    . TYR C 1 253 ? 67.775  4.425   55.421  1.000 29.508  0 253 TYR CCC CG    1 ? 3 
ATOM   9335  C CD1   . TYR C 1 253 ? 67.529  3.359   56.270  1.000 29.195  0 253 TYR CCC CD1   1 ? 3 
ATOM   9336  C CD2   . TYR C 1 253 ? 68.925  5.182   55.633  1.000 29.104  0 253 TYR CCC CD2   1 ? 3 
ATOM   9337  C CE1   . TYR C 1 253 ? 68.364  3.100   57.357  1.000 30.097  0 253 TYR CCC CE1   1 ? 3 
ATOM   9338  C CE2   . TYR C 1 253 ? 69.766  4.940   56.703  1.000 28.375  0 253 TYR CCC CE2   1 ? 3 
ATOM   9339  C CZ    . TYR C 1 253 ? 69.491  3.886   57.568  1.000 30.400  0 253 TYR CCC CZ    1 ? 3 
ATOM   9340  O OH    . TYR C 1 253 ? 70.308  3.610   58.647  1.000 31.391  0 253 TYR CCC OH    1 ? 3 
ATOM   9341  N N     . MET C 1 254 ? 66.080  1.814   53.123  1.000 31.365  0 254 MET CCC N     1 ? 3 
ATOM   9342  C CA    . MET C 1 254 ? 65.991  0.343   53.308  1.000 33.134  0 254 MET CCC CA    1 ? 3 
ATOM   9343  C C     . MET C 1 254 ? 66.786  -0.396  52.209  1.000 33.829  0 254 MET CCC C     1 ? 3 
ATOM   9344  O O     . MET C 1 254 ? 67.437  -1.389  52.545  1.000 33.432  0 254 MET CCC O     1 ? 3 
ATOM   9345  C CB    . MET C 1 254 ? 64.537  -0.117  53.298  1.000 33.589  0 254 MET CCC CB    1 ? 3 
ATOM   9346  C CG    . MET C 1 254 ? 63.756  0.446   54.480  1.000 32.585  0 254 MET CCC CG    1 ? 3 
ATOM   9347  S SD    . MET C 1 254 ? 62.099  -0.259  54.636  1.000 32.517  0 254 MET CCC SD    1 ? 3 
ATOM   9348  C CE    . MET C 1 254 ? 62.504  -2.006  54.770  1.000 33.538  0 254 MET CCC CE    1 ? 3 
ATOM   9349  N N     . LYS C 1 255 ? 66.732  0.074   50.964  1.000 34.185  0 255 LYS CCC N     1 ? 3 
ATOM   9350  C CA    . LYS C 1 255 ? 67.497  -0.473  49.817  1.000 35.958  0 255 LYS CCC CA    1 ? 3 
ATOM   9351  C C     . LYS C 1 255 ? 68.998  -0.344  50.080  1.000 33.957  0 255 LYS CCC C     1 ? 3 
ATOM   9352  O O     . LYS C 1 255 ? 69.706  -1.349  49.881  1.000 30.050  0 255 LYS CCC O     1 ? 3 
ATOM   9353  C CB    . LYS C 1 255 ? 67.181  0.258   48.510  1.000 40.735  0 255 LYS CCC CB    1 ? 3 
ATOM   9354  C CG    . LYS C 1 255 ? 66.068  -0.354  47.663  1.000 44.424  0 255 LYS CCC CG    1 ? 3 
ATOM   9355  C CD    . LYS C 1 255 ? 65.728  0.493   46.447  1.000 48.493  0 255 LYS CCC CD    1 ? 3 
ATOM   9356  C CE    . LYS C 1 255 ? 64.727  -0.159  45.503  1.000 53.446  0 255 LYS CCC CE    1 ? 3 
ATOM   9357  N NZ    . LYS C 1 255 ? 64.945  0.244   44.079  1.000 55.358  0 255 LYS CCC NZ    1 ? 3 
ATOM   9358  N N     . ALA C 1 256 ? 69.449  0.833   50.536  1.000 33.225  0 256 ALA CCC N     1 ? 3 
ATOM   9359  C CA    . ALA C 1 256 ? 70.870  1.148   50.800  1.000 32.034  0 256 ALA CCC CA    1 ? 3 
ATOM   9360  C C     . ALA C 1 256 ? 71.379  0.324   51.988  1.000 31.549  0 256 ALA CCC C     1 ? 3 
ATOM   9361  O O     . ALA C 1 256 ? 72.634  0.196   52.098  1.000 34.291  0 256 ALA CCC O     1 ? 3 
ATOM   9362  C CB    . ALA C 1 256 ? 71.064  2.617   51.033  1.000 31.248  0 256 ALA CCC CB    1 ? 3 
ATOM   9363  N N     . THR C 1 257 ? 70.505  -0.264  52.810  1.000 28.683  0 257 THR CCC N     1 ? 3 
ATOM   9364  C CA    . THR C 1 257 ? 70.942  -1.075  53.972  1.000 29.529  0 257 THR CCC CA    1 ? 3 
ATOM   9365  C C     . THR C 1 257 ? 70.678  -2.562  53.753  1.000 30.114  0 257 THR CCC C     1 ? 3 
ATOM   9366  O O     . THR C 1 257 ? 70.918  -3.319  54.685  1.000 29.717  0 257 THR CCC O     1 ? 3 
ATOM   9367  C CB    . THR C 1 257 ? 70.317  -0.612  55.305  1.000 29.299  0 257 THR CCC CB    1 ? 3 
ATOM   9368  O OG1   . THR C 1 257 ? 68.868  -0.623  55.259  1.000 28.065  0 257 THR CCC OG1   1 ? 3 
ATOM   9369  C CG2   . THR C 1 257 ? 70.857  0.743   55.717  1.000 28.676  0 257 THR CCC CG2   1 ? 3 
ATOM   9370  N N     . GLY C 1 258 ? 70.166  -2.978  52.601  1.000 34.161  0 258 GLY CCC N     1 ? 3 
ATOM   9371  C CA    . GLY C 1 258 ? 70.200  -4.398  52.160  1.000 36.689  0 258 GLY CCC CA    1 ? 3 
ATOM   9372  C C     . GLY C 1 258 ? 68.831  -5.037  51.938  1.000 37.621  0 258 GLY CCC C     1 ? 3 
ATOM   9373  O O     . GLY C 1 258 ? 68.779  -6.225  51.596  1.000 37.676  0 258 GLY CCC O     1 ? 3 
ATOM   9374  N N     . THR C 1 259 ? 67.739  -4.311  52.112  1.000 36.734  0 259 THR CCC N     1 ? 3 
ATOM   9375  C CA    . THR C 1 259 ? 66.410  -4.866  51.765  1.000 36.826  0 259 THR CCC CA    1 ? 3 
ATOM   9376  C C     . THR C 1 259 ? 66.241  -4.823  50.240  1.000 38.610  0 259 THR CCC C     1 ? 3 
ATOM   9377  O O     . THR C 1 259 ? 66.514  -3.787  49.612  1.000 38.713  0 259 THR CCC O     1 ? 3 
ATOM   9378  C CB    . THR C 1 259 ? 65.305  -4.189  52.581  1.000 34.790  0 259 THR CCC CB    1 ? 3 
ATOM   9379  O OG1   . THR C 1 259 ? 65.677  -4.220  53.971  1.000 33.459  0 259 THR CCC OG1   1 ? 3 
ATOM   9380  C CG2   . THR C 1 259 ? 63.975  -4.893  52.357  1.000 34.430  0 259 THR CCC CG2   1 ? 3 
ATOM   9381  N N     . LYS C 1 260 ? 65.835  -5.936  49.641  1.000 40.854  0 260 LYS CCC N     1 ? 3 
ATOM   9382  C CA    . LYS C 1 260 ? 65.613  -6.030  48.177  1.000 41.808  0 260 LYS CCC CA    1 ? 3 
ATOM   9383  C C     . LYS C 1 260 ? 64.119  -5.846  47.946  1.000 42.163  0 260 LYS CCC C     1 ? 3 
ATOM   9384  O O     . LYS C 1 260 ? 63.361  -6.370  48.768  1.000 43.029  0 260 LYS CCC O     1 ? 3 
ATOM   9385  C CB    . LYS C 1 260 ? 66.135  -7.363  47.633  1.000 43.685  0 260 LYS CCC CB    1 ? 3 
ATOM   9386  C CG    . LYS C 1 260 ? 67.661  -7.450  47.566  1.000 44.748  0 260 LYS CCC CG    1 ? 3 
ATOM   9387  C CD    . LYS C 1 260 ? 68.191  -8.867  47.427  1.000 46.384  0 260 LYS CCC CD    1 ? 3 
ATOM   9388  C CE    . LYS C 1 260 ? 67.996  -9.694  48.687  1.000 47.127  0 260 LYS CCC CE    1 ? 3 
ATOM   9389  N NZ    . LYS C 1 260 ? 68.203  -11.133 48.414  1.000 47.962  0 260 LYS CCC NZ    1 ? 3 
ATOM   9390  N N     . PHE C 1 261 ? 63.757  -5.099  46.905  1.000 41.395  0 261 PHE CCC N     1 ? 3 
ATOM   9391  C CA    . PHE C 1 261 ? 62.370  -4.748  46.504  1.000 41.207  0 261 PHE CCC CA    1 ? 3 
ATOM   9392  C C     . PHE C 1 261 ? 62.069  -5.251  45.084  1.000 40.474  0 261 PHE CCC C     1 ? 3 
ATOM   9393  O O     . PHE C 1 261 ? 62.740  -4.791  44.147  1.000 38.995  0 261 PHE CCC O     1 ? 3 
ATOM   9394  C CB    . PHE C 1 261 ? 62.181  -3.230  46.563  1.000 38.472  0 261 PHE CCC CB    1 ? 3 
ATOM   9395  C CG    . PHE C 1 261 ? 62.103  -2.700  47.959  1.000 37.239  0 261 PHE CCC CG    1 ? 3 
ATOM   9396  C CD1   . PHE C 1 261 ? 63.262  -2.435  48.674  1.000 35.687  0 261 PHE CCC CD1   1 ? 3 
ATOM   9397  C CD2   . PHE C 1 261 ? 60.875  -2.511  48.580  1.000 34.906  0 261 PHE CCC CD2   1 ? 3 
ATOM   9398  C CE1   . PHE C 1 261 ? 63.205  -1.952  49.970  1.000 32.355  0 261 PHE CCC CE1   1 ? 3 
ATOM   9399  C CE2   . PHE C 1 261 ? 60.825  -2.040  49.877  1.000 33.721  0 261 PHE CCC CE2   1 ? 3 
ATOM   9400  C CZ    . PHE C 1 261 ? 61.990  -1.759  50.558  1.000 33.244  0 261 PHE CCC CZ    1 ? 3 
ATOM   9401  N N     . LEU C 1 262 ? 61.083  -6.149  44.972  1.000 41.650  0 262 LEU CCC N     1 ? 3 
ATOM   9402  C CA    . LEU C 1 262 ? 60.420  -6.585  43.717  1.000 43.068  0 262 LEU CCC CA    1 ? 3 
ATOM   9403  C C     . LEU C 1 262 ? 59.194  -5.702  43.494  1.000 41.330  0 262 LEU CCC C     1 ? 3 
ATOM   9404  O O     . LEU C 1 262 ? 58.207  -5.856  44.216  1.000 37.415  0 262 LEU CCC O     1 ? 3 
ATOM   9405  C CB    . LEU C 1 262 ? 60.011  -8.053  43.839  1.000 45.577  0 262 LEU CCC CB    1 ? 3 
ATOM   9406  C CG    . LEU C 1 262 ? 61.091  -9.003  44.338  1.000 48.578  0 262 LEU CCC CG    1 ? 3 
ATOM   9407  C CD1   . LEU C 1 262 ? 60.523  -10.418 44.414  1.000 49.971  0 262 LEU CCC CD1   1 ? 3 
ATOM   9408  C CD2   . LEU C 1 262 ? 62.336  -8.960  43.448  1.000 49.019  0 262 LEU CCC CD2   1 ? 3 
ATOM   9409  N N     . VAL C 1 263 ? 59.282  -4.785  42.537  1.000 43.153  0 263 VAL CCC N     1 ? 3 
ATOM   9410  C CA    . VAL C 1 263 ? 58.250  -3.737  42.301  1.000 45.745  0 263 VAL CCC CA    1 ? 3 
ATOM   9411  C C     . VAL C 1 263 ? 57.262  -4.234  41.227  1.000 47.178  0 263 VAL CCC C     1 ? 3 
ATOM   9412  O O     . VAL C 1 263 ? 57.697  -4.706  40.220  1.000 47.204  0 263 VAL CCC O     1 ? 3 
ATOM   9413  C CB    . VAL C 1 263 ? 58.917  -2.389  41.976  1.000 45.681  0 263 VAL CCC CB    1 ? 3 
ATOM   9414  C CG1   . VAL C 1 263 ? 57.911  -1.255  41.882  1.000 46.801  0 263 VAL CCC CG1   1 ? 3 
ATOM   9415  C CG2   . VAL C 1 263 ? 59.949  -2.046  43.023  1.000 44.969  0 263 VAL CCC CG2   1 ? 3 
ATOM   9416  N N     . GLY C 1 264 ? 55.959  -4.149  41.492  1.000 51.012  0 264 GLY CCC N     1 ? 3 
ATOM   9417  C CA    . GLY C 1 264 ? 54.875  -4.459  40.537  1.000 49.167  0 264 GLY CCC CA    1 ? 3 
ATOM   9418  C C     . GLY C 1 264 ? 54.681  -5.954  40.369  1.000 49.970  0 264 GLY CCC C     1 ? 3 
ATOM   9419  O O     . GLY C 1 264 ? 54.167  -6.377  39.299  1.000 48.729  0 264 GLY CCC O     1 ? 3 
ATOM   9420  N N     . VAL C 1 265 ? 55.091  -6.725  41.375  1.000 48.586  0 265 VAL CCC N     1 ? 3 
ATOM   9421  C CA    . VAL C 1 265 ? 55.185  -8.206  41.322  1.000 52.391  0 265 VAL CCC CA    1 ? 3 
ATOM   9422  C C     . VAL C 1 265 ? 54.563  -8.739  42.607  1.000 55.762  0 265 VAL CCC C     1 ? 3 
ATOM   9423  O O     . VAL C 1 265 ? 54.857  -8.164  43.721  1.000 64.936  0 265 VAL CCC O     1 ? 3 
ATOM   9424  C CB    . VAL C 1 265 ? 56.657  -8.645  41.180  1.000 58.872  0 265 VAL CCC CB    1 ? 3 
ATOM   9425  C CG1   . VAL C 1 265 ? 56.853  -10.132 41.410  1.000 62.320  0 265 VAL CCC CG1   1 ? 3 
ATOM   9426  C CG2   . VAL C 1 265 ? 57.235  -8.267  39.816  1.000 57.291  0 265 VAL CCC CG2   1 ? 3 
ATOM   9427  N N     . VAL C 1 266 ? 53.760  -9.795  42.486  1.000 53.332  0 266 VAL CCC N     1 ? 3 
ATOM   9428  C CA    . VAL C 1 266 ? 53.212  -10.539 43.650  1.000 53.090  0 266 VAL CCC CA    1 ? 3 
ATOM   9429  C C     . VAL C 1 266 ? 53.380  -12.039 43.415  1.000 52.015  0 266 VAL CCC C     1 ? 3 
ATOM   9430  O O     . VAL C 1 266 ? 53.482  -12.511 42.280  1.000 50.251  0 266 VAL CCC O     1 ? 3 
ATOM   9431  C CB    . VAL C 1 266 ? 51.746  -10.152 43.911  1.000 55.057  0 266 VAL CCC CB    1 ? 3 
ATOM   9432  C CG1   . VAL C 1 266 ? 51.602  -8.657  44.160  1.000 58.654  0 266 VAL CCC CG1   1 ? 3 
ATOM   9433  C CG2   . VAL C 1 266 ? 50.817  -10.560 42.787  1.000 54.643  0 266 VAL CCC CG2   1 ? 3 
ATOM   9434  N N     . PRO C 1 267 ? 53.416  -12.842 44.498  1.000 50.207  0 267 PRO CCC N     1 ? 3 
ATOM   9435  C CA    . PRO C 1 267 ? 53.357  -14.300 44.368  1.000 48.939  0 267 PRO CCC CA    1 ? 3 
ATOM   9436  C C     . PRO C 1 267 ? 52.056  -14.780 43.702  1.000 49.430  0 267 PRO CCC C     1 ? 3 
ATOM   9437  O O     . PRO C 1 267 ? 51.011  -14.204 43.982  1.000 44.016  0 267 PRO CCC O     1 ? 3 
ATOM   9438  C CB    . PRO C 1 267 ? 53.397  -14.822 45.805  1.000 49.855  0 267 PRO CCC CB    1 ? 3 
ATOM   9439  C CG    . PRO C 1 267 ? 53.926  -13.652 46.635  1.000 48.020  0 267 PRO CCC CG    1 ? 3 
ATOM   9440  C CD    . PRO C 1 267 ? 53.520  -12.393 45.896  1.000 48.520  0 267 PRO CCC CD    1 ? 3 
ATOM   9441  N N     . ILE C 1 268 ? 52.168  -15.803 42.836  1.000 47.910  0 268 ILE CCC N     1 ? 3 
ATOM   9442  C CA    . ILE C 1 268 ? 51.015  -16.511 42.206  1.000 48.299  0 268 ILE CCC CA    1 ? 3 
ATOM   9443  C C     . ILE C 1 268 ? 51.021  -17.982 42.634  1.000 48.486  0 268 ILE CCC C     1 ? 3 
ATOM   9444  O O     . ILE C 1 268 ? 49.991  -18.638 42.444  1.000 50.449  0 268 ILE CCC O     1 ? 3 
ATOM   9445  C CB    . ILE C 1 268 ? 51.018  -16.343 40.671  1.000 49.504  0 268 ILE CCC CB    1 ? 3 
ATOM   9446  C CG1   . ILE C 1 268 ? 52.298  -16.886 40.031  1.000 49.235  0 268 ILE CCC CG1   1 ? 3 
ATOM   9447  C CG2   . ILE C 1 268 ? 50.751  -14.888 40.293  1.000 48.821  0 268 ILE CCC CG2   1 ? 3 
ATOM   9448  C CD1   . ILE C 1 268 ? 52.295  -16.866 38.531  1.000 52.036  0 268 ILE CCC CD1   1 ? 3 
ATOM   9449  N N     . ASN C 1 269 ? 52.123  -18.484 43.196  1.000 47.848  0 269 ASN CCC N     1 ? 3 
ATOM   9450  C CA    . ASN C 1 269 ? 52.194  -19.892 43.675  1.000 50.205  0 269 ASN CCC CA    1 ? 3 
ATOM   9451  C C     . ASN C 1 269 ? 53.238  -20.026 44.772  1.000 49.101  0 269 ASN CCC C     1 ? 3 
ATOM   9452  O O     . ASN C 1 269 ? 54.298  -19.376 44.668  1.000 51.128  0 269 ASN CCC O     1 ? 3 
ATOM   9453  C CB    . ASN C 1 269 ? 52.490  -20.916 42.568  1.000 52.344  0 269 ASN CCC CB    1 ? 3 
ATOM   9454  C CG    . ASN C 1 269 ? 52.265  -22.350 43.030  1.000 54.044  0 269 ASN CCC CG    1 ? 3 
ATOM   9455  O OD1   . ASN C 1 269 ? 51.178  -22.681 43.521  1.000 53.636  0 269 ASN CCC OD1   1 ? 3 
ATOM   9456  N ND2   . ASN C 1 269 ? 53.270  -23.208 42.919  1.000 53.827  0 269 ASN CCC ND2   1 ? 3 
ATOM   9457  N N     . ILE C 1 270 ? 52.951  -20.865 45.761  1.000 48.452  0 270 ILE CCC N     1 ? 3 
ATOM   9458  C CA    . ILE C 1 270 ? 53.795  -21.082 46.965  1.000 51.910  0 270 ILE CCC CA    1 ? 3 
ATOM   9459  C C     . ILE C 1 270 ? 53.835  -22.596 47.246  1.000 56.684  0 270 ILE CCC C     1 ? 3 
ATOM   9460  O O     . ILE C 1 270 ? 52.789  -23.168 47.589  1.000 55.630  0 270 ILE CCC O     1 ? 3 
ATOM   9461  C CB    . ILE C 1 270 ? 53.269  -20.207 48.132  1.000 49.874  0 270 ILE CCC CB    1 ? 3 
ATOM   9462  C CG1   . ILE C 1 270 ? 53.482  -18.719 47.817  1.000 48.065  0 270 ILE CCC CG1   1 ? 3 
ATOM   9463  C CG2   . ILE C 1 270 ? 53.915  -20.616 49.446  1.000 50.382  0 270 ILE CCC CG2   1 ? 3 
ATOM   9464  C CD1   . ILE C 1 270 ? 52.894  -17.741 48.801  1.000 46.371  0 270 ILE CCC CD1   1 ? 3 
ATOM   9465  N N     . GLU C 1 271 ? 54.999  -23.231 47.078  1.000 63.597  0 271 GLU CCC N     1 ? 3 
ATOM   9466  C CA    . GLU C 1 271 ? 55.169  -24.702 47.239  1.000 68.786  0 271 GLU CCC CA    1 ? 3 
ATOM   9467  C C     . GLU C 1 271 ? 56.373  -24.969 48.143  1.000 71.245  0 271 GLU CCC C     1 ? 3 
ATOM   9468  O O     . GLU C 1 271 ? 57.326  -24.184 48.087  1.000 63.482  0 271 GLU CCC O     1 ? 3 
ATOM   9469  C CB    . GLU C 1 271 ? 55.352  -25.415 45.892  1.000 74.183  0 271 GLU CCC CB    1 ? 3 
ATOM   9470  C CG    . GLU C 1 271 ? 56.004  -24.551 44.812  1.000 78.700  0 271 GLU CCC CG    1 ? 3 
ATOM   9471  C CD    . GLU C 1 271 ? 56.213  -25.243 43.468  1.000 79.264  0 271 GLU CCC CD    1 ? 3 
ATOM   9472  O OE1   . GLU C 1 271 ? 56.367  -26.480 43.452  1.000 76.338  0 271 GLU CCC OE1   1 ? 3 
ATOM   9473  O OE2   . GLU C 1 271 ? 56.231  -24.536 42.432  1.000 81.173  0 271 GLU CCC OE2   1 ? 3 
ATOM   9474  N N     . LYS C 1 272 ? 56.321  -26.063 48.910  1.000 76.588  0 272 LYS CCC N     1 ? 3 
ATOM   9475  C CA    . LYS C 1 272 ? 57.464  -26.636 49.663  1.000 79.972  0 272 LYS CCC CA    1 ? 3 
ATOM   9476  C C     . LYS C 1 272 ? 58.331  -27.477 48.715  1.000 83.181  0 272 LYS CCC C     1 ? 3 
ATOM   9477  O O     . LYS C 1 272 ? 57.871  -28.535 48.266  1.000 83.402  0 272 LYS CCC O     1 ? 3 
ATOM   9478  C CB    . LYS C 1 272 ? 56.964  -27.445 50.865  1.000 82.914  0 272 LYS CCC CB    1 ? 3 
ATOM   9479  C CG    . LYS C 1 272 ? 58.015  -27.741 51.926  1.000 88.297  0 272 LYS CCC CG    1 ? 3 
ATOM   9480  C CD    . LYS C 1 272 ? 57.554  -27.633 53.354  1.000 90.527  0 272 LYS CCC CD    1 ? 3 
ATOM   9481  C CE    . LYS C 1 272 ? 58.722  -27.759 54.309  1.000 92.294  0 272 LYS CCC CE    1 ? 3 
ATOM   9482  N NZ    . LYS C 1 272 ? 58.322  -27.467 55.706  1.000 90.708  0 272 LYS CCC NZ    1 ? 3 
ATOM   9483  N N     . VAL C 1 273 ? 59.542  -26.995 48.416  1.000 86.902  0 273 VAL CCC N     1 ? 3 
ATOM   9484  C CA    . VAL C 1 273 ? 60.600  -27.745 47.674  1.000 92.858  0 273 VAL CCC CA    1 ? 3 
ATOM   9485  C C     . VAL C 1 273 ? 61.680  -28.138 48.690  1.000 96.462  0 273 VAL CCC C     1 ? 3 
ATOM   9486  O O     . VAL C 1 273 ? 62.597  -27.313 48.971  1.000 89.158  0 273 VAL CCC O     1 ? 3 
ATOM   9487  C CB    . VAL C 1 273 ? 61.158  -26.942 46.482  1.000 91.663  0 273 VAL CCC CB    1 ? 3 
ATOM   9488  C CG1   . VAL C 1 273 ? 62.404  -27.580 45.875  1.000 90.881  0 273 VAL CCC CG1   1 ? 3 
ATOM   9489  C CG2   . VAL C 1 273 ? 60.092  -26.760 45.413  1.000 91.854  0 273 VAL CCC CG2   1 ? 3 
ATOM   9490  N N     . ASN C 1 274 ? 61.543  -29.357 49.224  1.000 99.062  0 274 ASN CCC N     1 ? 3 
ATOM   9491  C CA    . ASN C 1 274 ? 62.382  -29.916 50.314  1.000 98.584  0 274 ASN CCC CA    1 ? 3 
ATOM   9492  C C     . ASN C 1 274 ? 62.102  -29.106 51.587  1.000 91.046  0 274 ASN CCC C     1 ? 3 
ATOM   9493  O O     . ASN C 1 274 ? 60.924  -29.117 52.039  1.000 92.800  0 274 ASN CCC O     1 ? 3 
ATOM   9494  C CB    . ASN C 1 274 ? 63.859  -29.980 49.899  1.000 102.039 0 274 ASN CCC CB    1 ? 3 
ATOM   9495  C CG    . ASN C 1 274 ? 64.112  -30.928 48.738  1.000 103.606 0 274 ASN CCC CG    1 ? 3 
ATOM   9496  O OD1   . ASN C 1 274 ? 64.614  -30.518 47.691  1.000 104.734 0 274 ASN CCC OD1   1 ? 3 
ATOM   9497  N ND2   . ASN C 1 274 ? 63.781  -32.202 48.909  1.000 101.679 0 274 ASN CCC ND2   1 ? 3 
ATOM   9498  N N     . GLU C 1 275 ? 63.113  -28.408 52.117  1.000 84.098  0 275 GLU CCC N     1 ? 3 
ATOM   9499  C CA    . GLU C 1 275 ? 63.014  -27.643 53.388  1.000 77.715  0 275 GLU CCC CA    1 ? 3 
ATOM   9500  C C     . GLU C 1 275 ? 62.730  -26.169 53.081  1.000 70.787  0 275 GLU CCC C     1 ? 3 
ATOM   9501  O O     . GLU C 1 275 ? 62.415  -25.448 54.029  1.000 69.548  0 275 GLU CCC O     1 ? 3 
ATOM   9502  C CB    . GLU C 1 275 ? 64.291  -27.808 54.225  1.000 76.793  0 275 GLU CCC CB    1 ? 3 
ATOM   9503  C CG    . GLU C 1 275 ? 65.553  -27.221 53.594  1.000 75.943  0 275 GLU CCC CG    1 ? 3 
ATOM   9504  C CD    . GLU C 1 275 ? 66.321  -28.123 52.641  1.000 75.266  0 275 GLU CCC CD    1 ? 3 
ATOM   9505  O OE1   . GLU C 1 275 ? 65.972  -29.311 52.531  1.000 73.647  0 275 GLU CCC OE1   1 ? 3 
ATOM   9506  O OE2   . GLU C 1 275 ? 67.325  -27.634 52.057  1.000 72.073  0 275 GLU CCC OE2   1 ? 3 
ATOM   9507  N N     . ASN C 1 276 ? 62.853  -25.745 51.813  1.000 64.683  0 276 ASN CCC N     1 ? 3 
ATOM   9508  C CA    . ASN C 1 276 ? 62.669  -24.333 51.390  1.000 58.612  0 276 ASN CCC CA    1 ? 3 
ATOM   9509  C C     . ASN C 1 276 ? 61.240  -24.151 50.882  1.000 55.283  0 276 ASN CCC C     1 ? 3 
ATOM   9510  O O     . ASN C 1 276 ? 60.567  -25.148 50.674  1.000 54.091  0 276 ASN CCC O     1 ? 3 
ATOM   9511  C CB    . ASN C 1 276 ? 63.686  -23.892 50.344  1.000 57.116  0 276 ASN CCC CB    1 ? 3 
ATOM   9512  C CG    . ASN C 1 276 ? 65.088  -23.709 50.891  1.000 59.426  0 276 ASN CCC CG    1 ? 3 
ATOM   9513  O OD1   . ASN C 1 276 ? 65.270  -23.322 52.051  1.000 54.027  0 276 ASN CCC OD1   1 ? 3 
ATOM   9514  N ND2   . ASN C 1 276 ? 66.079  -23.971 50.045  1.000 59.551  0 276 ASN CCC ND2   1 ? 3 
ATOM   9515  N N     . ILE C 1 277 ? 60.826  -22.896 50.687  1.000 52.555  0 277 ILE CCC N     1 ? 3 
ATOM   9516  C CA    . ILE C 1 277 ? 59.563  -22.514 49.995  1.000 52.713  0 277 ILE CCC CA    1 ? 3 
ATOM   9517  C C     . ILE C 1 277 ? 59.930  -21.823 48.673  1.000 51.193  0 277 ILE CCC C     1 ? 3 
ATOM   9518  O O     . ILE C 1 277 ? 60.489  -20.711 48.693  1.000 47.191  0 277 ILE CCC O     1 ? 3 
ATOM   9519  C CB    . ILE C 1 277 ? 58.668  -21.656 50.916  1.000 53.918  0 277 ILE CCC CB    1 ? 3 
ATOM   9520  C CG1   . ILE C 1 277 ? 58.268  -22.451 52.167  1.000 53.742  0 277 ILE CCC CG1   1 ? 3 
ATOM   9521  C CG2   . ILE C 1 277 ? 57.449  -21.123 50.169  1.000 51.702  0 277 ILE CCC CG2   1 ? 3 
ATOM   9522  C CD1   . ILE C 1 277 ? 57.826  -21.596 53.335  1.000 52.849  0 277 ILE CCC CD1   1 ? 3 
ATOM   9523  N N     . LYS C 1 278 ? 59.650  -22.508 47.560  1.000 50.990  0 278 LYS CCC N     1 ? 3 
ATOM   9524  C CA    . LYS C 1 278 ? 59.738  -21.970 46.184  1.000 51.057  0 278 LYS CCC CA    1 ? 3 
ATOM   9525  C C     . LYS C 1 278 ? 58.504  -21.095 45.961  1.000 49.205  0 278 LYS CCC C     1 ? 3 
ATOM   9526  O O     . LYS C 1 278 ? 57.354  -21.612 46.035  1.000 48.741  0 278 LYS CCC O     1 ? 3 
ATOM   9527  C CB    . LYS C 1 278 ? 59.812  -23.128 45.189  1.000 54.923  0 278 LYS CCC CB    1 ? 3 
ATOM   9528  C CG    . LYS C 1 278 ? 60.135  -22.782 43.744  1.000 56.467  0 278 LYS CCC CG    1 ? 3 
ATOM   9529  C CD    . LYS C 1 278 ? 59.858  -23.929 42.784  1.000 59.739  0 278 LYS CCC CD    1 ? 3 
ATOM   9530  C CE    . LYS C 1 278 ? 60.161  -23.572 41.345  1.000 62.644  0 278 LYS CCC CE    1 ? 3 
ATOM   9531  N NZ    . LYS C 1 278 ? 59.971  -24.724 40.430  1.000 63.214  0 278 LYS CCC NZ    1 ? 3 
ATOM   9532  N N     . VAL C 1 279 ? 58.734  -19.812 45.711  1.000 46.336  0 279 VAL CCC N     1 ? 3 
ATOM   9533  C CA    . VAL C 1 279 ? 57.655  -18.835 45.406  1.000 43.202  0 279 VAL CCC CA    1 ? 3 
ATOM   9534  C C     . VAL C 1 279 ? 57.719  -18.509 43.915  1.000 43.657  0 279 VAL CCC C     1 ? 3 
ATOM   9535  O O     . VAL C 1 279 ? 58.784  -18.181 43.414  1.000 40.741  0 279 VAL CCC O     1 ? 3 
ATOM   9536  C CB    . VAL C 1 279 ? 57.790  -17.589 46.295  1.000 41.728  0 279 VAL CCC CB    1 ? 3 
ATOM   9537  C CG1   . VAL C 1 279 ? 56.885  -16.448 45.830  1.000 41.969  0 279 VAL CCC CG1   1 ? 3 
ATOM   9538  C CG2   . VAL C 1 279 ? 57.520  -17.953 47.748  1.000 40.935  0 279 VAL CCC CG2   1 ? 3 
ATOM   9539  N N     . SER C 1 280 ? 56.593  -18.647 43.223  1.000 45.692  0 280 SER CCC N     1 ? 3 
ATOM   9540  C CA    . SER C 1 280 ? 56.486  -18.310 41.779  1.000 47.218  0 280 SER CCC CA    1 ? 3 
ATOM   9541  C C     . SER C 1 280 ? 55.777  -16.963 41.693  1.000 44.599  0 280 SER CCC C     1 ? 3 
ATOM   9542  O O     . SER C 1 280 ? 54.722  -16.835 42.302  1.000 42.183  0 280 SER CCC O     1 ? 3 
ATOM   9543  C CB    . SER C 1 280 ? 55.798  -19.403 40.985  1.000 45.853  0 280 SER CCC CB    1 ? 3 
ATOM   9544  O OG    . SER C 1 280 ? 56.559  -20.594 41.022  1.000 46.509  0 280 SER CCC OG    1 ? 3 
ATOM   9545  N N     . PHE C 1 281 ? 56.399  -15.996 41.022  1.000 45.057  0 281 PHE CCC N     1 ? 3 
ATOM   9546  C CA    . PHE C 1 281 ? 55.946  -14.589 40.974  1.000 46.023  0 281 PHE CCC CA    1 ? 3 
ATOM   9547  C C     . PHE C 1 281 ? 55.207  -14.319 39.661  1.000 48.802  0 281 PHE CCC C     1 ? 3 
ATOM   9548  O O     . PHE C 1 281 ? 55.447  -15.015 38.644  1.000 47.526  0 281 PHE CCC O     1 ? 3 
ATOM   9549  C CB    . PHE C 1 281 ? 57.137  -13.649 41.145  1.000 47.187  0 281 PHE CCC CB    1 ? 3 
ATOM   9550  C CG    . PHE C 1 281 ? 57.718  -13.615 42.536  1.000 47.297  0 281 PHE CCC CG    1 ? 3 
ATOM   9551  C CD1   . PHE C 1 281 ? 57.101  -12.885 43.544  1.000 46.721  0 281 PHE CCC CD1   1 ? 3 
ATOM   9552  C CD2   . PHE C 1 281 ? 58.865  -14.338 42.846  1.000 48.463  0 281 PHE CCC CD2   1 ? 3 
ATOM   9553  C CE1   . PHE C 1 281 ? 57.647  -12.843 44.826  1.000 46.831  0 281 PHE CCC CE1   1 ? 3 
ATOM   9554  C CE2   . PHE C 1 281 ? 59.398  -14.307 44.131  1.000 48.929  0 281 PHE CCC CE2   1 ? 3 
ATOM   9555  C CZ    . PHE C 1 281 ? 58.794  -13.553 45.115  1.000 47.469  0 281 PHE CCC CZ    1 ? 3 
ATOM   9556  N N     . SER C 1 282 ? 54.340  -13.303 39.705  1.000 50.288  0 282 SER CCC N     1 ? 3 
ATOM   9557  C CA    . SER C 1 282 ? 53.425  -12.874 38.615  1.000 50.617  0 282 SER CCC CA    1 ? 3 
ATOM   9558  C C     . SER C 1 282 ? 54.189  -12.479 37.342  1.000 50.091  0 282 SER CCC C     1 ? 3 
ATOM   9559  O O     . SER C 1 282 ? 53.560  -12.423 36.294  1.000 48.959  0 282 SER CCC O     1 ? 3 
ATOM   9560  C CB    . SER C 1 282 ? 52.565  -11.733 39.097  1.000 51.625  0 282 SER CCC CB    1 ? 3 
ATOM   9561  O OG    . SER C 1 282 ? 53.335  -10.552 39.250  1.000 50.628  0 282 SER CCC OG    1 ? 3 
ATOM   9562  N N     . ASP C 1 283 ? 55.488  -12.183 37.430  1.000 49.654  0 283 ASP CCC N     1 ? 3 
ATOM   9563  C CA    . ASP C 1 283 ? 56.328  -11.809 36.258  1.000 49.640  0 283 ASP CCC CA    1 ? 3 
ATOM   9564  C C     . ASP C 1 283 ? 57.038  -13.056 35.692  1.000 48.749  0 283 ASP CCC C     1 ? 3 
ATOM   9565  O O     . ASP C 1 283 ? 57.894  -12.872 34.842  1.000 47.668  0 283 ASP CCC O     1 ? 3 
ATOM   9566  C CB    . ASP C 1 283 ? 57.299  -10.668 36.608  1.000 49.801  0 283 ASP CCC CB    1 ? 3 
ATOM   9567  C CG    . ASP C 1 283 ? 58.433  -11.036 37.551  1.000 49.307  0 283 ASP CCC CG    1 ? 3 
ATOM   9568  O OD1   . ASP C 1 283 ? 58.341  -12.109 38.218  1.000 47.142  0 283 ASP CCC OD1   1 ? 3 
ATOM   9569  O OD2   . ASP C 1 283 ? 59.399  -10.231 37.624  1.000 53.208  0 283 ASP CCC OD2   1 ? 3 
ATOM   9570  N N     . GLY C 1 284 ? 56.683  -14.268 36.138  1.000 49.409  0 284 GLY CCC N     1 ? 3 
ATOM   9571  C CA    . GLY C 1 284 ? 57.309  -15.535 35.708  1.000 51.867  0 284 GLY CCC CA    1 ? 3 
ATOM   9572  C C     . GLY C 1 284 ? 58.677  -15.790 36.355  1.000 55.273  0 284 GLY CCC C     1 ? 3 
ATOM   9573  O O     . GLY C 1 284 ? 59.340  -16.783 35.992  1.000 56.986  0 284 GLY CCC O     1 ? 3 
ATOM   9574  N N     . SER C 1 285 ? 59.128  -14.955 37.289  1.000 53.664  0 285 SER CCC N     1 ? 3 
ATOM   9575  C CA    . SER C 1 285 ? 60.367  -15.219 38.068  1.000 53.519  0 285 SER CCC CA    1 ? 3 
ATOM   9576  C C     . SER C 1 285 ? 60.033  -16.160 39.236  1.000 52.131  0 285 SER CCC C     1 ? 3 
ATOM   9577  O O     . SER C 1 285 ? 58.853  -16.259 39.645  1.000 53.521  0 285 SER CCC O     1 ? 3 
ATOM   9578  C CB    . SER C 1 285 ? 61.040  -13.942 38.512  1.000 51.605  0 285 SER CCC CB    1 ? 3 
ATOM   9579  O OG    . SER C 1 285 ? 60.308  -13.329 39.545  1.000 51.034  0 285 SER CCC OG    1 ? 3 
ATOM   9580  N N     . VAL C 1 286 ? 61.043  -16.872 39.712  1.000 52.358  0 286 VAL CCC N     1 ? 3 
ATOM   9581  C CA    . VAL C 1 286 ? 60.957  -17.875 40.812  1.000 52.464  0 286 VAL CCC CA    1 ? 3 
ATOM   9582  C C     . VAL C 1 286 ? 62.083  -17.548 41.803  1.000 51.086  0 286 VAL CCC C     1 ? 3 
ATOM   9583  O O     . VAL C 1 286 ? 63.131  -17.005 41.367  1.000 50.050  0 286 VAL CCC O     1 ? 3 
ATOM   9584  C CB    . VAL C 1 286 ? 61.042  -19.298 40.218  1.000 56.962  0 286 VAL CCC CB    1 ? 3 
ATOM   9585  C CG1   . VAL C 1 286 ? 61.376  -20.366 41.243  1.000 58.568  0 286 VAL CCC CG1   1 ? 3 
ATOM   9586  C CG2   . VAL C 1 286 ? 59.753  -19.667 39.487  1.000 58.399  0 286 VAL CCC CG2   1 ? 3 
ATOM   9587  N N     . GLU C 1 287 ? 61.880  -17.811 43.090  1.000 51.319  0 287 GLU CCC N     1 ? 3 
ATOM   9588  C CA    . GLU C 1 287 ? 62.953  -17.682 44.119  1.000 53.174  0 287 GLU CCC CA    1 ? 3 
ATOM   9589  C C     . GLU C 1 287 ? 62.585  -18.510 45.349  1.000 52.491  0 287 GLU CCC C     1 ? 3 
ATOM   9590  O O     . GLU C 1 287 ? 61.374  -18.613 45.676  1.000 52.294  0 287 GLU CCC O     1 ? 3 
ATOM   9591  C CB    . GLU C 1 287 ? 63.180  -16.218 44.480  1.000 55.533  0 287 GLU CCC CB    1 ? 3 
ATOM   9592  C CG    . GLU C 1 287 ? 64.543  -15.940 45.086  1.000 58.847  0 287 GLU CCC CG    1 ? 3 
ATOM   9593  C CD    . GLU C 1 287 ? 64.824  -14.478 45.404  1.000 59.768  0 287 GLU CCC CD    1 ? 3 
ATOM   9594  O OE1   . GLU C 1 287 ? 63.920  -13.641 45.177  1.000 60.900  0 287 GLU CCC OE1   1 ? 3 
ATOM   9595  O OE2   . GLU C 1 287 ? 65.903  -14.194 45.978  1.000 59.393  0 287 GLU CCC OE2   1 ? 3 
ATOM   9596  N N     . GLU C 1 288 ? 63.591  -19.104 45.985  1.000 52.570  0 288 GLU CCC N     1 ? 3 
ATOM   9597  C CA    . GLU C 1 288 ? 63.442  -19.944 47.204  1.000 53.452  0 288 GLU CCC CA    1 ? 3 
ATOM   9598  C C     . GLU C 1 288 ? 63.648  -19.064 48.442  1.000 50.815  0 288 GLU CCC C     1 ? 3 
ATOM   9599  O O     . GLU C 1 288 ? 64.503  -18.165 48.419  1.000 45.118  0 288 GLU CCC O     1 ? 3 
ATOM   9600  C CB    . GLU C 1 288 ? 64.369  -21.156 47.139  1.000 58.349  0 288 GLU CCC CB    1 ? 3 
ATOM   9601  C CG    . GLU C 1 288 ? 63.957  -22.122 46.030  1.000 62.573  0 288 GLU CCC CG    1 ? 3 
ATOM   9602  C CD    . GLU C 1 288 ? 64.487  -23.541 46.124  1.000 68.110  0 288 GLU CCC CD    1 ? 3 
ATOM   9603  O OE1   . GLU C 1 288 ? 64.842  -23.969 47.238  1.000 75.524  0 288 GLU CCC OE1   1 ? 3 
ATOM   9604  O OE2   . GLU C 1 288 ? 64.569  -24.207 45.075  1.000 70.303  0 288 GLU CCC OE2   1 ? 3 
ATOM   9605  N N     . PHE C 1 289 ? 62.811  -19.268 49.459  1.000 50.469  0 289 PHE CCC N     1 ? 3 
ATOM   9606  C CA    . PHE C 1 289 ? 62.903  -18.605 50.785  1.000 49.507  0 289 PHE CCC CA    1 ? 3 
ATOM   9607  C C     . PHE C 1 289 ? 62.724  -19.653 51.875  1.000 50.096  0 289 PHE CCC C     1 ? 3 
ATOM   9608  O O     . PHE C 1 289 ? 62.097  -20.691 51.608  1.000 53.334  0 289 PHE CCC O     1 ? 3 
ATOM   9609  C CB    . PHE C 1 289 ? 61.851  -17.502 50.922  1.000 45.934  0 289 PHE CCC CB    1 ? 3 
ATOM   9610  C CG    . PHE C 1 289 ? 61.875  -16.478 49.814  1.000 44.208  0 289 PHE CCC CG    1 ? 3 
ATOM   9611  C CD1   . PHE C 1 289 ? 61.148  -16.689 48.657  1.000 43.695  0 289 PHE CCC CD1   1 ? 3 
ATOM   9612  C CD2   . PHE C 1 289 ? 62.646  -15.326 49.917  1.000 42.256  0 289 PHE CCC CD2   1 ? 3 
ATOM   9613  C CE1   . PHE C 1 289 ? 61.171  -15.755 47.625  1.000 43.219  0 289 PHE CCC CE1   1 ? 3 
ATOM   9614  C CE2   . PHE C 1 289 ? 62.671  -14.405 48.890  1.000 41.529  0 289 PHE CCC CE2   1 ? 3 
ATOM   9615  C CZ    . PHE C 1 289 ? 61.940  -14.621 47.744  1.000 42.256  0 289 PHE CCC CZ    1 ? 3 
ATOM   9616  N N     . GLU C 1 290 ? 63.246  -19.377 53.071  1.000 48.265  0 290 GLU CCC N     1 ? 3 
ATOM   9617  C CA    . GLU C 1 290 ? 62.988  -20.216 54.260  1.000 47.642  0 290 GLU CCC CA    1 ? 3 
ATOM   9618  C C     . GLU C 1 290 ? 61.629  -19.828 54.874  1.000 46.259  0 290 GLU CCC C     1 ? 3 
ATOM   9619  O O     . GLU C 1 290 ? 60.911  -20.726 55.366  1.000 45.011  0 290 GLU CCC O     1 ? 3 
ATOM   9620  C CB    . GLU C 1 290 ? 64.147  -20.052 55.219  1.000 52.136  0 290 GLU CCC CB    1 ? 3 
ATOM   9621  C CG    . GLU C 1 290 ? 64.100  -21.074 56.321  1.000 58.367  0 290 GLU CCC CG    1 ? 3 
ATOM   9622  C CD    . GLU C 1 290 ? 65.322  -21.122 57.210  1.000 62.341  0 290 GLU CCC CD    1 ? 3 
ATOM   9623  O OE1   . GLU C 1 290 ? 65.107  -21.452 58.406  1.000 60.495  0 290 GLU CCC OE1   1 ? 3 
ATOM   9624  O OE2   . GLU C 1 290 ? 66.474  -20.842 56.687  1.000 66.142  0 290 GLU CCC OE2   1 ? 3 
ATOM   9625  N N     . THR C 1 291 ? 61.269  -18.540 54.816  1.000 41.862  0 291 THR CCC N     1 ? 3 
ATOM   9626  C CA    . THR C 1 291 ? 60.065  -17.972 55.460  1.000 40.016  0 291 THR CCC CA    1 ? 3 
ATOM   9627  C C     . THR C 1 291 ? 59.361  -17.036 54.485  1.000 37.900  0 291 THR CCC C     1 ? 3 
ATOM   9628  O O     . THR C 1 291 ? 60.024  -16.231 53.830  1.000 35.157  0 291 THR CCC O     1 ? 3 
ATOM   9629  C CB    . THR C 1 291 ? 60.410  -17.239 56.761  1.000 40.377  0 291 THR CCC CB    1 ? 3 
ATOM   9630  O OG1   . THR C 1 291 ? 61.058  -18.137 57.663  1.000 41.270  0 291 THR CCC OG1   1 ? 3 
ATOM   9631  C CG2   . THR C 1 291 ? 59.210  -16.668 57.480  1.000 38.299  0 291 THR CCC CG2   1 ? 3 
ATOM   9632  N N     . VAL C 1 292 ? 58.045  -17.159 54.422  1.000 36.374  0 292 VAL CCC N     1 ? 3 
ATOM   9633  C CA    . VAL C 1 292 ? 57.190  -16.231 53.635  1.000 37.056  0 292 VAL CCC CA    1 ? 3 
ATOM   9634  C C     . VAL C 1 292 ? 56.145  -15.666 54.587  1.000 36.283  0 292 VAL CCC C     1 ? 3 
ATOM   9635  O O     . VAL C 1 292 ? 55.385  -16.459 55.182  1.000 34.904  0 292 VAL CCC O     1 ? 3 
ATOM   9636  C CB    . VAL C 1 292 ? 56.531  -16.915 52.424  1.000 36.751  0 292 VAL CCC CB    1 ? 3 
ATOM   9637  C CG1   . VAL C 1 292 ? 55.619  -15.966 51.687  1.000 37.842  0 292 VAL CCC CG1   1 ? 3 
ATOM   9638  C CG2   . VAL C 1 292 ? 57.551  -17.497 51.466  1.000 36.674  0 292 VAL CCC CG2   1 ? 3 
ATOM   9639  N N     . LEU C 1 293 ? 56.130  -14.337 54.693  1.000 35.844  0 293 LEU CCC N     1 ? 3 
ATOM   9640  C CA    . LEU C 1 293 ? 55.241  -13.594 55.605  1.000 35.902  0 293 LEU CCC CA    1 ? 3 
ATOM   9641  C C     . LEU C 1 293 ? 54.322  -12.704 54.783  1.000 34.481  0 293 LEU CCC C     1 ? 3 
ATOM   9642  O O     . LEU C 1 293 ? 54.862  -11.832 54.070  1.000 32.337  0 293 LEU CCC O     1 ? 3 
ATOM   9643  C CB    . LEU C 1 293 ? 56.097  -12.760 56.553  1.000 37.305  0 293 LEU CCC CB    1 ? 3 
ATOM   9644  C CG    . LEU C 1 293 ? 55.318  -12.176 57.741  1.000 39.161  0 293 LEU CCC CG    1 ? 3 
ATOM   9645  C CD1   . LEU C 1 293 ? 56.222  -12.022 58.955  1.000 39.220  0 293 LEU CCC CD1   1 ? 3 
ATOM   9646  C CD2   . LEU C 1 293 ? 54.683  -10.845 57.365  1.000 38.466  0 293 LEU CCC CD2   1 ? 3 
ATOM   9647  N N     . TYR C 1 294 ? 53.012  -12.910 54.907  1.000 32.601  0 294 TYR CCC N     1 ? 3 
ATOM   9648  C CA    . TYR C 1 294 ? 51.983  -12.036 54.274  1.000 34.769  0 294 TYR CCC CA    1 ? 3 
ATOM   9649  C C     . TYR C 1 294 ? 51.649  -10.854 55.200  1.000 32.540  0 294 TYR CCC C     1 ? 3 
ATOM   9650  O O     . TYR C 1 294 ? 51.118  -11.099 56.304  1.000 30.872  0 294 TYR CCC O     1 ? 3 
ATOM   9651  C CB    . TYR C 1 294 ? 50.702  -12.816 53.921  1.000 34.740  0 294 TYR CCC CB    1 ? 3 
ATOM   9652  C CG    . TYR C 1 294 ? 50.716  -13.334 52.507  1.000 35.974  0 294 TYR CCC CG    1 ? 3 
ATOM   9653  C CD1   . TYR C 1 294 ? 50.417  -12.507 51.429  1.000 36.172  0 294 TYR CCC CD1   1 ? 3 
ATOM   9654  C CD2   . TYR C 1 294 ? 51.098  -14.642 52.230  1.000 38.208  0 294 TYR CCC CD2   1 ? 3 
ATOM   9655  C CE1   . TYR C 1 294 ? 50.495  -12.962 50.119  1.000 36.015  0 294 TYR CCC CE1   1 ? 3 
ATOM   9656  C CE2   . TYR C 1 294 ? 51.183  -15.112 50.927  1.000 36.203  0 294 TYR CCC CE2   1 ? 3 
ATOM   9657  C CZ    . TYR C 1 294 ? 50.882  -14.272 49.872  1.000 36.380  0 294 TYR CCC CZ    1 ? 3 
ATOM   9658  O OH    . TYR C 1 294 ? 50.932  -14.754 48.591  1.000 39.541  0 294 TYR CCC OH    1 ? 3 
ATOM   9659  N N     . ALA C 1 295 ? 51.933  -9.632  54.745  1.000 31.588  0 295 ALA CCC N     1 ? 3 
ATOM   9660  C CA    . ALA C 1 295 ? 51.541  -8.378  55.431  1.000 32.039  0 295 ALA CCC CA    1 ? 3 
ATOM   9661  C C     . ALA C 1 295 ? 50.688  -7.544  54.480  1.000 31.378  0 295 ALA CCC C     1 ? 3 
ATOM   9662  O O     . ALA C 1 295 ? 51.014  -6.364  54.235  1.000 32.283  0 295 ALA CCC O     1 ? 3 
ATOM   9663  C CB    . ALA C 1 295 ? 52.770  -7.630  55.888  1.000 33.510  0 295 ALA CCC CB    1 ? 3 
ATOM   9664  N N     . THR C 1 296 ? 49.638  -8.142  53.935  1.000 31.311  0 296 THR CCC N     1 ? 3 
ATOM   9665  C CA    . THR C 1 296 ? 48.877  -7.534  52.814  1.000 31.203  0 296 THR CCC CA    1 ? 3 
ATOM   9666  C C     . THR C 1 296 ? 47.711  -6.740  53.394  1.000 32.809  0 296 THR CCC C     1 ? 3 
ATOM   9667  O O     . THR C 1 296 ? 47.176  -5.840  52.684  1.000 35.866  0 296 THR CCC O     1 ? 3 
ATOM   9668  C CB    . THR C 1 296 ? 48.507  -8.584  51.763  1.000 29.758  0 296 THR CCC CB    1 ? 3 
ATOM   9669  O OG1   . THR C 1 296 ? 48.065  -9.781  52.421  1.000 28.704  0 296 THR CCC OG1   1 ? 3 
ATOM   9670  C CG2   . THR C 1 296 ? 49.689  -8.888  50.859  1.000 29.898  0 296 THR CCC CG2   1 ? 3 
ATOM   9671  N N     . GLY C 1 297 ? 47.333  -7.055  54.627  1.000 33.072  0 297 GLY CCC N     1 ? 3 
ATOM   9672  C CA    . GLY C 1 297 ? 46.234  -6.354  55.310  1.000 32.064  0 297 GLY CCC CA    1 ? 3 
ATOM   9673  C C     . GLY C 1 297 ? 45.621  -7.214  56.387  1.000 32.111  0 297 GLY CCC C     1 ? 3 
ATOM   9674  O O     . GLY C 1 297 ? 46.182  -8.298  56.714  1.000 27.851  0 297 GLY CCC O     1 ? 3 
ATOM   9675  N N     . ARG C 1 298 ? 44.496  -6.731  56.909  1.000 33.676  0 298 ARG CCC N     1 ? 3 
ATOM   9676  C CA    . ARG C 1 298 ? 43.791  -7.324  58.077  1.000 33.888  0 298 ARG CCC CA    1 ? 3 
ATOM   9677  C C     . ARG C 1 298 ? 42.299  -7.192  57.828  1.000 35.706  0 298 ARG CCC C     1 ? 3 
ATOM   9678  O O     . ARG C 1 298 ? 41.861  -6.113  57.438  1.000 40.270  0 298 ARG CCC O     1 ? 3 
ATOM   9679  C CB    . ARG C 1 298 ? 44.231  -6.627  59.380  1.000 33.194  0 298 ARG CCC CB    1 ? 3 
ATOM   9680  C CG    . ARG C 1 298 ? 45.673  -6.898  59.805  1.000 32.829  0 298 ARG CCC CG    1 ? 3 
ATOM   9681  C CD    . ARG C 1 298 ? 46.190  -5.990  60.914  1.000 32.847  0 298 ARG CCC CD    1 ? 3 
ATOM   9682  N NE    . ARG C 1 298 ? 45.522  -6.278  62.179  1.000 32.524  0 298 ARG CCC NE    1 ? 3 
ATOM   9683  C CZ    . ARG C 1 298 ? 45.844  -7.249  63.029  1.000 33.691  0 298 ARG CCC CZ    1 ? 3 
ATOM   9684  N NH1   . ARG C 1 298 ? 46.838  -8.083  62.806  1.000 36.184  0 298 ARG CCC NH1   1 ? 3 
ATOM   9685  N NH2   . ARG C 1 298 ? 45.160  -7.406  64.133  1.000 36.269  0 298 ARG CCC NH2   1 ? 3 
ATOM   9686  N N     . ASN C 1 299 ? 41.548  -8.258  58.079  1.000 38.184  0 299 ASN CCC N     1 ? 3 
ATOM   9687  C CA    . ASN C 1 299 ? 40.062  -8.257  58.074  1.000 36.403  0 299 ASN CCC CA    1 ? 3 
ATOM   9688  C C     . ASN C 1 299 ? 39.537  -8.139  59.486  1.000 37.859  0 299 ASN CCC C     1 ? 3 
ATOM   9689  O O     . ASN C 1 299 ? 40.105  -8.725  60.400  1.000 42.726  0 299 ASN CCC O     1 ? 3 
ATOM   9690  C CB    . ASN C 1 299 ? 39.496  -9.541  57.490  1.000 37.200  0 299 ASN CCC CB    1 ? 3 
ATOM   9691  C CG    . ASN C 1 299 ? 39.869  -9.701  56.027  1.000 36.587  0 299 ASN CCC CG    1 ? 3 
ATOM   9692  O OD1   . ASN C 1 299 ? 40.311  -10.758 55.601  1.000 35.483  0 299 ASN CCC OD1   1 ? 3 
ATOM   9693  N ND2   . ASN C 1 299 ? 39.720  -8.637  55.263  1.000 36.869  0 299 ASN CCC ND2   1 ? 3 
ATOM   9694  N N     . PRO C 1 300 ? 38.454  -7.370  59.695  1.000 36.169  0 300 PRO CCC N     1 ? 3 
ATOM   9695  C CA    . PRO C 1 300 ? 37.798  -7.290  61.001  1.000 36.323  0 300 PRO CCC CA    1 ? 3 
ATOM   9696  C C     . PRO C 1 300 ? 37.199  -8.637  61.416  1.000 35.289  0 300 PRO CCC C     1 ? 3 
ATOM   9697  O O     . PRO C 1 300 ? 36.544  -9.259  60.634  1.000 38.122  0 300 PRO CCC O     1 ? 3 
ATOM   9698  C CB    . PRO C 1 300 ? 36.675  -6.261  60.773  1.000 36.919  0 300 PRO CCC CB    1 ? 3 
ATOM   9699  C CG    . PRO C 1 300 ? 36.453  -6.276  59.273  1.000 36.175  0 300 PRO CCC CG    1 ? 3 
ATOM   9700  C CD    . PRO C 1 300 ? 37.820  -6.513  58.689  1.000 35.655  0 300 PRO CCC CD    1 ? 3 
ATOM   9701  N N     . ASP C 1 301 ? 37.494  -9.078  62.625  1.000 35.477  0 301 ASP CCC N     1 ? 3 
ATOM   9702  C CA    . ASP C 1 301 ? 37.098  -10.413 63.140  1.000 36.048  0 301 ASP CCC CA    1 ? 3 
ATOM   9703  C C     . ASP C 1 301 ? 35.686  -10.295 63.715  1.000 37.833  0 301 ASP CCC C     1 ? 3 
ATOM   9704  O O     . ASP C 1 301 ? 35.546  -10.161 64.938  1.000 35.674  0 301 ASP CCC O     1 ? 3 
ATOM   9705  C CB    . ASP C 1 301 ? 38.114  -10.918 64.148  1.000 36.420  0 301 ASP CCC CB    1 ? 3 
ATOM   9706  C CG    . ASP C 1 301 ? 37.847  -12.340 64.584  1.000 37.896  0 301 ASP CCC CG    1 ? 3 
ATOM   9707  O OD1   . ASP C 1 301 ? 37.295  -13.131 63.757  1.000 38.341  0 301 ASP CCC OD1   1 ? 3 
ATOM   9708  O OD2   . ASP C 1 301 ? 38.162  -12.630 65.767  1.000 36.573  0 301 ASP CCC OD2   1 ? 3 
ATOM   9709  N N     . VAL C 1 302 ? 34.685  -10.297 62.828  1.000 39.948  0 302 VAL CCC N     1 ? 3 
ATOM   9710  C CA    . VAL C 1 302 ? 33.270  -10.029 63.186  1.000 43.588  0 302 VAL CCC CA    1 ? 3 
ATOM   9711  C C     . VAL C 1 302 ? 32.366  -11.182 62.744  1.000 47.653  0 302 VAL CCC C     1 ? 3 
ATOM   9712  O O     . VAL C 1 302 ? 31.136  -11.132 63.080  1.000 50.212  0 302 VAL CCC O     1 ? 3 
ATOM   9713  C CB    . VAL C 1 302 ? 32.817  -8.688  62.590  1.000 41.784  0 302 VAL CCC CB    1 ? 3 
ATOM   9714  C CG1   . VAL C 1 302 ? 33.586  -7.545  63.236  1.000 42.356  0 302 VAL CCC CG1   1 ? 3 
ATOM   9715  C CG2   . VAL C 1 302 ? 32.918  -8.661  61.076  1.000 39.946  0 302 VAL CCC CG2   1 ? 3 
ATOM   9716  N N     . LYS C 1 303 ? 32.927  -12.183 62.057  1.000 49.257  0 303 LYS CCC N     1 ? 3 
ATOM   9717  C CA    . LYS C 1 303 ? 32.131  -13.275 61.445  1.000 54.574  0 303 LYS CCC CA    1 ? 3 
ATOM   9718  C C     . LYS C 1 303 ? 31.409  -14.071 62.548  1.000 52.046  0 303 LYS CCC C     1 ? 3 
ATOM   9719  O O     . LYS C 1 303 ? 30.243  -14.424 62.349  1.000 53.084  0 303 LYS CCC O     1 ? 3 
ATOM   9720  C CB    . LYS C 1 303 ? 33.052  -14.112 60.551  1.000 58.464  0 303 LYS CCC CB    1 ? 3 
ATOM   9721  C CG    . LYS C 1 303 ? 33.597  -13.371 59.335  1.000 61.720  0 303 LYS CCC CG    1 ? 3 
ATOM   9722  C CD    . LYS C 1 303 ? 34.339  -14.276 58.363  1.000 67.940  0 303 LYS CCC CD    1 ? 3 
ATOM   9723  C CE    . LYS C 1 303 ? 34.290  -13.813 56.914  1.000 70.455  0 303 LYS CCC CE    1 ? 3 
ATOM   9724  N NZ    . LYS C 1 303 ? 34.955  -14.795 56.020  1.000 74.643  0 303 LYS CCC NZ    1 ? 3 
ATOM   9725  N N     . GLY C 1 304 ? 32.054  -14.280 63.697  1.000 50.250  0 304 GLY CCC N     1 ? 3 
ATOM   9726  C CA    . GLY C 1 304 ? 31.493  -15.058 64.813  1.000 49.078  0 304 GLY CCC CA    1 ? 3 
ATOM   9727  C C     . GLY C 1 304 ? 30.468  -14.271 65.614  1.000 47.015  0 304 GLY CCC C     1 ? 3 
ATOM   9728  O O     . GLY C 1 304 ? 29.885  -14.870 66.530  1.000 46.707  0 304 GLY CCC O     1 ? 3 
ATOM   9729  N N     . LEU C 1 305 ? 30.225  -12.995 65.301  1.000 45.633  0 305 LEU CCC N     1 ? 3 
ATOM   9730  C CA    . LEU C 1 305 ? 29.458  -12.090 66.202  1.000 46.145  0 305 LEU CCC CA    1 ? 3 
ATOM   9731  C C     . LEU C 1 305 ? 27.948  -12.187 65.949  1.000 47.433  0 305 LEU CCC C     1 ? 3 
ATOM   9732  O O     . LEU C 1 305 ? 27.195  -11.708 66.833  1.000 50.365  0 305 LEU CCC O     1 ? 3 
ATOM   9733  C CB    . LEU C 1 305 ? 29.943  -10.647 66.024  1.000 44.574  0 305 LEU CCC CB    1 ? 3 
ATOM   9734  C CG    . LEU C 1 305 ? 31.302  -10.345 66.637  1.000 43.239  0 305 LEU CCC CG    1 ? 3 
ATOM   9735  C CD1   . LEU C 1 305 ? 31.732  -8.913  66.354  1.000 43.162  0 305 LEU CCC CD1   1 ? 3 
ATOM   9736  C CD2   . LEU C 1 305 ? 31.298  -10.624 68.129  1.000 42.376  0 305 LEU CCC CD2   1 ? 3 
ATOM   9737  N N     . ASN C 1 306 ? 27.516  -12.733 64.807  1.000 47.507  0 306 ASN CCC N     1 ? 3 
ATOM   9738  C CA    . ASN C 1 306 ? 26.076  -12.824 64.449  1.000 49.898  0 306 ASN CCC CA    1 ? 3 
ATOM   9739  C C     . ASN C 1 306 ? 25.517  -11.416 64.195  1.000 49.222  0 306 ASN CCC C     1 ? 3 
ATOM   9740  O O     . ASN C 1 306 ? 24.384  -11.130 64.677  1.000 48.585  0 306 ASN CCC O     1 ? 3 
ATOM   9741  C CB    . ASN C 1 306 ? 25.295  -13.559 65.543  1.000 50.775  0 306 ASN CCC CB    1 ? 3 
ATOM   9742  C CG    . ASN C 1 306 ? 23.962  -14.098 65.075  1.000 53.080  0 306 ASN CCC CG    1 ? 3 
ATOM   9743  O OD1   . ASN C 1 306 ? 23.773  -14.372 63.883  1.000 54.735  0 306 ASN CCC OD1   1 ? 3 
ATOM   9744  N ND2   . ASN C 1 306 ? 23.034  -14.250 66.016  1.000 52.703  0 306 ASN CCC ND2   1 ? 3 
ATOM   9745  N N     . LEU C 1 307 ? 26.256  -10.581 63.450  1.000 48.563  0 307 LEU CCC N     1 ? 3 
ATOM   9746  C CA    . LEU C 1 307 ? 25.882  -9.149  63.211  1.000 49.179  0 307 LEU CCC CA    1 ? 3 
ATOM   9747  C C     . LEU C 1 307 ? 24.646  -9.054  62.306  1.000 51.044  0 307 LEU CCC C     1 ? 3 
ATOM   9748  O O     . LEU C 1 307 ? 23.750  -8.231  62.594  1.000 50.313  0 307 LEU CCC O     1 ? 3 
ATOM   9749  C CB    . LEU C 1 307 ? 27.046  -8.373  62.595  1.000 46.156  0 307 LEU CCC CB    1 ? 3 
ATOM   9750  C CG    . LEU C 1 307 ? 28.315  -8.276  63.454  1.000 45.202  0 307 LEU CCC CG    1 ? 3 
ATOM   9751  C CD1   . LEU C 1 307 ? 29.378  -7.484  62.734  1.000 43.179  0 307 LEU CCC CD1   1 ? 3 
ATOM   9752  C CD2   . LEU C 1 307 ? 28.024  -7.641  64.812  1.000 45.113  0 307 LEU CCC CD2   1 ? 3 
ATOM   9753  N N     . ASN C 1 308 ? 24.615  -9.871  61.253  1.000 53.278  0 308 ASN CCC N     1 ? 3 
ATOM   9754  C CA    . ASN C 1 308 ? 23.565  -9.860  60.210  1.000 55.032  0 308 ASN CCC CA    1 ? 3 
ATOM   9755  C C     . ASN C 1 308 ? 22.179  -9.994  60.854  1.000 54.606  0 308 ASN CCC C     1 ? 3 
ATOM   9756  O O     . ASN C 1 308 ? 21.305  -9.142  60.568  1.000 50.403  0 308 ASN CCC O     1 ? 3 
ATOM   9757  C CB    . ASN C 1 308 ? 23.796  -10.975 59.193  1.000 57.701  0 308 ASN CCC CB    1 ? 3 
ATOM   9758  C CG    . ASN C 1 308 ? 22.998  -10.782 57.929  1.000 58.910  0 308 ASN CCC CG    1 ? 3 
ATOM   9759  O OD1   . ASN C 1 308 ? 21.991  -10.071 57.922  1.000 59.977  0 308 ASN CCC OD1   1 ? 3 
ATOM   9760  N ND2   . ASN C 1 308 ? 23.462  -11.415 56.860  1.000 63.810  0 308 ASN CCC ND2   1 ? 3 
ATOM   9761  N N     . ALA C 1 309 ? 22.004  -11.017 61.695  1.000 55.064  0 309 ALA CCC N     1 ? 3 
ATOM   9762  C CA    . ALA C 1 309 ? 20.709  -11.389 62.314  1.000 53.418  0 309 ALA CCC CA    1 ? 3 
ATOM   9763  C C     . ALA C 1 309 ? 20.241  -10.298 63.294  1.000 54.383  0 309 ALA CCC C     1 ? 3 
ATOM   9764  O O     . ALA C 1 309 ? 18.996  -10.162 63.478  1.000 53.667  0 309 ALA CCC O     1 ? 3 
ATOM   9765  C CB    . ALA C 1 309 ? 20.829  -12.736 62.983  1.000 51.024  0 309 ALA CCC CB    1 ? 3 
ATOM   9766  N N     . ILE C 1 310 ? 21.165  -9.530  63.901  1.000 50.876  0 310 ILE CCC N     1 ? 3 
ATOM   9767  C CA    . ILE C 1 310 ? 20.812  -8.540  64.961  1.000 50.186  0 310 ILE CCC CA    1 ? 3 
ATOM   9768  C C     . ILE C 1 310 ? 20.511  -7.176  64.337  1.000 48.216  0 310 ILE CCC C     1 ? 3 
ATOM   9769  O O     . ILE C 1 310 ? 19.860  -6.366  65.000  1.000 48.184  0 310 ILE CCC O     1 ? 3 
ATOM   9770  C CB    . ILE C 1 310 ? 21.916  -8.458  66.027  1.000 55.062  0 310 ILE CCC CB    1 ? 3 
ATOM   9771  C CG1   . ILE C 1 310 ? 22.242  -9.844  66.589  1.000 57.000  0 310 ILE CCC CG1   1 ? 3 
ATOM   9772  C CG2   . ILE C 1 310 ? 21.532  -7.479  67.129  1.000 55.545  0 310 ILE CCC CG2   1 ? 3 
ATOM   9773  C CD1   . ILE C 1 310 ? 21.014  -10.701 66.890  1.000 59.785  0 310 ILE CCC CD1   1 ? 3 
ATOM   9774  N N     . GLY C 1 311 ? 20.943  -6.946  63.099  1.000 48.598  0 311 GLY CCC N     1 ? 3 
ATOM   9775  C CA    . GLY C 1 311 ? 20.742  -5.681  62.356  1.000 47.614  0 311 GLY CCC CA    1 ? 3 
ATOM   9776  C C     . GLY C 1 311 ? 21.911  -4.706  62.538  1.000 45.861  0 311 GLY CCC C     1 ? 3 
ATOM   9777  O O     . GLY C 1 311 ? 21.684  -3.506  62.385  1.000 47.437  0 311 GLY CCC O     1 ? 3 
ATOM   9778  N N     . VAL C 1 312 ? 23.121  -5.186  62.835  1.000 41.582  0 312 VAL CCC N     1 ? 3 
ATOM   9779  C CA    . VAL C 1 312 ? 24.320  -4.306  62.946  1.000 44.473  0 312 VAL CCC CA    1 ? 3 
ATOM   9780  C C     . VAL C 1 312 ? 24.908  -4.157  61.549  1.000 43.731  0 312 VAL CCC C     1 ? 3 
ATOM   9781  O O     . VAL C 1 312 ? 25.404  -5.182  61.007  1.000 42.665  0 312 VAL CCC O     1 ? 3 
ATOM   9782  C CB    . VAL C 1 312 ? 25.387  -4.834  63.926  1.000 43.904  0 312 VAL CCC CB    1 ? 3 
ATOM   9783  C CG1   . VAL C 1 312 ? 26.676  -4.043  63.772  1.000 43.658  0 312 VAL CCC CG1   1 ? 3 
ATOM   9784  C CG2   . VAL C 1 312 ? 24.904  -4.816  65.375  1.000 42.704  0 312 VAL CCC CG2   1 ? 3 
ATOM   9785  N N     . GLU C 1 313 ? 24.871  -2.937  60.997  1.000 42.555  0 313 GLU CCC N     1 ? 3 
ATOM   9786  C CA    . GLU C 1 313 ? 25.206  -2.707  59.569  1.000 44.969  0 313 GLU CCC CA    1 ? 3 
ATOM   9787  C C     . GLU C 1 313 ? 26.717  -2.814  59.376  1.000 43.988  0 313 GLU CCC C     1 ? 3 
ATOM   9788  O O     . GLU C 1 313 ? 27.481  -2.311  60.230  1.000 41.055  0 313 GLU CCC O     1 ? 3 
ATOM   9789  C CB    . GLU C 1 313 ? 24.630  -1.379  59.072  1.000 49.412  0 313 GLU CCC CB    1 ? 3 
ATOM   9790  C CG    . GLU C 1 313 ? 23.086  -1.352  59.005  1.000 55.803  0 313 GLU CCC CG    1 ? 3 
ATOM   9791  C CD    . GLU C 1 313 ? 22.330  -2.414  58.180  1.000 59.244  0 313 GLU CCC CD    1 ? 3 
ATOM   9792  O OE1   . GLU C 1 313 ? 22.637  -2.612  56.949  1.000 56.896  0 313 GLU CCC OE1   1 ? 3 
ATOM   9793  O OE2   . GLU C 1 313 ? 21.404  -3.049  58.761  1.000 62.550  0 313 GLU CCC OE2   1 ? 3 
ATOM   9794  N N     . VAL C 1 314 ? 27.126  -3.447  58.276  1.000 46.163  0 314 VAL CCC N     1 ? 3 
ATOM   9795  C CA    . VAL C 1 314 ? 28.562  -3.587  57.903  1.000 46.391  0 314 VAL CCC CA    1 ? 3 
ATOM   9796  C C     . VAL C 1 314 ? 28.752  -2.989  56.504  1.000 45.826  0 314 VAL CCC C     1 ? 3 
ATOM   9797  O O     . VAL C 1 314 ? 27.799  -3.029  55.687  1.000 42.224  0 314 VAL CCC O     1 ? 3 
ATOM   9798  C CB    . VAL C 1 314 ? 29.047  -5.049  57.992  1.000 46.917  0 314 VAL CCC CB    1 ? 3 
ATOM   9799  C CG1   . VAL C 1 314 ? 28.890  -5.604  59.394  1.000 44.538  0 314 VAL CCC CG1   1 ? 3 
ATOM   9800  C CG2   . VAL C 1 314 ? 28.345  -5.956  56.979  1.000 48.302  0 314 VAL CCC CG2   1 ? 3 
ATOM   9801  N N     . SER C 1 315 ? 29.943  -2.439  56.251  1.000 43.396  0 315 SER CCC N     1 ? 3 
ATOM   9802  C CA    . SER C 1 315 ? 30.352  -1.915  54.931  1.000 41.465  0 315 SER CCC CA    1 ? 3 
ATOM   9803  C C     . SER C 1 315 ? 30.750  -3.080  54.012  1.000 41.718  0 315 SER CCC C     1 ? 3 
ATOM   9804  O O     . SER C 1 315 ? 30.708  -4.242  54.465  1.000 36.546  0 315 SER CCC O     1 ? 3 
ATOM   9805  C CB    . SER C 1 315 ? 31.454  -0.926  55.091  1.000 42.266  0 315 SER CCC CB    1 ? 3 
ATOM   9806  O OG    . SER C 1 315 ? 32.679  -1.578  55.362  1.000 41.558  0 315 SER CCC OG    1 ? 3 
ATOM   9807  N N     . ASP C 1 316 ? 31.140  -2.774  52.770  1.000 43.731  0 316 ASP CCC N     1 ? 3 
ATOM   9808  C CA    . ASP C 1 316 ? 31.587  -3.791  51.774  1.000 47.887  0 316 ASP CCC CA    1 ? 3 
ATOM   9809  C C     . ASP C 1 316 ? 32.863  -4.483  52.276  1.000 47.665  0 316 ASP CCC C     1 ? 3 
ATOM   9810  O O     . ASP C 1 316 ? 33.050  -5.670  51.957  1.000 48.937  0 316 ASP CCC O     1 ? 3 
ATOM   9811  C CB    . ASP C 1 316 ? 31.786  -3.190  50.383  1.000 48.417  0 316 ASP CCC CB    1 ? 3 
ATOM   9812  C CG    . ASP C 1 316 ? 30.504  -2.743  49.704  1.000 49.722  0 316 ASP CCC CG    1 ? 3 
ATOM   9813  O OD1   . ASP C 1 316 ? 29.427  -3.359  49.958  1.000 44.602  0 316 ASP CCC OD1   1 ? 3 
ATOM   9814  O OD2   . ASP C 1 316 ? 30.610  -1.814  48.868  1.000 52.984  0 316 ASP CCC OD2   1 ? 3 
ATOM   9815  N N     . SER C 1 317 ? 33.664  -3.787  53.081  1.000 48.511  0 317 SER CCC N     1 ? 3 
ATOM   9816  C CA    . SER C 1 317 ? 34.949  -4.303  53.636  1.000 49.397  0 317 SER CCC CA    1 ? 3 
ATOM   9817  C C     . SER C 1 317 ? 34.707  -5.212  54.853  1.000 48.359  0 317 SER CCC C     1 ? 3 
ATOM   9818  O O     . SER C 1 317 ? 35.686  -5.857  55.293  1.000 39.689  0 317 SER CCC O     1 ? 3 
ATOM   9819  C CB    . SER C 1 317 ? 35.888  -3.178  53.988  1.000 47.795  0 317 SER CCC CB    1 ? 3 
ATOM   9820  O OG    . SER C 1 317 ? 35.355  -2.405  55.048  1.000 46.208  0 317 SER CCC OG    1 ? 3 
ATOM   9821  N N     . GLY C 1 318 ? 33.459  -5.292  55.351  1.000 45.397  0 318 GLY CCC N     1 ? 3 
ATOM   9822  C CA    . GLY C 1 318 ? 33.104  -6.092  56.540  1.000 43.509  0 318 GLY CCC CA    1 ? 3 
ATOM   9823  C C     . GLY C 1 318 ? 33.254  -5.278  57.813  1.000 42.010  0 318 GLY CCC C     1 ? 3 
ATOM   9824  O O     . GLY C 1 318 ? 32.983  -5.809  58.900  1.000 44.384  0 318 GLY CCC O     1 ? 3 
ATOM   9825  N N     . LYS C 1 319 ? 33.652  -4.010  57.715  1.000 41.217  0 319 LYS CCC N     1 ? 3 
ATOM   9826  C CA    . LYS C 1 319 ? 33.800  -3.137  58.908  1.000 40.389  0 319 LYS CCC CA    1 ? 3 
ATOM   9827  C C     . LYS C 1 319 ? 32.410  -2.662  59.356  1.000 40.882  0 319 LYS CCC C     1 ? 3 
ATOM   9828  O O     . LYS C 1 319 ? 31.499  -2.480  58.509  1.000 42.146  0 319 LYS CCC O     1 ? 3 
ATOM   9829  C CB    . LYS C 1 319 ? 34.756  -1.983  58.615  1.000 39.265  0 319 LYS CCC CB    1 ? 3 
ATOM   9830  C CG    . LYS C 1 319 ? 36.230  -2.378  58.646  1.000 39.289  0 319 LYS CCC CG    1 ? 3 
ATOM   9831  C CD    . LYS C 1 319 ? 37.205  -1.219  58.851  1.000 38.929  0 319 LYS CCC CD    1 ? 3 
ATOM   9832  C CE    . LYS C 1 319 ? 38.646  -1.691  58.934  1.000 39.166  0 319 LYS CCC CE    1 ? 3 
ATOM   9833  N NZ    . LYS C 1 319 ? 39.532  -0.713  59.616  1.000 40.582  0 319 LYS CCC NZ    1 ? 3 
ATOM   9834  N N     . ILE C 1 320 ? 32.234  -2.513  60.667  1.000 39.919  0 320 ILE CCC N     1 ? 3 
ATOM   9835  C CA    . ILE C 1 320 ? 30.978  -2.011  61.276  1.000 39.212  0 320 ILE CCC CA    1 ? 3 
ATOM   9836  C C     . ILE C 1 320 ? 30.847  -0.519  60.972  1.000 37.871  0 320 ILE CCC C     1 ? 3 
ATOM   9837  O O     . ILE C 1 320 ? 31.843  0.203   61.121  1.000 34.020  0 320 ILE CCC O     1 ? 3 
ATOM   9838  C CB    . ILE C 1 320 ? 30.972  -2.288  62.783  1.000 42.411  0 320 ILE CCC CB    1 ? 3 
ATOM   9839  C CG1   . ILE C 1 320 ? 31.081  -3.793  63.058  1.000 43.250  0 320 ILE CCC CG1   1 ? 3 
ATOM   9840  C CG2   . ILE C 1 320 ? 29.744  -1.637  63.422  1.000 41.597  0 320 ILE CCC CG2   1 ? 3 
ATOM   9841  C CD1   . ILE C 1 320 ? 31.035  -4.149  64.508  1.000 42.007  0 320 ILE CCC CD1   1 ? 3 
ATOM   9842  N N     . ILE C 1 321 ? 29.647  -0.090  60.574  1.000 39.164  0 321 ILE CCC N     1 ? 3 
ATOM   9843  C CA    . ILE C 1 321 ? 29.326  1.342   60.336  1.000 41.953  0 321 ILE CCC CA    1 ? 3 
ATOM   9844  C C     . ILE C 1 321 ? 28.967  1.922   61.700  1.000 42.293  0 321 ILE CCC C     1 ? 3 
ATOM   9845  O O     . ILE C 1 321 ? 27.984  1.474   62.292  1.000 49.044  0 321 ILE CCC O     1 ? 3 
ATOM   9846  C CB    . ILE C 1 321 ? 28.221  1.502   59.260  1.000 44.912  0 321 ILE CCC CB    1 ? 3 
ATOM   9847  C CG1   . ILE C 1 321 ? 28.734  1.097   57.871  1.000 46.785  0 321 ILE CCC CG1   1 ? 3 
ATOM   9848  C CG2   . ILE C 1 321 ? 27.654  2.916   59.239  1.000 44.500  0 321 ILE CCC CG2   1 ? 3 
ATOM   9849  C CD1   . ILE C 1 321 ? 27.616  0.736   56.912  1.000 47.381  0 321 ILE CCC CD1   1 ? 3 
ATOM   9850  N N     . ALA C 1 322 ? 29.796  2.828   62.209  1.000 41.785  0 322 ALA CCC N     1 ? 3 
ATOM   9851  C CA    . ALA C 1 322 ? 29.648  3.459   63.544  1.000 43.147  0 322 ALA CCC CA    1 ? 3 
ATOM   9852  C C     . ALA C 1 322 ? 30.491  4.723   63.595  1.000 41.453  0 322 ALA CCC C     1 ? 3 
ATOM   9853  O O     . ALA C 1 322 ? 31.420  4.805   64.372  1.000 37.448  0 322 ALA CCC O     1 ? 3 
ATOM   9854  C CB    . ALA C 1 322 ? 30.019  2.486   64.644  1.000 43.173  0 322 ALA CCC CB    1 ? 3 
ATOM   9855  N N     . PRO C 1 323 ? 30.186  5.731   62.746  1.000 43.995  0 323 PRO CCC N     1 ? 3 
ATOM   9856  C CA    . PRO C 1 323 ? 31.067  6.886   62.579  1.000 43.888  0 323 PRO CCC CA    1 ? 3 
ATOM   9857  C C     . PRO C 1 323 ? 31.249  7.645   63.907  1.000 42.777  0 323 PRO CCC C     1 ? 3 
ATOM   9858  O O     . PRO C 1 323 ? 32.224  8.337   64.012  1.000 41.432  0 323 PRO CCC O     1 ? 3 
ATOM   9859  C CB    . PRO C 1 323 ? 30.379  7.743   61.484  1.000 43.693  0 323 PRO CCC CB    1 ? 3 
ATOM   9860  C CG    . PRO C 1 323 ? 28.932  7.260   61.440  1.000 43.556  0 323 PRO CCC CG    1 ? 3 
ATOM   9861  C CD    . PRO C 1 323 ? 28.979  5.807   61.892  1.000 44.246  0 323 PRO CCC CD    1 ? 3 
ATOM   9862  N N     . LYS C 1 324 ? 30.304  7.508   64.841  1.000 43.257  0 324 LYS CCC N     1 ? 3 
ATOM   9863  C CA    . LYS C 1 324 ? 30.321  8.105   66.202  1.000 45.231  0 324 LYS CCC CA    1 ? 3 
ATOM   9864  C C     . LYS C 1 324 ? 30.278  6.993   67.262  1.000 41.442  0 324 LYS CCC C     1 ? 3 
ATOM   9865  O O     . LYS C 1 324 ? 29.719  7.222   68.335  1.000 44.080  0 324 LYS CCC O     1 ? 3 
ATOM   9866  C CB    . LYS C 1 324 ? 29.102  9.027   66.341  1.000 52.120  0 324 LYS CCC CB    1 ? 3 
ATOM   9867  C CG    . LYS C 1 324 ? 29.157  10.306  65.519  1.000 56.032  0 324 LYS CCC CG    1 ? 3 
ATOM   9868  C CD    . LYS C 1 324 ? 28.679  11.519  66.301  1.000 61.931  0 324 LYS CCC CD    1 ? 3 
ATOM   9869  C CE    . LYS C 1 324 ? 28.685  12.806  65.499  1.000 64.466  0 324 LYS CCC CE    1 ? 3 
ATOM   9870  N NZ    . LYS C 1 324 ? 27.495  13.663  65.771  1.000 67.375  0 324 LYS CCC NZ    1 ? 3 
ATOM   9871  N N     . ASP C 1 325 ? 30.796  5.808   66.962  1.000 37.348  0 325 ASP CCC N     1 ? 3 
ATOM   9872  C CA    . ASP C 1 325 ? 30.872  4.625   67.867  1.000 37.708  0 325 ASP CCC CA    1 ? 3 
ATOM   9873  C C     . ASP C 1 325 ? 29.511  3.908   67.972  1.000 37.192  0 325 ASP CCC C     1 ? 3 
ATOM   9874  O O     . ASP C 1 325 ? 29.516  2.705   68.292  1.000 36.450  0 325 ASP CCC O     1 ? 3 
ATOM   9875  C CB    . ASP C 1 325 ? 31.413  5.008   69.246  1.000 40.500  0 325 ASP CCC CB    1 ? 3 
ATOM   9876  C CG    . ASP C 1 325 ? 32.691  5.829   69.271  1.000 39.694  0 325 ASP CCC CG    1 ? 3 
ATOM   9877  O OD1   . ASP C 1 325 ? 33.487  5.713   68.328  1.000 36.111  0 325 ASP CCC OD1   1 ? 3 
ATOM   9878  O OD2   . ASP C 1 325 ? 32.883  6.562   70.252  1.000 42.622  0 325 ASP CCC OD2   1 ? 3 
ATOM   9879  N N     . ALA C 1 326 ? 28.392  4.595   67.694  1.000 35.786  0 326 ALA CCC N     1 ? 3 
ATOM   9880  C CA    . ALA C 1 326 ? 27.022  4.028   67.717  1.000 36.423  0 326 ALA CCC CA    1 ? 3 
ATOM   9881  C C     . ALA C 1 326 ? 26.754  3.281   66.397  1.000 37.361  0 326 ALA CCC C     1 ? 3 
ATOM   9882  O O     . ALA C 1 326 ? 26.842  3.911   65.324  1.000 36.254  0 326 ALA CCC O     1 ? 3 
ATOM   9883  C CB    . ALA C 1 326 ? 26.001  5.120   67.972  1.000 35.927  0 326 ALA CCC CB    1 ? 3 
ATOM   9884  N N     . THR C 1 327 ? 26.466  1.978   66.472  1.000 36.801  0 327 THR CCC N     1 ? 3 
ATOM   9885  C CA    . THR C 1 327 ? 26.065  1.164   65.295  1.000 38.655  0 327 THR CCC CA    1 ? 3 
ATOM   9886  C C     . THR C 1 327 ? 24.623  1.514   64.887  1.000 39.208  0 327 THR CCC C     1 ? 3 
ATOM   9887  O O     . THR C 1 327 ? 23.984  2.394   65.534  1.000 38.100  0 327 THR CCC O     1 ? 3 
ATOM   9888  C CB    . THR C 1 327 ? 26.159  -0.343  65.567  1.000 39.026  0 327 THR CCC CB    1 ? 3 
ATOM   9889  O OG1   . THR C 1 327 ? 25.103  -0.698  66.457  1.000 39.776  0 327 THR CCC OG1   1 ? 3 
ATOM   9890  C CG2   . THR C 1 327 ? 27.509  -0.755  66.124  1.000 37.648  0 327 THR CCC CG2   1 ? 3 
ATOM   9891  N N     . SER C 1 328 ? 24.115  0.830   63.867  1.000 38.005  0 328 SER CCC N     1 ? 3 
ATOM   9892  C CA    . SER C 1 328 ? 22.701  0.906   63.417  1.000 39.375  0 328 SER CCC CA    1 ? 3 
ATOM   9893  C C     . SER C 1 328 ? 21.734  0.420   64.516  1.000 38.642  0 328 SER CCC C     1 ? 3 
ATOM   9894  O O     . SER C 1 328 ? 20.558  0.729   64.424  1.000 40.146  0 328 SER CCC O     1 ? 3 
ATOM   9895  C CB    . SER C 1 328 ? 22.544  0.116   62.141  1.000 39.482  0 328 SER CCC CB    1 ? 3 
ATOM   9896  O OG    . SER C 1 328 ? 23.076  -1.192  62.283  1.000 39.915  0 328 SER CCC OG    1 ? 3 
ATOM   9897  N N     . VAL C 1 329 ? 22.226  -0.340  65.500  1.000 37.905  0 329 VAL CCC N     1 ? 3 
ATOM   9898  C CA    . VAL C 1 329 ? 21.460  -0.838  66.677  1.000 37.412  0 329 VAL CCC CA    1 ? 3 
ATOM   9899  C C     . VAL C 1 329 ? 21.837  0.002   67.898  1.000 37.558  0 329 VAL CCC C     1 ? 3 
ATOM   9900  O O     . VAL C 1 329 ? 22.968  -0.010  68.356  1.000 37.334  0 329 VAL CCC O     1 ? 3 
ATOM   9901  C CB    . VAL C 1 329 ? 21.685  -2.347  66.885  1.000 37.201  0 329 VAL CCC CB    1 ? 3 
ATOM   9902  C CG1   . VAL C 1 329 ? 21.068  -2.848  68.185  1.000 37.793  0 329 VAL CCC CG1   1 ? 3 
ATOM   9903  C CG2   . VAL C 1 329 ? 21.156  -3.143  65.697  1.000 35.602  0 329 VAL CCC CG2   1 ? 3 
ATOM   9904  N N     . PRO C 1 330 ? 20.893  0.772   68.482  1.000 39.212  0 330 PRO CCC N     1 ? 3 
ATOM   9905  C CA    . PRO C 1 330 ? 21.250  1.838   69.423  1.000 38.996  0 330 PRO CCC CA    1 ? 3 
ATOM   9906  C C     . PRO C 1 330 ? 21.722  1.416   70.827  1.000 39.404  0 330 PRO CCC C     1 ? 3 
ATOM   9907  O O     . PRO C 1 330 ? 22.202  2.273   71.561  1.000 38.867  0 330 PRO CCC O     1 ? 3 
ATOM   9908  C CB    . PRO C 1 330 ? 19.971  2.683   69.514  1.000 41.527  0 330 PRO CCC CB    1 ? 3 
ATOM   9909  C CG    . PRO C 1 330 ? 18.822  1.763   69.105  1.000 42.114  0 330 PRO CCC CG    1 ? 3 
ATOM   9910  C CD    . PRO C 1 330 ? 19.440  0.666   68.248  1.000 40.716  0 330 PRO CCC CD    1 ? 3 
ATOM   9911  N N     . SER C 1 331 ? 21.628  0.126   71.167  1.000 39.915  0 331 SER CCC N     1 ? 3 
ATOM   9912  C CA    . SER C 1 331 ? 22.177  -0.450  72.425  1.000 39.375  0 331 SER CCC CA    1 ? 3 
ATOM   9913  C C     . SER C 1 331 ? 23.596  -0.985  72.163  1.000 40.643  0 331 SER CCC C     1 ? 3 
ATOM   9914  O O     . SER C 1 331 ? 24.250  -1.446  73.143  1.000 39.743  0 331 SER CCC O     1 ? 3 
ATOM   9915  C CB    . SER C 1 331 ? 21.300  -1.531  72.972  1.000 38.327  0 331 SER CCC CB    1 ? 3 
ATOM   9916  O OG    . SER C 1 331 ? 21.197  -2.581  72.019  1.000 39.879  0 331 SER CCC OG    1 ? 3 
ATOM   9917  N N     . ILE C 1 332 ? 24.032  -0.988  70.897  1.000 38.519  0 332 ILE CCC N     1 ? 3 
ATOM   9918  C CA    . ILE C 1 332 ? 25.295  -1.669  70.497  1.000 36.725  0 332 ILE CCC CA    1 ? 3 
ATOM   9919  C C     . ILE C 1 332 ? 26.265  -0.644  69.910  1.000 35.773  0 332 ILE CCC C     1 ? 3 
ATOM   9920  O O     . ILE C 1 332 ? 25.945  -0.005  68.904  1.000 31.724  0 332 ILE CCC O     1 ? 3 
ATOM   9921  C CB    . ILE C 1 332 ? 25.037  -2.839  69.536  1.000 35.932  0 332 ILE CCC CB    1 ? 3 
ATOM   9922  C CG1   . ILE C 1 332 ? 24.264  -3.940  70.253  1.000 35.476  0 332 ILE CCC CG1   1 ? 3 
ATOM   9923  C CG2   . ILE C 1 332 ? 26.365  -3.359  68.983  1.000 36.191  0 332 ILE CCC CG2   1 ? 3 
ATOM   9924  C CD1   . ILE C 1 332 ? 24.011  -5.163  69.427  1.000 34.893  0 332 ILE CCC CD1   1 ? 3 
ATOM   9925  N N     . PHE C 1 333 ? 27.438  -0.561  70.526  1.000 35.211  0 333 PHE CCC N     1 ? 3 
ATOM   9926  C CA    . PHE C 1 333 ? 28.511  0.397   70.185  1.000 34.819  0 333 PHE CCC CA    1 ? 3 
ATOM   9927  C C     . PHE C 1 333 ? 29.689  -0.415  69.662  1.000 34.759  0 333 PHE CCC C     1 ? 3 
ATOM   9928  O O     . PHE C 1 333 ? 29.693  -1.673  69.810  1.000 37.212  0 333 PHE CCC O     1 ? 3 
ATOM   9929  C CB    . PHE C 1 333 ? 28.823  1.254   71.410  1.000 35.698  0 333 PHE CCC CB    1 ? 3 
ATOM   9930  C CG    . PHE C 1 333 ? 27.664  2.134   71.809  1.000 36.509  0 333 PHE CCC CG    1 ? 3 
ATOM   9931  C CD1   . PHE C 1 333 ? 26.664  1.651   72.646  1.000 36.835  0 333 PHE CCC CD1   1 ? 3 
ATOM   9932  C CD2   . PHE C 1 333 ? 27.551  3.426   71.318  1.000 35.538  0 333 PHE CCC CD2   1 ? 3 
ATOM   9933  C CE1   . PHE C 1 333 ? 25.575  2.453   72.972  1.000 38.516  0 333 PHE CCC CE1   1 ? 3 
ATOM   9934  C CE2   . PHE C 1 333 ? 26.475  4.232   71.682  1.000 37.098  0 333 PHE CCC CE2   1 ? 3 
ATOM   9935  C CZ    . PHE C 1 333 ? 25.476  3.742   72.497  1.000 37.350  0 333 PHE CCC CZ    1 ? 3 
ATOM   9936  N N     . ALA C 1 334 ? 30.637  0.265   69.024  1.000 31.972  0 334 ALA CCC N     1 ? 3 
ATOM   9937  C CA    . ALA C 1 334 ? 31.857  -0.360  68.489  1.000 30.149  0 334 ALA CCC CA    1 ? 3 
ATOM   9938  C C     . ALA C 1 334 ? 33.002  0.653   68.543  1.000 29.439  0 334 ALA CCC C     1 ? 3 
ATOM   9939  O O     . ALA C 1 334 ? 32.756  1.857   68.367  1.000 29.582  0 334 ALA CCC O     1 ? 3 
ATOM   9940  C CB    . ALA C 1 334 ? 31.567  -0.866  67.097  1.000 29.511  0 334 ALA CCC CB    1 ? 3 
ATOM   9941  N N     . VAL C 1 335 ? 34.211  0.175   68.803  1.000 29.285  0 335 VAL CCC N     1 ? 3 
ATOM   9942  C CA    . VAL C 1 335 ? 35.466  0.979   68.716  1.000 30.280  0 335 VAL CCC CA    1 ? 3 
ATOM   9943  C C     . VAL C 1 335 ? 36.576  0.077   68.198  1.000 30.684  0 335 VAL CCC C     1 ? 3 
ATOM   9944  O O     . VAL C 1 335 ? 36.329  -1.122  68.033  1.000 30.446  0 335 VAL CCC O     1 ? 3 
ATOM   9945  C CB    . VAL C 1 335 ? 35.863  1.562   70.086  1.000 32.298  0 335 VAL CCC CB    1 ? 3 
ATOM   9946  C CG1   . VAL C 1 335 ? 34.780  2.477   70.639  1.000 32.624  0 335 VAL CCC CG1   1 ? 3 
ATOM   9947  C CG2   . VAL C 1 335 ? 36.210  0.457   71.097  1.000 31.996  0 335 VAL CCC CG2   1 ? 3 
ATOM   9948  N N     . GLY C 1 336 ? 37.754  0.670   67.943  1.000 32.151  0 336 GLY CCC N     1 ? 3 
ATOM   9949  C CA    . GLY C 1 336 ? 38.964  -0.008  67.444  1.000 30.523  0 336 GLY CCC CA    1 ? 3 
ATOM   9950  C C     . GLY C 1 336 ? 38.898  -0.361  65.966  1.000 31.659  0 336 GLY CCC C     1 ? 3 
ATOM   9951  O O     . GLY C 1 336 ? 38.058  0.229   65.214  1.000 29.600  0 336 GLY CCC O     1 ? 3 
ATOM   9952  N N     . ASP C 1 337 ? 39.753  -1.317  65.567  1.000 32.238  0 337 ASP CCC N     1 ? 3 
ATOM   9953  C CA    . ASP C 1 337 ? 40.085  -1.646  64.161  1.000 31.964  0 337 ASP CCC CA    1 ? 3 
ATOM   9954  C C     . ASP C 1 337 ? 38.855  -2.092  63.355  1.000 33.110  0 337 ASP CCC C     1 ? 3 
ATOM   9955  O O     . ASP C 1 337 ? 38.931  -2.008  62.104  1.000 32.500  0 337 ASP CCC O     1 ? 3 
ATOM   9956  C CB    . ASP C 1 337 ? 41.138  -2.746  64.084  1.000 33.227  0 337 ASP CCC CB    1 ? 3 
ATOM   9957  C CG    . ASP C 1 337 ? 42.551  -2.360  64.501  1.000 34.730  0 337 ASP CCC CG    1 ? 3 
ATOM   9958  O OD1   . ASP C 1 337 ? 42.778  -1.180  64.852  1.000 34.208  0 337 ASP CCC OD1   1 ? 3 
ATOM   9959  O OD2   . ASP C 1 337 ? 43.406  -3.275  64.535  1.000 36.507  0 337 ASP CCC OD2   1 ? 3 
ATOM   9960  N N     . ILE C 1 338 ? 37.782  -2.572  63.994  1.000 33.330  0 338 ILE CCC N     1 ? 3 
ATOM   9961  C CA    . ILE C 1 338 ? 36.569  -3.105  63.291  1.000 32.296  0 338 ILE CCC CA    1 ? 3 
ATOM   9962  C C     . ILE C 1 338 ? 35.692  -1.966  62.763  1.000 32.807  0 338 ILE CCC C     1 ? 3 
ATOM   9963  O O     . ILE C 1 338 ? 34.766  -2.266  61.988  1.000 32.823  0 338 ILE CCC O     1 ? 3 
ATOM   9964  C CB    . ILE C 1 338 ? 35.743  -4.056  64.187  1.000 32.266  0 338 ILE CCC CB    1 ? 3 
ATOM   9965  C CG1   . ILE C 1 338 ? 35.027  -3.317  65.332  1.000 31.783  0 338 ILE CCC CG1   1 ? 3 
ATOM   9966  C CG2   . ILE C 1 338 ? 36.621  -5.200  64.666  1.000 32.107  0 338 ILE CCC CG2   1 ? 3 
ATOM   9967  C CD1   . ILE C 1 338 ? 34.288  -4.201  66.339  1.000 32.057  0 338 ILE CCC CD1   1 ? 3 
ATOM   9968  N N     . VAL C 1 339 ? 35.918  -0.711  63.158  1.000 34.079  0 339 VAL CCC N     1 ? 3 
ATOM   9969  C CA    . VAL C 1 339 ? 34.998  0.396   62.760  1.000 35.747  0 339 VAL CCC CA    1 ? 3 
ATOM   9970  C C     . VAL C 1 339 ? 35.512  1.042   61.475  1.000 36.756  0 339 VAL CCC C     1 ? 3 
ATOM   9971  O O     . VAL C 1 339 ? 36.699  1.416   61.409  1.000 37.199  0 339 VAL CCC O     1 ? 3 
ATOM   9972  C CB    . VAL C 1 339 ? 34.809  1.421   63.897  1.000 35.582  0 339 VAL CCC CB    1 ? 3 
ATOM   9973  C CG1   . VAL C 1 339 ? 33.905  2.564   63.464  1.000 34.531  0 339 VAL CCC CG1   1 ? 3 
ATOM   9974  C CG2   . VAL C 1 339 ? 34.259  0.751   65.156  1.000 36.265  0 339 VAL CCC CG2   1 ? 3 
ATOM   9975  N N     . GLU C 1 340 ? 34.625  1.193   60.506  1.000 39.304  0 340 GLU CCC N     1 ? 3 
ATOM   9976  C CA    . GLU C 1 340 ? 34.922  1.822   59.201  1.000 42.081  0 340 GLU CCC CA    1 ? 3 
ATOM   9977  C C     . GLU C 1 340 ? 35.224  3.306   59.386  1.000 40.721  0 340 GLU CCC C     1 ? 3 
ATOM   9978  O O     . GLU C 1 340 ? 34.510  3.986   60.187  1.000 38.398  0 340 GLU CCC O     1 ? 3 
ATOM   9979  C CB    . GLU C 1 340 ? 33.722  1.686   58.264  1.000 46.984  0 340 GLU CCC CB    1 ? 3 
ATOM   9980  C CG    . GLU C 1 340 ? 33.786  2.616   57.066  1.000 54.072  0 340 GLU CCC CG    1 ? 3 
ATOM   9981  C CD    . GLU C 1 340 ? 33.290  1.943   55.792  1.000 63.994  0 340 GLU CCC CD    1 ? 3 
ATOM   9982  O OE1   . GLU C 1 340 ? 32.151  2.316   55.315  1.000 64.166  0 340 GLU CCC OE1   1 ? 3 
ATOM   9983  O OE2   . GLU C 1 340 ? 34.075  1.064   55.260  1.000 75.173  0 340 GLU CCC OE2   1 ? 3 
ATOM   9984  N N     . GLY C 1 341 ? 36.221  3.786   58.641  1.000 37.053  0 341 GLY CCC N     1 ? 3 
ATOM   9985  C CA    . GLY C 1 341 ? 36.487  5.228   58.467  1.000 36.062  0 341 GLY CCC CA    1 ? 3 
ATOM   9986  C C     . GLY C 1 341 ? 37.398  5.793   59.539  1.000 34.717  0 341 GLY CCC C     1 ? 3 
ATOM   9987  O O     . GLY C 1 341 ? 37.510  7.019   59.588  1.000 33.516  0 341 GLY CCC O     1 ? 3 
ATOM   9988  N N     . ARG C 1 342 ? 38.051  4.956   60.350  1.000 32.801  0 342 ARG CCC N     1 ? 3 
ATOM   9989  C CA    . ARG C 1 342 ? 38.969  5.471   61.391  1.000 32.631  0 342 ARG CCC CA    1 ? 3 
ATOM   9990  C C     . ARG C 1 342 ? 40.284  4.686   61.371  1.000 31.531  0 342 ARG CCC C     1 ? 3 
ATOM   9991  O O     . ARG C 1 342 ? 40.325  3.480   61.089  1.000 31.268  0 342 ARG CCC O     1 ? 3 
ATOM   9992  C CB    . ARG C 1 342 ? 38.312  5.490   62.774  1.000 30.773  0 342 ARG CCC CB    1 ? 3 
ATOM   9993  C CG    . ARG C 1 342 ? 38.110  4.107   63.367  1.000 31.089  0 342 ARG CCC CG    1 ? 3 
ATOM   9994  C CD    . ARG C 1 342 ? 37.524  4.136   64.757  1.000 31.203  0 342 ARG CCC CD    1 ? 3 
ATOM   9995  N NE    . ARG C 1 342 ? 36.171  4.670   64.758  1.000 30.938  0 342 ARG CCC NE    1 ? 3 
ATOM   9996  C CZ    . ARG C 1 342 ? 35.430  4.835   65.858  1.000 32.608  0 342 ARG CCC CZ    1 ? 3 
ATOM   9997  N NH1   . ARG C 1 342 ? 35.919  4.538   67.063  1.000 32.113  0 342 ARG CCC NH1   1 ? 3 
ATOM   9998  N NH2   . ARG C 1 342 ? 34.199  5.314   65.737  1.000 32.421  0 342 ARG CCC NH2   1 ? 3 
ATOM   9999  N N     . PRO C 1 343 ? 41.392  5.370   61.706  1.000 29.500  0 343 PRO CCC N     1 ? 3 
ATOM   10000 C CA    . PRO C 1 343 ? 42.713  4.748   61.667  1.000 28.362  0 343 PRO CCC CA    1 ? 3 
ATOM   10001 C C     . PRO C 1 343 ? 42.803  3.571   62.650  1.000 28.933  0 343 PRO CCC C     1 ? 3 
ATOM   10002 O O     . PRO C 1 343 ? 42.241  3.644   63.726  1.000 28.633  0 343 PRO CCC O     1 ? 3 
ATOM   10003 C CB    . PRO C 1 343 ? 43.662  5.882   62.096  1.000 28.860  0 343 PRO CCC CB    1 ? 3 
ATOM   10004 C CG    . PRO C 1 343 ? 42.880  7.170   61.920  1.000 29.566  0 343 PRO CCC CG    1 ? 3 
ATOM   10005 C CD    . PRO C 1 343 ? 41.419  6.776   62.150  1.000 29.915  0 343 PRO CCC CD    1 ? 3 
ATOM   10006 N N     . GLU C 1 344 ? 43.483  2.503   62.241  1.000 30.523  0 344 GLU CCC N     1 ? 3 
ATOM   10007 C CA    . GLU C 1 344 ? 43.690  1.279   63.032  1.000 30.660  0 344 GLU CCC CA    1 ? 3 
ATOM   10008 C C     . GLU C 1 344 ? 44.912  1.494   63.942  1.000 30.025  0 344 GLU CCC C     1 ? 3 
ATOM   10009 O O     . GLU C 1 344 ? 45.950  0.801   63.730  1.000 28.713  0 344 GLU CCC O     1 ? 3 
ATOM   10010 C CB    . GLU C 1 344 ? 43.940  0.072   62.120  1.000 34.103  0 344 GLU CCC CB    1 ? 3 
ATOM   10011 C CG    . GLU C 1 344 ? 42.808  -0.272  61.180  1.000 36.653  0 344 GLU CCC CG    1 ? 3 
ATOM   10012 C CD    . GLU C 1 344 ? 42.895  -1.588  60.408  1.000 39.321  0 344 GLU CCC CD    1 ? 3 
ATOM   10013 O OE1   . GLU C 1 344 ? 43.925  -2.323  60.523  1.000 40.469  0 344 GLU CCC OE1   1 ? 3 
ATOM   10014 O OE2   . GLU C 1 344 ? 41.932  -1.882  59.662  1.000 41.868  0 344 GLU CCC OE2   1 ? 3 
ATOM   10015 N N     . LEU C 1 345 ? 44.799  2.378   64.935  1.000 28.904  0 345 LEU CCC N     1 ? 3 
ATOM   10016 C CA    . LEU C 1 345 ? 45.902  2.725   65.870  1.000 30.597  0 345 LEU CCC CA    1 ? 3 
ATOM   10017 C C     . LEU C 1 345 ? 45.469  2.468   67.315  1.000 30.369  0 345 LEU CCC C     1 ? 3 
ATOM   10018 O O     . LEU C 1 345 ? 44.264  2.599   67.591  1.000 30.354  0 345 LEU CCC O     1 ? 3 
ATOM   10019 C CB    . LEU C 1 345 ? 46.304  4.191   65.647  1.000 31.401  0 345 LEU CCC CB    1 ? 3 
ATOM   10020 C CG    . LEU C 1 345 ? 46.871  4.515   64.253  1.000 31.151  0 345 LEU CCC CG    1 ? 3 
ATOM   10021 C CD1   . LEU C 1 345 ? 47.056  6.002   64.024  1.000 30.645  0 345 LEU CCC CD1   1 ? 3 
ATOM   10022 C CD2   . LEU C 1 345 ? 48.208  3.813   64.055  1.000 31.438  0 345 LEU CCC CD2   1 ? 3 
ATOM   10023 N N     . THR C 1 346 ? 46.408  2.125   68.206  1.000 30.905  0 346 THR CCC N     1 ? 3 
ATOM   10024 C CA    . THR C 1 346 ? 46.056  1.749   69.604  1.000 30.679  0 346 THR CCC CA    1 ? 3 
ATOM   10025 C C     . THR C 1 346 ? 45.486  2.952   70.353  1.000 29.857  0 346 THR CCC C     1 ? 3 
ATOM   10026 O O     . THR C 1 346 ? 44.410  2.837   70.935  1.000 29.234  0 346 THR CCC O     1 ? 3 
ATOM   10027 C CB    . THR C 1 346 ? 47.226  1.094   70.332  1.000 31.006  0 346 THR CCC CB    1 ? 3 
ATOM   10028 O OG1   . THR C 1 346 ? 47.074  -0.295  70.085  1.000 32.594  0 346 THR CCC OG1   1 ? 3 
ATOM   10029 C CG2   . THR C 1 346 ? 47.219  1.257   71.840  1.000 31.592  0 346 THR CCC CG2   1 ? 3 
ATOM   10030 N N     . PRO C 1 347 ? 46.177  4.119   70.386  1.000 28.382  0 347 PRO CCC N     1 ? 3 
ATOM   10031 C CA    . PRO C 1 347 ? 45.663  5.292   71.093  1.000 28.094  0 347 PRO CCC CA    1 ? 3 
ATOM   10032 C C     . PRO C 1 347 ? 44.246  5.722   70.653  1.000 27.667  0 347 PRO CCC C     1 ? 3 
ATOM   10033 O O     . PRO C 1 347 ? 43.532  6.198   71.437  1.000 26.798  0 347 PRO CCC O     1 ? 3 
ATOM   10034 C CB    . PRO C 1 347 ? 46.731  6.375   70.837  1.000 27.266  0 347 PRO CCC CB    1 ? 3 
ATOM   10035 C CG    . PRO C 1 347 ? 47.975  5.628   70.471  1.000 26.747  0 347 PRO CCC CG    1 ? 3 
ATOM   10036 C CD    . PRO C 1 347 ? 47.480  4.384   69.768  1.000 27.413  0 347 PRO CCC CD    1 ? 3 
ATOM   10037 N N     . VAL C 1 348 ? 43.875  5.494   69.400  1.000 29.657  0 348 VAL CCC N     1 ? 3 
ATOM   10038 C CA    . VAL C 1 348 ? 42.534  5.812   68.843  1.000 30.034  0 348 VAL CCC CA    1 ? 3 
ATOM   10039 C C     . VAL C 1 348 ? 41.522  4.845   69.440  1.000 29.055  0 348 VAL CCC C     1 ? 3 
ATOM   10040 O O     . VAL C 1 348 ? 40.446  5.289   69.818  1.000 30.595  0 348 VAL CCC O     1 ? 3 
ATOM   10041 C CB    . VAL C 1 348 ? 42.563  5.755   67.305  1.000 31.005  0 348 VAL CCC CB    1 ? 3 
ATOM   10042 C CG1   . VAL C 1 348 ? 41.210  6.064   66.690  1.000 30.255  0 348 VAL CCC CG1   1 ? 3 
ATOM   10043 C CG2   . VAL C 1 348 ? 43.601  6.723   66.784  1.000 32.430  0 348 VAL CCC CG2   1 ? 3 
ATOM   10044 N N     . ALA C 1 349 ? 41.843  3.560   69.482  1.000 28.840  0 349 ALA CCC N     1 ? 3 
ATOM   10045 C CA    . ALA C 1 349 ? 41.018  2.507   70.116  1.000 28.647  0 349 ALA CCC CA    1 ? 3 
ATOM   10046 C C     . ALA C 1 349 ? 40.756  2.877   71.583  1.000 30.212  0 349 ALA CCC C     1 ? 3 
ATOM   10047 O O     . ALA C 1 349 ? 39.588  2.957   71.984  1.000 33.702  0 349 ALA CCC O     1 ? 3 
ATOM   10048 C CB    . ALA C 1 349 ? 41.721  1.176   69.996  1.000 28.036  0 349 ALA CCC CB    1 ? 3 
ATOM   10049 N N     . VAL C 1 350 ? 41.824  3.102   72.355  1.000 31.203  0 350 VAL CCC N     1 ? 3 
ATOM   10050 C CA    . VAL C 1 350 ? 41.798  3.436   73.810  1.000 31.029  0 350 VAL CCC CA    1 ? 3 
ATOM   10051 C C     . VAL C 1 350 ? 40.938  4.689   74.016  1.000 31.177  0 350 VAL CCC C     1 ? 3 
ATOM   10052 O O     . VAL C 1 350 ? 40.027  4.606   74.836  1.000 30.936  0 350 VAL CCC O     1 ? 3 
ATOM   10053 C CB    . VAL C 1 350 ? 43.231  3.658   74.361  1.000 30.743  0 350 VAL CCC CB    1 ? 3 
ATOM   10054 C CG1   . VAL C 1 350 ? 43.223  4.262   75.769  1.000 30.139  0 350 VAL CCC CG1   1 ? 3 
ATOM   10055 C CG2   . VAL C 1 350 ? 44.059  2.370   74.352  1.000 31.455  0 350 VAL CCC CG2   1 ? 3 
ATOM   10056 N N     . LYS C 1 351 ? 41.250  5.821   73.372  1.000 30.553  0 351 LYS CCC N     1 ? 3 
ATOM   10057 C CA    . LYS C 1 351 ? 40.564  7.100   73.672  1.000 32.635  0 351 LYS CCC CA    1 ? 3 
ATOM   10058 C C     . LYS C 1 351 ? 39.084  6.958   73.288  1.000 32.804  0 351 LYS CCC C     1 ? 3 
ATOM   10059 O O     . LYS C 1 351 ? 38.237  7.486   73.998  1.000 33.179  0 351 LYS CCC O     1 ? 3 
ATOM   10060 C CB    . LYS C 1 351 ? 41.176  8.326   72.981  1.000 33.107  0 351 LYS CCC CB    1 ? 3 
ATOM   10061 C CG    . LYS C 1 351 ? 40.535  9.632   73.447  1.000 34.667  0 351 LYS CCC CG    1 ? 3 
ATOM   10062 C CD    . LYS C 1 351 ? 41.195  10.934  73.014  1.000 37.716  0 351 LYS CCC CD    1 ? 3 
ATOM   10063 C CE    . LYS C 1 351 ? 42.582  11.240  73.598  1.000 37.519  0 351 LYS CCC CE    1 ? 3 
ATOM   10064 N NZ    . LYS C 1 351 ? 42.541  11.461  75.065  1.000 37.755  0 351 LYS CCC NZ    1 ? 3 
ATOM   10065 N N     . ALA C 1 352 ? 38.769  6.279   72.194  1.000 33.787  0 352 ALA CCC N     1 ? 3 
ATOM   10066 C CA    . ALA C 1 352 ? 37.363  6.065   71.797  1.000 35.669  0 352 ALA CCC CA    1 ? 3 
ATOM   10067 C C     . ALA C 1 352 ? 36.661  5.258   72.898  1.000 35.460  0 352 ALA CCC C     1 ? 3 
ATOM   10068 O O     . ALA C 1 352 ? 35.521  5.585   73.220  1.000 37.052  0 352 ALA CCC O     1 ? 3 
ATOM   10069 C CB    . ALA C 1 352 ? 37.261  5.389   70.434  1.000 36.469  0 352 ALA CCC CB    1 ? 3 
ATOM   10070 N N     . GLY C 1 353 ? 37.334  4.251   73.447  1.000 35.572  0 353 GLY CCC N     1 ? 3 
ATOM   10071 C CA    . GLY C 1 353 ? 36.792  3.380   74.510  1.000 38.378  0 353 GLY CCC CA    1 ? 3 
ATOM   10072 C C     . GLY C 1 353 ? 36.509  4.183   75.771  1.000 40.314  0 353 GLY CCC C     1 ? 3 
ATOM   10073 O O     . GLY C 1 353 ? 35.417  4.039   76.342  1.000 42.330  0 353 GLY CCC O     1 ? 3 
ATOM   10074 N N     . ILE C 1 354 ? 37.451  5.033   76.167  1.000 39.688  0 354 ILE CCC N     1 ? 3 
ATOM   10075 C CA    . ILE C 1 354 ? 37.321  5.901   77.367  1.000 42.178  0 354 ILE CCC CA    1 ? 3 
ATOM   10076 C C     . ILE C 1 354 ? 36.210  6.936   77.151  1.000 44.040  0 354 ILE CCC C     1 ? 3 
ATOM   10077 O O     . ILE C 1 354 ? 35.373  7.074   78.066  1.000 44.911  0 354 ILE CCC O     1 ? 3 
ATOM   10078 C CB    . ILE C 1 354 ? 38.672  6.533   77.740  1.000 43.410  0 354 ILE CCC CB    1 ? 3 
ATOM   10079 C CG1   . ILE C 1 354 ? 39.698  5.459   78.150  1.000 42.555  0 354 ILE CCC CG1   1 ? 3 
ATOM   10080 C CG2   . ILE C 1 354 ? 38.467  7.563   78.835  1.000 44.035  0 354 ILE CCC CG2   1 ? 3 
ATOM   10081 C CD1   . ILE C 1 354 ? 41.093  5.997   78.409  1.000 42.522  0 354 ILE CCC CD1   1 ? 3 
ATOM   10082 N N     . LEU C 1 355 ? 36.187  7.631   76.012  1.000 42.695  0 355 LEU CCC N     1 ? 3 
ATOM   10083 C CA    . LEU C 1 355 ? 35.204  8.711   75.753  1.000 41.495  0 355 LEU CCC CA    1 ? 3 
ATOM   10084 C C     . LEU C 1 355 ? 33.798  8.079   75.684  1.000 42.488  0 355 LEU CCC C     1 ? 3 
ATOM   10085 O O     . LEU C 1 355 ? 32.844  8.685   76.230  1.000 39.525  0 355 LEU CCC O     1 ? 3 
ATOM   10086 C CB    . LEU C 1 355 ? 35.566  9.477   74.468  1.000 41.205  0 355 LEU CCC CB    1 ? 3 
ATOM   10087 C CG    . LEU C 1 355 ? 36.853  10.313  74.470  1.000 40.917  0 355 LEU CCC CG    1 ? 3 
ATOM   10088 C CD1   . LEU C 1 355 ? 36.875  11.236  73.281  1.000 40.684  0 355 LEU CCC CD1   1 ? 3 
ATOM   10089 C CD2   . LEU C 1 355 ? 37.088  11.122  75.746  1.000 40.015  0 355 LEU CCC CD2   1 ? 3 
ATOM   10090 N N     . LEU C 1 356 ? 33.672  6.898   75.064  1.000 40.774  0 356 LEU CCC N     1 ? 3 
ATOM   10091 C CA    . LEU C 1 356 ? 32.386  6.168   74.986  1.000 40.079  0 356 LEU CCC CA    1 ? 3 
ATOM   10092 C C     . LEU C 1 356 ? 31.903  5.906   76.423  1.000 40.566  0 356 LEU CCC C     1 ? 3 
ATOM   10093 O O     . LEU C 1 356 ? 30.779  6.346   76.779  1.000 43.417  0 356 LEU CCC O     1 ? 3 
ATOM   10094 C CB    . LEU C 1 356 ? 32.536  4.862   74.192  1.000 38.880  0 356 LEU CCC CB    1 ? 3 
ATOM   10095 C CG    . LEU C 1 356 ? 31.313  3.927   74.244  1.000 40.387  0 356 LEU CCC CG    1 ? 3 
ATOM   10096 C CD1   . LEU C 1 356 ? 30.088  4.559   73.605  1.000 39.873  0 356 LEU CCC CD1   1 ? 3 
ATOM   10097 C CD2   . LEU C 1 356 ? 31.588  2.586   73.602  1.000 40.948  0 356 LEU CCC CD2   1 ? 3 
ATOM   10098 N N     . ALA C 1 357 ? 32.701  5.202   77.217  1.000 39.248  0 357 ALA CCC N     1 ? 3 
ATOM   10099 C CA    . ALA C 1 357 ? 32.428  4.940   78.644  1.000 41.645  0 357 ALA CCC CA    1 ? 3 
ATOM   10100 C C     . ALA C 1 357 ? 31.901  6.211   79.344  1.000 42.665  0 357 ALA CCC C     1 ? 3 
ATOM   10101 O O     . ALA C 1 357 ? 30.852  6.120   80.016  1.000 38.574  0 357 ALA CCC O     1 ? 3 
ATOM   10102 C CB    . ALA C 1 357 ? 33.675  4.406   79.295  1.000 40.628  0 357 ALA CCC CB    1 ? 3 
ATOM   10103 N N     . ARG C 1 358 ? 32.571  7.357   79.163  1.000 44.028  0 358 ARG CCC N     1 ? 3 
ATOM   10104 C CA    . ARG C 1 358 ? 32.180  8.634   79.816  1.000 45.597  0 358 ARG CCC CA    1 ? 3 
ATOM   10105 C C     . ARG C 1 358 ? 30.830  9.144   79.283  1.000 46.072  0 358 ARG CCC C     1 ? 3 
ATOM   10106 O O     . ARG C 1 358 ? 30.031  9.619   80.106  1.000 46.542  0 358 ARG CCC O     1 ? 3 
ATOM   10107 C CB    . ARG C 1 358 ? 33.243  9.708   79.596  1.000 47.118  0 358 ARG CCC CB    1 ? 3 
ATOM   10108 C CG    . ARG C 1 358 ? 34.475  9.509   80.453  1.000 49.091  0 358 ARG CCC CG    1 ? 3 
ATOM   10109 C CD    . ARG C 1 358 ? 35.581  10.497  80.164  1.000 51.349  0 358 ARG CCC CD    1 ? 3 
ATOM   10110 N NE    . ARG C 1 358 ? 36.804  10.031  80.813  1.000 53.176  0 358 ARG CCC NE    1 ? 3 
ATOM   10111 C CZ    . ARG C 1 358 ? 38.013  10.531  80.574  1.000 52.468  0 358 ARG CCC CZ    1 ? 3 
ATOM   10112 N NH1   . ARG C 1 358 ? 38.154  11.515  79.699  1.000 53.691  0 358 ARG CCC NH1   1 ? 3 
ATOM   10113 N NH2   . ARG C 1 358 ? 39.070  10.044  81.199  1.000 48.611  0 358 ARG CCC NH2   1 ? 3 
ATOM   10114 N N     . ARG C 1 359 ? 30.598  9.103   77.964  1.000 43.848  0 359 ARG CCC N     1 ? 3 
ATOM   10115 C CA    . ARG C 1 359 ? 29.346  9.587   77.344  1.000 41.818  0 359 ARG CCC CA    1 ? 3 
ATOM   10116 C C     . ARG C 1 359 ? 28.175  8.753   77.875  1.000 44.762  0 359 ARG CCC C     1 ? 3 
ATOM   10117 O O     . ARG C 1 359 ? 27.074  9.327   78.077  1.000 46.204  0 359 ARG CCC O     1 ? 3 
ATOM   10118 C CB    . ARG C 1 359 ? 29.410  9.520   75.816  1.000 40.199  0 359 ARG CCC CB    1 ? 3 
ATOM   10119 C CG    . ARG C 1 359 ? 30.310  10.556  75.166  1.000 39.025  0 359 ARG CCC CG    1 ? 3 
ATOM   10120 C CD    . ARG C 1 359 ? 29.991  10.798  73.706  1.000 36.584  0 359 ARG CCC CD    1 ? 3 
ATOM   10121 N NE    . ARG C 1 359 ? 29.963  9.571   72.920  1.000 34.885  0 359 ARG CCC NE    1 ? 3 
ATOM   10122 C CZ    . ARG C 1 359 ? 31.042  8.901   72.499  1.000 35.120  0 359 ARG CCC CZ    1 ? 3 
ATOM   10123 N NH1   . ARG C 1 359 ? 32.262  9.345   72.767  1.000 35.140  0 359 ARG CCC NH1   1 ? 3 
ATOM   10124 N NH2   . ARG C 1 359 ? 30.914  7.780   71.808  1.000 33.305  0 359 ARG CCC NH2   1 ? 3 
ATOM   10125 N N     . LEU C 1 360 ? 28.380  7.446   78.058  1.000 47.212  0 360 LEU CCC N     1 ? 3 
ATOM   10126 C CA    . LEU C 1 360 ? 27.311  6.505   78.502  1.000 49.943  0 360 LEU CCC CA    1 ? 3 
ATOM   10127 C C     . LEU C 1 360 ? 26.982  6.764   79.982  1.000 51.849  0 360 LEU CCC C     1 ? 3 
ATOM   10128 O O     . LEU C 1 360 ? 25.776  6.702   80.327  1.000 51.011  0 360 LEU CCC O     1 ? 3 
ATOM   10129 C CB    . LEU C 1 360 ? 27.748  5.049   78.279  1.000 51.033  0 360 LEU CCC CB    1 ? 3 
ATOM   10130 C CG    . LEU C 1 360 ? 27.838  4.586   76.818  1.000 51.882  0 360 LEU CCC CG    1 ? 3 
ATOM   10131 C CD1   . LEU C 1 360 ? 28.283  3.137   76.735  1.000 50.767  0 360 LEU CCC CD1   1 ? 3 
ATOM   10132 C CD2   . LEU C 1 360 ? 26.516  4.759   76.066  1.000 51.590  0 360 LEU CCC CD2   1 ? 3 
ATOM   10133 N N     . PHE C 1 361 ? 27.984  7.066   80.822  1.000 50.182  0 361 PHE CCC N     1 ? 3 
ATOM   10134 C CA    . PHE C 1 361 ? 27.882  6.899   82.304  1.000 52.321  0 361 PHE CCC CA    1 ? 3 
ATOM   10135 C C     . PHE C 1 361 ? 28.312  8.129   83.124  1.000 54.209  0 361 PHE CCC C     1 ? 3 
ATOM   10136 O O     . PHE C 1 361 ? 28.083  8.078   84.345  1.000 60.255  0 361 PHE CCC O     1 ? 3 
ATOM   10137 C CB    . PHE C 1 361 ? 28.678  5.672   82.752  1.000 50.080  0 361 PHE CCC CB    1 ? 3 
ATOM   10138 C CG    . PHE C 1 361 ? 28.208  4.374   82.151  1.000 49.826  0 361 PHE CCC CG    1 ? 3 
ATOM   10139 C CD1   . PHE C 1 361 ? 26.883  3.956   82.291  1.000 50.700  0 361 PHE CCC CD1   1 ? 3 
ATOM   10140 C CD2   . PHE C 1 361 ? 29.085  3.563   81.444  1.000 49.194  0 361 PHE CCC CD2   1 ? 3 
ATOM   10141 C CE1   . PHE C 1 361 ? 26.445  2.771   81.722  1.000 49.888  0 361 PHE CCC CE1   1 ? 3 
ATOM   10142 C CE2   . PHE C 1 361 ? 28.655  2.362   80.901  1.000 49.206  0 361 PHE CCC CE2   1 ? 3 
ATOM   10143 C CZ    . PHE C 1 361 ? 27.334  1.980   81.026  1.000 50.863  0 361 PHE CCC CZ    1 ? 3 
ATOM   10144 N N     . ALA C 1 362 ? 28.876  9.179   82.517  1.000 54.666  0 362 ALA CCC N     1 ? 3 
ATOM   10145 C CA    . ALA C 1 362 ? 29.347  10.405  83.213  1.000 55.398  0 362 ALA CCC CA    1 ? 3 
ATOM   10146 C C     . ALA C 1 362 ? 28.874  11.668  82.480  1.000 53.622  0 362 ALA CCC C     1 ? 3 
ATOM   10147 O O     . ALA C 1 362 ? 29.512  12.714  82.649  1.000 52.586  0 362 ALA CCC O     1 ? 3 
ATOM   10148 C CB    . ALA C 1 362 ? 30.866  10.364  83.343  1.000 57.442  0 362 ALA CCC CB    1 ? 3 
ATOM   10149 N N     . GLY C 1 363 ? 27.811  11.574  81.681  1.000 54.315  0 363 GLY CCC N     1 ? 3 
ATOM   10150 C CA    . GLY C 1 363 ? 27.171  12.738  81.047  1.000 55.703  0 363 GLY CCC CA    1 ? 3 
ATOM   10151 C C     . GLY C 1 363 ? 28.101  13.530  80.133  1.000 56.325  0 363 GLY CCC C     1 ? 3 
ATOM   10152 O O     . GLY C 1 363 ? 27.781  14.707  79.893  1.000 56.883  0 363 GLY CCC O     1 ? 3 
ATOM   10153 N N     . SER C 1 364 ? 29.189  12.929  79.622  1.000 56.801  0 364 SER CCC N     1 ? 3 
ATOM   10154 C CA    . SER C 1 364 ? 30.149  13.557  78.663  1.000 53.955  0 364 SER CCC CA    1 ? 3 
ATOM   10155 C C     . SER C 1 364 ? 29.517  13.578  77.260  1.000 52.119  0 364 SER CCC C     1 ? 3 
ATOM   10156 O O     . SER C 1 364 ? 28.612  12.754  76.993  1.000 52.576  0 364 SER CCC O     1 ? 3 
ATOM   10157 C CB    . SER C 1 364 ? 31.503  12.851  78.690  1.000 52.843  0 364 SER CCC CB    1 ? 3 
ATOM   10158 O OG    . SER C 1 364 ? 32.313  13.190  77.563  1.000 51.945  0 364 SER CCC OG    1 ? 3 
ATOM   10159 N N     . ASN C 1 365 ? 29.916  14.519  76.410  1.000 51.382  0 365 ASN CCC N     1 ? 3 
ATOM   10160 C CA    . ASN C 1 365 ? 29.508  14.499  74.980  1.000 55.455  0 365 ASN CCC CA    1 ? 3 
ATOM   10161 C C     . ASN C 1 365 ? 30.746  14.681  74.081  1.000 54.158  0 365 ASN CCC C     1 ? 3 
ATOM   10162 O O     . ASN C 1 365 ? 30.576  15.137  72.946  1.000 56.210  0 365 ASN CCC O     1 ? 3 
ATOM   10163 C CB    . ASN C 1 365 ? 28.401  15.514  74.690  1.000 57.539  0 365 ASN CCC CB    1 ? 3 
ATOM   10164 C CG    . ASN C 1 365 ? 27.438  14.966  73.657  1.000 62.500  0 365 ASN CCC CG    1 ? 3 
ATOM   10165 O OD1   . ASN C 1 365 ? 27.581  15.224  72.463  1.000 65.652  0 365 ASN CCC OD1   1 ? 3 
ATOM   10166 N ND2   . ASN C 1 365 ? 26.488  14.149  74.097  1.000 62.570  0 365 ASN CCC ND2   1 ? 3 
ATOM   10167 N N     . GLU C 1 366 ? 31.922  14.275  74.568  1.000 54.685  0 366 GLU CCC N     1 ? 3 
ATOM   10168 C CA    . GLU C 1 366 ? 33.221  14.465  73.887  1.000 54.334  0 366 GLU CCC CA    1 ? 3 
ATOM   10169 C C     . GLU C 1 366 ? 33.489  13.281  72.957  1.000 50.201  0 366 GLU CCC C     1 ? 3 
ATOM   10170 O O     . GLU C 1 366 ? 33.359  12.126  73.414  1.000 45.927  0 366 GLU CCC O     1 ? 3 
ATOM   10171 C CB    . GLU C 1 366 ? 34.346  14.634  74.913  1.000 59.429  0 366 GLU CCC CB    1 ? 3 
ATOM   10172 C CG    . GLU C 1 366 ? 34.406  16.018  75.537  1.000 61.971  0 366 GLU CCC CG    1 ? 3 
ATOM   10173 C CD    . GLU C 1 366 ? 35.797  16.402  76.021  1.000 63.149  0 366 GLU CCC CD    1 ? 3 
ATOM   10174 O OE1   . GLU C 1 366 ? 36.060  16.218  77.218  1.000 65.135  0 366 GLU CCC OE1   1 ? 3 
ATOM   10175 O OE2   . GLU C 1 366 ? 36.631  16.864  75.195  1.000 63.556  0 366 GLU CCC OE2   1 ? 3 
ATOM   10176 N N     . PHE C 1 367 ? 33.815  13.593  71.701  1.000 49.038  0 367 PHE CCC N     1 ? 3 
ATOM   10177 C CA    . PHE C 1 367 ? 34.329  12.656  70.662  1.000 46.127  0 367 PHE CCC CA    1 ? 3 
ATOM   10178 C C     . PHE C 1 367 ? 35.781  13.019  70.314  1.000 43.409  0 367 PHE CCC C     1 ? 3 
ATOM   10179 O O     . PHE C 1 367 ? 36.200  14.137  70.593  1.000 39.848  0 367 PHE CCC O     1 ? 3 
ATOM   10180 C CB    . PHE C 1 367 ? 33.408  12.658  69.436  1.000 45.772  0 367 PHE CCC CB    1 ? 3 
ATOM   10181 C CG    . PHE C 1 367 ? 32.026  12.110  69.701  1.000 46.441  0 367 PHE CCC CG    1 ? 3 
ATOM   10182 C CD1   . PHE C 1 367 ? 31.036  12.895  70.302  1.000 45.723  0 367 PHE CCC CD1   1 ? 3 
ATOM   10183 C CD2   . PHE C 1 367 ? 31.720  10.789  69.405  1.000 46.272  0 367 PHE CCC CD2   1 ? 3 
ATOM   10184 C CE1   . PHE C 1 367 ? 29.777  12.373  70.570  1.000 43.318  0 367 PHE CCC CE1   1 ? 3 
ATOM   10185 C CE2   . PHE C 1 367 ? 30.445  10.287  69.668  1.000 46.177  0 367 PHE CCC CE2   1 ? 3 
ATOM   10186 C CZ    . PHE C 1 367 ? 29.483  11.073  70.258  1.000 42.818  0 367 PHE CCC CZ    1 ? 3 
ATOM   10187 N N     . ILE C 1 368 ? 36.527  12.068  69.739  1.000 42.498  0 368 ILE CCC N     1 ? 3 
ATOM   10188 C CA    . ILE C 1 368 ? 37.871  12.320  69.138  1.000 41.230  0 368 ILE CCC CA    1 ? 3 
ATOM   10189 C C     . ILE C 1 368 ? 37.736  13.330  67.983  1.000 38.946  0 368 ILE CCC C     1 ? 3 
ATOM   10190 O O     . ILE C 1 368 ? 36.699  13.288  67.261  1.000 33.140  0 368 ILE CCC O     1 ? 3 
ATOM   10191 C CB    . ILE C 1 368 ? 38.528  11.003  68.653  1.000 41.283  0 368 ILE CCC CB    1 ? 3 
ATOM   10192 C CG1   . ILE C 1 368 ? 38.891  10.082  69.816  1.000 42.029  0 368 ILE CCC CG1   1 ? 3 
ATOM   10193 C CG2   . ILE C 1 368 ? 39.748  11.292  67.800  1.000 40.257  0 368 ILE CCC CG2   1 ? 3 
ATOM   10194 C CD1   . ILE C 1 368 ? 39.225  8.673   69.384  1.000 42.152  0 368 ILE CCC CD1   1 ? 3 
ATOM   10195 N N     . ASP C 1 369 ? 38.768  14.176  67.839  1.000 38.864  0 369 ASP CCC N     1 ? 3 
ATOM   10196 C CA    . ASP C 1 369 ? 39.015  15.028  66.648  1.000 38.705  0 369 ASP CCC CA    1 ? 3 
ATOM   10197 C C     . ASP C 1 369 ? 39.891  14.219  65.678  1.000 39.762  0 369 ASP CCC C     1 ? 3 
ATOM   10198 O O     . ASP C 1 369 ? 41.128  14.130  65.876  1.000 38.223  0 369 ASP CCC O     1 ? 3 
ATOM   10199 C CB    . ASP C 1 369 ? 39.596  16.377  67.085  1.000 37.707  0 369 ASP CCC CB    1 ? 3 
ATOM   10200 C CG    . ASP C 1 369 ? 39.753  17.392  65.959  1.000 38.826  0 369 ASP CCC CG    1 ? 3 
ATOM   10201 O OD1   . ASP C 1 369 ? 39.582  17.007  64.761  1.000 39.988  0 369 ASP CCC OD1   1 ? 3 
ATOM   10202 O OD2   . ASP C 1 369 ? 40.057  18.578  66.279  1.000 39.168  0 369 ASP CCC OD2   1 ? 3 
ATOM   10203 N N     . TYR C 1 370 ? 39.288  13.628  64.649  1.000 41.588  0 370 TYR CCC N     1 ? 3 
ATOM   10204 C CA    . TYR C 1 370 ? 39.995  12.692  63.730  1.000 40.127  0 370 TYR CCC CA    1 ? 3 
ATOM   10205 C C     . TYR C 1 370 ? 40.866  13.460  62.735  1.000 43.921  0 370 TYR CCC C     1 ? 3 
ATOM   10206 O O     . TYR C 1 370 ? 41.615  12.791  61.964  1.000 41.731  0 370 TYR CCC O     1 ? 3 
ATOM   10207 C CB    . TYR C 1 370 ? 39.049  11.733  63.027  1.000 36.839  0 370 TYR CCC CB    1 ? 3 
ATOM   10208 C CG    . TYR C 1 370 ? 38.486  10.685  63.944  1.000 37.192  0 370 TYR CCC CG    1 ? 3 
ATOM   10209 C CD1   . TYR C 1 370 ? 39.255  9.590   64.325  1.000 36.426  0 370 TYR CCC CD1   1 ? 3 
ATOM   10210 C CD2   . TYR C 1 370 ? 37.177  10.771  64.430  1.000 36.844  0 370 TYR CCC CD2   1 ? 3 
ATOM   10211 C CE1   . TYR C 1 370 ? 38.746  8.587   65.142  1.000 35.192  0 370 TYR CCC CE1   1 ? 3 
ATOM   10212 C CE2   . TYR C 1 370 ? 36.663  9.782   65.253  1.000 37.566  0 370 TYR CCC CE2   1 ? 3 
ATOM   10213 C CZ    . TYR C 1 370 ? 37.449  8.694   65.615  1.000 38.519  0 370 TYR CCC CZ    1 ? 3 
ATOM   10214 O OH    . TYR C 1 370 ? 36.950  7.736   66.456  1.000 42.716  0 370 TYR CCC OH    1 ? 3 
ATOM   10215 N N     . ASP C 1 371 ? 40.856  14.795  62.791  1.000 48.642  0 371 ASP CCC N     1 ? 3 
ATOM   10216 C CA    . ASP C 1 371 ? 41.717  15.646  61.912  1.000 48.959  0 371 ASP CCC CA    1 ? 3 
ATOM   10217 C C     . ASP C 1 371 ? 43.169  15.633  62.423  1.000 48.211  0 371 ASP CCC C     1 ? 3 
ATOM   10218 O O     . ASP C 1 371 ? 44.060  16.002  61.646  1.000 50.515  0 371 ASP CCC O     1 ? 3 
ATOM   10219 C CB    . ASP C 1 371 ? 41.202  17.089  61.831  1.000 50.489  0 371 ASP CCC CB    1 ? 3 
ATOM   10220 C CG    . ASP C 1 371 ? 39.850  17.225  61.142  1.000 53.091  0 371 ASP CCC CG    1 ? 3 
ATOM   10221 O OD1   . ASP C 1 371 ? 39.608  16.456  60.192  1.000 50.360  0 371 ASP CCC OD1   1 ? 3 
ATOM   10222 O OD2   . ASP C 1 371 ? 39.033  18.095  61.574  1.000 57.455  0 371 ASP CCC OD2   1 ? 3 
ATOM   10223 N N     . PHE C 1 372 ? 43.397  15.274  63.691  1.000 45.076  0 372 PHE CCC N     1 ? 3 
ATOM   10224 C CA    . PHE C 1 372 ? 44.706  15.405  64.375  1.000 42.930  0 372 PHE CCC CA    1 ? 3 
ATOM   10225 C C     . PHE C 1 372 ? 45.068  14.085  65.050  1.000 39.716  0 372 PHE CCC C     1 ? 3 
ATOM   10226 O O     . PHE C 1 372 ? 45.138  14.009  66.279  1.000 43.207  0 372 PHE CCC O     1 ? 3 
ATOM   10227 C CB    . PHE C 1 372 ? 44.666  16.611  65.318  1.000 44.432  0 372 PHE CCC CB    1 ? 3 
ATOM   10228 C CG    . PHE C 1 372 ? 44.507  17.925  64.588  1.000 46.153  0 372 PHE CCC CG    1 ? 3 
ATOM   10229 C CD1   . PHE C 1 372 ? 45.544  18.456  63.826  1.000 44.422  0 372 PHE CCC CD1   1 ? 3 
ATOM   10230 C CD2   . PHE C 1 372 ? 43.294  18.600  64.619  1.000 47.624  0 372 PHE CCC CD2   1 ? 3 
ATOM   10231 C CE1   . PHE C 1 372 ? 45.371  19.645  63.138  1.000 46.052  0 372 PHE CCC CE1   1 ? 3 
ATOM   10232 C CE2   . PHE C 1 372 ? 43.118  19.791  63.925  1.000 48.411  0 372 PHE CCC CE2   1 ? 3 
ATOM   10233 C CZ    . PHE C 1 372 ? 44.162  20.315  63.187  1.000 46.493  0 372 PHE CCC CZ    1 ? 3 
ATOM   10234 N N     . VAL C 1 373 ? 45.282  13.064  64.233  1.000 37.386  0 373 VAL CCC N     1 ? 3 
ATOM   10235 C CA    . VAL C 1 373 ? 45.704  11.704  64.669  1.000 35.826  0 373 VAL CCC CA    1 ? 3 
ATOM   10236 C C     . VAL C 1 373 ? 47.115  11.482  64.151  1.000 33.671  0 373 VAL CCC C     1 ? 3 
ATOM   10237 O O     . VAL C 1 373 ? 47.294  11.198  62.983  1.000 36.436  0 373 VAL CCC O     1 ? 3 
ATOM   10238 C CB    . VAL C 1 373 ? 44.735  10.605  64.189  1.000 34.520  0 373 VAL CCC CB    1 ? 3 
ATOM   10239 C CG1   . VAL C 1 373 ? 45.261  9.218   64.581  1.000 33.589  0 373 VAL CCC CG1   1 ? 3 
ATOM   10240 C CG2   . VAL C 1 373 ? 43.333  10.834  64.779  1.000 34.475  0 373 VAL CCC CG2   1 ? 3 
ATOM   10241 N N     . PRO C 1 374 ? 48.156  11.609  64.990  1.000 32.310  0 374 PRO CCC N     1 ? 3 
ATOM   10242 C CA    . PRO C 1 374 ? 49.526  11.383  64.554  1.000 32.426  0 374 PRO CCC CA    1 ? 3 
ATOM   10243 C C     . PRO C 1 374 ? 49.808  9.876   64.481  1.000 32.832  0 374 PRO CCC C     1 ? 3 
ATOM   10244 O O     . PRO C 1 374 ? 49.109  9.090   65.061  1.000 32.260  0 374 PRO CCC O     1 ? 3 
ATOM   10245 C CB    . PRO C 1 374 ? 50.369  12.035  65.666  1.000 30.763  0 374 PRO CCC CB    1 ? 3 
ATOM   10246 C CG    . PRO C 1 374 ? 49.528  11.841  66.898  1.000 31.603  0 374 PRO CCC CG    1 ? 3 
ATOM   10247 C CD    . PRO C 1 374 ? 48.093  11.944  66.427  1.000 32.402  0 374 PRO CCC CD    1 ? 3 
ATOM   10248 N N     . THR C 1 375 ? 50.842  9.511   63.741  1.000 33.633  0 375 THR CCC N     1 ? 3 
ATOM   10249 C CA    . THR C 1 375 ? 51.251  8.103   63.553  1.000 35.332  0 375 THR CCC CA    1 ? 3 
ATOM   10250 C C     . THR C 1 375 ? 52.755  8.119   63.375  1.000 31.595  0 375 THR CCC C     1 ? 3 
ATOM   10251 O O     . THR C 1 375 ? 53.248  9.138   62.966  1.000 31.382  0 375 THR CCC O     1 ? 3 
ATOM   10252 C CB    . THR C 1 375 ? 50.475  7.432   62.408  1.000 39.958  0 375 THR CCC CB    1 ? 3 
ATOM   10253 O OG1   . THR C 1 375 ? 51.068  6.160   62.103  1.000 45.490  0 375 THR CCC OG1   1 ? 3 
ATOM   10254 C CG2   . THR C 1 375 ? 50.489  8.262   61.153  1.000 40.273  0 375 THR CCC CG2   1 ? 3 
ATOM   10255 N N     . THR C 1 376 ? 53.413  7.070   63.837  1.000 29.678  0 376 THR CCC N     1 ? 3 
ATOM   10256 C CA    . THR C 1 376 ? 54.825  6.782   63.523  1.000 29.343  0 376 THR CCC CA    1 ? 3 
ATOM   10257 C C     . THR C 1 376 ? 54.968  5.367   62.965  1.000 27.253  0 376 THR CCC C     1 ? 3 
ATOM   10258 O O     . THR C 1 376 ? 54.406  4.459   63.531  1.000 24.965  0 376 THR CCC O     1 ? 3 
ATOM   10259 C CB    . THR C 1 376 ? 55.762  6.992   64.707  1.000 28.932  0 376 THR CCC CB    1 ? 3 
ATOM   10260 O OG1   . THR C 1 376 ? 55.813  8.374   65.036  1.000 28.932  0 376 THR CCC OG1   1 ? 3 
ATOM   10261 C CG2   . THR C 1 376 ? 57.161  6.517   64.383  1.000 29.601  0 376 THR CCC CG2   1 ? 3 
ATOM   10262 N N     . VAL C 1 377 ? 55.733  5.244   61.884  1.000 26.484  0 377 VAL CCC N     1 ? 3 
ATOM   10263 C CA    . VAL C 1 377 ? 56.117  3.963   61.251  1.000 26.078  0 377 VAL CCC CA    1 ? 3 
ATOM   10264 C C     . VAL C 1 377 ? 57.517  3.663   61.764  1.000 26.391  0 377 VAL CCC C     1 ? 3 
ATOM   10265 O O     . VAL C 1 377 ? 58.397  4.566   61.598  1.000 25.334  0 377 VAL CCC O     1 ? 3 
ATOM   10266 C CB    . VAL C 1 377 ? 56.073  4.109   59.713  1.000 26.840  0 377 VAL CCC CB    1 ? 3 
ATOM   10267 C CG1   . VAL C 1 377 ? 56.611  2.866   59.034  1.000 27.117  0 377 VAL CCC CG1   1 ? 3 
ATOM   10268 C CG2   . VAL C 1 377 ? 54.663  4.453   59.221  1.000 26.093  0 377 VAL CCC CG2   1 ? 3 
ATOM   10269 N N     . PHE C 1 378 ? 57.721  2.505   62.413  1.000 25.502  0 378 PHE CCC N     1 ? 3 
ATOM   10270 C CA    . PHE C 1 378 ? 59.020  2.196   63.067  1.000 25.612  0 378 PHE CCC CA    1 ? 3 
ATOM   10271 C C     . PHE C 1 378 ? 59.920  1.414   62.098  1.000 25.265  0 378 PHE CCC C     1 ? 3 
ATOM   10272 O O     . PHE C 1 378 ? 60.379  0.302   62.408  1.000 23.969  0 378 PHE CCC O     1 ? 3 
ATOM   10273 C CB    . PHE C 1 378 ? 58.816  1.498   64.413  1.000 25.854  0 378 PHE CCC CB    1 ? 3 
ATOM   10274 C CG    . PHE C 1 378 ? 58.150  2.396   65.411  1.000 24.626  0 378 PHE CCC CG    1 ? 3 
ATOM   10275 C CD1   . PHE C 1 378 ? 58.918  3.261   66.171  1.000 24.076  0 378 PHE CCC CD1   1 ? 3 
ATOM   10276 C CD2   . PHE C 1 378 ? 56.758  2.426   65.522  1.000 24.203  0 378 PHE CCC CD2   1 ? 3 
ATOM   10277 C CE1   . PHE C 1 378 ? 58.313  4.121   67.075  1.000 24.140  0 378 PHE CCC CE1   1 ? 3 
ATOM   10278 C CE2   . PHE C 1 378 ? 56.137  3.288   66.418  1.000 24.212  0 378 PHE CCC CE2   1 ? 3 
ATOM   10279 C CZ    . PHE C 1 378 ? 56.917  4.136   67.188  1.000 24.321  0 378 PHE CCC CZ    1 ? 3 
ATOM   10280 N N     . THR C 1 379 ? 60.226  2.053   60.981  1.000 24.717  0 379 THR CCC N     1 ? 3 
ATOM   10281 C CA    . THR C 1 379 ? 61.175  1.545   59.977  1.000 25.524  0 379 THR CCC CA    1 ? 3 
ATOM   10282 C C     . THR C 1 379 ? 62.586  1.876   60.444  1.000 24.929  0 379 THR CCC C     1 ? 3 
ATOM   10283 O O     . THR C 1 379 ? 62.751  2.673   61.364  1.000 24.083  0 379 THR CCC O     1 ? 3 
ATOM   10284 C CB    . THR C 1 379 ? 60.762  2.080   58.603  1.000 25.795  0 379 THR CCC CB    1 ? 3 
ATOM   10285 O OG1   . THR C 1 379 ? 60.237  3.399   58.736  1.000 24.574  0 379 THR CCC OG1   1 ? 3 
ATOM   10286 C CG2   . THR C 1 379 ? 59.716  1.197   57.965  1.000 26.158  0 379 THR CCC CG2   1 ? 3 
ATOM   10287 N N     . PRO C 1 380 ? 63.634  1.252   59.861  1.000 25.230  0 380 PRO CCC N     1 ? 3 
ATOM   10288 C CA    . PRO C 1 380 ? 65.022  1.437   60.321  1.000 25.734  0 380 PRO CCC CA    1 ? 3 
ATOM   10289 C C     . PRO C 1 380 ? 65.408  2.907   60.520  1.000 26.280  0 380 PRO CCC C     1 ? 3 
ATOM   10290 O O     . PRO C 1 380 ? 66.089  3.166   61.448  1.000 31.397  0 380 PRO CCC O     1 ? 3 
ATOM   10291 C CB    . PRO C 1 380 ? 65.881  0.761   59.256  1.000 25.505  0 380 PRO CCC CB    1 ? 3 
ATOM   10292 C CG    . PRO C 1 380 ? 64.956  -0.314  58.724  1.000 25.906  0 380 PRO CCC CG    1 ? 3 
ATOM   10293 C CD    . PRO C 1 380 ? 63.559  0.309   58.745  1.000 25.956  0 380 PRO CCC CD    1 ? 3 
ATOM   10294 N N     . ILE C 1 381 ? 64.949  3.813   59.666  1.000 27.221  0 381 ILE CCC N     1 ? 3 
ATOM   10295 C CA    . ILE C 1 381 ? 64.695  5.236   60.034  1.000 27.324  0 381 ILE CCC CA    1 ? 3 
ATOM   10296 C C     . ILE C 1 381 ? 63.171  5.354   60.106  1.000 26.187  0 381 ILE CCC C     1 ? 3 
ATOM   10297 O O     . ILE C 1 381 ? 62.486  4.814   59.239  1.000 24.786  0 381 ILE CCC O     1 ? 3 
ATOM   10298 C CB    . ILE C 1 381 ? 65.312  6.256   59.045  1.000 29.002  0 381 ILE CCC CB    1 ? 3 
ATOM   10299 C CG1   . ILE C 1 381 ? 64.891  5.996   57.605  1.000 29.514  0 381 ILE CCC CG1   1 ? 3 
ATOM   10300 C CG2   . ILE C 1 381 ? 66.824  6.350   59.179  1.000 29.421  0 381 ILE CCC CG2   1 ? 3 
ATOM   10301 C CD1   . ILE C 1 381 ? 65.502  6.954   56.610  1.000 31.012  0 381 ILE CCC CD1   1 ? 3 
ATOM   10302 N N     . GLU C 1 382 ? 62.688  6.012   61.147  1.000 26.385  0 382 GLU CCC N     1 ? 3 
ATOM   10303 C CA    . GLU C 1 382 ? 61.266  6.077   61.532  1.000 26.714  0 382 GLU CCC CA    1 ? 3 
ATOM   10304 C C     . GLU C 1 382 ? 60.601  7.223   60.784  1.000 25.340  0 382 GLU CCC C     1 ? 3 
ATOM   10305 O O     . GLU C 1 382 ? 61.314  8.119   60.313  1.000 26.574  0 382 GLU CCC O     1 ? 3 
ATOM   10306 C CB    . GLU C 1 382 ? 61.143  6.250   63.040  1.000 27.188  0 382 GLU CCC CB    1 ? 3 
ATOM   10307 C CG    . GLU C 1 382 ? 62.045  5.304   63.830  1.000 28.178  0 382 GLU CCC CG    1 ? 3 
ATOM   10308 C CD    . GLU C 1 382 ? 61.865  5.352   65.340  1.000 28.749  0 382 GLU CCC CD    1 ? 3 
ATOM   10309 O OE1   . GLU C 1 382 ? 61.318  6.387   65.873  1.000 30.039  0 382 GLU CCC OE1   1 ? 3 
ATOM   10310 O OE2   . GLU C 1 382 ? 62.262  4.369   65.978  1.000 29.423  0 382 GLU CCC OE2   1 ? 3 
ATOM   10311 N N     . TYR C 1 383 ? 59.282  7.207   60.703  1.000 24.069  0 383 TYR CCC N     1 ? 3 
ATOM   10312 C CA    . TYR C 1 383 ? 58.526  8.276   60.009  1.000 25.254  0 383 TYR CCC CA    1 ? 3 
ATOM   10313 C C     . TYR C 1 383 ? 57.316  8.628   60.857  1.000 23.777  0 383 TYR CCC C     1 ? 3 
ATOM   10314 O O     . TYR C 1 383 ? 56.430  7.777   61.069  1.000 22.257  0 383 TYR CCC O     1 ? 3 
ATOM   10315 C CB    . TYR C 1 383 ? 58.201  7.879   58.564  1.000 26.103  0 383 TYR CCC CB    1 ? 3 
ATOM   10316 C CG    . TYR C 1 383 ? 57.191  8.771   57.895  1.000 27.682  0 383 TYR CCC CG    1 ? 3 
ATOM   10317 C CD1   . TYR C 1 383 ? 57.295  10.145  58.016  1.000 28.388  0 383 TYR CCC CD1   1 ? 3 
ATOM   10318 C CD2   . TYR C 1 383 ? 56.148  8.255   57.139  1.000 27.878  0 383 TYR CCC CD2   1 ? 3 
ATOM   10319 C CE1   . TYR C 1 383 ? 56.366  10.988  57.434  1.000 28.547  0 383 TYR CCC CE1   1 ? 3 
ATOM   10320 C CE2   . TYR C 1 383 ? 55.217  9.091   56.548  1.000 28.717  0 383 TYR CCC CE2   1 ? 3 
ATOM   10321 C CZ    . TYR C 1 383 ? 55.311  10.465  56.704  1.000 29.088  0 383 TYR CCC CZ    1 ? 3 
ATOM   10322 O OH    . TYR C 1 383 ? 54.399  11.303  56.116  1.000 27.197  0 383 TYR CCC OH    1 ? 3 
ATOM   10323 N N     . GLY C 1 384 ? 57.334  9.848   61.371  1.000 23.238  0 384 GLY CCC N     1 ? 3 
ATOM   10324 C CA    . GLY C 1 384 ? 56.232  10.379  62.177  1.000 23.968  0 384 GLY CCC CA    1 ? 3 
ATOM   10325 C C     . GLY C 1 384 ? 55.578  11.524  61.432  1.000 24.399  0 384 GLY CCC C     1 ? 3 
ATOM   10326 O O     . GLY C 1 384 ? 56.326  12.313  60.776  1.000 24.606  0 384 GLY CCC O     1 ? 3 
ATOM   10327 N N     . HIS C 1 385 ? 54.253  11.610  61.471  1.000 23.860  0 385 HIS CCC N     1 ? 3 
ATOM   10328 C CA    . HIS C 1 385 ? 53.514  12.707  60.799  1.000 25.121  0 385 HIS CCC CA    1 ? 3 
ATOM   10329 C C     . HIS C 1 385 ? 52.193  12.952  61.531  1.000 26.123  0 385 HIS CCC C     1 ? 3 
ATOM   10330 O O     . HIS C 1 385 ? 51.717  12.044  62.209  1.000 26.165  0 385 HIS CCC O     1 ? 3 
ATOM   10331 C CB    . HIS C 1 385 ? 53.309  12.398  59.295  1.000 24.524  0 385 HIS CCC CB    1 ? 3 
ATOM   10332 C CG    . HIS C 1 385 ? 52.028  11.708  58.972  1.000 24.439  0 385 HIS CCC CG    1 ? 3 
ATOM   10333 N ND1   . HIS C 1 385 ? 51.903  10.346  58.862  1.000 24.028  0 385 HIS CCC ND1   1 ? 3 
ATOM   10334 C CD2   . HIS C 1 385 ? 50.791  12.206  58.697  1.000 24.318  0 385 HIS CCC CD2   1 ? 3 
ATOM   10335 C CE1   . HIS C 1 385 ? 50.631  10.048  58.594  1.000 23.741  0 385 HIS CCC CE1   1 ? 3 
ATOM   10336 N NE2   . HIS C 1 385 ? 49.938  11.163  58.520  1.000 23.341  0 385 HIS CCC NE2   1 ? 3 
ATOM   10337 N N     . VAL C 1 386 ? 51.646  14.146  61.360  1.000 27.510  0 386 VAL CCC N     1 ? 3 
ATOM   10338 C CA    . VAL C 1 386 ? 50.221  14.474  61.649  1.000 28.816  0 386 VAL CCC CA    1 ? 3 
ATOM   10339 C C     . VAL C 1 386 ? 49.723  15.405  60.547  1.000 30.915  0 386 VAL CCC C     1 ? 3 
ATOM   10340 O O     . VAL C 1 386 ? 50.570  16.199  59.966  1.000 30.313  0 386 VAL CCC O     1 ? 3 
ATOM   10341 C CB    . VAL C 1 386 ? 50.040  15.119  63.023  1.000 28.804  0 386 VAL CCC CB    1 ? 3 
ATOM   10342 C CG1   . VAL C 1 386 ? 50.687  16.496  63.075  1.000 28.645  0 386 VAL CCC CG1   1 ? 3 
ATOM   10343 C CG2   . VAL C 1 386 ? 48.572  15.154  63.427  1.000 28.924  0 386 VAL CCC CG2   1 ? 3 
ATOM   10344 N N     . GLY C 1 387 ? 48.430  15.284  60.257  1.000 30.763  0 387 GLY CCC N     1 ? 3 
ATOM   10345 C CA    . GLY C 1 387 ? 47.758  16.097  59.244  1.000 32.871  0 387 GLY CCC CA    1 ? 3 
ATOM   10346 C C     . GLY C 1 387 ? 48.067  15.573  57.859  1.000 35.377  0 387 GLY CCC C     1 ? 3 
ATOM   10347 O O     . GLY C 1 387 ? 48.276  14.341  57.730  1.000 33.287  0 387 GLY CCC O     1 ? 3 
ATOM   10348 N N     . LEU C 1 388 ? 48.138  16.485  56.881  1.000 37.614  0 388 LEU CCC N     1 ? 3 
ATOM   10349 C CA    . LEU C 1 388 ? 48.053  16.139  55.444  1.000 38.205  0 388 LEU CCC CA    1 ? 3 
ATOM   10350 C C     . LEU C 1 388 ? 49.460  15.952  54.875  1.000 38.260  0 388 LEU CCC C     1 ? 3 
ATOM   10351 O O     . LEU C 1 388 ? 50.385  16.721  55.231  1.000 34.528  0 388 LEU CCC O     1 ? 3 
ATOM   10352 C CB    . LEU C 1 388 ? 47.304  17.249  54.702  1.000 39.280  0 388 LEU CCC CB    1 ? 3 
ATOM   10353 C CG    . LEU C 1 388 ? 45.931  17.630  55.271  1.000 40.181  0 388 LEU CCC CG    1 ? 3 
ATOM   10354 C CD1   . LEU C 1 388 ? 45.319  18.768  54.445  1.000 41.297  0 388 LEU CCC CD1   1 ? 3 
ATOM   10355 C CD2   . LEU C 1 388 ? 44.967  16.451  55.284  1.000 38.858  0 388 LEU CCC CD2   1 ? 3 
ATOM   10356 N N     . SER C 1 389 ? 49.577  14.958  54.003  1.000 38.206  0 389 SER CCC N     1 ? 3 
ATOM   10357 C CA    . SER C 1 389 ? 50.672  14.817  53.027  1.000 38.645  0 389 SER CCC CA    1 ? 3 
ATOM   10358 C C     . SER C 1 389 ? 50.681  16.049  52.113  1.000 39.016  0 389 SER CCC C     1 ? 3 
ATOM   10359 O O     . SER C 1 389 ? 49.670  16.787  52.074  1.000 35.940  0 389 SER CCC O     1 ? 3 
ATOM   10360 C CB    . SER C 1 389 ? 50.481  13.555  52.234  1.000 39.608  0 389 SER CCC CB    1 ? 3 
ATOM   10361 O OG    . SER C 1 389 ? 49.228  13.593  51.555  1.000 41.691  0 389 SER CCC OG    1 ? 3 
ATOM   10362 N N     . SER C 1 390 ? 51.805  16.275  51.433  1.000 39.124  0 390 SER CCC N     1 ? 3 
ATOM   10363 C CA    . SER C 1 390 ? 51.922  17.206  50.282  1.000 40.351  0 390 SER CCC CA    1 ? 3 
ATOM   10364 C C     . SER C 1 390 ? 50.743  16.967  49.325  1.000 40.356  0 390 SER CCC C     1 ? 3 
ATOM   10365 O O     . SER C 1 390 ? 50.061  17.934  48.992  1.000 41.129  0 390 SER CCC O     1 ? 3 
ATOM   10366 C CB    . SER C 1 390 ? 53.273  17.045  49.601  1.000 38.920  0 390 SER CCC CB    1 ? 3 
ATOM   10367 O OG    . SER C 1 390 ? 54.327  17.301  50.513  1.000 37.094  0 390 SER CCC OG    1 ? 3 
ATOM   10368 N N     . GLU C 1 391 ? 50.481  15.703  48.973  1.000 41.820  0 391 GLU CCC N     1 ? 3 
ATOM   10369 C CA    . GLU C 1 391 ? 49.455  15.301  47.969  1.000 42.909  0 391 GLU CCC CA    1 ? 3 
ATOM   10370 C C     . GLU C 1 391 ? 48.056  15.732  48.471  1.000 45.017  0 391 GLU CCC C     1 ? 3 
ATOM   10371 O O     . GLU C 1 391 ? 47.338  16.414  47.703  1.000 46.455  0 391 GLU CCC O     1 ? 3 
ATOM   10372 C CB    . GLU C 1 391 ? 49.526  13.796  47.659  1.000 41.300  0 391 GLU CCC CB    1 ? 3 
ATOM   10373 C CG    . GLU C 1 391 ? 50.758  13.386  46.867  1.000 43.140  0 391 GLU CCC CG    1 ? 3 
ATOM   10374 C CD    . GLU C 1 391 ? 52.091  13.382  47.629  1.000 44.661  0 391 GLU CCC CD    1 ? 3 
ATOM   10375 O OE1   . GLU C 1 391 ? 52.125  12.956  48.843  1.000 40.702  0 391 GLU CCC OE1   1 ? 3 
ATOM   10376 O OE2   . GLU C 1 391 ? 53.097  13.833  47.017  1.000 44.523  0 391 GLU CCC OE2   1 ? 3 
ATOM   10377 N N     . ALA C 1 392 ? 47.659  15.365  49.692  1.000 43.656  0 392 ALA CCC N     1 ? 3 
ATOM   10378 C CA    . ALA C 1 392 ? 46.325  15.711  50.239  1.000 42.976  0 392 ALA CCC CA    1 ? 3 
ATOM   10379 C C     . ALA C 1 392 ? 46.224  17.235  50.427  1.000 43.719  0 392 ALA CCC C     1 ? 3 
ATOM   10380 O O     . ALA C 1 392 ? 45.094  17.773  50.325  1.000 45.496  0 392 ALA CCC O     1 ? 3 
ATOM   10381 C CB    . ALA C 1 392 ? 46.040  14.964  51.521  1.000 40.472  0 392 ALA CCC CB    1 ? 3 
ATOM   10382 N N     . ALA C 1 393 ? 47.342  17.925  50.667  1.000 42.489  0 393 ALA CCC N     1 ? 3 
ATOM   10383 C CA    . ALA C 1 393 ? 47.374  19.394  50.871  1.000 44.254  0 393 ALA CCC CA    1 ? 3 
ATOM   10384 C C     . ALA C 1 393 ? 47.133  20.097  49.529  1.000 47.174  0 393 ALA CCC C     1 ? 3 
ATOM   10385 O O     . ALA C 1 393 ? 46.263  21.001  49.464  1.000 49.118  0 393 ALA CCC O     1 ? 3 
ATOM   10386 C CB    . ALA C 1 393 ? 48.668  19.821  51.494  1.000 41.986  0 393 ALA CCC CB    1 ? 3 
ATOM   10387 N N     . ILE C 1 394 ? 47.867  19.672  48.501  1.000 48.038  0 394 ILE CCC N     1 ? 3 
ATOM   10388 C CA    . ILE C 1 394 ? 47.737  20.182  47.108  1.000 51.432  0 394 ILE CCC CA    1 ? 3 
ATOM   10389 C C     . ILE C 1 394 ? 46.295  19.917  46.602  1.000 51.393  0 394 ILE CCC C     1 ? 3 
ATOM   10390 O O     . ILE C 1 394 ? 45.662  20.873  46.138  1.000 51.068  0 394 ILE CCC O     1 ? 3 
ATOM   10391 C CB    . ILE C 1 394 ? 48.864  19.609  46.228  1.000 51.384  0 394 ILE CCC CB    1 ? 3 
ATOM   10392 C CG1   . ILE C 1 394 ? 50.198  20.274  46.588  1.000 53.598  0 394 ILE CCC CG1   1 ? 3 
ATOM   10393 C CG2   . ILE C 1 394 ? 48.531  19.746  44.742  1.000 51.327  0 394 ILE CCC CG2   1 ? 3 
ATOM   10394 C CD1   . ILE C 1 394 ? 51.431  19.705  45.881  1.000 54.239  0 394 ILE CCC CD1   1 ? 3 
ATOM   10395 N N     . ALA C 1 395 ? 45.763  18.704  46.763  1.000 48.583  0 395 ALA CCC N     1 ? 3 
ATOM   10396 C CA    . ALA C 1 395 ? 44.385  18.311  46.362  1.000 48.764  0 395 ALA CCC CA    1 ? 3 
ATOM   10397 C C     . ALA C 1 395 ? 43.333  19.211  47.028  1.000 49.041  0 395 ALA CCC C     1 ? 3 
ATOM   10398 O O     . ALA C 1 395 ? 42.394  19.603  46.334  1.000 51.023  0 395 ALA CCC O     1 ? 3 
ATOM   10399 C CB    . ALA C 1 395 ? 44.113  16.852  46.679  1.000 47.789  0 395 ALA CCC CB    1 ? 3 
ATOM   10400 N N     . LYS C 1 396 ? 43.477  19.536  48.313  1.000 51.372  0 396 LYS CCC N     1 ? 3 
ATOM   10401 C CA    . LYS C 1 396 ? 42.422  20.229  49.109  1.000 51.015  0 396 LYS CCC CA    1 ? 3 
ATOM   10402 C C     . LYS C 1 396 ? 42.449  21.745  48.869  1.000 50.724  0 396 LYS CCC C     1 ? 3 
ATOM   10403 O O     . LYS C 1 396 ? 41.364  22.316  48.774  1.000 48.657  0 396 LYS CCC O     1 ? 3 
ATOM   10404 C CB    . LYS C 1 396 ? 42.577  19.926  50.603  1.000 53.321  0 396 LYS CCC CB    1 ? 3 
ATOM   10405 C CG    . LYS C 1 396 ? 41.495  20.509  51.502  1.000 54.451  0 396 LYS CCC CG    1 ? 3 
ATOM   10406 C CD    . LYS C 1 396 ? 41.784  20.272  52.973  1.000 56.331  0 396 LYS CCC CD    1 ? 3 
ATOM   10407 C CE    . LYS C 1 396 ? 40.882  21.044  53.918  1.000 60.302  0 396 LYS CCC CE    1 ? 3 
ATOM   10408 N NZ    . LYS C 1 396 ? 39.452  20.625  53.797  1.000 62.688  0 396 LYS CCC NZ    1 ? 3 
ATOM   10409 N N     . TYR C 1 397 ? 43.631  22.376  48.802  1.000 52.925  0 397 TYR CCC N     1 ? 3 
ATOM   10410 C CA    . TYR C 1 397 ? 43.803  23.861  48.786  1.000 52.241  0 397 TYR CCC CA    1 ? 3 
ATOM   10411 C C     . TYR C 1 397 ? 44.232  24.372  47.397  1.000 50.449  0 397 TYR CCC C     1 ? 3 
ATOM   10412 O O     . TYR C 1 397 ? 44.098  25.582  47.152  1.000 45.498  0 397 TYR CCC O     1 ? 3 
ATOM   10413 C CB    . TYR C 1 397 ? 44.775  24.307  49.891  1.000 53.048  0 397 TYR CCC CB    1 ? 3 
ATOM   10414 C CG    . TYR C 1 397 ? 44.234  24.115  51.288  1.000 55.382  0 397 TYR CCC CG    1 ? 3 
ATOM   10415 C CD1   . TYR C 1 397 ? 43.236  24.935  51.787  1.000 57.273  0 397 TYR CCC CD1   1 ? 3 
ATOM   10416 C CD2   . TYR C 1 397 ? 44.671  23.079  52.102  1.000 58.143  0 397 TYR CCC CD2   1 ? 3 
ATOM   10417 C CE1   . TYR C 1 397 ? 42.686  24.737  53.044  1.000 59.676  0 397 TYR CCC CE1   1 ? 3 
ATOM   10418 C CE2   . TYR C 1 397 ? 44.134  22.868  53.368  1.000 57.225  0 397 TYR CCC CE2   1 ? 3 
ATOM   10419 C CZ    . TYR C 1 397 ? 43.135  23.700  53.843  1.000 58.362  0 397 TYR CCC CZ    1 ? 3 
ATOM   10420 O OH    . TYR C 1 397 ? 42.587  23.517  55.081  1.000 57.901  0 397 TYR CCC OH    1 ? 3 
ATOM   10421 N N     . GLY C 1 398 ? 44.735  23.483  46.534  1.000 49.829  0 398 GLY CCC N     1 ? 3 
ATOM   10422 C CA    . GLY C 1 398 ? 45.406  23.827  45.271  1.000 51.479  0 398 GLY CCC CA    1 ? 3 
ATOM   10423 C C     . GLY C 1 398 ? 46.899  24.083  45.460  1.000 53.056  0 398 GLY CCC C     1 ? 3 
ATOM   10424 O O     . GLY C 1 398 ? 47.285  24.636  46.491  1.000 49.575  0 398 GLY CCC O     1 ? 3 
ATOM   10425 N N     . GLU C 1 399 ? 47.684  23.753  44.434  1.000 57.033  0 399 GLU CCC N     1 ? 3 
ATOM   10426 C CA    . GLU C 1 399 ? 49.163  23.874  44.355  1.000 60.127  0 399 GLU CCC CA    1 ? 3 
ATOM   10427 C C     . GLU C 1 399 ? 49.618  25.276  44.771  1.000 63.094  0 399 GLU CCC C     1 ? 3 
ATOM   10428 O O     . GLU C 1 399 ? 50.706  25.377  45.365  1.000 67.185  0 399 GLU CCC O     1 ? 3 
ATOM   10429 C CB    . GLU C 1 399 ? 49.611  23.586  42.921  1.000 65.779  0 399 GLU CCC CB    1 ? 3 
ATOM   10430 C CG    . GLU C 1 399 ? 51.113  23.629  42.711  1.000 70.260  0 399 GLU CCC CG    1 ? 3 
ATOM   10431 C CD    . GLU C 1 399 ? 51.845  22.407  43.245  1.000 75.626  0 399 GLU CCC CD    1 ? 3 
ATOM   10432 O OE1   . GLU C 1 399 ? 51.398  21.268  42.927  1.000 78.087  0 399 GLU CCC OE1   1 ? 3 
ATOM   10433 O OE2   . GLU C 1 399 ? 52.859  22.588  43.978  1.000 72.250  0 399 GLU CCC OE2   1 ? 3 
ATOM   10434 N N     . ASP C 1 400 ? 48.852  26.323  44.461  1.000 63.719  0 400 ASP CCC N     1 ? 3 
ATOM   10435 C CA    . ASP C 1 400 ? 49.311  27.728  44.625  1.000 66.584  0 400 ASP CCC CA    1 ? 3 
ATOM   10436 C C     . ASP C 1 400 ? 49.063  28.234  46.040  1.000 62.765  0 400 ASP CCC C     1 ? 3 
ATOM   10437 O O     . ASP C 1 400 ? 49.691  29.249  46.398  1.000 63.859  0 400 ASP CCC O     1 ? 3 
ATOM   10438 C CB    . ASP C 1 400 ? 48.633  28.670  43.634  1.000 71.776  0 400 ASP CCC CB    1 ? 3 
ATOM   10439 C CG    . ASP C 1 400 ? 49.464  28.858  42.386  1.000 74.419  0 400 ASP CCC CG    1 ? 3 
ATOM   10440 O OD1   . ASP C 1 400 ? 50.202  27.915  42.023  1.000 76.567  0 400 ASP CCC OD1   1 ? 3 
ATOM   10441 O OD2   . ASP C 1 400 ? 49.392  29.951  41.816  1.000 83.356  0 400 ASP CCC OD2   1 ? 3 
ATOM   10442 N N     . ASP C 1 401 ? 48.170  27.587  46.789  1.000 59.254  0 401 ASP CCC N     1 ? 3 
ATOM   10443 C CA    . ASP C 1 401 ? 47.873  27.982  48.187  1.000 61.356  0 401 ASP CCC CA    1 ? 3 
ATOM   10444 C C     . ASP C 1 401 ? 48.765  27.161  49.141  1.000 61.587  0 401 ASP CCC C     1 ? 3 
ATOM   10445 O O     . ASP C 1 401 ? 48.560  27.268  50.366  1.000 62.443  0 401 ASP CCC O     1 ? 3 
ATOM   10446 C CB    . ASP C 1 401 ? 46.370  27.875  48.468  1.000 59.736  0 401 ASP CCC CB    1 ? 3 
ATOM   10447 C CG    . ASP C 1 401 ? 45.868  28.788  49.585  1.000 61.856  0 401 ASP CCC CG    1 ? 3 
ATOM   10448 O OD1   . ASP C 1 401 ? 46.564  29.776  49.918  1.000 62.053  0 401 ASP CCC OD1   1 ? 3 
ATOM   10449 O OD2   . ASP C 1 401 ? 44.780  28.506  50.126  1.000 64.099  0 401 ASP CCC OD2   1 ? 3 
ATOM   10450 N N     . ILE C 1 402 ? 49.723  26.379  48.613  1.000 61.044  0 402 ILE CCC N     1 ? 3 
ATOM   10451 C CA    . ILE C 1 402 ? 50.571  25.419  49.390  1.000 57.567  0 402 ILE CCC CA    1 ? 3 
ATOM   10452 C C     . ILE C 1 402 ? 52.044  25.824  49.308  1.000 58.235  0 402 ILE CCC C     1 ? 3 
ATOM   10453 O O     . ILE C 1 402 ? 52.580  25.964  48.191  1.000 61.266  0 402 ILE CCC O     1 ? 3 
ATOM   10454 C CB    . ILE C 1 402 ? 50.373  23.970  48.897  1.000 54.471  0 402 ILE CCC CB    1 ? 3 
ATOM   10455 C CG1   . ILE C 1 402 ? 48.990  23.434  49.274  1.000 53.378  0 402 ILE CCC CG1   1 ? 3 
ATOM   10456 C CG2   . ILE C 1 402 ? 51.485  23.060  49.404  1.000 55.305  0 402 ILE CCC CG2   1 ? 3 
ATOM   10457 C CD1   . ILE C 1 402 ? 48.587  23.686  50.709  1.000 52.108  0 402 ILE CCC CD1   1 ? 3 
ATOM   10458 N N     . GLU C 1 403 ? 52.695  25.938  50.462  1.000 54.477  0 403 GLU CCC N     1 ? 3 
ATOM   10459 C CA    . GLU C 1 403 ? 54.174  25.986  50.546  1.000 52.033  0 403 GLU CCC CA    1 ? 3 
ATOM   10460 C C     . GLU C 1 403 ? 54.634  24.734  51.306  1.000 48.835  0 403 GLU CCC C     1 ? 3 
ATOM   10461 O O     . GLU C 1 403 ? 54.033  24.389  52.329  1.000 45.844  0 403 GLU CCC O     1 ? 3 
ATOM   10462 C CB    . GLU C 1 403 ? 54.630  27.285  51.213  1.000 53.366  0 403 GLU CCC CB    1 ? 3 
ATOM   10463 C CG    . GLU C 1 403 ? 55.972  27.797  50.709  1.000 54.121  0 403 GLU CCC CG    1 ? 3 
ATOM   10464 C CD    . GLU C 1 403 ? 55.954  28.406  49.316  1.000 54.604  0 403 GLU CCC CD    1 ? 3 
ATOM   10465 O OE1   . GLU C 1 403 ? 55.239  29.398  49.105  1.000 51.841  0 403 GLU CCC OE1   1 ? 3 
ATOM   10466 O OE2   . GLU C 1 403 ? 56.660  27.875  48.442  1.000 56.820  0 403 GLU CCC OE2   1 ? 3 
ATOM   10467 N N     . GLU C 1 404 ? 55.676  24.082  50.802  1.000 48.577  0 404 GLU CCC N     1 ? 3 
ATOM   10468 C CA    . GLU C 1 404 ? 56.411  23.001  51.504  1.000 46.068  0 404 GLU CCC CA    1 ? 3 
ATOM   10469 C C     . GLU C 1 404 ? 57.801  23.525  51.861  1.000 45.327  0 404 GLU CCC C     1 ? 3 
ATOM   10470 O O     . GLU C 1 404 ? 58.592  23.841  50.943  1.000 47.720  0 404 GLU CCC O     1 ? 3 
ATOM   10471 C CB    . GLU C 1 404 ? 56.447  21.739  50.652  1.000 46.741  0 404 GLU CCC CB    1 ? 3 
ATOM   10472 C CG    . GLU C 1 404 ? 55.068  21.304  50.167  1.000 48.676  0 404 GLU CCC CG    1 ? 3 
ATOM   10473 C CD    . GLU C 1 404 ? 55.107  20.199  49.117  1.000 49.427  0 404 GLU CCC CD    1 ? 3 
ATOM   10474 O OE1   . GLU C 1 404 ? 55.865  19.281  49.303  1.000 50.556  0 404 GLU CCC OE1   1 ? 3 
ATOM   10475 O OE2   . GLU C 1 404 ? 54.387  20.274  48.107  1.000 56.391  0 404 GLU CCC OE2   1 ? 3 
ATOM   10476 N N     . TYR C 1 405 ? 58.072  23.646  53.157  1.000 41.990  0 405 TYR CCC N     1 ? 3 
ATOM   10477 C CA    . TYR C 1 405 ? 59.411  23.952  53.706  1.000 40.757  0 405 TYR CCC CA    1 ? 3 
ATOM   10478 C C     . TYR C 1 405 ? 60.018  22.635  54.170  1.000 40.718  0 405 TYR CCC C     1 ? 3 
ATOM   10479 O O     . TYR C 1 405 ? 59.325  21.850  54.830  1.000 42.378  0 405 TYR CCC O     1 ? 3 
ATOM   10480 C CB    . TYR C 1 405 ? 59.278  24.938  54.863  1.000 40.705  0 405 TYR CCC CB    1 ? 3 
ATOM   10481 C CG    . TYR C 1 405 ? 58.814  26.325  54.486  1.000 42.109  0 405 TYR CCC CG    1 ? 3 
ATOM   10482 C CD1   . TYR C 1 405 ? 59.735  27.342  54.237  1.000 42.277  0 405 TYR CCC CD1   1 ? 3 
ATOM   10483 C CD2   . TYR C 1 405 ? 57.462  26.655  54.478  1.000 41.670  0 405 TYR CCC CD2   1 ? 3 
ATOM   10484 C CE1   . TYR C 1 405 ? 59.322  28.641  53.974  1.000 42.952  0 405 TYR CCC CE1   1 ? 3 
ATOM   10485 C CE2   . TYR C 1 405 ? 57.035  27.946  54.203  1.000 41.936  0 405 TYR CCC CE2   1 ? 3 
ATOM   10486 C CZ    . TYR C 1 405 ? 57.966  28.937  53.938  1.000 43.244  0 405 TYR CCC CZ    1 ? 3 
ATOM   10487 O OH    . TYR C 1 405 ? 57.559  30.203  53.643  1.000 44.885  0 405 TYR CCC OH    1 ? 3 
ATOM   10488 N N     . LEU C 1 406 ? 61.274  22.372  53.839  1.000 40.211  0 406 LEU CCC N     1 ? 3 
ATOM   10489 C CA    . LEU C 1 406 ? 61.888  21.069  54.157  1.000 38.143  0 406 LEU CCC CA    1 ? 3 
ATOM   10490 C C     . LEU C 1 406 ? 63.404  21.189  54.232  1.000 36.969  0 406 LEU CCC C     1 ? 3 
ATOM   10491 O O     . LEU C 1 406 ? 63.986  22.206  53.800  1.000 36.992  0 406 LEU CCC O     1 ? 3 
ATOM   10492 C CB    . LEU C 1 406 ? 61.405  20.000  53.176  1.000 41.082  0 406 LEU CCC CB    1 ? 3 
ATOM   10493 C CG    . LEU C 1 406 ? 61.921  20.027  51.726  1.000 44.870  0 406 LEU CCC CG    1 ? 3 
ATOM   10494 C CD1   . LEU C 1 406 ? 61.427  18.781  50.973  1.000 45.737  0 406 LEU CCC CD1   1 ? 3 
ATOM   10495 C CD2   . LEU C 1 406 ? 61.492  21.275  50.942  1.000 45.305  0 406 LEU CCC CD2   1 ? 3 
ATOM   10496 N N     . SER C 1 407 ? 63.989  20.211  54.904  1.000 34.713  0 407 SER CCC N     1 ? 3 
ATOM   10497 C CA    . SER C 1 407 ? 65.438  20.072  55.129  1.000 34.987  0 407 SER CCC CA    1 ? 3 
ATOM   10498 C C     . SER C 1 407 ? 65.771  18.573  55.231  1.000 34.986  0 407 SER CCC C     1 ? 3 
ATOM   10499 O O     . SER C 1 407 ? 65.024  17.857  55.902  1.000 33.196  0 407 SER CCC O     1 ? 3 
ATOM   10500 C CB    . SER C 1 407 ? 65.837  20.847  56.344  1.000 32.884  0 407 SER CCC CB    1 ? 3 
ATOM   10501 O OG    . SER C 1 407 ? 67.233  20.731  56.542  1.000 32.423  0 407 SER CCC OG    1 ? 3 
ATOM   10502 N N     . GLU C 1 408 ? 66.808  18.117  54.530  1.000 35.720  0 408 GLU CCC N     1 ? 3 
ATOM   10503 C CA    . GLU C 1 408 ? 67.333  16.733  54.611  1.000 35.610  0 408 GLU CCC CA    1 ? 3 
ATOM   10504 C C     . GLU C 1 408 ? 68.736  16.843  55.188  1.000 37.415  0 408 GLU CCC C     1 ? 3 
ATOM   10505 O O     . GLU C 1 408 ? 69.547  17.627  54.648  1.000 40.399  0 408 GLU CCC O     1 ? 3 
ATOM   10506 C CB    . GLU C 1 408 ? 67.404  16.078  53.239  1.000 35.424  0 408 GLU CCC CB    1 ? 3 
ATOM   10507 C CG    . GLU C 1 408 ? 67.602  14.580  53.276  1.000 35.728  0 408 GLU CCC CG    1 ? 3 
ATOM   10508 C CD    . GLU C 1 408 ? 67.573  13.904  51.910  1.000 38.028  0 408 GLU CCC CD    1 ? 3 
ATOM   10509 O OE1   . GLU C 1 408 ? 67.866  14.604  50.902  1.000 42.089  0 408 GLU CCC OE1   1 ? 3 
ATOM   10510 O OE2   . GLU C 1 408 ? 67.243  12.694  51.833  1.000 37.421  0 408 GLU CCC OE2   1 ? 3 
ATOM   10511 N N     . PHE C 1 409 ? 69.024  16.101  56.245  1.000 35.675  0 409 PHE CCC N     1 ? 3 
ATOM   10512 C CA    . PHE C 1 409 ? 70.292  16.247  56.991  1.000 33.273  0 409 PHE CCC CA    1 ? 3 
ATOM   10513 C C     . PHE C 1 409 ? 70.556  14.977  57.785  1.000 32.174  0 409 PHE CCC C     1 ? 3 
ATOM   10514 O O     . PHE C 1 409 ? 69.700  14.056  57.839  1.000 33.623  0 409 PHE CCC O     1 ? 3 
ATOM   10515 C CB    . PHE C 1 409 ? 70.191  17.416  57.969  1.000 31.223  0 409 PHE CCC CB    1 ? 3 
ATOM   10516 C CG    . PHE C 1 409 ? 69.078  17.238  58.964  1.000 29.822  0 409 PHE CCC CG    1 ? 3 
ATOM   10517 C CD1   . PHE C 1 409 ? 67.771  17.465  58.587  1.000 28.589  0 409 PHE CCC CD1   1 ? 3 
ATOM   10518 C CD2   . PHE C 1 409 ? 69.332  16.808  60.259  1.000 27.948  0 409 PHE CCC CD2   1 ? 3 
ATOM   10519 C CE1   . PHE C 1 409 ? 66.741  17.298  59.504  1.000 28.240  0 409 PHE CCC CE1   1 ? 3 
ATOM   10520 C CE2   . PHE C 1 409 ? 68.288  16.621  61.150  1.000 27.751  0 409 PHE CCC CE2   1 ? 3 
ATOM   10521 C CZ    . PHE C 1 409 ? 66.999  16.884  60.780  1.000 26.173  0 409 PHE CCC CZ    1 ? 3 
ATOM   10522 N N     . SER C 1 410 ? 71.694  14.973  58.462  1.000 30.697  0 410 SER CCC N     1 ? 3 
ATOM   10523 C CA    . SER C 1 410 ? 72.106  13.823  59.293  1.000 30.230  0 410 SER CCC CA    1 ? 3 
ATOM   10524 C C     . SER C 1 410 ? 72.038  14.224  60.753  1.000 27.996  0 410 SER CCC C     1 ? 3 
ATOM   10525 O O     . SER C 1 410 ? 72.370  15.359  61.055  1.000 27.796  0 410 SER CCC O     1 ? 3 
ATOM   10526 C CB    . SER C 1 410 ? 73.448  13.334  58.897  1.000 30.556  0 410 SER CCC CB    1 ? 3 
ATOM   10527 O OG    . SER C 1 410 ? 73.891  12.404  59.850  1.000 32.022  0 410 SER CCC OG    1 ? 3 
ATOM   10528 N N     . THR C 1 411 ? 71.523  13.337  61.598  1.000 27.438  0 411 THR CCC N     1 ? 3 
ATOM   10529 C CA    . THR C 1 411 ? 71.759  13.380  63.065  1.000 26.977  0 411 THR CCC CA    1 ? 3 
ATOM   10530 C C     . THR C 1 411 ? 73.264  13.616  63.267  1.000 27.643  0 411 THR CCC C     1 ? 3 
ATOM   10531 O O     . THR C 1 411 ? 74.060  13.062  62.483  1.000 27.461  0 411 THR CCC O     1 ? 3 
ATOM   10532 C CB    . THR C 1 411 ? 71.291  12.085  63.731  1.000 25.852  0 411 THR CCC CB    1 ? 3 
ATOM   10533 O OG1   . THR C 1 411 ? 69.927  11.914  63.376  1.000 24.170  0 411 THR CCC OG1   1 ? 3 
ATOM   10534 C CG2   . THR C 1 411 ? 71.414  12.088  65.245  1.000 25.509  0 411 THR CCC CG2   1 ? 3 
ATOM   10535 N N     . LEU C 1 412 ? 73.616  14.450  64.231  1.000 28.296  0 412 LEU CCC N     1 ? 3 
ATOM   10536 C CA    . LEU C 1 412 ? 75.009  14.772  64.620  1.000 31.314  0 412 LEU CCC CA    1 ? 3 
ATOM   10537 C C     . LEU C 1 412 ? 75.824  13.490  64.890  1.000 32.593  0 412 LEU CCC C     1 ? 3 
ATOM   10538 O O     . LEU C 1 412 ? 76.896  13.327  64.319  1.000 33.646  0 412 LEU CCC O     1 ? 3 
ATOM   10539 C CB    . LEU C 1 412 ? 74.901  15.621  65.890  1.000 31.949  0 412 LEU CCC CB    1 ? 3 
ATOM   10540 C CG    . LEU C 1 412 ? 76.223  16.005  66.541  1.000 32.244  0 412 LEU CCC CG    1 ? 3 
ATOM   10541 C CD1   . LEU C 1 412 ? 77.122  16.690  65.541  1.000 33.706  0 412 LEU CCC CD1   1 ? 3 
ATOM   10542 C CD2   . LEU C 1 412 ? 75.979  16.917  67.732  1.000 32.305  0 412 LEU CCC CD2   1 ? 3 
ATOM   10543 N N     . GLU C 1 413 ? 75.310  12.613  65.746  1.000 33.841  0 413 GLU CCC N     1 ? 3 
ATOM   10544 C CA    . GLU C 1 413 ? 75.986  11.383  66.216  1.000 34.892  0 413 GLU CCC CA    1 ? 3 
ATOM   10545 C C     . GLU C 1 413 ? 76.192  10.453  65.039  1.000 33.523  0 413 GLU CCC C     1 ? 3 
ATOM   10546 O O     . GLU C 1 413 ? 77.275  9.854   64.893  1.000 35.243  0 413 GLU CCC O     1 ? 3 
ATOM   10547 C CB    . GLU C 1 413 ? 75.124  10.652  67.248  1.000 39.362  0 413 GLU CCC CB    1 ? 3 
ATOM   10548 C CG    . GLU C 1 413 ? 74.731  11.487  68.456  1.000 40.766  0 413 GLU CCC CG    1 ? 3 
ATOM   10549 C CD    . GLU C 1 413 ? 73.396  12.193  68.377  1.000 41.546  0 413 GLU CCC CD    1 ? 3 
ATOM   10550 O OE1   . GLU C 1 413 ? 73.221  12.986  67.445  1.000 43.622  0 413 GLU CCC OE1   1 ? 3 
ATOM   10551 O OE2   . GLU C 1 413 ? 72.533  11.947  69.258  1.000 45.560  0 413 GLU CCC OE2   1 ? 3 
ATOM   10552 N N     . ILE C 1 414 ? 75.165  10.303  64.226  1.000 33.212  0 414 ILE CCC N     1 ? 3 
ATOM   10553 C CA    . ILE C 1 414 ? 75.238  9.469   62.984  1.000 32.348  0 414 ILE CCC CA    1 ? 3 
ATOM   10554 C C     . ILE C 1 414 ? 76.254  10.096  62.031  1.000 30.722  0 414 ILE CCC C     1 ? 3 
ATOM   10555 O O     . ILE C 1 414 ? 77.073  9.350   61.494  1.000 30.332  0 414 ILE CCC O     1 ? 3 
ATOM   10556 C CB    . ILE C 1 414 ? 73.853  9.300   62.356  1.000 32.302  0 414 ILE CCC CB    1 ? 3 
ATOM   10557 C CG1   . ILE C 1 414 ? 72.827  8.890   63.429  1.000 33.020  0 414 ILE CCC CG1   1 ? 3 
ATOM   10558 C CG2   . ILE C 1 414 ? 73.904  8.322   61.198  1.000 31.777  0 414 ILE CCC CG2   1 ? 3 
ATOM   10559 C CD1   . ILE C 1 414 ? 73.033  7.528   64.012  1.000 33.416  0 414 ILE CCC CD1   1 ? 3 
ATOM   10560 N N     . ALA C 1 415 ? 76.231  11.411  61.847  1.000 29.757  0 415 ALA CCC N     1 ? 3 
ATOM   10561 C CA    . ALA C 1 415 ? 77.181  12.080  60.943  1.000 30.298  0 415 ALA CCC CA    1 ? 3 
ATOM   10562 C C     . ALA C 1 415 ? 78.613  11.721  61.374  1.000 29.287  0 415 ALA CCC C     1 ? 3 
ATOM   10563 O O     . ALA C 1 415 ? 79.401  11.405  60.517  1.000 28.823  0 415 ALA CCC O     1 ? 3 
ATOM   10564 C CB    . ALA C 1 415 ? 76.938  13.572  60.908  1.000 30.702  0 415 ALA CCC CB    1 ? 3 
ATOM   10565 N N     . ALA C 1 416 ? 78.926  11.750  62.669  1.000 29.938  0 416 ALA CCC N     1 ? 3 
ATOM   10566 C CA    . ALA C 1 416 ? 80.284  11.500  63.214  1.000 30.377  0 416 ALA CCC CA    1 ? 3 
ATOM   10567 C C     . ALA C 1 416 ? 80.680  10.009  63.080  1.000 31.342  0 416 ALA CCC C     1 ? 3 
ATOM   10568 O O     . ALA C 1 416 ? 81.904  9.682   63.058  1.000 29.842  0 416 ALA CCC O     1 ? 3 
ATOM   10569 C CB    . ALA C 1 416 ? 80.346  11.984  64.631  1.000 30.787  0 416 ALA CCC CB    1 ? 3 
ATOM   10570 N N     . ALA C 1 417 ? 79.703  9.116   62.962  1.000 32.057  0 417 ALA CCC N     1 ? 3 
ATOM   10571 C CA    . ALA C 1 417 ? 79.936  7.662   62.799  1.000 34.164  0 417 ALA CCC CA    1 ? 3 
ATOM   10572 C C     . ALA C 1 417 ? 80.388  7.321   61.369  1.000 35.116  0 417 ALA CCC C     1 ? 3 
ATOM   10573 O O     . ALA C 1 417 ? 81.041  6.296   61.204  1.000 37.199  0 417 ALA CCC O     1 ? 3 
ATOM   10574 C CB    . ALA C 1 417 ? 78.687  6.904   63.160  1.000 35.419  0 417 ALA CCC CB    1 ? 3 
ATOM   10575 N N     . HIS C 1 418 ? 80.043  8.126   60.362  1.000 35.671  0 418 HIS CCC N     1 ? 3 
ATOM   10576 C CA    . HIS C 1 418 ? 80.366  7.882   58.929  1.000 36.071  0 418 HIS CCC CA    1 ? 3 
ATOM   10577 C C     . HIS C 1 418 ? 79.810  6.510   58.545  1.000 34.763  0 418 HIS CCC C     1 ? 3 
ATOM   10578 O O     . HIS C 1 418 ? 80.604  5.654   58.122  1.000 35.347  0 418 HIS CCC O     1 ? 3 
ATOM   10579 C CB    . HIS C 1 418 ? 81.882  8.000   58.666  1.000 39.578  0 418 HIS CCC CB    1 ? 3 
ATOM   10580 C CG    . HIS C 1 418 ? 82.430  9.387   58.785  1.000 42.200  0 418 HIS CCC CG    1 ? 3 
ATOM   10581 N ND1   . HIS C 1 418 ? 82.335  10.309  57.772  1.000 45.674  0 418 HIS CCC ND1   1 ? 3 
ATOM   10582 C CD2   . HIS C 1 418 ? 83.062  10.032  59.796  1.000 45.359  0 418 HIS CCC CD2   1 ? 3 
ATOM   10583 C CE1   . HIS C 1 418 ? 82.880  11.462  58.148  1.000 45.041  0 418 HIS CCC CE1   1 ? 3 
ATOM   10584 N NE2   . HIS C 1 418 ? 83.335  11.316  59.376  1.000 45.725  0 418 HIS CCC NE2   1 ? 3 
ATOM   10585 N N     . ARG C 1 419 ? 78.492  6.312   58.708  1.000 32.604  0 419 ARG CCC N     1 ? 3 
ATOM   10586 C CA    . ARG C 1 419 ? 77.803  5.035   58.408  1.000 33.143  0 419 ARG CCC CA    1 ? 3 
ATOM   10587 C C     . ARG C 1 419 ? 77.958  4.698   56.907  1.000 34.808  0 419 ARG CCC C     1 ? 3 
ATOM   10588 O O     . ARG C 1 419 ? 77.701  5.589   56.051  1.000 31.817  0 419 ARG CCC O     1 ? 3 
ATOM   10589 C CB    . ARG C 1 419 ? 76.320  5.141   58.772  1.000 34.500  0 419 ARG CCC CB    1 ? 3 
ATOM   10590 C CG    . ARG C 1 419 ? 76.032  5.186   60.267  1.000 33.968  0 419 ARG CCC CG    1 ? 3 
ATOM   10591 C CD    . ARG C 1 419 ? 74.623  4.723   60.612  1.000 33.280  0 419 ARG CCC CD    1 ? 3 
ATOM   10592 N NE    . ARG C 1 419 ? 74.524  4.428   62.028  1.000 33.428  0 419 ARG CCC NE    1 ? 3 
ATOM   10593 C CZ    . ARG C 1 419 ? 73.433  3.980   62.655  1.000 32.268  0 419 ARG CCC CZ    1 ? 3 
ATOM   10594 N NH1   . ARG C 1 419 ? 72.324  3.777   61.965  1.000 32.064  0 419 ARG CCC NH1   1 ? 3 
ATOM   10595 N NH2   . ARG C 1 419 ? 73.483  3.733   63.956  1.000 28.616  0 419 ARG CCC NH2   1 ? 3 
ATOM   10596 N N     . GLU C 1 420 ? 78.362  3.467   56.599  1.000 36.558  0 420 GLU CCC N     1 ? 3 
ATOM   10597 C CA    . GLU C 1 420 ? 78.676  2.981   55.226  1.000 40.471  0 420 GLU CCC CA    1 ? 3 
ATOM   10598 C C     . GLU C 1 420 ? 77.669  1.909   54.788  1.000 39.657  0 420 GLU CCC C     1 ? 3 
ATOM   10599 O O     . GLU C 1 420 ? 77.247  1.083   55.648  1.000 36.022  0 420 GLU CCC O     1 ? 3 
ATOM   10600 C CB    . GLU C 1 420 ? 80.082  2.394   55.165  1.000 43.313  0 420 GLU CCC CB    1 ? 3 
ATOM   10601 C CG    . GLU C 1 420 ? 81.165  3.415   55.393  1.000 46.966  0 420 GLU CCC CG    1 ? 3 
ATOM   10602 C CD    . GLU C 1 420 ? 82.526  3.019   54.867  1.000 49.523  0 420 GLU CCC CD    1 ? 3 
ATOM   10603 O OE1   . GLU C 1 420 ? 82.597  2.511   53.694  1.000 52.323  0 420 GLU CCC OE1   1 ? 3 
ATOM   10604 O OE2   . GLU C 1 420 ? 83.503  3.283   55.605  1.000 52.251  0 420 GLU CCC OE2   1 ? 3 
ATOM   10605 N N     . LYS C 1 421 ? 77.324  1.937   53.497  1.000 38.555  0 421 LYS CCC N     1 ? 3 
ATOM   10606 C CA    . LYS C 1 421 ? 76.658  0.834   52.760  1.000 40.411  0 421 LYS CCC CA    1 ? 3 
ATOM   10607 C C     . LYS C 1 421 ? 77.399  -0.476  53.006  1.000 40.574  0 421 LYS CCC C     1 ? 3 
ATOM   10608 O O     . LYS C 1 421 ? 78.623  -0.482  53.090  1.000 38.072  0 421 LYS CCC O     1 ? 3 
ATOM   10609 C CB    . LYS C 1 421 ? 76.679  1.102   51.253  1.000 43.288  0 421 LYS CCC CB    1 ? 3 
ATOM   10610 C CG    . LYS C 1 421 ? 75.662  2.129   50.788  1.000 45.291  0 421 LYS CCC CG    1 ? 3 
ATOM   10611 C CD    . LYS C 1 421 ? 75.308  2.138   49.321  1.000 47.796  0 421 LYS CCC CD    1 ? 3 
ATOM   10612 C CE    . LYS C 1 421 ? 74.353  3.290   49.109  1.000 49.413  0 421 LYS CCC CE    1 ? 3 
ATOM   10613 N NZ    . LYS C 1 421 ? 74.150  3.567   47.678  1.000 51.254  0 421 LYS CCC NZ    1 ? 3 
ATOM   10614 N N     . PRO C 1 422 ? 76.691  -1.624  53.106  1.000 43.524  0 422 PRO CCC N     1 ? 3 
ATOM   10615 C CA    . PRO C 1 422 ? 77.345  -2.934  53.080  1.000 46.708  0 422 PRO CCC CA    1 ? 3 
ATOM   10616 C C     . PRO C 1 422 ? 78.110  -3.065  51.755  1.000 47.133  0 422 PRO CCC C     1 ? 3 
ATOM   10617 O O     . PRO C 1 422 ? 77.659  -2.498  50.778  1.000 44.941  0 422 PRO CCC O     1 ? 3 
ATOM   10618 C CB    . PRO C 1 422 ? 76.206  -3.959  53.189  1.000 46.595  0 422 PRO CCC CB    1 ? 3 
ATOM   10619 C CG    . PRO C 1 422 ? 75.051  -3.149  53.759  1.000 46.818  0 422 PRO CCC CG    1 ? 3 
ATOM   10620 C CD    . PRO C 1 422 ? 75.236  -1.737  53.222  1.000 45.611  0 422 PRO CCC CD    1 ? 3 
ATOM   10621 N N     . GLU C 1 423 ? 79.239  -3.769  51.750  1.000 51.494  0 423 GLU CCC N     1 ? 3 
ATOM   10622 C CA    . GLU C 1 423 ? 80.232  -3.739  50.638  1.000 57.720  0 423 GLU CCC CA    1 ? 3 
ATOM   10623 C C     . GLU C 1 423 ? 79.620  -4.372  49.382  1.000 56.945  0 423 GLU CCC C     1 ? 3 
ATOM   10624 O O     . GLU C 1 423 ? 80.016  -4.002  48.267  1.000 57.785  0 423 GLU CCC O     1 ? 3 
ATOM   10625 C CB    . GLU C 1 423 ? 81.509  -4.445  51.100  1.000 63.440  0 423 GLU CCC CB    1 ? 3 
ATOM   10626 C CG    . GLU C 1 423 ? 82.610  -4.545  50.056  1.000 70.152  0 423 GLU CCC CG    1 ? 3 
ATOM   10627 C CD    . GLU C 1 423 ? 83.993  -4.840  50.628  1.000 77.305  0 423 GLU CCC CD    1 ? 3 
ATOM   10628 O OE1   . GLU C 1 423 ? 84.340  -4.259  51.689  1.000 77.535  0 423 GLU CCC OE1   1 ? 3 
ATOM   10629 O OE2   . GLU C 1 423 ? 84.736  -5.644  50.011  1.000 83.248  0 423 GLU CCC OE2   1 ? 3 
ATOM   10630 N N     . HIS C 1 424 ? 78.624  -5.248  49.549  1.000 58.641  0 424 HIS CCC N     1 ? 3 
ATOM   10631 C CA    . HIS C 1 424 ? 77.969  -5.958  48.417  1.000 59.365  0 424 HIS CCC CA    1 ? 3 
ATOM   10632 C C     . HIS C 1 424 ? 77.039  -5.023  47.637  1.000 56.934  0 424 HIS CCC C     1 ? 3 
ATOM   10633 O O     . HIS C 1 424 ? 76.613  -5.459  46.550  1.000 57.407  0 424 HIS CCC O     1 ? 3 
ATOM   10634 C CB    . HIS C 1 424 ? 77.281  -7.259  48.864  1.000 63.538  0 424 HIS CCC CB    1 ? 3 
ATOM   10635 C CG    . HIS C 1 424 ? 76.141  -7.110  49.816  1.000 63.864  0 424 HIS CCC CG    1 ? 3 
ATOM   10636 N ND1   . HIS C 1 424 ? 74.853  -6.832  49.379  1.000 64.317  0 424 HIS CCC ND1   1 ? 3 
ATOM   10637 C CD2   . HIS C 1 424 ? 76.084  -7.240  51.167  1.000 65.445  0 424 HIS CCC CD2   1 ? 3 
ATOM   10638 C CE1   . HIS C 1 424 ? 74.047  -6.760  50.425  1.000 67.397  0 424 HIS CCC CE1   1 ? 3 
ATOM   10639 N NE2   . HIS C 1 424 ? 74.785  -7.013  51.548  1.000 67.463  0 424 HIS CCC NE2   1 ? 3 
ATOM   10640 N N     . LEU C 1 425 ? 76.765  -3.794  48.101  1.000 52.736  0 425 LEU CCC N     1 ? 3 
ATOM   10641 C CA    . LEU C 1 425 ? 75.862  -2.842  47.394  1.000 53.867  0 425 LEU CCC CA    1 ? 3 
ATOM   10642 C C     . LEU C 1 425 ? 76.622  -1.639  46.829  1.000 53.509  0 425 LEU CCC C     1 ? 3 
ATOM   10643 O O     . LEU C 1 425 ? 75.945  -0.755  46.248  1.000 53.137  0 425 LEU CCC O     1 ? 3 
ATOM   10644 C CB    . LEU C 1 425 ? 74.772  -2.380  48.360  1.000 54.567  0 425 LEU CCC CB    1 ? 3 
ATOM   10645 C CG    . LEU C 1 425 ? 73.767  -3.459  48.757  1.000 56.704  0 425 LEU CCC CG    1 ? 3 
ATOM   10646 C CD1   . LEU C 1 425 ? 73.040  -3.041  50.030  1.000 55.251  0 425 LEU CCC CD1   1 ? 3 
ATOM   10647 C CD2   . LEU C 1 425 ? 72.802  -3.740  47.608  1.000 58.927  0 425 LEU CCC CD2   1 ? 3 
ATOM   10648 N N     . ARG C 1 426 ? 77.949  -1.601  46.988  1.000 55.908  0 426 ARG CCC N     1 ? 3 
ATOM   10649 C CA    . ARG C 1 426 ? 78.803  -0.470  46.534  1.000 56.943  0 426 ARG CCC CA    1 ? 3 
ATOM   10650 C C     . ARG C 1 426 ? 78.903  -0.468  45.001  1.000 62.316  0 426 ARG CCC C     1 ? 3 
ATOM   10651 O O     . ARG C 1 426 ? 79.149  -1.551  44.446  1.000 61.267  0 426 ARG CCC O     1 ? 3 
ATOM   10652 C CB    . ARG C 1 426 ? 80.183  -0.580  47.184  1.000 55.680  0 426 ARG CCC CB    1 ? 3 
ATOM   10653 C CG    . ARG C 1 426 ? 80.210  -0.269  48.676  1.000 52.209  0 426 ARG CCC CG    1 ? 3 
ATOM   10654 C CD    . ARG C 1 426 ? 80.016  1.218   48.939  1.000 50.844  0 426 ARG CCC CD    1 ? 3 
ATOM   10655 N NE    . ARG C 1 426 ? 80.993  2.046   48.233  1.000 51.353  0 426 ARG CCC NE    1 ? 3 
ATOM   10656 C CZ    . ARG C 1 426 ? 82.224  2.329   48.669  1.000 49.875  0 426 ARG CCC CZ    1 ? 3 
ATOM   10657 N NH1   . ARG C 1 426 ? 82.641  1.859   49.838  1.000 48.526  0 426 ARG CCC NH1   1 ? 3 
ATOM   10658 N NH2   . ARG C 1 426 ? 83.026  3.123   47.952  1.000 50.217  0 426 ARG CCC NH2   1 ? 3 
ATOM   10659 N N     . GLU C 1 427 ? 78.708  0.695   44.356  1.000 69.625  0 427 GLU CCC N     1 ? 3 
ATOM   10660 C CA    . GLU C 1 427 ? 78.704  0.889   42.872  1.000 72.990  0 427 GLU CCC CA    1 ? 3 
ATOM   10661 C C     . GLU C 1 427 ? 79.992  1.598   42.404  1.000 75.649  0 427 GLU CCC C     1 ? 3 
ATOM   10662 O O     . GLU C 1 427 ? 80.300  1.465   41.206  1.000 79.719  0 427 GLU CCC O     1 ? 3 
ATOM   10663 C CB    . GLU C 1 427 ? 77.479  1.697   42.422  1.000 74.121  0 427 GLU CCC CB    1 ? 3 
ATOM   10664 C CG    . GLU C 1 427 ? 76.395  0.896   41.694  1.000 77.114  0 427 GLU CCC CG    1 ? 3 
ATOM   10665 C CD    . GLU C 1 427 ? 75.233  1.700   41.100  1.000 76.203  0 427 GLU CCC CD    1 ? 3 
ATOM   10666 O OE1   . GLU C 1 427 ? 74.087  1.389   41.465  1.000 78.730  0 427 GLU CCC OE1   1 ? 3 
ATOM   10667 O OE2   . GLU C 1 427 ? 75.453  2.628   40.265  1.000 70.324  0 427 GLU CCC OE2   1 ? 3 
ATOM   10668 N N     . ASN C 1 428 ? 80.715  2.316   43.276  1.000 73.083  0 428 ASN CCC N     1 ? 3 
ATOM   10669 C CA    . ASN C 1 428 ? 81.922  3.090   42.875  1.000 76.055  0 428 ASN CCC CA    1 ? 3 
ATOM   10670 C C     . ASN C 1 428 ? 82.702  3.534   44.119  1.000 74.391  0 428 ASN CCC C     1 ? 3 
ATOM   10671 O O     . ASN C 1 428 ? 82.492  2.938   45.180  1.000 70.110  0 428 ASN CCC O     1 ? 3 
ATOM   10672 C CB    . ASN C 1 428 ? 81.553  4.277   41.977  1.000 80.703  0 428 ASN CCC CB    1 ? 3 
ATOM   10673 C CG    . ASN C 1 428 ? 80.455  5.147   42.555  1.000 79.190  0 428 ASN CCC CG    1 ? 3 
ATOM   10674 O OD1   . ASN C 1 428 ? 80.563  5.650   43.665  1.000 81.364  0 428 ASN CCC OD1   1 ? 3 
ATOM   10675 N ND2   . ASN C 1 428 ? 79.392  5.347   41.801  1.000 78.648  0 428 ASN CCC ND2   1 ? 3 
ATOM   10676 N N     . GLU C 1 429 ? 83.565  4.547   43.991  1.000 73.089  0 429 GLU CCC N     1 ? 3 
ATOM   10677 C CA    . GLU C 1 429 ? 84.440  5.048   45.089  1.000 73.520  0 429 GLU CCC CA    1 ? 3 
ATOM   10678 C C     . GLU C 1 429 ? 83.795  6.256   45.790  1.000 70.563  0 429 GLU CCC C     1 ? 3 
ATOM   10679 O O     . GLU C 1 429 ? 84.427  6.782   46.716  1.000 71.171  0 429 GLU CCC O     1 ? 3 
ATOM   10680 C CB    . GLU C 1 429 ? 85.827  5.441   44.555  1.000 73.644  0 429 GLU CCC CB    1 ? 3 
ATOM   10681 C CG    . GLU C 1 429 ? 86.454  4.401   43.642  1.000 73.999  0 429 GLU CCC CG    1 ? 3 
ATOM   10682 C CD    . GLU C 1 429 ? 86.312  2.965   44.111  1.000 71.640  0 429 GLU CCC CD    1 ? 3 
ATOM   10683 O OE1   . GLU C 1 429 ? 86.672  2.704   45.280  1.000 68.183  0 429 GLU CCC OE1   1 ? 3 
ATOM   10684 O OE2   . GLU C 1 429 ? 85.827  2.121   43.315  1.000 68.853  0 429 GLU CCC OE2   1 ? 3 
ATOM   10685 N N     . MET C 1 430 ? 82.592  6.673   45.381  1.000 69.583  0 430 MET CCC N     1 ? 3 
ATOM   10686 C CA    . MET C 1 430 ? 81.842  7.833   45.936  1.000 69.200  0 430 MET CCC CA    1 ? 3 
ATOM   10687 C C     . MET C 1 430 ? 80.442  7.400   46.428  1.000 63.978  0 430 MET CCC C     1 ? 3 
ATOM   10688 O O     . MET C 1 430 ? 79.644  8.295   46.798  1.000 62.732  0 430 MET CCC O     1 ? 3 
ATOM   10689 C CB    . MET C 1 430 ? 81.676  8.918   44.861  1.000 74.760  0 430 MET CCC CB    1 ? 3 
ATOM   10690 C CG    . MET C 1 430 ? 82.669  10.064  44.918  1.000 77.659  0 430 MET CCC CG    1 ? 3 
ATOM   10691 S SD    . MET C 1 430 ? 82.982  10.834  46.540  1.000 79.805  0 430 MET CCC SD    1 ? 3 
ATOM   10692 C CE    . MET C 1 430 ? 81.291  11.135  47.066  1.000 84.494  0 430 MET CCC CE    1 ? 3 
ATOM   10693 N N     . ASP C 1 431 ? 80.166  6.091   46.469  1.000 56.582  0 431 ASP CCC N     1 ? 3 
ATOM   10694 C CA    . ASP C 1 431 ? 78.857  5.518   46.867  1.000 54.732  0 431 ASP CCC CA    1 ? 3 
ATOM   10695 C C     . ASP C 1 431 ? 78.887  4.945   48.304  1.000 49.725  0 431 ASP CCC C     1 ? 3 
ATOM   10696 O O     . ASP C 1 431 ? 78.089  4.073   48.615  1.000 47.455  0 431 ASP CCC O     1 ? 3 
ATOM   10697 C CB    . ASP C 1 431 ? 78.534  4.472   45.809  1.000 58.359  0 431 ASP CCC CB    1 ? 3 
ATOM   10698 C CG    . ASP C 1 431 ? 77.327  3.622   46.061  1.000 64.187  0 431 ASP CCC CG    1 ? 3 
ATOM   10699 O OD1   . ASP C 1 431 ? 76.297  4.180   46.527  1.000 64.833  0 431 ASP CCC OD1   1 ? 3 
ATOM   10700 O OD2   . ASP C 1 431 ? 77.430  2.423   45.754  1.000 69.076  0 431 ASP CCC OD2   1 ? 3 
ATOM   10701 N N     . PHE C 1 432 ? 79.799  5.422   49.152  1.000 44.776  0 432 PHE CCC N     1 ? 3 
ATOM   10702 C CA    . PHE C 1 432 ? 80.230  4.742   50.402  1.000 42.818  0 432 PHE CCC CA    1 ? 3 
ATOM   10703 C C     . PHE C 1 432 ? 79.157  4.949   51.489  1.000 41.342  0 432 PHE CCC C     1 ? 3 
ATOM   10704 O O     . PHE C 1 432 ? 78.892  3.997   52.240  1.000 41.718  0 432 PHE CCC O     1 ? 3 
ATOM   10705 C CB    . PHE C 1 432 ? 81.621  5.237   50.841  1.000 42.118  0 432 PHE CCC CB    1 ? 3 
ATOM   10706 C CG    . PHE C 1 432 ? 81.819  6.740   50.859  1.000 42.997  0 432 PHE CCC CG    1 ? 3 
ATOM   10707 C CD1   . PHE C 1 432 ? 81.504  7.492   51.985  1.000 41.514  0 432 PHE CCC CD1   1 ? 3 
ATOM   10708 C CD2   . PHE C 1 432 ? 82.332  7.413   49.750  1.000 45.483  0 432 PHE CCC CD2   1 ? 3 
ATOM   10709 C CE1   . PHE C 1 432 ? 81.661  8.874   51.990  1.000 42.123  0 432 PHE CCC CE1   1 ? 3 
ATOM   10710 C CE2   . PHE C 1 432 ? 82.494  8.796   49.758  1.000 44.904  0 432 PHE CCC CE2   1 ? 3 
ATOM   10711 C CZ    . PHE C 1 432 ? 82.149  9.528   50.876  1.000 43.272  0 432 PHE CCC CZ    1 ? 3 
ATOM   10712 N N     . ALA C 1 433 ? 78.573  6.148   51.553  1.000 39.398  0 433 ALA CCC N     1 ? 3 
ATOM   10713 C CA    . ALA C 1 433 ? 77.708  6.645   52.651  1.000 38.289  0 433 ALA CCC CA    1 ? 3 
ATOM   10714 C C     . ALA C 1 433 ? 76.316  6.033   52.545  1.000 37.594  0 433 ALA CCC C     1 ? 3 
ATOM   10715 O O     . ALA C 1 433 ? 75.816  5.831   51.434  1.000 40.278  0 433 ALA CCC O     1 ? 3 
ATOM   10716 C CB    . ALA C 1 433 ? 77.577  8.153   52.623  1.000 37.734  0 433 ALA CCC CB    1 ? 3 
ATOM   10717 N N     . LEU C 1 434 ? 75.695  5.764   53.679  1.000 35.247  0 434 LEU CCC N     1 ? 3 
ATOM   10718 C CA    . LEU C 1 434 ? 74.222  5.670   53.802  1.000 34.612  0 434 LEU CCC CA    1 ? 3 
ATOM   10719 C C     . LEU C 1 434 ? 73.611  7.020   53.463  1.000 33.439  0 434 LEU CCC C     1 ? 3 
ATOM   10720 O O     . LEU C 1 434 ? 74.222  8.052   53.686  1.000 31.836  0 434 LEU CCC O     1 ? 3 
ATOM   10721 C CB    . LEU C 1 434 ? 73.856  5.279   55.228  1.000 34.793  0 434 LEU CCC CB    1 ? 3 
ATOM   10722 C CG    . LEU C 1 434 ? 74.277  3.883   55.659  1.000 35.796  0 434 LEU CCC CG    1 ? 3 
ATOM   10723 C CD1   . LEU C 1 434 ? 73.604  3.557   57.002  1.000 37.758  0 434 LEU CCC CD1   1 ? 3 
ATOM   10724 C CD2   . LEU C 1 434 ? 73.918  2.851   54.591  1.000 36.701  0 434 LEU CCC CD2   1 ? 3 
ATOM   10725 N N     . PRO C 1 435 ? 72.379  7.063   52.925  1.000 34.327  0 435 PRO CCC N     1 ? 3 
ATOM   10726 C CA    . PRO C 1 435 ? 71.671  8.330   52.780  1.000 34.387  0 435 PRO CCC CA    1 ? 3 
ATOM   10727 C C     . PRO C 1 435 ? 71.609  9.090   54.110  1.000 33.611  0 435 PRO CCC C     1 ? 3 
ATOM   10728 O O     . PRO C 1 435 ? 71.638  8.497   55.200  1.000 31.054  0 435 PRO CCC O     1 ? 3 
ATOM   10729 C CB    . PRO C 1 435 ? 70.243  7.901   52.386  1.000 33.982  0 435 PRO CCC CB    1 ? 3 
ATOM   10730 C CG    . PRO C 1 435 ? 70.414  6.532   51.746  1.000 34.803  0 435 PRO CCC CG    1 ? 3 
ATOM   10731 C CD    . PRO C 1 435 ? 71.614  5.903   52.443  1.000 34.623  0 435 PRO CCC CD    1 ? 3 
ATOM   10732 N N     . LEU C 1 436 ? 71.505  10.407  54.010  1.000 34.792  0 436 LEU CCC N     1 ? 3 
ATOM   10733 C CA    . LEU C 1 436 ? 71.177  11.277  55.163  1.000 31.959  0 436 LEU CCC CA    1 ? 3 
ATOM   10734 C C     . LEU C 1 436 ? 69.960  10.642  55.870  1.000 29.885  0 436 LEU CCC C     1 ? 3 
ATOM   10735 O O     . LEU C 1 436 ? 69.035  10.206  55.200  1.000 28.716  0 436 LEU CCC O     1 ? 3 
ATOM   10736 C CB    . LEU C 1 436 ? 70.877  12.688  54.646  1.000 32.651  0 436 LEU CCC CB    1 ? 3 
ATOM   10737 C CG    . LEU C 1 436 ? 72.008  13.361  53.868  1.000 33.728  0 436 LEU CCC CG    1 ? 3 
ATOM   10738 C CD1   . LEU C 1 436 ? 71.481  14.583  53.115  1.000 34.241  0 436 LEU CCC CD1   1 ? 3 
ATOM   10739 C CD2   . LEU C 1 436 ? 73.162  13.747  54.798  1.000 33.619  0 436 LEU CCC CD2   1 ? 3 
ATOM   10740 N N     . ASN C 1 437 ? 69.976  10.562  57.197  1.000 27.418  0 437 ASN CCC N     1 ? 3 
ATOM   10741 C CA    . ASN C 1 437 ? 69.026  9.722   57.940  1.000 26.741  0 437 ASN CCC CA    1 ? 3 
ATOM   10742 C C     . ASN C 1 437 ? 67.731  10.516  58.170  1.000 26.242  0 437 ASN CCC C     1 ? 3 
ATOM   10743 O O     . ASN C 1 437 ? 66.744  9.844   58.482  1.000 25.423  0 437 ASN CCC O     1 ? 3 
ATOM   10744 C CB    . ASN C 1 437 ? 69.678  9.132   59.191  1.000 26.695  0 437 ASN CCC CB    1 ? 3 
ATOM   10745 C CG    . ASN C 1 437 ? 69.981  10.152  60.264  1.000 27.538  0 437 ASN CCC CG    1 ? 3 
ATOM   10746 O OD1   . ASN C 1 437 ? 70.350  11.288  59.970  1.000 27.514  0 437 ASN CCC OD1   1 ? 3 
ATOM   10747 N ND2   . ASN C 1 437 ? 69.802  9.754   61.519  1.000 29.051  0 437 ASN CCC ND2   1 ? 3 
ATOM   10748 N N     . CYS C 1 438 ? 67.737  11.854  58.058  1.000 26.031  0 438 CYS CCC N     1 ? 3 
ATOM   10749 C CA    . CYS C 1 438 ? 66.622  12.723  58.479  1.000 26.301  0 438 CYS CCC CA    1 ? 3 
ATOM   10750 C C     . CYS C 1 438 ? 66.047  13.528  57.317  1.000 28.520  0 438 CYS CCC C     1 ? 3 
ATOM   10751 O O     . CYS C 1 438 ? 66.806  14.013  56.461  1.000 27.751  0 438 CYS CCC O     1 ? 3 
ATOM   10752 C CB    . CYS C 1 438 ? 67.001  13.723  59.545  1.000 26.067  0 438 CYS CCC CB    1 ? 3 
ATOM   10753 S SG    . CYS C 1 438 ? 67.506  12.917  61.078  1.000 26.492  0 438 CYS CCC SG    1 ? 3 
ATOM   10754 N N     . LEU C 1 439 ? 64.719  13.711  57.387  1.000 28.950  0 439 LEU CCC N     1 ? 3 
ATOM   10755 C CA    . LEU C 1 439 ? 63.968  14.642  56.533  1.000 29.133  0 439 LEU CCC CA    1 ? 3 
ATOM   10756 C C     . LEU C 1 439 ? 62.867  15.299  57.335  1.000 28.424  0 439 LEU CCC C     1 ? 3 
ATOM   10757 O O     . LEU C 1 439 ? 61.998  14.581  57.842  1.000 29.084  0 439 LEU CCC O     1 ? 3 
ATOM   10758 C CB    . LEU C 1 439 ? 63.357  13.861  55.375  1.000 30.346  0 439 LEU CCC CB    1 ? 3 
ATOM   10759 C CG    . LEU C 1 439 ? 62.545  14.702  54.408  1.000 30.336  0 439 LEU CCC CG    1 ? 3 
ATOM   10760 C CD1   . LEU C 1 439 ? 63.465  15.655  53.671  1.000 31.334  0 439 LEU CCC CD1   1 ? 3 
ATOM   10761 C CD2   . LEU C 1 439 ? 61.790  13.788  53.469  1.000 30.695  0 439 LEU CCC CD2   1 ? 3 
ATOM   10762 N N     . ALA C 1 440 ? 62.886  16.622  57.383  1.000 29.280  0 440 ALA CCC N     1 ? 3 
ATOM   10763 C CA    . ALA C 1 440 ? 61.887  17.454  58.083  1.000 29.413  0 440 ALA CCC CA    1 ? 3 
ATOM   10764 C C     . ALA C 1 440 ? 61.088  18.222  57.041  1.000 31.349  0 440 ALA CCC C     1 ? 3 
ATOM   10765 O O     . ALA C 1 440 ? 61.718  18.812  56.147  1.000 30.369  0 440 ALA CCC O     1 ? 3 
ATOM   10766 C CB    . ALA C 1 440 ? 62.553  18.391  59.024  1.000 29.864  0 440 ALA CCC CB    1 ? 3 
ATOM   10767 N N     . LYS C 1 441 ? 59.752  18.206  57.146  1.000 31.387  0 441 LYS CCC N     1 ? 3 
ATOM   10768 C CA    . LYS C 1 441 ? 58.878  18.936  56.219  1.000 32.479  0 441 LYS CCC CA    1 ? 3 
ATOM   10769 C C     . LYS C 1 441 ? 57.650  19.481  56.942  1.000 33.924  0 441 LYS CCC C     1 ? 3 
ATOM   10770 O O     . LYS C 1 441 ? 56.942  18.678  57.624  1.000 33.598  0 441 LYS CCC O     1 ? 3 
ATOM   10771 C CB    . LYS C 1 441 ? 58.436  17.993  55.105  1.000 33.695  0 441 LYS CCC CB    1 ? 3 
ATOM   10772 C CG    . LYS C 1 441 ? 57.453  18.619  54.125  1.000 35.133  0 441 LYS CCC CG    1 ? 3 
ATOM   10773 C CD    . LYS C 1 441 ? 57.478  17.946  52.793  1.000 36.101  0 441 LYS CCC CD    1 ? 3 
ATOM   10774 C CE    . LYS C 1 441 ? 56.788  16.604  52.807  1.000 39.807  0 441 LYS CCC CE    1 ? 3 
ATOM   10775 N NZ    . LYS C 1 441 ? 56.814  15.967  51.464  1.000 43.010  0 441 LYS CCC NZ    1 ? 3 
ATOM   10776 N N     . LEU C 1 442 ? 57.376  20.768  56.731  1.000 35.234  0 442 LEU CCC N     1 ? 3 
ATOM   10777 C CA    . LEU C 1 442 ? 56.081  21.431  57.046  1.000 34.868  0 442 LEU CCC CA    1 ? 3 
ATOM   10778 C C     . LEU C 1 442 ? 55.328  21.756  55.758  1.000 37.759  0 442 LEU CCC C     1 ? 3 
ATOM   10779 O O     . LEU C 1 442 ? 55.916  22.285  54.795  1.000 34.248  0 442 LEU CCC O     1 ? 3 
ATOM   10780 C CB    . LEU C 1 442 ? 56.310  22.720  57.833  1.000 34.434  0 442 LEU CCC CB    1 ? 3 
ATOM   10781 C CG    . LEU C 1 442 ? 57.015  22.549  59.171  1.000 32.859  0 442 LEU CCC CG    1 ? 3 
ATOM   10782 C CD1   . LEU C 1 442 ? 57.368  23.910  59.745  1.000 33.377  0 442 LEU CCC CD1   1 ? 3 
ATOM   10783 C CD2   . LEU C 1 442 ? 56.153  21.752  60.118  1.000 31.329  0 442 LEU CCC CD2   1 ? 3 
ATOM   10784 N N     . VAL C 1 443 ? 54.031  21.477  55.779  1.000 40.613  0 443 VAL CCC N     1 ? 3 
ATOM   10785 C CA    . VAL C 1 443 ? 53.096  21.820  54.684  1.000 44.076  0 443 VAL CCC CA    1 ? 3 
ATOM   10786 C C     . VAL C 1 443 ? 52.168  22.892  55.246  1.000 45.936  0 443 VAL CCC C     1 ? 3 
ATOM   10787 O O     . VAL C 1 443 ? 51.516  22.615  56.286  1.000 49.021  0 443 VAL CCC O     1 ? 3 
ATOM   10788 C CB    . VAL C 1 443 ? 52.379  20.546  54.202  1.000 44.268  0 443 VAL CCC CB    1 ? 3 
ATOM   10789 C CG1   . VAL C 1 443 ? 51.465  20.822  53.032  1.000 42.883  0 443 VAL CCC CG1   1 ? 3 
ATOM   10790 C CG2   . VAL C 1 443 ? 53.387  19.455  53.847  1.000 44.152  0 443 VAL CCC CG2   1 ? 3 
ATOM   10791 N N     . VAL C 1 444 ? 52.172  24.075  54.626  1.000 47.193  0 444 VAL CCC N     1 ? 3 
ATOM   10792 C CA    . VAL C 1 444 ? 51.462  25.293  55.117  1.000 48.668  0 444 VAL CCC CA    1 ? 3 
ATOM   10793 C C     . VAL C 1 444 ? 50.538  25.871  54.027  1.000 47.270  0 444 VAL CCC C     1 ? 3 
ATOM   10794 O O     . VAL C 1 444 ? 50.843  25.750  52.836  1.000 46.730  0 444 VAL CCC O     1 ? 3 
ATOM   10795 C CB    . VAL C 1 444 ? 52.469  26.343  55.634  1.000 49.159  0 444 VAL CCC CB    1 ? 3 
ATOM   10796 C CG1   . VAL C 1 444 ? 53.460  25.728  56.592  1.000 49.092  0 444 VAL CCC CG1   1 ? 3 
ATOM   10797 C CG2   . VAL C 1 444 ? 53.204  27.065  54.517  1.000 49.311  0 444 VAL CCC CG2   1 ? 3 
ATOM   10798 N N     . VAL C 1 445 ? 49.448  26.491  54.460  1.000 47.705  0 445 VAL CCC N     1 ? 3 
ATOM   10799 C CA    . VAL C 1 445 ? 48.447  27.193  53.609  1.000 49.675  0 445 VAL CCC CA    1 ? 3 
ATOM   10800 C C     . VAL C 1 445 ? 48.734  28.701  53.656  1.000 50.091  0 445 VAL CCC C     1 ? 3 
ATOM   10801 O O     . VAL C 1 445 ? 48.632  29.321  54.738  1.000 48.648  0 445 VAL CCC O     1 ? 3 
ATOM   10802 C CB    . VAL C 1 445 ? 47.010  26.878  54.063  1.000 48.294  0 445 VAL CCC CB    1 ? 3 
ATOM   10803 C CG1   . VAL C 1 445 ? 45.992  27.620  53.220  1.000 50.066  0 445 VAL CCC CG1   1 ? 3 
ATOM   10804 C CG2   . VAL C 1 445 ? 46.734  25.391  54.036  1.000 46.797  0 445 VAL CCC CG2   1 ? 3 
ATOM   10805 N N     . LYS C 1 446 ? 49.062  29.268  52.501  1.000 51.398  0 446 LYS CCC N     1 ? 3 
ATOM   10806 C CA    . LYS C 1 446 ? 49.437  30.696  52.350  1.000 54.613  0 446 LYS CCC CA    1 ? 3 
ATOM   10807 C C     . LYS C 1 446 ? 48.267  31.600  52.739  1.000 54.265  0 446 LYS CCC C     1 ? 3 
ATOM   10808 O O     . LYS C 1 446 ? 48.517  32.556  53.482  1.000 55.530  0 446 LYS CCC O     1 ? 3 
ATOM   10809 C CB    . LYS C 1 446 ? 49.923  30.936  50.927  1.000 57.461  0 446 LYS CCC CB    1 ? 3 
ATOM   10810 C CG    . LYS C 1 446 ? 51.144  30.098  50.584  1.000 60.043  0 446 LYS CCC CG    1 ? 3 
ATOM   10811 C CD    . LYS C 1 446 ? 52.208  30.867  49.892  1.000 64.703  0 446 LYS CCC CD    1 ? 3 
ATOM   10812 C CE    . LYS C 1 446 ? 51.990  30.975  48.403  1.000 69.444  0 446 LYS CCC CE    1 ? 3 
ATOM   10813 N NZ    . LYS C 1 446 ? 53.199  31.534  47.753  1.000 72.247  0 446 LYS CCC NZ    1 ? 3 
ATOM   10814 N N     . SER C 1 447 ? 47.044  31.278  52.321  1.000 53.676  0 447 SER CCC N     1 ? 3 
ATOM   10815 C CA    . SER C 1 447 ? 45.845  32.127  52.534  1.000 53.717  0 447 SER CCC CA    1 ? 3 
ATOM   10816 C C     . SER C 1 447 ? 45.437  32.137  54.011  1.000 54.425  0 447 SER CCC C     1 ? 3 
ATOM   10817 O O     . SER C 1 447 ? 44.433  32.794  54.312  1.000 55.523  0 447 SER CCC O     1 ? 3 
ATOM   10818 C CB    . SER C 1 447 ? 44.691  31.700  51.639  1.000 52.469  0 447 SER CCC CB    1 ? 3 
ATOM   10819 O OG    . SER C 1 447 ? 44.302  30.367  51.904  1.000 48.737  0 447 SER CCC OG    1 ? 3 
ATOM   10820 N N     . GLN C 1 448 ? 46.167  31.450  54.898  1.000 54.586  0 448 GLN CCC N     1 ? 3 
ATOM   10821 C CA    . GLN C 1 448 ? 45.872  31.453  56.362  1.000 55.498  0 448 GLN CCC CA    1 ? 3 
ATOM   10822 C C     . GLN C 1 448 ? 47.140  31.790  57.157  1.000 54.514  0 448 GLN CCC C     1 ? 3 
ATOM   10823 O O     . GLN C 1 448 ? 47.322  31.227  58.255  1.000 52.608  0 448 GLN CCC O     1 ? 3 
ATOM   10824 C CB    . GLN C 1 448 ? 45.269  30.111  56.784  1.000 55.299  0 448 GLN CCC CB    1 ? 3 
ATOM   10825 C CG    . GLN C 1 448 ? 44.002  29.776  56.004  1.000 56.041  0 448 GLN CCC CG    1 ? 3 
ATOM   10826 C CD    . GLN C 1 448 ? 43.447  28.423  56.358  1.000 55.012  0 448 GLN CCC CD    1 ? 3 
ATOM   10827 O OE1   . GLN C 1 448 ? 43.494  28.000  57.508  1.000 54.461  0 448 GLN CCC OE1   1 ? 3 
ATOM   10828 N NE2   . GLN C 1 448 ? 42.940  27.726  55.358  1.000 55.707  0 448 GLN CCC NE2   1 ? 3 
ATOM   10829 N N     . GLY C 1 449 ? 47.940  32.725  56.641  1.000 55.665  0 449 GLY CCC N     1 ? 3 
ATOM   10830 C CA    . GLY C 1 449 ? 49.197  33.186  57.257  1.000 58.400  0 449 GLY CCC CA    1 ? 3 
ATOM   10831 C C     . GLY C 1 449 ? 50.171  32.040  57.450  1.000 58.919  0 449 GLY CCC C     1 ? 3 
ATOM   10832 O O     . GLY C 1 449 ? 50.774  31.974  58.525  1.000 62.057  0 449 GLY CCC O     1 ? 3 
ATOM   10833 N N     . GLU C 1 450 ? 50.277  31.158  56.449  1.000 58.963  0 450 GLU CCC N     1 ? 3 
ATOM   10834 C CA    . GLU C 1 450 ? 51.111  29.921  56.442  1.000 57.104  0 450 GLU CCC CA    1 ? 3 
ATOM   10835 C C     . GLU C 1 450 ? 50.751  29.016  57.634  1.000 53.882  0 450 GLU CCC C     1 ? 3 
ATOM   10836 O O     . GLU C 1 450 ? 51.673  28.586  58.328  1.000 51.031  0 450 GLU CCC O     1 ? 3 
ATOM   10837 C CB    . GLU C 1 450 ? 52.595  30.298  56.416  1.000 58.746  0 450 GLU CCC CB    1 ? 3 
ATOM   10838 C CG    . GLU C 1 450 ? 53.011  30.954  55.115  1.000 60.838  0 450 GLU CCC CG    1 ? 3 
ATOM   10839 C CD    . GLU C 1 450 ? 54.506  30.948  54.852  1.000 61.707  0 450 GLU CCC CD    1 ? 3 
ATOM   10840 O OE1   . GLU C 1 450 ? 55.277  31.387  55.740  1.000 65.422  0 450 GLU CCC OE1   1 ? 3 
ATOM   10841 O OE2   . GLU C 1 450 ? 54.898  30.502  53.761  1.000 61.675  0 450 GLU CCC OE2   1 ? 3 
ATOM   10842 N N     . LYS C 1 451 ? 49.462  28.714  57.855  1.000 52.134  0 451 LYS CCC N     1 ? 3 
ATOM   10843 C CA    . LYS C 1 451 ? 49.033  27.745  58.904  1.000 47.274  0 451 LYS CCC CA    1 ? 3 
ATOM   10844 C C     . LYS C 1 451 ? 49.645  26.377  58.589  1.000 43.364  0 451 LYS CCC C     1 ? 3 
ATOM   10845 O O     . LYS C 1 451 ? 49.638  25.991  57.401  1.000 43.016  0 451 LYS CCC O     1 ? 3 
ATOM   10846 C CB    . LYS C 1 451 ? 47.510  27.603  58.991  1.000 48.860  0 451 LYS CCC CB    1 ? 3 
ATOM   10847 C CG    . LYS C 1 451 ? 47.016  26.835  60.211  1.000 48.142  0 451 LYS CCC CG    1 ? 3 
ATOM   10848 C CD    . LYS C 1 451 ? 45.519  26.620  60.225  1.000 49.144  0 451 LYS CCC CD    1 ? 3 
ATOM   10849 C CE    . LYS C 1 451 ? 44.981  26.501  61.632  1.000 49.765  0 451 LYS CCC CE    1 ? 3 
ATOM   10850 N NZ    . LYS C 1 451 ? 43.602  27.030  61.778  1.000 50.132  0 451 LYS CCC NZ    1 ? 3 
ATOM   10851 N N     . VAL C 1 452 ? 50.140  25.662  59.603  1.000 38.193  0 452 VAL CCC N     1 ? 3 
ATOM   10852 C CA    . VAL C 1 452 ? 50.703  24.296  59.392  1.000 36.451  0 452 VAL CCC CA    1 ? 3 
ATOM   10853 C C     . VAL C 1 452 ? 49.530  23.299  59.332  1.000 35.201  0 452 VAL CCC C     1 ? 3 
ATOM   10854 O O     . VAL C 1 452 ? 48.741  23.218  60.291  1.000 35.720  0 452 VAL CCC O     1 ? 3 
ATOM   10855 C CB    . VAL C 1 452 ? 51.736  23.930  60.469  1.000 35.760  0 452 VAL CCC CB    1 ? 3 
ATOM   10856 C CG1   . VAL C 1 452 ? 52.313  22.536  60.260  1.000 35.846  0 452 VAL CCC CG1   1 ? 3 
ATOM   10857 C CG2   . VAL C 1 452 ? 52.852  24.955  60.501  1.000 36.939  0 452 VAL CCC CG2   1 ? 3 
ATOM   10858 N N     . VAL C 1 453 ? 49.382  22.606  58.208  1.000 33.611  0 453 VAL CCC N     1 ? 3 
ATOM   10859 C CA    . VAL C 1 453 ? 48.303  21.601  58.010  1.000 32.988  0 453 VAL CCC CA    1 ? 3 
ATOM   10860 C C     . VAL C 1 453 ? 48.932  20.218  57.892  1.000 30.464  0 453 VAL CCC C     1 ? 3 
ATOM   10861 O O     . VAL C 1 453 ? 48.189  19.241  58.001  1.000 29.606  0 453 VAL CCC O     1 ? 3 
ATOM   10862 C CB    . VAL C 1 453 ? 47.398  21.938  56.802  1.000 34.560  0 453 VAL CCC CB    1 ? 3 
ATOM   10863 C CG1   . VAL C 1 453 ? 46.606  23.238  57.009  1.000 35.235  0 453 VAL CCC CG1   1 ? 3 
ATOM   10864 C CG2   . VAL C 1 453 ? 48.175  21.985  55.509  1.000 34.551  0 453 VAL CCC CG2   1 ? 3 
ATOM   10865 N N     . GLY C 1 454 ? 50.248  20.146  57.702  1.000 29.601  0 454 GLY CCC N     1 ? 3 
ATOM   10866 C CA    . GLY C 1 454 ? 51.001  18.885  57.586  1.000 29.072  0 454 GLY CCC CA    1 ? 3 
ATOM   10867 C C     . GLY C 1 454 ? 52.383  19.007  58.202  1.000 29.339  0 454 GLY CCC C     1 ? 3 
ATOM   10868 O O     . GLY C 1 454 ? 53.113  19.963  57.854  1.000 30.996  0 454 GLY CCC O     1 ? 3 
ATOM   10869 N N     . PHE C 1 455 ? 52.708  18.096  59.120  1.000 28.212  0 455 PHE CCC N     1 ? 3 
ATOM   10870 C CA    . PHE C 1 455 ? 54.025  17.944  59.771  1.000 26.725  0 455 PHE CCC CA    1 ? 3 
ATOM   10871 C C     . PHE C 1 455 ? 54.537  16.518  59.517  1.000 25.241  0 455 PHE CCC C     1 ? 3 
ATOM   10872 O O     . PHE C 1 455 ? 53.784  15.565  59.734  1.000 24.799  0 455 PHE CCC O     1 ? 3 
ATOM   10873 C CB    . PHE C 1 455 ? 53.897  18.267  61.267  1.000 26.330  0 455 PHE CCC CB    1 ? 3 
ATOM   10874 C CG    . PHE C 1 455 ? 55.116  17.891  62.068  1.000 26.076  0 455 PHE CCC CG    1 ? 3 
ATOM   10875 C CD1   . PHE C 1 455 ? 55.380  16.568  62.377  1.000 26.022  0 455 PHE CCC CD1   1 ? 3 
ATOM   10876 C CD2   . PHE C 1 455 ? 55.958  18.867  62.546  1.000 25.804  0 455 PHE CCC CD2   1 ? 3 
ATOM   10877 C CE1   . PHE C 1 455 ? 56.493  16.221  63.135  1.000 26.010  0 455 PHE CCC CE1   1 ? 3 
ATOM   10878 C CE2   . PHE C 1 455 ? 57.081  18.524  63.291  1.000 26.936  0 455 PHE CCC CE2   1 ? 3 
ATOM   10879 C CZ    . PHE C 1 455 ? 57.356  17.209  63.574  1.000 25.777  0 455 PHE CCC CZ    1 ? 3 
ATOM   10880 N N     . HIS C 1 456 ? 55.791  16.379  59.114  1.000 25.214  0 456 HIS CCC N     1 ? 3 
ATOM   10881 C CA    . HIS C 1 456 ? 56.408  15.118  58.636  1.000 25.349  0 456 HIS CCC CA    1 ? 3 
ATOM   10882 C C     . HIS C 1 456 ? 57.850  15.057  59.111  1.000 25.903  0 456 HIS CCC C     1 ? 3 
ATOM   10883 O O     . HIS C 1 456 ? 58.620  16.009  58.830  1.000 25.753  0 456 HIS CCC O     1 ? 3 
ATOM   10884 C CB    . HIS C 1 456 ? 56.379  15.068  57.107  1.000 27.157  0 456 HIS CCC CB    1 ? 3 
ATOM   10885 C CG    . HIS C 1 456 ? 54.983  15.094  56.560  1.000 28.432  0 456 HIS CCC CG    1 ? 3 
ATOM   10886 N ND1   . HIS C 1 456 ? 54.265  13.935  56.340  1.000 28.604  0 456 HIS CCC ND1   1 ? 3 
ATOM   10887 C CD2   . HIS C 1 456 ? 54.153  16.131  56.286  1.000 28.123  0 456 HIS CCC CD2   1 ? 3 
ATOM   10888 C CE1   . HIS C 1 456 ? 53.050  14.258  55.937  1.000 28.931  0 456 HIS CCC CE1   1 ? 3 
ATOM   10889 N NE2   . HIS C 1 456 ? 52.964  15.599  55.892  1.000 27.904  0 456 HIS CCC NE2   1 ? 3 
ATOM   10890 N N     . PHE C 1 457 ? 58.236  13.983  59.787  1.000 25.591  0 457 PHE CCC N     1 ? 3 
ATOM   10891 C CA    . PHE C 1 457 ? 59.650  13.827  60.192  1.000 24.766  0 457 PHE CCC CA    1 ? 3 
ATOM   10892 C C     . PHE C 1 457 ? 60.086  12.388  59.971  1.000 25.045  0 457 PHE CCC C     1 ? 3 
ATOM   10893 O O     . PHE C 1 457 ? 59.460  11.471  60.581  1.000 25.345  0 457 PHE CCC O     1 ? 3 
ATOM   10894 C CB    . PHE C 1 457 ? 59.859  14.245  61.640  1.000 23.936  0 457 PHE CCC CB    1 ? 3 
ATOM   10895 C CG    . PHE C 1 457 ? 61.303  14.084  62.043  1.000 23.798  0 457 PHE CCC CG    1 ? 3 
ATOM   10896 C CD1   . PHE C 1 457 ? 62.235  15.039  61.662  1.000 23.278  0 457 PHE CCC CD1   1 ? 3 
ATOM   10897 C CD2   . PHE C 1 457 ? 61.740  12.941  62.708  1.000 22.703  0 457 PHE CCC CD2   1 ? 3 
ATOM   10898 C CE1   . PHE C 1 457 ? 63.572  14.879  61.952  1.000 22.751  0 457 PHE CCC CE1   1 ? 3 
ATOM   10899 C CE2   . PHE C 1 457 ? 63.080  12.791  63.009  1.000 22.879  0 457 PHE CCC CE2   1 ? 3 
ATOM   10900 C CZ    . PHE C 1 457 ? 63.983  13.765  62.647  1.000 22.731  0 457 PHE CCC CZ    1 ? 3 
ATOM   10901 N N     . VAL C 1 458 ? 61.100  12.213  59.119  1.000 23.943  0 458 VAL CCC N     1 ? 3 
ATOM   10902 C CA    . VAL C 1 458 ? 61.787  10.915  58.927  1.000 23.783  0 458 VAL CCC CA    1 ? 3 
ATOM   10903 C C     . VAL C 1 458 ? 63.104  11.017  59.668  1.000 23.888  0 458 VAL CCC C     1 ? 3 
ATOM   10904 O O     . VAL C 1 458 ? 63.797  12.055  59.464  1.000 22.756  0 458 VAL CCC O     1 ? 3 
ATOM   10905 C CB    . VAL C 1 458 ? 62.006  10.638  57.424  1.000 25.447  0 458 VAL CCC CB    1 ? 3 
ATOM   10906 C CG1   . VAL C 1 458 ? 62.804  9.343   57.186  1.000 25.551  0 458 VAL CCC CG1   1 ? 3 
ATOM   10907 C CG2   . VAL C 1 458 ? 60.670  10.654  56.657  1.000 25.208  0 458 VAL CCC CG2   1 ? 3 
ATOM   10908 N N     . GLY C 1 459 ? 63.434  9.992   60.470  1.000 24.233  0 459 GLY CCC N     1 ? 3 
ATOM   10909 C CA    . GLY C 1 459 ? 64.684  9.954   61.256  1.000 24.604  0 459 GLY CCC CA    1 ? 3 
ATOM   10910 C C     . GLY C 1 459 ? 64.547  9.186   62.560  1.000 24.065  0 459 GLY CCC C     1 ? 3 
ATOM   10911 O O     . GLY C 1 459 ? 63.543  8.567   62.794  1.000 25.517  0 459 GLY CCC O     1 ? 3 
ATOM   10912 N N     . PRO C 1 460 ? 65.564  9.180   63.440  1.000 24.718  0 460 PRO CCC N     1 ? 3 
ATOM   10913 C CA    . PRO C 1 460 ? 65.483  8.462   64.715  1.000 24.856  0 460 PRO CCC CA    1 ? 3 
ATOM   10914 C C     . PRO C 1 460 ? 64.447  9.073   65.669  1.000 25.274  0 460 PRO CCC C     1 ? 3 
ATOM   10915 O O     . PRO C 1 460 ? 64.207  10.254  65.592  1.000 26.635  0 460 PRO CCC O     1 ? 3 
ATOM   10916 C CB    . PRO C 1 460 ? 66.864  8.623   65.344  1.000 24.419  0 460 PRO CCC CB    1 ? 3 
ATOM   10917 C CG    . PRO C 1 460 ? 67.758  9.098   64.189  1.000 25.248  0 460 PRO CCC CG    1 ? 3 
ATOM   10918 C CD    . PRO C 1 460 ? 66.852  9.864   63.249  1.000 24.995  0 460 PRO CCC CD    1 ? 3 
ATOM   10919 N N     . ASN C 1 461 ? 63.854  8.262   66.523  1.000 24.921  0 461 ASN CCC N     1 ? 3 
ATOM   10920 C CA    . ASN C 1 461 ? 62.952  8.763   67.577  1.000 25.944  0 461 ASN CCC CA    1 ? 3 
ATOM   10921 C C     . ASN C 1 461 ? 61.855  9.656   66.939  1.000 25.698  0 461 ASN CCC C     1 ? 3 
ATOM   10922 O O     . ASN C 1 461 ? 61.555  10.771  67.480  1.000 24.460  0 461 ASN CCC O     1 ? 3 
ATOM   10923 C CB    . ASN C 1 461 ? 63.777  9.503   68.622  1.000 26.041  0 461 ASN CCC CB    1 ? 3 
ATOM   10924 C CG    . ASN C 1 461 ? 65.030  8.715   68.979  1.000 27.512  0 461 ASN CCC CG    1 ? 3 
ATOM   10925 O OD1   . ASN C 1 461 ? 64.933  7.561   69.386  1.000 27.554  0 461 ASN CCC OD1   1 ? 3 
ATOM   10926 N ND2   . ASN C 1 461 ? 66.214  9.290   68.792  1.000 26.236  0 461 ASN CCC ND2   1 ? 3 
ATOM   10927 N N     . ALA C 1 462 ? 61.286  9.237   65.822  1.000 24.479  0 462 ALA CCC N     1 ? 3 
ATOM   10928 C CA    . ALA C 1 462 ? 60.360  10.109  65.065  1.000 27.893  0 462 ALA CCC CA    1 ? 3 
ATOM   10929 C C     . ALA C 1 462 ? 59.038  10.271  65.848  1.000 29.955  0 462 ALA CCC C     1 ? 3 
ATOM   10930 O O     . ALA C 1 462 ? 58.439  11.347  65.765  1.000 32.663  0 462 ALA CCC O     1 ? 3 
ATOM   10931 C CB    . ALA C 1 462 ? 60.119  9.590   63.685  1.000 26.727  0 462 ALA CCC CB    1 ? 3 
ATOM   10932 N N     . GLY C 1 463 ? 58.590  9.220   66.525  1.000 29.576  0 463 GLY CCC N     1 ? 3 
ATOM   10933 C CA    . GLY C 1 463 ? 57.408  9.306   67.390  1.000 33.604  0 463 GLY CCC CA    1 ? 3 
ATOM   10934 C C     . GLY C 1 463 ? 57.644  10.221  68.575  1.000 32.979  0 463 GLY CCC C     1 ? 3 
ATOM   10935 O O     . GLY C 1 463 ? 56.762  11.031  68.892  1.000 33.185  0 463 GLY CCC O     1 ? 3 
ATOM   10936 N N     . GLU C 1 464 ? 58.814  10.130  69.193  1.000 33.301  0 464 GLU CCC N     1 ? 3 
ATOM   10937 C CA    . GLU C 1 464 ? 59.182  11.017  70.324  1.000 33.750  0 464 GLU CCC CA    1 ? 3 
ATOM   10938 C C     . GLU C 1 464 ? 59.144  12.476  69.831  1.000 32.336  0 464 GLU CCC C     1 ? 3 
ATOM   10939 O O     . GLU C 1 464 ? 58.712  13.359  70.591  1.000 33.276  0 464 GLU CCC O     1 ? 3 
ATOM   10940 C CB    . GLU C 1 464 ? 60.524  10.575  70.912  1.000 33.812  0 464 GLU CCC CB    1 ? 3 
ATOM   10941 C CG    . GLU C 1 464 ? 60.543  9.118   71.417  1.000 34.954  0 464 GLU CCC CG    1 ? 3 
ATOM   10942 C CD    . GLU C 1 464 ? 59.609  8.716   72.561  1.000 35.282  0 464 GLU CCC CD    1 ? 3 
ATOM   10943 O OE1   . GLU C 1 464 ? 59.050  9.621   73.200  1.000 38.029  0 464 GLU CCC OE1   1 ? 3 
ATOM   10944 O OE2   . GLU C 1 464 ? 59.443  7.500   72.824  1.000 33.946  0 464 GLU CCC OE2   1 ? 3 
ATOM   10945 N N     . ILE C 1 465 ? 59.541  12.735  68.592  1.000 29.848  0 465 ILE CCC N     1 ? 3 
ATOM   10946 C CA    . ILE C 1 465 ? 59.626  14.122  68.062  1.000 29.227  0 465 ILE CCC CA    1 ? 3 
ATOM   10947 C C     . ILE C 1 465 ? 58.213  14.597  67.703  1.000 29.760  0 465 ILE CCC C     1 ? 3 
ATOM   10948 O O     . ILE C 1 465 ? 57.900  15.785  67.923  1.000 31.174  0 465 ILE CCC O     1 ? 3 
ATOM   10949 C CB    . ILE C 1 465 ? 60.612  14.212  66.904  1.000 28.260  0 465 ILE CCC CB    1 ? 3 
ATOM   10950 C CG1   . ILE C 1 465 ? 62.046  14.093  67.429  1.000 29.886  0 465 ILE CCC CG1   1 ? 3 
ATOM   10951 C CG2   . ILE C 1 465 ? 60.431  15.501  66.151  1.000 29.469  0 465 ILE CCC CG2   1 ? 3 
ATOM   10952 C CD1   . ILE C 1 465 ? 63.107  13.808  66.358  1.000 28.159  0 465 ILE CCC CD1   1 ? 3 
ATOM   10953 N N     . THR C 1 466 ? 57.369  13.697  67.221  1.000 28.862  0 466 THR CCC N     1 ? 3 
ATOM   10954 C CA    . THR C 1 466 ? 56.133  14.099  66.542  1.000 29.680  0 466 THR CCC CA    1 ? 3 
ATOM   10955 C C     . THR C 1 466 ? 55.048  14.393  67.576  1.000 29.797  0 466 THR CCC C     1 ? 3 
ATOM   10956 O O     . THR C 1 466 ? 54.150  15.223  67.260  1.000 28.554  0 466 THR CCC O     1 ? 3 
ATOM   10957 C CB    . THR C 1 466 ? 55.641  13.036  65.569  1.000 28.774  0 466 THR CCC CB    1 ? 3 
ATOM   10958 O OG1   . THR C 1 466 ? 56.567  13.024  64.493  1.000 31.705  0 466 THR CCC OG1   1 ? 3 
ATOM   10959 C CG2   . THR C 1 466 ? 54.265  13.350  65.024  1.000 28.615  0 466 THR CCC CG2   1 ? 3 
ATOM   10960 N N     . GLN C 1 467 ? 55.077  13.686  68.701  1.000 28.980  0 467 GLN CCC N     1 ? 3 
ATOM   10961 C CA    . GLN C 1 467 ? 53.997  13.792  69.715  1.000 29.448  0 467 GLN CCC CA    1 ? 3 
ATOM   10962 C C     . GLN C 1 467 ? 53.741  15.271  70.014  1.000 29.530  0 467 GLN CCC C     1 ? 3 
ATOM   10963 O O     . GLN C 1 467 ? 52.600  15.743  69.805  1.000 34.463  0 467 GLN CCC O     1 ? 3 
ATOM   10964 C CB    . GLN C 1 467 ? 54.346  13.033  70.983  1.000 28.237  0 467 GLN CCC CB    1 ? 3 
ATOM   10965 C CG    . GLN C 1 467 ? 53.195  12.959  71.960  1.000 28.815  0 467 GLN CCC CG    1 ? 3 
ATOM   10966 C CD    . GLN C 1 467 ? 52.021  12.157  71.458  1.000 28.232  0 467 GLN CCC CD    1 ? 3 
ATOM   10967 O OE1   . GLN C 1 467 ? 51.999  10.944  71.577  1.000 26.942  0 467 GLN CCC OE1   1 ? 3 
ATOM   10968 N NE2   . GLN C 1 467 ? 51.020  12.832  70.922  1.000 28.764  0 467 GLN CCC NE2   1 ? 3 
ATOM   10969 N N     . GLY C 1 468 ? 54.769  15.992  70.417  1.000 29.138  0 468 GLY CCC N     1 ? 3 
ATOM   10970 C CA    . GLY C 1 468 ? 54.655  17.396  70.843  1.000 30.134  0 468 GLY CCC CA    1 ? 3 
ATOM   10971 C C     . GLY C 1 468 ? 54.185  18.302  69.721  1.000 30.408  0 468 GLY CCC C     1 ? 3 
ATOM   10972 O O     . GLY C 1 468 ? 53.295  19.160  69.923  1.000 30.543  0 468 GLY CCC O     1 ? 3 
ATOM   10973 N N     . PHE C 1 469 ? 54.819  18.161  68.578  1.000 31.428  0 469 PHE CCC N     1 ? 3 
ATOM   10974 C CA    . PHE C 1 469 ? 54.547  18.993  67.397  1.000 32.180  0 469 PHE CCC CA    1 ? 3 
ATOM   10975 C C     . PHE C 1 469 ? 53.118  18.744  66.973  1.000 34.132  0 469 PHE CCC C     1 ? 3 
ATOM   10976 O O     . PHE C 1 469 ? 52.454  19.727  66.622  1.000 38.939  0 469 PHE CCC O     1 ? 3 
ATOM   10977 C CB    . PHE C 1 469 ? 55.556  18.674  66.304  1.000 32.379  0 469 PHE CCC CB    1 ? 3 
ATOM   10978 C CG    . PHE C 1 469 ? 56.847  19.424  66.482  1.000 30.824  0 469 PHE CCC CG    1 ? 3 
ATOM   10979 C CD1   . PHE C 1 469 ? 56.850  20.806  66.471  1.000 30.250  0 469 PHE CCC CD1   1 ? 3 
ATOM   10980 C CD2   . PHE C 1 469 ? 58.041  18.754  66.640  1.000 30.162  0 469 PHE CCC CD2   1 ? 3 
ATOM   10981 C CE1   . PHE C 1 469 ? 58.038  21.506  66.590  1.000 30.295  0 469 PHE CCC CE1   1 ? 3 
ATOM   10982 C CE2   . PHE C 1 469 ? 59.229  19.455  66.754  1.000 29.591  0 469 PHE CCC CE2   1 ? 3 
ATOM   10983 C CZ    . PHE C 1 469 ? 59.225  20.829  66.735  1.000 29.564  0 469 PHE CCC CZ    1 ? 3 
ATOM   10984 N N     . SER C 1 470 ? 52.631  17.503  67.073  1.000 33.363  0 470 SER CCC N     1 ? 3 
ATOM   10985 C CA    . SER C 1 470 ? 51.208  17.196  66.738  1.000 32.367  0 470 SER CCC CA    1 ? 3 
ATOM   10986 C C     . SER C 1 470 ? 50.260  18.069  67.577  1.000 32.249  0 470 SER CCC C     1 ? 3 
ATOM   10987 O O     . SER C 1 470 ? 49.339  18.619  67.020  1.000 33.391  0 470 SER CCC O     1 ? 3 
ATOM   10988 C CB    . SER C 1 470 ? 50.903  15.734  66.844  1.000 31.360  0 470 SER CCC CB    1 ? 3 
ATOM   10989 O OG    . SER C 1 470 ? 50.778  15.316  68.172  1.000 30.574  0 470 SER CCC OG    1 ? 3 
ATOM   10990 N N     . LEU C 1 471 ? 50.486  18.197  68.880  1.000 33.417  0 471 LEU CCC N     1 ? 3 
ATOM   10991 C CA    . LEU C 1 471 ? 49.679  19.101  69.739  1.000 34.069  0 471 LEU CCC CA    1 ? 3 
ATOM   10992 C C     . LEU C 1 471 ? 49.814  20.557  69.277  1.000 37.342  0 471 LEU CCC C     1 ? 3 
ATOM   10993 O O     . LEU C 1 471 ? 48.776  21.229  69.208  1.000 40.001  0 471 LEU CCC O     1 ? 3 
ATOM   10994 C CB    . LEU C 1 471 ? 50.131  18.972  71.187  1.000 33.804  0 471 LEU CCC CB    1 ? 3 
ATOM   10995 C CG    . LEU C 1 471 ? 49.386  19.899  72.138  1.000 33.674  0 471 LEU CCC CG    1 ? 3 
ATOM   10996 C CD1   . LEU C 1 471 ? 47.890  19.639  72.030  1.000 33.883  0 471 LEU CCC CD1   1 ? 3 
ATOM   10997 C CD2   . LEU C 1 471 ? 49.917  19.766  73.552  1.000 33.195  0 471 LEU CCC CD2   1 ? 3 
ATOM   10998 N N     . ALA C 1 472 ? 51.035  21.039  69.018  1.000 38.701  0 472 ALA CCC N     1 ? 3 
ATOM   10999 C CA    . ALA C 1 472 ? 51.291  22.416  68.524  1.000 39.319  0 472 ALA CCC CA    1 ? 3 
ATOM   11000 C C     . ALA C 1 472 ? 50.516  22.636  67.229  1.000 41.144  0 472 ALA CCC C     1 ? 3 
ATOM   11001 O O     . ALA C 1 472 ? 49.886  23.721  67.056  1.000 41.874  0 472 ALA CCC O     1 ? 3 
ATOM   11002 C CB    . ALA C 1 472 ? 52.759  22.671  68.302  1.000 38.375  0 472 ALA CCC CB    1 ? 3 
ATOM   11003 N N     . VAL C 1 473 ? 50.543  21.644  66.340  1.000 40.887  0 473 VAL CCC N     1 ? 3 
ATOM   11004 C CA    . VAL C 1 473 ? 49.888  21.802  65.019  1.000 41.891  0 473 VAL CCC CA    1 ? 3 
ATOM   11005 C C     . VAL C 1 473 ? 48.377  21.866  65.274  1.000 44.203  0 473 VAL CCC C     1 ? 3 
ATOM   11006 O O     . VAL C 1 473 ? 47.712  22.699  64.639  1.000 45.951  0 473 VAL CCC O     1 ? 3 
ATOM   11007 C CB    . VAL C 1 473 ? 50.291  20.693  64.027  1.000 43.144  0 473 VAL CCC CB    1 ? 3 
ATOM   11008 C CG1   . VAL C 1 473 ? 49.382  20.673  62.803  1.000 46.477  0 473 VAL CCC CG1   1 ? 3 
ATOM   11009 C CG2   . VAL C 1 473 ? 51.732  20.830  63.581  1.000 42.146  0 473 VAL CCC CG2   1 ? 3 
ATOM   11010 N N     . LYS C 1 474 ? 47.865  21.068  66.219  1.000 43.155  0 474 LYS CCC N     1 ? 3 
ATOM   11011 C CA    . LYS C 1 474 ? 46.414  21.023  66.561  1.000 43.129  0 474 LYS CCC CA    1 ? 3 
ATOM   11012 C C     . LYS C 1 474 ? 45.963  22.375  67.123  1.000 44.751  0 474 LYS CCC C     1 ? 3 
ATOM   11013 O O     . LYS C 1 474 ? 44.814  22.775  66.834  1.000 45.592  0 474 LYS CCC O     1 ? 3 
ATOM   11014 C CB    . LYS C 1 474 ? 46.148  19.879  67.536  1.000 42.220  0 474 LYS CCC CB    1 ? 3 
ATOM   11015 C CG    . LYS C 1 474 ? 44.700  19.699  67.930  1.000 41.086  0 474 LYS CCC CG    1 ? 3 
ATOM   11016 C CD    . LYS C 1 474 ? 44.512  18.584  68.910  1.000 39.728  0 474 LYS CCC CD    1 ? 3 
ATOM   11017 C CE    . LYS C 1 474 ? 43.090  18.078  68.959  1.000 38.062  0 474 LYS CCC CE    1 ? 3 
ATOM   11018 N NZ    . LYS C 1 474 ? 43.027  16.814  69.716  1.000 38.774  0 474 LYS CCC NZ    1 ? 3 
ATOM   11019 N N     . LEU C 1 475 ? 46.844  23.070  67.857  1.000 46.295  0 475 LEU CCC N     1 ? 3 
ATOM   11020 C CA    . LEU C 1 475 ? 46.545  24.391  68.486  1.000 48.571  0 475 LEU CCC CA    1 ? 3 
ATOM   11021 C C     . LEU C 1 475 ? 46.616  25.532  67.458  1.000 49.840  0 475 LEU CCC C     1 ? 3 
ATOM   11022 O O     . LEU C 1 475 ? 46.236  26.652  67.826  1.000 55.852  0 475 LEU CCC O     1 ? 3 
ATOM   11023 C CB    . LEU C 1 475 ? 47.491  24.644  69.663  1.000 47.297  0 475 LEU CCC CB    1 ? 3 
ATOM   11024 C CG    . LEU C 1 475 ? 47.233  23.790  70.908  1.000 48.961  0 475 LEU CCC CG    1 ? 3 
ATOM   11025 C CD1   . LEU C 1 475 ? 48.295  24.026  71.985  1.000 49.648  0 475 LEU CCC CD1   1 ? 3 
ATOM   11026 C CD2   . LEU C 1 475 ? 45.840  24.041  71.465  1.000 48.820  0 475 LEU CCC CD2   1 ? 3 
ATOM   11027 N N     . GLY C 1 476 ? 47.038  25.260  66.217  1.000 48.375  0 476 GLY CCC N     1 ? 3 
ATOM   11028 C CA    . GLY C 1 476 ? 46.966  26.211  65.091  1.000 45.772  0 476 GLY CCC CA    1 ? 3 
ATOM   11029 C C     . GLY C 1 476 ? 48.269  26.935  64.850  1.000 44.807  0 476 GLY CCC C     1 ? 3 
ATOM   11030 O O     . GLY C 1 476 ? 48.222  28.113  64.485  1.000 47.795  0 476 GLY CCC O     1 ? 3 
ATOM   11031 N N     . ALA C 1 477 ? 49.394  26.253  65.043  1.000 44.659  0 477 ALA CCC N     1 ? 3 
ATOM   11032 C CA    . ALA C 1 477 ? 50.759  26.780  64.832  1.000 45.537  0 477 ALA CCC CA    1 ? 3 
ATOM   11033 C C     . ALA C 1 477 ? 50.923  27.216  63.366  1.000 45.761  0 477 ALA CCC C     1 ? 3 
ATOM   11034 O O     . ALA C 1 477 ? 50.512  26.474  62.459  1.000 44.615  0 477 ALA CCC O     1 ? 3 
ATOM   11035 C CB    . ALA C 1 477 ? 51.782  25.745  65.224  1.000 45.071  0 477 ALA CCC CB    1 ? 3 
ATOM   11036 N N     . THR C 1 478 ? 51.508  28.396  63.153  1.000 44.019  0 478 THR CCC N     1 ? 3 
ATOM   11037 C CA    . THR C 1 478 ? 51.854  28.932  61.821  1.000 44.180  0 478 THR CCC CA    1 ? 3 
ATOM   11038 C C     . THR C 1 478 ? 53.351  28.724  61.547  1.000 45.271  0 478 THR CCC C     1 ? 3 
ATOM   11039 O O     . THR C 1 478 ? 54.143  28.502  62.529  1.000 42.007  0 478 THR CCC O     1 ? 3 
ATOM   11040 C CB    . THR C 1 478 ? 51.527  30.420  61.750  1.000 45.873  0 478 THR CCC CB    1 ? 3 
ATOM   11041 O OG1   . THR C 1 478 ? 52.392  31.077  62.667  1.000 46.587  0 478 THR CCC OG1   1 ? 3 
ATOM   11042 C CG2   . THR C 1 478 ? 50.080  30.751  62.090  1.000 46.797  0 478 THR CCC CG2   1 ? 3 
ATOM   11043 N N     . LYS C 1 479 ? 53.767  28.873  60.288  1.000 43.079  0 479 LYS CCC N     1 ? 3 
ATOM   11044 C CA    . LYS C 1 479 ? 55.208  28.842  59.947  1.000 43.535  0 479 LYS CCC CA    1 ? 3 
ATOM   11045 C C     . LYS C 1 479 ? 55.962  29.881  60.803  1.000 44.608  0 479 LYS CCC C     1 ? 3 
ATOM   11046 O O     . LYS C 1 479 ? 57.086  29.577  61.212  1.000 43.331  0 479 LYS CCC O     1 ? 3 
ATOM   11047 C CB    . LYS C 1 479 ? 55.442  29.021  58.445  1.000 42.350  0 479 LYS CCC CB    1 ? 3 
ATOM   11048 C CG    . LYS C 1 479 ? 56.905  28.958  58.019  1.000 40.325  0 479 LYS CCC CG    1 ? 3 
ATOM   11049 C CD    . LYS C 1 479 ? 57.628  27.736  58.545  1.000 39.681  0 479 LYS CCC CD    1 ? 3 
ATOM   11050 C CE    . LYS C 1 479 ? 58.924  27.395  57.821  1.000 37.507  0 479 LYS CCC CE    1 ? 3 
ATOM   11051 N NZ    . LYS C 1 479 ? 59.859  28.537  57.819  1.000 37.263  0 479 LYS CCC NZ    1 ? 3 
ATOM   11052 N N     . LYS C 1 480 ? 55.358  31.038  61.096  1.000 46.386  0 480 LYS CCC N     1 ? 3 
ATOM   11053 C CA    . LYS C 1 480 ? 55.999  32.117  61.897  1.000 47.684  0 480 LYS CCC CA    1 ? 3 
ATOM   11054 C C     . LYS C 1 480 ? 56.260  31.580  63.305  1.000 44.734  0 480 LYS CCC C     1 ? 3 
ATOM   11055 O O     . LYS C 1 480 ? 57.379  31.747  63.799  1.000 44.978  0 480 LYS CCC O     1 ? 3 
ATOM   11056 C CB    . LYS C 1 480 ? 55.161  33.402  61.883  1.000 50.290  0 480 LYS CCC CB    1 ? 3 
ATOM   11057 C CG    . LYS C 1 480 ? 55.662  34.510  62.812  1.000 51.673  0 480 LYS CCC CG    1 ? 3 
ATOM   11058 C CD    . LYS C 1 480 ? 55.447  35.938  62.301  1.000 55.191  0 480 LYS CCC CD    1 ? 3 
ATOM   11059 C CE    . LYS C 1 480 ? 55.431  36.986  63.396  1.000 56.692  0 480 LYS CCC CE    1 ? 3 
ATOM   11060 N NZ    . LYS C 1 480 ? 56.712  36.971  64.157  1.000 58.762  0 480 LYS CCC NZ    1 ? 3 
ATOM   11061 N N     . ASP C 1 481 ? 55.270  30.923  63.905  1.000 43.221  0 481 ASP CCC N     1 ? 3 
ATOM   11062 C CA    . ASP C 1 481 ? 55.394  30.274  65.242  1.000 42.421  0 481 ASP CCC CA    1 ? 3 
ATOM   11063 C C     . ASP C 1 481 ? 56.602  29.320  65.265  1.000 39.259  0 481 ASP CCC C     1 ? 3 
ATOM   11064 O O     . ASP C 1 481 ? 57.324  29.307  66.258  1.000 38.527  0 481 ASP CCC O     1 ? 3 
ATOM   11065 C CB    . ASP C 1 481 ? 54.131  29.496  65.594  1.000 42.097  0 481 ASP CCC CB    1 ? 3 
ATOM   11066 C CG    . ASP C 1 481 ? 52.924  30.386  65.788  1.000 44.174  0 481 ASP CCC CG    1 ? 3 
ATOM   11067 O OD1   . ASP C 1 481 ? 53.107  31.534  66.212  1.000 46.413  0 481 ASP CCC OD1   1 ? 3 
ATOM   11068 O OD2   . ASP C 1 481 ? 51.817  29.905  65.521  1.000 46.153  0 481 ASP CCC OD2   1 ? 3 
ATOM   11069 N N     . PHE C 1 482 ? 56.781  28.535  64.200  1.000 38.537  0 482 PHE CCC N     1 ? 3 
ATOM   11070 C CA    . PHE C 1 482 ? 57.885  27.557  64.064  1.000 38.063  0 482 PHE CCC CA    1 ? 3 
ATOM   11071 C C     . PHE C 1 482 ? 59.225  28.305  63.961  1.000 37.736  0 482 PHE CCC C     1 ? 3 
ATOM   11072 O O     . PHE C 1 482 ? 60.164  27.882  64.619  1.000 35.836  0 482 PHE CCC O     1 ? 3 
ATOM   11073 C CB    . PHE C 1 482 ? 57.614  26.639  62.875  1.000 36.764  0 482 PHE CCC CB    1 ? 3 
ATOM   11074 C CG    . PHE C 1 482 ? 56.819  25.408  63.189  1.000 34.849  0 482 PHE CCC CG    1 ? 3 
ATOM   11075 C CD1   . PHE C 1 482 ? 55.441  25.449  63.233  1.000 35.898  0 482 PHE CCC CD1   1 ? 3 
ATOM   11076 C CD2   . PHE C 1 482 ? 57.442  24.184  63.357  1.000 34.895  0 482 PHE CCC CD2   1 ? 3 
ATOM   11077 C CE1   . PHE C 1 482 ? 54.704  24.295  63.451  1.000 34.215  0 482 PHE CCC CE1   1 ? 3 
ATOM   11078 C CE2   . PHE C 1 482 ? 56.710  23.034  63.592  1.000 33.644  0 482 PHE CCC CE2   1 ? 3 
ATOM   11079 C CZ    . PHE C 1 482 ? 55.341  23.096  63.647  1.000 34.528  0 482 PHE CCC CZ    1 ? 3 
ATOM   11080 N N     . ASP C 1 483 ? 59.294  29.404  63.199  1.000 39.495  0 483 ASP CCC N     1 ? 3 
ATOM   11081 C CA    . ASP C 1 483 ? 60.536  30.206  63.015  1.000 41.796  0 483 ASP CCC CA    1 ? 3 
ATOM   11082 C C     . ASP C 1 483 ? 60.934  30.896  64.326  1.000 44.098  0 483 ASP CCC C     1 ? 3 
ATOM   11083 O O     . ASP C 1 483 ? 62.144  31.086  64.539  1.000 48.754  0 483 ASP CCC O     1 ? 3 
ATOM   11084 C CB    . ASP C 1 483 ? 60.407  31.263  61.921  1.000 41.860  0 483 ASP CCC CB    1 ? 3 
ATOM   11085 C CG    . ASP C 1 483 ? 60.253  30.704  60.514  1.000 42.542  0 483 ASP CCC CG    1 ? 3 
ATOM   11086 O OD1   . ASP C 1 483 ? 60.596  29.524  60.331  1.000 43.753  0 483 ASP CCC OD1   1 ? 3 
ATOM   11087 O OD2   . ASP C 1 483 ? 59.782  31.455  59.611  1.000 43.352  0 483 ASP CCC OD2   1 ? 3 
ATOM   11088 N N     . ASP C 1 484 ? 59.970  31.306  65.146  1.000 42.697  0 484 ASP CCC N     1 ? 3 
ATOM   11089 C CA    . ASP C 1 484 ? 60.213  32.088  66.380  1.000 43.840  0 484 ASP CCC CA    1 ? 3 
ATOM   11090 C C     . ASP C 1 484 ? 60.373  31.141  67.587  1.000 42.605  0 484 ASP CCC C     1 ? 3 
ATOM   11091 O O     . ASP C 1 484 ? 60.617  31.644  68.696  1.000 38.708  0 484 ASP CCC O     1 ? 3 
ATOM   11092 C CB    . ASP C 1 484 ? 59.073  33.087  66.622  1.000 46.951  0 484 ASP CCC CB    1 ? 3 
ATOM   11093 C CG    . ASP C 1 484 ? 58.875  34.134  65.527  1.000 49.066  0 484 ASP CCC CG    1 ? 3 
ATOM   11094 O OD1   . ASP C 1 484 ? 59.655  34.164  64.559  1.000 49.633  0 484 ASP CCC OD1   1 ? 3 
ATOM   11095 O OD2   . ASP C 1 484 ? 57.942  34.925  65.652  1.000 51.710  0 484 ASP CCC OD2   1 ? 3 
ATOM   11096 N N     . MET C 1 485 ? 60.211  29.826  67.377  1.000 41.020  0 485 MET CCC N     1 ? 3 
ATOM   11097 C CA    . MET C 1 485 ? 60.457  28.763  68.388  1.000 39.990  0 485 MET CCC CA    1 ? 3 
ATOM   11098 C C     . MET C 1 485 ? 61.969  28.652  68.666  1.000 41.208  0 485 MET CCC C     1 ? 3 
ATOM   11099 O O     . MET C 1 485 ? 62.774  28.460  67.705  1.000 38.268  0 485 MET CCC O     1 ? 3 
ATOM   11100 C CB    . MET C 1 485 ? 59.934  27.412  67.891  1.000 39.536  0 485 MET CCC CB    1 ? 3 
ATOM   11101 C CG    . MET C 1 485 ? 60.318  26.237  68.746  1.000 37.077  0 485 MET CCC CG    1 ? 3 
ATOM   11102 S SD    . MET C 1 485 ? 59.725  24.694  67.998  1.000 39.527  0 485 MET CCC SD    1 ? 3 
ATOM   11103 C CE    . MET C 1 485 ? 60.508  24.662  66.379  1.000 38.882  0 485 MET CCC CE    1 ? 3 
ATOM   11104 N N     . ILE C 1 486 ? 62.357  28.741  69.939  1.000 41.150  0 486 ILE CCC N     1 ? 3 
ATOM   11105 C CA    . ILE C 1 486 ? 63.765  28.514  70.338  1.000 40.132  0 486 ILE CCC CA    1 ? 3 
ATOM   11106 C C     . ILE C 1 486 ? 64.042  27.011  70.292  1.000 38.102  0 486 ILE CCC C     1 ? 3 
ATOM   11107 O O     . ILE C 1 486 ? 63.222  26.221  70.828  1.000 35.235  0 486 ILE CCC O     1 ? 3 
ATOM   11108 C CB    . ILE C 1 486 ? 64.106  29.111  71.707  1.000 42.509  0 486 ILE CCC CB    1 ? 3 
ATOM   11109 C CG1   . ILE C 1 486 ? 63.685  30.578  71.832  1.000 44.202  0 486 ILE CCC CG1   1 ? 3 
ATOM   11110 C CG2   . ILE C 1 486 ? 65.611  28.929  71.952  1.000 45.146  0 486 ILE CCC CG2   1 ? 3 
ATOM   11111 C CD1   . ILE C 1 486 ? 64.563  31.557  71.068  1.000 45.208  0 486 ILE CCC CD1   1 ? 3 
ATOM   11112 N N     . GLY C 1 487 ? 65.178  26.665  69.667  1.000 37.122  0 487 GLY CCC N     1 ? 3 
ATOM   11113 C CA    . GLY C 1 487 ? 65.689  25.291  69.508  1.000 35.214  0 487 GLY CCC CA    1 ? 3 
ATOM   11114 C C     . GLY C 1 487 ? 66.331  24.787  70.785  1.000 34.249  0 487 GLY CCC C     1 ? 3 
ATOM   11115 O O     . GLY C 1 487 ? 66.859  25.633  71.539  1.000 31.089  0 487 GLY CCC O     1 ? 3 
ATOM   11116 N N     . ILE C 1 488 ? 66.222  23.476  71.016  1.000 34.679  0 488 ILE CCC N     1 ? 3 
ATOM   11117 C CA    . ILE C 1 488 ? 67.108  22.688  71.925  1.000 35.397  0 488 ILE CCC CA    1 ? 3 
ATOM   11118 C C     . ILE C 1 488 ? 68.212  22.089  71.057  1.000 34.829  0 488 ILE CCC C     1 ? 3 
ATOM   11119 O O     . ILE C 1 488 ? 67.912  21.387  70.061  1.000 36.716  0 488 ILE CCC O     1 ? 3 
ATOM   11120 C CB    . ILE C 1 488 ? 66.350  21.554  72.642  1.000 35.579  0 488 ILE CCC CB    1 ? 3 
ATOM   11121 C CG1   . ILE C 1 488 ? 65.033  22.026  73.267  1.000 36.169  0 488 ILE CCC CG1   1 ? 3 
ATOM   11122 C CG2   . ILE C 1 488 ? 67.259  20.876  73.641  1.000 33.605  0 488 ILE CCC CG2   1 ? 3 
ATOM   11123 C CD1   . ILE C 1 488 ? 64.176  20.885  73.778  1.000 36.611  0 488 ILE CCC CD1   1 ? 3 
ATOM   11124 N N     . HIS C 1 489 ? 69.447  22.365  71.418  1.000 36.105  0 489 HIS CCC N     1 ? 3 
ATOM   11125 C CA    . HIS C 1 489 ? 70.664  21.941  70.683  1.000 36.217  0 489 HIS CCC CA    1 ? 3 
ATOM   11126 C C     . HIS C 1 489 ? 71.495  21.048  71.586  1.000 32.808  0 489 HIS CCC C     1 ? 3 
ATOM   11127 O O     . HIS C 1 489 ? 71.595  21.315  72.770  1.000 30.754  0 489 HIS CCC O     1 ? 3 
ATOM   11128 C CB    . HIS C 1 489 ? 71.455  23.188  70.297  1.000 38.614  0 489 HIS CCC CB    1 ? 3 
ATOM   11129 C CG    . HIS C 1 489 ? 72.629  22.912  69.446  1.000 38.679  0 489 HIS CCC CG    1 ? 3 
ATOM   11130 N ND1   . HIS C 1 489 ? 72.499  22.316  68.210  1.000 42.294  0 489 HIS CCC ND1   1 ? 3 
ATOM   11131 C CD2   . HIS C 1 489 ? 73.938  23.195  69.612  1.000 39.751  0 489 HIS CCC CD2   1 ? 3 
ATOM   11132 C CE1   . HIS C 1 489 ? 73.696  22.231  67.651  1.000 42.665  0 489 HIS CCC CE1   1 ? 3 
ATOM   11133 N NE2   . HIS C 1 489 ? 74.602  22.755  68.492  1.000 39.897  0 489 HIS CCC NE2   1 ? 3 
ATOM   11134 N N     . PRO C 1 490 ? 72.122  19.968  71.081  1.000 30.509  0 490 PRO CCC N     1 ? 3 
ATOM   11135 C CA    . PRO C 1 490 ? 71.923  19.482  69.725  1.000 28.668  0 490 PRO CCC CA    1 ? 3 
ATOM   11136 C C     . PRO C 1 490 ? 70.797  18.444  69.673  1.000 28.234  0 490 PRO CCC C     1 ? 3 
ATOM   11137 O O     . PRO C 1 490 ? 70.881  17.472  70.402  1.000 28.316  0 490 PRO CCC O     1 ? 3 
ATOM   11138 C CB    . PRO C 1 490 ? 73.267  18.834  69.397  1.000 28.656  0 490 PRO CCC CB    1 ? 3 
ATOM   11139 C CG    . PRO C 1 490 ? 74.090  18.953  70.687  1.000 29.852  0 490 PRO CCC CG    1 ? 3 
ATOM   11140 C CD    . PRO C 1 490 ? 73.098  19.151  71.813  1.000 29.388  0 490 PRO CCC CD    1 ? 3 
ATOM   11141 N N     . THR C 1 491 ? 69.770  18.685  68.852  1.000 26.715  0 491 THR CCC N     1 ? 3 
ATOM   11142 C CA    . THR C 1 491 ? 68.690  17.702  68.577  1.000 26.016  0 491 THR CCC CA    1 ? 3 
ATOM   11143 C C     . THR C 1 491 ? 68.446  17.647  67.074  1.000 24.925  0 491 THR CCC C     1 ? 3 
ATOM   11144 O O     . THR C 1 491 ? 68.928  18.511  66.382  1.000 23.965  0 491 THR CCC O     1 ? 3 
ATOM   11145 C CB    . THR C 1 491 ? 67.387  18.043  69.331  1.000 25.583  0 491 THR CCC CB    1 ? 3 
ATOM   11146 O OG1   . THR C 1 491 ? 66.825  19.247  68.805  1.000 25.633  0 491 THR CCC OG1   1 ? 3 
ATOM   11147 C CG2   . THR C 1 491 ? 67.608  18.200  70.819  1.000 25.180  0 491 THR CCC CG2   1 ? 3 
ATOM   11148 N N     . ASP C 1 492 ? 67.698  16.656  66.621  1.000 26.225  0 492 ASP CCC N     1 ? 3 
ATOM   11149 C CA    . ASP C 1 492 ? 67.128  16.652  65.248  1.000 27.330  0 492 ASP CCC CA    1 ? 3 
ATOM   11150 C C     . ASP C 1 492 ? 65.880  17.540  65.217  1.000 27.616  0 492 ASP CCC C     1 ? 3 
ATOM   11151 O O     . ASP C 1 492 ? 65.667  18.188  64.179  1.000 29.002  0 492 ASP CCC O     1 ? 3 
ATOM   11152 C CB    . ASP C 1 492 ? 66.871  15.229  64.796  1.000 27.031  0 492 ASP CCC CB    1 ? 3 
ATOM   11153 C CG    . ASP C 1 492 ? 68.128  14.410  64.647  1.000 28.208  0 492 ASP CCC CG    1 ? 3 
ATOM   11154 O OD1   . ASP C 1 492 ? 69.209  15.014  64.439  1.000 30.993  0 492 ASP CCC OD1   1 ? 3 
ATOM   11155 O OD2   . ASP C 1 492 ? 68.025  13.164  64.709  1.000 26.965  0 492 ASP CCC OD2   1 ? 3 
ATOM   11156 N N     . ALA C 1 493 ? 65.110  17.623  66.294  1.000 27.090  0 493 ALA CCC N     1 ? 3 
ATOM   11157 C CA    . ALA C 1 493 ? 63.800  18.321  66.285  1.000 28.153  0 493 ALA CCC CA    1 ? 3 
ATOM   11158 C C     . ALA C 1 493 ? 63.994  19.834  66.173  1.000 28.649  0 493 ALA CCC C     1 ? 3 
ATOM   11159 O O     . ALA C 1 493 ? 63.033  20.507  65.795  1.000 26.959  0 493 ALA CCC O     1 ? 3 
ATOM   11160 C CB    . ALA C 1 493 ? 63.012  17.995  67.540  1.000 28.402  0 493 ALA CCC CB    1 ? 3 
ATOM   11161 N N     . GLU C 1 494 ? 65.182  20.365  66.497  1.000 30.910  0 494 GLU CCC N     1 ? 3 
ATOM   11162 C CA    . GLU C 1 494 ? 65.434  21.837  66.411  1.000 32.961  0 494 GLU CCC CA    1 ? 3 
ATOM   11163 C C     . GLU C 1 494 ? 65.403  22.271  64.943  1.000 32.391  0 494 GLU CCC C     1 ? 3 
ATOM   11164 O O     . GLU C 1 494 ? 65.182  23.470  64.650  1.000 30.698  0 494 GLU CCC O     1 ? 3 
ATOM   11165 C CB    . GLU C 1 494 ? 66.723  22.231  67.122  1.000 36.091  0 494 GLU CCC CB    1 ? 3 
ATOM   11166 C CG    . GLU C 1 494 ? 67.974  21.755  66.444  1.000 39.253  0 494 GLU CCC CG    1 ? 3 
ATOM   11167 C CD    . GLU C 1 494 ? 69.255  22.315  67.060  1.000 43.745  0 494 GLU CCC CD    1 ? 3 
ATOM   11168 O OE1   . GLU C 1 494 ? 69.257  23.549  67.385  1.000 42.049  0 494 GLU CCC OE1   1 ? 3 
ATOM   11169 O OE2   . GLU C 1 494 ? 70.256  21.518  67.225  1.000 47.628  0 494 GLU CCC OE2   1 ? 3 
ATOM   11170 N N     . VAL C 1 495 ? 65.555  21.325  64.017  1.000 32.296  0 495 VAL CCC N     1 ? 3 
ATOM   11171 C CA    . VAL C 1 495 ? 65.509  21.652  62.565  1.000 31.910  0 495 VAL CCC CA    1 ? 3 
ATOM   11172 C C     . VAL C 1 495 ? 64.201  22.377  62.244  1.000 30.540  0 495 VAL CCC C     1 ? 3 
ATOM   11173 O O     . VAL C 1 495 ? 64.254  23.324  61.462  1.000 29.245  0 495 VAL CCC O     1 ? 3 
ATOM   11174 C CB    . VAL C 1 495 ? 65.722  20.415  61.679  1.000 32.252  0 495 VAL CCC CB    1 ? 3 
ATOM   11175 C CG1   . VAL C 1 495 ? 64.451  19.574  61.589  1.000 32.715  0 495 VAL CCC CG1   1 ? 3 
ATOM   11176 C CG2   . VAL C 1 495 ? 66.209  20.832  60.297  1.000 31.714  0 495 VAL CCC CG2   1 ? 3 
ATOM   11177 N N     . PHE C 1 496 ? 63.095  22.017  62.894  1.000 31.046  0 496 PHE CCC N     1 ? 3 
ATOM   11178 C CA    . PHE C 1 496 ? 61.754  22.608  62.652  1.000 31.507  0 496 PHE CCC CA    1 ? 3 
ATOM   11179 C C     . PHE C 1 496 ? 61.679  24.108  62.956  1.000 31.496  0 496 PHE CCC C     1 ? 3 
ATOM   11180 O O     . PHE C 1 496 ? 60.646  24.694  62.643  1.000 32.813  0 496 PHE CCC O     1 ? 3 
ATOM   11181 C CB    . PHE C 1 496 ? 60.686  21.851  63.424  1.000 32.064  0 496 PHE CCC CB    1 ? 3 
ATOM   11182 C CG    . PHE C 1 496 ? 60.367  20.573  62.716  1.000 32.657  0 496 PHE CCC CG    1 ? 3 
ATOM   11183 C CD1   . PHE C 1 496 ? 59.622  20.597  61.544  1.000 33.174  0 496 PHE CCC CD1   1 ? 3 
ATOM   11184 C CD2   . PHE C 1 496 ? 60.865  19.373  63.187  1.000 33.531  0 496 PHE CCC CD2   1 ? 3 
ATOM   11185 C CE1   . PHE C 1 496 ? 59.367  19.426  60.865  1.000 34.319  0 496 PHE CCC CE1   1 ? 3 
ATOM   11186 C CE2   . PHE C 1 496 ? 60.622  18.197  62.496  1.000 33.671  0 496 PHE CCC CE2   1 ? 3 
ATOM   11187 C CZ    . PHE C 1 496 ? 59.870  18.225  61.342  1.000 35.138  0 496 PHE CCC CZ    1 ? 3 
ATOM   11188 N N     . GLY C 1 497 ? 62.724  24.705  63.484  1.000 31.858  0 497 GLY CCC N     1 ? 3 
ATOM   11189 C CA    . GLY C 1 497 ? 62.752  26.148  63.761  1.000 35.469  0 497 GLY CCC CA    1 ? 3 
ATOM   11190 C C     . GLY C 1 497 ? 63.536  26.951  62.744  1.000 36.561  0 497 GLY CCC C     1 ? 3 
ATOM   11191 O O     . GLY C 1 497 ? 63.551  28.155  62.874  1.000 41.937  0 497 GLY CCC O     1 ? 3 
ATOM   11192 N N     . ILE C 1 498 ? 64.174  26.322  61.773  1.000 35.426  0 498 ILE CCC N     1 ? 3 
ATOM   11193 C CA    . ILE C 1 498 ? 65.094  27.017  60.830  1.000 38.334  0 498 ILE CCC CA    1 ? 3 
ATOM   11194 C C     . ILE C 1 498 ? 64.859  26.479  59.415  1.000 38.697  0 498 ILE CCC C     1 ? 3 
ATOM   11195 O O     . ILE C 1 498 ? 65.814  26.468  58.629  1.000 39.464  0 498 ILE CCC O     1 ? 3 
ATOM   11196 C CB    . ILE C 1 498 ? 66.563  26.835  61.271  1.000 40.439  0 498 ILE CCC CB    1 ? 3 
ATOM   11197 C CG1   . ILE C 1 498 ? 66.950  25.356  61.321  1.000 41.027  0 498 ILE CCC CG1   1 ? 3 
ATOM   11198 C CG2   . ILE C 1 498 ? 66.827  27.513  62.619  1.000 40.612  0 498 ILE CCC CG2   1 ? 3 
ATOM   11199 C CD1   . ILE C 1 498 ? 68.436  25.092  61.259  1.000 41.509  0 498 ILE CCC CD1   1 ? 3 
ATOM   11200 N N     . LEU C 1 499 ? 63.648  26.017  59.114  1.000 36.253  0 499 LEU CCC N     1 ? 3 
ATOM   11201 C CA    . LEU C 1 499 ? 63.337  25.527  57.765  1.000 37.911  0 499 LEU CCC CA    1 ? 3 
ATOM   11202 C C     . LEU C 1 499 ? 63.158  26.756  56.867  1.000 38.979  0 499 LEU CCC C     1 ? 3 
ATOM   11203 O O     . LEU C 1 499 ? 62.438  27.678  57.312  1.000 41.236  0 499 LEU CCC O     1 ? 3 
ATOM   11204 C CB    . LEU C 1 499 ? 62.077  24.662  57.832  1.000 37.078  0 499 LEU CCC CB    1 ? 3 
ATOM   11205 C CG    . LEU C 1 499 ? 62.205  23.311  58.532  1.000 35.899  0 499 LEU CCC CG    1 ? 3 
ATOM   11206 C CD1   . LEU C 1 499 ? 60.827  22.727  58.746  1.000 35.371  0 499 LEU CCC CD1   1 ? 3 
ATOM   11207 C CD2   . LEU C 1 499 ? 63.076  22.342  57.731  1.000 37.082  0 499 LEU CCC CD2   1 ? 3 
ATOM   11208 N N     . GLU C 1 500 ? 63.808  26.802  55.700  1.000 39.898  0 500 GLU CCC N     1 ? 3 
ATOM   11209 C CA    . GLU C 1 500 ? 63.724  28.006  54.822  1.000 45.619  0 500 GLU CCC CA    1 ? 3 
ATOM   11210 C C     . GLU C 1 500 ? 63.587  27.659  53.336  1.000 45.123  0 500 GLU CCC C     1 ? 3 
ATOM   11211 O O     . GLU C 1 500 ? 63.045  28.492  52.617  1.000 45.937  0 500 GLU CCC O     1 ? 3 
ATOM   11212 C CB    . GLU C 1 500 ? 64.917  28.937  55.046  1.000 50.113  0 500 GLU CCC CB    1 ? 3 
ATOM   11213 C CG    . GLU C 1 500 ? 66.274  28.271  54.921  1.000 53.130  0 500 GLU CCC CG    1 ? 3 
ATOM   11214 C CD    . GLU C 1 500 ? 67.397  29.103  55.512  1.000 56.980  0 500 GLU CCC CD    1 ? 3 
ATOM   11215 O OE1   . GLU C 1 500 ? 67.127  30.275  55.928  1.000 56.915  0 500 GLU CCC OE1   1 ? 3 
ATOM   11216 O OE2   . GLU C 1 500 ? 68.536  28.578  55.564  1.000 59.395  0 500 GLU CCC OE2   1 ? 3 
ATOM   11217 N N     . VAL C 1 501 ? 64.035  26.484  52.900  1.000 45.655  0 501 VAL CCC N     1 ? 3 
ATOM   11218 C CA    . VAL C 1 501 ? 63.995  26.065  51.473  1.000 44.939  0 501 VAL CCC CA    1 ? 3 
ATOM   11219 C C     . VAL C 1 501 ? 62.585  25.569  51.179  1.000 46.944  0 501 VAL CCC C     1 ? 3 
ATOM   11220 O O     . VAL C 1 501 ? 62.065  24.795  51.981  1.000 48.274  0 501 VAL CCC O     1 ? 3 
ATOM   11221 C CB    . VAL C 1 501 ? 65.054  24.991  51.173  1.000 43.601  0 501 VAL CCC CB    1 ? 3 
ATOM   11222 C CG1   . VAL C 1 501 ? 64.967  24.490  49.737  1.000 41.928  0 501 VAL CCC CG1   1 ? 3 
ATOM   11223 C CG2   . VAL C 1 501 ? 66.456  25.513  51.483  1.000 43.997  0 501 VAL CCC CG2   1 ? 3 
ATOM   11224 N N     . THR C 1 502 ? 61.976  26.027  50.087  1.000 49.347  0 502 THR CCC N     1 ? 3 
ATOM   11225 C CA    . THR C 1 502 ? 60.620  25.590  49.666  1.000 50.314  0 502 THR CCC CA    1 ? 3 
ATOM   11226 C C     . THR C 1 502 ? 60.789  24.631  48.483  1.000 51.013  0 502 THR CCC C     1 ? 3 
ATOM   11227 O O     . THR C 1 502 ? 61.803  24.750  47.773  1.000 50.222  0 502 THR CCC O     1 ? 3 
ATOM   11228 C CB    . THR C 1 502 ? 59.728  26.802  49.369  1.000 51.043  0 502 THR CCC CB    1 ? 3 
ATOM   11229 O OG1   . THR C 1 502 ? 60.159  27.354  48.122  1.000 52.121  0 502 THR CCC OG1   1 ? 3 
ATOM   11230 C CG2   . THR C 1 502 ? 59.775  27.847  50.464  1.000 49.146  0 502 THR CCC CG2   1 ? 3 
ATOM   11231 N N     . LYS C 1 503 ? 59.884  23.666  48.332  1.000 52.936  0 503 LYS CCC N     1 ? 3 
ATOM   11232 C CA    . LYS C 1 503 ? 59.798  22.828  47.115  1.000 55.771  0 503 LYS CCC CA    1 ? 3 
ATOM   11233 C C     . LYS C 1 503 ? 59.699  23.771  45.914  1.000 58.090  0 503 LYS CCC C     1 ? 3 
ATOM   11234 O O     . LYS C 1 503 ? 60.585  23.686  45.028  1.000 59.179  0 503 LYS CCC O     1 ? 3 
ATOM   11235 C CB    . LYS C 1 503 ? 58.606  21.867  47.168  1.000 57.478  0 503 LYS CCC CB    1 ? 3 
ATOM   11236 C CG    . LYS C 1 503 ? 58.592  20.864  46.026  1.000 60.055  0 503 LYS CCC CG    1 ? 3 
ATOM   11237 C CD    . LYS C 1 503 ? 57.636  19.725  46.175  1.000 61.943  0 503 LYS CCC CD    1 ? 3 
ATOM   11238 C CE    . LYS C 1 503 ? 57.934  18.651  45.152  1.000 65.722  0 503 LYS CCC CE    1 ? 3 
ATOM   11239 N NZ    . LYS C 1 503 ? 57.353  17.339  45.526  1.000 66.325  0 503 LYS CCC NZ    1 ? 3 
ATOM   11240 N N     . ARG C 1 504 ? 58.713  24.675  45.929  1.000 59.426  0 504 ARG CCC N     1 ? 3 
ATOM   11241 C CA    . ARG C 1 504 ? 58.465  25.664  44.842  1.000 63.375  0 504 ARG CCC CA    1 ? 3 
ATOM   11242 C C     . ARG C 1 504 ? 59.786  26.323  44.409  1.000 64.866  0 504 ARG CCC C     1 ? 3 
ATOM   11243 O O     . ARG C 1 504 ? 60.011  26.399  43.186  1.000 66.041  0 504 ARG CCC O     1 ? 3 
ATOM   11244 C CB    . ARG C 1 504 ? 57.450  26.726  45.271  1.000 62.590  0 504 ARG CCC CB    1 ? 3 
ATOM   11245 C CG    . ARG C 1 504 ? 57.355  27.912  44.319  1.000 62.359  0 504 ARG CCC CG    1 ? 3 
ATOM   11246 C CD    . ARG C 1 504 ? 56.193  28.854  44.577  1.000 63.174  0 504 ARG CCC CD    1 ? 3 
ATOM   11247 N NE    . ARG C 1 504 ? 54.909  28.162  44.465  1.000 64.683  0 504 ARG CCC NE    1 ? 3 
ATOM   11248 C CZ    . ARG C 1 504 ? 54.011  28.058  45.439  1.000 66.465  0 504 ARG CCC CZ    1 ? 3 
ATOM   11249 N NH1   . ARG C 1 504 ? 54.228  28.607  46.623  1.000 69.833  0 504 ARG CCC NH1   1 ? 3 
ATOM   11250 N NH2   . ARG C 1 504 ? 52.900  27.383  45.229  1.000 68.073  0 504 ARG CCC NH2   1 ? 3 
ATOM   11251 N N     . SER C 1 505 ? 60.622  26.777  45.350  1.000 62.908  0 505 SER CCC N     1 ? 3 
ATOM   11252 C CA    . SER C 1 505 ? 61.908  27.473  45.050  1.000 62.982  0 505 SER CCC CA    1 ? 3 
ATOM   11253 C C     . SER C 1 505 ? 62.805  26.597  44.157  1.000 60.870  0 505 SER CCC C     1 ? 3 
ATOM   11254 O O     . SER C 1 505 ? 63.684  27.173  43.502  1.000 61.897  0 505 SER CCC O     1 ? 3 
ATOM   11255 C CB    . SER C 1 505 ? 62.652  27.891  46.300  1.000 61.557  0 505 SER CCC CB    1 ? 3 
ATOM   11256 O OG    . SER C 1 505 ? 63.387  26.802  46.828  1.000 62.110  0 505 SER CCC OG    1 ? 3 
ATOM   11257 N N     . GLY C 1 506 ? 62.629  25.269  44.162  1.000 58.038  0 506 GLY CCC N     1 ? 3 
ATOM   11258 C CA    . GLY C 1 506 ? 63.463  24.303  43.408  1.000 58.249  0 506 GLY CCC CA    1 ? 3 
ATOM   11259 C C     . GLY C 1 506 ? 64.919  24.253  43.882  1.000 56.417  0 506 GLY CCC C     1 ? 3 
ATOM   11260 O O     . GLY C 1 506 ? 65.717  23.508  43.289  1.000 52.662  0 506 GLY CCC O     1 ? 3 
ATOM   11261 N N     . GLU C 1 507 ? 65.271  25.013  44.915  1.000 58.723  0 507 GLU CCC N     1 ? 3 
ATOM   11262 C CA    . GLU C 1 507 ? 66.647  25.025  45.493  1.000 61.737  0 507 GLU CCC CA    1 ? 3 
ATOM   11263 C C     . GLU C 1 507 ? 66.904  23.707  46.258  1.000 58.625  0 507 GLU CCC C     1 ? 3 
ATOM   11264 O O     . GLU C 1 507 ? 65.910  22.968  46.591  1.000 56.785  0 507 GLU CCC O     1 ? 3 
ATOM   11265 C CB    . GLU C 1 507 ? 66.838  26.269  46.360  1.000 66.556  0 507 GLU CCC CB    1 ? 3 
ATOM   11266 C CG    . GLU C 1 507 ? 66.969  27.554  45.553  1.000 73.261  0 507 GLU CCC CG    1 ? 3 
ATOM   11267 C CD    . GLU C 1 507 ? 67.049  28.837  46.375  1.000 81.225  0 507 GLU CCC CD    1 ? 3 
ATOM   11268 O OE1   . GLU C 1 507 ? 66.135  29.096  47.219  1.000 85.839  0 507 GLU CCC OE1   1 ? 3 
ATOM   11269 O OE2   . GLU C 1 507 ? 68.029  29.584  46.171  1.000 85.092  0 507 GLU CCC OE2   1 ? 3 
ATOM   11270 N N     . SER C 1 508 ? 68.180  23.389  46.487  1.000 52.792  0 508 SER CCC N     1 ? 3 
ATOM   11271 C CA    . SER C 1 508 ? 68.653  22.182  47.229  1.000 51.572  0 508 SER CCC CA    1 ? 3 
ATOM   11272 C C     . SER C 1 508 ? 68.221  22.276  48.702  1.000 46.255  0 508 SER CCC C     1 ? 3 
ATOM   11273 O O     . SER C 1 508 ? 68.515  23.312  49.333  1.000 43.072  0 508 SER CCC O     1 ? 3 
ATOM   11274 C CB    . SER C 1 508 ? 70.171  22.019  47.132  1.000 49.908  0 508 SER CCC CB    1 ? 3 
ATOM   11275 O OG    . SER C 1 508 ? 70.601  20.930  47.929  1.000 49.423  0 508 SER CCC OG    1 ? 3 
ATOM   11276 N N     . PHE C 1 509 ? 67.540  21.248  49.213  1.000 44.457  0 509 PHE CCC N     1 ? 3 
ATOM   11277 C CA    . PHE C 1 509 ? 67.078  21.176  50.626  1.000 43.990  0 509 PHE CCC CA    1 ? 3 
ATOM   11278 C C     . PHE C 1 509 ? 68.042  20.288  51.434  1.000 45.453  0 509 PHE CCC C     1 ? 3 
ATOM   11279 O O     . PHE C 1 509 ? 67.866  20.141  52.656  1.000 46.565  0 509 PHE CCC O     1 ? 3 
ATOM   11280 C CB    . PHE C 1 509 ? 65.604  20.761  50.715  1.000 40.826  0 509 PHE CCC CB    1 ? 3 
ATOM   11281 C CG    . PHE C 1 509 ? 65.236  19.488  50.015  1.000 40.168  0 509 PHE CCC CG    1 ? 3 
ATOM   11282 C CD1   . PHE C 1 509 ? 65.462  18.266  50.619  1.000 39.333  0 509 PHE CCC CD1   1 ? 3 
ATOM   11283 C CD2   . PHE C 1 509 ? 64.683  19.506  48.737  1.000 39.708  0 509 PHE CCC CD2   1 ? 3 
ATOM   11284 C CE1   . PHE C 1 509 ? 65.097  17.083  49.983  1.000 40.219  0 509 PHE CCC CE1   1 ? 3 
ATOM   11285 C CE2   . PHE C 1 509 ? 64.376  18.324  48.083  1.000 39.716  0 509 PHE CCC CE2   1 ? 3 
ATOM   11286 C CZ    . PHE C 1 509 ? 64.569  17.112  48.710  1.000 39.446  0 509 PHE CCC CZ    1 ? 3 
ATOM   11287 N N     . VAL C 1 510 ? 69.087  19.771  50.798  1.000 49.912  0 510 VAL CCC N     1 ? 3 
ATOM   11288 C CA    . VAL C 1 510 ? 70.199  19.064  51.499  1.000 51.880  0 510 VAL CCC CA    1 ? 3 
ATOM   11289 C C     . VAL C 1 510 ? 71.037  20.086  52.284  1.000 53.657  0 510 VAL CCC C     1 ? 3 
ATOM   11290 O O     . VAL C 1 510 ? 71.263  21.207  51.759  1.000 48.049  0 510 VAL CCC O     1 ? 3 
ATOM   11291 C CB    . VAL C 1 510 ? 71.066  18.267  50.505  1.000 52.048  0 510 VAL CCC CB    1 ? 3 
ATOM   11292 C CG1   . VAL C 1 510 ? 72.315  17.698  51.169  1.000 51.509  0 510 VAL CCC CG1   1 ? 3 
ATOM   11293 C CG2   . VAL C 1 510 ? 70.250  17.171  49.830  1.000 53.164  0 510 VAL CCC CG2   1 ? 3 
ATOM   11294 N N     . SER C 1 511 ? 71.414  19.726  53.519  1.000 56.673  0 511 SER CCC N     1 ? 3 
ATOM   11295 C CA    . SER C 1 511 ? 72.439  20.415  54.327  1.000 59.707  0 511 SER CCC CA    1 ? 3 
ATOM   11296 C C     . SER C 1 511 ? 73.552  19.410  54.624  1.000 64.158  0 511 SER CCC C     1 ? 3 
ATOM   11297 O O     . SER C 1 511 ? 73.245  18.325  55.151  1.000 58.851  0 511 SER CCC O     1 ? 3 
ATOM   11298 C CB    . SER C 1 511 ? 71.827  21.019  55.547  1.000 61.023  0 511 SER CCC CB    1 ? 3 
ATOM   11299 O OG    . SER C 1 511 ? 70.898  22.016  55.149  1.000 59.770  0 511 SER CCC OG    1 ? 3 
ATOM   11300 N N     . SER C 1 512 ? 74.782  19.765  54.227  1.000 76.011  0 512 SER CCC N     1 ? 3 
ATOM   11301 C CA    . SER C 1 512 ? 75.973  18.873  54.171  1.000 83.576  0 512 SER CCC CA    1 ? 3 
ATOM   11302 C C     . SER C 1 512 ? 76.797  18.989  55.465  1.000 87.798  0 512 SER CCC C     1 ? 3 
ATOM   11303 O O     . SER C 1 512 ? 77.353  17.950  55.892  1.000 84.465  0 512 SER CCC O     1 ? 3 
ATOM   11304 C CB    . SER C 1 512 ? 76.826  19.166  52.946  1.000 84.285  0 512 SER CCC CB    1 ? 3 
ATOM   11305 O OG    . SER C 1 512 ? 76.130  18.863  51.733  1.000 87.110  0 512 SER CCC OG    1 ? 3 
ATOM   11306 N N     . GLY C 1 513 ? 76.897  20.189  56.057  1.000 89.283  0 513 GLY CCC N     1 ? 3 
ATOM   11307 C CA    . GLY C 1 513 ? 77.553  20.406  57.366  1.000 91.977  0 513 GLY CCC CA    1 ? 3 
ATOM   11308 C C     . GLY C 1 513 ? 76.843  19.617  58.461  1.000 96.441  0 513 GLY CCC C     1 ? 3 
ATOM   11309 O O     . GLY C 1 513 ? 75.594  19.490  58.370  1.000 97.554  0 513 GLY CCC O     1 ? 3 
ATOM   11310 N N     . GLY C 1 514 ? 77.584  19.092  59.450  1.000 91.055  0 514 GLY CCC N     1 ? 3 
ATOM   11311 C CA    . GLY C 1 514 ? 77.074  18.087  60.405  1.000 85.834  0 514 GLY CCC CA    1 ? 3 
ATOM   11312 C C     . GLY C 1 514 ? 76.893  18.648  61.806  1.000 83.055  0 514 GLY CCC C     1 ? 3 
ATOM   11313 O O     . GLY C 1 514 ? 77.443  18.041  62.737  1.000 82.595  0 514 GLY CCC O     1 ? 3 
ATOM   11314 N N     . CYS C 1 515 ? 76.142  19.749  61.968  1.000 81.002  0 515 CYS CCC N     1 ? 3 
ATOM   11315 C CA    . CYS C 1 515 ? 75.711  20.296  63.296  1.000 79.962  0 515 CYS CCC CA    1 ? 3 
ATOM   11316 C C     . CYS C 1 515 ? 74.366  19.654  63.685  1.000 73.887  0 515 CYS CCC C     1 ? 3 
ATOM   11317 O O     . CYS C 1 515 ? 73.734  20.125  64.665  1.000 75.141  0 515 CYS CCC O     1 ? 3 
ATOM   11318 C CB    . CYS C 1 515 ? 75.647  21.833  63.338  1.000 79.997  0 515 CYS CCC CB    1 ? 3 
ATOM   11319 S SG    . CYS C 1 515 ? 77.090  22.643  64.117  1.000 85.636  0 515 CYS CCC SG    1 ? 3 
ATOM   11320 N N     . GLY C 1 516 ? 73.957  18.599  62.984  1.000 70.274  0 516 GLY CCC N     1 ? 3 
ATOM   11321 C CA    . GLY C 1 516 ? 72.691  17.887  63.232  1.000 73.016  0 516 GLY CCC CA    1 ? 3 
ATOM   11322 C C     . GLY C 1 516 ? 71.504  18.679  62.695  1.000 73.163  0 516 GLY CCC C     1 ? 3 
ATOM   11323 O O     . GLY C 1 516 ? 71.598  19.192  61.552  1.000 65.799  0 516 GLY CCC O     1 ? 3 
ATOM   11324 N N     . GLY C 1 517 ? 70.441  18.799  63.500  1.000 73.893  0 517 GLY CCC N     1 ? 3 
ATOM   11325 C CA    . GLY C 1 517 ? 69.209  19.521  63.144  1.000 73.416  0 517 GLY CCC CA    1 ? 3 
ATOM   11326 C C     . GLY C 1 517 ? 69.372  21.032  63.107  1.000 75.577  0 517 GLY CCC C     1 ? 3 
ATOM   11327 O O     . GLY C 1 517 ? 68.478  21.687  62.547  1.000 68.417  0 517 GLY CCC O     1 ? 3 
ATOM   11328 N N     . GLY C 1 518 ? 70.404  21.605  63.735  1.000 79.827  0 518 GLY CCC N     1 ? 3 
ATOM   11329 C CA    . GLY C 1 518 ? 70.401  23.038  64.098  1.000 79.589  0 518 GLY CCC CA    1 ? 3 
ATOM   11330 C C     . GLY C 1 518 ? 71.423  23.836  63.320  1.000 82.882  0 518 GLY CCC C     1 ? 3 
ATOM   11331 O O     . GLY C 1 518 ? 71.702  23.497  62.139  1.000 82.050  0 518 GLY CCC O     1 ? 3 
ATOM   11332 N N     . LYS C 1 519 ? 71.892  24.919  63.927  1.000 85.239  0 519 LYS CCC N     1 ? 3 
ATOM   11333 C CA    . LYS C 1 519 ? 73.178  25.542  63.546  1.000 84.887  0 519 LYS CCC CA    1 ? 3 
ATOM   11334 C C     . LYS C 1 519 ? 73.855  26.013  64.825  1.000 79.255  0 519 LYS CCC C     1 ? 3 
ATOM   11335 O O     . LYS C 1 519 ? 73.186  26.649  65.638  1.000 75.645  0 519 LYS CCC O     1 ? 3 
ATOM   11336 C CB    . LYS C 1 519 ? 73.017  26.641  62.493  1.000 87.358  0 519 LYS CCC CB    1 ? 3 
ATOM   11337 C CG    . LYS C 1 519 ? 71.945  27.699  62.719  1.000 89.103  0 519 LYS CCC CG    1 ? 3 
ATOM   11338 C CD    . LYS C 1 519 ? 71.284  28.096  61.393  1.000 91.639  0 519 LYS CCC CD    1 ? 3 
ATOM   11339 C CE    . LYS C 1 519 ? 70.940  29.567  61.243  1.000 90.502  0 519 LYS CCC CE    1 ? 3 
ATOM   11340 N NZ    . LYS C 1 519 ? 69.543  29.860  61.631  1.000 87.081  0 519 LYS CCC NZ    1 ? 3 
ATOM   11341 N N     . CYS C 1 520 ? 75.110  25.591  65.000  0.900 75.593  0 520 CYS CCC N     1 ? 3 
ATOM   11342 C CA    A CYS C 1 520 ? 76.065  26.102  66.012  0.500 76.875  0 520 CYS CCC CA    1 ? 3 
ATOM   11343 C CA    B CYS C 1 520 ? 76.031  26.137  66.047  0.500 72.328  0 520 CYS CCC CA    1 ? 3 
ATOM   11344 C C     . CYS C 1 520 ? 76.489  27.531  65.625  0.900 74.508  0 520 CYS CCC C     1 ? 3 
ATOM   11345 O O     . CYS C 1 520 ? 77.169  28.191  66.439  0.900 70.441  0 520 CYS CCC O     1 ? 3 
ATOM   11346 C CB    A CYS C 1 520 ? 77.224  25.110  66.091  0.500 75.304  0 520 CYS CCC CB    1 ? 3 
ATOM   11347 C CB    B CYS C 1 520 ? 77.311  25.337  66.291  0.500 64.653  0 520 CYS CCC CB    1 ? 3 
ATOM   11348 S SG    A CYS C 1 520 ? 76.646  23.386  65.990  0.500 71.510  0 520 CYS CCC SG    1 ? 3 
ATOM   11349 S SG    B CYS C 1 520 ? 77.139  23.966  67.458  0.500 57.638  0 520 CYS CCC SG    1 ? 3 
ATOM   11350 N N     . GLY C 1 521 ? 76.130  27.944  64.404  1.000 75.672  0 521 GLY CCC N     1 ? 3 
ATOM   11351 C CA    . GLY C 1 521 ? 76.360  29.289  63.837  1.000 78.843  0 521 GLY CCC CA    1 ? 3 
ATOM   11352 C C     . GLY C 1 521 ? 76.082  29.323  62.337  1.000 79.323  0 521 GLY CCC C     1 ? 3 
ATOM   11353 O O     . GLY C 1 521 ? 75.576  28.355  61.750  1.000 77.690  0 521 GLY CCC O     1 ? 3 
ATOM   11354 O OXT   . GLY C 1 521 ? 76.357  30.322  61.672  1.000 77.369  0 521 GLY CCC OXT   1 ? 3 
ATOM   11355 N N     . LEU D 1 24  ? 79.292  57.144  55.161  1.000 114.092 0 24  LEU DDD N     1 ? 4 
ATOM   11356 C CA    . LEU D 1 24  ? 80.425  56.161  55.080  1.000 112.522 0 24  LEU DDD CA    1 ? 4 
ATOM   11357 C C     . LEU D 1 24  ? 81.702  56.806  55.646  1.000 112.665 0 24  LEU DDD C     1 ? 4 
ATOM   11358 O O     . LEU D 1 24  ? 82.794  56.575  55.087  1.000 109.532 0 24  LEU DDD O     1 ? 4 
ATOM   11359 C CB    . LEU D 1 24  ? 80.612  55.700  53.625  1.000 111.414 0 24  LEU DDD CB    1 ? 4 
ATOM   11360 C CG    . LEU D 1 24  ? 79.726  54.552  53.120  1.000 109.189 0 24  LEU DDD CG    1 ? 4 
ATOM   11361 C CD1   . LEU D 1 24  ? 79.820  53.313  54.010  1.000 105.547 0 24  LEU DDD CD1   1 ? 4 
ATOM   11362 C CD2   . LEU D 1 24  ? 78.273  54.984  52.938  1.000 107.659 0 24  LEU DDD CD2   1 ? 4 
ATOM   11363 N N     . THR D 1 25  ? 81.587  57.548  56.758  1.000 114.710 0 25  THR DDD N     1 ? 4 
ATOM   11364 C CA    . THR D 1 25  ? 82.723  57.873  57.672  1.000 115.001 0 25  THR DDD CA    1 ? 4 
ATOM   11365 C C     . THR D 1 25  ? 83.092  56.623  58.501  1.000 111.990 0 25  THR DDD C     1 ? 4 
ATOM   11366 O O     . THR D 1 25  ? 83.788  56.777  59.514  1.000 104.677 0 25  THR DDD O     1 ? 4 
ATOM   11367 C CB    . THR D 1 25  ? 82.389  59.095  58.541  1.000 118.000 0 25  THR DDD CB    1 ? 4 
ATOM   11368 O OG1   . THR D 1 25  ? 81.102  58.877  59.120  1.000 117.179 0 25  THR DDD OG1   1 ? 4 
ATOM   11369 C CG2   . THR D 1 25  ? 82.378  60.392  57.761  1.000 117.894 0 25  THR DDD CG2   1 ? 4 
ATOM   11370 N N     . PHE D 1 26  ? 82.661  55.427  58.077  1.000 113.032 0 26  PHE DDD N     1 ? 4 
ATOM   11371 C CA    . PHE D 1 26  ? 82.964  54.111  58.696  1.000 111.437 0 26  PHE DDD CA    1 ? 4 
ATOM   11372 C C     . PHE D 1 26  ? 83.408  53.119  57.612  1.000 107.616 0 26  PHE DDD C     1 ? 4 
ATOM   11373 O O     . PHE D 1 26  ? 82.668  52.925  56.611  1.000 104.274 0 26  PHE DDD O     1 ? 4 
ATOM   11374 C CB    . PHE D 1 26  ? 81.743  53.570  59.439  1.000 111.196 0 26  PHE DDD CB    1 ? 4 
ATOM   11375 C CG    . PHE D 1 26  ? 81.178  54.510  60.473  1.000 112.997 0 26  PHE DDD CG    1 ? 4 
ATOM   11376 C CD1   . PHE D 1 26  ? 81.939  54.899  61.565  1.000 112.126 0 26  PHE DDD CD1   1 ? 4 
ATOM   11377 C CD2   . PHE D 1 26  ? 79.892  55.018  60.345  1.000 116.753 0 26  PHE DDD CD2   1 ? 4 
ATOM   11378 C CE1   . PHE D 1 26  ? 81.423  55.769  62.516  1.000 115.944 0 26  PHE DDD CE1   1 ? 4 
ATOM   11379 C CE2   . PHE D 1 26  ? 79.375  55.886  61.297  1.000 118.981 0 26  PHE DDD CE2   1 ? 4 
ATOM   11380 C CZ    . PHE D 1 26  ? 80.142  56.260  62.382  1.000 117.662 0 26  PHE DDD CZ    1 ? 4 
ATOM   11381 N N     . MET D 1 27  ? 84.566  52.479  57.825  1.000 100.310 0 27  MET DDD N     1 ? 4 
ATOM   11382 C CA    . MET D 1 27  ? 85.096  51.405  56.943  1.000 94.070  0 27  MET DDD CA    1 ? 4 
ATOM   11383 C C     . MET D 1 27  ? 84.056  50.283  56.843  1.000 85.866  0 27  MET DDD C     1 ? 4 
ATOM   11384 O O     . MET D 1 27  ? 83.807  49.815  55.718  1.000 79.209  0 27  MET DDD O     1 ? 4 
ATOM   11385 C CB    . MET D 1 27  ? 86.424  50.844  57.465  1.000 95.015  0 27  MET DDD CB    1 ? 4 
ATOM   11386 C CG    . MET D 1 27  ? 87.571  51.840  57.353  1.000 98.466  0 27  MET DDD CG    1 ? 4 
ATOM   11387 S SD    . MET D 1 27  ? 89.059  51.376  58.288  1.000 103.769 0 27  MET DDD SD    1 ? 4 
ATOM   11388 C CE    . MET D 1 27  ? 89.702  50.055  57.260  1.000 100.873 0 27  MET DDD CE    1 ? 4 
ATOM   11389 N N     . TYR D 1 28  ? 83.443  49.888  57.966  1.000 81.899  0 28  TYR DDD N     1 ? 4 
ATOM   11390 C CA    . TYR D 1 28  ? 82.488  48.746  58.028  1.000 76.024  0 28  TYR DDD CA    1 ? 4 
ATOM   11391 C C     . TYR D 1 28  ? 81.116  49.196  58.540  1.000 72.472  0 28  TYR DDD C     1 ? 4 
ATOM   11392 O O     . TYR D 1 28  ? 81.027  50.205  59.259  1.000 69.145  0 28  TYR DDD O     1 ? 4 
ATOM   11393 C CB    . TYR D 1 28  ? 83.043  47.632  58.917  1.000 71.928  0 28  TYR DDD CB    1 ? 4 
ATOM   11394 C CG    . TYR D 1 28  ? 84.287  46.969  58.388  1.000 69.629  0 28  TYR DDD CG    1 ? 4 
ATOM   11395 C CD1   . TYR D 1 28  ? 85.541  47.509  58.639  1.000 68.155  0 28  TYR DDD CD1   1 ? 4 
ATOM   11396 C CD2   . TYR D 1 28  ? 84.206  45.794  57.655  1.000 65.522  0 28  TYR DDD CD2   1 ? 4 
ATOM   11397 C CE1   . TYR D 1 28  ? 86.692  46.906  58.158  1.000 64.176  0 28  TYR DDD CE1   1 ? 4 
ATOM   11398 C CE2   . TYR D 1 28  ? 85.347  45.189  57.168  1.000 63.030  0 28  TYR DDD CE2   1 ? 4 
ATOM   11399 C CZ    . TYR D 1 28  ? 86.590  45.746  57.416  1.000 61.902  0 28  TYR DDD CZ    1 ? 4 
ATOM   11400 O OH    . TYR D 1 28  ? 87.709  45.130  56.942  1.000 61.196  0 28  TYR DDD OH    1 ? 4 
ATOM   11401 N N     . ASP D 1 29  ? 80.075  48.438  58.181  1.000 71.441  0 29  ASP DDD N     1 ? 4 
ATOM   11402 C CA    . ASP D 1 29  ? 78.702  48.575  58.734  1.000 70.729  0 29  ASP DDD CA    1 ? 4 
ATOM   11403 C C     . ASP D 1 29  ? 78.654  47.859  60.088  1.000 70.721  0 29  ASP DDD C     1 ? 4 
ATOM   11404 O O     . ASP D 1 29  ? 78.019  48.400  61.026  1.000 74.359  0 29  ASP DDD O     1 ? 4 
ATOM   11405 C CB    . ASP D 1 29  ? 77.658  48.043  57.749  1.000 72.953  0 29  ASP DDD CB    1 ? 4 
ATOM   11406 C CG    . ASP D 1 29  ? 77.569  48.858  56.472  1.000 74.737  0 29  ASP DDD CG    1 ? 4 
ATOM   11407 O OD1   . ASP D 1 29  ? 77.038  49.980  56.554  1.000 74.029  0 29  ASP DDD OD1   1 ? 4 
ATOM   11408 O OD2   . ASP D 1 29  ? 78.033  48.357  55.408  1.000 77.832  0 29  ASP DDD OD2   1 ? 4 
ATOM   11409 N N     . LEU D 1 30  ? 79.335  46.711  60.183  1.000 68.567  0 30  LEU DDD N     1 ? 4 
ATOM   11410 C CA    . LEU D 1 30  ? 79.299  45.804  61.354  1.000 65.772  0 30  LEU DDD CA    1 ? 4 
ATOM   11411 C C     . LEU D 1 30  ? 80.634  45.078  61.531  1.000 63.047  0 30  LEU DDD C     1 ? 4 
ATOM   11412 O O     . LEU D 1 30  ? 81.119  44.456  60.559  1.000 57.597  0 30  LEU DDD O     1 ? 4 
ATOM   11413 C CB    . LEU D 1 30  ? 78.176  44.790  61.165  1.000 66.577  0 30  LEU DDD CB    1 ? 4 
ATOM   11414 C CG    . LEU D 1 30  ? 78.075  43.747  62.270  1.000 67.001  0 30  LEU DDD CG    1 ? 4 
ATOM   11415 C CD1   . LEU D 1 30  ? 77.638  44.388  63.582  1.000 67.224  0 30  LEU DDD CD1   1 ? 4 
ATOM   11416 C CD2   . LEU D 1 30  ? 77.115  42.649  61.845  1.000 69.414  0 30  LEU DDD CD2   1 ? 4 
ATOM   11417 N N     . VAL D 1 31  ? 81.181  45.164  62.743  1.000 61.264  0 31  VAL DDD N     1 ? 4 
ATOM   11418 C CA    . VAL D 1 31  ? 82.378  44.395  63.176  1.000 63.844  0 31  VAL DDD CA    1 ? 4 
ATOM   11419 C C     . VAL D 1 31  ? 81.938  43.535  64.353  1.000 61.761  0 31  VAL DDD C     1 ? 4 
ATOM   11420 O O     . VAL D 1 31  ? 81.326  44.083  65.299  1.000 63.817  0 31  VAL DDD O     1 ? 4 
ATOM   11421 C CB    . VAL D 1 31  ? 83.568  45.298  63.552  1.000 66.179  0 31  VAL DDD CB    1 ? 4 
ATOM   11422 C CG1   . VAL D 1 31  ? 84.671  44.505  64.237  1.000 63.436  0 31  VAL DDD CG1   1 ? 4 
ATOM   11423 C CG2   . VAL D 1 31  ? 84.131  46.019  62.343  1.000 69.170  0 31  VAL DDD CG2   1 ? 4 
ATOM   11424 N N     . VAL D 1 32  ? 82.197  42.239  64.252  1.000 59.296  0 32  VAL DDD N     1 ? 4 
ATOM   11425 C CA    . VAL D 1 32  ? 81.792  41.225  65.263  1.000 56.445  0 32  VAL DDD CA    1 ? 4 
ATOM   11426 C C     . VAL D 1 32  ? 83.080  40.729  65.909  1.000 53.175  0 32  VAL DDD C     1 ? 4 
ATOM   11427 O O     . VAL D 1 32  ? 83.961  40.256  65.164  1.000 48.278  0 32  VAL DDD O     1 ? 4 
ATOM   11428 C CB    . VAL D 1 32  ? 80.992  40.079  64.620  1.000 56.353  0 32  VAL DDD CB    1 ? 4 
ATOM   11429 C CG1   . VAL D 1 32  ? 80.608  39.028  65.641  1.000 57.696  0 32  VAL DDD CG1   1 ? 4 
ATOM   11430 C CG2   . VAL D 1 32  ? 79.768  40.591  63.869  1.000 56.461  0 32  VAL DDD CG2   1 ? 4 
ATOM   11431 N N     . ILE D 1 33  ? 83.194  40.873  67.227  1.000 53.737  0 33  ILE DDD N     1 ? 4 
ATOM   11432 C CA    . ILE D 1 33  ? 84.326  40.275  67.985  1.000 57.042  0 33  ILE DDD CA    1 ? 4 
ATOM   11433 C C     . ILE D 1 33  ? 83.865  38.958  68.632  1.000 56.587  0 33  ILE DDD C     1 ? 4 
ATOM   11434 O O     . ILE D 1 33  ? 83.179  38.989  69.681  1.000 57.879  0 33  ILE DDD O     1 ? 4 
ATOM   11435 C CB    . ILE D 1 33  ? 84.912  41.277  68.990  1.000 57.625  0 33  ILE DDD CB    1 ? 4 
ATOM   11436 C CG1   . ILE D 1 33  ? 85.273  42.593  68.296  1.000 60.443  0 33  ILE DDD CG1   1 ? 4 
ATOM   11437 C CG2   . ILE D 1 33  ? 86.114  40.649  69.682  1.000 58.039  0 33  ILE DDD CG2   1 ? 4 
ATOM   11438 C CD1   . ILE D 1 33  ? 85.661  43.712  69.241  1.000 62.367  0 33  ILE DDD CD1   1 ? 4 
ATOM   11439 N N     . GLY D 1 34  ? 84.271  37.837  68.030  1.000 56.346  0 34  GLY DDD N     1 ? 4 
ATOM   11440 C CA    . GLY D 1 34  ? 83.933  36.481  68.490  1.000 53.503  0 34  GLY DDD CA    1 ? 4 
ATOM   11441 C C     . GLY D 1 34  ? 83.250  35.714  67.387  1.000 52.994  0 34  GLY DDD C     1 ? 4 
ATOM   11442 O O     . GLY D 1 34  ? 82.178  36.186  66.887  1.000 57.778  0 34  GLY DDD O     1 ? 4 
ATOM   11443 N N     . GLY D 1 35  ? 83.834  34.578  67.020  1.000 50.189  0 35  GLY DDD N     1 ? 4 
ATOM   11444 C CA    . GLY D 1 35  ? 83.326  33.703  65.958  1.000 51.129  0 35  GLY DDD CA    1 ? 4 
ATOM   11445 C C     . GLY D 1 35  ? 82.746  32.428  66.538  1.000 50.187  0 35  GLY DDD C     1 ? 4 
ATOM   11446 O O     . GLY D 1 35  ? 83.068  31.330  66.024  1.000 51.977  0 35  GLY DDD O     1 ? 4 
ATOM   11447 N N     . GLY D 1 36  ? 81.926  32.558  67.577  1.000 47.280  0 36  GLY DDD N     1 ? 4 
ATOM   11448 C CA    . GLY D 1 36  ? 81.080  31.454  68.063  1.000 49.121  0 36  GLY DDD CA    1 ? 4 
ATOM   11449 C C     . GLY D 1 36  ? 79.641  31.612  67.591  1.000 46.367  0 36  GLY DDD C     1 ? 4 
ATOM   11450 O O     . GLY D 1 36  ? 79.400  32.268  66.566  1.000 42.317  0 36  GLY DDD O     1 ? 4 
ATOM   11451 N N     . SER D 1 37  ? 78.700  31.049  68.337  1.000 47.537  0 37  SER DDD N     1 ? 4 
ATOM   11452 C CA    . SER D 1 37  ? 77.312  30.844  67.869  1.000 46.661  0 37  SER DDD CA    1 ? 4 
ATOM   11453 C C     . SER D 1 37  ? 76.680  32.208  67.579  1.000 48.621  0 37  SER DDD C     1 ? 4 
ATOM   11454 O O     . SER D 1 37  ? 76.069  32.352  66.506  1.000 48.351  0 37  SER DDD O     1 ? 4 
ATOM   11455 C CB    . SER D 1 37  ? 76.540  30.036  68.872  1.000 48.679  0 37  SER DDD CB    1 ? 4 
ATOM   11456 O OG    . SER D 1 37  ? 77.187  28.792  69.111  1.000 47.836  0 37  SER DDD OG    1 ? 4 
ATOM   11457 N N     . GLY D 1 38  ? 76.863  33.175  68.482  1.000 47.970  0 38  GLY DDD N     1 ? 4 
ATOM   11458 C CA    . GLY D 1 38  ? 76.252  34.506  68.380  1.000 47.641  0 38  GLY DDD CA    1 ? 4 
ATOM   11459 C C     . GLY D 1 38  ? 76.862  35.305  67.266  1.000 46.394  0 38  GLY DDD C     1 ? 4 
ATOM   11460 O O     . GLY D 1 38  ? 76.098  35.798  66.448  1.000 44.543  0 38  GLY DDD O     1 ? 4 
ATOM   11461 N N     . GLY D 1 39  ? 78.193  35.404  67.251  1.000 48.304  0 39  GLY DDD N     1 ? 4 
ATOM   11462 C CA    . GLY D 1 39  ? 78.973  36.227  66.306  1.000 50.951  0 39  GLY DDD CA    1 ? 4 
ATOM   11463 C C     . GLY D 1 39  ? 78.792  35.801  64.855  1.000 50.502  0 39  GLY DDD C     1 ? 4 
ATOM   11464 O O     . GLY D 1 39  ? 78.465  36.661  64.017  1.000 52.487  0 39  GLY DDD O     1 ? 4 
ATOM   11465 N N     . MET D 1 40  ? 79.001  34.521  64.550  1.000 50.185  0 40  MET DDD N     1 ? 4 
ATOM   11466 C CA    . MET D 1 40  ? 78.907  34.015  63.157  1.000 52.386  0 40  MET DDD CA    1 ? 4 
ATOM   11467 C C     . MET D 1 40  ? 77.465  34.184  62.659  1.000 52.002  0 40  MET DDD C     1 ? 4 
ATOM   11468 O O     . MET D 1 40  ? 77.283  34.532  61.495  1.000 54.068  0 40  MET DDD O     1 ? 4 
ATOM   11469 C CB    . MET D 1 40  ? 79.356  32.556  63.062  1.000 51.825  0 40  MET DDD CB    1 ? 4 
ATOM   11470 C CG    . MET D 1 40  ? 80.873  32.411  63.169  1.000 52.767  0 40  MET DDD CG    1 ? 4 
ATOM   11471 S SD    . MET D 1 40  ? 81.452  30.774  62.670  1.000 52.986  0 40  MET DDD SD    1 ? 4 
ATOM   11472 C CE    . MET D 1 40  ? 80.408  29.734  63.684  1.000 52.492  0 40  MET DDD CE    1 ? 4 
ATOM   11473 N N     . ALA D 1 41  ? 76.475  34.008  63.526  1.000 50.284  0 41  ALA DDD N     1 ? 4 
ATOM   11474 C CA    . ALA D 1 41  ? 75.046  34.135  63.163  1.000 51.994  0 41  ALA DDD CA    1 ? 4 
ATOM   11475 C C     . ALA D 1 41  ? 74.733  35.601  62.832  1.000 52.918  0 41  ALA DDD C     1 ? 4 
ATOM   11476 O O     . ALA D 1 41  ? 74.172  35.848  61.738  1.000 52.688  0 41  ALA DDD O     1 ? 4 
ATOM   11477 C CB    . ALA D 1 41  ? 74.183  33.617  64.274  1.000 50.895  0 41  ALA DDD CB    1 ? 4 
ATOM   11478 N N     . ALA D 1 42  ? 75.115  36.543  63.700  1.000 51.184  0 42  ALA DDD N     1 ? 4 
ATOM   11479 C CA    . ALA D 1 42  ? 74.911  37.986  63.464  1.000 53.059  0 42  ALA DDD CA    1 ? 4 
ATOM   11480 C C     . ALA D 1 42  ? 75.550  38.384  62.133  1.000 57.007  0 42  ALA DDD C     1 ? 4 
ATOM   11481 O O     . ALA D 1 42  ? 74.827  38.987  61.294  1.000 59.749  0 42  ALA DDD O     1 ? 4 
ATOM   11482 C CB    . ALA D 1 42  ? 75.454  38.806  64.603  1.000 51.975  0 42  ALA DDD CB    1 ? 4 
ATOM   11483 N N     . ALA D 1 43  ? 76.825  38.006  61.947  1.000 58.292  0 43  ALA DDD N     1 ? 4 
ATOM   11484 C CA    . ALA D 1 43  ? 77.727  38.407  60.842  1.000 59.827  0 43  ALA DDD CA    1 ? 4 
ATOM   11485 C C     . ALA D 1 43  ? 77.165  37.971  59.480  1.000 64.717  0 43  ALA DDD C     1 ? 4 
ATOM   11486 O O     . ALA D 1 43  ? 77.068  38.841  58.576  1.000 68.495  0 43  ALA DDD O     1 ? 4 
ATOM   11487 C CB    . ALA D 1 43  ? 79.104  37.838  61.099  1.000 61.937  0 43  ALA DDD CB    1 ? 4 
ATOM   11488 N N     . LYS D 1 44  ? 76.826  36.682  59.324  1.000 68.238  0 44  LYS DDD N     1 ? 4 
ATOM   11489 C CA    . LYS D 1 44  ? 76.263  36.093  58.074  1.000 66.093  0 44  LYS DDD CA    1 ? 4 
ATOM   11490 C C     . LYS D 1 44  ? 74.922  36.745  57.753  1.000 65.264  0 44  LYS DDD C     1 ? 4 
ATOM   11491 O O     . LYS D 1 44  ? 74.659  36.965  56.556  1.000 65.541  0 44  LYS DDD O     1 ? 4 
ATOM   11492 C CB    . LYS D 1 44  ? 76.077  34.576  58.182  1.000 66.267  0 44  LYS DDD CB    1 ? 4 
ATOM   11493 C CG    . LYS D 1 44  ? 77.349  33.769  57.968  1.000 67.705  0 44  LYS DDD CG    1 ? 4 
ATOM   11494 C CD    . LYS D 1 44  ? 77.129  32.267  57.926  1.000 66.844  0 44  LYS DDD CD    1 ? 4 
ATOM   11495 C CE    . LYS D 1 44  ? 77.380  31.587  59.249  1.000 65.301  0 44  LYS DDD CE    1 ? 4 
ATOM   11496 N NZ    . LYS D 1 44  ? 77.632  30.136  59.071  1.000 69.266  0 44  LYS DDD NZ    1 ? 4 
ATOM   11497 N N     . GLU D 1 45  ? 74.088  36.998  58.765  1.000 65.683  0 45  GLU DDD N     1 ? 4 
ATOM   11498 C CA    . GLU D 1 45  ? 72.749  37.608  58.548  1.000 66.052  0 45  GLU DDD CA    1 ? 4 
ATOM   11499 C C     . GLU D 1 45  ? 72.910  39.078  58.123  1.000 65.295  0 45  GLU DDD C     1 ? 4 
ATOM   11500 O O     . GLU D 1 45  ? 72.164  39.509  57.234  1.000 67.339  0 45  GLU DDD O     1 ? 4 
ATOM   11501 C CB    . GLU D 1 45  ? 71.871  37.507  59.787  1.000 66.002  0 45  GLU DDD CB    1 ? 4 
ATOM   11502 C CG    . GLU D 1 45  ? 70.429  37.845  59.486  1.000 68.270  0 45  GLU DDD CG    1 ? 4 
ATOM   11503 C CD    . GLU D 1 45  ? 69.669  36.721  58.797  1.000 71.063  0 45  GLU DDD CD    1 ? 4 
ATOM   11504 O OE1   . GLU D 1 45  ? 70.296  35.713  58.434  1.000 71.627  0 45  GLU DDD OE1   1 ? 4 
ATOM   11505 O OE2   . GLU D 1 45  ? 68.425  36.822  58.686  1.000 73.001  0 45  GLU DDD OE2   1 ? 4 
ATOM   11506 N N     . ALA D 1 46  ? 73.837  39.822  58.727  1.000 61.683  0 46  ALA DDD N     1 ? 4 
ATOM   11507 C CA    . ALA D 1 46  ? 74.118  41.228  58.359  1.000 62.384  0 46  ALA DDD CA    1 ? 4 
ATOM   11508 C C     . ALA D 1 46  ? 74.566  41.264  56.898  1.000 64.100  0 46  ALA DDD C     1 ? 4 
ATOM   11509 O O     . ALA D 1 46  ? 73.971  42.021  56.121  1.000 66.413  0 46  ALA DDD O     1 ? 4 
ATOM   11510 C CB    . ALA D 1 46  ? 75.165  41.813  59.266  1.000 62.842  0 46  ALA DDD CB    1 ? 4 
ATOM   11511 N N     . ALA D 1 47  ? 75.549  40.424  56.553  1.000 65.925  0 47  ALA DDD N     1 ? 4 
ATOM   11512 C CA    . ALA D 1 47  ? 76.173  40.324  55.216  1.000 65.759  0 47  ALA DDD CA    1 ? 4 
ATOM   11513 C C     . ALA D 1 47  ? 75.119  39.978  54.156  1.000 68.084  0 47  ALA DDD C     1 ? 4 
ATOM   11514 O O     . ALA D 1 47  ? 75.297  40.441  53.006  1.000 66.933  0 47  ALA DDD O     1 ? 4 
ATOM   11515 C CB    . ALA D 1 47  ? 77.287  39.311  55.245  1.000 64.119  0 47  ALA DDD CB    1 ? 4 
ATOM   11516 N N     . LYS D 1 48  ? 74.076  39.211  54.525  1.000 67.075  0 48  LYS DDD N     1 ? 4 
ATOM   11517 C CA    . LYS D 1 48  ? 72.906  38.875  53.661  1.000 69.439  0 48  LYS DDD CA    1 ? 4 
ATOM   11518 C C     . LYS D 1 48  ? 72.273  40.139  53.048  1.000 70.028  0 48  LYS DDD C     1 ? 4 
ATOM   11519 O O     . LYS D 1 48  ? 71.730  40.041  51.932  1.000 68.214  0 48  LYS DDD O     1 ? 4 
ATOM   11520 C CB    . LYS D 1 48  ? 71.814  38.137  54.448  1.000 69.086  0 48  LYS DDD CB    1 ? 4 
ATOM   11521 C CG    . LYS D 1 48  ? 71.626  36.663  54.118  1.000 69.935  0 48  LYS DDD CG    1 ? 4 
ATOM   11522 C CD    . LYS D 1 48  ? 70.341  36.075  54.641  1.000 71.507  0 48  LYS DDD CD    1 ? 4 
ATOM   11523 C CE    . LYS D 1 48  ? 69.084  36.638  54.017  1.000 72.900  0 48  LYS DDD CE    1 ? 4 
ATOM   11524 N NZ    . LYS D 1 48  ? 67.904  35.943  54.576  1.000 72.889  0 48  LYS DDD NZ    1 ? 4 
ATOM   11525 N N     . TYR D 1 49  ? 72.289  41.263  53.773  1.000 71.336  0 49  TYR DDD N     1 ? 4 
ATOM   11526 C CA    . TYR D 1 49  ? 71.574  42.515  53.401  1.000 73.421  0 49  TYR DDD CA    1 ? 4 
ATOM   11527 C C     . TYR D 1 49  ? 72.538  43.491  52.700  1.000 76.261  0 49  TYR DDD C     1 ? 4 
ATOM   11528 O O     . TYR D 1 49  ? 72.223  44.684  52.629  1.000 74.970  0 49  TYR DDD O     1 ? 4 
ATOM   11529 C CB    . TYR D 1 49  ? 70.878  43.082  54.642  1.000 72.075  0 49  TYR DDD CB    1 ? 4 
ATOM   11530 C CG    . TYR D 1 49  ? 69.814  42.159  55.187  1.000 70.578  0 49  TYR DDD CG    1 ? 4 
ATOM   11531 C CD1   . TYR D 1 49  ? 68.720  41.791  54.416  1.000 69.209  0 49  TYR DDD CD1   1 ? 4 
ATOM   11532 C CD2   . TYR D 1 49  ? 69.923  41.607  56.453  1.000 67.396  0 49  TYR DDD CD2   1 ? 4 
ATOM   11533 C CE1   . TYR D 1 49  ? 67.748  40.930  54.900  1.000 67.685  0 49  TYR DDD CE1   1 ? 4 
ATOM   11534 C CE2   . TYR D 1 49  ? 68.971  40.729  56.945  1.000 65.763  0 49  TYR DDD CE2   1 ? 4 
ATOM   11535 C CZ    . TYR D 1 49  ? 67.875  40.390  56.169  1.000 68.242  0 49  TYR DDD CZ    1 ? 4 
ATOM   11536 O OH    . TYR D 1 49  ? 66.917  39.557  56.682  1.000 64.548  0 49  TYR DDD OH    1 ? 4 
ATOM   11537 N N     . GLY D 1 50  ? 73.645  42.974  52.147  1.000 78.480  0 50  GLY DDD N     1 ? 4 
ATOM   11538 C CA    . GLY D 1 50  ? 74.632  43.725  51.346  1.000 77.261  0 50  GLY DDD CA    1 ? 4 
ATOM   11539 C C     . GLY D 1 50  ? 75.558  44.561  52.211  1.000 78.713  0 50  GLY DDD C     1 ? 4 
ATOM   11540 O O     . GLY D 1 50  ? 76.260  45.432  51.650  1.000 82.786  0 50  GLY DDD O     1 ? 4 
ATOM   11541 N N     . LYS D 1 51  ? 75.605  44.303  53.516  1.000 74.536  0 51  LYS DDD N     1 ? 4 
ATOM   11542 C CA    . LYS D 1 51  ? 76.416  45.113  54.452  1.000 73.985  0 51  LYS DDD CA    1 ? 4 
ATOM   11543 C C     . LYS D 1 51  ? 77.850  44.576  54.440  1.000 77.467  0 51  LYS DDD C     1 ? 4 
ATOM   11544 O O     . LYS D 1 51  ? 78.047  43.372  54.162  1.000 76.975  0 51  LYS DDD O     1 ? 4 
ATOM   11545 C CB    . LYS D 1 51  ? 75.779  45.076  55.841  1.000 72.335  0 51  LYS DDD CB    1 ? 4 
ATOM   11546 C CG    . LYS D 1 51  ? 74.356  45.618  55.910  1.000 71.285  0 51  LYS DDD CG    1 ? 4 
ATOM   11547 C CD    . LYS D 1 51  ? 74.105  46.848  55.059  1.000 69.770  0 51  LYS DDD CD    1 ? 4 
ATOM   11548 C CE    . LYS D 1 51  ? 72.864  47.585  55.506  1.000 69.984  0 51  LYS DDD CE    1 ? 4 
ATOM   11549 N NZ    . LYS D 1 51  ? 72.035  48.105  54.398  1.000 70.034  0 51  LYS DDD NZ    1 ? 4 
ATOM   11550 N N     . LYS D 1 52  ? 78.816  45.461  54.669  1.000 79.712  0 52  LYS DDD N     1 ? 4 
ATOM   11551 C CA    . LYS D 1 52  ? 80.240  45.093  54.820  1.000 81.056  0 52  LYS DDD CA    1 ? 4 
ATOM   11552 C C     . LYS D 1 52  ? 80.462  44.673  56.278  1.000 80.414  0 52  LYS DDD C     1 ? 4 
ATOM   11553 O O     . LYS D 1 52  ? 80.148  45.470  57.193  1.000 79.632  0 52  LYS DDD O     1 ? 4 
ATOM   11554 C CB    . LYS D 1 52  ? 81.146  46.253  54.401  1.000 90.099  0 52  LYS DDD CB    1 ? 4 
ATOM   11555 C CG    . LYS D 1 52  ? 82.520  45.818  53.903  1.000 94.743  0 52  LYS DDD CG    1 ? 4 
ATOM   11556 C CD    . LYS D 1 52  ? 83.588  46.886  53.969  1.000 98.044  0 52  LYS DDD CD    1 ? 4 
ATOM   11557 C CE    . LYS D 1 52  ? 84.981  46.301  53.849  1.000 98.463  0 52  LYS DDD CE    1 ? 4 
ATOM   11558 N NZ    . LYS D 1 52  ? 86.038  47.304  54.109  1.000 99.569  0 52  LYS DDD NZ    1 ? 4 
ATOM   11559 N N     . VAL D 1 53  ? 80.966  43.457  56.472  1.000 80.039  0 53  VAL DDD N     1 ? 4 
ATOM   11560 C CA    . VAL D 1 53  ? 81.010  42.748  57.781  1.000 77.834  0 53  VAL DDD CA    1 ? 4 
ATOM   11561 C C     . VAL D 1 53  ? 82.413  42.168  57.938  1.000 76.033  0 53  VAL DDD C     1 ? 4 
ATOM   11562 O O     . VAL D 1 53  ? 82.898  41.520  56.977  1.000 72.706  0 53  VAL DDD O     1 ? 4 
ATOM   11563 C CB    . VAL D 1 53  ? 79.940  41.638  57.879  1.000 78.752  0 53  VAL DDD CB    1 ? 4 
ATOM   11564 C CG1   . VAL D 1 53  ? 79.847  41.071  59.287  1.000 78.773  0 53  VAL DDD CG1   1 ? 4 
ATOM   11565 C CG2   . VAL D 1 53  ? 78.572  42.112  57.409  1.000 79.835  0 53  VAL DDD CG2   1 ? 4 
ATOM   11566 N N     . ALA D 1 54  ? 83.029  42.407  59.104  1.000 73.852  0 54  ALA DDD N     1 ? 4 
ATOM   11567 C CA    . ALA D 1 54  ? 84.276  41.741  59.546  1.000 72.167  0 54  ALA DDD CA    1 ? 4 
ATOM   11568 C C     . ALA D 1 54  ? 83.987  40.963  60.822  1.000 66.922  0 54  ALA DDD C     1 ? 4 
ATOM   11569 O O     . ALA D 1 54  ? 83.217  41.493  61.675  1.000 69.810  0 54  ALA DDD O     1 ? 4 
ATOM   11570 C CB    . ALA D 1 54  ? 85.375  42.741  59.785  1.000 75.661  0 54  ALA DDD CB    1 ? 4 
ATOM   11571 N N     . LEU D 1 55  ? 84.581  39.776  60.941  1.000 59.965  0 55  LEU DDD N     1 ? 4 
ATOM   11572 C CA    . LEU D 1 55  ? 84.462  38.945  62.161  1.000 57.081  0 55  LEU DDD CA    1 ? 4 
ATOM   11573 C C     . LEU D 1 55  ? 85.866  38.593  62.641  1.000 54.372  0 55  LEU DDD C     1 ? 4 
ATOM   11574 O O     . LEU D 1 55  ? 86.685  38.170  61.809  1.000 52.852  0 55  LEU DDD O     1 ? 4 
ATOM   11575 C CB    . LEU D 1 55  ? 83.626  37.694  61.874  1.000 54.587  0 55  LEU DDD CB    1 ? 4 
ATOM   11576 C CG    . LEU D 1 55  ? 83.315  36.828  63.092  1.000 53.227  0 55  LEU DDD CG    1 ? 4 
ATOM   11577 C CD1   . LEU D 1 55  ? 81.944  36.173  62.979  1.000 54.706  0 55  LEU DDD CD1   1 ? 4 
ATOM   11578 C CD2   . LEU D 1 55  ? 84.387  35.784  63.281  1.000 53.890  0 55  LEU DDD CD2   1 ? 4 
ATOM   11579 N N     . PHE D 1 56  ? 86.104  38.805  63.933  1.000 51.942  0 56  PHE DDD N     1 ? 4 
ATOM   11580 C CA    . PHE D 1 56  ? 87.324  38.387  64.654  1.000 53.190  0 56  PHE DDD CA    1 ? 4 
ATOM   11581 C C     . PHE D 1 56  ? 87.000  37.137  65.467  1.000 52.648  0 56  PHE DDD C     1 ? 4 
ATOM   11582 O O     . PHE D 1 56  ? 85.961  37.095  66.156  1.000 55.152  0 56  PHE DDD O     1 ? 4 
ATOM   11583 C CB    . PHE D 1 56  ? 87.839  39.531  65.528  1.000 55.132  0 56  PHE DDD CB    1 ? 4 
ATOM   11584 C CG    . PHE D 1 56  ? 88.335  40.718  64.735  1.000 56.411  0 56  PHE DDD CG    1 ? 4 
ATOM   11585 C CD1   . PHE D 1 56  ? 89.636  40.759  64.261  1.000 56.216  0 56  PHE DDD CD1   1 ? 4 
ATOM   11586 C CD2   . PHE D 1 56  ? 87.499  41.784  64.437  1.000 55.476  0 56  PHE DDD CD2   1 ? 4 
ATOM   11587 C CE1   . PHE D 1 56  ? 90.092  41.838  63.520  1.000 56.339  0 56  PHE DDD CE1   1 ? 4 
ATOM   11588 C CE2   . PHE D 1 56  ? 87.956  42.859  63.689  1.000 54.983  0 56  PHE DDD CE2   1 ? 4 
ATOM   11589 C CZ    . PHE D 1 56  ? 89.250  42.883  63.230  1.000 55.764  0 56  PHE DDD CZ    1 ? 4 
ATOM   11590 N N     . ASP D 1 57  ? 87.850  36.124  65.338  1.000 52.103  0 57  ASP DDD N     1 ? 4 
ATOM   11591 C CA    . ASP D 1 57  ? 87.893  34.955  66.257  1.000 48.750  0 57  ASP DDD CA    1 ? 4 
ATOM   11592 C C     . ASP D 1 57  ? 89.351  34.574  66.456  1.000 47.280  0 57  ASP DDD C     1 ? 4 
ATOM   11593 O O     . ASP D 1 57  ? 90.024  34.425  65.435  1.000 45.821  0 57  ASP DDD O     1 ? 4 
ATOM   11594 C CB    . ASP D 1 57  ? 87.131  33.736  65.736  1.000 47.898  0 57  ASP DDD CB    1 ? 4 
ATOM   11595 C CG    . ASP D 1 57  ? 86.928  32.709  66.830  1.000 47.525  0 57  ASP DDD CG    1 ? 4 
ATOM   11596 O OD1   . ASP D 1 57  ? 86.211  33.018  67.782  1.000 46.846  0 57  ASP DDD OD1   1 ? 4 
ATOM   11597 O OD2   . ASP D 1 57  ? 87.556  31.653  66.761  1.000 48.753  0 57  ASP DDD OD2   1 ? 4 
ATOM   11598 N N     . PHE D 1 58  ? 89.807  34.475  67.708  1.000 44.795  0 58  PHE DDD N     1 ? 4 
ATOM   11599 C CA    . PHE D 1 58  ? 91.100  33.852  68.072  1.000 47.062  0 58  PHE DDD CA    1 ? 4 
ATOM   11600 C C     . PHE D 1 58  ? 90.904  33.071  69.365  1.000 47.102  0 58  PHE DDD C     1 ? 4 
ATOM   11601 O O     . PHE D 1 58  ? 90.204  33.557  70.286  1.000 46.356  0 58  PHE DDD O     1 ? 4 
ATOM   11602 C CB    . PHE D 1 58  ? 92.210  34.896  68.208  1.000 49.465  0 58  PHE DDD CB    1 ? 4 
ATOM   11603 C CG    . PHE D 1 58  ? 93.586  34.350  68.529  1.000 49.793  0 58  PHE DDD CG    1 ? 4 
ATOM   11604 C CD1   . PHE D 1 58  ? 93.999  34.153  69.840  1.000 50.814  0 58  PHE DDD CD1   1 ? 4 
ATOM   11605 C CD2   . PHE D 1 58  ? 94.487  34.074  67.512  1.000 51.181  0 58  PHE DDD CD2   1 ? 4 
ATOM   11606 C CE1   . PHE D 1 58  ? 95.268  33.656  70.118  1.000 51.487  0 58  PHE DDD CE1   1 ? 4 
ATOM   11607 C CE2   . PHE D 1 58  ? 95.773  33.614  67.792  1.000 51.927  0 58  PHE DDD CE2   1 ? 4 
ATOM   11608 C CZ    . PHE D 1 58  ? 96.155  33.389  69.094  1.000 50.959  0 58  PHE DDD CZ    1 ? 4 
ATOM   11609 N N     . VAL D 1 59  ? 91.519  31.899  69.450  1.000 48.593  0 59  VAL DDD N     1 ? 4 
ATOM   11610 C CA    . VAL D 1 59  ? 91.331  31.014  70.631  1.000 50.281  0 59  VAL DDD CA    1 ? 4 
ATOM   11611 C C     . VAL D 1 59  ? 92.550  31.167  71.543  1.000 50.846  0 59  VAL DDD C     1 ? 4 
ATOM   11612 O O     . VAL D 1 59  ? 93.629  30.663  71.176  1.000 48.757  0 59  VAL DDD O     1 ? 4 
ATOM   11613 C CB    . VAL D 1 59  ? 91.089  29.559  70.186  1.000 51.684  0 59  VAL DDD CB    1 ? 4 
ATOM   11614 C CG1   . VAL D 1 59  ? 90.892  28.629  71.375  1.000 52.455  0 59  VAL DDD CG1   1 ? 4 
ATOM   11615 C CG2   . VAL D 1 59  ? 89.904  29.451  69.237  1.000 50.287  0 59  VAL DDD CG2   1 ? 4 
ATOM   11616 N N     . LYS D 1 60  ? 92.380  31.840  72.686  1.000 53.369  0 60  LYS DDD N     1 ? 4 
ATOM   11617 C CA    . LYS D 1 60  ? 93.372  31.813  73.802  1.000 53.553  0 60  LYS DDD CA    1 ? 4 
ATOM   11618 C C     . LYS D 1 60  ? 93.437  30.380  74.335  1.000 51.061  0 60  LYS DDD C     1 ? 4 
ATOM   11619 O O     . LYS D 1 60  ? 92.408  29.764  74.607  1.000 49.266  0 60  LYS DDD O     1 ? 4 
ATOM   11620 C CB    . LYS D 1 60  ? 93.017  32.867  74.862  1.000 56.117  0 60  LYS DDD CB    1 ? 4 
ATOM   11621 C CG    . LYS D 1 60  ? 93.305  34.296  74.420  1.000 56.418  0 60  LYS DDD CG    1 ? 4 
ATOM   11622 C CD    . LYS D 1 60  ? 93.034  35.366  75.461  1.000 58.477  0 60  LYS DDD CD    1 ? 4 
ATOM   11623 C CE    . LYS D 1 60  ? 91.576  35.500  75.889  1.000 59.440  0 60  LYS DDD CE    1 ? 4 
ATOM   11624 N NZ    . LYS D 1 60  ? 90.704  35.798  74.727  1.000 60.306  0 60  LYS DDD NZ    1 ? 4 
ATOM   11625 N N     . PRO D 1 61  ? 94.634  29.773  74.484  1.000 51.965  0 61  PRO DDD N     1 ? 4 
ATOM   11626 C CA    . PRO D 1 61  ? 94.741  28.422  75.051  1.000 51.549  0 61  PRO DDD CA    1 ? 4 
ATOM   11627 C C     . PRO D 1 61  ? 94.148  28.305  76.466  1.000 53.201  0 61  PRO DDD C     1 ? 4 
ATOM   11628 O O     . PRO D 1 61  ? 94.188  29.271  77.237  1.000 53.793  0 61  PRO DDD O     1 ? 4 
ATOM   11629 C CB    . PRO D 1 61  ? 96.255  28.116  75.075  1.000 50.281  0 61  PRO DDD CB    1 ? 4 
ATOM   11630 C CG    . PRO D 1 61  ? 96.860  29.095  74.091  1.000 50.877  0 61  PRO DDD CG    1 ? 4 
ATOM   11631 C CD    . PRO D 1 61  ? 95.953  30.317  74.119  1.000 52.529  0 61  PRO DDD CD    1 ? 4 
ATOM   11632 N N     . SER D 1 62  ? 93.581  27.136  76.773  1.000 50.589  0 62  SER DDD N     1 ? 4 
ATOM   11633 C CA    . SER D 1 62  ? 93.007  26.818  78.103  1.000 50.567  0 62  SER DDD CA    1 ? 4 
ATOM   11634 C C     . SER D 1 62  ? 94.099  26.915  79.183  1.000 52.115  0 62  SER DDD C     1 ? 4 
ATOM   11635 O O     . SER D 1 62  ? 95.301  27.052  78.836  1.000 49.752  0 62  SER DDD O     1 ? 4 
ATOM   11636 C CB    . SER D 1 62  ? 92.385  25.448  78.089  1.000 49.896  0 62  SER DDD CB    1 ? 4 
ATOM   11637 O OG    . SER D 1 62  ? 93.385  24.448  78.015  1.000 46.342  0 62  SER DDD OG    1 ? 4 
ATOM   11638 N N     . THR D 1 63  ? 93.715  26.766  80.449  1.000 52.687  0 63  THR DDD N     1 ? 4 
ATOM   11639 C CA    . THR D 1 63  ? 94.680  26.694  81.582  1.000 53.926  0 63  THR DDD CA    1 ? 4 
ATOM   11640 C C     . THR D 1 63  ? 95.670  25.544  81.367  1.000 55.262  0 63  THR DDD C     1 ? 4 
ATOM   11641 O O     . THR D 1 63  ? 96.732  25.596  81.987  1.000 55.451  0 63  THR DDD O     1 ? 4 
ATOM   11642 C CB    . THR D 1 63  ? 93.964  26.625  82.932  1.000 51.927  0 63  THR DDD CB    1 ? 4 
ATOM   11643 O OG1   . THR D 1 63  ? 93.164  25.448  82.949  1.000 50.769  0 63  THR DDD OG1   1 ? 4 
ATOM   11644 C CG2   . THR D 1 63  ? 93.131  27.866  83.165  1.000 52.085  0 63  THR DDD CG2   1 ? 4 
ATOM   11645 N N     . GLN D 1 64  ? 95.370  24.571  80.493  1.000 57.787  0 64  GLN DDD N     1 ? 4 
ATOM   11646 C CA    . GLN D 1 64  ? 96.272  23.400  80.249  1.000 55.709  0 64  GLN DDD CA    1 ? 4 
ATOM   11647 C C     . GLN D 1 64  ? 96.835  23.408  78.819  1.000 51.813  0 64  GLN DDD C     1 ? 4 
ATOM   11648 O O     . GLN D 1 64  ? 97.326  22.354  78.389  1.000 54.512  0 64  GLN DDD O     1 ? 4 
ATOM   11649 C CB    . GLN D 1 64  ? 95.531  22.097  80.593  1.000 56.666  0 64  GLN DDD CB    1 ? 4 
ATOM   11650 C CG    . GLN D 1 64  ? 95.237  21.940  82.089  1.000 57.065  0 64  GLN DDD CG    1 ? 4 
ATOM   11651 C CD    . GLN D 1 64  ? 96.491  21.782  82.918  1.000 55.956  0 64  GLN DDD CD    1 ? 4 
ATOM   11652 O OE1   . GLN D 1 64  ? 97.476  21.236  82.456  1.000 56.397  0 64  GLN DDD OE1   1 ? 4 
ATOM   11653 N NE2   . GLN D 1 64  ? 96.467  22.222  84.167  1.000 55.349  0 64  GLN DDD NE2   1 ? 4 
ATOM   11654 N N     . GLY D 1 65  ? 96.826  24.547  78.120  1.000 49.153  0 65  GLY DDD N     1 ? 4 
ATOM   11655 C CA    . GLY D 1 65  ? 97.451  24.681  76.788  1.000 48.356  0 65  GLY DDD CA    1 ? 4 
ATOM   11656 C C     . GLY D 1 65  ? 96.594  24.147  75.638  1.000 47.020  0 65  GLY DDD C     1 ? 4 
ATOM   11657 O O     . GLY D 1 65  ? 97.107  24.136  74.515  1.000 45.556  0 65  GLY DDD O     1 ? 4 
ATOM   11658 N N     . THR D 1 66  ? 95.325  23.764  75.853  1.000 45.327  0 66  THR DDD N     1 ? 4 
ATOM   11659 C CA    . THR D 1 66  ? 94.447  23.259  74.761  1.000 44.227  0 66  THR DDD CA    1 ? 4 
ATOM   11660 C C     . THR D 1 66  ? 93.941  24.430  73.921  1.000 43.320  0 66  THR DDD C     1 ? 4 
ATOM   11661 O O     . THR D 1 66  ? 93.491  25.414  74.521  1.000 44.086  0 66  THR DDD O     1 ? 4 
ATOM   11662 C CB    . THR D 1 66  ? 93.265  22.427  75.261  1.000 44.511  0 66  THR DDD CB    1 ? 4 
ATOM   11663 O OG1   . THR D 1 66  ? 93.749  21.521  76.244  1.000 45.973  0 66  THR DDD OG1   1 ? 4 
ATOM   11664 C CG2   . THR D 1 66  ? 92.596  21.645  74.157  1.000 43.834  0 66  THR DDD CG2   1 ? 4 
ATOM   11665 N N     . LYS D 1 67  ? 93.986  24.293  72.587  1.000 43.449  0 67  LYS DDD N     1 ? 4 
ATOM   11666 C CA    . LYS D 1 67  ? 93.448  25.291  71.620  1.000 45.271  0 67  LYS DDD CA    1 ? 4 
ATOM   11667 C C     . LYS D 1 67  ? 92.780  24.566  70.440  1.000 41.696  0 67  LYS DDD C     1 ? 4 
ATOM   11668 O O     . LYS D 1 67  ? 92.929  23.349  70.354  1.000 38.074  0 67  LYS DDD O     1 ? 4 
ATOM   11669 C CB    . LYS D 1 67  ? 94.552  26.261  71.174  1.000 47.698  0 67  LYS DDD CB    1 ? 4 
ATOM   11670 C CG    . LYS D 1 67  ? 95.559  25.692  70.196  1.000 51.627  0 67  LYS DDD CG    1 ? 4 
ATOM   11671 C CD    . LYS D 1 67  ? 96.599  26.718  69.752  1.000 53.053  0 67  LYS DDD CD    1 ? 4 
ATOM   11672 C CE    . LYS D 1 67  ? 97.689  26.103  68.893  1.000 54.855  0 67  LYS DDD CE    1 ? 4 
ATOM   11673 N NZ    . LYS D 1 67  ? 99.074  26.434  69.362  1.000 55.060  0 67  LYS DDD NZ    1 ? 4 
ATOM   11674 N N     . TRP D 1 68  ? 92.053  25.311  69.596  1.000 40.316  0 68  TRP DDD N     1 ? 4 
ATOM   11675 C CA    . TRP D 1 68  ? 91.106  24.762  68.586  1.000 38.414  0 68  TRP DDD CA    1 ? 4 
ATOM   11676 C C     . TRP D 1 68  ? 90.762  25.828  67.533  1.000 37.742  0 68  TRP DDD C     1 ? 4 
ATOM   11677 O O     . TRP D 1 68  ? 91.185  27.001  67.708  1.000 37.657  0 68  TRP DDD O     1 ? 4 
ATOM   11678 C CB    . TRP D 1 68  ? 89.841  24.216  69.284  1.000 37.962  0 68  TRP DDD CB    1 ? 4 
ATOM   11679 C CG    . TRP D 1 68  ? 89.195  25.163  70.253  1.000 38.484  0 68  TRP DDD CG    1 ? 4 
ATOM   11680 C CD1   . TRP D 1 68  ? 88.322  26.181  69.962  1.000 39.389  0 68  TRP DDD CD1   1 ? 4 
ATOM   11681 C CD2   . TRP D 1 68  ? 89.365  25.189  71.683  1.000 38.925  0 68  TRP DDD CD2   1 ? 4 
ATOM   11682 N NE1   . TRP D 1 68  ? 87.938  26.825  71.107  1.000 39.430  0 68  TRP DDD NE1   1 ? 4 
ATOM   11683 C CE2   . TRP D 1 68  ? 88.555  26.241  72.176  1.000 38.070  0 68  TRP DDD CE2   1 ? 4 
ATOM   11684 C CE3   . TRP D 1 68  ? 90.114  24.433  72.597  1.000 38.947  0 68  TRP DDD CE3   1 ? 4 
ATOM   11685 C CZ2   . TRP D 1 68  ? 88.485  26.555  73.530  1.000 37.637  0 68  TRP DDD CZ2   1 ? 4 
ATOM   11686 C CZ3   . TRP D 1 68  ? 90.057  24.756  73.936  1.000 39.307  0 68  TRP DDD CZ3   1 ? 4 
ATOM   11687 C CH2   . TRP D 1 68  ? 89.235  25.790  74.397  1.000 38.745  0 68  TRP DDD CH2   1 ? 4 
ATOM   11688 N N     . GLY D 1 69  ? 90.022  25.415  66.489  1.000 36.261  0 69  GLY DDD N     1 ? 4 
ATOM   11689 C CA    . GLY D 1 69  ? 89.690  26.218  65.309  1.000 36.447  0 69  GLY DDD CA    1 ? 4 
ATOM   11690 C C     . GLY D 1 69  ? 88.446  27.068  65.518  1.000 37.610  0 69  GLY DDD C     1 ? 4 
ATOM   11691 O O     . GLY D 1 69  ? 88.006  27.234  66.671  1.000 38.832  0 69  GLY DDD O     1 ? 4 
ATOM   11692 N N     . LEU D 1 70  ? 87.937  27.616  64.416  1.000 38.716  0 70  LEU DDD N     1 ? 4 
ATOM   11693 C CA    . LEU D 1 70  ? 86.757  28.509  64.357  1.000 41.512  0 70  LEU DDD CA    1 ? 4 
ATOM   11694 C C     . LEU D 1 70  ? 85.486  27.779  64.819  1.000 40.647  0 70  LEU DDD C     1 ? 4 
ATOM   11695 O O     . LEU D 1 70  ? 85.370  26.561  64.555  1.000 38.059  0 70  LEU DDD O     1 ? 4 
ATOM   11696 C CB    . LEU D 1 70  ? 86.612  28.968  62.905  1.000 42.596  0 70  LEU DDD CB    1 ? 4 
ATOM   11697 C CG    . LEU D 1 70  ? 85.364  29.815  62.625  1.000 46.603  0 70  LEU DDD CG    1 ? 4 
ATOM   11698 C CD1   . LEU D 1 70  ? 85.445  31.167  63.320  1.000 46.230  0 70  LEU DDD CD1   1 ? 4 
ATOM   11699 C CD2   . LEU D 1 70  ? 85.122  29.976  61.126  1.000 48.771  0 70  LEU DDD CD2   1 ? 4 
ATOM   11700 N N     . GLY D 1 71  ? 84.525  28.513  65.382  1.000 40.080  0 71  GLY DDD N     1 ? 4 
ATOM   11701 C CA    . GLY D 1 71  ? 83.156  28.007  65.648  1.000 39.201  0 71  GLY DDD CA    1 ? 4 
ATOM   11702 C C     . GLY D 1 71  ? 82.733  28.201  67.095  1.000 37.772  0 71  GLY DDD C     1 ? 4 
ATOM   11703 O O     . GLY D 1 71  ? 81.532  28.131  67.399  1.000 38.397  0 71  GLY DDD O     1 ? 4 
ATOM   11704 N N     . GLY D 1 72  ? 83.701  28.421  67.973  1.000 38.282  0 72  GLY DDD N     1 ? 4 
ATOM   11705 C CA    . GLY D 1 72  ? 83.454  28.865  69.352  1.000 37.616  0 72  GLY DDD CA    1 ? 4 
ATOM   11706 C C     . GLY D 1 72  ? 83.223  27.688  70.256  1.000 37.133  0 72  GLY DDD C     1 ? 4 
ATOM   11707 O O     . GLY D 1 72  ? 83.606  26.561  69.900  1.000 39.352  0 72  GLY DDD O     1 ? 4 
ATOM   11708 N N     . THR D 1 73  ? 82.659  27.936  71.421  1.000 35.977  0 73  THR DDD N     1 ? 4 
ATOM   11709 C CA    . THR D 1 73  ? 82.531  26.928  72.499  1.000 37.546  0 73  THR DDD CA    1 ? 4 
ATOM   11710 C C     . THR D 1 73  ? 81.630  25.759  72.046  1.000 36.260  0 73  THR DDD C     1 ? 4 
ATOM   11711 O O     . THR D 1 73  ? 82.022  24.601  72.295  1.000 35.338  0 73  THR DDD O     1 ? 4 
ATOM   11712 C CB    . THR D 1 73  ? 82.120  27.630  73.798  1.000 37.706  0 73  THR DDD CB    1 ? 4 
ATOM   11713 O OG1   . THR D 1 73  ? 83.268  28.418  74.121  1.000 35.840  0 73  THR DDD OG1   1 ? 4 
ATOM   11714 C CG2   . THR D 1 73  ? 81.756  26.674  74.909  1.000 38.140  0 73  THR DDD CG2   1 ? 4 
ATOM   11715 N N     . CYS D 1 74  ? 80.492  26.026  71.422  1.000 36.878  0 74  CYS DDD N     1 ? 4 
ATOM   11716 C CA    A CYS D 1 74  ? 79.551  24.926  71.097  0.500 35.974  0 74  CYS DDD CA    1 ? 4 
ATOM   11717 C CA    B CYS D 1 74  ? 79.495  25.029  70.902  0.500 38.076  0 74  CYS DDD CA    1 ? 4 
ATOM   11718 C C     . CYS D 1 74  ? 80.209  23.914  70.142  1.000 35.213  0 74  CYS DDD C     1 ? 4 
ATOM   11719 O O     . CYS D 1 74  ? 80.109  22.690  70.467  1.000 38.543  0 74  CYS DDD O     1 ? 4 
ATOM   11720 C CB    A CYS D 1 74  ? 78.220  25.435  70.585  0.500 36.225  0 74  CYS DDD CB    1 ? 4 
ATOM   11721 C CB    B CYS D 1 74  ? 78.550  25.689  69.888  0.500 42.102  0 74  CYS DDD CB    1 ? 4 
ATOM   11722 S SG    A CYS D 1 74  ? 77.019  24.085  70.471  0.500 37.215  0 74  CYS DDD SG    1 ? 4 
ATOM   11723 S SG    B CYS D 1 74  ? 77.126  24.676  69.383  0.500 46.334  0 74  CYS DDD SG    1 ? 4 
ATOM   11724 N N     . VAL D 1 75  ? 80.882  24.369  69.104  1.000 32.599  0 75  VAL DDD N     1 ? 4 
ATOM   11725 C CA    . VAL D 1 75  ? 81.501  23.517  68.060  1.000 32.053  0 75  VAL DDD CA    1 ? 4 
ATOM   11726 C C     . VAL D 1 75  ? 82.671  22.711  68.636  1.000 29.232  0 75  VAL DDD C     1 ? 4 
ATOM   11727 O O     . VAL D 1 75  ? 82.788  21.503  68.308  1.000 27.284  0 75  VAL DDD O     1 ? 4 
ATOM   11728 C CB    . VAL D 1 75  ? 81.963  24.368  66.867  1.000 33.811  0 75  VAL DDD CB    1 ? 4 
ATOM   11729 C CG1   . VAL D 1 75  ? 82.896  23.586  65.961  1.000 34.545  0 75  VAL DDD CG1   1 ? 4 
ATOM   11730 C CG2   . VAL D 1 75  ? 80.765  24.893  66.083  1.000 34.460  0 75  VAL DDD CG2   1 ? 4 
ATOM   11731 N N     . ASN D 1 76  ? 83.523  23.369  69.415  1.000 27.910  0 76  ASN DDD N     1 ? 4 
ATOM   11732 C CA    . ASN D 1 76  ? 84.863  22.855  69.761  1.000 28.246  0 76  ASN DDD CA    1 ? 4 
ATOM   11733 C C     . ASN D 1 76  ? 84.871  22.200  71.145  1.000 29.333  0 76  ASN DDD C     1 ? 4 
ATOM   11734 O O     . ASN D 1 76  ? 85.578  21.163  71.281  1.000 32.474  0 76  ASN DDD O     1 ? 4 
ATOM   11735 C CB    . ASN D 1 76  ? 85.920  23.959  69.639  1.000 29.233  0 76  ASN DDD CB    1 ? 4 
ATOM   11736 C CG    . ASN D 1 76  ? 86.069  24.449  68.214  1.000 28.486  0 76  ASN DDD CG    1 ? 4 
ATOM   11737 O OD1   . ASN D 1 76  ? 86.737  23.814  67.423  1.000 27.924  0 76  ASN DDD OD1   1 ? 4 
ATOM   11738 N ND2   . ASN D 1 76  ? 85.402  25.538  67.877  1.000 28.830  0 76  ASN DDD ND2   1 ? 4 
ATOM   11739 N N     . VAL D 1 77  ? 84.218  22.779  72.162  1.000 28.178  0 77  VAL DDD N     1 ? 4 
ATOM   11740 C CA    . VAL D 1 77  ? 84.471  22.377  73.581  1.000 28.527  0 77  VAL DDD CA    1 ? 4 
ATOM   11741 C C     . VAL D 1 77  ? 83.165  22.471  74.357  1.000 28.195  0 77  VAL DDD C     1 ? 4 
ATOM   11742 O O     . VAL D 1 77  ? 83.220  22.661  75.550  1.000 28.421  0 77  VAL DDD O     1 ? 4 
ATOM   11743 C CB    . VAL D 1 77  ? 85.593  23.207  74.252  1.000 28.278  0 77  VAL DDD CB    1 ? 4 
ATOM   11744 C CG1   . VAL D 1 77  ? 86.975  22.849  73.733  1.000 29.005  0 77  VAL DDD CG1   1 ? 4 
ATOM   11745 C CG2   . VAL D 1 77  ? 85.397  24.705  74.106  1.000 28.787  0 77  VAL DDD CG2   1 ? 4 
ATOM   11746 N N     . GLY D 1 78  ? 82.037  22.249  73.700  1.000 30.008  0 78  GLY DDD N     1 ? 4 
ATOM   11747 C CA    . GLY D 1 78  ? 80.715  22.348  74.346  1.000 29.527  0 78  GLY DDD CA    1 ? 4 
ATOM   11748 C C     . GLY D 1 78  ? 79.744  21.358  73.774  1.000 30.640  0 78  GLY DDD C     1 ? 4 
ATOM   11749 O O     . GLY D 1 78  ? 80.021  20.144  73.847  1.000 32.880  0 78  GLY DDD O     1 ? 4 
ATOM   11750 N N     . CYS D 1 79  ? 78.636  21.849  73.234  1.000 30.933  0 79  CYS DDD N     1 ? 4 
ATOM   11751 C CA    . CYS D 1 79  ? 77.453  21.021  72.919  1.000 30.832  0 79  CYS DDD CA    1 ? 4 
ATOM   11752 C C     . CYS D 1 79  ? 77.884  19.883  72.002  1.000 30.351  0 79  CYS DDD C     1 ? 4 
ATOM   11753 O O     . CYS D 1 79  ? 77.438  18.736  72.248  1.000 30.792  0 79  CYS DDD O     1 ? 4 
ATOM   11754 C CB    . CYS D 1 79  ? 76.331  21.818  72.257  1.000 33.684  0 79  CYS DDD CB    1 ? 4 
ATOM   11755 S SG    . CYS D 1 79  ? 76.497  23.621  72.406  1.000 37.433  0 79  CYS DDD SG    1 ? 4 
ATOM   11756 N N     . VAL D 1 80  ? 78.712  20.165  70.988  1.000 27.520  0 80  VAL DDD N     1 ? 4 
ATOM   11757 C CA    . VAL D 1 80  ? 79.019  19.137  69.955  1.000 26.090  0 80  VAL DDD CA    1 ? 4 
ATOM   11758 C C     . VAL D 1 80  ? 79.795  17.980  70.567  1.000 24.286  0 80  VAL DDD C     1 ? 4 
ATOM   11759 O O     . VAL D 1 80  ? 79.324  16.848  70.550  1.000 22.273  0 80  VAL DDD O     1 ? 4 
ATOM   11760 C CB    . VAL D 1 80  ? 79.719  19.733  68.723  1.000 27.150  0 80  VAL DDD CB    1 ? 4 
ATOM   11761 C CG1   . VAL D 1 80  ? 80.236  18.622  67.826  1.000 27.952  0 80  VAL DDD CG1   1 ? 4 
ATOM   11762 C CG2   . VAL D 1 80  ? 78.763  20.646  67.955  1.000 27.131  0 80  VAL DDD CG2   1 ? 4 
ATOM   11763 N N     . PRO D 1 81  ? 81.019  18.182  71.097  1.000 24.840  0 81  PRO DDD N     1 ? 4 
ATOM   11764 C CA    . PRO D 1 81  ? 81.778  17.073  71.671  1.000 25.743  0 81  PRO DDD CA    1 ? 4 
ATOM   11765 C C     . PRO D 1 81  ? 81.047  16.422  72.861  1.000 27.241  0 81  PRO DDD C     1 ? 4 
ATOM   11766 O O     . PRO D 1 81  ? 81.137  15.191  72.975  1.000 26.320  0 81  PRO DDD O     1 ? 4 
ATOM   11767 C CB    . PRO D 1 81  ? 83.129  17.649  72.075  1.000 25.122  0 81  PRO DDD CB    1 ? 4 
ATOM   11768 C CG    . PRO D 1 81  ? 82.952  19.168  72.013  1.000 25.413  0 81  PRO DDD CG    1 ? 4 
ATOM   11769 C CD    . PRO D 1 81  ? 81.777  19.441  71.109  1.000 25.629  0 81  PRO DDD CD    1 ? 4 
ATOM   11770 N N     . LYS D 1 82  ? 80.356  17.204  73.692  1.000 26.162  0 82  LYS DDD N     1 ? 4 
ATOM   11771 C CA    . LYS D 1 82  ? 79.620  16.641  74.847  1.000 28.904  0 82  LYS DDD CA    1 ? 4 
ATOM   11772 C C     . LYS D 1 82  ? 78.597  15.618  74.315  1.000 28.203  0 82  LYS DDD C     1 ? 4 
ATOM   11773 O O     . LYS D 1 82  ? 78.506  14.487  74.841  1.000 28.243  0 82  LYS DDD O     1 ? 4 
ATOM   11774 C CB    . LYS D 1 82  ? 78.968  17.781  75.648  1.000 30.796  0 82  LYS DDD CB    1 ? 4 
ATOM   11775 C CG    . LYS D 1 82  ? 77.995  17.371  76.746  1.000 32.123  0 82  LYS DDD CG    1 ? 4 
ATOM   11776 C CD    . LYS D 1 82  ? 76.564  17.122  76.305  1.000 33.918  0 82  LYS DDD CD    1 ? 4 
ATOM   11777 C CE    . LYS D 1 82  ? 75.833  18.311  75.706  1.000 34.491  0 82  LYS DDD CE    1 ? 4 
ATOM   11778 N NZ    . LYS D 1 82  ? 75.602  19.413  76.656  1.000 34.184  0 82  LYS DDD NZ    1 ? 4 
ATOM   11779 N N     . LYS D 1 83  ? 77.868  15.976  73.267  1.000 29.042  0 83  LYS DDD N     1 ? 4 
ATOM   11780 C CA    . LYS D 1 83  ? 76.781  15.122  72.686  1.000 27.828  0 83  LYS DDD CA    1 ? 4 
ATOM   11781 C C     . LYS D 1 83  ? 77.379  13.844  72.078  1.000 25.087  0 83  LYS DDD C     1 ? 4 
ATOM   11782 O O     . LYS D 1 83  ? 76.762  12.752  72.240  1.000 23.250  0 83  LYS DDD O     1 ? 4 
ATOM   11783 C CB    . LYS D 1 83  ? 75.981  15.954  71.695  1.000 28.362  0 83  LYS DDD CB    1 ? 4 
ATOM   11784 C CG    . LYS D 1 83  ? 74.774  15.254  71.099  1.000 30.959  0 83  LYS DDD CG    1 ? 4 
ATOM   11785 C CD    . LYS D 1 83  ? 73.560  15.171  71.986  1.000 30.040  0 83  LYS DDD CD    1 ? 4 
ATOM   11786 C CE    . LYS D 1 83  ? 72.535  14.217  71.437  1.000 30.475  0 83  LYS DDD CE    1 ? 4 
ATOM   11787 N NZ    . LYS D 1 83  ? 71.306  14.934  71.066  1.000 31.882  0 83  LYS DDD NZ    1 ? 4 
ATOM   11788 N N     . LEU D 1 84  ? 78.557  13.940  71.443  1.000 23.314  0 84  LEU DDD N     1 ? 4 
ATOM   11789 C CA    . LEU D 1 84  ? 79.228  12.741  70.896  1.000 22.430  0 84  LEU DDD CA    1 ? 4 
ATOM   11790 C C     . LEU D 1 84  ? 79.709  11.861  72.071  1.000 23.680  0 84  LEU DDD C     1 ? 4 
ATOM   11791 O O     . LEU D 1 84  ? 79.565  10.628  72.012  1.000 23.014  0 84  LEU DDD O     1 ? 4 
ATOM   11792 C CB    . LEU D 1 84  ? 80.400  13.197  70.014  1.000 22.557  0 84  LEU DDD CB    1 ? 4 
ATOM   11793 C CG    . LEU D 1 84  ? 80.008  14.008  68.785  1.000 22.370  0 84  LEU DDD CG    1 ? 4 
ATOM   11794 C CD1   . LEU D 1 84  ? 81.211  14.499  68.010  1.000 22.470  0 84  LEU DDD CD1   1 ? 4 
ATOM   11795 C CD2   . LEU D 1 84  ? 79.092  13.233  67.881  1.000 23.147  0 84  LEU DDD CD2   1 ? 4 
ATOM   11796 N N     . MET D 1 85  ? 80.241  12.451  73.144  1.000 23.673  0 85  MET DDD N     1 ? 4 
ATOM   11797 C CA    . MET D 1 85  ? 80.644  11.627  74.297  1.000 26.092  0 85  MET DDD CA    1 ? 4 
ATOM   11798 C C     . MET D 1 85  ? 79.413  10.937  74.905  1.000 24.035  0 85  MET DDD C     1 ? 4 
ATOM   11799 O O     . MET D 1 85  ? 79.497  9.754   75.215  1.000 24.003  0 85  MET DDD O     1 ? 4 
ATOM   11800 C CB    . MET D 1 85  ? 81.382  12.439  75.358  1.000 28.827  0 85  MET DDD CB    1 ? 4 
ATOM   11801 C CG    . MET D 1 85  ? 82.600  13.107  74.821  1.000 32.250  0 85  MET DDD CG    1 ? 4 
ATOM   11802 S SD    . MET D 1 85  ? 84.143  12.267  74.923  1.000 39.568  0 85  MET DDD SD    1 ? 4 
ATOM   11803 C CE    . MET D 1 85  ? 84.229  12.148  76.707  1.000 36.444  0 85  MET DDD CE    1 ? 4 
ATOM   11804 N N     . HIS D 1 86  ? 78.320  11.641  75.065  1.000 23.717  0 86  HIS DDD N     1 ? 4 
ATOM   11805 C CA    . HIS D 1 86  ? 77.025  11.107  75.582  1.000 23.724  0 86  HIS DDD CA    1 ? 4 
ATOM   11806 C C     . HIS D 1 86  ? 76.599  9.920   74.721  1.000 23.472  0 86  HIS DDD C     1 ? 4 
ATOM   11807 O O     . HIS D 1 86  ? 76.261  8.871   75.291  1.000 24.472  0 86  HIS DDD O     1 ? 4 
ATOM   11808 C CB    . HIS D 1 86  ? 76.013  12.255  75.646  1.000 23.830  0 86  HIS DDD CB    1 ? 4 
ATOM   11809 C CG    . HIS D 1 86  ? 74.632  11.851  76.028  1.000 25.604  0 86  HIS DDD CG    1 ? 4 
ATOM   11810 N ND1   . HIS D 1 86  ? 74.331  11.315  77.269  1.000 26.612  0 86  HIS DDD ND1   1 ? 4 
ATOM   11811 C CD2   . HIS D 1 86  ? 73.450  11.985  75.372  1.000 26.476  0 86  HIS DDD CD2   1 ? 4 
ATOM   11812 C CE1   . HIS D 1 86  ? 73.023  11.131  77.362  1.000 26.831  0 86  HIS DDD CE1   1 ? 4 
ATOM   11813 N NE2   . HIS D 1 86  ? 72.454  11.525  76.214  1.000 27.585  0 86  HIS DDD NE2   1 ? 4 
ATOM   11814 N N     . TYR D 1 87  ? 76.706  10.050  73.395  1.000 23.766  0 87  TYR DDD N     1 ? 4 
ATOM   11815 C CA    . TYR D 1 87  ? 76.349  8.989   72.424  1.000 23.289  0 87  TYR DDD CA    1 ? 4 
ATOM   11816 C C     . TYR D 1 87  ? 77.212  7.756   72.680  1.000 22.640  0 87  TYR DDD C     1 ? 4 
ATOM   11817 O O     . TYR D 1 87  ? 76.651  6.633   72.791  1.000 21.819  0 87  TYR DDD O     1 ? 4 
ATOM   11818 C CB    . TYR D 1 87  ? 76.425  9.501   70.987  1.000 25.666  0 87  TYR DDD CB    1 ? 4 
ATOM   11819 C CG    . TYR D 1 87  ? 75.817  8.540   69.999  1.000 28.863  0 87  TYR DDD CG    1 ? 4 
ATOM   11820 C CD1   . TYR D 1 87  ? 74.460  8.247   70.048  1.000 32.208  0 87  TYR DDD CD1   1 ? 4 
ATOM   11821 C CD2   . TYR D 1 87  ? 76.592  7.852   69.074  1.000 31.037  0 87  TYR DDD CD2   1 ? 4 
ATOM   11822 C CE1   . TYR D 1 87  ? 73.888  7.336   69.173  1.000 34.358  0 87  TYR DDD CE1   1 ? 4 
ATOM   11823 C CE2   . TYR D 1 87  ? 76.033  6.929   68.205  1.000 31.608  0 87  TYR DDD CE2   1 ? 4 
ATOM   11824 C CZ    . TYR D 1 87  ? 74.679  6.674   68.253  1.000 33.965  0 87  TYR DDD CZ    1 ? 4 
ATOM   11825 O OH    . TYR D 1 87  ? 74.101  5.768   67.410  1.000 38.363  0 87  TYR DDD OH    1 ? 4 
ATOM   11826 N N     . SER D 1 88  ? 78.532  7.932   72.816  1.000 21.620  0 88  SER DDD N     1 ? 4 
ATOM   11827 C CA    . SER D 1 88  ? 79.449  6.828   73.170  1.000 22.053  0 88  SER DDD CA    1 ? 4 
ATOM   11828 C C     . SER D 1 88  ? 78.965  6.176   74.472  1.000 22.807  0 88  SER DDD C     1 ? 4 
ATOM   11829 O O     . SER D 1 88  ? 79.045  4.963   74.572  1.000 23.038  0 88  SER DDD O     1 ? 4 
ATOM   11830 C CB    . SER D 1 88  ? 80.889  7.318   73.324  1.000 22.157  0 88  SER DDD CB    1 ? 4 
ATOM   11831 O OG    . SER D 1 88  ? 81.759  6.243   73.599  1.000 21.628  0 88  SER DDD OG    1 ? 4 
ATOM   11832 N N     . ALA D 1 89  ? 78.540  6.977   75.445  1.000 23.875  0 89  ALA DDD N     1 ? 4 
ATOM   11833 C CA    . ALA D 1 89  ? 78.064  6.510   76.779  1.000 26.393  0 89  ALA DDD CA    1 ? 4 
ATOM   11834 C C     . ALA D 1 89  ? 76.779  5.672   76.606  1.000 28.130  0 89  ALA DDD C     1 ? 4 
ATOM   11835 O O     . ALA D 1 89  ? 76.726  4.558   77.201  1.000 26.501  0 89  ALA DDD O     1 ? 4 
ATOM   11836 C CB    . ALA D 1 89  ? 77.817  7.681   77.721  1.000 26.292  0 89  ALA DDD CB    1 ? 4 
ATOM   11837 N N     . LEU D 1 90  ? 75.816  6.171   75.804  1.000 28.460  0 90  LEU DDD N     1 ? 4 
ATOM   11838 C CA    . LEU D 1 90  ? 74.533  5.482   75.525  1.000 29.269  0 90  LEU DDD CA    1 ? 4 
ATOM   11839 C C     . LEU D 1 90  ? 74.880  4.162   74.873  1.000 28.544  0 90  LEU DDD C     1 ? 4 
ATOM   11840 O O     . LEU D 1 90  ? 74.199  3.177   75.164  1.000 31.354  0 90  LEU DDD O     1 ? 4 
ATOM   11841 C CB    . LEU D 1 90  ? 73.618  6.323   74.622  1.000 28.348  0 90  LEU DDD CB    1 ? 4 
ATOM   11842 C CG    . LEU D 1 90  ? 72.973  7.529   75.310  1.000 29.521  0 90  LEU DDD CG    1 ? 4 
ATOM   11843 C CD1   . LEU D 1 90  ? 72.148  8.395   74.350  1.000 27.888  0 90  LEU DDD CD1   1 ? 4 
ATOM   11844 C CD2   . LEU D 1 90  ? 72.094  7.070   76.475  1.000 30.388  0 90  LEU DDD CD2   1 ? 4 
ATOM   11845 N N     . ILE D 1 91  ? 75.926  4.141   74.059  1.000 28.284  0 91  ILE DDD N     1 ? 4 
ATOM   11846 C CA    . ILE D 1 91  ? 76.325  2.867   73.374  1.000 27.279  0 91  ILE DDD CA    1 ? 4 
ATOM   11847 C C     . ILE D 1 91  ? 76.859  1.902   74.438  1.000 27.581  0 91  ILE DDD C     1 ? 4 
ATOM   11848 O O     . ILE D 1 91  ? 76.399  0.751   74.476  1.000 27.540  0 91  ILE DDD O     1 ? 4 
ATOM   11849 C CB    . ILE D 1 91  ? 77.310  3.104   72.222  1.000 25.051  0 91  ILE DDD CB    1 ? 4 
ATOM   11850 C CG1   . ILE D 1 91  ? 76.604  3.795   71.065  1.000 23.788  0 91  ILE DDD CG1   1 ? 4 
ATOM   11851 C CG2   . ILE D 1 91  ? 77.919  1.788   71.785  1.000 24.927  0 91  ILE DDD CG2   1 ? 4 
ATOM   11852 C CD1   . ILE D 1 91  ? 77.539  4.090   69.893  1.000 24.131  0 91  ILE DDD CD1   1 ? 4 
ATOM   11853 N N     . ALA D 1 92  ? 77.784  2.351   75.279  1.000 29.050  0 92  ALA DDD N     1 ? 4 
ATOM   11854 C CA    . ALA D 1 92  ? 78.299  1.561   76.430  1.000 31.312  0 92  ALA DDD CA    1 ? 4 
ATOM   11855 C C     . ALA D 1 92  ? 77.127  0.952   77.222  1.000 30.435  0 92  ALA DDD C     1 ? 4 
ATOM   11856 O O     . ALA D 1 92  ? 77.076  -0.264  77.430  1.000 28.751  0 92  ALA DDD O     1 ? 4 
ATOM   11857 C CB    . ALA D 1 92  ? 79.163  2.445   77.309  1.000 32.484  0 92  ALA DDD CB    1 ? 4 
ATOM   11858 N N     . SER D 1 93  ? 76.213  1.803   77.664  1.000 32.163  0 93  SER DDD N     1 ? 4 
ATOM   11859 C CA    . SER D 1 93  ? 75.007  1.429   78.463  1.000 33.024  0 93  SER DDD CA    1 ? 4 
ATOM   11860 C C     . SER D 1 93  ? 74.174  0.355   77.735  1.000 30.982  0 93  SER DDD C     1 ? 4 
ATOM   11861 O O     . SER D 1 93  ? 73.862  -0.684  78.301  1.000 30.727  0 93  SER DDD O     1 ? 4 
ATOM   11862 C CB    . SER D 1 93  ? 74.232  2.670   78.734  1.000 33.986  0 93  SER DDD CB    1 ? 4 
ATOM   11863 O OG    . SER D 1 93  ? 73.120  2.395   79.537  1.000 39.788  0 93  SER DDD OG    1 ? 4 
ATOM   11864 N N     . SER D 1 94  ? 73.841  0.610   76.479  1.000 29.705  0 94  SER DDD N     1 ? 4 
ATOM   11865 C CA    . SER D 1 94  ? 73.066  -0.308  75.611  1.000 29.666  0 94  SER DDD CA    1 ? 4 
ATOM   11866 C C     . SER D 1 94  ? 73.786  -1.664  75.509  1.000 29.392  0 94  SER DDD C     1 ? 4 
ATOM   11867 O O     . SER D 1 94  ? 73.123  -2.700  75.578  1.000 29.137  0 94  SER DDD O     1 ? 4 
ATOM   11868 C CB    . SER D 1 94  ? 72.825  0.347   74.302  1.000 29.045  0 94  SER DDD CB    1 ? 4 
ATOM   11869 O OG    . SER D 1 94  ? 72.810  -0.604  73.281  1.000 31.390  0 94  SER DDD OG    1 ? 4 
ATOM   11870 N N     . ILE D 1 95  ? 75.106  -1.674  75.375  1.000 29.614  0 95  ILE DDD N     1 ? 4 
ATOM   11871 C CA    . ILE D 1 95  ? 75.926  -2.918  75.248  1.000 29.292  0 95  ILE DDD CA    1 ? 4 
ATOM   11872 C C     . ILE D 1 95  ? 75.963  -3.634  76.595  1.000 30.048  0 95  ILE DDD C     1 ? 4 
ATOM   11873 O O     . ILE D 1 95  ? 75.777  -4.833  76.595  1.000 31.235  0 95  ILE DDD O     1 ? 4 
ATOM   11874 C CB    . ILE D 1 95  ? 77.349  -2.614  74.765  1.000 29.710  0 95  ILE DDD CB    1 ? 4 
ATOM   11875 C CG1   . ILE D 1 95  ? 77.358  -2.222  73.288  1.000 30.003  0 95  ILE DDD CG1   1 ? 4 
ATOM   11876 C CG2   . ILE D 1 95  ? 78.284  -3.778  75.065  1.000 30.331  0 95  ILE DDD CG2   1 ? 4 
ATOM   11877 C CD1   . ILE D 1 95  ? 78.745  -1.891  72.751  1.000 30.391  0 95  ILE DDD CD1   1 ? 4 
ATOM   11878 N N     . HIS D 1 96  ? 76.228  -2.928  77.698  1.000 31.477  0 96  HIS DDD N     1 ? 4 
ATOM   11879 C CA    . HIS D 1 96  ? 76.284  -3.521  79.058  1.000 33.031  0 96  HIS DDD CA    1 ? 4 
ATOM   11880 C C     . HIS D 1 96  ? 74.913  -4.098  79.443  1.000 32.543  0 96  HIS DDD C     1 ? 4 
ATOM   11881 O O     . HIS D 1 96  ? 74.850  -5.258  79.817  1.000 30.555  0 96  HIS DDD O     1 ? 4 
ATOM   11882 C CB    . HIS D 1 96  ? 76.766  -2.491  80.075  1.000 35.836  0 96  HIS DDD CB    1 ? 4 
ATOM   11883 C CG    . HIS D 1 96  ? 76.907  -3.060  81.444  1.000 42.082  0 96  HIS DDD CG    1 ? 4 
ATOM   11884 N ND1   . HIS D 1 96  ? 76.040  -2.738  82.492  1.000 46.754  0 96  HIS DDD ND1   1 ? 4 
ATOM   11885 C CD2   . HIS D 1 96  ? 77.803  -3.944  81.945  1.000 47.069  0 96  HIS DDD CD2   1 ? 4 
ATOM   11886 C CE1   . HIS D 1 96  ? 76.389  -3.406  83.578  1.000 49.348  0 96  HIS DDD CE1   1 ? 4 
ATOM   11887 N NE2   . HIS D 1 96  ? 77.487  -4.154  83.270  1.000 50.975  0 96  HIS DDD NE2   1 ? 4 
ATOM   11888 N N     . HIS D 1 97  ? 73.835  -3.316  79.301  1.000 32.795  0 97  HIS DDD N     1 ? 4 
ATOM   11889 C CA    . HIS D 1 97  ? 72.495  -3.620  79.884  1.000 33.081  0 97  HIS DDD CA    1 ? 4 
ATOM   11890 C C     . HIS D 1 97  ? 71.604  -4.398  78.920  1.000 34.126  0 97  HIS DDD C     1 ? 4 
ATOM   11891 O O     . HIS D 1 97  ? 70.827  -5.209  79.398  1.000 36.384  0 97  HIS DDD O     1 ? 4 
ATOM   11892 C CB    . HIS D 1 97  ? 71.762  -2.359  80.295  1.000 30.521  0 97  HIS DDD CB    1 ? 4 
ATOM   11893 C CG    . HIS D 1 97  ? 72.366  -1.691  81.471  1.000 31.839  0 97  HIS DDD CG    1 ? 4 
ATOM   11894 N ND1   . HIS D 1 97  ? 72.426  -2.324  82.728  1.000 33.275  0 97  HIS DDD ND1   1 ? 4 
ATOM   11895 C CD2   . HIS D 1 97  ? 72.933  -0.476  81.608  1.000 31.742  0 97  HIS DDD CD2   1 ? 4 
ATOM   11896 C CE1   . HIS D 1 97  ? 72.988  -1.495  83.582  1.000 33.021  0 97  HIS DDD CE1   1 ? 4 
ATOM   11897 N NE2   . HIS D 1 97  ? 73.300  -0.358  82.924  1.000 33.743  0 97  HIS DDD NE2   1 ? 4 
ATOM   11898 N N     . ASP D 1 98  ? 71.663  -4.102  77.622  1.000 33.970  0 98  ASP DDD N     1 ? 4 
ATOM   11899 C CA    . ASP D 1 98  ? 70.511  -4.354  76.696  1.000 32.584  0 98  ASP DDD CA    1 ? 4 
ATOM   11900 C C     . ASP D 1 98  ? 70.851  -5.381  75.622  1.000 31.873  0 98  ASP DDD C     1 ? 4 
ATOM   11901 O O     . ASP D 1 98  ? 69.955  -6.188  75.290  1.000 33.332  0 98  ASP DDD O     1 ? 4 
ATOM   11902 C CB    . ASP D 1 98  ? 70.032  -3.110  75.946  1.000 31.255  0 98  ASP DDD CB    1 ? 4 
ATOM   11903 C CG    . ASP D 1 98  ? 69.454  -2.009  76.812  1.000 30.061  0 98  ASP DDD CG    1 ? 4 
ATOM   11904 O OD1   . ASP D 1 98  ? 69.251  -2.235  77.991  1.000 31.388  0 98  ASP DDD OD1   1 ? 4 
ATOM   11905 O OD2   . ASP D 1 98  ? 69.238  -0.913  76.276  1.000 30.203  0 98  ASP DDD OD2   1 ? 4 
ATOM   11906 N N     . ALA D 1 99  ? 72.086  -5.377  75.130  1.000 31.028  0 99  ALA DDD N     1 ? 4 
ATOM   11907 C CA    . ALA D 1 99  ? 72.468  -6.130  73.928  1.000 32.312  0 99  ALA DDD CA    1 ? 4 
ATOM   11908 C C     . ALA D 1 99  ? 72.141  -7.608  74.144  1.000 35.273  0 99  ALA DDD C     1 ? 4 
ATOM   11909 O O     . ALA D 1 99  ? 71.462  -8.181  73.278  1.000 39.678  0 99  ALA DDD O     1 ? 4 
ATOM   11910 C CB    . ALA D 1 99  ? 73.907  -5.908  73.592  1.000 32.069  0 99  ALA DDD CB    1 ? 4 
ATOM   11911 N N     . GLN D 1 100 ? 72.606  -8.209  75.231  1.000 36.505  0 100 GLN DDD N     1 ? 4 
ATOM   11912 C CA    . GLN D 1 100 ? 72.420  -9.652  75.518  1.000 38.362  0 100 GLN DDD CA    1 ? 4 
ATOM   11913 C C     . GLN D 1 100 ? 70.907  -9.983  75.515  1.000 36.087  0 100 GLN DDD C     1 ? 4 
ATOM   11914 O O     . GLN D 1 100 ? 70.485  -10.940 74.861  1.000 34.995  0 100 GLN DDD O     1 ? 4 
ATOM   11915 C CB    . GLN D 1 100 ? 73.058  -9.954  76.885  1.000 41.899  0 100 GLN DDD CB    1 ? 4 
ATOM   11916 C CG    . GLN D 1 100 ? 72.752  -11.339 77.455  1.000 45.873  0 100 GLN DDD CG    1 ? 4 
ATOM   11917 C CD    . GLN D 1 100 ? 73.469  -12.358 76.619  1.000 52.596  0 100 GLN DDD CD    1 ? 4 
ATOM   11918 O OE1   . GLN D 1 100 ? 72.879  -13.126 75.861  1.000 56.049  0 100 GLN DDD OE1   1 ? 4 
ATOM   11919 N NE2   . GLN D 1 100 ? 74.781  -12.266 76.666  1.000 59.872  0 100 GLN DDD NE2   1 ? 4 
ATOM   11920 N N     . MET D 1 101 ? 70.117  -9.188  76.227  1.000 33.828  0 101 MET DDD N     1 ? 4 
ATOM   11921 C CA    . MET D 1 101 ? 68.677  -9.428  76.448  1.000 33.544  0 101 MET DDD CA    1 ? 4 
ATOM   11922 C C     . MET D 1 101 ? 67.951  -9.384  75.106  1.000 30.956  0 101 MET DDD C     1 ? 4 
ATOM   11923 O O     . MET D 1 101 ? 66.935  -10.126 74.961  1.000 29.822  0 101 MET DDD O     1 ? 4 
ATOM   11924 C CB    . MET D 1 101 ? 68.091  -8.369  77.384  1.000 34.797  0 101 MET DDD CB    1 ? 4 
ATOM   11925 C CG    . MET D 1 101 ? 68.466  -8.564  78.854  1.000 36.651  0 101 MET DDD CG    1 ? 4 
ATOM   11926 S SD    . MET D 1 101 ? 67.787  -10.108 79.537  1.000 41.933  0 101 MET DDD SD    1 ? 4 
ATOM   11927 C CE    . MET D 1 101 ? 66.020  -9.823  79.511  1.000 40.706  0 101 MET DDD CE    1 ? 4 
ATOM   11928 N N     . PHE D 1 102 ? 68.425  -8.545  74.177  1.000 28.549  0 102 PHE DDD N     1 ? 4 
ATOM   11929 C CA    . PHE D 1 102 ? 67.778  -8.361  72.857  1.000 28.178  0 102 PHE DDD CA    1 ? 4 
ATOM   11930 C C     . PHE D 1 102 ? 68.468  -9.248  71.823  1.000 29.221  0 102 PHE DDD C     1 ? 4 
ATOM   11931 O O     . PHE D 1 102 ? 68.255  -9.008  70.642  1.000 29.626  0 102 PHE DDD O     1 ? 4 
ATOM   11932 C CB    . PHE D 1 102 ? 67.687  -6.878  72.492  1.000 26.929  0 102 PHE DDD CB    1 ? 4 
ATOM   11933 C CG    . PHE D 1 102 ? 66.602  -6.161  73.253  1.000 25.418  0 102 PHE DDD CG    1 ? 4 
ATOM   11934 C CD1   . PHE D 1 102 ? 66.840  -5.692  74.520  1.000 26.285  0 102 PHE DDD CD1   1 ? 4 
ATOM   11935 C CD2   . PHE D 1 102 ? 65.327  -6.049  72.740  1.000 25.121  0 102 PHE DDD CD2   1 ? 4 
ATOM   11936 C CE1   . PHE D 1 102 ? 65.837  -5.054  75.238  1.000 26.763  0 102 PHE DDD CE1   1 ? 4 
ATOM   11937 C CE2   . PHE D 1 102 ? 64.312  -5.445  73.461  1.000 25.133  0 102 PHE DDD CE2   1 ? 4 
ATOM   11938 C CZ    . PHE D 1 102 ? 64.565  -4.969  74.725  1.000 26.149  0 102 PHE DDD CZ    1 ? 4 
ATOM   11939 N N     . GLY D 1 103 ? 69.218  -10.257 72.282  1.000 31.819  0 103 GLY DDD N     1 ? 4 
ATOM   11940 C CA    . GLY D 1 103 ? 69.694  -11.405 71.495  1.000 33.136  0 103 GLY DDD CA    1 ? 4 
ATOM   11941 C C     . GLY D 1 103 ? 71.131  -11.224 71.021  1.000 34.567  0 103 GLY DDD C     1 ? 4 
ATOM   11942 O O     . GLY D 1 103 ? 71.637  -12.097 70.259  1.000 35.947  0 103 GLY DDD O     1 ? 4 
ATOM   11943 N N     . HIS D 1 104 ? 71.773  -10.115 71.374  1.000 33.405  0 104 HIS DDD N     1 ? 4 
ATOM   11944 C CA    . HIS D 1 104 ? 73.133  -9.779  70.887  1.000 34.325  0 104 HIS DDD CA    1 ? 4 
ATOM   11945 C C     . HIS D 1 104 ? 74.127  -10.049 72.034  1.000 36.637  0 104 HIS DDD C     1 ? 4 
ATOM   11946 O O     . HIS D 1 104 ? 74.314  -9.141  72.870  1.000 35.586  0 104 HIS DDD O     1 ? 4 
ATOM   11947 C CB    . HIS D 1 104 ? 73.175  -8.343  70.363  1.000 32.078  0 104 HIS DDD CB    1 ? 4 
ATOM   11948 C CG    . HIS D 1 104 ? 72.205  -8.072  69.267  1.000 31.277  0 104 HIS DDD CG    1 ? 4 
ATOM   11949 N ND1   . HIS D 1 104 ? 72.494  -8.326  67.956  1.000 31.136  0 104 HIS DDD ND1   1 ? 4 
ATOM   11950 C CD2   . HIS D 1 104 ? 70.962  -7.537  69.270  1.000 31.225  0 104 HIS DDD CD2   1 ? 4 
ATOM   11951 C CE1   . HIS D 1 104 ? 71.465  -7.994  67.201  1.000 30.665  0 104 HIS DDD CE1   1 ? 4 
ATOM   11952 N NE2   . HIS D 1 104 ? 70.510  -7.518  67.980  1.000 30.320  0 104 HIS DDD NE2   1 ? 4 
ATOM   11953 N N     . LYS D 1 105 ? 74.688  -11.266 72.092  1.000 37.861  0 105 LYS DDD N     1 ? 4 
ATOM   11954 C CA    . LYS D 1 105 ? 75.842  -11.609 72.961  1.000 41.908  0 105 LYS DDD CA    1 ? 4 
ATOM   11955 C C     . LYS D 1 105 ? 77.087  -10.901 72.410  1.000 38.873  0 105 LYS DDD C     1 ? 4 
ATOM   11956 O O     . LYS D 1 105 ? 77.463  -11.151 71.252  1.000 38.760  0 105 LYS DDD O     1 ? 4 
ATOM   11957 C CB    . LYS D 1 105 ? 76.046  -13.126 73.056  1.000 46.550  0 105 LYS DDD CB    1 ? 4 
ATOM   11958 C CG    . LYS D 1 105 ? 77.164  -13.560 74.002  1.000 51.862  0 105 LYS DDD CG    1 ? 4 
ATOM   11959 C CD    . LYS D 1 105 ? 76.759  -13.405 75.459  1.000 55.478  0 105 LYS DDD CD    1 ? 4 
ATOM   11960 C CE    . LYS D 1 105 ? 77.836  -12.967 76.439  1.000 56.551  0 105 LYS DDD CE    1 ? 4 
ATOM   11961 N NZ    . LYS D 1 105 ? 78.853  -14.019 76.640  1.000 58.520  0 105 LYS DDD NZ    1 ? 4 
ATOM   11962 N N     . THR D 1 106 ? 77.668  -10.006 73.195  1.000 37.486  0 106 THR DDD N     1 ? 4 
ATOM   11963 C CA    . THR D 1 106 ? 78.759  -9.116  72.740  1.000 38.668  0 106 THR DDD CA    1 ? 4 
ATOM   11964 C C     . THR D 1 106 ? 79.951  -9.201  73.700  1.000 38.635  0 106 THR DDD C     1 ? 4 
ATOM   11965 O O     . THR D 1 106 ? 79.736  -9.316  74.894  1.000 38.927  0 106 THR DDD O     1 ? 4 
ATOM   11966 C CB    . THR D 1 106 ? 78.290  -7.665  72.665  1.000 36.191  0 106 THR DDD CB    1 ? 4 
ATOM   11967 O OG1   . THR D 1 106 ? 78.166  -7.282  74.028  1.000 38.062  0 106 THR DDD OG1   1 ? 4 
ATOM   11968 C CG2   . THR D 1 106 ? 76.986  -7.489  71.930  1.000 35.730  0 106 THR DDD CG2   1 ? 4 
ATOM   11969 N N     . SER D 1 107 ? 81.162  -9.092  73.181  1.000 39.748  0 107 SER DDD N     1 ? 4 
ATOM   11970 C CA    . SER D 1 107 ? 82.327  -8.664  73.991  1.000 40.899  0 107 SER DDD CA    1 ? 4 
ATOM   11971 C C     . SER D 1 107 ? 82.793  -7.328  73.430  1.000 41.037  0 107 SER DDD C     1 ? 4 
ATOM   11972 O O     . SER D 1 107 ? 82.703  -7.115  72.224  1.000 42.048  0 107 SER DDD O     1 ? 4 
ATOM   11973 C CB    . SER D 1 107 ? 83.414  -9.691  74.071  1.000 40.834  0 107 SER DDD CB    1 ? 4 
ATOM   11974 O OG    . SER D 1 107 ? 83.850  -10.053 72.779  1.000 42.214  0 107 SER DDD OG    1 ? 4 
ATOM   11975 N N     . SER D 1 108 ? 83.192  -6.448  74.330  1.000 41.588  0 108 SER DDD N     1 ? 4 
ATOM   11976 C CA    . SER D 1 108 ? 83.462  -5.030  74.052  1.000 42.186  0 108 SER DDD CA    1 ? 4 
ATOM   11977 C C     . SER D 1 108 ? 84.631  -4.599  74.921  1.000 40.155  0 108 SER DDD C     1 ? 4 
ATOM   11978 O O     . SER D 1 108 ? 84.700  -5.054  76.073  1.000 40.465  0 108 SER DDD O     1 ? 4 
ATOM   11979 C CB    . SER D 1 108 ? 82.213  -4.233  74.339  1.000 43.932  0 108 SER DDD CB    1 ? 4 
ATOM   11980 O OG    . SER D 1 108 ? 82.382  -2.849  74.051  1.000 47.238  0 108 SER DDD OG    1 ? 4 
ATOM   11981 N N     . SER D 1 109 ? 85.503  -3.753  74.403  1.000 39.963  0 109 SER DDD N     1 ? 4 
ATOM   11982 C CA    . SER D 1 109 ? 86.433  -2.961  75.251  1.000 40.937  0 109 SER DDD CA    1 ? 4 
ATOM   11983 C C     . SER D 1 109 ? 86.507  -1.555  74.683  1.000 39.027  0 109 SER DDD C     1 ? 4 
ATOM   11984 O O     . SER D 1 109 ? 86.559  -1.408  73.461  1.000 39.610  0 109 SER DDD O     1 ? 4 
ATOM   11985 C CB    . SER D 1 109 ? 87.831  -3.563  75.444  1.000 42.701  0 109 SER DDD CB    1 ? 4 
ATOM   11986 O OG    . SER D 1 109 ? 88.318  -4.088  74.249  1.000 44.448  0 109 SER DDD OG    1 ? 4 
ATOM   11987 N N     . PHE D 1 110 ? 86.575  -0.586  75.588  1.000 38.364  0 110 PHE DDD N     1 ? 4 
ATOM   11988 C CA    . PHE D 1 110 ? 86.534  0.866   75.298  1.000 37.294  0 110 PHE DDD CA    1 ? 4 
ATOM   11989 C C     . PHE D 1 110 ? 87.950  1.420   75.071  1.000 35.403  0 110 PHE DDD C     1 ? 4 
ATOM   11990 O O     . PHE D 1 110 ? 88.829  1.088   75.790  1.000 33.177  0 110 PHE DDD O     1 ? 4 
ATOM   11991 C CB    . PHE D 1 110 ? 85.896  1.597   76.471  1.000 35.833  0 110 PHE DDD CB    1 ? 4 
ATOM   11992 C CG    . PHE D 1 110 ? 85.897  3.078   76.255  1.000 34.319  0 110 PHE DDD CG    1 ? 4 
ATOM   11993 C CD1   . PHE D 1 110 ? 85.208  3.601   75.173  1.000 33.021  0 110 PHE DDD CD1   1 ? 4 
ATOM   11994 C CD2   . PHE D 1 110 ? 86.621  3.924   77.075  1.000 32.997  0 110 PHE DDD CD2   1 ? 4 
ATOM   11995 C CE1   . PHE D 1 110 ? 85.191  4.968   74.951  1.000 32.495  0 110 PHE DDD CE1   1 ? 4 
ATOM   11996 C CE2   . PHE D 1 110 ? 86.629  5.287   76.826  1.000 32.602  0 110 PHE DDD CE2   1 ? 4 
ATOM   11997 C CZ    . PHE D 1 110 ? 85.911  5.807   75.772  1.000 32.535  0 110 PHE DDD CZ    1 ? 4 
ATOM   11998 N N     . GLU D 1 111 ? 88.136  2.243   74.055  1.000 36.887  0 111 GLU DDD N     1 ? 4 
ATOM   11999 C CA    . GLU D 1 111 ? 89.474  2.812   73.693  1.000 37.215  0 111 GLU DDD CA    1 ? 4 
ATOM   12000 C C     . GLU D 1 111 ? 89.294  4.324   73.600  1.000 33.754  0 111 GLU DDD C     1 ? 4 
ATOM   12001 O O     . GLU D 1 111 ? 88.772  4.783   72.584  1.000 35.625  0 111 GLU DDD O     1 ? 4 
ATOM   12002 C CB    . GLU D 1 111 ? 89.991  2.194   72.395  1.000 39.915  0 111 GLU DDD CB    1 ? 4 
ATOM   12003 C CG    . GLU D 1 111 ? 90.030  0.659   72.394  1.000 43.255  0 111 GLU DDD CG    1 ? 4 
ATOM   12004 C CD    . GLU D 1 111 ? 91.042  -0.014  73.326  1.000 46.830  0 111 GLU DDD CD    1 ? 4 
ATOM   12005 O OE1   . GLU D 1 111 ? 90.835  -1.237  73.575  1.000 48.740  0 111 GLU DDD OE1   1 ? 4 
ATOM   12006 O OE2   . GLU D 1 111 ? 92.030  0.673   73.800  1.000 47.047  0 111 GLU DDD OE2   1 ? 4 
ATOM   12007 N N     . TRP D 1 112 ? 89.636  5.049   74.667  1.000 32.928  0 112 TRP DDD N     1 ? 4 
ATOM   12008 C CA    . TRP D 1 112 ? 89.420  6.512   74.815  1.000 31.942  0 112 TRP DDD CA    1 ? 4 
ATOM   12009 C C     . TRP D 1 112 ? 89.923  7.258   73.555  1.000 31.588  0 112 TRP DDD C     1 ? 4 
ATOM   12010 O O     . TRP D 1 112 ? 89.167  8.109   73.040  1.000 34.050  0 112 TRP DDD O     1 ? 4 
ATOM   12011 C CB    . TRP D 1 112 ? 90.089  7.013   76.097  1.000 31.012  0 112 TRP DDD CB    1 ? 4 
ATOM   12012 C CG    . TRP D 1 112 ? 90.093  8.509   76.232  1.000 30.414  0 112 TRP DDD CG    1 ? 4 
ATOM   12013 C CD1   . TRP D 1 112 ? 91.114  9.340   75.881  1.000 30.002  0 112 TRP DDD CD1   1 ? 4 
ATOM   12014 C CD2   . TRP D 1 112 ? 89.050  9.356   76.764  1.000 29.089  0 112 TRP DDD CD2   1 ? 4 
ATOM   12015 N NE1   . TRP D 1 112 ? 90.755  10.645  76.132  1.000 29.927  0 112 TRP DDD NE1   1 ? 4 
ATOM   12016 C CE2   . TRP D 1 112 ? 89.521  10.679  76.694  1.000 28.387  0 112 TRP DDD CE2   1 ? 4 
ATOM   12017 C CE3   . TRP D 1 112 ? 87.772  9.131   77.299  1.000 28.516  0 112 TRP DDD CE3   1 ? 4 
ATOM   12018 C CZ2   . TRP D 1 112 ? 88.755  11.765  77.097  1.000 29.468  0 112 TRP DDD CZ2   1 ? 4 
ATOM   12019 C CZ3   . TRP D 1 112 ? 87.026  10.198  77.734  1.000 27.325  0 112 TRP DDD CZ3   1 ? 4 
ATOM   12020 C CH2   . TRP D 1 112 ? 87.501  11.506  77.616  1.000 28.057  0 112 TRP DDD CH2   1 ? 4 
ATOM   12021 N N     . GLY D 1 113 ? 91.127  6.956   73.069  1.000 30.424  0 113 GLY DDD N     1 ? 4 
ATOM   12022 C CA    . GLY D 1 113 ? 91.786  7.683   71.967  1.000 30.822  0 113 GLY DDD CA    1 ? 4 
ATOM   12023 C C     . GLY D 1 113 ? 91.070  7.527   70.632  1.000 30.373  0 113 GLY DDD C     1 ? 4 
ATOM   12024 O O     . GLY D 1 113 ? 91.186  8.406   69.778  1.000 31.084  0 113 GLY DDD O     1 ? 4 
ATOM   12025 N N     . LYS D 1 114 ? 90.348  6.440   70.436  1.000 30.308  0 114 LYS DDD N     1 ? 4 
ATOM   12026 C CA    . LYS D 1 114 ? 89.517  6.234   69.219  1.000 30.355  0 114 LYS DDD CA    1 ? 4 
ATOM   12027 C C     . LYS D 1 114 ? 88.352  7.221   69.221  1.000 30.061  0 114 LYS DDD C     1 ? 4 
ATOM   12028 O O     . LYS D 1 114 ? 88.092  7.827   68.162  1.000 30.358  0 114 LYS DDD O     1 ? 4 
ATOM   12029 C CB    . LYS D 1 114 ? 89.029  4.782   69.188  1.000 30.041  0 114 LYS DDD CB    1 ? 4 
ATOM   12030 C CG    . LYS D 1 114 ? 88.201  4.397   67.983  1.000 28.783  0 114 LYS DDD CG    1 ? 4 
ATOM   12031 C CD    . LYS D 1 114 ? 88.731  4.904   66.688  1.000 29.030  0 114 LYS DDD CD    1 ? 4 
ATOM   12032 C CE    . LYS D 1 114 ? 88.257  4.096   65.503  1.000 29.317  0 114 LYS DDD CE    1 ? 4 
ATOM   12033 N NZ    . LYS D 1 114 ? 88.410  4.847   64.237  1.000 30.005  0 114 LYS DDD NZ    1 ? 4 
ATOM   12034 N N     . LEU D 1 115 ? 87.674  7.381   70.376  1.000 30.127  0 115 LEU DDD N     1 ? 4 
ATOM   12035 C CA    . LEU D 1 115 ? 86.491  8.278   70.539  1.000 27.986  0 115 LEU DDD CA    1 ? 4 
ATOM   12036 C C     . LEU D 1 115 ? 86.957  9.718   70.353  1.000 28.522  0 115 LEU DDD C     1 ? 4 
ATOM   12037 O O     . LEU D 1 115 ? 86.327  10.480  69.618  1.000 27.833  0 115 LEU DDD O     1 ? 4 
ATOM   12038 C CB    . LEU D 1 115 ? 85.891  8.053   71.929  1.000 27.061  0 115 LEU DDD CB    1 ? 4 
ATOM   12039 C CG    . LEU D 1 115 ? 84.862  9.086   72.391  1.000 25.666  0 115 LEU DDD CG    1 ? 4 
ATOM   12040 C CD1   . LEU D 1 115 ? 83.654  9.070   71.495  1.000 25.309  0 115 LEU DDD CD1   1 ? 4 
ATOM   12041 C CD2   . LEU D 1 115 ? 84.484  8.837   73.835  1.000 25.834  0 115 LEU DDD CD2   1 ? 4 
ATOM   12042 N N     . VAL D 1 116 ? 88.052  10.068  71.013  1.000 30.720  0 116 VAL DDD N     1 ? 4 
ATOM   12043 C CA    . VAL D 1 116 ? 88.730  11.386  70.844  1.000 30.618  0 116 VAL DDD CA    1 ? 4 
ATOM   12044 C C     . VAL D 1 116 ? 88.968  11.608  69.350  1.000 28.820  0 116 VAL DDD C     1 ? 4 
ATOM   12045 O O     . VAL D 1 116 ? 88.515  12.627  68.843  1.000 28.258  0 116 VAL DDD O     1 ? 4 
ATOM   12046 C CB    . VAL D 1 116 ? 90.010  11.444  71.682  1.000 30.872  0 116 VAL DDD CB    1 ? 4 
ATOM   12047 C CG1   . VAL D 1 116 ? 90.945  12.560  71.245  1.000 32.111  0 116 VAL DDD CG1   1 ? 4 
ATOM   12048 C CG2   . VAL D 1 116 ? 89.627  11.613  73.127  1.000 32.399  0 116 VAL DDD CG2   1 ? 4 
ATOM   12049 N N     . GLU D 1 117 ? 89.550  10.638  68.670  1.000 29.550  0 117 GLU DDD N     1 ? 4 
ATOM   12050 C CA    . GLU D 1 117 ? 89.863  10.754  67.217  1.000 32.267  0 117 GLU DDD CA    1 ? 4 
ATOM   12051 C C     . GLU D 1 117 ? 88.557  11.008  66.426  1.000 29.432  0 117 GLU DDD C     1 ? 4 
ATOM   12052 O O     . GLU D 1 117 ? 88.530  11.942  65.619  1.000 29.594  0 117 GLU DDD O     1 ? 4 
ATOM   12053 C CB    . GLU D 1 117 ? 90.731  9.547   66.798  1.000 34.056  0 117 GLU DDD CB    1 ? 4 
ATOM   12054 C CG    . GLU D 1 117 ? 91.022  9.465   65.315  1.000 36.912  0 117 GLU DDD CG    1 ? 4 
ATOM   12055 C CD    . GLU D 1 117 ? 91.168  8.037   64.778  1.000 40.993  0 117 GLU DDD CD    1 ? 4 
ATOM   12056 O OE1   . GLU D 1 117 ? 90.297  7.606   63.979  1.000 43.975  0 117 GLU DDD OE1   1 ? 4 
ATOM   12057 O OE2   . GLU D 1 117 ? 92.146  7.343   65.145  1.000 44.823  0 117 GLU DDD OE2   1 ? 4 
ATOM   12058 N N     . THR D 1 118 ? 87.479  10.298  66.707  1.000 30.156  0 118 THR DDD N     1 ? 4 
ATOM   12059 C CA    . THR D 1 118 ? 86.146  10.524  66.062  1.000 31.256  0 118 THR DDD CA    1 ? 4 
ATOM   12060 C C     . THR D 1 118 ? 85.625  11.938  66.354  1.000 31.846  0 118 THR DDD C     1 ? 4 
ATOM   12061 O O     . THR D 1 118 ? 85.104  12.563  65.411  1.000 34.192  0 118 THR DDD O     1 ? 4 
ATOM   12062 C CB    . THR D 1 118 ? 85.155  9.427   66.470  1.000 30.571  0 118 THR DDD CB    1 ? 4 
ATOM   12063 O OG1   . THR D 1 118 ? 85.583  8.233   65.826  1.000 28.709  0 118 THR DDD OG1   1 ? 4 
ATOM   12064 C CG2   . THR D 1 118 ? 83.706  9.723   66.129  1.000 30.083  0 118 THR DDD CG2   1 ? 4 
ATOM   12065 N N     . LEU D 1 119 ? 85.756  12.439  67.585  1.000 34.204  0 119 LEU DDD N     1 ? 4 
ATOM   12066 C CA    . LEU D 1 119 ? 85.374  13.837  67.949  1.000 35.988  0 119 LEU DDD CA    1 ? 4 
ATOM   12067 C C     . LEU D 1 119 ? 86.201  14.824  67.136  1.000 36.445  0 119 LEU DDD C     1 ? 4 
ATOM   12068 O O     . LEU D 1 119 ? 85.566  15.674  66.453  1.000 30.810  0 119 LEU DDD O     1 ? 4 
ATOM   12069 C CB    . LEU D 1 119 ? 85.607  14.132  69.429  1.000 37.653  0 119 LEU DDD CB    1 ? 4 
ATOM   12070 C CG    . LEU D 1 119 ? 84.392  13.899  70.318  1.000 39.929  0 119 LEU DDD CG    1 ? 4 
ATOM   12071 C CD1   . LEU D 1 119 ? 83.952  12.437  70.264  1.000 41.883  0 119 LEU DDD CD1   1 ? 4 
ATOM   12072 C CD2   . LEU D 1 119 ? 84.684  14.304  71.751  1.000 39.539  0 119 LEU DDD CD2   1 ? 4 
ATOM   12073 N N     . ARG D 1 120 ? 87.547  14.716  67.240  1.000 38.305  0 120 ARG DDD N     1 ? 4 
ATOM   12074 C CA    . ARG D 1 120 ? 88.512  15.639  66.594  1.000 40.931  0 120 ARG DDD CA    1 ? 4 
ATOM   12075 C C     . ARG D 1 120 ? 88.160  15.747  65.116  1.000 39.186  0 120 ARG DDD C     1 ? 4 
ATOM   12076 O O     . ARG D 1 120 ? 88.067  16.885  64.625  1.000 36.705  0 120 ARG DDD O     1 ? 4 
ATOM   12077 C CB    . ARG D 1 120 ? 89.967  15.202  66.788  1.000 49.702  0 120 ARG DDD CB    1 ? 4 
ATOM   12078 C CG    . ARG D 1 120 ? 90.676  15.858  67.972  1.000 59.766  0 120 ARG DDD CG    1 ? 4 
ATOM   12079 C CD    . ARG D 1 120 ? 92.201  15.697  67.998  1.000 70.971  0 120 ARG DDD CD    1 ? 4 
ATOM   12080 N NE    . ARG D 1 120 ? 92.700  14.455  68.621  1.000 76.478  0 120 ARG DDD NE    1 ? 4 
ATOM   12081 C CZ    . ARG D 1 120 ? 92.993  13.296  67.992  1.000 79.764  0 120 ARG DDD CZ    1 ? 4 
ATOM   12082 N NH1   . ARG D 1 120 ? 92.832  13.159  66.680  1.000 82.381  0 120 ARG DDD NH1   1 ? 4 
ATOM   12083 N NH2   . ARG D 1 120 ? 93.435  12.260  68.695  1.000 75.785  0 120 ARG DDD NH2   1 ? 4 
ATOM   12084 N N     . ASN D 1 121 ? 87.984  14.608  64.431  1.000 39.127  0 121 ASN DDD N     1 ? 4 
ATOM   12085 C CA    . ASN D 1 121 ? 87.736  14.584  62.960  1.000 40.867  0 121 ASN DDD CA    1 ? 4 
ATOM   12086 C C     . ASN D 1 121 ? 86.422  15.313  62.651  1.000 36.677  0 121 ASN DDD C     1 ? 4 
ATOM   12087 O O     . ASN D 1 121 ? 86.396  16.108  61.727  1.000 37.961  0 121 ASN DDD O     1 ? 4 
ATOM   12088 C CB    . ASN D 1 121 ? 87.679  13.165  62.381  1.000 45.404  0 121 ASN DDD CB    1 ? 4 
ATOM   12089 C CG    . ASN D 1 121 ? 88.998  12.416  62.451  1.000 49.097  0 121 ASN DDD CG    1 ? 4 
ATOM   12090 O OD1   . ASN D 1 121 ? 90.033  12.973  62.841  1.000 55.502  0 121 ASN DDD OD1   1 ? 4 
ATOM   12091 N ND2   . ASN D 1 121 ? 88.971  11.137  62.094  1.000 52.516  0 121 ASN DDD ND2   1 ? 4 
ATOM   12092 N N     . HIS D 1 122 ? 85.376  15.088  63.419  1.000 32.810  0 122 HIS DDD N     1 ? 4 
ATOM   12093 C CA    . HIS D 1 122 ? 84.065  15.723  63.159  1.000 33.445  0 122 HIS DDD CA    1 ? 4 
ATOM   12094 C C     . HIS D 1 122 ? 84.149  17.240  63.400  1.000 32.182  0 122 HIS DDD C     1 ? 4 
ATOM   12095 O O     . HIS D 1 122 ? 83.688  18.034  62.559  1.000 31.457  0 122 HIS DDD O     1 ? 4 
ATOM   12096 C CB    . HIS D 1 122 ? 82.958  15.004  63.940  1.000 33.539  0 122 HIS DDD CB    1 ? 4 
ATOM   12097 C CG    . HIS D 1 122 ? 81.634  15.525  63.525  1.000 34.948  0 122 HIS DDD CG    1 ? 4 
ATOM   12098 N ND1   . HIS D 1 122 ? 80.953  15.023  62.441  1.000 35.551  0 122 HIS DDD ND1   1 ? 4 
ATOM   12099 C CD2   . HIS D 1 122 ? 80.967  16.611  63.966  1.000 37.536  0 122 HIS DDD CD2   1 ? 4 
ATOM   12100 C CE1   . HIS D 1 122 ? 79.865  15.750  62.272  1.000 40.400  0 122 HIS DDD CE1   1 ? 4 
ATOM   12101 N NE2   . HIS D 1 122 ? 79.850  16.745  63.204  1.000 40.321  0 122 HIS DDD NE2   1 ? 4 
ATOM   12102 N N     . ILE D 1 123 ? 84.778  17.643  64.499  1.000 33.306  0 123 ILE DDD N     1 ? 4 
ATOM   12103 C CA    . ILE D 1 123 ? 84.973  19.085  64.831  1.000 34.853  0 123 ILE DDD CA    1 ? 4 
ATOM   12104 C C     . ILE D 1 123 ? 85.874  19.760  63.772  1.000 35.092  0 123 ILE DDD C     1 ? 4 
ATOM   12105 O O     . ILE D 1 123 ? 85.554  20.887  63.384  1.000 33.140  0 123 ILE DDD O     1 ? 4 
ATOM   12106 C CB    . ILE D 1 123 ? 85.506  19.207  66.262  1.000 35.509  0 123 ILE DDD CB    1 ? 4 
ATOM   12107 C CG1   . ILE D 1 123 ? 84.415  18.776  67.249  1.000 35.758  0 123 ILE DDD CG1   1 ? 4 
ATOM   12108 C CG2   . ILE D 1 123 ? 86.094  20.599  66.519  1.000 34.307  0 123 ILE DDD CG2   1 ? 4 
ATOM   12109 C CD1   . ILE D 1 123 ? 84.948  18.535  68.659  1.000 36.085  0 123 ILE DDD CD1   1 ? 4 
ATOM   12110 N N     . ARG D 1 124 ? 86.935  19.093  63.297  1.000 37.348  0 124 ARG DDD N     1 ? 4 
ATOM   12111 C CA    . ARG D 1 124 ? 87.787  19.644  62.212  1.000 40.608  0 124 ARG DDD CA    1 ? 4 
ATOM   12112 C C     . ARG D 1 124 ? 86.908  19.924  60.975  1.000 41.830  0 124 ARG DDD C     1 ? 4 
ATOM   12113 O O     . ARG D 1 124 ? 86.936  21.069  60.445  1.000 41.781  0 124 ARG DDD O     1 ? 4 
ATOM   12114 C CB    . ARG D 1 124 ? 88.954  18.707  61.912  1.000 42.519  0 124 ARG DDD CB    1 ? 4 
ATOM   12115 C CG    . ARG D 1 124 ? 90.160  19.412  61.315  1.000 46.207  0 124 ARG DDD CG    1 ? 4 
ATOM   12116 C CD    . ARG D 1 124 ? 91.353  18.469  61.086  1.000 50.361  0 124 ARG DDD CD    1 ? 4 
ATOM   12117 N NE    . ARG D 1 124 ? 91.723  17.699  62.282  1.000 52.170  0 124 ARG DDD NE    1 ? 4 
ATOM   12118 C CZ    . ARG D 1 124 ? 91.555  16.379  62.451  1.000 52.070  0 124 ARG DDD CZ    1 ? 4 
ATOM   12119 N NH1   . ARG D 1 124 ? 91.058  15.611  61.480  1.000 51.354  0 124 ARG DDD NH1   1 ? 4 
ATOM   12120 N NH2   . ARG D 1 124 ? 91.914  15.831  63.602  1.000 50.140  0 124 ARG DDD NH2   1 ? 4 
ATOM   12121 N N     . MET D 1 125 ? 86.098  18.955  60.550  1.000 42.376  0 125 MET DDD N     1 ? 4 
ATOM   12122 C CA    . MET D 1 125 ? 85.169  19.123  59.395  1.000 42.945  0 125 MET DDD CA    1 ? 4 
ATOM   12123 C C     . MET D 1 125 ? 84.325  20.395  59.623  1.000 40.669  0 125 MET DDD C     1 ? 4 
ATOM   12124 O O     . MET D 1 125 ? 84.182  21.182  58.649  1.000 40.478  0 125 MET DDD O     1 ? 4 
ATOM   12125 C CB    . MET D 1 125 ? 84.306  17.865  59.215  1.000 46.897  0 125 MET DDD CB    1 ? 4 
ATOM   12126 C CG    . MET D 1 125 ? 83.309  17.911  58.038  1.000 52.964  0 125 MET DDD CG    1 ? 4 
ATOM   12127 S SD    . MET D 1 125 ? 81.719  18.844  58.397  1.000 63.094  0 125 MET DDD SD    1 ? 4 
ATOM   12128 C CE    . MET D 1 125 ? 81.104  17.934  59.827  1.000 63.757  0 125 MET DDD CE    1 ? 4 
ATOM   12129 N N     . LEU D 1 126 ? 83.832  20.629  60.862  1.000 39.246  0 126 LEU DDD N     1 ? 4 
ATOM   12130 C CA    . LEU D 1 126 ? 82.967  21.785  61.237  1.000 35.309  0 126 LEU DDD CA    1 ? 4 
ATOM   12131 C C     . LEU D 1 126 ? 83.790  23.067  61.227  1.000 33.639  0 126 LEU DDD C     1 ? 4 
ATOM   12132 O O     . LEU D 1 126 ? 83.268  24.082  60.784  1.000 32.535  0 126 LEU DDD O     1 ? 4 
ATOM   12133 C CB    . LEU D 1 126 ? 82.337  21.577  62.624  1.000 35.660  0 126 LEU DDD CB    1 ? 4 
ATOM   12134 C CG    . LEU D 1 126 ? 81.162  20.607  62.703  1.000 36.566  0 126 LEU DDD CG    1 ? 4 
ATOM   12135 C CD1   . LEU D 1 126 ? 80.845  20.264  64.140  1.000 38.579  0 126 LEU DDD CD1   1 ? 4 
ATOM   12136 C CD2   . LEU D 1 126 ? 79.936  21.178  62.032  1.000 35.082  0 126 LEU DDD CD2   1 ? 4 
ATOM   12137 N N     . ASN D 1 127 ? 85.027  23.043  61.719  1.000 33.245  0 127 ASN DDD N     1 ? 4 
ATOM   12138 C CA    . ASN D 1 127 ? 85.899  24.241  61.617  1.000 35.442  0 127 ASN DDD CA    1 ? 4 
ATOM   12139 C C     . ASN D 1 127 ? 85.894  24.684  60.136  1.000 34.348  0 127 ASN DDD C     1 ? 4 
ATOM   12140 O O     . ASN D 1 127 ? 85.618  25.828  59.865  1.000 34.009  0 127 ASN DDD O     1 ? 4 
ATOM   12141 C CB    . ASN D 1 127 ? 87.332  23.993  62.123  1.000 34.927  0 127 ASN DDD CB    1 ? 4 
ATOM   12142 C CG    . ASN D 1 127 ? 87.448  23.599  63.578  1.000 33.860  0 127 ASN DDD CG    1 ? 4 
ATOM   12143 O OD1   . ASN D 1 127 ? 88.250  22.753  63.925  1.000 33.210  0 127 ASN DDD OD1   1 ? 4 
ATOM   12144 N ND2   . ASN D 1 127 ? 86.657  24.181  64.454  1.000 34.823  0 127 ASN DDD ND2   1 ? 4 
ATOM   12145 N N     . PHE D 1 128 ? 86.199  23.778  59.218  1.000 36.411  0 128 PHE DDD N     1 ? 4 
ATOM   12146 C CA    . PHE D 1 128 ? 86.366  24.081  57.771  1.000 39.115  0 128 PHE DDD CA    1 ? 4 
ATOM   12147 C C     . PHE D 1 128 ? 85.026  24.541  57.186  1.000 40.187  0 128 PHE DDD C     1 ? 4 
ATOM   12148 O O     . PHE D 1 128 ? 84.946  25.615  56.537  1.000 42.043  0 128 PHE DDD O     1 ? 4 
ATOM   12149 C CB    . PHE D 1 128 ? 86.992  22.896  57.039  1.000 38.630  0 128 PHE DDD CB    1 ? 4 
ATOM   12150 C CG    . PHE D 1 128 ? 88.497  22.886  57.185  1.000 39.139  0 128 PHE DDD CG    1 ? 4 
ATOM   12151 C CD1   . PHE D 1 128 ? 89.269  23.968  56.783  1.000 39.628  0 128 PHE DDD CD1   1 ? 4 
ATOM   12152 C CD2   . PHE D 1 128 ? 89.138  21.815  57.775  1.000 39.996  0 128 PHE DDD CD2   1 ? 4 
ATOM   12153 C CE1   . PHE D 1 128 ? 90.651  23.957  56.934  1.000 40.587  0 128 PHE DDD CE1   1 ? 4 
ATOM   12154 C CE2   . PHE D 1 128 ? 90.524  21.799  57.925  1.000 39.989  0 128 PHE DDD CE2   1 ? 4 
ATOM   12155 C CZ    . PHE D 1 128 ? 91.276  22.878  57.523  1.000 40.097  0 128 PHE DDD CZ    1 ? 4 
ATOM   12156 N N     . SER D 1 129 ? 83.987  23.790  57.482  1.000 39.542  0 129 SER DDD N     1 ? 4 
ATOM   12157 C CA    . SER D 1 129 ? 82.599  24.100  57.069  1.000 42.968  0 129 SER DDD CA    1 ? 4 
ATOM   12158 C C     . SER D 1 129 ? 82.217  25.548  57.447  1.000 46.442  0 129 SER DDD C     1 ? 4 
ATOM   12159 O O     . SER D 1 129 ? 81.616  26.257  56.618  1.000 50.743  0 129 SER DDD O     1 ? 4 
ATOM   12160 C CB    . SER D 1 129 ? 81.692  23.054  57.661  1.000 41.855  0 129 SER DDD CB    1 ? 4 
ATOM   12161 O OG    . SER D 1 129 ? 80.385  23.277  57.221  1.000 44.298  0 129 SER DDD OG    1 ? 4 
ATOM   12162 N N     . TYR D 1 130 ? 82.565  26.009  58.649  1.000 49.390  0 130 TYR DDD N     1 ? 4 
ATOM   12163 C CA    . TYR D 1 130 ? 82.222  27.378  59.118  1.000 51.788  0 130 TYR DDD CA    1 ? 4 
ATOM   12164 C C     . TYR D 1 130 ? 83.108  28.433  58.433  1.000 52.398  0 130 TYR DDD C     1 ? 4 
ATOM   12165 O O     . TYR D 1 130 ? 82.564  29.502  58.092  1.000 51.761  0 130 TYR DDD O     1 ? 4 
ATOM   12166 C CB    . TYR D 1 130 ? 82.284  27.472  60.649  1.000 53.615  0 130 TYR DDD CB    1 ? 4 
ATOM   12167 C CG    . TYR D 1 130 ? 81.084  26.891  61.339  1.000 55.095  0 130 TYR DDD CG    1 ? 4 
ATOM   12168 C CD1   . TYR D 1 130 ? 79.827  27.403  61.069  1.000 55.506  0 130 TYR DDD CD1   1 ? 4 
ATOM   12169 C CD2   . TYR D 1 130 ? 81.182  25.818  62.217  1.000 57.194  0 130 TYR DDD CD2   1 ? 4 
ATOM   12170 C CE1   . TYR D 1 130 ? 78.691  26.874  61.653  1.000 57.693  0 130 TYR DDD CE1   1 ? 4 
ATOM   12171 C CE2   . TYR D 1 130 ? 80.054  25.280  62.817  1.000 57.718  0 130 TYR DDD CE2   1 ? 4 
ATOM   12172 C CZ    . TYR D 1 130 ? 78.808  25.816  62.537  1.000 58.098  0 130 TYR DDD CZ    1 ? 4 
ATOM   12173 O OH    . TYR D 1 130 ? 77.665  25.325  63.091  1.000 62.660  0 130 TYR DDD OH    1 ? 4 
ATOM   12174 N N     . ARG D 1 131 ? 84.407  28.174  58.247  1.000 52.350  0 131 ARG DDD N     1 ? 4 
ATOM   12175 C CA    . ARG D 1 131 ? 85.283  29.100  57.486  1.000 58.213  0 131 ARG DDD CA    1 ? 4 
ATOM   12176 C C     . ARG D 1 131 ? 84.639  29.384  56.131  1.000 58.352  0 131 ARG DDD C     1 ? 4 
ATOM   12177 O O     . ARG D 1 131 ? 84.558  30.545  55.773  1.000 60.752  0 131 ARG DDD O     1 ? 4 
ATOM   12178 C CB    . ARG D 1 131 ? 86.691  28.535  57.249  1.000 59.174  0 131 ARG DDD CB    1 ? 4 
ATOM   12179 C CG    . ARG D 1 131 ? 87.737  29.136  58.170  1.000 60.169  0 131 ARG DDD CG    1 ? 4 
ATOM   12180 C CD    . ARG D 1 131 ? 88.964  28.276  58.252  1.000 62.206  0 131 ARG DDD CD    1 ? 4 
ATOM   12181 N NE    . ARG D 1 131 ? 89.684  28.297  56.989  1.000 62.540  0 131 ARG DDD NE    1 ? 4 
ATOM   12182 C CZ    . ARG D 1 131 ? 90.902  27.790  56.816  1.000 63.702  0 131 ARG DDD CZ    1 ? 4 
ATOM   12183 N NH1   . ARG D 1 131 ? 91.549  27.228  57.830  1.000 62.980  0 131 ARG DDD NH1   1 ? 4 
ATOM   12184 N NH2   . ARG D 1 131 ? 91.466  27.838  55.624  1.000 64.149  0 131 ARG DDD NH2   1 ? 4 
ATOM   12185 N N     . THR D 1 132 ? 84.251  28.332  55.412  1.000 59.369  0 132 THR DDD N     1 ? 4 
ATOM   12186 C CA    . THR D 1 132 ? 83.646  28.401  54.058  1.000 62.275  0 132 THR DDD CA    1 ? 4 
ATOM   12187 C C     . THR D 1 132 ? 82.319  29.169  54.148  1.000 62.732  0 132 THR DDD C     1 ? 4 
ATOM   12188 O O     . THR D 1 132 ? 82.107  30.051  53.285  1.000 70.128  0 132 THR DDD O     1 ? 4 
ATOM   12189 C CB    . THR D 1 132 ? 83.493  26.999  53.454  1.000 64.543  0 132 THR DDD CB    1 ? 4 
ATOM   12190 O OG1   . THR D 1 132 ? 84.819  26.491  53.285  1.000 70.660  0 132 THR DDD OG1   1 ? 4 
ATOM   12191 C CG2   . THR D 1 132 ? 82.750  26.973  52.135  1.000 61.492  0 132 THR DDD CG2   1 ? 4 
ATOM   12192 N N     . GLY D 1 133 ? 81.474  28.842  55.129  1.000 60.410  0 133 GLY DDD N     1 ? 4 
ATOM   12193 C CA    . GLY D 1 133 ? 80.145  29.460  55.318  1.000 61.272  0 133 GLY DDD CA    1 ? 4 
ATOM   12194 C C     . GLY D 1 133 ? 80.244  30.980  55.439  1.000 63.981  0 133 GLY DDD C     1 ? 4 
ATOM   12195 O O     . GLY D 1 133 ? 79.360  31.696  54.890  1.000 60.401  0 133 GLY DDD O     1 ? 4 
ATOM   12196 N N     . LEU D 1 134 ? 81.298  31.452  56.117  1.000 64.016  0 134 LEU DDD N     1 ? 4 
ATOM   12197 C CA    . LEU D 1 134 ? 81.611  32.890  56.280  1.000 62.966  0 134 LEU DDD CA    1 ? 4 
ATOM   12198 C C     . LEU D 1 134 ? 82.088  33.476  54.945  1.000 66.788  0 134 LEU DDD C     1 ? 4 
ATOM   12199 O O     . LEU D 1 134 ? 81.554  34.510  54.528  1.000 70.478  0 134 LEU DDD O     1 ? 4 
ATOM   12200 C CB    . LEU D 1 134 ? 82.698  33.053  57.348  1.000 60.874  0 134 LEU DDD CB    1 ? 4 
ATOM   12201 C CG    . LEU D 1 134 ? 82.260  32.969  58.798  1.000 59.704  0 134 LEU DDD CG    1 ? 4 
ATOM   12202 C CD1   . LEU D 1 134 ? 83.453  33.259  59.693  1.000 59.889  0 134 LEU DDD CD1   1 ? 4 
ATOM   12203 C CD2   . LEU D 1 134 ? 81.139  33.958  59.059  1.000 58.228  0 134 LEU DDD CD2   1 ? 4 
ATOM   12204 N N     . ARG D 1 135 ? 83.071  32.850  54.302  1.000 70.788  0 135 ARG DDD N     1 ? 4 
ATOM   12205 C CA    . ARG D 1 135 ? 83.652  33.356  53.028  1.000 77.004  0 135 ARG DDD CA    1 ? 4 
ATOM   12206 C C     . ARG D 1 135 ? 82.538  33.415  51.968  1.000 76.564  0 135 ARG DDD C     1 ? 4 
ATOM   12207 O O     . ARG D 1 135 ? 82.362  34.486  51.374  1.000 72.210  0 135 ARG DDD O     1 ? 4 
ATOM   12208 C CB    . ARG D 1 135 ? 84.841  32.488  52.606  1.000 80.576  0 135 ARG DDD CB    1 ? 4 
ATOM   12209 C CG    . ARG D 1 135 ? 85.823  33.174  51.666  1.000 85.495  0 135 ARG DDD CG    1 ? 4 
ATOM   12210 C CD    . ARG D 1 135 ? 87.054  32.337  51.351  1.000 87.603  0 135 ARG DDD CD    1 ? 4 
ATOM   12211 N NE    . ARG D 1 135 ? 86.690  31.020  50.817  1.000 88.772  0 135 ARG DDD NE    1 ? 4 
ATOM   12212 C CZ    . ARG D 1 135 ? 86.729  29.872  51.492  1.000 89.301  0 135 ARG DDD CZ    1 ? 4 
ATOM   12213 N NH1   . ARG D 1 135 ? 87.139  29.842  52.752  1.000 89.125  0 135 ARG DDD NH1   1 ? 4 
ATOM   12214 N NH2   . ARG D 1 135 ? 86.335  28.753  50.907  1.000 90.053  0 135 ARG DDD NH2   1 ? 4 
ATOM   12215 N N     . VAL D 1 136 ? 81.791  32.323  51.765  1.000 71.997  0 136 VAL DDD N     1 ? 4 
ATOM   12216 C CA    . VAL D 1 136 ? 80.631  32.249  50.827  1.000 70.690  0 136 VAL DDD CA    1 ? 4 
ATOM   12217 C C     . VAL D 1 136 ? 79.621  33.335  51.225  1.000 72.608  0 136 VAL DDD C     1 ? 4 
ATOM   12218 O O     . VAL D 1 136 ? 79.105  34.000  50.319  1.000 74.074  0 136 VAL DDD O     1 ? 4 
ATOM   12219 C CB    . VAL D 1 136 ? 80.008  30.833  50.808  1.000 70.279  0 136 VAL DDD CB    1 ? 4 
ATOM   12220 C CG1   . VAL D 1 136 ? 78.562  30.803  50.304  1.000 67.652  0 136 VAL DDD CG1   1 ? 4 
ATOM   12221 C CG2   . VAL D 1 136 ? 80.876  29.864  50.008  1.000 68.841  0 136 VAL DDD CG2   1 ? 4 
ATOM   12222 N N     . GLY D 1 137 ? 79.376  33.529  52.528  1.000 72.439  0 137 GLY DDD N     1 ? 4 
ATOM   12223 C CA    . GLY D 1 137 ? 78.383  34.491  53.057  1.000 70.434  0 137 GLY DDD CA    1 ? 4 
ATOM   12224 C C     . GLY D 1 137 ? 78.873  35.935  53.053  1.000 69.341  0 137 GLY DDD C     1 ? 4 
ATOM   12225 O O     . GLY D 1 137 ? 78.162  36.800  53.558  1.000 64.318  0 137 GLY DDD O     1 ? 4 
ATOM   12226 N N     . ASN D 1 138 ? 80.069  36.171  52.517  1.000 73.843  0 138 ASN DDD N     1 ? 4 
ATOM   12227 C CA    . ASN D 1 138 ? 80.682  37.499  52.243  1.000 72.018  0 138 ASN DDD CA    1 ? 4 
ATOM   12228 C C     . ASN D 1 138 ? 81.006  38.195  53.567  1.000 68.307  0 138 ASN DDD C     1 ? 4 
ATOM   12229 O O     . ASN D 1 138 ? 80.812  39.413  53.673  1.000 66.033  0 138 ASN DDD O     1 ? 4 
ATOM   12230 C CB    . ASN D 1 138 ? 79.823  38.337  51.294  1.000 73.918  0 138 ASN DDD CB    1 ? 4 
ATOM   12231 C CG    . ASN D 1 138 ? 80.580  39.562  50.808  1.000 74.300  0 138 ASN DDD CG    1 ? 4 
ATOM   12232 O OD1   . ASN D 1 138 ? 81.778  39.498  50.538  1.000 70.415  0 138 ASN DDD OD1   1 ? 4 
ATOM   12233 N ND2   . ASN D 1 138 ? 79.908  40.699  50.735  1.000 73.041  0 138 ASN DDD ND2   1 ? 4 
ATOM   12234 N N     . VAL D 1 139 ? 81.499  37.428  54.536  1.000 70.696  0 139 VAL DDD N     1 ? 4 
ATOM   12235 C CA    . VAL D 1 139 ? 82.030  37.946  55.830  1.000 66.722  0 139 VAL DDD CA    1 ? 4 
ATOM   12236 C C     . VAL D 1 139 ? 83.551  37.802  55.800  1.000 66.476  0 139 VAL DDD C     1 ? 4 
ATOM   12237 O O     . VAL D 1 139 ? 84.023  36.672  55.462  1.000 64.752  0 139 VAL DDD O     1 ? 4 
ATOM   12238 C CB    . VAL D 1 139 ? 81.448  37.188  57.028  1.000 65.331  0 139 VAL DDD CB    1 ? 4 
ATOM   12239 C CG1   . VAL D 1 139 ? 82.025  37.702  58.351  1.000 65.303  0 139 VAL DDD CG1   1 ? 4 
ATOM   12240 C CG2   . VAL D 1 139 ? 79.930  37.229  57.030  1.000 65.753  0 139 VAL DDD CG2   1 ? 4 
ATOM   12241 N N     . GLU D 1 140 ? 84.255  38.892  56.134  1.000 65.380  0 140 GLU DDD N     1 ? 4 
ATOM   12242 C CA    . GLU D 1 140 ? 85.730  38.919  56.250  1.000 68.385  0 140 GLU DDD CA    1 ? 4 
ATOM   12243 C C     . GLU D 1 140 ? 86.158  38.372  57.618  1.000 66.734  0 140 GLU DDD C     1 ? 4 
ATOM   12244 O O     . GLU D 1 140 ? 85.979  39.072  58.641  1.000 63.639  0 140 GLU DDD O     1 ? 4 
ATOM   12245 C CB    . GLU D 1 140 ? 86.242  40.348  56.049  1.000 72.397  0 140 GLU DDD CB    1 ? 4 
ATOM   12246 C CG    . GLU D 1 140 ? 87.736  40.450  55.820  1.000 74.130  0 140 GLU DDD CG    1 ? 4 
ATOM   12247 C CD    . GLU D 1 140 ? 88.078  41.780  55.152  1.000 75.618  0 140 GLU DDD CD    1 ? 4 
ATOM   12248 O OE1   . GLU D 1 140 ? 87.707  42.805  55.736  1.000 72.506  0 140 GLU DDD OE1   1 ? 4 
ATOM   12249 O OE2   . GLU D 1 140 ? 88.614  41.774  54.011  1.000 75.277  0 140 GLU DDD OE2   1 ? 4 
ATOM   12250 N N     . TYR D 1 141 ? 86.693  37.154  57.620  1.000 66.940  0 141 TYR DDD N     1 ? 4 
ATOM   12251 C CA    . TYR D 1 141 ? 87.168  36.425  58.828  1.000 64.039  0 141 TYR DDD CA    1 ? 4 
ATOM   12252 C C     . TYR D 1 141 ? 88.625  36.802  59.072  1.000 62.097  0 141 TYR DDD C     1 ? 4 
ATOM   12253 O O     . TYR D 1 141 ? 89.408  36.650  58.150  1.000 61.017  0 141 TYR DDD O     1 ? 4 
ATOM   12254 C CB    . TYR D 1 141 ? 87.015  34.906  58.653  1.000 64.358  0 141 TYR DDD CB    1 ? 4 
ATOM   12255 C CG    . TYR D 1 141 ? 87.726  34.069  59.692  1.000 63.387  0 141 TYR DDD CG    1 ? 4 
ATOM   12256 C CD1   . TYR D 1 141 ? 87.603  34.353  61.048  1.000 61.779  0 141 TYR DDD CD1   1 ? 4 
ATOM   12257 C CD2   . TYR D 1 141 ? 88.508  32.980  59.333  1.000 58.835  0 141 TYR DDD CD2   1 ? 4 
ATOM   12258 C CE1   . TYR D 1 141 ? 88.235  33.584  62.014  1.000 57.831  0 141 TYR DDD CE1   1 ? 4 
ATOM   12259 C CE2   . TYR D 1 141 ? 89.130  32.186  60.287  1.000 56.609  0 141 TYR DDD CE2   1 ? 4 
ATOM   12260 C CZ    . TYR D 1 141 ? 88.997  32.496  61.635  1.000 56.718  0 141 TYR DDD CZ    1 ? 4 
ATOM   12261 O OH    . TYR D 1 141 ? 89.608  31.771  62.617  1.000 51.556  0 141 TYR DDD OH    1 ? 4 
ATOM   12262 N N     . ILE D 1 142 ? 88.970  37.228  60.288  1.000 64.237  0 142 ILE DDD N     1 ? 4 
ATOM   12263 C CA    . ILE D 1 142 ? 90.369  37.542  60.707  1.000 62.481  0 142 ILE DDD CA    1 ? 4 
ATOM   12264 C C     . ILE D 1 142 ? 90.680  36.762  61.987  1.000 60.401  0 142 ILE DDD C     1 ? 4 
ATOM   12265 O O     . ILE D 1 142 ? 89.989  36.999  63.007  1.000 57.891  0 142 ILE DDD O     1 ? 4 
ATOM   12266 C CB    . ILE D 1 142 ? 90.531  39.058  60.921  1.000 67.326  0 142 ILE DDD CB    1 ? 4 
ATOM   12267 C CG1   . ILE D 1 142 ? 90.245  39.838  59.632  1.000 67.412  0 142 ILE DDD CG1   1 ? 4 
ATOM   12268 C CG2   . ILE D 1 142 ? 91.906  39.400  61.504  1.000 67.425  0 142 ILE DDD CG2   1 ? 4 
ATOM   12269 C CD1   . ILE D 1 142 ? 90.051  41.316  59.859  1.000 67.735  0 142 ILE DDD CD1   1 ? 4 
ATOM   12270 N N     . ASN D 1 143 ? 91.666  35.865  61.923  1.000 55.505  0 143 ASN DDD N     1 ? 4 
ATOM   12271 C CA    . ASN D 1 143 ? 92.090  35.004  63.055  1.000 53.332  0 143 ASN DDD CA    1 ? 4 
ATOM   12272 C C     . ASN D 1 143 ? 93.084  35.817  63.884  1.000 52.814  0 143 ASN DDD C     1 ? 4 
ATOM   12273 O O     . ASN D 1 143 ? 94.292  35.538  63.766  1.000 52.627  0 143 ASN DDD O     1 ? 4 
ATOM   12274 C CB    . ASN D 1 143 ? 92.644  33.658  62.553  1.000 53.084  0 143 ASN DDD CB    1 ? 4 
ATOM   12275 C CG    . ASN D 1 143 ? 92.923  32.612  63.623  1.000 50.868  0 143 ASN DDD CG    1 ? 4 
ATOM   12276 O OD1   . ASN D 1 143 ? 92.397  32.645  64.736  1.000 49.598  0 143 ASN DDD OD1   1 ? 4 
ATOM   12277 N ND2   . ASN D 1 143 ? 93.747  31.638  63.284  1.000 49.939  0 143 ASN DDD ND2   1 ? 4 
ATOM   12278 N N     . ALA D 1 144 ? 92.593  36.793  64.660  1.000 52.072  0 144 ALA DDD N     1 ? 4 
ATOM   12279 C CA    . ALA D 1 144 ? 93.375  37.571  65.651  1.000 52.359  0 144 ALA DDD CA    1 ? 4 
ATOM   12280 C C     . ALA D 1 144 ? 92.480  38.037  66.811  1.000 55.536  0 144 ALA DDD C     1 ? 4 
ATOM   12281 O O     . ALA D 1 144 ? 91.243  38.154  66.618  1.000 55.596  0 144 ALA DDD O     1 ? 4 
ATOM   12282 C CB    . ALA D 1 144 ? 94.014  38.761  64.974  1.000 53.957  0 144 ALA DDD CB    1 ? 4 
ATOM   12283 N N     . LEU D 1 145 ? 93.085  38.337  67.966  1.000 56.806  0 145 LEU DDD N     1 ? 4 
ATOM   12284 C CA    . LEU D 1 145 ? 92.394  38.985  69.115  1.000 58.378  0 145 LEU DDD CA    1 ? 4 
ATOM   12285 C C     . LEU D 1 145 ? 92.132  40.457  68.794  1.000 60.090  0 145 LEU DDD C     1 ? 4 
ATOM   12286 O O     . LEU D 1 145 ? 93.086  41.161  68.394  1.000 59.738  0 145 LEU DDD O     1 ? 4 
ATOM   12287 C CB    . LEU D 1 145 ? 93.253  38.878  70.376  1.000 60.287  0 145 LEU DDD CB    1 ? 4 
ATOM   12288 C CG    . LEU D 1 145 ? 93.275  37.510  71.047  1.000 60.123  0 145 LEU DDD CG    1 ? 4 
ATOM   12289 C CD1   . LEU D 1 145 ? 94.240  37.490  72.217  1.000 62.741  0 145 LEU DDD CD1   1 ? 4 
ATOM   12290 C CD2   . LEU D 1 145 ? 91.888  37.104  71.505  1.000 59.401  0 145 LEU DDD CD2   1 ? 4 
ATOM   12291 N N     . ALA D 1 146 ? 90.890  40.900  68.997  1.000 62.536  0 146 ALA DDD N     1 ? 4 
ATOM   12292 C CA    . ALA D 1 146 ? 90.419  42.285  68.777  1.000 64.065  0 146 ALA DDD CA    1 ? 4 
ATOM   12293 C C     . ALA D 1 146 ? 90.171  42.943  70.136  1.000 69.280  0 146 ALA DDD C     1 ? 4 
ATOM   12294 O O     . ALA D 1 146 ? 89.870  42.199  71.074  1.000 68.886  0 146 ALA DDD O     1 ? 4 
ATOM   12295 C CB    . ALA D 1 146 ? 89.178  42.266  67.926  1.000 63.997  0 146 ALA DDD CB    1 ? 4 
ATOM   12296 N N     . LYS D 1 147 ? 90.336  44.267  70.244  1.000 71.652  0 147 LYS DDD N     1 ? 4 
ATOM   12297 C CA    . LYS D 1 147 ? 89.922  45.058  71.440  1.000 75.099  0 147 LYS DDD CA    1 ? 4 
ATOM   12298 C C     . LYS D 1 147 ? 89.273  46.386  70.988  1.000 76.417  0 147 LYS DDD C     1 ? 4 
ATOM   12299 O O     . LYS D 1 147 ? 89.482  46.818  69.834  1.000 75.181  0 147 LYS DDD O     1 ? 4 
ATOM   12300 C CB    . LYS D 1 147 ? 91.111  45.264  72.392  1.000 76.513  0 147 LYS DDD CB    1 ? 4 
ATOM   12301 C CG    . LYS D 1 147 ? 92.282  46.083  71.841  1.000 81.222  0 147 LYS DDD CG    1 ? 4 
ATOM   12302 C CD    . LYS D 1 147 ? 93.064  46.865  72.882  1.000 82.479  0 147 LYS DDD CD    1 ? 4 
ATOM   12303 C CE    . LYS D 1 147 ? 94.262  46.117  73.420  1.000 81.075  0 147 LYS DDD CE    1 ? 4 
ATOM   12304 N NZ    . LYS D 1 147 ? 94.763  46.746  74.664  1.000 79.278  0 147 LYS DDD NZ    1 ? 4 
ATOM   12305 N N     . LEU D 1 148 ? 88.464  46.998  71.852  1.000 79.910  0 148 LEU DDD N     1 ? 4 
ATOM   12306 C CA    . LEU D 1 148 ? 87.795  48.299  71.568  1.000 83.918  0 148 LEU DDD CA    1 ? 4 
ATOM   12307 C C     . LEU D 1 148 ? 88.798  49.438  71.776  1.000 88.606  0 148 LEU DDD C     1 ? 4 
ATOM   12308 O O     . LEU D 1 148 ? 89.569  49.400  72.769  1.000 94.547  0 148 LEU DDD O     1 ? 4 
ATOM   12309 C CB    . LEU D 1 148 ? 86.576  48.464  72.482  1.000 80.999  0 148 LEU DDD CB    1 ? 4 
ATOM   12310 C CG    . LEU D 1 148 ? 85.489  47.406  72.306  1.000 80.776  0 148 LEU DDD CG    1 ? 4 
ATOM   12311 C CD1   . LEU D 1 148 ? 84.433  47.529  73.389  1.000 83.142  0 148 LEU DDD CD1   1 ? 4 
ATOM   12312 C CD2   . LEU D 1 148 ? 84.848  47.497  70.929  1.000 80.593  0 148 LEU DDD CD2   1 ? 4 
ATOM   12313 N N     . ILE D 1 149 ? 88.817  50.390  70.845  1.000 94.139  0 149 ILE DDD N     1 ? 4 
ATOM   12314 C CA    . ILE D 1 149 ? 89.597  51.657  70.958  1.000 102.918 0 149 ILE DDD CA    1 ? 4 
ATOM   12315 C C     . ILE D 1 149 ? 88.621  52.768  71.358  1.000 101.430 0 149 ILE DDD C     1 ? 4 
ATOM   12316 O O     . ILE D 1 149 ? 88.964  53.527  72.260  1.000 105.476 0 149 ILE DDD O     1 ? 4 
ATOM   12317 C CB    . ILE D 1 149 ? 90.375  51.947  69.654  1.000 108.074 0 149 ILE DDD CB    1 ? 4 
ATOM   12318 C CG1   . ILE D 1 149 ? 91.551  50.977  69.471  1.000 106.040 0 149 ILE DDD CG1   1 ? 4 
ATOM   12319 C CG2   . ILE D 1 149 ? 90.819  53.403  69.568  1.000 111.683 0 149 ILE DDD CG2   1 ? 4 
ATOM   12320 C CD1   . ILE D 1 149 ? 92.594  51.050  70.564  1.000 105.522 0 149 ILE DDD CD1   1 ? 4 
ATOM   12321 N N     . ASP D 1 150 ? 87.440  52.821  70.733  1.000 98.343  0 150 ASP DDD N     1 ? 4 
ATOM   12322 C CA    . ASP D 1 150 ? 86.354  53.796  71.042  1.000 96.860  0 150 ASP DDD CA    1 ? 4 
ATOM   12323 C C     . ASP D 1 150 ? 85.028  53.258  70.497  1.000 91.130  0 150 ASP DDD C     1 ? 4 
ATOM   12324 O O     . ASP D 1 150 ? 84.988  52.203  69.877  1.000 92.997  0 150 ASP DDD O     1 ? 4 
ATOM   12325 C CB    . ASP D 1 150 ? 86.747  55.191  70.538  1.000 102.057 0 150 ASP DDD CB    1 ? 4 
ATOM   12326 C CG    . ASP D 1 150 ? 86.775  55.361  69.024  1.000 105.599 0 150 ASP DDD CG    1 ? 4 
ATOM   12327 O OD1   . ASP D 1 150 ? 85.919  54.754  68.338  1.000 109.228 0 150 ASP DDD OD1   1 ? 4 
ATOM   12328 O OD2   . ASP D 1 150 ? 87.658  56.115  68.539  1.000 105.583 0 150 ASP DDD OD2   1 ? 4 
ATOM   12329 N N     . PRO D 1 151 ? 83.884  53.948  70.700  1.000 89.052  0 151 PRO DDD N     1 ? 4 
ATOM   12330 C CA    . PRO D 1 151 ? 82.587  53.439  70.246  1.000 86.362  0 151 PRO DDD CA    1 ? 4 
ATOM   12331 C C     . PRO D 1 151 ? 82.477  52.986  68.784  1.000 82.570  0 151 PRO DDD C     1 ? 4 
ATOM   12332 O O     . PRO D 1 151 ? 81.478  52.385  68.475  1.000 79.127  0 151 PRO DDD O     1 ? 4 
ATOM   12333 C CB    . PRO D 1 151 ? 81.645  54.644  70.439  1.000 88.146  0 151 PRO DDD CB    1 ? 4 
ATOM   12334 C CG    . PRO D 1 151 ? 82.260  55.382  71.615  1.000 89.363  0 151 PRO DDD CG    1 ? 4 
ATOM   12335 C CD    . PRO D 1 151 ? 83.759  55.240  71.395  1.000 89.544  0 151 PRO DDD CD    1 ? 4 
ATOM   12336 N N     . HIS D 1 152 ? 83.450  53.301  67.920  1.000 85.749  0 152 HIS DDD N     1 ? 4 
ATOM   12337 C CA    . HIS D 1 152 ? 83.399  52.951  66.470  1.000 87.668  0 152 HIS DDD CA    1 ? 4 
ATOM   12338 C C     . HIS D 1 152 ? 84.701  52.319  65.958  1.000 87.811  0 152 HIS DDD C     1 ? 4 
ATOM   12339 O O     . HIS D 1 152 ? 84.809  52.172  64.722  1.000 89.537  0 152 HIS DDD O     1 ? 4 
ATOM   12340 C CB    . HIS D 1 152 ? 83.055  54.186  65.626  1.000 86.634  0 152 HIS DDD CB    1 ? 4 
ATOM   12341 C CG    . HIS D 1 152 ? 81.669  54.678  65.849  1.000 87.808  0 152 HIS DDD CG    1 ? 4 
ATOM   12342 N ND1   . HIS D 1 152 ? 80.564  53.978  65.408  1.000 89.986  0 152 HIS DDD ND1   1 ? 4 
ATOM   12343 C CD2   . HIS D 1 152 ? 81.204  55.772  66.488  1.000 87.751  0 152 HIS DDD CD2   1 ? 4 
ATOM   12344 C CE1   . HIS D 1 152 ? 79.473  54.629  65.752  1.000 87.924  0 152 HIS DDD CE1   1 ? 4 
ATOM   12345 N NE2   . HIS D 1 152 ? 79.838  55.733  66.419  1.000 89.519  0 152 HIS DDD NE2   1 ? 4 
ATOM   12346 N N     . SER D 1 153 ? 85.644  51.946  66.827  1.000 86.869  0 153 SER DDD N     1 ? 4 
ATOM   12347 C CA    . SER D 1 153 ? 87.002  51.508  66.397  1.000 93.662  0 153 SER DDD CA    1 ? 4 
ATOM   12348 C C     . SER D 1 153 ? 87.457  50.277  67.177  1.000 88.889  0 153 SER DDD C     1 ? 4 
ATOM   12349 O O     . SER D 1 153 ? 87.264  50.252  68.406  1.000 93.550  0 153 SER DDD O     1 ? 4 
ATOM   12350 C CB    . SER D 1 153 ? 87.999  52.630  66.528  1.000 97.451  0 153 SER DDD CB    1 ? 4 
ATOM   12351 O OG    . SER D 1 153 ? 87.454  53.819  65.971  1.000 99.178  0 153 SER DDD OG    1 ? 4 
ATOM   12352 N N     . VAL D 1 154 ? 88.070  49.319  66.483  1.000 85.439  0 154 VAL DDD N     1 ? 4 
ATOM   12353 C CA    . VAL D 1 154 ? 88.600  48.053  67.071  1.000 82.552  0 154 VAL DDD CA    1 ? 4 
ATOM   12354 C C     . VAL D 1 154 ? 90.040  47.872  66.580  1.000 79.027  0 154 VAL DDD C     1 ? 4 
ATOM   12355 O O     . VAL D 1 154 ? 90.320  48.273  65.435  1.000 76.466  0 154 VAL DDD O     1 ? 4 
ATOM   12356 C CB    . VAL D 1 154 ? 87.705  46.854  66.705  1.000 82.279  0 154 VAL DDD CB    1 ? 4 
ATOM   12357 C CG1   . VAL D 1 154 ? 87.840  46.488  65.249  1.000 84.371  0 154 VAL DDD CG1   1 ? 4 
ATOM   12358 C CG2   . VAL D 1 154 ? 87.977  45.639  67.563  1.000 85.360  0 154 VAL DDD CG2   1 ? 4 
ATOM   12359 N N     . GLU D 1 155 ? 90.913  47.320  67.429  1.000 78.717  0 155 GLU DDD N     1 ? 4 
ATOM   12360 C CA    . GLU D 1 155 ? 92.361  47.123  67.159  1.000 81.732  0 155 GLU DDD CA    1 ? 4 
ATOM   12361 C C     . GLU D 1 155 ? 92.683  45.629  67.158  1.000 79.330  0 155 GLU DDD C     1 ? 4 
ATOM   12362 O O     . GLU D 1 155 ? 92.228  44.943  68.080  1.000 82.192  0 155 GLU DDD O     1 ? 4 
ATOM   12363 C CB    . GLU D 1 155 ? 93.192  47.813  68.239  1.000 85.983  0 155 GLU DDD CB    1 ? 4 
ATOM   12364 C CG    . GLU D 1 155 ? 94.706  47.770  67.999  1.000 90.374  0 155 GLU DDD CG    1 ? 4 
ATOM   12365 C CD    . GLU D 1 155 ? 95.471  48.674  68.954  1.000 93.142  0 155 GLU DDD CD    1 ? 4 
ATOM   12366 O OE1   . GLU D 1 155 ? 95.266  48.500  70.187  1.000 97.578  0 155 GLU DDD OE1   1 ? 4 
ATOM   12367 O OE2   . GLU D 1 155 ? 96.226  49.573  68.474  1.000 91.986  0 155 GLU DDD OE2   1 ? 4 
ATOM   12368 N N     . TYR D 1 156 ? 93.488  45.169  66.200  1.000 74.984  0 156 TYR DDD N     1 ? 4 
ATOM   12369 C CA    . TYR D 1 156 ? 94.088  43.811  66.213  1.000 72.127  0 156 TYR DDD CA    1 ? 4 
ATOM   12370 C C     . TYR D 1 156 ? 95.542  43.854  65.718  1.000 72.436  0 156 TYR DDD C     1 ? 4 
ATOM   12371 O O     . TYR D 1 156 ? 95.909  44.737  64.901  1.000 66.843  0 156 TYR DDD O     1 ? 4 
ATOM   12372 C CB    . TYR D 1 156 ? 93.236  42.854  65.375  1.000 69.800  0 156 TYR DDD CB    1 ? 4 
ATOM   12373 C CG    . TYR D 1 156 ? 93.265  43.111  63.894  1.000 66.749  0 156 TYR DDD CG    1 ? 4 
ATOM   12374 C CD1   . TYR D 1 156 ? 92.519  44.128  63.318  1.000 66.223  0 156 TYR DDD CD1   1 ? 4 
ATOM   12375 C CD2   . TYR D 1 156 ? 94.054  42.329  63.068  1.000 66.371  0 156 TYR DDD CD2   1 ? 4 
ATOM   12376 C CE1   . TYR D 1 156 ? 92.538  44.343  61.946  1.000 65.418  0 156 TYR DDD CE1   1 ? 4 
ATOM   12377 C CE2   . TYR D 1 156 ? 94.101  42.542  61.699  1.000 66.232  0 156 TYR DDD CE2   1 ? 4 
ATOM   12378 C CZ    . TYR D 1 156 ? 93.338  43.549  61.141  1.000 65.657  0 156 TYR DDD CZ    1 ? 4 
ATOM   12379 O OH    . TYR D 1 156 ? 93.398  43.718  59.795  1.000 64.104  0 156 TYR DDD OH    1 ? 4 
ATOM   12380 N N     . GLU D 1 157 ? 96.336  42.899  66.209  1.000 75.136  0 157 GLU DDD N     1 ? 4 
ATOM   12381 C CA    . GLU D 1 157 ? 97.716  42.608  65.756  1.000 78.927  0 157 GLU DDD CA    1 ? 4 
ATOM   12382 C C     . GLU D 1 157 ? 97.661  41.774  64.476  1.000 80.206  0 157 GLU DDD C     1 ? 4 
ATOM   12383 O O     . GLU D 1 157 ? 96.757  40.924  64.355  1.000 81.095  0 157 GLU DDD O     1 ? 4 
ATOM   12384 C CB    . GLU D 1 157 ? 98.462  41.804  66.826  1.000 79.939  0 157 GLU DDD CB    1 ? 4 
ATOM   12385 C CG    . GLU D 1 157 ? 99.352  42.620  67.738  1.000 83.165  0 157 GLU DDD CG    1 ? 4 
ATOM   12386 C CD    . GLU D 1 157 ? 100.572 41.863  68.257  1.000 86.078  0 157 GLU DDD CD    1 ? 4 
ATOM   12387 O OE1   . GLU D 1 157 ? 100.912 40.783  67.699  1.000 76.744  0 157 GLU DDD OE1   1 ? 4 
ATOM   12388 O OE2   . GLU D 1 157 ? 101.193 42.363  69.215  1.000 92.587  0 157 GLU DDD OE2   1 ? 4 
ATOM   12389 N N     . ASP D 1 158 ? 98.621  42.003  63.583  1.000 84.633  0 158 ASP DDD N     1 ? 4 
ATOM   12390 C CA    . ASP D 1 158 ? 98.752  41.308  62.275  1.000 85.322  0 158 ASP DDD CA    1 ? 4 
ATOM   12391 C C     . ASP D 1 158 ? 100.227 41.368  61.865  1.000 82.995  0 158 ASP DDD C     1 ? 4 
ATOM   12392 O O     . ASP D 1 158 ? 100.669 42.450  61.468  1.000 80.441  0 158 ASP DDD O     1 ? 4 
ATOM   12393 C CB    . ASP D 1 158 ? 97.801  41.945  61.262  1.000 87.183  0 158 ASP DDD CB    1 ? 4 
ATOM   12394 C CG    . ASP D 1 158 ? 97.998  41.471  59.837  1.000 91.811  0 158 ASP DDD CG    1 ? 4 
ATOM   12395 O OD1   . ASP D 1 158 ? 98.166  40.254  59.627  1.000 93.748  0 158 ASP DDD OD1   1 ? 4 
ATOM   12396 O OD2   . ASP D 1 158 ? 97.961  42.335  58.951  1.000 94.115  0 158 ASP DDD OD2   1 ? 4 
ATOM   12397 N N     . ASN D 1 159 ? 100.954 40.256  62.009  1.000 85.383  0 159 ASN DDD N     1 ? 4 
ATOM   12398 C CA    . ASN D 1 159 ? 102.442 40.203  61.926  1.000 92.722  0 159 ASN DDD CA    1 ? 4 
ATOM   12399 C C     . ASN D 1 159 ? 103.030 41.190  62.950  1.000 96.098  0 159 ASN DDD C     1 ? 4 
ATOM   12400 O O     . ASN D 1 159 ? 103.943 41.956  62.584  1.000 96.109  0 159 ASN DDD O     1 ? 4 
ATOM   12401 C CB    . ASN D 1 159 ? 102.945 40.493  60.506  1.000 96.013  0 159 ASN DDD CB    1 ? 4 
ATOM   12402 C CG    . ASN D 1 159 ? 102.621 39.398  59.513  1.000 98.464  0 159 ASN DDD CG    1 ? 4 
ATOM   12403 O OD1   . ASN D 1 159 ? 103.374 38.434  59.381  1.000 98.582  0 159 ASN DDD OD1   1 ? 4 
ATOM   12404 N ND2   . ASN D 1 159 ? 101.517 39.550  58.795  1.000 100.224 0 159 ASN DDD ND2   1 ? 4 
ATOM   12405 N N     . GLY D 1 160 ? 102.506 41.186  64.181  1.000 96.176  0 160 GLY DDD N     1 ? 4 
ATOM   12406 C CA    . GLY D 1 160 ? 102.956 42.048  65.294  1.000 96.726  0 160 GLY DDD CA    1 ? 4 
ATOM   12407 C C     . GLY D 1 160 ? 102.905 43.528  64.938  1.000 98.545  0 160 GLY DDD C     1 ? 4 
ATOM   12408 O O     . GLY D 1 160 ? 103.802 44.288  65.367  1.000 93.204  0 160 GLY DDD O     1 ? 4 
ATOM   12409 N N     . GLN D 1 161 ? 101.891 43.927  64.169  1.000 100.485 0 161 GLN DDD N     1 ? 4 
ATOM   12410 C CA    . GLN D 1 161 ? 101.645 45.335  63.762  1.000 98.770  0 161 GLN DDD CA    1 ? 4 
ATOM   12411 C C     . GLN D 1 161 ? 100.175 45.669  64.014  1.000 94.658  0 161 GLN DDD C     1 ? 4 
ATOM   12412 O O     . GLN D 1 161 ? 99.298  45.204  63.247  1.000 94.049  0 161 GLN DDD O     1 ? 4 
ATOM   12413 C CB    . GLN D 1 161 ? 102.028 45.524  62.293  1.000 103.425 0 161 GLN DDD CB    1 ? 4 
ATOM   12414 C CG    . GLN D 1 161 ? 103.533 45.483  62.050  1.000 110.303 0 161 GLN DDD CG    1 ? 4 
ATOM   12415 C CD    . GLN D 1 161 ? 103.900 44.797  60.751  1.000 115.396 0 161 GLN DDD CD    1 ? 4 
ATOM   12416 O OE1   . GLN D 1 161 ? 103.254 43.830  60.363  1.000 117.719 0 161 GLN DDD OE1   1 ? 4 
ATOM   12417 N NE2   . GLN D 1 161 ? 104.940 45.274  60.075  1.000 117.121 0 161 GLN DDD NE2   1 ? 4 
ATOM   12418 N N     . LYS D 1 162 ? 99.933  46.451  65.065  1.000 90.710  0 162 LYS DDD N     1 ? 4 
ATOM   12419 C CA    . LYS D 1 162 ? 98.603  47.018  65.412  1.000 86.560  0 162 LYS DDD CA    1 ? 4 
ATOM   12420 C C     . LYS D 1 162 ? 97.933  47.545  64.143  1.000 84.303  0 162 LYS DDD C     1 ? 4 
ATOM   12421 O O     . LYS D 1 162 ? 98.595  48.285  63.387  1.000 79.684  0 162 LYS DDD O     1 ? 4 
ATOM   12422 C CB    . LYS D 1 162 ? 98.747  48.179  66.400  1.000 86.379  0 162 LYS DDD CB    1 ? 4 
ATOM   12423 C CG    . LYS D 1 162 ? 99.389  47.838  67.732  1.000 85.372  0 162 LYS DDD CG    1 ? 4 
ATOM   12424 C CD    . LYS D 1 162 ? 98.687  46.740  68.490  1.000 83.299  0 162 LYS DDD CD    1 ? 4 
ATOM   12425 C CE    . LYS D 1 162 ? 99.498  46.290  69.681  1.000 83.195  0 162 LYS DDD CE    1 ? 4 
ATOM   12426 N NZ    . LYS D 1 162 ? 98.655  45.598  70.683  1.000 80.852  0 162 LYS DDD NZ    1 ? 4 
ATOM   12427 N N     . LYS D 1 163 ? 96.680  47.156  63.919  1.000 83.150  0 163 LYS DDD N     1 ? 4 
ATOM   12428 C CA    . LYS D 1 163 ? 95.795  47.764  62.895  1.000 85.967  0 163 LYS DDD CA    1 ? 4 
ATOM   12429 C C     . LYS D 1 163 ? 94.505  48.200  63.586  1.000 85.008  0 163 LYS DDD C     1 ? 4 
ATOM   12430 O O     . LYS D 1 163 ? 94.109  47.547  64.563  1.000 90.832  0 163 LYS DDD O     1 ? 4 
ATOM   12431 C CB    . LYS D 1 163 ? 95.511  46.783  61.757  1.000 88.301  0 163 LYS DDD CB    1 ? 4 
ATOM   12432 C CG    . LYS D 1 163 ? 96.744  46.336  60.981  1.000 89.074  0 163 LYS DDD CG    1 ? 4 
ATOM   12433 C CD    . LYS D 1 163 ? 96.433  45.887  59.577  1.000 89.392  0 163 LYS DDD CD    1 ? 4 
ATOM   12434 C CE    . LYS D 1 163 ? 97.671  45.704  58.730  1.000 91.147  0 163 LYS DDD CE    1 ? 4 
ATOM   12435 N NZ    . LYS D 1 163 ? 97.324  45.399  57.322  1.000 89.625  0 163 LYS DDD NZ    1 ? 4 
ATOM   12436 N N     . THR D 1 164 ? 93.913  49.294  63.118  1.000 82.750  0 164 THR DDD N     1 ? 4 
ATOM   12437 C CA    . THR D 1 164 ? 92.651  49.860  63.651  1.000 79.700  0 164 THR DDD CA    1 ? 4 
ATOM   12438 C C     . THR D 1 164 ? 91.681  49.949  62.476  1.000 78.775  0 164 THR DDD C     1 ? 4 
ATOM   12439 O O     . THR D 1 164 ? 92.124  50.309  61.381  1.000 74.020  0 164 THR DDD O     1 ? 4 
ATOM   12440 C CB    . THR D 1 164 ? 92.899  51.192  64.374  1.000 79.934  0 164 THR DDD CB    1 ? 4 
ATOM   12441 O OG1   . THR D 1 164 ? 93.761  50.952  65.489  1.000 75.686  0 164 THR DDD OG1   1 ? 4 
ATOM   12442 C CG2   . THR D 1 164 ? 91.628  51.858  64.861  1.000 79.479  0 164 THR DDD CG2   1 ? 4 
ATOM   12443 N N     . ILE D 1 165 ? 90.430  49.555  62.687  1.000 80.172  0 165 ILE DDD N     1 ? 4 
ATOM   12444 C CA    . ILE D 1 165 ? 89.360  49.610  61.646  1.000 81.153  0 165 ILE DDD CA    1 ? 4 
ATOM   12445 C C     . ILE D 1 165 ? 88.091  50.178  62.290  1.000 76.117  0 165 ILE DDD C     1 ? 4 
ATOM   12446 O O     . ILE D 1 165 ? 87.923  50.021  63.524  1.000 70.295  0 165 ILE DDD O     1 ? 4 
ATOM   12447 C CB    . ILE D 1 165 ? 89.125  48.225  61.007  1.000 82.735  0 165 ILE DDD CB    1 ? 4 
ATOM   12448 C CG1   . ILE D 1 165 ? 88.577  47.221  62.022  1.000 83.482  0 165 ILE DDD CG1   1 ? 4 
ATOM   12449 C CG2   . ILE D 1 165 ? 90.395  47.719  60.343  1.000 84.655  0 165 ILE DDD CG2   1 ? 4 
ATOM   12450 C CD1   . ILE D 1 165 ? 87.936  46.007  61.397  1.000 83.355  0 165 ILE DDD CD1   1 ? 4 
ATOM   12451 N N     . THR D 1 166 ? 87.236  50.802  61.478  1.000 73.836  0 166 THR DDD N     1 ? 4 
ATOM   12452 C CA    . THR D 1 166 ? 86.090  51.605  61.964  1.000 77.558  0 166 THR DDD CA    1 ? 4 
ATOM   12453 C C     . THR D 1 166 ? 84.791  50.946  61.510  1.000 74.330  0 166 THR DDD C     1 ? 4 
ATOM   12454 O O     . THR D 1 166 ? 84.758  50.408  60.376  1.000 76.167  0 166 THR DDD O     1 ? 4 
ATOM   12455 C CB    . THR D 1 166 ? 86.205  53.062  61.500  1.000 79.339  0 166 THR DDD CB    1 ? 4 
ATOM   12456 O OG1   . THR D 1 166 ? 86.251  53.003  60.073  1.000 81.944  0 166 THR DDD OG1   1 ? 4 
ATOM   12457 C CG2   . THR D 1 166 ? 87.415  53.777  62.073  1.000 78.770  0 166 THR DDD CG2   1 ? 4 
ATOM   12458 N N     . SER D 1 167 ? 83.763  51.007  62.357  1.000 71.989  0 167 SER DDD N     1 ? 4 
ATOM   12459 C CA    . SER D 1 167 ? 82.436  50.413  62.074  1.000 76.423  0 167 SER DDD CA    1 ? 4 
ATOM   12460 C C     . SER D 1 167 ? 81.305  51.308  62.589  1.000 78.087  0 167 SER DDD C     1 ? 4 
ATOM   12461 O O     . SER D 1 167 ? 81.479  51.943  63.649  1.000 76.397  0 167 SER DDD O     1 ? 4 
ATOM   12462 C CB    . SER D 1 167 ? 82.342  49.026  62.654  1.000 77.196  0 167 SER DDD CB    1 ? 4 
ATOM   12463 O OG    . SER D 1 167 ? 81.456  48.233  61.869  1.000 80.517  0 167 SER DDD OG    1 ? 4 
ATOM   12464 N N     . ARG D 1 168 ? 80.182  51.330  61.860  1.000 81.707  0 168 ARG DDD N     1 ? 4 
ATOM   12465 C CA    . ARG D 1 168 ? 78.907  51.959  62.304  1.000 83.924  0 168 ARG DDD CA    1 ? 4 
ATOM   12466 C C     . ARG D 1 168 ? 78.506  51.272  63.612  1.000 81.840  0 168 ARG DDD C     1 ? 4 
ATOM   12467 O O     . ARG D 1 168 ? 78.247  51.975  64.610  1.000 75.781  0 168 ARG DDD O     1 ? 4 
ATOM   12468 C CB    . ARG D 1 168 ? 77.866  51.857  61.180  1.000 86.669  0 168 ARG DDD CB    1 ? 4 
ATOM   12469 C CG    . ARG D 1 168 ? 76.590  52.670  61.373  1.000 88.298  0 168 ARG DDD CG    1 ? 4 
ATOM   12470 C CD    . ARG D 1 168 ? 75.841  52.716  60.055  1.000 89.957  0 168 ARG DDD CD    1 ? 4 
ATOM   12471 N NE    . ARG D 1 168 ? 74.436  53.104  60.136  1.000 89.865  0 168 ARG DDD NE    1 ? 4 
ATOM   12472 C CZ    . ARG D 1 168 ? 73.500  52.759  59.249  1.000 92.188  0 168 ARG DDD CZ    1 ? 4 
ATOM   12473 N NH1   . ARG D 1 168 ? 73.783  51.996  58.205  1.000 89.752  0 168 ARG DDD NH1   1 ? 4 
ATOM   12474 N NH2   . ARG D 1 168 ? 72.256  53.171  59.413  1.000 95.472  0 168 ARG DDD NH2   1 ? 4 
ATOM   12475 N N     . TYR D 1 169 ? 78.548  49.935  63.613  1.000 82.672  0 169 TYR DDD N     1 ? 4 
ATOM   12476 C CA    . TYR D 1 169 ? 78.055  49.061  64.708  1.000 81.810  0 169 TYR DDD CA    1 ? 4 
ATOM   12477 C C     . TYR D 1 169 ? 79.151  48.057  65.090  1.000 77.069  0 169 TYR DDD C     1 ? 4 
ATOM   12478 O O     . TYR D 1 169 ? 79.894  47.588  64.228  1.000 77.862  0 169 TYR DDD O     1 ? 4 
ATOM   12479 C CB    . TYR D 1 169 ? 76.742  48.386  64.288  1.000 81.075  0 169 TYR DDD CB    1 ? 4 
ATOM   12480 C CG    . TYR D 1 169 ? 75.600  49.335  63.998  1.000 81.035  0 169 TYR DDD CG    1 ? 4 
ATOM   12481 C CD1   . TYR D 1 169 ? 75.118  50.206  64.962  1.000 80.664  0 169 TYR DDD CD1   1 ? 4 
ATOM   12482 C CD2   . TYR D 1 169 ? 75.004  49.372  62.748  1.000 84.054  0 169 TYR DDD CD2   1 ? 4 
ATOM   12483 C CE1   . TYR D 1 169 ? 74.066  51.071  64.701  1.000 81.101  0 169 TYR DDD CE1   1 ? 4 
ATOM   12484 C CE2   . TYR D 1 169 ? 73.955  50.232  62.463  1.000 83.600  0 169 TYR DDD CE2   1 ? 4 
ATOM   12485 C CZ    . TYR D 1 169 ? 73.492  51.095  63.440  1.000 82.733  0 169 TYR DDD CZ    1 ? 4 
ATOM   12486 O OH    . TYR D 1 169 ? 72.459  51.944  63.174  1.000 77.800  0 169 TYR DDD OH    1 ? 4 
ATOM   12487 N N     . ILE D 1 170 ? 79.283  47.764  66.379  1.000 73.788  0 170 ILE DDD N     1 ? 4 
ATOM   12488 C CA    . ILE D 1 170 ? 80.206  46.717  66.900  1.000 72.762  0 170 ILE DDD CA    1 ? 4 
ATOM   12489 C C     . ILE D 1 170 ? 79.365  45.739  67.721  1.000 70.309  0 170 ILE DDD C     1 ? 4 
ATOM   12490 O O     . ILE D 1 170 ? 78.499  46.203  68.474  1.000 73.873  0 170 ILE DDD O     1 ? 4 
ATOM   12491 C CB    . ILE D 1 170 ? 81.367  47.328  67.706  1.000 74.459  0 170 ILE DDD CB    1 ? 4 
ATOM   12492 C CG1   . ILE D 1 170 ? 82.212  48.250  66.822  1.000 77.190  0 170 ILE DDD CG1   1 ? 4 
ATOM   12493 C CG2   . ILE D 1 170 ? 82.204  46.235  68.354  1.000 73.387  0 170 ILE DDD CG2   1 ? 4 
ATOM   12494 C CD1   . ILE D 1 170 ? 83.241  49.079  67.558  1.000 80.244  0 170 ILE DDD CD1   1 ? 4 
ATOM   12495 N N     . LEU D 1 171 ? 79.572  44.439  67.516  1.000 67.243  0 171 LEU DDD N     1 ? 4 
ATOM   12496 C CA    . LEU D 1 171 ? 78.901  43.359  68.280  1.000 64.976  0 171 LEU DDD CA    1 ? 4 
ATOM   12497 C C     . LEU D 1 171 ? 79.958  42.587  69.064  1.000 60.966  0 171 LEU DDD C     1 ? 4 
ATOM   12498 O O     . LEU D 1 171 ? 80.889  42.071  68.438  1.000 62.400  0 171 LEU DDD O     1 ? 4 
ATOM   12499 C CB    . LEU D 1 171 ? 78.160  42.417  67.329  1.000 65.230  0 171 LEU DDD CB    1 ? 4 
ATOM   12500 C CG    . LEU D 1 171 ? 77.607  41.153  67.985  1.000 62.099  0 171 LEU DDD CG    1 ? 4 
ATOM   12501 C CD1   . LEU D 1 171 ? 76.667  41.509  69.114  1.000 61.475  0 171 LEU DDD CD1   1 ? 4 
ATOM   12502 C CD2   . LEU D 1 171 ? 76.893  40.277  66.970  1.000 62.341  0 171 LEU DDD CD2   1 ? 4 
ATOM   12503 N N     . LEU D 1 172 ? 79.804  42.526  70.380  1.000 58.291  0 172 LEU DDD N     1 ? 4 
ATOM   12504 C CA    . LEU D 1 172 ? 80.630  41.678  71.270  1.000 56.888  0 172 LEU DDD CA    1 ? 4 
ATOM   12505 C C     . LEU D 1 172 ? 79.913  40.343  71.461  1.000 54.093  0 172 LEU DDD C     1 ? 4 
ATOM   12506 O O     . LEU D 1 172 ? 78.714  40.355  71.851  1.000 47.983  0 172 LEU DDD O     1 ? 4 
ATOM   12507 C CB    . LEU D 1 172 ? 80.817  42.411  72.597  1.000 58.806  0 172 LEU DDD CB    1 ? 4 
ATOM   12508 C CG    . LEU D 1 172 ? 81.331  43.840  72.478  1.000 61.081  0 172 LEU DDD CG    1 ? 4 
ATOM   12509 C CD1   . LEU D 1 172 ? 81.350  44.498  73.848  1.000 62.946  0 172 LEU DDD CD1   1 ? 4 
ATOM   12510 C CD2   . LEU D 1 172 ? 82.719  43.857  71.859  1.000 59.860  0 172 LEU DDD CD2   1 ? 4 
ATOM   12511 N N     . ALA D 1 173 ? 80.616  39.247  71.165  1.000 53.204  0 173 ALA DDD N     1 ? 4 
ATOM   12512 C CA    . ALA D 1 173 ? 80.132  37.863  71.393  1.000 50.741  0 173 ALA DDD CA    1 ? 4 
ATOM   12513 C C     . ALA D 1 173 ? 81.332  36.960  71.612  1.000 46.236  0 173 ALA DDD C     1 ? 4 
ATOM   12514 O O     . ALA D 1 173 ? 81.504  36.026  70.855  1.000 45.543  0 173 ALA DDD O     1 ? 4 
ATOM   12515 C CB    . ALA D 1 173 ? 79.290  37.390  70.233  1.000 52.047  0 173 ALA DDD CB    1 ? 4 
ATOM   12516 N N     . THR D 1 174 ? 82.106  37.265  72.646  1.000 46.236  0 174 THR DDD N     1 ? 4 
ATOM   12517 C CA    . THR D 1 174 ? 83.420  36.645  72.957  1.000 46.081  0 174 THR DDD CA    1 ? 4 
ATOM   12518 C C     . THR D 1 174 ? 83.246  35.400  73.827  1.000 45.494  0 174 THR DDD C     1 ? 4 
ATOM   12519 O O     . THR D 1 174 ? 84.257  34.689  74.032  1.000 48.709  0 174 THR DDD O     1 ? 4 
ATOM   12520 C CB    . THR D 1 174 ? 84.336  37.688  73.605  1.000 44.478  0 174 THR DDD CB    1 ? 4 
ATOM   12521 O OG1   . THR D 1 174 ? 83.627  38.286  74.693  1.000 42.592  0 174 THR DDD OG1   1 ? 4 
ATOM   12522 C CG2   . THR D 1 174 ? 84.772  38.724  72.596  1.000 45.213  0 174 THR DDD CG2   1 ? 4 
ATOM   12523 N N     . GLY D 1 175 ? 82.027  35.126  74.293  1.000 45.889  0 175 GLY DDD N     1 ? 4 
ATOM   12524 C CA    . GLY D 1 175 ? 81.696  33.942  75.112  1.000 44.143  0 175 GLY DDD CA    1 ? 4 
ATOM   12525 C C     . GLY D 1 175 ? 82.392  33.965  76.463  1.000 42.858  0 175 GLY DDD C     1 ? 4 
ATOM   12526 O O     . GLY D 1 175 ? 83.005  35.000  76.817  1.000 43.062  0 175 GLY DDD O     1 ? 4 
ATOM   12527 N N     . GLY D 1 176 ? 82.303  32.852  77.197  1.000 39.823  0 176 GLY DDD N     1 ? 4 
ATOM   12528 C CA    . GLY D 1 176 ? 83.027  32.637  78.458  1.000 40.233  0 176 GLY DDD CA    1 ? 4 
ATOM   12529 C C     . GLY D 1 176 ? 84.227  31.706  78.282  1.000 39.741  0 176 GLY DDD C     1 ? 4 
ATOM   12530 O O     . GLY D 1 176 ? 84.523  31.255  77.144  1.000 39.227  0 176 GLY DDD O     1 ? 4 
ATOM   12531 N N     . ARG D 1 177 ? 84.908  31.458  79.398  1.000 40.578  0 177 ARG DDD N     1 ? 4 
ATOM   12532 C CA    . ARG D 1 177 ? 85.853  30.333  79.600  1.000 41.682  0 177 ARG DDD CA    1 ? 4 
ATOM   12533 C C     . ARG D 1 177 ? 85.569  29.718  80.969  1.000 40.147  0 177 ARG DDD C     1 ? 4 
ATOM   12534 O O     . ARG D 1 177 ? 84.997  30.346  81.859  1.000 38.109  0 177 ARG DDD O     1 ? 4 
ATOM   12535 C CB    . ARG D 1 177 ? 87.289  30.827  79.371  1.000 42.752  0 177 ARG DDD CB    1 ? 4 
ATOM   12536 C CG    . ARG D 1 177 ? 87.520  31.349  77.952  1.000 44.626  0 177 ARG DDD CG    1 ? 4 
ATOM   12537 C CD    . ARG D 1 177 ? 87.296  30.321  76.842  1.000 43.413  0 177 ARG DDD CD    1 ? 4 
ATOM   12538 N NE    . ARG D 1 177 ? 88.368  29.351  76.917  1.000 44.913  0 177 ARG DDD NE    1 ? 4 
ATOM   12539 C CZ    . ARG D 1 177 ? 89.559  29.517  76.355  1.000 45.482  0 177 ARG DDD CZ    1 ? 4 
ATOM   12540 N NH1   . ARG D 1 177 ? 89.821  30.603  75.646  1.000 46.092  0 177 ARG DDD NH1   1 ? 4 
ATOM   12541 N NH2   . ARG D 1 177 ? 90.485  28.586  76.493  1.000 47.031  0 177 ARG DDD NH2   1 ? 4 
ATOM   12542 N N     . PRO D 1 178 ? 85.977  28.451  81.174  1.000 42.470  0 178 PRO DDD N     1 ? 4 
ATOM   12543 C CA    . PRO D 1 178 ? 85.826  27.801  82.474  1.000 43.841  0 178 PRO DDD CA    1 ? 4 
ATOM   12544 C C     . PRO D 1 178 ? 86.448  28.655  83.587  1.000 46.980  0 178 PRO DDD C     1 ? 4 
ATOM   12545 O O     . PRO D 1 178 ? 87.454  29.288  83.357  1.000 44.383  0 178 PRO DDD O     1 ? 4 
ATOM   12546 C CB    . PRO D 1 178 ? 86.608  26.493  82.293  1.000 41.560  0 178 PRO DDD CB    1 ? 4 
ATOM   12547 C CG    . PRO D 1 178 ? 86.541  26.222  80.800  1.000 40.671  0 178 PRO DDD CG    1 ? 4 
ATOM   12548 C CD    . PRO D 1 178 ? 86.616  27.588  80.168  1.000 40.903  0 178 PRO DDD CD    1 ? 4 
ATOM   12549 N N     . SER D 1 179 ? 85.821  28.672  84.757  1.000 52.160  0 179 SER DDD N     1 ? 4 
ATOM   12550 C CA    . SER D 1 179 ? 86.369  29.356  85.956  1.000 56.477  0 179 SER DDD CA    1 ? 4 
ATOM   12551 C C     . SER D 1 179 ? 86.938  28.328  86.935  1.000 56.055  0 179 SER DDD C     1 ? 4 
ATOM   12552 O O     . SER D 1 179 ? 86.246  27.349  87.255  1.000 53.342  0 179 SER DDD O     1 ? 4 
ATOM   12553 C CB    . SER D 1 179 ? 85.364  30.263  86.607  1.000 58.241  0 179 SER DDD CB    1 ? 4 
ATOM   12554 O OG    . SER D 1 179 ? 86.036  31.112  87.520  1.000 68.933  0 179 SER DDD OG    1 ? 4 
ATOM   12555 N N     . ILE D 1 180 ? 88.185  28.553  87.345  1.000 57.688  0 180 ILE DDD N     1 ? 4 
ATOM   12556 C CA    . ILE D 1 180 ? 88.901  27.765  88.383  1.000 61.111  0 180 ILE DDD CA    1 ? 4 
ATOM   12557 C C     . ILE D 1 180 ? 89.182  28.680  89.572  1.000 64.348  0 180 ILE DDD C     1 ? 4 
ATOM   12558 O O     . ILE D 1 180 ? 89.759  29.751  89.388  1.000 69.192  0 180 ILE DDD O     1 ? 4 
ATOM   12559 C CB    . ILE D 1 180 ? 90.198  27.170  87.824  1.000 61.616  0 180 ILE DDD CB    1 ? 4 
ATOM   12560 C CG1   . ILE D 1 180 ? 89.946  26.334  86.567  1.000 61.340  0 180 ILE DDD CG1   1 ? 4 
ATOM   12561 C CG2   . ILE D 1 180 ? 90.907  26.366  88.899  1.000 61.696  0 180 ILE DDD CG2   1 ? 4 
ATOM   12562 C CD1   . ILE D 1 180 ? 91.206  25.807  85.938  1.000 61.965  0 180 ILE DDD CD1   1 ? 4 
ATOM   12563 N N     . PRO D 1 181 ? 88.797  28.284  90.809  1.000 60.133  0 181 PRO DDD N     1 ? 4 
ATOM   12564 C CA    . PRO D 1 181 ? 89.079  29.079  92.005  1.000 61.598  0 181 PRO DDD CA    1 ? 4 
ATOM   12565 C C     . PRO D 1 181 ? 90.577  29.350  92.250  1.000 61.636  0 181 PRO DDD C     1 ? 4 
ATOM   12566 O O     . PRO D 1 181 ? 91.336  28.403  92.421  1.000 55.785  0 181 PRO DDD O     1 ? 4 
ATOM   12567 C CB    . PRO D 1 181 ? 88.497  28.244  93.159  1.000 60.971  0 181 PRO DDD CB    1 ? 4 
ATOM   12568 C CG    . PRO D 1 181 ? 88.339  26.852  92.597  1.000 62.099  0 181 PRO DDD CG    1 ? 4 
ATOM   12569 C CD    . PRO D 1 181 ? 88.086  27.035  91.120  1.000 59.540  0 181 PRO DDD CD    1 ? 4 
ATOM   12570 N N     . GLU D 1 182 ? 90.950  30.642  92.254  1.000 66.915  0 182 GLU DDD N     1 ? 4 
ATOM   12571 C CA    . GLU D 1 182 ? 92.316  31.185  92.511  1.000 77.513  0 182 GLU DDD CA    1 ? 4 
ATOM   12572 C C     . GLU D 1 182 ? 92.678  30.987  93.988  1.000 76.794  0 182 GLU DDD C     1 ? 4 
ATOM   12573 O O     . GLU D 1 182 ? 93.880  30.856  94.262  1.000 78.145  0 182 GLU DDD O     1 ? 4 
ATOM   12574 C CB    . GLU D 1 182 ? 92.377  32.654  92.064  1.000 83.695  0 182 GLU DDD CB    1 ? 4 
ATOM   12575 C CG    . GLU D 1 182 ? 92.418  32.781  90.540  1.000 88.335  0 182 GLU DDD CG    1 ? 4 
ATOM   12576 C CD    . GLU D 1 182 ? 91.536  33.821  89.860  1.000 90.768  0 182 GLU DDD CD    1 ? 4 
ATOM   12577 O OE1   . GLU D 1 182 ? 90.648  34.406  90.523  1.000 87.324  0 182 GLU DDD OE1   1 ? 4 
ATOM   12578 O OE2   . GLU D 1 182 ? 91.743  34.037  88.649  1.000 92.793  0 182 GLU DDD OE2   1 ? 4 
ATOM   12579 N N     . THR D 1 183 ? 91.668  30.883  94.865  1.000 74.745  0 183 THR DDD N     1 ? 4 
ATOM   12580 C CA    . THR D 1 183 ? 91.804  30.705  96.338  1.000 74.104  0 183 THR DDD CA    1 ? 4 
ATOM   12581 C C     . THR D 1 183 ? 92.331  29.294  96.678  1.000 74.679  0 183 THR DDD C     1 ? 4 
ATOM   12582 O O     . THR D 1 183 ? 93.117  29.178  97.640  1.000 74.155  0 183 THR DDD O     1 ? 4 
ATOM   12583 C CB    . THR D 1 183 ? 90.482  31.032  97.044  1.000 72.620  0 183 THR DDD CB    1 ? 4 
ATOM   12584 O OG1   . THR D 1 183 ? 89.497  30.068  96.679  1.000 70.406  0 183 THR DDD OG1   1 ? 4 
ATOM   12585 C CG2   . THR D 1 183 ? 89.953  32.408  96.701  1.000 72.853  0 183 THR DDD CG2   1 ? 4 
ATOM   12586 N N     . VAL D 1 184 ? 91.929  28.258  95.931  1.000 71.801  0 184 VAL DDD N     1 ? 4 
ATOM   12587 C CA    . VAL D 1 184 ? 92.289  26.835  96.229  1.000 68.306  0 184 VAL DDD CA    1 ? 4 
ATOM   12588 C C     . VAL D 1 184 ? 93.669  26.537  95.658  1.000 69.595  0 184 VAL DDD C     1 ? 4 
ATOM   12589 O O     . VAL D 1 184 ? 93.854  26.527  94.448  1.000 74.135  0 184 VAL DDD O     1 ? 4 
ATOM   12590 C CB    . VAL D 1 184 ? 91.249  25.834  95.703  1.000 62.890  0 184 VAL DDD CB    1 ? 4 
ATOM   12591 C CG1   . VAL D 1 184 ? 91.753  24.414  95.833  1.000 59.520  0 184 VAL DDD CG1   1 ? 4 
ATOM   12592 C CG2   . VAL D 1 184 ? 89.907  25.985  96.411  1.000 61.476  0 184 VAL DDD CG2   1 ? 4 
ATOM   12593 N N     . PRO D 1 185 ? 94.687  26.284  96.512  1.000 68.709  0 185 PRO DDD N     1 ? 4 
ATOM   12594 C CA    . PRO D 1 185 ? 96.041  25.994  96.031  1.000 64.987  0 185 PRO DDD CA    1 ? 4 
ATOM   12595 C C     . PRO D 1 185 ? 96.162  24.697  95.221  1.000 62.533  0 185 PRO DDD C     1 ? 4 
ATOM   12596 O O     . PRO D 1 185 ? 95.618  23.694  95.649  1.000 58.872  0 185 PRO DDD O     1 ? 4 
ATOM   12597 C CB    . PRO D 1 185 ? 96.875  25.853  97.314  1.000 66.175  0 185 PRO DDD CB    1 ? 4 
ATOM   12598 C CG    . PRO D 1 185 ? 96.024  26.503  98.404  1.000 67.934  0 185 PRO DDD CG    1 ? 4 
ATOM   12599 C CD    . PRO D 1 185 ? 94.590  26.279  97.981  1.000 67.802  0 185 PRO DDD CD    1 ? 4 
ATOM   12600 N N     . GLY D 1 186 ? 96.905  24.755  94.107  1.000 62.750  0 186 GLY DDD N     1 ? 4 
ATOM   12601 C CA    . GLY D 1 186 ? 97.115  23.641  93.155  1.000 63.351  0 186 GLY DDD CA    1 ? 4 
ATOM   12602 C C     . GLY D 1 186 ? 96.058  23.549  92.049  1.000 62.009  0 186 GLY DDD C     1 ? 4 
ATOM   12603 O O     . GLY D 1 186 ? 96.344  22.882  91.040  1.000 61.618  0 186 GLY DDD O     1 ? 4 
ATOM   12604 N N     . ALA D 1 187 ? 94.891  24.191  92.212  1.000 60.605  0 187 ALA DDD N     1 ? 4 
ATOM   12605 C CA    . ALA D 1 187 ? 93.709  24.092  91.314  1.000 59.831  0 187 ALA DDD CA    1 ? 4 
ATOM   12606 C C     . ALA D 1 187 ? 94.078  24.433  89.865  1.000 58.792  0 187 ALA DDD C     1 ? 4 
ATOM   12607 O O     . ALA D 1 187 ? 93.848  23.583  88.983  1.000 55.960  0 187 ALA DDD O     1 ? 4 
ATOM   12608 C CB    . ALA D 1 187 ? 92.601  24.995  91.821  1.000 57.743  0 187 ALA DDD CB    1 ? 4 
ATOM   12609 N N     . ILE D 1 188 ? 94.623  25.632  89.638  1.000 60.704  0 188 ILE DDD N     1 ? 4 
ATOM   12610 C CA    . ILE D 1 188 ? 94.935  26.185  88.288  1.000 61.600  0 188 ILE DDD CA    1 ? 4 
ATOM   12611 C C     . ILE D 1 188 ? 95.976  25.277  87.622  1.000 63.110  0 188 ILE DDD C     1 ? 4 
ATOM   12612 O O     . ILE D 1 188 ? 95.888  25.026  86.395  1.000 62.865  0 188 ILE DDD O     1 ? 4 
ATOM   12613 C CB    . ILE D 1 188 ? 95.391  27.657  88.404  1.000 64.579  0 188 ILE DDD CB    1 ? 4 
ATOM   12614 C CG1   . ILE D 1 188 ? 94.181  28.597  88.520  1.000 65.576  0 188 ILE DDD CG1   1 ? 4 
ATOM   12615 C CG2   . ILE D 1 188 ? 96.315  28.045  87.251  1.000 65.147  0 188 ILE DDD CG2   1 ? 4 
ATOM   12616 C CD1   . ILE D 1 188 ? 94.490  29.990  89.002  1.000 65.499  0 188 ILE DDD CD1   1 ? 4 
ATOM   12617 N N     . GLN D 1 189 ? 96.930  24.783  88.409  1.000 63.892  0 189 GLN DDD N     1 ? 4 
ATOM   12618 C CA    . GLN D 1 189 ? 98.134  24.104  87.877  1.000 62.631  0 189 GLN DDD CA    1 ? 4 
ATOM   12619 C C     . GLN D 1 189 ? 97.783  22.673  87.467  1.000 61.538  0 189 GLN DDD C     1 ? 4 
ATOM   12620 O O     . GLN D 1 189 ? 98.296  22.225  86.399  1.000 62.114  0 189 GLN DDD O     1 ? 4 
ATOM   12621 C CB    . GLN D 1 189 ? 99.259  24.118  88.911  1.000 62.515  0 189 GLN DDD CB    1 ? 4 
ATOM   12622 C CG    . GLN D 1 189 ? 100.635 23.933  88.286  1.000 63.310  0 189 GLN DDD CG    1 ? 4 
ATOM   12623 C CD    . GLN D 1 189 ? 101.711 23.583  89.290  1.000 64.496  0 189 GLN DDD CD    1 ? 4 
ATOM   12624 O OE1   . GLN D 1 189 ? 101.754 24.116  90.405  1.000 60.642  0 189 GLN DDD OE1   1 ? 4 
ATOM   12625 N NE2   . GLN D 1 189 ? 102.609 22.698  88.880  1.000 64.526  0 189 GLN DDD NE2   1 ? 4 
ATOM   12626 N N     . TYR D 1 190 ? 96.962  21.979  88.268  1.000 57.879  0 190 TYR DDD N     1 ? 4 
ATOM   12627 C CA    . TYR D 1 190 ? 96.817  20.499  88.195  1.000 57.143  0 190 TYR DDD CA    1 ? 4 
ATOM   12628 C C     . TYR D 1 190 ? 95.455  20.058  87.627  1.000 51.233  0 190 TYR DDD C     1 ? 4 
ATOM   12629 O O     . TYR D 1 190 ? 95.416  18.941  87.098  1.000 47.769  0 190 TYR DDD O     1 ? 4 
ATOM   12630 C CB    . TYR D 1 190 ? 97.105  19.893  89.569  1.000 59.038  0 190 TYR DDD CB    1 ? 4 
ATOM   12631 C CG    . TYR D 1 190 ? 98.541  20.015  90.017  1.000 61.983  0 190 TYR DDD CG    1 ? 4 
ATOM   12632 C CD1   . TYR D 1 190 ? 99.575  19.552  89.220  1.000 61.520  0 190 TYR DDD CD1   1 ? 4 
ATOM   12633 C CD2   . TYR D 1 190 ? 98.868  20.584  91.241  1.000 66.040  0 190 TYR DDD CD2   1 ? 4 
ATOM   12634 C CE1   . TYR D 1 190 ? 100.894 19.664  89.618  1.000 64.305  0 190 TYR DDD CE1   1 ? 4 
ATOM   12635 C CE2   . TYR D 1 190 ? 100.187 20.698  91.657  1.000 67.554  0 190 TYR DDD CE2   1 ? 4 
ATOM   12636 C CZ    . TYR D 1 190 ? 101.205 20.236  90.840  1.000 66.514  0 190 TYR DDD CZ    1 ? 4 
ATOM   12637 O OH    . TYR D 1 190 ? 102.512 20.342  91.224  1.000 65.726  0 190 TYR DDD OH    1 ? 4 
ATOM   12638 N N     . SER D 1 191 ? 94.423  20.900  87.705  1.000 46.982  0 191 SER DDD N     1 ? 4 
ATOM   12639 C CA    . SER D 1 191 ? 93.032  20.583  87.280  1.000 46.705  0 191 SER DDD CA    1 ? 4 
ATOM   12640 C C     . SER D 1 191 ? 92.813  20.903  85.802  1.000 43.300  0 191 SER DDD C     1 ? 4 
ATOM   12641 O O     . SER D 1 191 ? 93.407  21.858  85.292  1.000 44.763  0 191 SER DDD O     1 ? 4 
ATOM   12642 C CB    . SER D 1 191 ? 91.992  21.329  88.064  1.000 45.977  0 191 SER DDD CB    1 ? 4 
ATOM   12643 O OG    . SER D 1 191 ? 92.313  21.402  89.428  1.000 51.384  0 191 SER DDD OG    1 ? 4 
ATOM   12644 N N     . ILE D 1 192 ? 91.933  20.144  85.163  1.000 41.886  0 192 ILE DDD N     1 ? 4 
ATOM   12645 C CA    . ILE D 1 192 ? 91.464  20.399  83.766  1.000 40.612  0 192 ILE DDD CA    1 ? 4 
ATOM   12646 C C     . ILE D 1 192 ? 90.055  21.000  83.856  1.000 39.815  0 192 ILE DDD C     1 ? 4 
ATOM   12647 O O     . ILE D 1 192 ? 89.512  21.106  84.968  1.000 39.461  0 192 ILE DDD O     1 ? 4 
ATOM   12648 C CB    . ILE D 1 192 ? 91.510  19.113  82.913  1.000 38.673  0 192 ILE DDD CB    1 ? 4 
ATOM   12649 C CG1   . ILE D 1 192 ? 90.561  18.033  83.438  1.000 40.319  0 192 ILE DDD CG1   1 ? 4 
ATOM   12650 C CG2   . ILE D 1 192 ? 92.921  18.566  82.820  1.000 39.879  0 192 ILE DDD CG2   1 ? 4 
ATOM   12651 C CD1   . ILE D 1 192 ? 90.306  16.907  82.444  1.000 38.455  0 192 ILE DDD CD1   1 ? 4 
ATOM   12652 N N     . THR D 1 193 ? 89.515  21.422  82.713  1.000 39.781  0 193 THR DDD N     1 ? 4 
ATOM   12653 C CA    . THR D 1 193 ? 88.160  21.981  82.545  1.000 39.337  0 193 THR DDD CA    1 ? 4 
ATOM   12654 C C     . THR D 1 193 ? 87.523  21.341  81.312  1.000 39.156  0 193 THR DDD C     1 ? 4 
ATOM   12655 O O     . THR D 1 193 ? 88.173  20.481  80.705  1.000 41.814  0 193 THR DDD O     1 ? 4 
ATOM   12656 C CB    . THR D 1 193 ? 88.250  23.495  82.422  1.000 40.081  0 193 THR DDD CB    1 ? 4 
ATOM   12657 O OG1   . THR D 1 193 ? 88.905  23.835  81.203  1.000 38.049  0 193 THR DDD OG1   1 ? 4 
ATOM   12658 C CG2   . THR D 1 193 ? 88.990  24.115  83.584  1.000 42.096  0 193 THR DDD CG2   1 ? 4 
ATOM   12659 N N     . SER D 1 194 ? 86.331  21.797  80.926  1.000 37.385  0 194 SER DDD N     1 ? 4 
ATOM   12660 C CA    . SER D 1 194 ? 85.605  21.336  79.712  1.000 36.127  0 194 SER DDD CA    1 ? 4 
ATOM   12661 C C     . SER D 1 194 ? 86.416  21.693  78.454  1.000 35.638  0 194 SER DDD C     1 ? 4 
ATOM   12662 O O     . SER D 1 194 ? 86.241  21.041  77.424  1.000 35.312  0 194 SER DDD O     1 ? 4 
ATOM   12663 C CB    . SER D 1 194 ? 84.199  21.864  79.669  1.000 33.318  0 194 SER DDD CB    1 ? 4 
ATOM   12664 O OG    . SER D 1 194 ? 84.185  23.261  79.880  1.000 35.924  0 194 SER DDD OG    1 ? 4 
ATOM   12665 N N     . ASP D 1 195 ? 87.272  22.705  78.534  1.000 37.061  0 195 ASP DDD N     1 ? 4 
ATOM   12666 C CA    . ASP D 1 195 ? 88.200  23.066  77.435  1.000 38.948  0 195 ASP DDD CA    1 ? 4 
ATOM   12667 C C     . ASP D 1 195 ? 89.177  21.912  77.100  1.000 38.515  0 195 ASP DDD C     1 ? 4 
ATOM   12668 O O     . ASP D 1 195 ? 89.694  21.900  75.976  1.000 38.395  0 195 ASP DDD O     1 ? 4 
ATOM   12669 C CB    . ASP D 1 195 ? 88.967  24.340  77.799  1.000 40.939  0 195 ASP DDD CB    1 ? 4 
ATOM   12670 C CG    . ASP D 1 195 ? 88.170  25.616  77.677  1.000 41.701  0 195 ASP DDD CG    1 ? 4 
ATOM   12671 O OD1   . ASP D 1 195 ? 86.939  25.538  77.422  1.000 40.322  0 195 ASP DDD OD1   1 ? 4 
ATOM   12672 O OD2   . ASP D 1 195 ? 88.802  26.683  77.841  1.000 46.385  0 195 ASP DDD OD2   1 ? 4 
ATOM   12673 N N     . ASP D 1 196 ? 89.448  20.981  78.018  1.000 38.309  0 196 ASP DDD N     1 ? 4 
ATOM   12674 C CA    . ASP D 1 196 ? 90.501  19.958  77.813  1.000 38.984  0 196 ASP DDD CA    1 ? 4 
ATOM   12675 C C     . ASP D 1 196 ? 89.936  18.539  77.700  1.000 39.505  0 196 ASP DDD C     1 ? 4 
ATOM   12676 O O     . ASP D 1 196 ? 90.640  17.662  77.080  1.000 38.331  0 196 ASP DDD O     1 ? 4 
ATOM   12677 C CB    . ASP D 1 196 ? 91.502  20.009  78.973  1.000 40.000  0 196 ASP DDD CB    1 ? 4 
ATOM   12678 C CG    . ASP D 1 196 ? 91.941  21.420  79.321  1.000 38.255  0 196 ASP DDD CG    1 ? 4 
ATOM   12679 O OD1   . ASP D 1 196 ? 92.570  22.059  78.455  1.000 37.683  0 196 ASP DDD OD1   1 ? 4 
ATOM   12680 O OD2   . ASP D 1 196 ? 91.651  21.849  80.443  1.000 38.654  0 196 ASP DDD OD2   1 ? 4 
ATOM   12681 N N     . ILE D 1 197 ? 88.777  18.270  78.311  1.000 37.401  0 197 ILE DDD N     1 ? 4 
ATOM   12682 C CA    . ILE D 1 197 ? 88.277  16.885  78.581  1.000 36.086  0 197 ILE DDD CA    1 ? 4 
ATOM   12683 C C     . ILE D 1 197 ? 88.021  16.132  77.265  1.000 35.365  0 197 ILE DDD C     1 ? 4 
ATOM   12684 O O     . ILE D 1 197 ? 88.205  14.910  77.244  1.000 36.973  0 197 ILE DDD O     1 ? 4 
ATOM   12685 C CB    . ILE D 1 197 ? 87.015  16.902  79.474  1.000 34.900  0 197 ILE DDD CB    1 ? 4 
ATOM   12686 C CG1   . ILE D 1 197 ? 86.562  15.482  79.826  1.000 35.125  0 197 ILE DDD CG1   1 ? 4 
ATOM   12687 C CG2   . ILE D 1 197 ? 85.901  17.696  78.844  1.000 33.234  0 197 ILE DDD CG2   1 ? 4 
ATOM   12688 C CD1   . ILE D 1 197 ? 87.652  14.617  80.427  1.000 34.599  0 197 ILE DDD CD1   1 ? 4 
ATOM   12689 N N     . PHE D 1 198 ? 87.635  16.799  76.186  1.000 34.392  0 198 PHE DDD N     1 ? 4 
ATOM   12690 C CA    . PHE D 1 198 ? 87.230  16.088  74.947  1.000 35.379  0 198 PHE DDD CA    1 ? 4 
ATOM   12691 C C     . PHE D 1 198 ? 88.464  15.707  74.124  1.000 41.003  0 198 PHE DDD C     1 ? 4 
ATOM   12692 O O     . PHE D 1 198 ? 88.283  14.872  73.182  1.000 44.114  0 198 PHE DDD O     1 ? 4 
ATOM   12693 C CB    . PHE D 1 198 ? 86.231  16.925  74.148  1.000 32.941  0 198 PHE DDD CB    1 ? 4 
ATOM   12694 C CG    . PHE D 1 198 ? 85.030  17.325  74.960  1.000 31.071  0 198 PHE DDD CG    1 ? 4 
ATOM   12695 C CD1   . PHE D 1 198 ? 84.195  16.362  75.470  1.000 29.686  0 198 PHE DDD CD1   1 ? 4 
ATOM   12696 C CD2   . PHE D 1 198 ? 84.783  18.654  75.271  1.000 31.800  0 198 PHE DDD CD2   1 ? 4 
ATOM   12697 C CE1   . PHE D 1 198 ? 83.114  16.714  76.256  1.000 29.778  0 198 PHE DDD CE1   1 ? 4 
ATOM   12698 C CE2   . PHE D 1 198 ? 83.674  19.011  76.022  1.000 32.341  0 198 PHE DDD CE2   1 ? 4 
ATOM   12699 C CZ    . PHE D 1 198 ? 82.843  18.030  76.517  1.000 30.836  0 198 PHE DDD CZ    1 ? 4 
ATOM   12700 N N     . PHE D 1 199 ? 89.659  16.243  74.444  1.000 44.837  0 199 PHE DDD N     1 ? 4 
ATOM   12701 C CA    . PHE D 1 199 ? 90.899  16.104  73.630  1.000 44.807  0 199 PHE DDD CA    1 ? 4 
ATOM   12702 C C     . PHE D 1 199 ? 92.046  15.468  74.412  1.000 43.371  0 199 PHE DDD C     1 ? 4 
ATOM   12703 O O     . PHE D 1 199 ? 93.139  15.402  73.863  1.000 43.714  0 199 PHE DDD O     1 ? 4 
ATOM   12704 C CB    . PHE D 1 199 ? 91.318  17.469  73.081  1.000 48.180  0 199 PHE DDD CB    1 ? 4 
ATOM   12705 C CG    . PHE D 1 199 ? 90.204  18.138  72.324  1.000 52.811  0 199 PHE DDD CG    1 ? 4 
ATOM   12706 C CD1   . PHE D 1 199 ? 89.620  17.505  71.238  1.000 57.159  0 199 PHE DDD CD1   1 ? 4 
ATOM   12707 C CD2   . PHE D 1 199 ? 89.703  19.365  72.718  1.000 54.561  0 199 PHE DDD CD2   1 ? 4 
ATOM   12708 C CE1   . PHE D 1 199 ? 88.577  18.106  70.545  1.000 57.992  0 199 PHE DDD CE1   1 ? 4 
ATOM   12709 C CE2   . PHE D 1 199 ? 88.664  19.959  72.024  1.000 54.497  0 199 PHE DDD CE2   1 ? 4 
ATOM   12710 C CZ    . PHE D 1 199 ? 88.107  19.334  70.941  1.000 56.810  0 199 PHE DDD CZ    1 ? 4 
ATOM   12711 N N     . LEU D 1 200 ? 91.838  15.016  75.644  1.000 42.562  0 200 LEU DDD N     1 ? 4 
ATOM   12712 C CA    . LEU D 1 200 ? 92.922  14.336  76.395  1.000 45.616  0 200 LEU DDD CA    1 ? 4 
ATOM   12713 C C     . LEU D 1 200 ? 93.587  13.288  75.493  1.000 45.125  0 200 LEU DDD C     1 ? 4 
ATOM   12714 O O     . LEU D 1 200 ? 92.843  12.435  74.977  1.000 46.364  0 200 LEU DDD O     1 ? 4 
ATOM   12715 C CB    . LEU D 1 200 ? 92.325  13.639  77.618  1.000 46.117  0 200 LEU DDD CB    1 ? 4 
ATOM   12716 C CG    . LEU D 1 200 ? 91.924  14.542  78.765  1.000 47.292  0 200 LEU DDD CG    1 ? 4 
ATOM   12717 C CD1   . LEU D 1 200 ? 91.515  13.693  79.952  1.000 48.065  0 200 LEU DDD CD1   1 ? 4 
ATOM   12718 C CD2   . LEU D 1 200 ? 93.065  15.496  79.128  1.000 46.814  0 200 LEU DDD CD2   1 ? 4 
ATOM   12719 N N     . SER D 1 201 ? 94.903  13.320  75.339  1.000 45.583  0 201 SER DDD N     1 ? 4 
ATOM   12720 C CA    . SER D 1 201 ? 95.670  12.274  74.617  1.000 51.425  0 201 SER DDD CA    1 ? 4 
ATOM   12721 C C     . SER D 1 201 ? 95.537  10.929  75.341  1.000 53.454  0 201 SER DDD C     1 ? 4 
ATOM   12722 O O     . SER D 1 201 ? 95.583  9.893   74.669  1.000 57.371  0 201 SER DDD O     1 ? 4 
ATOM   12723 C CB    . SER D 1 201 ? 97.122  12.654  74.427  1.000 52.889  0 201 SER DDD CB    1 ? 4 
ATOM   12724 O OG    . SER D 1 201 ? 97.727  12.972  75.662  1.000 53.909  0 201 SER DDD OG    1 ? 4 
ATOM   12725 N N     . LYS D 1 202 ? 95.376  10.951  76.662  1.000 55.494  0 202 LYS DDD N     1 ? 4 
ATOM   12726 C CA    . LYS D 1 202 ? 95.247  9.731   77.506  1.000 59.106  0 202 LYS DDD CA    1 ? 4 
ATOM   12727 C C     . LYS D 1 202 ? 93.881  9.723   78.215  1.000 51.836  0 202 LYS DDD C     1 ? 4 
ATOM   12728 O O     . LYS D 1 202 ? 93.332  10.802  78.513  1.000 47.191  0 202 LYS DDD O     1 ? 4 
ATOM   12729 C CB    . LYS D 1 202 ? 96.394  9.706   78.521  1.000 71.991  0 202 LYS DDD CB    1 ? 4 
ATOM   12730 C CG    . LYS D 1 202 ? 96.494  8.459   79.392  1.000 83.709  0 202 LYS DDD CG    1 ? 4 
ATOM   12731 C CD    . LYS D 1 202 ? 97.391  8.646   80.604  1.000 93.533  0 202 LYS DDD CD    1 ? 4 
ATOM   12732 C CE    . LYS D 1 202 ? 97.484  7.400   81.466  1.000 98.212  0 202 LYS DDD CE    1 ? 4 
ATOM   12733 N NZ    . LYS D 1 202 ? 96.213  7.093   82.158  1.000 100.660 0 202 LYS DDD NZ    1 ? 4 
ATOM   12734 N N     . SER D 1 203 ? 93.346  8.540   78.496  1.000 47.352  0 203 SER DDD N     1 ? 4 
ATOM   12735 C CA    . SER D 1 203 ? 92.078  8.395   79.247  1.000 46.901  0 203 SER DDD CA    1 ? 4 
ATOM   12736 C C     . SER D 1 203 ? 92.281  8.978   80.652  1.000 46.960  0 203 SER DDD C     1 ? 4 
ATOM   12737 O O     . SER D 1 203 ? 93.368  8.905   81.247  1.000 43.021  0 203 SER DDD O     1 ? 4 
ATOM   12738 C CB    . SER D 1 203 ? 91.576  6.971   79.242  1.000 46.485  0 203 SER DDD CB    1 ? 4 
ATOM   12739 O OG    . SER D 1 203 ? 92.329  6.126   80.073  1.000 50.848  0 203 SER DDD OG    1 ? 4 
ATOM   12740 N N     . PRO D 1 204 ? 91.233  9.610   81.215  1.000 44.464  0 204 PRO DDD N     1 ? 4 
ATOM   12741 C CA    . PRO D 1 204 ? 91.370  10.335  82.476  1.000 44.578  0 204 PRO DDD CA    1 ? 4 
ATOM   12742 C C     . PRO D 1 204 ? 91.491  9.472   83.746  1.000 45.655  0 204 PRO DDD C     1 ? 4 
ATOM   12743 O O     . PRO D 1 204 ? 91.814  10.033  84.811  1.000 44.145  0 204 PRO DDD O     1 ? 4 
ATOM   12744 C CB    . PRO D 1 204 ? 90.079  11.164  82.500  1.000 46.160  0 204 PRO DDD CB    1 ? 4 
ATOM   12745 C CG    . PRO D 1 204 ? 89.076  10.326  81.739  1.000 45.994  0 204 PRO DDD CG    1 ? 4 
ATOM   12746 C CD    . PRO D 1 204 ? 89.878  9.657   80.646  1.000 45.590  0 204 PRO DDD CD    1 ? 4 
ATOM   12747 N N     . GLY D 1 205 ? 91.243  8.157   83.631  1.000 45.338  0 205 GLY DDD N     1 ? 4 
ATOM   12748 C CA    . GLY D 1 205 ? 91.153  7.220   84.772  1.000 43.531  0 205 GLY DDD CA    1 ? 4 
ATOM   12749 C C     . GLY D 1 205 ? 90.194  7.735   85.845  1.000 43.084  0 205 GLY DDD C     1 ? 4 
ATOM   12750 O O     . GLY D 1 205 ? 89.190  8.417   85.506  1.000 37.988  0 205 GLY DDD O     1 ? 4 
ATOM   12751 N N     . LYS D 1 206 ? 90.526  7.451   87.100  1.000 45.300  0 206 LYS DDD N     1 ? 4 
ATOM   12752 C CA    . LYS D 1 206 ? 89.760  7.849   88.305  1.000 45.044  0 206 LYS DDD CA    1 ? 4 
ATOM   12753 C C     . LYS D 1 206 ? 89.631  9.377   88.311  1.000 43.440  0 206 LYS DDD C     1 ? 4 
ATOM   12754 O O     . LYS D 1 206 ? 90.666  10.058  88.340  1.000 45.282  0 206 LYS DDD O     1 ? 4 
ATOM   12755 C CB    . LYS D 1 206 ? 90.439  7.298   89.568  1.000 46.870  0 206 LYS DDD CB    1 ? 4 
ATOM   12756 C CG    . LYS D 1 206 ? 89.910  7.875   90.878  1.000 48.497  0 206 LYS DDD CG    1 ? 4 
ATOM   12757 C CD    . LYS D 1 206 ? 90.292  7.098   92.125  1.000 50.342  0 206 LYS DDD CD    1 ? 4 
ATOM   12758 C CE    . LYS D 1 206 ? 89.487  7.525   93.338  1.000 51.560  0 206 LYS DDD CE    1 ? 4 
ATOM   12759 N NZ    . LYS D 1 206 ? 90.150  7.134   94.600  1.000 54.669  0 206 LYS DDD NZ    1 ? 4 
ATOM   12760 N N     . THR D 1 207 ? 88.404  9.899   88.298  1.000 40.626  0 207 THR DDD N     1 ? 4 
ATOM   12761 C CA    . THR D 1 207 ? 88.144  11.332  88.052  1.000 38.782  0 207 THR DDD CA    1 ? 4 
ATOM   12762 C C     . THR D 1 207 ? 87.289  11.937  89.167  1.000 38.018  0 207 THR DDD C     1 ? 4 
ATOM   12763 O O     . THR D 1 207 ? 86.325  11.303  89.612  1.000 34.750  0 207 THR DDD O     1 ? 4 
ATOM   12764 C CB    . THR D 1 207 ? 87.473  11.559  86.696  1.000 37.780  0 207 THR DDD CB    1 ? 4 
ATOM   12765 O OG1   . THR D 1 207 ? 88.330  11.056  85.665  1.000 39.275  0 207 THR DDD OG1   1 ? 4 
ATOM   12766 C CG2   . THR D 1 207 ? 87.187  13.022  86.435  1.000 37.449  0 207 THR DDD CG2   1 ? 4 
ATOM   12767 N N     . LEU D 1 208 ? 87.658  13.153  89.573  1.000 39.748  0 208 LEU DDD N     1 ? 4 
ATOM   12768 C CA    . LEU D 1 208 ? 86.851  14.045  90.439  1.000 41.146  0 208 LEU DDD CA    1 ? 4 
ATOM   12769 C C     . LEU D 1 208 ? 86.332  15.199  89.575  1.000 41.327  0 208 LEU DDD C     1 ? 4 
ATOM   12770 O O     . LEU D 1 208 ? 87.166  15.871  88.918  1.000 40.375  0 208 LEU DDD O     1 ? 4 
ATOM   12771 C CB    . LEU D 1 208 ? 87.708  14.573  91.595  1.000 42.315  0 208 LEU DDD CB    1 ? 4 
ATOM   12772 C CG    . LEU D 1 208 ? 87.024  15.616  92.490  1.000 43.169  0 208 LEU DDD CG    1 ? 4 
ATOM   12773 C CD1   . LEU D 1 208 ? 85.872  14.998  93.283  1.000 42.783  0 208 LEU DDD CD1   1 ? 4 
ATOM   12774 C CD2   . LEU D 1 208 ? 88.038  16.258  93.421  1.000 45.557  0 208 LEU DDD CD2   1 ? 4 
ATOM   12775 N N     . VAL D 1 209 ? 85.021  15.423  89.605  1.000 40.797  0 209 VAL DDD N     1 ? 4 
ATOM   12776 C CA    . VAL D 1 209 ? 84.356  16.590  88.967  1.000 40.784  0 209 VAL DDD CA    1 ? 4 
ATOM   12777 C C     . VAL D 1 209 ? 83.836  17.471  90.112  1.000 42.271  0 209 VAL DDD C     1 ? 4 
ATOM   12778 O O     . VAL D 1 209 ? 83.063  16.969  90.938  1.000 43.331  0 209 VAL DDD O     1 ? 4 
ATOM   12779 C CB    . VAL D 1 209 ? 83.237  16.159  88.001  1.000 38.341  0 209 VAL DDD CB    1 ? 4 
ATOM   12780 C CG1   . VAL D 1 209 ? 82.484  17.339  87.418  1.000 37.329  0 209 VAL DDD CG1   1 ? 4 
ATOM   12781 C CG2   . VAL D 1 209 ? 83.752  15.300  86.870  1.000 38.883  0 209 VAL DDD CG2   1 ? 4 
ATOM   12782 N N     . ILE D 1 210 ? 84.247  18.735  90.150  1.000 42.263  0 210 ILE DDD N     1 ? 4 
ATOM   12783 C CA    . ILE D 1 210 ? 83.739  19.748  91.117  1.000 43.239  0 210 ILE DDD CA    1 ? 4 
ATOM   12784 C C     . ILE D 1 210 ? 82.671  20.579  90.406  1.000 42.650  0 210 ILE DDD C     1 ? 4 
ATOM   12785 O O     . ILE D 1 210 ? 82.986  21.170  89.370  1.000 43.707  0 210 ILE DDD O     1 ? 4 
ATOM   12786 C CB    . ILE D 1 210 ? 84.884  20.609  91.709  1.000 45.072  0 210 ILE DDD CB    1 ? 4 
ATOM   12787 C CG1   . ILE D 1 210 ? 86.025  19.757  92.284  1.000 44.126  0 210 ILE DDD CG1   1 ? 4 
ATOM   12788 C CG2   . ILE D 1 210 ? 84.361  21.573  92.765  1.000 45.650  0 210 ILE DDD CG2   1 ? 4 
ATOM   12789 C CD1   . ILE D 1 210 ? 87.261  19.715  91.414  1.000 44.119  0 210 ILE DDD CD1   1 ? 4 
ATOM   12790 N N     . GLY D 1 211 ? 81.457  20.589  90.953  1.000 41.466  0 211 GLY DDD N     1 ? 4 
ATOM   12791 C CA    . GLY D 1 211 ? 80.282  21.266  90.388  1.000 41.732  0 211 GLY DDD CA    1 ? 4 
ATOM   12792 C C     . GLY D 1 211 ? 79.191  20.269  90.054  1.000 42.466  0 211 GLY DDD C     1 ? 4 
ATOM   12793 O O     . GLY D 1 211 ? 79.450  19.320  89.273  1.000 42.202  0 211 GLY DDD O     1 ? 4 
ATOM   12794 N N     . ALA D 1 212 ? 78.003  20.476  90.612  1.000 42.756  0 212 ALA DDD N     1 ? 4 
ATOM   12795 C CA    . ALA D 1 212 ? 76.770  19.737  90.259  1.000 41.736  0 212 ALA DDD CA    1 ? 4 
ATOM   12796 C C     . ALA D 1 212 ? 75.871  20.619  89.381  1.000 39.411  0 212 ALA DDD C     1 ? 4 
ATOM   12797 O O     . ALA D 1 212 ? 74.623  20.412  89.385  1.000 37.836  0 212 ALA DDD O     1 ? 4 
ATOM   12798 C CB    . ALA D 1 212 ? 76.076  19.283  91.517  1.000 44.353  0 212 ALA DDD CB    1 ? 4 
ATOM   12799 N N     . SER D 1 213 ? 76.489  21.581  88.689  1.000 38.261  0 213 SER DDD N     1 ? 4 
ATOM   12800 C CA    . SER D 1 213 ? 75.992  22.267  87.461  1.000 39.386  0 213 SER DDD CA    1 ? 4 
ATOM   12801 C C     . SER D 1 213 ? 75.700  21.239  86.346  1.000 37.576  0 213 SER DDD C     1 ? 4 
ATOM   12802 O O     . SER D 1 213 ? 76.240  20.101  86.390  1.000 36.529  0 213 SER DDD O     1 ? 4 
ATOM   12803 C CB    . SER D 1 213 ? 77.087  23.222  86.968  1.000 40.129  0 213 SER DDD CB    1 ? 4 
ATOM   12804 O OG    . SER D 1 213 ? 78.285  22.467  86.645  1.000 37.018  0 213 SER DDD OG    1 ? 4 
ATOM   12805 N N     . TYR D 1 214 ? 74.979  21.650  85.313  1.000 37.311  0 214 TYR DDD N     1 ? 4 
ATOM   12806 C CA    . TYR D 1 214 ? 74.667  20.758  84.161  1.000 38.124  0 214 TYR DDD CA    1 ? 4 
ATOM   12807 C C     . TYR D 1 214 ? 75.967  20.247  83.508  1.000 37.465  0 214 TYR DDD C     1 ? 4 
ATOM   12808 O O     . TYR D 1 214 ? 76.035  19.051  83.139  1.000 38.972  0 214 TYR DDD O     1 ? 4 
ATOM   12809 C CB    . TYR D 1 214 ? 73.675  21.444  83.221  1.000 38.552  0 214 TYR DDD CB    1 ? 4 
ATOM   12810 C CG    . TYR D 1 214 ? 74.211  22.311  82.114  1.000 40.490  0 214 TYR DDD CG    1 ? 4 
ATOM   12811 C CD1   . TYR D 1 214 ? 74.501  21.770  80.863  1.000 42.021  0 214 TYR DDD CD1   1 ? 4 
ATOM   12812 C CD2   . TYR D 1 214 ? 74.325  23.685  82.255  1.000 40.572  0 214 TYR DDD CD2   1 ? 4 
ATOM   12813 C CE1   . TYR D 1 214 ? 74.942  22.556  79.813  1.000 42.397  0 214 TYR DDD CE1   1 ? 4 
ATOM   12814 C CE2   . TYR D 1 214 ? 74.795  24.483  81.219  1.000 41.886  0 214 TYR DDD CE2   1 ? 4 
ATOM   12815 C CZ    . TYR D 1 214 ? 75.082  23.919  79.989  1.000 44.452  0 214 TYR DDD CZ    1 ? 4 
ATOM   12816 O OH    . TYR D 1 214 ? 75.555  24.682  78.957  1.000 50.921  0 214 TYR DDD OH    1 ? 4 
ATOM   12817 N N     . ILE D 1 215 ? 76.995  21.089  83.391  1.000 35.379  0 215 ILE DDD N     1 ? 4 
ATOM   12818 C CA    . ILE D 1 215 ? 78.248  20.656  82.707  1.000 34.937  0 215 ILE DDD CA    1 ? 4 
ATOM   12819 C C     . ILE D 1 215 ? 78.884  19.540  83.559  1.000 34.456  0 215 ILE DDD C     1 ? 4 
ATOM   12820 O O     . ILE D 1 215 ? 79.226  18.489  82.995  1.000 32.455  0 215 ILE DDD O     1 ? 4 
ATOM   12821 C CB    . ILE D 1 215 ? 79.177  21.853  82.458  1.000 36.348  0 215 ILE DDD CB    1 ? 4 
ATOM   12822 C CG1   . ILE D 1 215 ? 78.605  22.799  81.407  1.000 35.462  0 215 ILE DDD CG1   1 ? 4 
ATOM   12823 C CG2   . ILE D 1 215 ? 80.595  21.386  82.082  1.000 39.274  0 215 ILE DDD CG2   1 ? 4 
ATOM   12824 C CD1   . ILE D 1 215 ? 79.110  24.207  81.526  1.000 36.649  0 215 ILE DDD CD1   1 ? 4 
ATOM   12825 N N     . GLY D 1 216 ? 78.986  19.754  84.878  1.000 33.045  0 216 GLY DDD N     1 ? 4 
ATOM   12826 C CA    . GLY D 1 216 ? 79.537  18.783  85.834  1.000 33.113  0 216 GLY DDD CA    1 ? 4 
ATOM   12827 C C     . GLY D 1 216 ? 78.811  17.449  85.799  1.000 33.356  0 216 GLY DDD C     1 ? 4 
ATOM   12828 O O     . GLY D 1 216 ? 79.490  16.396  85.683  1.000 33.298  0 216 GLY DDD O     1 ? 4 
ATOM   12829 N N     . LEU D 1 217 ? 77.482  17.467  85.907  1.000 34.842  0 217 LEU DDD N     1 ? 4 
ATOM   12830 C CA    . LEU D 1 217 ? 76.667  16.223  85.950  1.000 36.057  0 217 LEU DDD CA    1 ? 4 
ATOM   12831 C C     . LEU D 1 217 ? 76.770  15.499  84.605  1.000 34.325  0 217 LEU DDD C     1 ? 4 
ATOM   12832 O O     . LEU D 1 217 ? 76.965  14.263  84.642  1.000 34.225  0 217 LEU DDD O     1 ? 4 
ATOM   12833 C CB    . LEU D 1 217 ? 75.199  16.547  86.279  1.000 37.270  0 217 LEU DDD CB    1 ? 4 
ATOM   12834 C CG    . LEU D 1 217 ? 74.880  16.948  87.710  1.000 39.492  0 217 LEU DDD CG    1 ? 4 
ATOM   12835 C CD1   . LEU D 1 217 ? 73.386  16.742  88.004  1.000 41.995  0 217 LEU DDD CD1   1 ? 4 
ATOM   12836 C CD2   . LEU D 1 217 ? 75.704  16.161  88.720  1.000 41.182  0 217 LEU DDD CD2   1 ? 4 
ATOM   12837 N N     . GLU D 1 218 ? 76.630  16.221  83.480  1.000 32.779  0 218 GLU DDD N     1 ? 4 
ATOM   12838 C CA    . GLU D 1 218 ? 76.730  15.618  82.121  1.000 32.307  0 218 GLU DDD CA    1 ? 4 
ATOM   12839 C C     . GLU D 1 218 ? 78.099  14.938  81.996  1.000 30.811  0 218 GLU DDD C     1 ? 4 
ATOM   12840 O O     . GLU D 1 218 ? 78.153  13.781  81.541  1.000 27.782  0 218 GLU DDD O     1 ? 4 
ATOM   12841 C CB    . GLU D 1 218 ? 76.607  16.657  81.006  1.000 31.642  0 218 GLU DDD CB    1 ? 4 
ATOM   12842 C CG    . GLU D 1 218 ? 75.231  17.196  80.808  1.000 31.722  0 218 GLU DDD CG    1 ? 4 
ATOM   12843 C CD    . GLU D 1 218 ? 75.112  18.251  79.724  1.000 32.271  0 218 GLU DDD CD    1 ? 4 
ATOM   12844 O OE1   . GLU D 1 218 ? 76.125  18.906  79.412  1.000 32.865  0 218 GLU DDD OE1   1 ? 4 
ATOM   12845 O OE2   . GLU D 1 218 ? 73.987  18.425  79.179  1.000 33.436  0 218 GLU DDD OE2   1 ? 4 
ATOM   12846 N N     . THR D 1 219 ? 79.152  15.646  82.396  1.000 30.421  0 219 THR DDD N     1 ? 4 
ATOM   12847 C CA    . THR D 1 219 ? 80.553  15.161  82.267  1.000 32.158  0 219 THR DDD CA    1 ? 4 
ATOM   12848 C C     . THR D 1 219 ? 80.743  13.917  83.144  1.000 33.534  0 219 THR DDD C     1 ? 4 
ATOM   12849 O O     . THR D 1 219 ? 81.297  12.912  82.667  1.000 35.555  0 219 THR DDD O     1 ? 4 
ATOM   12850 C CB    . THR D 1 219 ? 81.544  16.276  82.614  1.000 32.242  0 219 THR DDD CB    1 ? 4 
ATOM   12851 O OG1   . THR D 1 219 ? 81.177  17.383  81.791  1.000 29.038  0 219 THR DDD OG1   1 ? 4 
ATOM   12852 C CG2   . THR D 1 219 ? 82.995  15.877  82.422  1.000 33.022  0 219 THR DDD CG2   1 ? 4 
ATOM   12853 N N     . ALA D 1 220 ? 80.309  13.982  84.400  1.000 34.745  0 220 ALA DDD N     1 ? 4 
ATOM   12854 C CA    . ALA D 1 220 ? 80.455  12.859  85.357  1.000 34.891  0 220 ALA DDD CA    1 ? 4 
ATOM   12855 C C     . ALA D 1 220 ? 79.637  11.665  84.834  1.000 32.628  0 220 ALA DDD C     1 ? 4 
ATOM   12856 O O     . ALA D 1 220 ? 80.105  10.516  84.905  1.000 30.161  0 220 ALA DDD O     1 ? 4 
ATOM   12857 C CB    . ALA D 1 220 ? 80.023  13.302  86.728  1.000 33.967  0 220 ALA DDD CB    1 ? 4 
ATOM   12858 N N     . GLY D 1 221 ? 78.440  11.960  84.344  1.000 33.020  0 221 GLY DDD N     1 ? 4 
ATOM   12859 C CA    . GLY D 1 221 ? 77.502  10.967  83.778  1.000 34.295  0 221 GLY DDD CA    1 ? 4 
ATOM   12860 C C     . GLY D 1 221 ? 78.144  10.155  82.656  1.000 33.333  0 221 GLY DDD C     1 ? 4 
ATOM   12861 O O     . GLY D 1 221 ? 78.073  8.897   82.723  1.000 34.671  0 221 GLY DDD O     1 ? 4 
ATOM   12862 N N     . PHE D 1 222 ? 78.781  10.811  81.683  1.000 31.818  0 222 PHE DDD N     1 ? 4 
ATOM   12863 C CA    . PHE D 1 222 ? 79.392  10.059  80.559  1.000 31.689  0 222 PHE DDD CA    1 ? 4 
ATOM   12864 C C     . PHE D 1 222 ? 80.698  9.389   81.034  1.000 31.901  0 222 PHE DDD C     1 ? 4 
ATOM   12865 O O     . PHE D 1 222 ? 80.977  8.236   80.622  1.000 31.001  0 222 PHE DDD O     1 ? 4 
ATOM   12866 C CB    . PHE D 1 222 ? 79.413  10.865  79.252  1.000 29.903  0 222 PHE DDD CB    1 ? 4 
ATOM   12867 C CG    . PHE D 1 222 ? 80.376  12.014  79.154  1.000 29.305  0 222 PHE DDD CG    1 ? 4 
ATOM   12868 C CD1   . PHE D 1 222 ? 81.740  11.801  79.163  1.000 30.911  0 222 PHE DDD CD1   1 ? 4 
ATOM   12869 C CD2   . PHE D 1 222 ? 79.914  13.305  78.954  1.000 29.726  0 222 PHE DDD CD2   1 ? 4 
ATOM   12870 C CE1   . PHE D 1 222 ? 82.633  12.861  79.066  1.000 31.212  0 222 PHE DDD CE1   1 ? 4 
ATOM   12871 C CE2   . PHE D 1 222 ? 80.792  14.368  78.829  1.000 29.724  0 222 PHE DDD CE2   1 ? 4 
ATOM   12872 C CZ    . PHE D 1 222 ? 82.158  14.149  78.916  1.000 31.907  0 222 PHE DDD CZ    1 ? 4 
ATOM   12873 N N     . LEU D 1 223 ? 81.489  10.011  81.904  1.000 31.881  0 223 LEU DDD N     1 ? 4 
ATOM   12874 C CA    . LEU D 1 223 ? 82.743  9.337   82.347  1.000 33.052  0 223 LEU DDD CA    1 ? 4 
ATOM   12875 C C     . LEU D 1 223 ? 82.404  8.048   83.109  1.000 33.221  0 223 LEU DDD C     1 ? 4 
ATOM   12876 O O     . LEU D 1 223 ? 83.090  7.018   82.885  1.000 30.869  0 223 LEU DDD O     1 ? 4 
ATOM   12877 C CB    . LEU D 1 223 ? 83.597  10.289  83.172  1.000 33.666  0 223 LEU DDD CB    1 ? 4 
ATOM   12878 C CG    . LEU D 1 223 ? 84.240  11.431  82.385  1.000 34.490  0 223 LEU DDD CG    1 ? 4 
ATOM   12879 C CD1   . LEU D 1 223 ? 85.073  12.294  83.304  1.000 36.366  0 223 LEU DDD CD1   1 ? 4 
ATOM   12880 C CD2   . LEU D 1 223 ? 85.125  10.917  81.240  1.000 34.865  0 223 LEU DDD CD2   1 ? 4 
ATOM   12881 N N     . ASN D 1 224 ? 81.364  8.067   83.944  1.000 34.457  0 224 ASN DDD N     1 ? 4 
ATOM   12882 C CA    . ASN D 1 224 ? 80.926  6.850   84.686  1.000 35.708  0 224 ASN DDD CA    1 ? 4 
ATOM   12883 C C     . ASN D 1 224 ? 80.390  5.813   83.689  1.000 36.307  0 224 ASN DDD C     1 ? 4 
ATOM   12884 O O     . ASN D 1 224 ? 80.829  4.660   83.773  1.000 37.649  0 224 ASN DDD O     1 ? 4 
ATOM   12885 C CB    . ASN D 1 224 ? 79.879  7.155   85.756  1.000 35.394  0 224 ASN DDD CB    1 ? 4 
ATOM   12886 C CG    . ASN D 1 224 ? 79.437  5.927   86.526  1.000 34.615  0 224 ASN DDD CG    1 ? 4 
ATOM   12887 O OD1   . ASN D 1 224 ? 80.127  5.443   87.398  1.000 32.615  0 224 ASN DDD OD1   1 ? 4 
ATOM   12888 N ND2   . ASN D 1 224 ? 78.263  5.415   86.217  1.000 36.208  0 224 ASN DDD ND2   1 ? 4 
ATOM   12889 N N     . GLU D 1 225 ? 79.499  6.206   82.776  1.000 37.038  0 225 GLU DDD N     1 ? 4 
ATOM   12890 C CA    . GLU D 1 225 ? 78.925  5.284   81.760  0.940 38.313  0 225 GLU DDD CA    1 ? 4 
ATOM   12891 C C     . GLU D 1 225 ? 80.070  4.630   80.974  1.000 37.080  0 225 GLU DDD C     1 ? 4 
ATOM   12892 O O     . GLU D 1 225 ? 79.894  3.478   80.547  1.000 39.698  0 225 GLU DDD O     1 ? 4 
ATOM   12893 C CB    . GLU D 1 225 ? 77.945  5.990   80.814  0.940 40.969  0 225 GLU DDD CB    1 ? 4 
ATOM   12894 C CG    . GLU D 1 225 ? 76.493  5.781   81.186  0.940 44.908  0 225 GLU DDD CG    1 ? 4 
ATOM   12895 C CD    . GLU D 1 225 ? 75.454  6.509   80.342  0.940 47.401  0 225 GLU DDD CD    1 ? 4 
ATOM   12896 O OE1   . GLU D 1 225 ? 75.421  7.769   80.354  0.940 47.958  0 225 GLU DDD OE1   1 ? 4 
ATOM   12897 O OE2   . GLU D 1 225 ? 74.656  5.818   79.682  0.940 55.980  0 225 GLU DDD OE2   1 ? 4 
ATOM   12898 N N     . LEU D 1 226 ? 81.185  5.335   80.783  1.000 33.929  0 226 LEU DDD N     1 ? 4 
ATOM   12899 C CA    . LEU D 1 226 ? 82.306  4.865   79.933  1.000 33.676  0 226 LEU DDD CA    1 ? 4 
ATOM   12900 C C     . LEU D 1 226 ? 83.293  4.029   80.752  1.000 36.743  0 226 LEU DDD C     1 ? 4 
ATOM   12901 O O     . LEU D 1 226 ? 84.352  3.633   80.184  1.000 35.646  0 226 LEU DDD O     1 ? 4 
ATOM   12902 C CB    . LEU D 1 226 ? 83.009  6.064   79.295  1.000 31.694  0 226 LEU DDD CB    1 ? 4 
ATOM   12903 C CG    . LEU D 1 226 ? 82.298  6.717   78.116  1.000 31.034  0 226 LEU DDD CG    1 ? 4 
ATOM   12904 C CD1   . LEU D 1 226 ? 83.102  7.916   77.649  1.000 32.028  0 226 LEU DDD CD1   1 ? 4 
ATOM   12905 C CD2   . LEU D 1 226 ? 82.098  5.744   76.967  1.000 30.528  0 226 LEU DDD CD2   1 ? 4 
ATOM   12906 N N     . GLY D 1 227 ? 83.004  3.840   82.048  1.000 39.625  0 227 GLY DDD N     1 ? 4 
ATOM   12907 C CA    . GLY D 1 227 ? 83.676  2.866   82.928  1.000 39.814  0 227 GLY DDD CA    1 ? 4 
ATOM   12908 C C     . GLY D 1 227 ? 84.716  3.493   83.835  1.000 39.908  0 227 GLY DDD C     1 ? 4 
ATOM   12909 O O     . GLY D 1 227 ? 85.405  2.727   84.513  1.000 39.940  0 227 GLY DDD O     1 ? 4 
ATOM   12910 N N     . PHE D 1 228 ? 84.825  4.824   83.871  1.000 37.437  0 228 PHE DDD N     1 ? 4 
ATOM   12911 C CA    . PHE D 1 228 ? 85.801  5.538   84.735  1.000 36.948  0 228 PHE DDD CA    1 ? 4 
ATOM   12912 C C     . PHE D 1 228 ? 85.252  5.670   86.157  1.000 36.979  0 228 PHE DDD C     1 ? 4 
ATOM   12913 O O     . PHE D 1 228 ? 84.036  5.874   86.303  1.000 38.083  0 228 PHE DDD O     1 ? 4 
ATOM   12914 C CB    . PHE D 1 228 ? 86.191  6.877   84.104  1.000 36.129  0 228 PHE DDD CB    1 ? 4 
ATOM   12915 C CG    . PHE D 1 228 ? 86.864  6.700   82.771  1.000 36.614  0 228 PHE DDD CG    1 ? 4 
ATOM   12916 C CD1   . PHE D 1 228 ? 88.098  6.068   82.692  1.000 36.911  0 228 PHE DDD CD1   1 ? 4 
ATOM   12917 C CD2   . PHE D 1 228 ? 86.234  7.073   81.592  1.000 37.135  0 228 PHE DDD CD2   1 ? 4 
ATOM   12918 C CE1   . PHE D 1 228 ? 88.694  5.833   81.473  1.000 36.709  0 228 PHE DDD CE1   1 ? 4 
ATOM   12919 C CE2   . PHE D 1 228 ? 86.850  6.869   80.370  1.000 36.737  0 228 PHE DDD CE2   1 ? 4 
ATOM   12920 C CZ    . PHE D 1 228 ? 88.074  6.250   80.316  1.000 37.670  0 228 PHE DDD CZ    1 ? 4 
ATOM   12921 N N     . ASP D 1 229 ? 86.131  5.546   87.162  1.000 38.183  0 229 ASP DDD N     1 ? 4 
ATOM   12922 C CA    . ASP D 1 229 ? 85.842  5.765   88.611  1.000 38.749  0 229 ASP DDD CA    1 ? 4 
ATOM   12923 C C     . ASP D 1 229 ? 85.601  7.260   88.793  1.000 37.159  0 229 ASP DDD C     1 ? 4 
ATOM   12924 O O     . ASP D 1 229 ? 86.547  8.048   88.604  1.000 38.127  0 229 ASP DDD O     1 ? 4 
ATOM   12925 C CB    . ASP D 1 229 ? 86.973  5.238   89.493  1.000 42.129  0 229 ASP DDD CB    1 ? 4 
ATOM   12926 C CG    . ASP D 1 229 ? 86.798  5.383   91.009  1.000 45.413  0 229 ASP DDD CG    1 ? 4 
ATOM   12927 O OD1   . ASP D 1 229 ? 86.058  6.285   91.464  1.000 47.421  0 229 ASP DDD OD1   1 ? 4 
ATOM   12928 O OD2   . ASP D 1 229 ? 87.452  4.609   91.742  1.000 48.124  0 229 ASP DDD OD2   1 ? 4 
ATOM   12929 N N     . THR D 1 230 ? 84.368  7.633   89.083  1.000 34.677  0 230 THR DDD N     1 ? 4 
ATOM   12930 C CA    . THR D 1 230 ? 83.884  9.010   88.943  1.000 35.463  0 230 THR DDD CA    1 ? 4 
ATOM   12931 C C     . THR D 1 230 ? 83.253  9.467   90.263  1.000 36.475  0 230 THR DDD C     1 ? 4 
ATOM   12932 O O     . THR D 1 230 ? 82.391  8.730   90.821  1.000 35.518  0 230 THR DDD O     1 ? 4 
ATOM   12933 C CB    . THR D 1 230 ? 82.912  9.089   87.760  1.000 36.213  0 230 THR DDD CB    1 ? 4 
ATOM   12934 O OG1   . THR D 1 230 ? 83.687  8.774   86.596  1.000 37.085  0 230 THR DDD OG1   1 ? 4 
ATOM   12935 C CG2   . THR D 1 230 ? 82.230  10.433  87.627  1.000 36.251  0 230 THR DDD CG2   1 ? 4 
ATOM   12936 N N     . THR D 1 231 ? 83.608  10.680  90.685  1.000 36.361  0 231 THR DDD N     1 ? 4 
ATOM   12937 C CA    . THR D 1 231 ? 83.159  11.296  91.945  1.000 37.229  0 231 THR DDD CA    1 ? 4 
ATOM   12938 C C     . THR D 1 231 ? 82.793  12.748  91.654  1.000 37.631  0 231 THR DDD C     1 ? 4 
ATOM   12939 O O     . THR D 1 231 ? 83.559  13.416  90.943  1.000 36.753  0 231 THR DDD O     1 ? 4 
ATOM   12940 C CB    . THR D 1 231 ? 84.233  11.143  93.022  1.000 41.243  0 231 THR DDD CB    1 ? 4 
ATOM   12941 O OG1   . THR D 1 231 ? 84.527  9.758   93.160  1.000 42.316  0 231 THR DDD OG1   1 ? 4 
ATOM   12942 C CG2   . THR D 1 231 ? 83.815  11.704  94.365  1.000 43.108  0 231 THR DDD CG2   1 ? 4 
ATOM   12943 N N     . VAL D 1 232 ? 81.618  13.185  92.116  1.000 39.024  0 232 VAL DDD N     1 ? 4 
ATOM   12944 C CA    . VAL D 1 232 ? 81.183  14.603  92.024  1.000 40.204  0 232 VAL DDD CA    1 ? 4 
ATOM   12945 C C     . VAL D 1 232 ? 81.220  15.222  93.431  1.000 42.772  0 232 VAL DDD C     1 ? 4 
ATOM   12946 O O     . VAL D 1 232 ? 80.554  14.669  94.317  1.000 41.220  0 232 VAL DDD O     1 ? 4 
ATOM   12947 C CB    . VAL D 1 232 ? 79.779  14.700  91.411  1.000 39.802  0 232 VAL DDD CB    1 ? 4 
ATOM   12948 C CG1   . VAL D 1 232 ? 79.200  16.100  91.583  1.000 39.851  0 232 VAL DDD CG1   1 ? 4 
ATOM   12949 C CG2   . VAL D 1 232 ? 79.758  14.236  89.962  1.000 38.499  0 232 VAL DDD CG2   1 ? 4 
ATOM   12950 N N     . ALA D 1 233 ? 81.983  16.310  93.598  1.000 44.395  0 233 ALA DDD N     1 ? 4 
ATOM   12951 C CA    . ALA D 1 233 ? 81.978  17.210  94.771  1.000 46.595  0 233 ALA DDD CA    1 ? 4 
ATOM   12952 C C     . ALA D 1 233 ? 80.937  18.300  94.536  1.000 49.334  0 233 ALA DDD C     1 ? 4 
ATOM   12953 O O     . ALA D 1 233 ? 81.172  19.184  93.705  1.000 48.460  0 233 ALA DDD O     1 ? 4 
ATOM   12954 C CB    . ALA D 1 233 ? 83.341  17.816  94.990  1.000 48.757  0 233 ALA DDD CB    1 ? 4 
ATOM   12955 N N     . MET D 1 234 ? 79.805  18.171  95.222  1.000 53.102  0 234 MET DDD N     1 ? 4 
ATOM   12956 C CA    . MET D 1 234 ? 78.625  19.047  95.147  1.000 53.067  0 234 MET DDD CA    1 ? 4 
ATOM   12957 C C     . MET D 1 234 ? 78.615  19.894  96.421  1.000 58.072  0 234 MET DDD C     1 ? 4 
ATOM   12958 O O     . MET D 1 234 ? 78.451  19.313  97.533  1.000 59.838  0 234 MET DDD O     1 ? 4 
ATOM   12959 C CB    . MET D 1 234 ? 77.391  18.151  95.054  1.000 52.616  0 234 MET DDD CB    1 ? 4 
ATOM   12960 C CG    . MET D 1 234 ? 76.091  18.879  95.137  1.000 52.635  0 234 MET DDD CG    1 ? 4 
ATOM   12961 S SD    . MET D 1 234 ? 74.713  17.884  94.521  1.000 53.772  0 234 MET DDD SD    1 ? 4 
ATOM   12962 C CE    . MET D 1 234 ? 74.756  16.438  95.578  1.000 56.509  0 234 MET DDD CE    1 ? 4 
ATOM   12963 N N     . ARG D 1 235 ? 78.852  21.199  96.288  1.000 61.393  0 235 ARG DDD N     1 ? 4 
ATOM   12964 C CA    . ARG D 1 235 ? 78.840  22.139  97.445  1.000 64.050  0 235 ARG DDD CA    1 ? 4 
ATOM   12965 C C     . ARG D 1 235 ? 77.483  22.064  98.178  1.000 64.315  0 235 ARG DDD C     1 ? 4 
ATOM   12966 O O     . ARG D 1 235 ? 77.489  22.017  99.439  1.000 67.616  0 235 ARG DDD O     1 ? 4 
ATOM   12967 C CB    . ARG D 1 235 ? 79.167  23.576  97.023  1.000 65.336  0 235 ARG DDD CB    1 ? 4 
ATOM   12968 C CG    . ARG D 1 235 ? 79.359  24.491  98.224  1.000 67.881  0 235 ARG DDD CG    1 ? 4 
ATOM   12969 C CD    . ARG D 1 235 ? 80.090  25.793  98.039  1.000 70.866  0 235 ARG DDD CD    1 ? 4 
ATOM   12970 N NE    . ARG D 1 235 ? 80.359  26.303  99.376  1.000 75.851  0 235 ARG DDD NE    1 ? 4 
ATOM   12971 C CZ    . ARG D 1 235 ? 79.470  26.922  100.160 1.000 79.770  0 235 ARG DDD CZ    1 ? 4 
ATOM   12972 N NH1   . ARG D 1 235 ? 78.232  27.130  99.735  1.000 78.712  0 235 ARG DDD NH1   1 ? 4 
ATOM   12973 N NH2   . ARG D 1 235 ? 79.825  27.340  101.368 1.000 81.013  0 235 ARG DDD NH2   1 ? 4 
ATOM   12974 N N     . SER D 1 236 ? 76.354  22.050  97.454  1.000 63.464  0 236 SER DDD N     1 ? 4 
ATOM   12975 C CA    . SER D 1 236 ? 75.007  22.023  98.087  1.000 59.737  0 236 SER DDD CA    1 ? 4 
ATOM   12976 C C     . SER D 1 236 ? 74.054  21.125  97.300  1.000 59.372  0 236 SER DDD C     1 ? 4 
ATOM   12977 O O     . SER D 1 236 ? 73.875  19.970  97.719  1.000 59.508  0 236 SER DDD O     1 ? 4 
ATOM   12978 C CB    . SER D 1 236 ? 74.447  23.408  98.295  1.000 56.480  0 236 SER DDD CB    1 ? 4 
ATOM   12979 O OG    . SER D 1 236 ? 74.507  24.156  97.108  1.000 50.565  0 236 SER DDD OG    1 ? 4 
ATOM   12980 N N     . ILE D 1 237 ? 73.455  21.636  96.225  1.000 60.147  0 237 ILE DDD N     1 ? 4 
ATOM   12981 C CA    . ILE D 1 237 ? 72.317  20.962  95.535  1.000 60.011  0 237 ILE DDD CA    1 ? 4 
ATOM   12982 C C     . ILE D 1 237 ? 72.646  20.800  94.054  1.000 57.682  0 237 ILE DDD C     1 ? 4 
ATOM   12983 O O     . ILE D 1 237 ? 73.417  21.579  93.500  1.000 55.796  0 237 ILE DDD O     1 ? 4 
ATOM   12984 C CB    . ILE D 1 237 ? 71.007  21.737  95.770  1.000 62.313  0 237 ILE DDD CB    1 ? 4 
ATOM   12985 C CG1   . ILE D 1 237 ? 71.073  23.146  95.168  1.000 64.149  0 237 ILE DDD CG1   1 ? 4 
ATOM   12986 C CG2   . ILE D 1 237 ? 70.665  21.769  97.266  1.000 61.927  0 237 ILE DDD CG2   1 ? 4 
ATOM   12987 C CD1   . ILE D 1 237 ? 69.742  23.882  95.114  1.000 64.978  0 237 ILE DDD CD1   1 ? 4 
ATOM   12988 N N     . PRO D 1 238 ? 72.079  19.770  93.388  1.000 56.625  0 238 PRO DDD N     1 ? 4 
ATOM   12989 C CA    . PRO D 1 238 ? 72.261  19.568  91.948  1.000 54.704  0 238 PRO DDD CA    1 ? 4 
ATOM   12990 C C     . PRO D 1 238 ? 71.438  20.484  91.031  1.000 51.231  0 238 PRO DDD C     1 ? 4 
ATOM   12991 O O     . PRO D 1 238 ? 70.306  20.711  91.309  1.000 50.084  0 238 PRO DDD O     1 ? 4 
ATOM   12992 C CB    . PRO D 1 238 ? 71.798  18.119  91.751  1.000 55.148  0 238 PRO DDD CB    1 ? 4 
ATOM   12993 C CG    . PRO D 1 238 ? 70.751  17.896  92.823  1.000 55.934  0 238 PRO DDD CG    1 ? 4 
ATOM   12994 C CD    . PRO D 1 238 ? 71.244  18.721  94.003  1.000 57.481  0 238 PRO DDD CD    1 ? 4 
ATOM   12995 N N     . LEU D 1 239 ? 72.049  20.988  89.958  1.000 51.365  0 239 LEU DDD N     1 ? 4 
ATOM   12996 C CA    . LEU D 1 239 ? 71.355  21.793  88.925  1.000 51.594  0 239 LEU DDD CA    1 ? 4 
ATOM   12997 C C     . LEU D 1 239 ? 70.566  22.923  89.586  1.000 53.560  0 239 LEU DDD C     1 ? 4 
ATOM   12998 O O     . LEU D 1 239 ? 69.346  22.996  89.398  1.000 51.211  0 239 LEU DDD O     1 ? 4 
ATOM   12999 C CB    . LEU D 1 239 ? 70.412  20.856  88.170  1.000 50.456  0 239 LEU DDD CB    1 ? 4 
ATOM   13000 C CG    . LEU D 1 239 ? 71.068  19.665  87.487  1.000 48.438  0 239 LEU DDD CG    1 ? 4 
ATOM   13001 C CD1   . LEU D 1 239 ? 70.028  18.824  86.785  1.000 47.810  0 239 LEU DDD CD1   1 ? 4 
ATOM   13002 C CD2   . LEU D 1 239 ? 72.098  20.130  86.480  1.000 48.074  0 239 LEU DDD CD2   1 ? 4 
ATOM   13003 N N     . ARG D 1 240 ? 71.246  23.783  90.322  1.000 58.457  0 240 ARG DDD N     1 ? 4 
ATOM   13004 C CA    . ARG D 1 240 ? 70.634  24.965  90.974  1.000 62.688  0 240 ARG DDD CA    1 ? 4 
ATOM   13005 C C     . ARG D 1 240 ? 69.875  25.793  89.927  1.000 59.524  0 240 ARG DDD C     1 ? 4 
ATOM   13006 O O     . ARG D 1 240 ? 70.475  26.135  88.886  1.000 54.884  0 240 ARG DDD O     1 ? 4 
ATOM   13007 C CB    . ARG D 1 240 ? 71.744  25.772  91.639  1.000 70.828  0 240 ARG DDD CB    1 ? 4 
ATOM   13008 C CG    . ARG D 1 240 ? 71.275  26.899  92.543  1.000 79.834  0 240 ARG DDD CG    1 ? 4 
ATOM   13009 C CD    . ARG D 1 240 ? 72.432  27.885  92.633  1.000 88.205  0 240 ARG DDD CD    1 ? 4 
ATOM   13010 N NE    . ARG D 1 240 ? 73.144  27.956  91.348  1.000 92.019  0 240 ARG DDD NE    1 ? 4 
ATOM   13011 C CZ    . ARG D 1 240 ? 72.696  28.572  90.245  1.000 93.446  0 240 ARG DDD CZ    1 ? 4 
ATOM   13012 N NH1   . ARG D 1 240 ? 71.549  29.232  90.257  1.000 96.666  0 240 ARG DDD NH1   1 ? 4 
ATOM   13013 N NH2   . ARG D 1 240 ? 73.405  28.538  89.131  1.000 89.064  0 240 ARG DDD NH2   1 ? 4 
ATOM   13014 N N     . GLY D 1 241 ? 68.611  26.132  90.222  1.000 56.235  0 241 GLY DDD N     1 ? 4 
ATOM   13015 C CA    . GLY D 1 241 ? 67.713  26.914  89.355  1.000 53.315  0 241 GLY DDD CA    1 ? 4 
ATOM   13016 C C     . GLY D 1 241 ? 66.719  26.015  88.659  1.000 53.115  0 241 GLY DDD C     1 ? 4 
ATOM   13017 O O     . GLY D 1 241 ? 65.639  26.486  88.275  1.000 58.017  0 241 GLY DDD O     1 ? 4 
ATOM   13018 N N     . PHE D 1 242 ? 67.072  24.748  88.485  1.000 54.017  0 242 PHE DDD N     1 ? 4 
ATOM   13019 C CA    . PHE D 1 242 ? 66.224  23.735  87.810  1.000 53.426  0 242 PHE DDD CA    1 ? 4 
ATOM   13020 C C     . PHE D 1 242 ? 65.259  23.142  88.837  1.000 49.445  0 242 PHE DDD C     1 ? 4 
ATOM   13021 O O     . PHE D 1 242 ? 65.540  23.164  90.068  1.000 51.411  0 242 PHE DDD O     1 ? 4 
ATOM   13022 C CB    . PHE D 1 242 ? 67.096  22.655  87.165  1.000 56.705  0 242 PHE DDD CB    1 ? 4 
ATOM   13023 C CG    . PHE D 1 242 ? 67.903  23.068  85.951  1.000 58.269  0 242 PHE DDD CG    1 ? 4 
ATOM   13024 C CD1   . PHE D 1 242 ? 68.877  24.052  86.032  1.000 57.347  0 242 PHE DDD CD1   1 ? 4 
ATOM   13025 C CD2   . PHE D 1 242 ? 67.711  22.445  84.714  1.000 59.382  0 242 PHE DDD CD2   1 ? 4 
ATOM   13026 C CE1   . PHE D 1 242 ? 69.645  24.388  84.920  1.000 59.696  0 242 PHE DDD CE1   1 ? 4 
ATOM   13027 C CE2   . PHE D 1 242 ? 68.466  22.795  83.600  1.000 57.341  0 242 PHE DDD CE2   1 ? 4 
ATOM   13028 C CZ    . PHE D 1 242 ? 69.436  23.767  83.700  1.000 57.368  0 242 PHE DDD CZ    1 ? 4 
ATOM   13029 N N     . ASP D 1 243 ? 64.160  22.595  88.346  1.000 45.676  0 243 ASP DDD N     1 ? 4 
ATOM   13030 C CA    . ASP D 1 243 ? 63.119  21.907  89.160  1.000 43.994  0 243 ASP DDD CA    1 ? 4 
ATOM   13031 C C     . ASP D 1 243 ? 63.767  20.903  90.113  1.000 43.283  0 243 ASP DDD C     1 ? 4 
ATOM   13032 O O     . ASP D 1 243 ? 64.580  20.101  89.640  1.000 40.881  0 243 ASP DDD O     1 ? 4 
ATOM   13033 C CB    . ASP D 1 243 ? 62.167  21.167  88.243  1.000 42.667  0 243 ASP DDD CB    1 ? 4 
ATOM   13034 C CG    . ASP D 1 243 ? 61.059  20.474  88.978  1.000 42.841  0 243 ASP DDD CG    1 ? 4 
ATOM   13035 O OD1   . ASP D 1 243 ? 60.143  21.186  89.404  1.000 42.310  0 243 ASP DDD OD1   1 ? 4 
ATOM   13036 O OD2   . ASP D 1 243 ? 61.137  19.228  89.120  1.000 42.767  0 243 ASP DDD OD2   1 ? 4 
ATOM   13037 N N     . ARG D 1 244 ? 63.419  20.962  91.405  1.000 42.856  0 244 ARG DDD N     1 ? 4 
ATOM   13038 C CA    . ARG D 1 244 ? 64.081  20.156  92.465  1.000 43.168  0 244 ARG DDD CA    1 ? 4 
ATOM   13039 C C     . ARG D 1 244 ? 63.778  18.674  92.231  1.000 41.084  0 244 ARG DDD C     1 ? 4 
ATOM   13040 O O     . ARG D 1 244 ? 64.750  17.882  92.198  1.000 43.367  0 244 ARG DDD O     1 ? 4 
ATOM   13041 C CB    . ARG D 1 244 ? 63.666  20.565  93.882  1.000 45.278  0 244 ARG DDD CB    1 ? 4 
ATOM   13042 C CG    . ARG D 1 244 ? 64.154  21.944  94.296  1.000 46.369  0 244 ARG DDD CG    1 ? 4 
ATOM   13043 C CD    . ARG D 1 244 ? 65.659  22.008  94.459  1.000 47.355  0 244 ARG DDD CD    1 ? 4 
ATOM   13044 N NE    . ARG D 1 244 ? 66.302  22.285  93.191  1.000 47.507  0 244 ARG DDD NE    1 ? 4 
ATOM   13045 C CZ    . ARG D 1 244 ? 67.433  21.741  92.756  1.000 47.462  0 244 ARG DDD CZ    1 ? 4 
ATOM   13046 N NH1   . ARG D 1 244 ? 68.121  20.870  93.486  1.000 48.612  0 244 ARG DDD NH1   1 ? 4 
ATOM   13047 N NH2   . ARG D 1 244 ? 67.854  22.075  91.557  1.000 47.544  0 244 ARG DDD NH2   1 ? 4 
ATOM   13048 N N     . GLN D 1 245 ? 62.504  18.315  92.059  1.000 38.891  0 245 GLN DDD N     1 ? 4 
ATOM   13049 C CA    . GLN D 1 245 ? 62.074  16.901  91.889  1.000 37.597  0 245 GLN DDD CA    1 ? 4 
ATOM   13050 C C     . GLN D 1 245 ? 62.887  16.248  90.763  1.000 37.232  0 245 GLN DDD C     1 ? 4 
ATOM   13051 O O     . GLN D 1 245 ? 63.452  15.168  91.013  1.000 38.117  0 245 GLN DDD O     1 ? 4 
ATOM   13052 C CB    . GLN D 1 245 ? 60.590  16.799  91.584  1.000 36.636  0 245 GLN DDD CB    1 ? 4 
ATOM   13053 C CG    . GLN D 1 245 ? 60.077  15.375  91.686  1.000 37.245  0 245 GLN DDD CG    1 ? 4 
ATOM   13054 C CD    . GLN D 1 245 ? 58.588  15.312  91.443  1.000 38.302  0 245 GLN DDD CD    1 ? 4 
ATOM   13055 O OE1   . GLN D 1 245 ? 57.974  16.248  90.936  1.000 40.732  0 245 GLN DDD OE1   1 ? 4 
ATOM   13056 N NE2   . GLN D 1 245 ? 57.982  14.191  91.787  1.000 38.386  0 245 GLN DDD NE2   1 ? 4 
ATOM   13057 N N     . CYS D 1 246 ? 62.953  16.885  89.586  1.000 36.277  0 246 CYS DDD N     1 ? 4 
ATOM   13058 C CA    . CYS D 1 246 ? 63.671  16.375  88.391  1.000 37.100  0 246 CYS DDD CA    1 ? 4 
ATOM   13059 C C     . CYS D 1 246 ? 65.175  16.333  88.664  1.000 39.161  0 246 CYS DDD C     1 ? 4 
ATOM   13060 O O     . CYS D 1 246 ? 65.808  15.299  88.345  1.000 43.264  0 246 CYS DDD O     1 ? 4 
ATOM   13061 C CB    . CYS D 1 246 ? 63.404  17.229  87.152  1.000 36.171  0 246 CYS DDD CB    1 ? 4 
ATOM   13062 S SG    . CYS D 1 246 ? 61.685  17.128  86.556  1.000 34.633  0 246 CYS DDD SG    1 ? 4 
ATOM   13063 N N     . SER D 1 247 ? 65.752  17.405  89.209  1.000 39.396  0 247 SER DDD N     1 ? 4 
ATOM   13064 C CA    . SER D 1 247 ? 67.206  17.459  89.484  1.000 39.480  0 247 SER DDD CA    1 ? 4 
ATOM   13065 C C     . SER D 1 247 ? 67.588  16.297  90.408  1.000 40.275  0 247 SER DDD C     1 ? 4 
ATOM   13066 O O     . SER D 1 247 ? 68.641  15.690  90.181  1.000 36.449  0 247 SER DDD O     1 ? 4 
ATOM   13067 C CB    . SER D 1 247 ? 67.617  18.794  90.014  1.000 40.110  0 247 SER DDD CB    1 ? 4 
ATOM   13068 O OG    . SER D 1 247 ? 67.308  19.827  89.087  1.000 39.781  0 247 SER DDD OG    1 ? 4 
ATOM   13069 N N     . GLU D 1 248 ? 66.725  15.938  91.361  1.000 43.222  0 248 GLU DDD N     1 ? 4 
ATOM   13070 C CA    . GLU D 1 248 ? 67.047  14.906  92.394  1.000 45.767  0 248 GLU DDD CA    1 ? 4 
ATOM   13071 C C     . GLU D 1 248 ? 66.860  13.498  91.804  1.000 43.006  0 248 GLU DDD C     1 ? 4 
ATOM   13072 O O     . GLU D 1 248 ? 67.671  12.601  92.118  1.000 43.931  0 248 GLU DDD O     1 ? 4 
ATOM   13073 C CB    . GLU D 1 248 ? 66.203  15.127  93.656  1.000 48.844  0 248 GLU DDD CB    1 ? 4 
ATOM   13074 C CG    . GLU D 1 248 ? 66.691  16.283  94.523  1.000 51.678  0 248 GLU DDD CG    1 ? 4 
ATOM   13075 C CD    . GLU D 1 248 ? 65.663  16.794  95.521  1.000 53.748  0 248 GLU DDD CD    1 ? 4 
ATOM   13076 O OE1   . GLU D 1 248 ? 64.758  16.028  95.880  1.000 54.444  0 248 GLU DDD OE1   1 ? 4 
ATOM   13077 O OE2   . GLU D 1 248 ? 65.770  17.958  95.945  1.000 57.590  0 248 GLU DDD OE2   1 ? 4 
ATOM   13078 N N     . LYS D 1 249 ? 65.846  13.307  90.963  1.000 40.396  0 249 LYS DDD N     1 ? 4 
ATOM   13079 C CA    . LYS D 1 249 ? 65.721  12.056  90.183  1.000 40.039  0 249 LYS DDD CA    1 ? 4 
ATOM   13080 C C     . LYS D 1 249 ? 67.025  11.791  89.397  1.000 38.535  0 249 LYS DDD C     1 ? 4 
ATOM   13081 O O     . LYS D 1 249 ? 67.548  10.653  89.462  1.000 37.248  0 249 LYS DDD O     1 ? 4 
ATOM   13082 C CB    . LYS D 1 249 ? 64.541  12.071  89.216  1.000 39.155  0 249 LYS DDD CB    1 ? 4 
ATOM   13083 C CG    . LYS D 1 249 ? 64.361  10.698  88.600  1.000 39.206  0 249 LYS DDD CG    1 ? 4 
ATOM   13084 C CD    . LYS D 1 249 ? 63.274  10.570  87.600  1.000 39.484  0 249 LYS DDD CD    1 ? 4 
ATOM   13085 C CE    . LYS D 1 249 ? 63.119  9.149   87.098  1.000 40.754  0 249 LYS DDD CE    1 ? 4 
ATOM   13086 N NZ    . LYS D 1 249 ? 63.250  8.151   88.200  1.000 41.606  0 249 LYS DDD NZ    1 ? 4 
ATOM   13087 N N     . ILE D 1 250 ? 67.583  12.793  88.726  1.000 36.541  0 250 ILE DDD N     1 ? 4 
ATOM   13088 C CA    . ILE D 1 250 ? 68.848  12.563  87.963  1.000 37.892  0 250 ILE DDD CA    1 ? 4 
ATOM   13089 C C     . ILE D 1 250 ? 69.942  12.032  88.900  1.000 37.122  0 250 ILE DDD C     1 ? 4 
ATOM   13090 O O     . ILE D 1 250 ? 70.554  10.980  88.590  1.000 35.516  0 250 ILE DDD O     1 ? 4 
ATOM   13091 C CB    . ILE D 1 250 ? 69.268  13.827  87.208  1.000 38.533  0 250 ILE DDD CB    1 ? 4 
ATOM   13092 C CG1   . ILE D 1 250 ? 68.257  14.120  86.103  1.000 39.343  0 250 ILE DDD CG1   1 ? 4 
ATOM   13093 C CG2   . ILE D 1 250 ? 70.669  13.688  86.639  1.000 37.926  0 250 ILE DDD CG2   1 ? 4 
ATOM   13094 C CD1   . ILE D 1 250 ? 68.180  15.567  85.758  1.000 41.624  0 250 ILE DDD CD1   1 ? 4 
ATOM   13095 N N     . VAL D 1 251 ? 70.162  12.714  90.021  1.000 38.348  0 251 VAL DDD N     1 ? 4 
ATOM   13096 C CA    . VAL D 1 251 ? 71.231  12.352  90.997  1.000 38.729  0 251 VAL DDD CA    1 ? 4 
ATOM   13097 C C     . VAL D 1 251 ? 70.950  10.950  91.539  1.000 40.255  0 251 VAL DDD C     1 ? 4 
ATOM   13098 O O     . VAL D 1 251 ? 71.898  10.150  91.578  1.000 40.161  0 251 VAL DDD O     1 ? 4 
ATOM   13099 C CB    . VAL D 1 251 ? 71.352  13.413  92.096  1.000 39.268  0 251 VAL DDD CB    1 ? 4 
ATOM   13100 C CG1   . VAL D 1 251 ? 72.204  12.939  93.289  1.000 39.579  0 251 VAL DDD CG1   1 ? 4 
ATOM   13101 C CG2   . VAL D 1 251 ? 71.861  14.711  91.473  1.000 37.610  0 251 VAL DDD CG2   1 ? 4 
ATOM   13102 N N     . GLU D 1 252 ? 69.696  10.644  91.873  1.000 42.531  0 252 GLU DDD N     1 ? 4 
ATOM   13103 C CA    . GLU D 1 252 ? 69.268  9.278   92.288  1.000 46.738  0 252 GLU DDD CA    1 ? 4 
ATOM   13104 C C     . GLU D 1 252 ? 69.727  8.259   91.230  1.000 45.091  0 252 GLU DDD C     1 ? 4 
ATOM   13105 O O     . GLU D 1 252 ? 70.354  7.242   91.614  1.000 43.827  0 252 GLU DDD O     1 ? 4 
ATOM   13106 C CB    . GLU D 1 252 ? 67.758  9.275   92.555  1.000 50.919  0 252 GLU DDD CB    1 ? 4 
ATOM   13107 C CG    . GLU D 1 252 ? 67.171  7.942   92.995  1.000 55.702  0 252 GLU DDD CG    1 ? 4 
ATOM   13108 C CD    . GLU D 1 252 ? 65.636  7.926   92.921  1.000 61.748  0 252 GLU DDD CD    1 ? 4 
ATOM   13109 O OE1   . GLU D 1 252 ? 64.961  8.740   93.640  1.000 63.331  0 252 GLU DDD OE1   1 ? 4 
ATOM   13110 O OE2   . GLU D 1 252 ? 65.089  7.138   92.097  1.000 62.992  0 252 GLU DDD OE2   1 ? 4 
ATOM   13111 N N     . TYR D 1 253 ? 69.475  8.524   89.937  1.000 43.348  0 253 TYR DDD N     1 ? 4 
ATOM   13112 C CA    . TYR D 1 253 ? 69.823  7.581   88.846  1.000 39.409  0 253 TYR DDD CA    1 ? 4 
ATOM   13113 C C     . TYR D 1 253 ? 71.357  7.490   88.729  1.000 38.100  0 253 TYR DDD C     1 ? 4 
ATOM   13114 O O     . TYR D 1 253 ? 71.922  6.360   88.643  1.000 36.203  0 253 TYR DDD O     1 ? 4 
ATOM   13115 C CB    . TYR D 1 253 ? 69.122  7.985   87.541  1.000 39.730  0 253 TYR DDD CB    1 ? 4 
ATOM   13116 C CG    . TYR D 1 253 ? 69.369  7.025   86.404  1.000 39.609  0 253 TYR DDD CG    1 ? 4 
ATOM   13117 C CD1   . TYR D 1 253 ? 70.484  7.147   85.584  1.000 38.947  0 253 TYR DDD CD1   1 ? 4 
ATOM   13118 C CD2   . TYR D 1 253 ? 68.536  5.938   86.204  1.000 37.996  0 253 TYR DDD CD2   1 ? 4 
ATOM   13119 C CE1   . TYR D 1 253 ? 70.744  6.219   84.586  1.000 38.651  0 253 TYR DDD CE1   1 ? 4 
ATOM   13120 C CE2   . TYR D 1 253 ? 68.799  4.988   85.227  1.000 38.517  0 253 TYR DDD CE2   1 ? 4 
ATOM   13121 C CZ    . TYR D 1 253 ? 69.892  5.144   84.393  1.000 38.677  0 253 TYR DDD CZ    1 ? 4 
ATOM   13122 O OH    . TYR D 1 253 ? 70.146  4.227   83.407  1.000 38.408  0 253 TYR DDD OH    1 ? 4 
ATOM   13123 N N     . MET D 1 254 ? 72.044  8.631   88.736  1.000 36.700  0 254 MET DDD N     1 ? 4 
ATOM   13124 C CA    . MET D 1 254 ? 73.526  8.640   88.586  1.000 37.943  0 254 MET DDD CA    1 ? 4 
ATOM   13125 C C     . MET D 1 254 ? 74.202  7.839   89.713  1.000 39.453  0 254 MET DDD C     1 ? 4 
ATOM   13126 O O     . MET D 1 254 ? 75.188  7.109   89.433  1.000 38.848  0 254 MET DDD O     1 ? 4 
ATOM   13127 C CB    . MET D 1 254 ? 74.053  10.075  88.577  1.000 37.291  0 254 MET DDD CB    1 ? 4 
ATOM   13128 C CG    . MET D 1 254 ? 73.535  10.867  87.386  1.000 36.558  0 254 MET DDD CG    1 ? 4 
ATOM   13129 S SD    . MET D 1 254 ? 74.341  12.466  87.187  1.000 36.898  0 254 MET DDD SD    1 ? 4 
ATOM   13130 C CE    . MET D 1 254 ? 76.071  11.991  87.111  1.000 36.385  0 254 MET DDD CE    1 ? 4 
ATOM   13131 N N     . LYS D 1 255 ? 73.704  7.974   90.946  1.000 40.896  0 255 LYS DDD N     1 ? 4 
ATOM   13132 C CA    . LYS D 1 255 ? 74.177  7.204   92.125  1.000 43.817  0 255 LYS DDD CA    1 ? 4 
ATOM   13133 C C     . LYS D 1 255 ? 73.959  5.711   91.892  1.000 40.768  0 255 LYS DDD C     1 ? 4 
ATOM   13134 O O     . LYS D 1 255 ? 74.898  4.950   92.163  1.000 42.918  0 255 LYS DDD O     1 ? 4 
ATOM   13135 C CB    . LYS D 1 255 ? 73.432  7.598   93.409  1.000 50.634  0 255 LYS DDD CB    1 ? 4 
ATOM   13136 C CG    . LYS D 1 255 ? 74.076  8.694   94.252  1.000 54.652  0 255 LYS DDD CG    1 ? 4 
ATOM   13137 C CD    . LYS D 1 255 ? 73.158  9.118   95.394  1.000 61.953  0 255 LYS DDD CD    1 ? 4 
ATOM   13138 C CE    . LYS D 1 255 ? 73.637  10.317  96.193  1.000 65.952  0 255 LYS DDD CE    1 ? 4 
ATOM   13139 N NZ    . LYS D 1 255 ? 72.478  10.955  96.870  1.000 66.721  0 255 LYS DDD NZ    1 ? 4 
ATOM   13140 N N     . ALA D 1 256 ? 72.776  5.308   91.419  1.000 38.348  0 256 ALA DDD N     1 ? 4 
ATOM   13141 C CA    . ALA D 1 256 ? 72.396  3.889   91.210  1.000 37.175  0 256 ALA DDD CA    1 ? 4 
ATOM   13142 C C     . ALA D 1 256 ? 73.234  3.278   90.074  1.000 37.064  0 256 ALA DDD C     1 ? 4 
ATOM   13143 O O     . ALA D 1 256 ? 73.256  2.037   89.984  1.000 36.265  0 256 ALA DDD O     1 ? 4 
ATOM   13144 C CB    . ALA D 1 256 ? 70.921  3.765   90.941  1.000 36.402  0 256 ALA DDD CB    1 ? 4 
ATOM   13145 N N     . THR D 1 257 ? 73.890  4.089   89.237  1.000 36.004  0 257 THR DDD N     1 ? 4 
ATOM   13146 C CA    . THR D 1 257 ? 74.728  3.564   88.122  1.000 36.248  0 257 THR DDD CA    1 ? 4 
ATOM   13147 C C     . THR D 1 257 ? 76.221  3.744   88.395  1.000 35.916  0 257 THR DDD C     1 ? 4 
ATOM   13148 O O     . THR D 1 257 ? 76.979  3.424   87.482  1.000 35.624  0 257 THR DDD O     1 ? 4 
ATOM   13149 C CB    . THR D 1 257 ? 74.360  4.174   86.755  1.000 36.345  0 257 THR DDD CB    1 ? 4 
ATOM   13150 O OG1   . THR D 1 257 ? 74.442  5.608   86.793  1.000 35.729  0 257 THR DDD OG1   1 ? 4 
ATOM   13151 C CG2   . THR D 1 257 ? 72.984  3.711   86.308  1.000 36.321  0 257 THR DDD CG2   1 ? 4 
ATOM   13152 N N     . GLY D 1 258 ? 76.624  4.266   89.558  1.000 35.468  0 258 GLY DDD N     1 ? 4 
ATOM   13153 C CA    . GLY D 1 258 ? 78.016  4.181   90.049  1.000 34.473  0 258 GLY DDD CA    1 ? 4 
ATOM   13154 C C     . GLY D 1 258 ? 78.707  5.529   90.256  1.000 35.440  0 258 GLY DDD C     1 ? 4 
ATOM   13155 O O     . GLY D 1 258 ? 79.858  5.530   90.660  1.000 35.755  0 258 GLY DDD O     1 ? 4 
ATOM   13156 N N     . THR D 1 259 ? 78.066  6.664   90.009  1.000 38.290  0 259 THR DDD N     1 ? 4 
ATOM   13157 C CA    . THR D 1 259 ? 78.693  7.969   90.318  1.000 39.462  0 259 THR DDD CA    1 ? 4 
ATOM   13158 C C     . THR D 1 259 ? 78.605  8.212   91.840  1.000 40.805  0 259 THR DDD C     1 ? 4 
ATOM   13159 O O     . THR D 1 259 ? 77.531  8.021   92.427  1.000 41.260  0 259 THR DDD O     1 ? 4 
ATOM   13160 C CB    . THR D 1 259 ? 78.092  9.083   89.456  1.000 39.384  0 259 THR DDD CB    1 ? 4 
ATOM   13161 O OG1   . THR D 1 259 ? 78.204  8.684   88.088  1.000 38.898  0 259 THR DDD OG1   1 ? 4 
ATOM   13162 C CG2   . THR D 1 259 ? 78.793  10.407  89.650  1.000 38.975  0 259 THR DDD CG2   1 ? 4 
ATOM   13163 N N     . LYS D 1 260 ? 79.708  8.593   92.455  1.000 41.588  0 260 LYS DDD N     1 ? 4 
ATOM   13164 C CA    . LYS D 1 260 ? 79.760  8.886   93.906  1.000 45.891  0 260 LYS DDD CA    1 ? 4 
ATOM   13165 C C     . LYS D 1 260 ? 79.629  10.393  94.076  1.000 47.389  0 260 LYS DDD C     1 ? 4 
ATOM   13166 O O     . LYS D 1 260 ? 80.211  11.109  93.243  1.000 44.579  0 260 LYS DDD O     1 ? 4 
ATOM   13167 C CB    . LYS D 1 260 ? 81.045  8.344   94.542  1.000 45.769  0 260 LYS DDD CB    1 ? 4 
ATOM   13168 C CG    . LYS D 1 260 ? 81.059  6.829   94.709  1.000 46.859  0 260 LYS DDD CG    1 ? 4 
ATOM   13169 C CD    . LYS D 1 260 ? 82.437  6.230   94.839  1.000 48.229  0 260 LYS DDD CD    1 ? 4 
ATOM   13170 C CE    . LYS D 1 260 ? 83.303  6.359   93.599  1.000 48.525  0 260 LYS DDD CE    1 ? 4 
ATOM   13171 N NZ    . LYS D 1 260 ? 84.725  6.144   93.954  1.000 49.711  0 260 LYS DDD NZ    1 ? 4 
ATOM   13172 N N     . PHE D 1 261 ? 78.845  10.809  95.077  1.000 49.205  0 261 PHE DDD N     1 ? 4 
ATOM   13173 C CA    . PHE D 1 261 ? 78.569  12.223  95.431  1.000 52.045  0 261 PHE DDD CA    1 ? 4 
ATOM   13174 C C     . PHE D 1 261 ? 79.026  12.532  96.869  1.000 51.046  0 261 PHE DDD C     1 ? 4 
ATOM   13175 O O     . PHE D 1 261 ? 78.484  11.913  97.789  1.000 49.911  0 261 PHE DDD O     1 ? 4 
ATOM   13176 C CB    . PHE D 1 261 ? 77.073  12.499  95.289  1.000 54.642  0 261 PHE DDD CB    1 ? 4 
ATOM   13177 C CG    . PHE D 1 261 ? 76.609  12.558  93.861  1.000 55.675  0 261 PHE DDD CG    1 ? 4 
ATOM   13178 C CD1   . PHE D 1 261 ? 76.300  11.390  93.180  1.000 54.502  0 261 PHE DDD CD1   1 ? 4 
ATOM   13179 C CD2   . PHE D 1 261 ? 76.510  13.770  93.204  1.000 54.999  0 261 PHE DDD CD2   1 ? 4 
ATOM   13180 C CE1   . PHE D 1 261 ? 75.850  11.437  91.877  1.000 53.461  0 261 PHE DDD CE1   1 ? 4 
ATOM   13181 C CE2   . PHE D 1 261 ? 76.074  13.812  91.892  1.000 56.285  0 261 PHE DDD CE2   1 ? 4 
ATOM   13182 C CZ    . PHE D 1 261 ? 75.739  12.650  91.236  1.000 54.648  0 261 PHE DDD CZ    1 ? 4 
ATOM   13183 N N     . LEU D 1 262 ? 79.957  13.478  97.012  1.000 49.378  0 262 LEU DDD N     1 ? 4 
ATOM   13184 C CA    . LEU D 1 262 ? 80.353  14.164  98.274  1.000 49.355  0 262 LEU DDD CA    1 ? 4 
ATOM   13185 C C     . LEU D 1 262 ? 79.491  15.424  98.422  1.000 49.627  0 262 LEU DDD C     1 ? 4 
ATOM   13186 O O     . LEU D 1 262 ? 79.748  16.411  97.692  1.000 46.998  0 262 LEU DDD O     1 ? 4 
ATOM   13187 C CB    . LEU D 1 262 ? 81.841  14.530  98.228  1.000 45.977  0 262 LEU DDD CB    1 ? 4 
ATOM   13188 C CG    . LEU D 1 262 ? 82.764  13.430  97.731  1.000 45.127  0 262 LEU DDD CG    1 ? 4 
ATOM   13189 C CD1   . LEU D 1 262 ? 84.201  13.943  97.608  1.000 46.731  0 262 LEU DDD CD1   1 ? 4 
ATOM   13190 C CD2   . LEU D 1 262 ? 82.671  12.224  98.636  1.000 44.759  0 262 LEU DDD CD2   1 ? 4 
ATOM   13191 N N     . VAL D 1 263 ? 78.522  15.392  99.332  1.000 51.900  0 263 VAL DDD N     1 ? 4 
ATOM   13192 C CA    . VAL D 1 263 ? 77.524  16.489  99.524  1.000 54.734  0 263 VAL DDD CA    1 ? 4 
ATOM   13193 C C     . VAL D 1 263 ? 78.057  17.462  100.594 1.000 56.263  0 263 VAL DDD C     1 ? 4 
ATOM   13194 O O     . VAL D 1 263 ? 78.463  16.997  101.639 1.000 58.185  0 263 VAL DDD O     1 ? 4 
ATOM   13195 C CB    . VAL D 1 263 ? 76.148  15.891  99.889  1.000 54.517  0 263 VAL DDD CB    1 ? 4 
ATOM   13196 C CG1   . VAL D 1 263 ? 75.050  16.943  99.954  1.000 53.927  0 263 VAL DDD CG1   1 ? 4 
ATOM   13197 C CG2   . VAL D 1 263 ? 75.767  14.772  98.923  1.000 54.733  0 263 VAL DDD CG2   1 ? 4 
ATOM   13198 N N     . GLY D 1 264 ? 78.096  18.763  100.299 1.000 57.428  0 264 GLY DDD N     1 ? 4 
ATOM   13199 C CA    . GLY D 1 264 ? 78.508  19.832  101.228 1.000 59.124  0 264 GLY DDD CA    1 ? 4 
ATOM   13200 C C     . GLY D 1 264 ? 80.014  19.872  101.413 1.000 60.044  0 264 GLY DDD C     1 ? 4 
ATOM   13201 O O     . GLY D 1 264 ? 80.463  20.404  102.449 1.000 59.594  0 264 GLY DDD O     1 ? 4 
ATOM   13202 N N     . VAL D 1 265 ? 80.764  19.318  100.457 1.000 59.670  0 265 VAL DDD N     1 ? 4 
ATOM   13203 C CA    . VAL D 1 265 ? 82.242  19.132  100.537 1.000 60.694  0 265 VAL DDD CA    1 ? 4 
ATOM   13204 C C     . VAL D 1 265 ? 82.861  19.662  99.247  1.000 61.084  0 265 VAL DDD C     1 ? 4 
ATOM   13205 O O     . VAL D 1 265 ? 82.315  19.356  98.168  1.000 65.296  0 265 VAL DDD O     1 ? 4 
ATOM   13206 C CB    . VAL D 1 265 ? 82.594  17.652  100.758 1.000 60.916  0 265 VAL DDD CB    1 ? 4 
ATOM   13207 C CG1   . VAL D 1 265 ? 84.092  17.419  100.636 1.000 61.440  0 265 VAL DDD CG1   1 ? 4 
ATOM   13208 C CG2   . VAL D 1 265 ? 82.082  17.134  102.104 1.000 62.939  0 265 VAL DDD CG2   1 ? 4 
ATOM   13209 N N     . VAL D 1 266 ? 83.927  20.447  99.357  1.000 61.163  0 266 VAL DDD N     1 ? 4 
ATOM   13210 C CA    . VAL D 1 266 ? 84.703  20.962  98.192  1.000 61.720  0 266 VAL DDD CA    1 ? 4 
ATOM   13211 C C     . VAL D 1 266 ? 86.197  20.838  98.483  1.000 58.780  0 266 VAL DDD C     1 ? 4 
ATOM   13212 O O     . VAL D 1 266 ? 86.625  20.763  99.633  1.000 61.068  0 266 VAL DDD O     1 ? 4 
ATOM   13213 C CB    . VAL D 1 266 ? 84.313  22.415  97.865  1.000 66.827  0 266 VAL DDD CB    1 ? 4 
ATOM   13214 C CG1   . VAL D 1 266 ? 82.839  22.534  97.496  1.000 67.973  0 266 VAL DDD CG1   1 ? 4 
ATOM   13215 C CG2   . VAL D 1 266 ? 84.674  23.386  98.992  1.000 67.402  0 266 VAL DDD CG2   1 ? 4 
ATOM   13216 N N     . PRO D 1 267 ? 87.050  20.794  97.441  1.000 57.032  0 267 PRO DDD N     1 ? 4 
ATOM   13217 C CA    . PRO D 1 267 ? 88.497  20.810  97.644  1.000 56.314  0 267 PRO DDD CA    1 ? 4 
ATOM   13218 C C     . PRO D 1 267 ? 88.984  22.102  98.319  1.000 56.085  0 267 PRO DDD C     1 ? 4 
ATOM   13219 O O     . PRO D 1 267 ? 88.458  23.157  98.015  1.000 55.099  0 267 PRO DDD O     1 ? 4 
ATOM   13220 C CB    . PRO D 1 267 ? 89.094  20.728  96.242  1.000 54.710  0 267 PRO DDD CB    1 ? 4 
ATOM   13221 C CG    . PRO D 1 267 ? 87.961  20.212  95.379  1.000 55.898  0 267 PRO DDD CG    1 ? 4 
ATOM   13222 C CD    . PRO D 1 267 ? 86.683  20.722  96.017  1.000 55.223  0 267 PRO DDD CD    1 ? 4 
ATOM   13223 N N     . ILE D 1 268 ? 89.971  21.969  99.210  1.000 56.538  0 268 ILE DDD N     1 ? 4 
ATOM   13224 C CA    . ILE D 1 268 ? 90.701  23.111  99.840  1.000 57.920  0 268 ILE DDD CA    1 ? 4 
ATOM   13225 C C     . ILE D 1 268 ? 92.186  23.049  99.457  1.000 56.773  0 268 ILE DDD C     1 ? 4 
ATOM   13226 O O     . ILE D 1 268 ? 92.872  24.074  99.647  1.000 58.414  0 268 ILE DDD O     1 ? 4 
ATOM   13227 C CB    . ILE D 1 268 ? 90.486  23.139  101.370 1.000 59.277  0 268 ILE DDD CB    1 ? 4 
ATOM   13228 C CG1   . ILE D 1 268 ? 90.951  21.847  102.040 1.000 60.618  0 268 ILE DDD CG1   1 ? 4 
ATOM   13229 C CG2   . ILE D 1 268 ? 89.030  23.466  101.703 1.000 58.666  0 268 ILE DDD CG2   1 ? 4 
ATOM   13230 C CD1   . ILE D 1 268 ? 90.892  21.887  103.554 1.000 64.967  0 268 ILE DDD CD1   1 ? 4 
ATOM   13231 N N     . ASN D 1 269 ? 92.668  21.912  98.946  1.000 53.741  0 269 ASN DDD N     1 ? 4 
ATOM   13232 C CA    . ASN D 1 269 ? 94.082  21.782  98.513  1.000 55.048  0 269 ASN DDD CA    1 ? 4 
ATOM   13233 C C     . ASN D 1 269 ? 94.221  20.695  97.448  1.000 53.733  0 269 ASN DDD C     1 ? 4 
ATOM   13234 O O     . ASN D 1 269 ? 93.536  19.647  97.557  1.000 55.587  0 269 ASN DDD O     1 ? 4 
ATOM   13235 C CB    . ASN D 1 269 ? 95.030  21.488  99.684  1.000 56.936  0 269 ASN DDD CB    1 ? 4 
ATOM   13236 C CG    . ASN D 1 269 ? 96.496  21.598  99.302  1.000 55.064  0 269 ASN DDD CG    1 ? 4 
ATOM   13237 O OD1   . ASN D 1 269 ? 97.209  20.606  99.333  1.000 56.832  0 269 ASN DDD OD1   1 ? 4 
ATOM   13238 N ND2   . ASN D 1 269 ? 96.942  22.782  98.905  1.000 53.537  0 269 ASN DDD ND2   1 ? 4 
ATOM   13239 N N     . ILE D 1 270 ? 95.111  20.934  96.487  1.000 52.571  0 270 ILE DDD N     1 ? 4 
ATOM   13240 C CA    . ILE D 1 270 ? 95.363  20.024  95.331  1.000 55.213  0 270 ILE DDD CA    1 ? 4 
ATOM   13241 C C     . ILE D 1 270 ? 96.887  19.913  95.104  1.000 57.119  0 270 ILE DDD C     1 ? 4 
ATOM   13242 O O     . ILE D 1 270 ? 97.525  20.931  94.764  1.000 59.746  0 270 ILE DDD O     1 ? 4 
ATOM   13243 C CB    . ILE D 1 270 ? 94.553  20.508  94.103  1.000 52.041  0 270 ILE DDD CB    1 ? 4 
ATOM   13244 C CG1   . ILE D 1 270 ? 93.049  20.302  94.344  1.000 52.401  0 270 ILE DDD CG1   1 ? 4 
ATOM   13245 C CG2   . ILE D 1 270 ? 95.001  19.817  92.835  1.000 50.553  0 270 ILE DDD CG2   1 ? 4 
ATOM   13246 C CD1   . ILE D 1 270 ? 92.115  20.901  93.298  1.000 49.679  0 270 ILE DDD CD1   1 ? 4 
ATOM   13247 N N     . GLU D 1 271 ? 97.457  18.723  95.306  1.000 59.538  0 271 GLU DDD N     1 ? 4 
ATOM   13248 C CA    . GLU D 1 271 ? 98.916  18.460  95.218  1.000 63.182  0 271 GLU DDD CA    1 ? 4 
ATOM   13249 C C     . GLU D 1 271 ? 99.165  17.279  94.272  1.000 62.778  0 271 GLU DDD C     1 ? 4 
ATOM   13250 O O     . GLU D 1 271 ? 98.304  16.373  94.220  1.000 60.343  0 271 GLU DDD O     1 ? 4 
ATOM   13251 C CB    . GLU D 1 271 ? 99.463  18.060  96.585  1.000 67.411  0 271 GLU DDD CB    1 ? 4 
ATOM   13252 C CG    . GLU D 1 271 ? 99.526  19.135  97.655  1.000 74.363  0 271 GLU DDD CG    1 ? 4 
ATOM   13253 C CD    . GLU D 1 271 ? 99.730  18.598  99.080  1.000 79.136  0 271 GLU DDD CD    1 ? 4 
ATOM   13254 O OE1   . GLU D 1 271 ? 99.382  17.407  99.342  1.000 81.206  0 271 GLU DDD OE1   1 ? 4 
ATOM   13255 O OE2   . GLU D 1 271 ? 100.246 19.361  99.941  1.000 78.820  0 271 GLU DDD OE2   1 ? 4 
ATOM   13256 N N     . LYS D 1 272 ? 100.302 17.289  93.568  1.000 65.763  0 272 LYS DDD N     1 ? 4 
ATOM   13257 C CA    . LYS D 1 272 ? 100.817 16.126  92.794  1.000 69.276  0 272 LYS DDD CA    1 ? 4 
ATOM   13258 C C     . LYS D 1 272 ? 101.574 15.176  93.732  1.000 70.459  0 272 LYS DDD C     1 ? 4 
ATOM   13259 O O     . LYS D 1 272 ? 102.650 15.568  94.235  1.000 68.112  0 272 LYS DDD O     1 ? 4 
ATOM   13260 C CB    . LYS D 1 272 ? 101.736 16.595  91.666  1.000 71.558  0 272 LYS DDD CB    1 ? 4 
ATOM   13261 C CG    . LYS D 1 272 ? 101.860 15.604  90.519  1.000 75.614  0 272 LYS DDD CG    1 ? 4 
ATOM   13262 C CD    . LYS D 1 272 ? 100.611 15.520  89.639  1.000 78.622  0 272 LYS DDD CD    1 ? 4 
ATOM   13263 C CE    . LYS D 1 272 ? 100.918 15.255  88.169  1.000 79.835  0 272 LYS DDD CE    1 ? 4 
ATOM   13264 N NZ    . LYS D 1 272 ? 101.479 16.454  87.495  1.000 79.931  0 272 LYS DDD NZ    1 ? 4 
ATOM   13265 N N     . VAL D 1 273 ? 101.029 13.979  93.977  1.000 72.378  0 273 VAL DDD N     1 ? 4 
ATOM   13266 C CA    . VAL D 1 273 ? 101.741 12.864  94.675  1.000 77.041  0 273 VAL DDD CA    1 ? 4 
ATOM   13267 C C     . VAL D 1 273 ? 102.123 11.811  93.625  1.000 76.136  0 273 VAL DDD C     1 ? 4 
ATOM   13268 O O     . VAL D 1 273 ? 101.286 10.943  93.303  1.000 72.045  0 273 VAL DDD O     1 ? 4 
ATOM   13269 C CB    . VAL D 1 273 ? 100.913 12.284  95.839  1.000 79.965  0 273 VAL DDD CB    1 ? 4 
ATOM   13270 C CG1   . VAL D 1 273 ? 101.545 11.022  96.419  1.000 82.167  0 273 VAL DDD CG1   1 ? 4 
ATOM   13271 C CG2   . VAL D 1 273 ? 100.710 13.320  96.940  1.000 81.170  0 273 VAL DDD CG2   1 ? 4 
ATOM   13272 N N     . ASN D 1 274 ? 103.351 11.922  93.110  1.000 77.721  0 274 ASN DDD N     1 ? 4 
ATOM   13273 C CA    . ASN D 1 274 ? 103.886 11.119  91.980  1.000 77.837  0 274 ASN DDD CA    1 ? 4 
ATOM   13274 C C     . ASN D 1 274 ? 103.103 11.508  90.721  1.000 75.740  0 274 ASN DDD C     1 ? 4 
ATOM   13275 O O     . ASN D 1 274 ? 103.165 12.679  90.324  1.000 75.032  0 274 ASN DDD O     1 ? 4 
ATOM   13276 C CB    . ASN D 1 274 ? 103.882 9.616   92.309  1.000 78.156  0 274 ASN DDD CB    1 ? 4 
ATOM   13277 C CG    . ASN D 1 274 ? 104.820 9.260   93.448  1.000 79.699  0 274 ASN DDD CG    1 ? 4 
ATOM   13278 O OD1   . ASN D 1 274 ? 104.395 8.751   94.493  1.000 80.527  0 274 ASN DDD OD1   1 ? 4 
ATOM   13279 N ND2   . ASN D 1 274 ? 106.106 9.515   93.255  1.000 76.817  0 274 ASN DDD ND2   1 ? 4 
ATOM   13280 N N     . GLU D 1 275 ? 102.392 10.559  90.119  1.000 76.335  0 275 GLU DDD N     1 ? 4 
ATOM   13281 C CA    . GLU D 1 275 ? 101.643 10.768  88.850  1.000 79.004  0 275 GLU DDD CA    1 ? 4 
ATOM   13282 C C     . GLU D 1 275 ? 100.162 10.996  89.172  1.000 70.754  0 275 GLU DDD C     1 ? 4 
ATOM   13283 O O     . GLU D 1 275 ? 99.440  11.372  88.245  1.000 68.453  0 275 GLU DDD O     1 ? 4 
ATOM   13284 C CB    . GLU D 1 275 ? 101.855 9.602   87.877  1.000 84.546  0 275 GLU DDD CB    1 ? 4 
ATOM   13285 C CG    . GLU D 1 275 ? 101.311 8.266   88.379  1.000 90.856  0 275 GLU DDD CG    1 ? 4 
ATOM   13286 C CD    . GLU D 1 275 ? 102.243 7.437   89.254  1.000 93.653  0 275 GLU DDD CD    1 ? 4 
ATOM   13287 O OE1   . GLU D 1 275 ? 103.445 7.803   89.384  1.000 95.189  0 275 GLU DDD OE1   1 ? 4 
ATOM   13288 O OE2   . GLU D 1 275 ? 101.763 6.431   89.825  1.000 94.140  0 275 GLU DDD OE2   1 ? 4 
ATOM   13289 N N     . ASN D 1 276 ? 99.737  10.790  90.426  1.000 64.078  0 276 ASN DDD N     1 ? 4 
ATOM   13290 C CA    . ASN D 1 276 ? 98.330  10.978  90.870  1.000 63.759  0 276 ASN DDD CA    1 ? 4 
ATOM   13291 C C     . ASN D 1 276 ? 98.173  12.370  91.486  1.000 61.585  0 276 ASN DDD C     1 ? 4 
ATOM   13292 O O     . ASN D 1 276 ? 99.200  13.048  91.672  1.000 58.868  0 276 ASN DDD O     1 ? 4 
ATOM   13293 C CB    . ASN D 1 276 ? 97.889  9.879   91.840  1.000 65.459  0 276 ASN DDD CB    1 ? 4 
ATOM   13294 C CG    . ASN D 1 276 ? 97.626  8.543   91.160  1.000 64.829  0 276 ASN DDD CG    1 ? 4 
ATOM   13295 O OD1   . ASN D 1 276 ? 97.251  8.470   89.995  1.000 66.191  0 276 ASN DDD OD1   1 ? 4 
ATOM   13296 N ND2   . ASN D 1 276 ? 97.800  7.456   91.888  1.000 62.430  0 276 ASN DDD ND2   1 ? 4 
ATOM   13297 N N     . ILE D 1 277 ? 96.933  12.792  91.737  1.000 59.234  0 277 ILE DDD N     1 ? 4 
ATOM   13298 C CA    . ILE D 1 277 ? 96.591  14.097  92.379  1.000 58.850  0 277 ILE DDD CA    1 ? 4 
ATOM   13299 C C     . ILE D 1 277 ? 95.879  13.805  93.704  1.000 58.707  0 277 ILE DDD C     1 ? 4 
ATOM   13300 O O     . ILE D 1 277 ? 94.729  13.285  93.685  1.000 55.477  0 277 ILE DDD O     1 ? 4 
ATOM   13301 C CB    . ILE D 1 277 ? 95.772  15.001  91.426  1.000 57.796  0 277 ILE DDD CB    1 ? 4 
ATOM   13302 C CG1   . ILE D 1 277 ? 96.611  15.360  90.192  1.000 58.628  0 277 ILE DDD CG1   1 ? 4 
ATOM   13303 C CG2   . ILE D 1 277 ? 95.271  16.247  92.128  1.000 56.168  0 277 ILE DDD CG2   1 ? 4 
ATOM   13304 C CD1   . ILE D 1 277 ? 95.806  15.756  88.974  1.000 56.930  0 277 ILE DDD CD1   1 ? 4 
ATOM   13305 N N     . LYS D 1 278 ? 96.561  14.116  94.814  1.000 57.773  0 278 LYS DDD N     1 ? 4 
ATOM   13306 C CA    . LYS D 1 278 ? 96.002  14.099  96.190  1.000 54.838  0 278 LYS DDD CA    1 ? 4 
ATOM   13307 C C     . LYS D 1 278 ? 95.145  15.349  96.370  1.000 51.231  0 278 LYS DDD C     1 ? 4 
ATOM   13308 O O     . LYS D 1 278 ? 95.679  16.465  96.269  1.000 46.733  0 278 LYS DDD O     1 ? 4 
ATOM   13309 C CB    . LYS D 1 278 ? 97.143  14.043  97.209  1.000 57.576  0 278 LYS DDD CB    1 ? 4 
ATOM   13310 C CG    . LYS D 1 278 ? 96.739  13.698  98.639  1.000 60.655  0 278 LYS DDD CG    1 ? 4 
ATOM   13311 C CD    . LYS D 1 278 ? 97.910  13.651  99.591  1.000 62.332  0 278 LYS DDD CD    1 ? 4 
ATOM   13312 C CE    . LYS D 1 278 ? 97.478  13.681  101.044 1.000 65.639  0 278 LYS DDD CE    1 ? 4 
ATOM   13313 N NZ    . LYS D 1 278 ? 98.635  13.793  101.970 1.000 67.880  0 278 LYS DDD NZ    1 ? 4 
ATOM   13314 N N     . VAL D 1 279 ? 93.853  15.159  96.608  1.000 50.474  0 279 VAL DDD N     1 ? 4 
ATOM   13315 C CA    . VAL D 1 279 ? 92.897  16.272  96.873  1.000 49.959  0 279 VAL DDD CA    1 ? 4 
ATOM   13316 C C     . VAL D 1 279 ? 92.537  16.258  98.359  1.000 49.522  0 279 VAL DDD C     1 ? 4 
ATOM   13317 O O     . VAL D 1 279 ? 92.140  15.184  98.884  1.000 49.914  0 279 VAL DDD O     1 ? 4 
ATOM   13318 C CB    . VAL D 1 279 ? 91.660  16.153  95.968  1.000 48.819  0 279 VAL DDD CB    1 ? 4 
ATOM   13319 C CG1   . VAL D 1 279 ? 90.542  17.114  96.377  1.000 49.364  0 279 VAL DDD CG1   1 ? 4 
ATOM   13320 C CG2   . VAL D 1 279 ? 92.061  16.364  94.511  1.000 48.266  0 279 VAL DDD CG2   1 ? 4 
ATOM   13321 N N     . SER D 1 280 ? 92.698  17.393  99.026  1.000 48.957  0 280 SER DDD N     1 ? 4 
ATOM   13322 C CA    . SER D 1 280 ? 92.301  17.551  100.445 1.000 50.662  0 280 SER DDD CA    1 ? 4 
ATOM   13323 C C     . SER D 1 280 ? 90.983  18.321  100.469 1.000 49.996  0 280 SER DDD C     1 ? 4 
ATOM   13324 O O     . SER D 1 280 ? 90.900  19.381  99.813  1.000 49.707  0 280 SER DDD O     1 ? 4 
ATOM   13325 C CB    . SER D 1 280 ? 93.404  18.195  101.261 1.000 50.522  0 280 SER DDD CB    1 ? 4 
ATOM   13326 O OG    . SER D 1 280 ? 94.498  17.290  101.424 1.000 47.780  0 280 SER DDD OG    1 ? 4 
ATOM   13327 N N     . PHE D 1 281 ? 89.973  17.751  101.123 1.000 51.661  0 281 PHE DDD N     1 ? 4 
ATOM   13328 C CA    . PHE D 1 281 ? 88.580  18.266  101.102 1.000 55.043  0 281 PHE DDD CA    1 ? 4 
ATOM   13329 C C     . PHE D 1 281 ? 88.267  19.065  102.369 1.000 56.805  0 281 PHE DDD C     1 ? 4 
ATOM   13330 O O     . PHE D 1 281 ? 88.910  18.845  103.394 1.000 57.877  0 281 PHE DDD O     1 ? 4 
ATOM   13331 C CB    . PHE D 1 281 ? 87.603  17.104  100.940 1.000 56.474  0 281 PHE DDD CB    1 ? 4 
ATOM   13332 C CG    . PHE D 1 281 ? 87.586  16.497  99.561  1.000 55.633  0 281 PHE DDD CG    1 ? 4 
ATOM   13333 C CD1   . PHE D 1 281 ? 86.903  17.119  98.526  1.000 54.601  0 281 PHE DDD CD1   1 ? 4 
ATOM   13334 C CD2   . PHE D 1 281 ? 88.251  15.308  99.306  1.000 54.622  0 281 PHE DDD CD2   1 ? 4 
ATOM   13335 C CE1   . PHE D 1 281 ? 86.872  16.549  97.264  1.000 54.405  0 281 PHE DDD CE1   1 ? 4 
ATOM   13336 C CE2   . PHE D 1 281 ? 88.211  14.741  98.046  1.000 56.024  0 281 PHE DDD CE2   1 ? 4 
ATOM   13337 C CZ    . PHE D 1 281 ? 87.519  15.359  97.025  1.000 54.434  0 281 PHE DDD CZ    1 ? 4 
ATOM   13338 N N     . SER D 1 282 ? 87.279  19.954  102.264 1.000 58.373  0 282 SER DDD N     1 ? 4 
ATOM   13339 C CA    . SER D 1 282 ? 86.835  20.925  103.297 1.000 60.802  0 282 SER DDD CA    1 ? 4 
ATOM   13340 C C     . SER D 1 282 ? 86.375  20.226  104.585 1.000 63.785  0 282 SER DDD C     1 ? 4 
ATOM   13341 O O     . SER D 1 282 ? 86.312  20.907  105.613 1.000 67.791  0 282 SER DDD O     1 ? 4 
ATOM   13342 C CB    . SER D 1 282 ? 85.742  21.803  102.753 1.000 60.230  0 282 SER DDD CB    1 ? 4 
ATOM   13343 O OG    . SER D 1 282 ? 84.534  21.063  102.596 1.000 60.189  0 282 SER DDD OG    1 ? 4 
ATOM   13344 N N     . ASP D 1 283 ? 86.039  18.932  104.534 1.000 64.514  0 283 ASP DDD N     1 ? 4 
ATOM   13345 C CA    . ASP D 1 283 ? 85.614  18.137  105.721 1.000 64.050  0 283 ASP DDD CA    1 ? 4 
ATOM   13346 C C     . ASP D 1 283 ? 86.835  17.415  106.344 1.000 63.812  0 283 ASP DDD C     1 ? 4 
ATOM   13347 O O     . ASP D 1 283 ? 86.623  16.561  107.208 1.000 62.568  0 283 ASP DDD O     1 ? 4 
ATOM   13348 C CB    . ASP D 1 283 ? 84.460  17.191  105.347 1.000 62.360  0 283 ASP DDD CB    1 ? 4 
ATOM   13349 C CG    . ASP D 1 283 ? 84.837  15.996  104.473 1.000 60.860  0 283 ASP DDD CG    1 ? 4 
ATOM   13350 O OD1   . ASP D 1 283 ? 85.942  16.028  103.865 1.000 56.997  0 283 ASP DDD OD1   1 ? 4 
ATOM   13351 O OD2   . ASP D 1 283 ? 84.014  15.031  104.412 1.000 59.787  0 283 ASP DDD OD2   1 ? 4 
ATOM   13352 N N     . GLY D 1 284 ? 88.062  17.737  105.922 1.000 63.194  0 284 GLY DDD N     1 ? 4 
ATOM   13353 C CA    . GLY D 1 284 ? 89.307  17.101  106.397 1.000 64.849  0 284 GLY DDD CA    1 ? 4 
ATOM   13354 C C     . GLY D 1 284 ? 89.580  15.732  105.788 1.000 64.621  0 284 GLY DDD C     1 ? 4 
ATOM   13355 O O     . GLY D 1 284 ? 90.594  15.133  106.184 1.000 68.202  0 284 GLY DDD O     1 ? 4 
ATOM   13356 N N     . SER D 1 285 ? 88.753  15.241  104.859 1.000 62.710  0 285 SER DDD N     1 ? 4 
ATOM   13357 C CA    . SER D 1 285 ? 88.992  13.943  104.173 1.000 62.259  0 285 SER DDD CA    1 ? 4 
ATOM   13358 C C     . SER D 1 285 ? 89.971  14.150  103.004 1.000 61.144  0 285 SER DDD C     1 ? 4 
ATOM   13359 O O     . SER D 1 285 ? 90.128  15.303  102.521 1.000 59.841  0 285 SER DDD O     1 ? 4 
ATOM   13360 C CB    . SER D 1 285 ? 87.703  13.290  103.726 1.000 60.954  0 285 SER DDD CB    1 ? 4 
ATOM   13361 O OG    . SER D 1 285 ? 87.144  13.976  102.606 1.000 57.420  0 285 SER DDD OG    1 ? 4 
ATOM   13362 N N     . VAL D 1 286 ? 90.645  13.073  102.609 1.000 62.373  0 286 VAL DDD N     1 ? 4 
ATOM   13363 C CA    . VAL D 1 286 ? 91.718  13.073  101.570 1.000 61.564  0 286 VAL DDD CA    1 ? 4 
ATOM   13364 C C     . VAL D 1 286 ? 91.407  11.939  100.582 1.000 60.930  0 286 VAL DDD C     1 ? 4 
ATOM   13365 O O     . VAL D 1 286 ? 90.814  10.929  101.016 1.000 59.995  0 286 VAL DDD O     1 ? 4 
ATOM   13366 C CB    . VAL D 1 286 ? 93.108  12.936  102.227 1.000 59.578  0 286 VAL DDD CB    1 ? 4 
ATOM   13367 C CG1   . VAL D 1 286 ? 94.209  12.649  101.219 1.000 58.984  0 286 VAL DDD CG1   1 ? 4 
ATOM   13368 C CG2   . VAL D 1 286 ? 93.472  14.161  103.054 1.000 60.106  0 286 VAL DDD CG2   1 ? 4 
ATOM   13369 N N     . GLU D 1 287 ? 91.727  12.119  99.293  1.000 59.826  0 287 GLU DDD N     1 ? 4 
ATOM   13370 C CA    . GLU D 1 287 ? 91.543  11.058  98.266  1.000 58.585  0 287 GLU DDD CA    1 ? 4 
ATOM   13371 C C     . GLU D 1 287 ? 92.429  11.362  97.052  1.000 55.584  0 287 GLU DDD C     1 ? 4 
ATOM   13372 O O     . GLU D 1 287 ? 92.591  12.548  96.702  1.000 56.551  0 287 GLU DDD O     1 ? 4 
ATOM   13373 C CB    . GLU D 1 287 ? 90.067  10.930  97.878  1.000 59.675  0 287 GLU DDD CB    1 ? 4 
ATOM   13374 C CG    . GLU D 1 287 ? 89.709  9.584   97.275  1.000 60.820  0 287 GLU DDD CG    1 ? 4 
ATOM   13375 C CD    . GLU D 1 287 ? 88.221  9.375   97.013  1.000 61.807  0 287 GLU DDD CD    1 ? 4 
ATOM   13376 O OE1   . GLU D 1 287 ? 87.413  10.173  97.522  1.000 62.838  0 287 GLU DDD OE1   1 ? 4 
ATOM   13377 O OE2   . GLU D 1 287 ? 87.862  8.386   96.349  1.000 61.974  0 287 GLU DDD OE2   1 ? 4 
ATOM   13378 N N     . GLU D 1 288 ? 92.974  10.309  96.448  1.000 53.003  0 288 GLU DDD N     1 ? 4 
ATOM   13379 C CA    . GLU D 1 288 ? 93.820  10.368  95.235  1.000 52.595  0 288 GLU DDD CA    1 ? 4 
ATOM   13380 C C     . GLU D 1 288 ? 92.935  10.203  93.992  1.000 49.750  0 288 GLU DDD C     1 ? 4 
ATOM   13381 O O     . GLU D 1 288 ? 92.000  9.381   94.025  1.000 46.939  0 288 GLU DDD O     1 ? 4 
ATOM   13382 C CB    . GLU D 1 288 ? 94.864  9.256   95.323  1.000 54.181  0 288 GLU DDD CB    1 ? 4 
ATOM   13383 C CG    . GLU D 1 288 ? 95.999  9.534   96.287  1.000 56.360  0 288 GLU DDD CG    1 ? 4 
ATOM   13384 C CD    . GLU D 1 288 ? 97.297  8.794   95.934  1.000 58.174  0 288 GLU DDD CD    1 ? 4 
ATOM   13385 O OE1   . GLU D 1 288 ? 97.425  8.307   94.777  1.000 57.102  0 288 GLU DDD OE1   1 ? 4 
ATOM   13386 O OE2   . GLU D 1 288 ? 98.183  8.685   96.804  1.000 57.600  0 288 GLU DDD OE2   1 ? 4 
ATOM   13387 N N     . PHE D 1 289 ? 93.205  10.998  92.958  1.000 48.632  0 289 PHE DDD N     1 ? 4 
ATOM   13388 C CA    . PHE D 1 289 ? 92.572  10.881  91.620  1.000 48.034  0 289 PHE DDD CA    1 ? 4 
ATOM   13389 C C     . PHE D 1 289 ? 93.661  10.995  90.553  1.000 46.213  0 289 PHE DDD C     1 ? 4 
ATOM   13390 O O     . PHE D 1 289 ? 94.687  11.602  90.808  1.000 43.405  0 289 PHE DDD O     1 ? 4 
ATOM   13391 C CB    . PHE D 1 289 ? 91.496  11.952  91.422  1.000 48.043  0 289 PHE DDD CB    1 ? 4 
ATOM   13392 C CG    . PHE D 1 289 ? 90.464  12.030  92.520  1.000 49.382  0 289 PHE DDD CG    1 ? 4 
ATOM   13393 C CD1   . PHE D 1 289 ? 90.695  12.781  93.665  1.000 49.964  0 289 PHE DDD CD1   1 ? 4 
ATOM   13394 C CD2   . PHE D 1 289 ? 89.263  11.341  92.409  1.000 48.549  0 289 PHE DDD CD2   1 ? 4 
ATOM   13395 C CE1   . PHE D 1 289 ? 89.741  12.845  94.673  1.000 51.340  0 289 PHE DDD CE1   1 ? 4 
ATOM   13396 C CE2   . PHE D 1 289 ? 88.300  11.411  93.407  1.000 48.463  0 289 PHE DDD CE2   1 ? 4 
ATOM   13397 C CZ    . PHE D 1 289 ? 88.540  12.171  94.538  1.000 50.054  0 289 PHE DDD CZ    1 ? 4 
ATOM   13398 N N     . GLU D 1 290 ? 93.402  10.447  89.371  1.000 48.019  0 290 GLU DDD N     1 ? 4 
ATOM   13399 C CA    . GLU D 1 290 ? 94.269  10.619  88.182  1.000 47.213  0 290 GLU DDD CA    1 ? 4 
ATOM   13400 C C     . GLU D 1 290 ? 93.960  11.969  87.510  1.000 45.039  0 290 GLU DDD C     1 ? 4 
ATOM   13401 O O     . GLU D 1 290 ? 94.894  12.621  87.004  1.000 44.845  0 290 GLU DDD O     1 ? 4 
ATOM   13402 C CB    . GLU D 1 290 ? 94.059  9.433   87.257  1.000 48.426  0 290 GLU DDD CB    1 ? 4 
ATOM   13403 C CG    . GLU D 1 290 ? 95.106  9.387   86.184  1.000 52.784  0 290 GLU DDD CG    1 ? 4 
ATOM   13404 C CD    . GLU D 1 290 ? 95.118  8.139   85.328  1.000 56.060  0 290 GLU DDD CD    1 ? 4 
ATOM   13405 O OE1   . GLU D 1 290 ? 95.459  8.276   84.141  1.000 57.543  0 290 GLU DDD OE1   1 ? 4 
ATOM   13406 O OE2   . GLU D 1 290 ? 94.781  7.050   85.854  1.000 58.149  0 290 GLU DDD OE2   1 ? 4 
ATOM   13407 N N     . THR D 1 291 ? 92.693  12.390  87.532  1.000 41.671  0 291 THR DDD N     1 ? 4 
ATOM   13408 C CA    . THR D 1 291 ? 92.209  13.614  86.850  1.000 40.435  0 291 THR DDD CA    1 ? 4 
ATOM   13409 C C     . THR D 1 291 ? 91.290  14.394  87.797  1.000 40.254  0 291 THR DDD C     1 ? 4 
ATOM   13410 O O     . THR D 1 291 ? 90.414  13.782  88.435  1.000 39.026  0 291 THR DDD O     1 ? 4 
ATOM   13411 C CB    . THR D 1 291 ? 91.472  13.255  85.550  1.000 38.789  0 291 THR DDD CB    1 ? 4 
ATOM   13412 O OG1   . THR D 1 291 ? 92.312  12.475  84.704  1.000 38.791  0 291 THR DDD OG1   1 ? 4 
ATOM   13413 C CG2   . THR D 1 291 ? 91.013  14.472  84.787  1.000 37.781  0 291 THR DDD CG2   1 ? 4 
ATOM   13414 N N     . VAL D 1 292 ? 91.465  15.708  87.839  1.000 39.326  0 292 VAL DDD N     1 ? 4 
ATOM   13415 C CA    . VAL D 1 292 ? 90.543  16.621  88.554  1.000 39.888  0 292 VAL DDD CA    1 ? 4 
ATOM   13416 C C     . VAL D 1 292 ? 90.054  17.671  87.567  1.000 38.239  0 292 VAL DDD C     1 ? 4 
ATOM   13417 O O     . VAL D 1 292 ? 90.890  18.356  86.967  1.000 35.157  0 292 VAL DDD O     1 ? 4 
ATOM   13418 C CB    . VAL D 1 292 ? 91.196  17.268  89.788  1.000 42.276  0 292 VAL DDD CB    1 ? 4 
ATOM   13419 C CG1   . VAL D 1 292 ? 90.265  18.273  90.461  1.000 43.097  0 292 VAL DDD CG1   1 ? 4 
ATOM   13420 C CG2   . VAL D 1 292 ? 91.649  16.227  90.797  1.000 43.989  0 292 VAL DDD CG2   1 ? 4 
ATOM   13421 N N     . LEU D 1 293 ? 88.728  17.781  87.444  1.000 39.660  0 293 LEU DDD N     1 ? 4 
ATOM   13422 C CA    . LEU D 1 293 ? 88.046  18.656  86.467  1.000 40.194  0 293 LEU DDD CA    1 ? 4 
ATOM   13423 C C     . LEU D 1 293 ? 87.167  19.628  87.231  1.000 41.031  0 293 LEU DDD C     1 ? 4 
ATOM   13424 O O     . LEU D 1 293 ? 86.278  19.159  87.940  1.000 41.048  0 293 LEU DDD O     1 ? 4 
ATOM   13425 C CB    . LEU D 1 293 ? 87.209  17.806  85.514  1.000 42.844  0 293 LEU DDD CB    1 ? 4 
ATOM   13426 C CG    . LEU D 1 293 ? 86.684  18.554  84.282  1.000 43.292  0 293 LEU DDD CG    1 ? 4 
ATOM   13427 C CD1   . LEU D 1 293 ? 86.514  17.613  83.084  1.000 42.403  0 293 LEU DDD CD1   1 ? 4 
ATOM   13428 C CD2   . LEU D 1 293 ? 85.394  19.289  84.592  1.000 43.174  0 293 LEU DDD CD2   1 ? 4 
ATOM   13429 N N     . TYR D 1 294 ? 87.418  20.927  87.079  1.000 42.528  0 294 TYR DDD N     1 ? 4 
ATOM   13430 C CA    . TYR D 1 294 ? 86.589  22.006  87.673  1.000 44.474  0 294 TYR DDD CA    1 ? 4 
ATOM   13431 C C     . TYR D 1 294 ? 85.471  22.388  86.700  1.000 44.164  0 294 TYR DDD C     1 ? 4 
ATOM   13432 O O     . TYR D 1 294 ? 85.788  22.914  85.604  1.000 41.662  0 294 TYR DDD O     1 ? 4 
ATOM   13433 C CB    . TYR D 1 294 ? 87.442  23.223  88.031  1.000 47.064  0 294 TYR DDD CB    1 ? 4 
ATOM   13434 C CG    . TYR D 1 294 ? 87.930  23.212  89.456  1.000 48.287  0 294 TYR DDD CG    1 ? 4 
ATOM   13435 C CD1   . TYR D 1 294 ? 87.102  23.596  90.500  1.000 50.920  0 294 TYR DDD CD1   1 ? 4 
ATOM   13436 C CD2   . TYR D 1 294 ? 89.192  22.760  89.768  1.000 47.469  0 294 TYR DDD CD2   1 ? 4 
ATOM   13437 C CE1   . TYR D 1 294 ? 87.519  23.541  91.824  1.000 50.601  0 294 TYR DDD CE1   1 ? 4 
ATOM   13438 C CE2   . TYR D 1 294 ? 89.635  22.702  91.077  1.000 48.483  0 294 TYR DDD CE2   1 ? 4 
ATOM   13439 C CZ    . TYR D 1 294 ? 88.802  23.099  92.109  1.000 50.914  0 294 TYR DDD CZ    1 ? 4 
ATOM   13440 O OH    . TYR D 1 294 ? 89.270  23.062  93.393  1.000 51.649  0 294 TYR DDD OH    1 ? 4 
ATOM   13441 N N     . ALA D 1 295 ? 84.214  22.144  87.090  1.000 44.818  0 295 ALA DDD N     1 ? 4 
ATOM   13442 C CA    . ALA D 1 295 ? 83.008  22.593  86.354  1.000 44.190  0 295 ALA DDD CA    1 ? 4 
ATOM   13443 C C     . ALA D 1 295 ? 82.166  23.462  87.289  1.000 44.304  0 295 ALA DDD C     1 ? 4 
ATOM   13444 O O     . ALA D 1 295 ? 80.957  23.189  87.473  1.000 42.214  0 295 ALA DDD O     1 ? 4 
ATOM   13445 C CB    . ALA D 1 295 ? 82.231  21.406  85.831  1.000 44.781  0 295 ALA DDD CB    1 ? 4 
ATOM   13446 N N     . THR D 1 296 ? 82.787  24.493  87.842  1.000 46.187  0 296 THR DDD N     1 ? 4 
ATOM   13447 C CA    . THR D 1 296 ? 82.200  25.288  88.951  1.000 47.672  0 296 THR DDD CA    1 ? 4 
ATOM   13448 C C     . THR D 1 296 ? 81.484  26.487  88.351  1.000 49.852  0 296 THR DDD C     1 ? 4 
ATOM   13449 O O     . THR D 1 296 ? 80.611  27.057  89.055  1.000 57.556  0 296 THR DDD O     1 ? 4 
ATOM   13450 C CB    . THR D 1 296 ? 83.263  25.661  89.994  1.000 47.421  0 296 THR DDD CB    1 ? 4 
ATOM   13451 O OG1   . THR D 1 296 ? 84.491  26.000  89.354  1.000 45.630  0 296 THR DDD OG1   1 ? 4 
ATOM   13452 C CG2   . THR D 1 296 ? 83.528  24.515  90.934  1.000 47.746  0 296 THR DDD CG2   1 ? 4 
ATOM   13453 N N     . GLY D 1 297 ? 81.845  26.837  87.116  1.000 46.330  0 297 GLY DDD N     1 ? 4 
ATOM   13454 C CA    . GLY D 1 297 ? 81.165  27.882  86.348  1.000 43.943  0 297 GLY DDD CA    1 ? 4 
ATOM   13455 C C     . GLY D 1 297 ? 82.069  28.413  85.265  1.000 42.974  0 297 GLY DDD C     1 ? 4 
ATOM   13456 O O     . GLY D 1 297 ? 83.132  27.802  85.007  1.000 42.153  0 297 GLY DDD O     1 ? 4 
ATOM   13457 N N     . ARG D 1 298 ? 81.651  29.531  84.678  1.000 41.883  0 298 ARG DDD N     1 ? 4 
ATOM   13458 C CA    . ARG D 1 298 ? 82.320  30.187  83.532  1.000 41.199  0 298 ARG DDD CA    1 ? 4 
ATOM   13459 C C     . ARG D 1 298 ? 82.264  31.702  83.761  1.000 43.525  0 298 ARG DDD C     1 ? 4 
ATOM   13460 O O     . ARG D 1 298 ? 81.168  32.207  84.096  1.000 40.867  0 298 ARG DDD O     1 ? 4 
ATOM   13461 C CB    . ARG D 1 298 ? 81.655  29.754  82.215  1.000 38.369  0 298 ARG DDD CB    1 ? 4 
ATOM   13462 C CG    . ARG D 1 298 ? 81.870  28.281  81.850  1.000 37.039  0 298 ARG DDD CG    1 ? 4 
ATOM   13463 C CD    . ARG D 1 298 ? 80.976  27.811  80.707  1.000 36.803  0 298 ARG DDD CD    1 ? 4 
ATOM   13464 N NE    . ARG D 1 298 ? 81.334  28.413  79.418  1.000 35.685  0 298 ARG DDD NE    1 ? 4 
ATOM   13465 C CZ    . ARG D 1 298 ? 82.347  28.022  78.641  1.000 33.446  0 298 ARG DDD CZ    1 ? 4 
ATOM   13466 N NH1   . ARG D 1 298 ? 83.089  26.975  78.964  1.000 33.094  0 298 ARG DDD NH1   1 ? 4 
ATOM   13467 N NH2   . ARG D 1 298 ? 82.599  28.668  77.525  1.000 32.818  0 298 ARG DDD NH2   1 ? 4 
ATOM   13468 N N     . ASN D 1 299 ? 83.397  32.386  83.561  1.000 45.928  0 299 ASN DDD N     1 ? 4 
ATOM   13469 C CA    . ASN D 1 299 ? 83.448  33.869  83.520  1.000 49.470  0 299 ASN DDD CA    1 ? 4 
ATOM   13470 C C     . ASN D 1 299 ? 83.466  34.344  82.077  1.000 49.682  0 299 ASN DDD C     1 ? 4 
ATOM   13471 O O     . ASN D 1 299 ? 84.111  33.731  81.230  1.000 53.914  0 299 ASN DDD O     1 ? 4 
ATOM   13472 C CB    . ASN D 1 299 ? 84.678  34.456  84.201  1.000 53.731  0 299 ASN DDD CB    1 ? 4 
ATOM   13473 C CG    . ASN D 1 299 ? 84.754  34.080  85.662  1.000 56.407  0 299 ASN DDD CG    1 ? 4 
ATOM   13474 O OD1   . ASN D 1 299 ? 85.783  33.582  86.112  1.000 62.214  0 299 ASN DDD OD1   1 ? 4 
ATOM   13475 N ND2   . ASN D 1 299 ? 83.660  34.249  86.387  1.000 59.121  0 299 ASN DDD ND2   1 ? 4 
ATOM   13476 N N     . PRO D 1 300 ? 82.750  35.449  81.768  1.000 47.253  0 300 PRO DDD N     1 ? 4 
ATOM   13477 C CA    . PRO D 1 300 ? 82.784  36.049  80.439  1.000 47.250  0 300 PRO DDD CA    1 ? 4 
ATOM   13478 C C     . PRO D 1 300 ? 84.189  36.543  80.088  1.000 50.493  0 300 PRO DDD C     1 ? 4 
ATOM   13479 O O     . PRO D 1 300 ? 84.813  37.219  80.898  1.000 49.354  0 300 PRO DDD O     1 ? 4 
ATOM   13480 C CB    . PRO D 1 300 ? 81.815  37.224  80.556  1.000 47.012  0 300 PRO DDD CB    1 ? 4 
ATOM   13481 C CG    . PRO D 1 300 ? 81.781  37.531  82.030  1.000 47.944  0 300 PRO DDD CG    1 ? 4 
ATOM   13482 C CD    . PRO D 1 300 ? 81.866  36.173  82.685  1.000 47.105  0 300 PRO DDD CD    1 ? 4 
ATOM   13483 N N     . ASP D 1 301 ? 84.656  36.198  78.893  1.000 53.940  0 301 ASP DDD N     1 ? 4 
ATOM   13484 C CA    . ASP D 1 301 ? 85.997  36.587  78.402  1.000 55.649  0 301 ASP DDD CA    1 ? 4 
ATOM   13485 C C     . ASP D 1 301 ? 85.894  38.004  77.835  1.000 59.338  0 301 ASP DDD C     1 ? 4 
ATOM   13486 O O     . ASP D 1 301 ? 85.791  38.144  76.610  1.000 60.110  0 301 ASP DDD O     1 ? 4 
ATOM   13487 C CB    . ASP D 1 301 ? 86.519  35.563  77.391  1.000 54.465  0 301 ASP DDD CB    1 ? 4 
ATOM   13488 C CG    . ASP D 1 301 ? 87.954  35.845  76.985  1.000 53.714  0 301 ASP DDD CG    1 ? 4 
ATOM   13489 O OD1   . ASP D 1 301 ? 88.735  36.367  77.853  1.000 54.451  0 301 ASP DDD OD1   1 ? 4 
ATOM   13490 O OD2   . ASP D 1 301 ? 88.272  35.588  75.820  1.000 49.533  0 301 ASP DDD OD2   1 ? 4 
ATOM   13491 N N     . VAL D 1 302 ? 85.921  39.008  78.714  1.000 63.365  0 302 VAL DDD N     1 ? 4 
ATOM   13492 C CA    . VAL D 1 302 ? 85.747  40.438  78.326  1.000 65.843  0 302 VAL DDD CA    1 ? 4 
ATOM   13493 C C     . VAL D 1 302 ? 86.937  41.288  78.794  1.000 63.959  0 302 VAL DDD C     1 ? 4 
ATOM   13494 O O     . VAL D 1 302 ? 86.965  42.489  78.452  1.000 67.570  0 302 VAL DDD O     1 ? 4 
ATOM   13495 C CB    . VAL D 1 302 ? 84.412  40.975  78.869  1.000 63.704  0 302 VAL DDD CB    1 ? 4 
ATOM   13496 C CG1   . VAL D 1 302 ? 83.254  40.288  78.168  1.000 62.632  0 302 VAL DDD CG1   1 ? 4 
ATOM   13497 C CG2   . VAL D 1 302 ? 84.319  40.858  80.390  1.000 62.844  0 302 VAL DDD CG2   1 ? 4 
ATOM   13498 N N     . LYS D 1 303 ? 87.885  40.701  79.512  1.000 61.492  0 303 LYS DDD N     1 ? 4 
ATOM   13499 C CA    . LYS D 1 303 ? 88.950  41.476  80.198  1.000 66.078  0 303 LYS DDD CA    1 ? 4 
ATOM   13500 C C     . LYS D 1 303 ? 89.856  42.120  79.136  1.000 66.440  0 303 LYS DDD C     1 ? 4 
ATOM   13501 O O     . LYS D 1 303 ? 90.268  43.269  79.332  1.000 66.658  0 303 LYS DDD O     1 ? 4 
ATOM   13502 C CB    . LYS D 1 303 ? 89.657  40.597  81.236  1.000 67.571  0 303 LYS DDD CB    1 ? 4 
ATOM   13503 C CG    . LYS D 1 303 ? 88.732  40.162  82.368  1.000 69.276  0 303 LYS DDD CG    1 ? 4 
ATOM   13504 C CD    . LYS D 1 303 ? 89.407  39.579  83.606  1.000 71.646  0 303 LYS DDD CD    1 ? 4 
ATOM   13505 C CE    . LYS D 1 303 ? 88.407  38.840  84.481  1.000 73.192  0 303 LYS DDD CE    1 ? 4 
ATOM   13506 N NZ    . LYS D 1 303 ? 88.838  38.719  85.901  1.000 73.281  0 303 LYS DDD NZ    1 ? 4 
ATOM   13507 N N     . GLY D 1 304 ? 90.099  41.442  78.016  1.000 66.350  0 304 GLY DDD N     1 ? 4 
ATOM   13508 C CA    . GLY D 1 304 ? 90.935  41.965  76.913  1.000 66.185  0 304 GLY DDD CA    1 ? 4 
ATOM   13509 C C     . GLY D 1 304 ? 90.244  43.037  76.076  1.000 63.976  0 304 GLY DDD C     1 ? 4 
ATOM   13510 O O     . GLY D 1 304 ? 90.920  43.634  75.225  1.000 60.807  0 304 GLY DDD O     1 ? 4 
ATOM   13511 N N     . LEU D 1 305 ? 88.958  43.302  76.306  1.000 65.855  0 305 LEU DDD N     1 ? 4 
ATOM   13512 C CA    . LEU D 1 305 ? 88.123  44.098  75.360  1.000 66.015  0 305 LEU DDD CA    1 ? 4 
ATOM   13513 C C     . LEU D 1 305 ? 88.261  45.605  75.618  1.000 70.959  0 305 LEU DDD C     1 ? 4 
ATOM   13514 O O     . LEU D 1 305 ? 87.884  46.367  74.716  1.000 72.835  0 305 LEU DDD O     1 ? 4 
ATOM   13515 C CB    . LEU D 1 305 ? 86.659  43.671  75.484  1.000 64.333  0 305 LEU DDD CB    1 ? 4 
ATOM   13516 C CG    . LEU D 1 305 ? 86.328  42.318  74.867  1.000 66.084  0 305 LEU DDD CG    1 ? 4 
ATOM   13517 C CD1   . LEU D 1 305 ? 84.861  41.957  75.089  1.000 69.769  0 305 LEU DDD CD1   1 ? 4 
ATOM   13518 C CD2   . LEU D 1 305 ? 86.634  42.304  73.387  1.000 65.602  0 305 LEU DDD CD2   1 ? 4 
ATOM   13519 N N     . ASN D 1 306 ? 88.754  46.015  76.793  1.000 73.203  0 306 ASN DDD N     1 ? 4 
ATOM   13520 C CA    . ASN D 1 306 ? 88.942  47.440  77.159  1.000 73.316  0 306 ASN DDD CA    1 ? 4 
ATOM   13521 C C     . ASN D 1 306 ? 87.569  48.088  77.358  1.000 73.684  0 306 ASN DDD C     1 ? 4 
ATOM   13522 O O     . ASN D 1 306 ? 87.373  49.219  76.874  1.000 73.296  0 306 ASN DDD O     1 ? 4 
ATOM   13523 C CB    . ASN D 1 306 ? 89.765  48.160  76.087  1.000 75.974  0 306 ASN DDD CB    1 ? 4 
ATOM   13524 C CG    . ASN D 1 306 ? 90.387  49.449  76.566  1.000 74.866  0 306 ASN DDD CG    1 ? 4 
ATOM   13525 O OD1   . ASN D 1 306 ? 90.645  49.613  77.756  1.000 69.627  0 306 ASN DDD OD1   1 ? 4 
ATOM   13526 N ND2   . ASN D 1 306 ? 90.634  50.358  75.637  1.000 77.592  0 306 ASN DDD ND2   1 ? 4 
ATOM   13527 N N     . LEU D 1 307 ? 86.651  47.394  78.040  1.000 75.432  0 307 LEU DDD N     1 ? 4 
ATOM   13528 C CA    . LEU D 1 307 ? 85.232  47.824  78.213  1.000 76.528  0 307 LEU DDD CA    1 ? 4 
ATOM   13529 C C     . LEU D 1 307 ? 85.159  49.046  79.132  1.000 75.499  0 307 LEU DDD C     1 ? 4 
ATOM   13530 O O     . LEU D 1 307 ? 84.388  49.963  78.819  1.000 73.823  0 307 LEU DDD O     1 ? 4 
ATOM   13531 C CB    . LEU D 1 307 ? 84.396  46.687  78.815  1.000 76.892  0 307 LEU DDD CB    1 ? 4 
ATOM   13532 C CG    . LEU D 1 307 ? 84.249  45.417  77.982  1.000 76.347  0 307 LEU DDD CG    1 ? 4 
ATOM   13533 C CD1   . LEU D 1 307 ? 83.335  44.446  78.717  1.000 76.177  0 307 LEU DDD CD1   1 ? 4 
ATOM   13534 C CD2   . LEU D 1 307 ? 83.706  45.721  76.595  1.000 76.672  0 307 LEU DDD CD2   1 ? 4 
ATOM   13535 N N     . ASN D 1 308 ? 85.908  49.031  80.239  1.000 78.861  0 308 ASN DDD N     1 ? 4 
ATOM   13536 C CA    . ASN D 1 308 ? 85.877  50.082  81.294  1.000 79.644  0 308 ASN DDD CA    1 ? 4 
ATOM   13537 C C     . ASN D 1 308 ? 86.131  51.450  80.655  1.000 78.832  0 308 ASN DDD C     1 ? 4 
ATOM   13538 O O     . ASN D 1 308 ? 85.322  52.357  80.883  1.000 79.745  0 308 ASN DDD O     1 ? 4 
ATOM   13539 C CB    . ASN D 1 308 ? 86.904  49.816  82.398  1.000 81.427  0 308 ASN DDD CB    1 ? 4 
ATOM   13540 C CG    . ASN D 1 308 ? 86.664  50.655  83.638  1.000 84.353  0 308 ASN DDD CG    1 ? 4 
ATOM   13541 O OD1   . ASN D 1 308 ? 86.029  51.705  83.577  1.000 84.837  0 308 ASN DDD OD1   1 ? 4 
ATOM   13542 N ND2   . ASN D 1 308 ? 87.151  50.193  84.781  1.000 85.877  0 308 ASN DDD ND2   1 ? 4 
ATOM   13543 N N     . ALA D 1 309 ? 87.207  51.566  79.873  1.000 76.763  0 309 ALA DDD N     1 ? 4 
ATOM   13544 C CA    . ALA D 1 309 ? 87.682  52.820  79.249  1.000 76.797  0 309 ALA DDD CA    1 ? 4 
ATOM   13545 C C     . ALA D 1 309 ? 86.671  53.348  78.209  1.000 75.363  0 309 ALA DDD C     1 ? 4 
ATOM   13546 O O     . ALA D 1 309 ? 86.631  54.576  78.010  1.000 74.215  0 309 ALA DDD O     1 ? 4 
ATOM   13547 C CB    . ALA D 1 309 ? 89.057  52.580  78.663  1.000 74.640  0 309 ALA DDD CB    1 ? 4 
ATOM   13548 N N     . ILE D 1 310 ? 85.872  52.488  77.573  1.000 74.675  0 310 ILE DDD N     1 ? 4 
ATOM   13549 C CA    . ILE D 1 310 ? 84.930  52.895  76.482  1.000 75.461  0 310 ILE DDD CA    1 ? 4 
ATOM   13550 C C     . ILE D 1 310 ? 83.563  53.269  77.067  1.000 73.392  0 310 ILE DDD C     1 ? 4 
ATOM   13551 O O     . ILE D 1 310 ? 82.800  53.959  76.365  1.000 70.521  0 310 ILE DDD O     1 ? 4 
ATOM   13552 C CB    . ILE D 1 310 ? 84.816  51.784  75.419  1.000 77.730  0 310 ILE DDD CB    1 ? 4 
ATOM   13553 C CG1   . ILE D 1 310 ? 86.196  51.370  74.893  1.000 81.028  0 310 ILE DDD CG1   1 ? 4 
ATOM   13554 C CG2   . ILE D 1 310 ? 83.871  52.196  74.292  1.000 75.569  0 310 ILE DDD CG2   1 ? 4 
ATOM   13555 C CD1   . ILE D 1 310 ? 87.129  52.540  74.600  1.000 82.631  0 310 ILE DDD CD1   1 ? 4 
ATOM   13556 N N     . GLY D 1 311 ? 83.267  52.835  78.294  1.000 72.269  0 311 GLY DDD N     1 ? 4 
ATOM   13557 C CA    . GLY D 1 311 ? 81.985  53.081  78.981  1.000 72.429  0 311 GLY DDD CA    1 ? 4 
ATOM   13558 C C     . GLY D 1 311 ? 80.955  51.978  78.754  1.000 70.157  0 311 GLY DDD C     1 ? 4 
ATOM   13559 O O     . GLY D 1 311 ? 79.753  52.277  78.843  1.000 66.716  0 311 GLY DDD O     1 ? 4 
ATOM   13560 N N     . VAL D 1 312 ? 81.384  50.739  78.499  1.000 68.326  0 312 VAL DDD N     1 ? 4 
ATOM   13561 C CA    . VAL D 1 312 ? 80.451  49.576  78.401  1.000 67.812  0 312 VAL DDD CA    1 ? 4 
ATOM   13562 C C     . VAL D 1 312 ? 80.215  49.034  79.809  1.000 67.191  0 312 VAL DDD C     1 ? 4 
ATOM   13563 O O     . VAL D 1 312 ? 81.174  48.497  80.391  1.000 69.296  0 312 VAL DDD O     1 ? 4 
ATOM   13564 C CB    . VAL D 1 312 ? 80.973  48.465  77.471  1.000 67.196  0 312 VAL DDD CB    1 ? 4 
ATOM   13565 C CG1   . VAL D 1 312 ? 80.156  47.189  77.631  1.000 66.689  0 312 VAL DDD CG1   1 ? 4 
ATOM   13566 C CG2   . VAL D 1 312 ? 81.020  48.914  76.016  1.000 66.731  0 312 VAL DDD CG2   1 ? 4 
ATOM   13567 N N     . GLU D 1 313 ? 78.988  49.146  80.308  1.000 70.085  0 313 GLU DDD N     1 ? 4 
ATOM   13568 C CA    . GLU D 1 313 ? 78.641  48.816  81.714  1.000 74.938  0 313 GLU DDD CA    1 ? 4 
ATOM   13569 C C     . GLU D 1 313 ? 78.676  47.292  81.913  1.000 72.909  0 313 GLU DDD C     1 ? 4 
ATOM   13570 O O     . GLU D 1 313 ? 78.144  46.554  81.041  1.000 70.857  0 313 GLU DDD O     1 ? 4 
ATOM   13571 C CB    . GLU D 1 313 ? 77.254  49.366  82.068  1.000 80.219  0 313 GLU DDD CB    1 ? 4 
ATOM   13572 C CG    . GLU D 1 313 ? 77.172  50.881  82.181  1.000 85.789  0 313 GLU DDD CG    1 ? 4 
ATOM   13573 C CD    . GLU D 1 313 ? 75.883  51.390  82.823  1.000 88.284  0 313 GLU DDD CD    1 ? 4 
ATOM   13574 O OE1   . GLU D 1 313 ? 75.978  52.153  83.815  1.000 90.012  0 313 GLU DDD OE1   1 ? 4 
ATOM   13575 O OE2   . GLU D 1 313 ? 74.777  51.017  82.337  1.000 91.189  0 313 GLU DDD OE2   1 ? 4 
ATOM   13576 N N     . VAL D 1 314 ? 79.217  46.847  83.050  1.000 69.644  0 314 VAL DDD N     1 ? 4 
ATOM   13577 C CA    . VAL D 1 314 ? 79.262  45.406  83.432  1.000 70.226  0 314 VAL DDD CA    1 ? 4 
ATOM   13578 C C     . VAL D 1 314 ? 78.590  45.225  84.794  1.000 67.320  0 314 VAL DDD C     1 ? 4 
ATOM   13579 O O     . VAL D 1 314 ? 78.615  46.150  85.581  1.000 69.331  0 314 VAL DDD O     1 ? 4 
ATOM   13580 C CB    . VAL D 1 314 ? 80.711  44.866  83.411  1.000 74.350  0 314 VAL DDD CB    1 ? 4 
ATOM   13581 C CG1   . VAL D 1 314 ? 81.358  45.018  82.033  1.000 74.027  0 314 VAL DDD CG1   1 ? 4 
ATOM   13582 C CG2   . VAL D 1 314 ? 81.597  45.498  84.477  1.000 74.606  0 314 VAL DDD CG2   1 ? 4 
ATOM   13583 N N     . SER D 1 315 ? 77.995  44.059  85.038  1.000 69.243  0 315 SER DDD N     1 ? 4 
ATOM   13584 C CA    . SER D 1 315 ? 77.368  43.678  86.331  1.000 70.052  0 315 SER DDD CA    1 ? 4 
ATOM   13585 C C     . SER D 1 315 ? 78.455  43.253  87.323  1.000 66.952  0 315 SER DDD C     1 ? 4 
ATOM   13586 O O     . SER D 1 315 ? 79.645  43.264  86.954  1.000 63.073  0 315 SER DDD O     1 ? 4 
ATOM   13587 C CB    . SER D 1 315 ? 76.357  42.587  86.130  1.000 72.372  0 315 SER DDD CB    1 ? 4 
ATOM   13588 O OG    . SER D 1 315 ? 77.017  41.349  85.880  1.000 74.299  0 315 SER DDD OG    1 ? 4 
ATOM   13589 N N     . ASP D 1 316 ? 78.051  42.878  88.539  1.000 71.231  0 316 ASP DDD N     1 ? 4 
ATOM   13590 C CA    . ASP D 1 316 ? 78.959  42.399  89.618  1.000 73.394  0 316 ASP DDD CA    1 ? 4 
ATOM   13591 C C     . ASP D 1 316 ? 79.660  41.112  89.157  1.000 76.387  0 316 ASP DDD C     1 ? 4 
ATOM   13592 O O     . ASP D 1 316 ? 80.791  40.885  89.586  1.000 74.068  0 316 ASP DDD O     1 ? 4 
ATOM   13593 C CB    . ASP D 1 316 ? 78.202  42.213  90.940  1.000 74.247  0 316 ASP DDD CB    1 ? 4 
ATOM   13594 C CG    . ASP D 1 316 ? 77.696  43.517  91.559  1.000 77.676  0 316 ASP DDD CG    1 ? 4 
ATOM   13595 O OD1   . ASP D 1 316 ? 78.430  44.533  91.501  1.000 76.329  0 316 ASP DDD OD1   1 ? 4 
ATOM   13596 O OD2   . ASP D 1 316 ? 76.564  43.523  92.091  1.000 77.828  0 316 ASP DDD OD2   1 ? 4 
ATOM   13597 N N     . SER D 1 317 ? 79.022  40.314  88.291  1.000 80.087  0 317 SER DDD N     1 ? 4 
ATOM   13598 C CA    . SER D 1 317 ? 79.563  39.023  87.769  1.000 78.189  0 317 SER DDD CA    1 ? 4 
ATOM   13599 C C     . SER D 1 317 ? 80.560  39.248  86.618  1.000 75.786  0 317 SER DDD C     1 ? 4 
ATOM   13600 O O     . SER D 1 317 ? 81.191  38.252  86.193  1.000 74.734  0 317 SER DDD O     1 ? 4 
ATOM   13601 C CB    . SER D 1 317 ? 78.450  38.102  87.342  1.000 74.561  0 317 SER DDD CB    1 ? 4 
ATOM   13602 O OG    . SER D 1 317 ? 77.762  38.640  86.228  1.000 75.635  0 317 SER DDD OG    1 ? 4 
ATOM   13603 N N     . GLY D 1 318 ? 80.706  40.487  86.131  1.000 74.872  0 318 GLY DDD N     1 ? 4 
ATOM   13604 C CA    . GLY D 1 318 ? 81.565  40.821  84.974  1.000 72.039  0 318 GLY DDD CA    1 ? 4 
ATOM   13605 C C     . GLY D 1 318 ? 80.820  40.704  83.647  1.000 70.576  0 318 GLY DDD C     1 ? 4 
ATOM   13606 O O     . GLY D 1 318 ? 81.420  40.974  82.599  1.000 68.986  0 318 GLY DDD O     1 ? 4 
ATOM   13607 N N     . LYS D 1 319 ? 79.542  40.329  83.666  1.000 70.023  0 319 LYS DDD N     1 ? 4 
ATOM   13608 C CA    . LYS D 1 319 ? 78.734  40.206  82.429  1.000 71.978  0 319 LYS DDD CA    1 ? 4 
ATOM   13609 C C     . LYS D 1 319 ? 78.310  41.603  81.959  1.000 72.431  0 319 LYS DDD C     1 ? 4 
ATOM   13610 O O     . LYS D 1 319 ? 78.088  42.490  82.804  1.000 79.466  0 319 LYS DDD O     1 ? 4 
ATOM   13611 C CB    . LYS D 1 319 ? 77.545  39.271  82.666  1.000 72.991  0 319 LYS DDD CB    1 ? 4 
ATOM   13612 C CG    . LYS D 1 319 ? 77.884  37.787  82.647  1.000 72.718  0 319 LYS DDD CG    1 ? 4 
ATOM   13613 C CD    . LYS D 1 319 ? 76.660  36.905  82.422  1.000 70.845  0 319 LYS DDD CD    1 ? 4 
ATOM   13614 C CE    . LYS D 1 319 ? 76.972  35.425  82.408  1.000 66.921  0 319 LYS DDD CE    1 ? 4 
ATOM   13615 N NZ    . LYS D 1 319 ? 75.746  34.658  82.128  1.000 66.958  0 319 LYS DDD NZ    1 ? 4 
ATOM   13616 N N     . ILE D 1 320 ? 78.203  41.786  80.647  1.000 70.033  0 320 ILE DDD N     1 ? 4 
ATOM   13617 C CA    . ILE D 1 320 ? 77.751  43.058  80.019  1.000 67.872  0 320 ILE DDD CA    1 ? 4 
ATOM   13618 C C     . ILE D 1 320 ? 76.252  43.233  80.269  1.000 66.645  0 320 ILE DDD C     1 ? 4 
ATOM   13619 O O     . ILE D 1 320 ? 75.494  42.273  80.095  1.000 63.691  0 320 ILE DDD O     1 ? 4 
ATOM   13620 C CB    . ILE D 1 320 ? 78.076  43.059  78.521  1.000 66.808  0 320 ILE DDD CB    1 ? 4 
ATOM   13621 C CG1   . ILE D 1 320 ? 79.581  42.904  78.294  1.000 66.717  0 320 ILE DDD CG1   1 ? 4 
ATOM   13622 C CG2   . ILE D 1 320 ? 77.489  44.297  77.855  1.000 69.641  0 320 ILE DDD CG2   1 ? 4 
ATOM   13623 C CD1   . ILE D 1 320 ? 79.986  42.869  76.844  1.000 69.343  0 320 ILE DDD CD1   1 ? 4 
ATOM   13624 N N     . ILE D 1 321 ? 75.848  44.434  80.668  1.000 68.678  0 321 ILE DDD N     1 ? 4 
ATOM   13625 C CA    . ILE D 1 321 ? 74.416  44.804  80.840  1.000 69.396  0 321 ILE DDD CA    1 ? 4 
ATOM   13626 C C     . ILE D 1 321 ? 73.899  45.190  79.447  1.000 68.986  0 321 ILE DDD C     1 ? 4 
ATOM   13627 O O     . ILE D 1 321 ? 74.433  46.166  78.864  1.000 72.598  0 321 ILE DDD O     1 ? 4 
ATOM   13628 C CB    . ILE D 1 321 ? 74.261  45.895  81.922  1.000 69.336  0 321 ILE DDD CB    1 ? 4 
ATOM   13629 C CG1   . ILE D 1 321 ? 74.554  45.328  83.319  1.000 66.716  0 321 ILE DDD CG1   1 ? 4 
ATOM   13630 C CG2   . ILE D 1 321 ? 72.877  46.538  81.866  1.000 71.046  0 321 ILE DDD CG2   1 ? 4 
ATOM   13631 C CD1   . ILE D 1 321 ? 74.853  46.373  84.368  1.000 68.247  0 321 ILE DDD CD1   1 ? 4 
ATOM   13632 N N     . ALA D 1 322 ? 72.980  44.397  78.900  1.000 65.428  0 322 ALA DDD N     1 ? 4 
ATOM   13633 C CA    . ALA D 1 322 ? 72.410  44.603  77.544  1.000 68.097  0 322 ALA DDD CA    1 ? 4 
ATOM   13634 C C     . ALA D 1 322 ? 71.101  43.823  77.413  1.000 65.867  0 322 ALA DDD C     1 ? 4 
ATOM   13635 O O     . ALA D 1 322 ? 71.005  42.918  76.594  1.000 62.593  0 322 ALA DDD O     1 ? 4 
ATOM   13636 C CB    . ALA D 1 322 ? 73.403  44.191  76.470  1.000 68.709  0 322 ALA DDD CB    1 ? 4 
ATOM   13637 N N     . PRO D 1 323 ? 70.065  44.152  78.222  1.000 63.808  0 323 PRO DDD N     1 ? 4 
ATOM   13638 C CA    . PRO D 1 323 ? 68.831  43.374  78.251  1.000 62.042  0 323 PRO DDD CA    1 ? 4 
ATOM   13639 C C     . PRO D 1 323 ? 68.156  43.300  76.874  1.000 61.949  0 323 PRO DDD C     1 ? 4 
ATOM   13640 O O     . PRO D 1 323 ? 67.402  42.367  76.655  1.000 62.405  0 323 PRO DDD O     1 ? 4 
ATOM   13641 C CB    . PRO D 1 323 ? 67.943  44.095  79.286  1.000 63.954  0 323 PRO DDD CB    1 ? 4 
ATOM   13642 C CG    . PRO D 1 323 ? 68.555  45.473  79.457  1.000 64.238  0 323 PRO DDD CG    1 ? 4 
ATOM   13643 C CD    . PRO D 1 323 ? 70.027  45.290  79.151  1.000 63.247  0 323 PRO DDD CD    1 ? 4 
ATOM   13644 N N     . LYS D 1 324 ? 68.446  44.266  75.990  1.000 61.174  0 324 LYS DDD N     1 ? 4 
ATOM   13645 C CA    . LYS D 1 324 ? 67.909  44.338  74.605  1.000 60.244  0 324 LYS DDD CA    1 ? 4 
ATOM   13646 C C     . LYS D 1 324 ? 69.037  44.238  73.580  1.000 56.728  0 324 LYS DDD C     1 ? 4 
ATOM   13647 O O     . LYS D 1 324 ? 68.857  44.757  72.486  1.000 51.279  0 324 LYS DDD O     1 ? 4 
ATOM   13648 C CB    . LYS D 1 324 ? 67.141  45.655  74.434  1.000 64.816  0 324 LYS DDD CB    1 ? 4 
ATOM   13649 C CG    . LYS D 1 324 ? 65.826  45.714  75.203  1.000 67.789  0 324 LYS DDD CG    1 ? 4 
ATOM   13650 C CD    . LYS D 1 324 ? 64.770  44.753  74.646  1.000 68.573  0 324 LYS DDD CD    1 ? 4 
ATOM   13651 C CE    . LYS D 1 324 ? 63.874  44.124  75.700  1.000 69.004  0 324 LYS DDD CE    1 ? 4 
ATOM   13652 N NZ    . LYS D 1 324 ? 63.446  42.764  75.296  1.000 66.384  0 324 LYS DDD NZ    1 ? 4 
ATOM   13653 N N     . ASP D 1 325 ? 70.176  43.640  73.950  1.000 59.376  0 325 ASP DDD N     1 ? 4 
ATOM   13654 C CA    . ASP D 1 325 ? 71.379  43.470  73.090  1.000 59.863  0 325 ASP DDD CA    1 ? 4 
ATOM   13655 C C     . ASP D 1 325 ? 72.183  44.774  73.045  1.000 60.191  0 325 ASP DDD C     1 ? 4 
ATOM   13656 O O     . ASP D 1 325 ? 73.395  44.694  72.798  1.000 61.563  0 325 ASP DDD O     1 ? 4 
ATOM   13657 C CB    . ASP D 1 325 ? 71.020  42.943  71.692  1.000 61.196  0 325 ASP DDD CB    1 ? 4 
ATOM   13658 C CG    . ASP D 1 325 ? 70.125  41.700  71.678  1.000 62.316  0 325 ASP DDD CG    1 ? 4 
ATOM   13659 O OD1   . ASP D 1 325 ? 70.180  40.916  72.649  1.000 62.656  0 325 ASP DDD OD1   1 ? 4 
ATOM   13660 O OD2   . ASP D 1 325 ? 69.343  41.525  70.707  1.000 64.111  0 325 ASP DDD OD2   1 ? 4 
ATOM   13661 N N     . ALA D 1 326 ? 71.557  45.926  73.308  1.000 64.089  0 326 ALA DDD N     1 ? 4 
ATOM   13662 C CA    . ALA D 1 326 ? 72.192  47.263  73.304  1.000 66.070  0 326 ALA DDD CA    1 ? 4 
ATOM   13663 C C     . ALA D 1 326 ? 72.891  47.481  74.657  1.000 68.082  0 326 ALA DDD C     1 ? 4 
ATOM   13664 O O     . ALA D 1 326 ? 72.218  47.428  75.712  1.000 68.851  0 326 ALA DDD O     1 ? 4 
ATOM   13665 C CB    . ALA D 1 326 ? 71.161  48.331  72.997  1.000 65.708  0 326 ALA DDD CB    1 ? 4 
ATOM   13666 N N     . THR D 1 327 ? 74.207  47.708  74.627  1.000 67.673  0 327 THR DDD N     1 ? 4 
ATOM   13667 C CA    . THR D 1 327 ? 75.005  48.092  75.821  1.000 67.768  0 327 THR DDD CA    1 ? 4 
ATOM   13668 C C     . THR D 1 327 ? 74.709  49.556  76.179  1.000 67.423  0 327 THR DDD C     1 ? 4 
ATOM   13669 O O     . THR D 1 327 ? 73.915  50.218  75.494  1.000 64.354  0 327 THR DDD O     1 ? 4 
ATOM   13670 C CB    . THR D 1 327 ? 76.516  47.905  75.588  1.000 67.644  0 327 THR DDD CB    1 ? 4 
ATOM   13671 O OG1   . THR D 1 327 ? 76.983  48.923  74.697  1.000 62.498  0 327 THR DDD OG1   1 ? 4 
ATOM   13672 C CG2   . THR D 1 327 ? 76.866  46.529  75.051  1.000 65.095  0 327 THR DDD CG2   1 ? 4 
ATOM   13673 N N     . SER D 1 328 ? 75.364  50.048  77.224  1.000 69.003  0 328 SER DDD N     1 ? 4 
ATOM   13674 C CA    . SER D 1 328 ? 75.354  51.467  77.655  1.000 67.962  0 328 SER DDD CA    1 ? 4 
ATOM   13675 C C     . SER D 1 328 ? 75.950  52.376  76.568  1.000 68.134  0 328 SER DDD C     1 ? 4 
ATOM   13676 O O     . SER D 1 328 ? 75.697  53.583  76.631  1.000 69.777  0 328 SER DDD O     1 ? 4 
ATOM   13677 C CB    . SER D 1 328 ? 76.099  51.607  78.957  1.000 67.881  0 328 SER DDD CB    1 ? 4 
ATOM   13678 O OG    . SER D 1 328 ? 77.370  50.978  78.896  1.000 65.398  0 328 SER DDD OG    1 ? 4 
ATOM   13679 N N     . VAL D 1 329 ? 76.725  51.828  75.627  1.000 67.745  0 329 VAL DDD N     1 ? 4 
ATOM   13680 C CA    . VAL D 1 329 ? 77.305  52.554  74.456  1.000 68.833  0 329 VAL DDD CA    1 ? 4 
ATOM   13681 C C     . VAL D 1 329 ? 76.504  52.182  73.211  1.000 67.475  0 329 VAL DDD C     1 ? 4 
ATOM   13682 O O     . VAL D 1 329 ? 76.506  51.043  72.771  1.000 67.904  0 329 VAL DDD O     1 ? 4 
ATOM   13683 C CB    . VAL D 1 329 ? 78.815  52.261  74.304  1.000 69.169  0 329 VAL DDD CB    1 ? 4 
ATOM   13684 C CG1   . VAL D 1 329 ? 79.393  52.842  73.026  1.000 68.957  0 329 VAL DDD CG1   1 ? 4 
ATOM   13685 C CG2   . VAL D 1 329 ? 79.592  52.759  75.512  1.000 69.696  0 329 VAL DDD CG2   1 ? 4 
ATOM   13686 N N     . PRO D 1 330 ? 75.781  53.138  72.593  1.000 69.751  0 330 PRO DDD N     1 ? 4 
ATOM   13687 C CA    . PRO D 1 330 ? 74.714  52.777  71.658  1.000 69.623  0 330 PRO DDD CA    1 ? 4 
ATOM   13688 C C     . PRO D 1 330 ? 75.135  52.242  70.276  1.000 68.258  0 330 PRO DDD C     1 ? 4 
ATOM   13689 O O     . PRO D 1 330 ? 74.279  51.760  69.553  1.000 70.095  0 330 PRO DDD O     1 ? 4 
ATOM   13690 C CB    . PRO D 1 330 ? 73.920  54.082  71.526  1.000 71.840  0 330 PRO DDD CB    1 ? 4 
ATOM   13691 C CG    . PRO D 1 330 ? 74.906  55.214  71.878  1.000 71.561  0 330 PRO DDD CG    1 ? 4 
ATOM   13692 C CD    . PRO D 1 330 ? 75.941  54.590  72.787  1.000 70.643  0 330 PRO DDD CD    1 ? 4 
ATOM   13693 N N     . SER D 1 331 ? 76.422  52.327  69.942  1.000 65.592  0 331 SER DDD N     1 ? 4 
ATOM   13694 C CA    . SER D 1 331 ? 77.026  51.760  68.705  1.000 65.858  0 331 SER DDD CA    1 ? 4 
ATOM   13695 C C     . SER D 1 331 ? 77.517  50.331  68.976  1.000 64.638  0 331 SER DDD C     1 ? 4 
ATOM   13696 O O     . SER D 1 331 ? 77.957  49.671  68.038  1.000 61.094  0 331 SER DDD O     1 ? 4 
ATOM   13697 C CB    . SER D 1 331 ? 78.150  52.633  68.223  1.000 64.184  0 331 SER DDD CB    1 ? 4 
ATOM   13698 O OG    . SER D 1 331 ? 79.156  52.735  69.212  1.000 61.281  0 331 SER DDD OG    1 ? 4 
ATOM   13699 N N     . ILE D 1 332 ? 77.481  49.897  70.236  1.000 66.590  0 332 ILE DDD N     1 ? 4 
ATOM   13700 C CA    . ILE D 1 332 ? 78.059  48.600  70.670  1.000 66.487  0 332 ILE DDD CA    1 ? 4 
ATOM   13701 C C     . ILE D 1 332 ? 76.952  47.712  71.238  1.000 66.764  0 332 ILE DDD C     1 ? 4 
ATOM   13702 O O     . ILE D 1 332 ? 76.298  48.079  72.229  1.000 62.022  0 332 ILE DDD O     1 ? 4 
ATOM   13703 C CB    . ILE D 1 332 ? 79.208  48.805  71.668  1.000 68.458  0 332 ILE DDD CB    1 ? 4 
ATOM   13704 C CG1   . ILE D 1 332 ? 80.357  49.578  71.010  1.000 68.097  0 332 ILE DDD CG1   1 ? 4 
ATOM   13705 C CG2   . ILE D 1 332 ? 79.639  47.458  72.241  1.000 65.970  0 332 ILE DDD CG2   1 ? 4 
ATOM   13706 C CD1   . ILE D 1 332 ? 81.571  49.753  71.875  1.000 67.612  0 332 ILE DDD CD1   1 ? 4 
ATOM   13707 N N     . PHE D 1 333 ? 76.804  46.551  70.621  1.000 65.858  0 333 PHE DDD N     1 ? 4 
ATOM   13708 C CA    . PHE D 1 333 ? 75.793  45.528  70.960  1.000 64.440  0 333 PHE DDD CA    1 ? 4 
ATOM   13709 C C     . PHE D 1 333 ? 76.536  44.315  71.525  1.000 61.790  0 333 PHE DDD C     1 ? 4 
ATOM   13710 O O     . PHE D 1 333 ? 77.789  44.243  71.424  1.000 56.399  0 333 PHE DDD O     1 ? 4 
ATOM   13711 C CB    . PHE D 1 333 ? 74.945  45.243  69.723  1.000 66.004  0 333 PHE DDD CB    1 ? 4 
ATOM   13712 C CG    . PHE D 1 333 ? 74.154  46.446  69.269  1.000 66.829  0 333 PHE DDD CG    1 ? 4 
ATOM   13713 C CD1   . PHE D 1 333 ? 74.722  47.403  68.436  1.000 67.789  0 333 PHE DDD CD1   1 ? 4 
ATOM   13714 C CD2   . PHE D 1 333 ? 72.860  46.645  69.715  1.000 67.013  0 333 PHE DDD CD2   1 ? 4 
ATOM   13715 C CE1   . PHE D 1 333 ? 73.987  48.493  68.007  1.000 68.257  0 333 PHE DDD CE1   1 ? 4 
ATOM   13716 C CE2   . PHE D 1 333 ? 72.135  47.760  69.316  1.000 70.070  0 333 PHE DDD CE2   1 ? 4 
ATOM   13717 C CZ    . PHE D 1 333 ? 72.696  48.676  68.455  1.000 69.692  0 333 PHE DDD CZ    1 ? 4 
ATOM   13718 N N     . ALA D 1 334 ? 75.787  43.417  72.154  1.000 58.348  0 334 ALA DDD N     1 ? 4 
ATOM   13719 C CA    . ALA D 1 334 ? 76.326  42.183  72.752  1.000 55.000  0 334 ALA DDD CA    1 ? 4 
ATOM   13720 C C     . ALA D 1 334 ? 75.253  41.092  72.678  1.000 54.772  0 334 ALA DDD C     1 ? 4 
ATOM   13721 O O     . ALA D 1 334 ? 74.047  41.418  72.795  1.000 52.715  0 334 ALA DDD O     1 ? 4 
ATOM   13722 C CB    . ALA D 1 334 ? 76.768  42.468  74.159  1.000 51.334  0 334 ALA DDD CB    1 ? 4 
ATOM   13723 N N     . VAL D 1 335 ? 75.684  39.856  72.434  1.000 53.358  0 335 VAL DDD N     1 ? 4 
ATOM   13724 C CA    . VAL D 1 335 ? 74.823  38.639  72.491  1.000 50.668  0 335 VAL DDD CA    1 ? 4 
ATOM   13725 C C     . VAL D 1 335 ? 75.641  37.489  73.071  1.000 47.671  0 335 VAL DDD C     1 ? 4 
ATOM   13726 O O     . VAL D 1 335 ? 76.843  37.670  73.271  1.000 46.575  0 335 VAL DDD O     1 ? 4 
ATOM   13727 C CB    . VAL D 1 335 ? 74.262  38.265  71.115  1.000 50.147  0 335 VAL DDD CB    1 ? 4 
ATOM   13728 C CG1   . VAL D 1 335 ? 73.425  39.393  70.517  1.000 50.864  0 335 VAL DDD CG1   1 ? 4 
ATOM   13729 C CG2   . VAL D 1 335 ? 75.374  37.854  70.168  1.000 49.515  0 335 VAL DDD CG2   1 ? 4 
ATOM   13730 N N     . GLY D 1 336 ? 74.979  36.373  73.348  1.000 46.531  0 336 GLY DDD N     1 ? 4 
ATOM   13731 C CA    . GLY D 1 336 ? 75.603  35.138  73.852  1.000 46.749  0 336 GLY DDD CA    1 ? 4 
ATOM   13732 C C     . GLY D 1 336 ? 75.908  35.177  75.340  1.000 47.534  0 336 GLY DDD C     1 ? 4 
ATOM   13733 O O     . GLY D 1 336 ? 75.277  36.007  76.086  1.000 48.682  0 336 GLY DDD O     1 ? 4 
ATOM   13734 N N     . ASP D 1 337 ? 76.865  34.331  75.761  1.000 47.856  0 337 ASP DDD N     1 ? 4 
ATOM   13735 C CA    . ASP D 1 337 ? 77.102  33.969  77.190  1.000 48.763  0 337 ASP DDD CA    1 ? 4 
ATOM   13736 C C     . ASP D 1 337 ? 77.534  35.190  78.002  1.000 48.644  0 337 ASP DDD C     1 ? 4 
ATOM   13737 O O     . ASP D 1 337 ? 77.419  35.125  79.238  1.000 52.983  0 337 ASP DDD O     1 ? 4 
ATOM   13738 C CB    . ASP D 1 337 ? 78.165  32.873  77.352  1.000 47.536  0 337 ASP DDD CB    1 ? 4 
ATOM   13739 C CG    . ASP D 1 337 ? 77.711  31.478  76.963  1.000 48.142  0 337 ASP DDD CG    1 ? 4 
ATOM   13740 O OD1   . ASP D 1 337 ? 76.516  31.330  76.551  1.000 48.109  0 337 ASP DDD OD1   1 ? 4 
ATOM   13741 O OD2   . ASP D 1 337 ? 78.567  30.540  77.046  1.000 45.686  0 337 ASP DDD OD2   1 ? 4 
ATOM   13742 N N     . ILE D 1 338 ? 78.067  36.233  77.352  1.000 48.267  0 338 ILE DDD N     1 ? 4 
ATOM   13743 C CA    . ILE D 1 338 ? 78.639  37.426  78.038  1.000 49.563  0 338 ILE DDD CA    1 ? 4 
ATOM   13744 C C     . ILE D 1 338 ? 77.517  38.360  78.521  1.000 53.330  0 338 ILE DDD C     1 ? 4 
ATOM   13745 O O     . ILE D 1 338 ? 77.836  39.286  79.301  1.000 51.449  0 338 ILE DDD O     1 ? 4 
ATOM   13746 C CB    . ILE D 1 338 ? 79.655  38.162  77.146  1.000 49.231  0 338 ILE DDD CB    1 ? 4 
ATOM   13747 C CG1   . ILE D 1 338 ? 78.990  38.915  75.993  1.000 50.877  0 338 ILE DDD CG1   1 ? 4 
ATOM   13748 C CG2   . ILE D 1 338 ? 80.748  37.205  76.662  1.000 48.881  0 338 ILE DDD CG2   1 ? 4 
ATOM   13749 C CD1   . ILE D 1 338 ? 79.977  39.584  75.045  1.000 51.705  0 338 ILE DDD CD1   1 ? 4 
ATOM   13750 N N     . VAL D 1 339 ? 76.260  38.169  78.105  1.000 54.590  0 339 VAL DDD N     1 ? 4 
ATOM   13751 C CA    . VAL D 1 339 ? 75.178  39.129  78.468  1.000 56.662  0 339 VAL DDD CA    1 ? 4 
ATOM   13752 C C     . VAL D 1 339 ? 74.481  38.653  79.738  1.000 58.735  0 339 VAL DDD C     1 ? 4 
ATOM   13753 O O     . VAL D 1 339 ? 74.055  37.493  79.793  1.000 57.200  0 339 VAL DDD O     1 ? 4 
ATOM   13754 C CB    . VAL D 1 339 ? 74.194  39.360  77.312  1.000 57.294  0 339 VAL DDD CB    1 ? 4 
ATOM   13755 C CG1   . VAL D 1 339 ? 73.078  40.331  77.721  1.000 56.600  0 339 VAL DDD CG1   1 ? 4 
ATOM   13756 C CG2   . VAL D 1 339 ? 74.920  39.841  76.048  1.000 56.870  0 339 VAL DDD CG2   1 ? 4 
ATOM   13757 N N     . GLU D 1 340 ? 74.371  39.551  80.718  1.000 64.331  0 340 GLU DDD N     1 ? 4 
ATOM   13758 C CA    . GLU D 1 340 ? 73.716  39.271  82.019  1.000 65.904  0 340 GLU DDD CA    1 ? 4 
ATOM   13759 C C     . GLU D 1 340 ? 72.216  39.077  81.806  1.000 58.942  0 340 GLU DDD C     1 ? 4 
ATOM   13760 O O     . GLU D 1 340 ? 71.618  39.851  81.037  1.000 59.170  0 340 GLU DDD O     1 ? 4 
ATOM   13761 C CB    . GLU D 1 340 ? 73.939  40.400  83.028  1.000 72.586  0 340 GLU DDD CB    1 ? 4 
ATOM   13762 C CG    . GLU D 1 340 ? 72.969  40.332  84.198  1.000 76.805  0 340 GLU DDD CG    1 ? 4 
ATOM   13763 C CD    . GLU D 1 340 ? 73.542  40.678  85.547  1.000 85.528  0 340 GLU DDD CD    1 ? 4 
ATOM   13764 O OE1   . GLU D 1 340 ? 73.137  41.715  86.107  1.000 91.906  0 340 GLU DDD OE1   1 ? 4 
ATOM   13765 O OE2   . GLU D 1 340 ? 74.399  39.909  86.028  1.000 91.710  0 340 GLU DDD OE2   1 ? 4 
ATOM   13766 N N     . GLY D 1 341 ? 71.645  38.093  82.506  1.000 57.362  0 341 GLY DDD N     1 ? 4 
ATOM   13767 C CA    . GLY D 1 341 ? 70.188  37.912  82.663  1.000 57.391  0 341 GLY DDD CA    1 ? 4 
ATOM   13768 C C     . GLY D 1 341 ? 69.583  37.093  81.546  1.000 54.425  0 341 GLY DDD C     1 ? 4 
ATOM   13769 O O     . GLY D 1 341 ? 68.358  37.078  81.450  1.000 54.700  0 341 GLY DDD O     1 ? 4 
ATOM   13770 N N     . ARG D 1 342 ? 70.393  36.389  80.752  1.000 53.652  0 342 ARG DDD N     1 ? 4 
ATOM   13771 C CA    . ARG D 1 342 ? 69.857  35.496  79.693  1.000 54.168  0 342 ARG DDD CA    1 ? 4 
ATOM   13772 C C     . ARG D 1 342 ? 70.577  34.149  79.746  1.000 51.627  0 342 ARG DDD C     1 ? 4 
ATOM   13773 O O     . ARG D 1 342 ? 71.753  34.062  80.081  1.000 47.778  0 342 ARG DDD O     1 ? 4 
ATOM   13774 C CB    . ARG D 1 342 ? 69.921  36.149  78.306  1.000 52.344  0 342 ARG DDD CB    1 ? 4 
ATOM   13775 C CG    . ARG D 1 342 ? 71.326  36.265  77.740  1.000 51.779  0 342 ARG DDD CG    1 ? 4 
ATOM   13776 C CD    . ARG D 1 342 ? 71.353  36.798  76.317  1.000 51.290  0 342 ARG DDD CD    1 ? 4 
ATOM   13777 N NE    . ARG D 1 342 ? 70.929  38.192  76.257  1.000 49.989  0 342 ARG DDD NE    1 ? 4 
ATOM   13778 C CZ    . ARG D 1 342 ? 70.897  38.941  75.162  1.000 48.720  0 342 ARG DDD CZ    1 ? 4 
ATOM   13779 N NH1   . ARG D 1 342 ? 71.234  38.447  73.987  1.000 48.345  0 342 ARG DDD NH1   1 ? 4 
ATOM   13780 N NH2   . ARG D 1 342 ? 70.487  40.189  75.245  1.000 50.894  0 342 ARG DDD NH2   1 ? 4 
ATOM   13781 N N     . PRO D 1 343 ? 69.862  33.059  79.397  1.000 49.886  0 343 PRO DDD N     1 ? 4 
ATOM   13782 C CA    . PRO D 1 343 ? 70.422  31.714  79.459  1.000 48.325  0 343 PRO DDD CA    1 ? 4 
ATOM   13783 C C     . PRO D 1 343 ? 71.643  31.579  78.538  1.000 45.324  0 343 PRO DDD C     1 ? 4 
ATOM   13784 O O     . PRO D 1 343 ? 71.649  32.131  77.452  1.000 41.759  0 343 PRO DDD O     1 ? 4 
ATOM   13785 C CB    . PRO D 1 343 ? 69.275  30.810  78.968  1.000 49.625  0 343 PRO DDD CB    1 ? 4 
ATOM   13786 C CG    . PRO D 1 343 ? 68.022  31.650  79.105  1.000 51.560  0 343 PRO DDD CG    1 ? 4 
ATOM   13787 C CD    . PRO D 1 343 ? 68.477  33.079  78.906  1.000 50.419  0 343 PRO DDD CD    1 ? 4 
ATOM   13788 N N     . GLU D 1 344 ? 72.656  30.870  79.018  1.000 46.387  0 344 GLU DDD N     1 ? 4 
ATOM   13789 C CA    . GLU D 1 344 ? 73.916  30.629  78.279  1.000 48.654  0 344 GLU DDD CA    1 ? 4 
ATOM   13790 C C     . GLU D 1 344 ? 73.707  29.389  77.405  1.000 45.057  0 344 GLU DDD C     1 ? 4 
ATOM   13791 O O     . GLU D 1 344 ? 74.308  28.350  77.722  1.000 46.930  0 344 GLU DDD O     1 ? 4 
ATOM   13792 C CB    . GLU D 1 344 ? 75.065  30.399  79.263  1.000 54.044  0 344 GLU DDD CB    1 ? 4 
ATOM   13793 C CG    . GLU D 1 344 ? 75.401  31.584  80.152  1.000 57.601  0 344 GLU DDD CG    1 ? 4 
ATOM   13794 C CD    . GLU D 1 344 ? 76.382  31.293  81.298  1.000 62.217  0 344 GLU DDD CD    1 ? 4 
ATOM   13795 O OE1   . GLU D 1 344 ? 77.179  30.310  81.200  1.000 60.339  0 344 GLU DDD OE1   1 ? 4 
ATOM   13796 O OE2   . GLU D 1 344 ? 76.388  32.092  82.285  1.000 66.101  0 344 GLU DDD OE2   1 ? 4 
ATOM   13797 N N     . LEU D 1 345 ? 72.891  29.499  76.353  1.000 40.991  0 345 LEU DDD N     1 ? 4 
ATOM   13798 C CA    . LEU D 1 345 ? 72.562  28.396  75.414  1.000 38.042  0 345 LEU DDD CA    1 ? 4 
ATOM   13799 C C     . LEU D 1 345 ? 72.881  28.837  73.978  1.000 37.057  0 345 LEU DDD C     1 ? 4 
ATOM   13800 O O     . LEU D 1 345 ? 72.765  30.033  73.681  1.000 34.662  0 345 LEU DDD O     1 ? 4 
ATOM   13801 C CB    . LEU D 1 345 ? 71.068  28.059  75.559  1.000 38.405  0 345 LEU DDD CB    1 ? 4 
ATOM   13802 C CG    . LEU D 1 345 ? 70.626  27.542  76.927  1.000 37.355  0 345 LEU DDD CG    1 ? 4 
ATOM   13803 C CD1   . LEU D 1 345 ? 69.109  27.453  77.014  1.000 36.362  0 345 LEU DDD CD1   1 ? 4 
ATOM   13804 C CD2   . LEU D 1 345 ? 71.265  26.185  77.200  1.000 37.136  0 345 LEU DDD CD2   1 ? 4 
ATOM   13805 N N     . THR D 1 346 ? 73.201  27.889  73.099  1.000 36.081  0 346 THR DDD N     1 ? 4 
ATOM   13806 C CA    . THR D 1 346 ? 73.636  28.168  71.714  1.000 35.366  0 346 THR DDD CA    1 ? 4 
ATOM   13807 C C     . THR D 1 346 ? 72.478  28.756  70.920  1.000 34.962  0 346 THR DDD C     1 ? 4 
ATOM   13808 O O     . THR D 1 346 ? 72.641  29.805  70.306  1.000 34.426  0 346 THR DDD O     1 ? 4 
ATOM   13809 C CB    . THR D 1 346 ? 74.262  26.934  71.056  1.000 36.052  0 346 THR DDD CB    1 ? 4 
ATOM   13810 O OG1   . THR D 1 346 ? 75.642  27.010  71.380  1.000 35.203  0 346 THR DDD OG1   1 ? 4 
ATOM   13811 C CG2   . THR D 1 346 ? 74.119  26.869  69.547  1.000 36.383  0 346 THR DDD CG2   1 ? 4 
ATOM   13812 N N     . PRO D 1 347 ? 71.286  28.117  70.875  1.000 35.832  0 347 PRO DDD N     1 ? 4 
ATOM   13813 C CA    . PRO D 1 347 ? 70.147  28.656  70.125  1.000 35.934  0 347 PRO DDD CA    1 ? 4 
ATOM   13814 C C     . PRO D 1 347 ? 69.761  30.098  70.507  1.000 40.065  0 347 PRO DDD C     1 ? 4 
ATOM   13815 O O     . PRO D 1 347 ? 69.344  30.821  69.648  1.000 43.367  0 347 PRO DDD O     1 ? 4 
ATOM   13816 C CB    . PRO D 1 347 ? 69.029  27.653  70.405  1.000 34.749  0 347 PRO DDD CB    1 ? 4 
ATOM   13817 C CG    . PRO D 1 347 ? 69.763  26.364  70.701  1.000 34.496  0 347 PRO DDD CG    1 ? 4 
ATOM   13818 C CD    . PRO D 1 347 ? 70.962  26.829  71.511  1.000 35.727  0 347 PRO DDD CD    1 ? 4 
ATOM   13819 N N     . VAL D 1 348 ? 69.942  30.489  71.769  1.000 43.365  0 348 VAL DDD N     1 ? 4 
ATOM   13820 C CA    . VAL D 1 348 ? 69.671  31.871  72.262  1.000 44.666  0 348 VAL DDD CA    1 ? 4 
ATOM   13821 C C     . VAL D 1 348 ? 70.714  32.821  71.670  1.000 46.353  0 348 VAL DDD C     1 ? 4 
ATOM   13822 O O     . VAL D 1 348 ? 70.324  33.895  71.227  1.000 44.546  0 348 VAL DDD O     1 ? 4 
ATOM   13823 C CB    . VAL D 1 348 ? 69.691  31.911  73.797  1.000 45.468  0 348 VAL DDD CB    1 ? 4 
ATOM   13824 C CG1   . VAL D 1 348 ? 69.409  33.296  74.335  1.000 47.763  0 348 VAL DDD CG1   1 ? 4 
ATOM   13825 C CG2   . VAL D 1 348 ? 68.699  30.923  74.361  1.000 47.064  0 348 VAL DDD CG2   1 ? 4 
ATOM   13826 N N     . ALA D 1 349 ? 71.990  32.435  71.678  1.000 45.952  0 349 ALA DDD N     1 ? 4 
ATOM   13827 C CA    . ALA D 1 349 ? 73.094  33.200  71.063  1.000 48.016  0 349 ALA DDD CA    1 ? 4 
ATOM   13828 C C     . ALA D 1 349 ? 72.794  33.448  69.575  1.000 48.927  0 349 ALA DDD C     1 ? 4 
ATOM   13829 O O     . ALA D 1 349 ? 72.781  34.618  69.150  1.000 47.277  0 349 ALA DDD O     1 ? 4 
ATOM   13830 C CB    . ALA D 1 349 ? 74.387  32.447  71.254  1.000 49.838  0 349 ALA DDD CB    1 ? 4 
ATOM   13831 N N     . VAL D 1 350 ? 72.537  32.375  68.821  1.000 52.119  0 350 VAL DDD N     1 ? 4 
ATOM   13832 C CA    . VAL D 1 350 ? 72.231  32.385  67.356  1.000 51.012  0 350 VAL DDD CA    1 ? 4 
ATOM   13833 C C     . VAL D 1 350 ? 71.045  33.304  67.084  1.000 50.335  0 350 VAL DDD C     1 ? 4 
ATOM   13834 O O     . VAL D 1 350 ? 71.218  34.227  66.283  1.000 53.915  0 350 VAL DDD O     1 ? 4 
ATOM   13835 C CB    . VAL D 1 350 ? 71.975  30.958  66.827  1.000 53.390  0 350 VAL DDD CB    1 ? 4 
ATOM   13836 C CG1   . VAL D 1 350 ? 71.421  30.938  65.415  1.000 54.601  0 350 VAL DDD CG1   1 ? 4 
ATOM   13837 C CG2   . VAL D 1 350 ? 73.239  30.107  66.884  1.000 56.738  0 350 VAL DDD CG2   1 ? 4 
ATOM   13838 N N     . LYS D 1 351 ? 69.883  33.055  67.692  1.000 49.080  0 351 LYS DDD N     1 ? 4 
ATOM   13839 C CA    . LYS D 1 351 ? 68.658  33.813  67.333  1.000 52.010  0 351 LYS DDD CA    1 ? 4 
ATOM   13840 C C     . LYS D 1 351 ? 68.857  35.292  67.708  1.000 53.427  0 351 LYS DDD C     1 ? 4 
ATOM   13841 O O     . LYS D 1 351 ? 68.386  36.163  66.978  1.000 52.697  0 351 LYS DDD O     1 ? 4 
ATOM   13842 C CB    . LYS D 1 351 ? 67.373  33.246  67.948  1.000 50.644  0 351 LYS DDD CB    1 ? 4 
ATOM   13843 C CG    . LYS D 1 351 ? 66.132  33.967  67.441  1.000 52.395  0 351 LYS DDD CG    1 ? 4 
ATOM   13844 C CD    . LYS D 1 351 ? 64.789  33.381  67.883  1.000 55.785  0 351 LYS DDD CD    1 ? 4 
ATOM   13845 C CE    . LYS D 1 351 ? 64.376  32.102  67.180  1.000 55.459  0 351 LYS DDD CE    1 ? 4 
ATOM   13846 N NZ    . LYS D 1 351 ? 64.053  32.333  65.756  1.000 54.567  0 351 LYS DDD NZ    1 ? 4 
ATOM   13847 N N     . ALA D 1 352 ? 69.511  35.586  68.822  1.000 55.092  0 352 ALA DDD N     1 ? 4 
ATOM   13848 C CA    . ALA D 1 352 ? 69.765  36.989  69.231  1.000 58.167  0 352 ALA DDD CA    1 ? 4 
ATOM   13849 C C     . ALA D 1 352 ? 70.637  37.649  68.166  1.000 59.281  0 352 ALA DDD C     1 ? 4 
ATOM   13850 O O     . ALA D 1 352 ? 70.344  38.804  67.818  1.000 61.732  0 352 ALA DDD O     1 ? 4 
ATOM   13851 C CB    . ALA D 1 352 ? 70.398  37.080  70.606  1.000 55.778  0 352 ALA DDD CB    1 ? 4 
ATOM   13852 N N     . GLY D 1 353 ? 71.641  36.925  67.659  1.000 57.690  0 353 GLY DDD N     1 ? 4 
ATOM   13853 C CA    . GLY D 1 353 ? 72.556  37.439  66.631  1.000 57.121  0 353 GLY DDD CA    1 ? 4 
ATOM   13854 C C     . GLY D 1 353 ? 71.813  37.734  65.340  1.000 57.362  0 353 GLY DDD C     1 ? 4 
ATOM   13855 O O     . GLY D 1 353 ? 72.027  38.819  64.756  1.000 53.698  0 353 GLY DDD O     1 ? 4 
ATOM   13856 N N     . ILE D 1 354 ? 70.959  36.801  64.905  1.000 58.099  0 354 ILE DDD N     1 ? 4 
ATOM   13857 C CA    . ILE D 1 354 ? 70.141  36.947  63.665  1.000 57.514  0 354 ILE DDD CA    1 ? 4 
ATOM   13858 C C     . ILE D 1 354 ? 69.137  38.107  63.840  1.000 57.226  0 354 ILE DDD C     1 ? 4 
ATOM   13859 O O     . ILE D 1 354 ? 69.065  38.938  62.933  1.000 52.515  0 354 ILE DDD O     1 ? 4 
ATOM   13860 C CB    . ILE D 1 354 ? 69.446  35.621  63.304  1.000 59.140  0 354 ILE DDD CB    1 ? 4 
ATOM   13861 C CG1   . ILE D 1 354 ? 70.444  34.506  62.970  1.000 59.359  0 354 ILE DDD CG1   1 ? 4 
ATOM   13862 C CG2   . ILE D 1 354 ? 68.459  35.839  62.177  1.000 60.073  0 354 ILE DDD CG2   1 ? 4 
ATOM   13863 C CD1   . ILE D 1 354 ? 69.822  33.138  62.737  1.000 57.100  0 354 ILE DDD CD1   1 ? 4 
ATOM   13864 N N     . LEU D 1 355 ? 68.388  38.167  64.947  1.000 56.513  0 355 LEU DDD N     1 ? 4 
ATOM   13865 C CA    . LEU D 1 355 ? 67.342  39.208  65.148  1.000 55.664  0 355 LEU DDD CA    1 ? 4 
ATOM   13866 C C     . LEU D 1 355 ? 68.015  40.581  65.259  1.000 56.930  0 355 LEU DDD C     1 ? 4 
ATOM   13867 O O     . LEU D 1 355 ? 67.475  41.544  64.694  1.000 60.010  0 355 LEU DDD O     1 ? 4 
ATOM   13868 C CB    . LEU D 1 355 ? 66.485  38.880  66.377  1.000 52.016  0 355 LEU DDD CB    1 ? 4 
ATOM   13869 C CG    . LEU D 1 355 ? 65.572  37.659  66.284  1.000 49.591  0 355 LEU DDD CG    1 ? 4 
ATOM   13870 C CD1   . LEU D 1 355 ? 64.606  37.636  67.446  1.000 47.252  0 355 LEU DDD CD1   1 ? 4 
ATOM   13871 C CD2   . LEU D 1 355 ? 64.776  37.640  65.002  1.000 51.274  0 355 LEU DDD CD2   1 ? 4 
ATOM   13872 N N     . LEU D 1 356 ? 69.165  40.667  65.919  1.000 60.777  0 356 LEU DDD N     1 ? 4 
ATOM   13873 C CA    . LEU D 1 356 ? 69.947  41.931  66.011  1.000 67.410  0 356 LEU DDD CA    1 ? 4 
ATOM   13874 C C     . LEU D 1 356 ? 70.281  42.393  64.585  1.000 69.583  0 356 LEU DDD C     1 ? 4 
ATOM   13875 O O     . LEU D 1 356 ? 69.888  43.523  64.218  1.000 78.926  0 356 LEU DDD O     1 ? 4 
ATOM   13876 C CB    . LEU D 1 356 ? 71.216  41.732  66.853  1.000 65.823  0 356 LEU DDD CB    1 ? 4 
ATOM   13877 C CG    . LEU D 1 356 ? 72.219  42.890  66.835  1.000 67.778  0 356 LEU DDD CG    1 ? 4 
ATOM   13878 C CD1   . LEU D 1 356 ? 71.618  44.145  67.455  1.000 71.435  0 356 LEU DDD CD1   1 ? 4 
ATOM   13879 C CD2   . LEU D 1 356 ? 73.512  42.512  67.552  1.000 67.051  0 356 LEU DDD CD2   1 ? 4 
ATOM   13880 N N     . ALA D 1 357 ? 70.976  41.558  63.812  1.000 67.352  0 357 ALA DDD N     1 ? 4 
ATOM   13881 C CA    . ALA D 1 357 ? 71.298  41.806  62.386  1.000 68.219  0 357 ALA DDD CA    1 ? 4 
ATOM   13882 C C     . ALA D 1 357 ? 70.062  42.365  61.651  1.000 66.382  0 357 ALA DDD C     1 ? 4 
ATOM   13883 O O     . ALA D 1 357 ? 70.194  43.402  60.985  1.000 60.776  0 357 ALA DDD O     1 ? 4 
ATOM   13884 C CB    . ALA D 1 357 ? 71.797  40.534  61.739  1.000 67.726  0 357 ALA DDD CB    1 ? 4 
ATOM   13885 N N     . ARG D 1 358 ? 68.894  41.734  61.802  1.000 64.815  0 358 ARG DDD N     1 ? 4 
ATOM   13886 C CA    . ARG D 1 358 ? 67.643  42.145  61.120  1.000 67.194  0 358 ARG DDD CA    1 ? 4 
ATOM   13887 C C     . ARG D 1 358 ? 67.171  43.517  61.610  1.000 69.439  0 358 ARG DDD C     1 ? 4 
ATOM   13888 O O     . ARG D 1 358 ? 66.758  44.319  60.754  1.000 71.742  0 358 ARG DDD O     1 ? 4 
ATOM   13889 C CB    . ARG D 1 358 ? 66.537  41.106  61.321  1.000 66.923  0 358 ARG DDD CB    1 ? 4 
ATOM   13890 C CG    . ARG D 1 358 ? 66.720  39.861  60.467  1.000 66.123  0 358 ARG DDD CG    1 ? 4 
ATOM   13891 C CD    . ARG D 1 358 ? 65.695  38.792  60.755  1.000 66.256  0 358 ARG DDD CD    1 ? 4 
ATOM   13892 N NE    . ARG D 1 358 ? 66.108  37.550  60.122  1.000 65.733  0 358 ARG DDD NE    1 ? 4 
ATOM   13893 C CZ    . ARG D 1 358 ? 65.557  36.362  60.355  1.000 65.870  0 358 ARG DDD CZ    1 ? 4 
ATOM   13894 N NH1   . ARG D 1 358 ? 64.550  36.259  61.199  1.000 66.519  0 358 ARG DDD NH1   1 ? 4 
ATOM   13895 N NH2   . ARG D 1 358 ? 66.010  35.275  59.754  1.000 64.865  0 358 ARG DDD NH2   1 ? 4 
ATOM   13896 N N     . ARG D 1 359 ? 67.172  43.766  62.924  1.000 68.314  0 359 ARG DDD N     1 ? 4 
ATOM   13897 C CA    . ARG D 1 359 ? 66.710  45.054  63.498  1.000 70.641  0 359 ARG DDD CA    1 ? 4 
ATOM   13898 C C     . ARG D 1 359 ? 67.596  46.189  62.977  1.000 72.956  0 359 ARG DDD C     1 ? 4 
ATOM   13899 O O     . ARG D 1 359 ? 67.059  47.287  62.718  1.000 76.397  0 359 ARG DDD O     1 ? 4 
ATOM   13900 C CB    . ARG D 1 359 ? 66.715  45.022  65.027  1.000 71.710  0 359 ARG DDD CB    1 ? 4 
ATOM   13901 C CG    . ARG D 1 359 ? 65.627  44.153  65.634  1.000 72.032  0 359 ARG DDD CG    1 ? 4 
ATOM   13902 C CD    . ARG D 1 359 ? 65.344  44.521  67.088  1.000 73.275  0 359 ARG DDD CD    1 ? 4 
ATOM   13903 N NE    . ARG D 1 359 ? 66.545  44.509  67.914  1.000 74.468  0 359 ARG DDD NE    1 ? 4 
ATOM   13904 C CZ    . ARG D 1 359 ? 67.157  43.405  68.365  1.000 79.965  0 359 ARG DDD CZ    1 ? 4 
ATOM   13905 N NH1   . ARG D 1 359 ? 66.678  42.199  68.087  1.000 78.895  0 359 ARG DDD NH1   1 ? 4 
ATOM   13906 N NH2   . ARG D 1 359 ? 68.266  43.505  69.085  1.000 78.793  0 359 ARG DDD NH2   1 ? 4 
ATOM   13907 N N     . LEU D 1 360 ? 68.900  45.942  62.852  1.000 74.346  0 360 LEU DDD N     1 ? 4 
ATOM   13908 C CA    . LEU D 1 360 ? 69.892  46.974  62.448  1.000 77.208  0 360 LEU DDD CA    1 ? 4 
ATOM   13909 C C     . LEU D 1 360 ? 69.727  47.304  60.961  1.000 77.901  0 360 LEU DDD C     1 ? 4 
ATOM   13910 O O     . LEU D 1 360 ? 69.868  48.499  60.619  1.000 80.766  0 360 LEU DDD O     1 ? 4 
ATOM   13911 C CB    . LEU D 1 360 ? 71.313  46.494  62.763  1.000 78.008  0 360 LEU DDD CB    1 ? 4 
ATOM   13912 C CG    . LEU D 1 360 ? 71.702  46.469  64.248  1.000 79.450  0 360 LEU DDD CG    1 ? 4 
ATOM   13913 C CD1   . LEU D 1 360 ? 73.135  45.972  64.409  1.000 79.726  0 360 LEU DDD CD1   1 ? 4 
ATOM   13914 C CD2   . LEU D 1 360 ? 71.561  47.849  64.891  1.000 80.881  0 360 LEU DDD CD2   1 ? 4 
ATOM   13915 N N     . PHE D 1 361 ? 69.419  46.309  60.120  1.000 76.963  0 361 PHE DDD N     1 ? 4 
ATOM   13916 C CA    . PHE D 1 361 ? 69.654  46.376  58.651  1.000 76.902  0 361 PHE DDD CA    1 ? 4 
ATOM   13917 C C     . PHE D 1 361 ? 68.441  45.957  57.802  1.000 78.320  0 361 PHE DDD C     1 ? 4 
ATOM   13918 O O     . PHE D 1 361 ? 68.562  46.144  56.575  1.000 82.494  0 361 PHE DDD O     1 ? 4 
ATOM   13919 C CB    . PHE D 1 361 ? 70.861  45.511  58.287  1.000 74.405  0 361 PHE DDD CB    1 ? 4 
ATOM   13920 C CG    . PHE D 1 361 ? 72.156  45.933  58.938  1.000 74.358  0 361 PHE DDD CG    1 ? 4 
ATOM   13921 C CD1   . PHE D 1 361 ? 72.653  47.221  58.782  1.000 74.573  0 361 PHE DDD CD1   1 ? 4 
ATOM   13922 C CD2   . PHE D 1 361 ? 72.889  45.037  59.705  1.000 72.888  0 361 PHE DDD CD2   1 ? 4 
ATOM   13923 C CE1   . PHE D 1 361 ? 73.852  47.596  59.370  1.000 71.807  0 361 PHE DDD CE1   1 ? 4 
ATOM   13924 C CE2   . PHE D 1 361 ? 74.078  45.414  60.307  1.000 67.636  0 361 PHE DDD CE2   1 ? 4 
ATOM   13925 C CZ    . PHE D 1 361 ? 74.553  46.696  60.142  1.000 68.739  0 361 PHE DDD CZ    1 ? 4 
ATOM   13926 N N     . ALA D 1 362 ? 67.349  45.427  58.377  1.000 77.354  0 362 ALA DDD N     1 ? 4 
ATOM   13927 C CA    . ALA D 1 362 ? 66.152  44.958  57.627  1.000 77.259  0 362 ALA DDD CA    1 ? 4 
ATOM   13928 C C     . ALA D 1 362 ? 64.856  45.457  58.273  1.000 75.716  0 362 ALA DDD C     1 ? 4 
ATOM   13929 O O     . ALA D 1 362 ? 63.804  44.836  58.048  1.000 73.381  0 362 ALA DDD O     1 ? 4 
ATOM   13930 C CB    . ALA D 1 362 ? 66.150  43.452  57.520  1.000 78.860  0 362 ALA DDD CB    1 ? 4 
ATOM   13931 N N     . GLY D 1 363 ? 64.913  46.537  59.051  1.000 77.294  0 363 GLY DDD N     1 ? 4 
ATOM   13932 C CA    . GLY D 1 363 ? 63.707  47.205  59.573  1.000 75.584  0 363 GLY DDD CA    1 ? 4 
ATOM   13933 C C     . GLY D 1 363 ? 62.879  46.315  60.486  1.000 76.243  0 363 GLY DDD C     1 ? 4 
ATOM   13934 O O     . GLY D 1 363 ? 61.688  46.630  60.651  1.000 77.255  0 363 GLY DDD O     1 ? 4 
ATOM   13935 N N     . SER D 1 364 ? 63.456  45.251  61.064  1.000 76.490  0 364 SER DDD N     1 ? 4 
ATOM   13936 C CA    . SER D 1 364 ? 62.764  44.333  62.014  1.000 77.383  0 364 SER DDD CA    1 ? 4 
ATOM   13937 C C     . SER D 1 364 ? 62.710  45.006  63.391  1.000 77.186  0 364 SER DDD C     1 ? 4 
ATOM   13938 O O     . SER D 1 364 ? 63.558  45.878  63.663  1.000 74.158  0 364 SER DDD O     1 ? 4 
ATOM   13939 C CB    . SER D 1 364 ? 63.434  42.962  62.054  1.000 78.990  0 364 SER DDD CB    1 ? 4 
ATOM   13940 O OG    . SER D 1 364 ? 62.978  42.175  63.150  1.000 81.012  0 364 SER DDD OG    1 ? 4 
ATOM   13941 N N     . ASN D 1 365 ? 61.725  44.662  64.223  1.000 82.300  0 365 ASN DDD N     1 ? 4 
ATOM   13942 C CA    . ASN D 1 365 ? 61.725  45.083  65.651  1.000 87.543  0 365 ASN DDD CA    1 ? 4 
ATOM   13943 C C     . ASN D 1 365 ? 61.459  43.876  66.558  1.000 84.315  0 365 ASN DDD C     1 ? 4 
ATOM   13944 O O     . ASN D 1 365 ? 60.965  44.062  67.685  1.000 81.550  0 365 ASN DDD O     1 ? 4 
ATOM   13945 C CB    . ASN D 1 365 ? 60.777  46.255  65.911  1.000 93.465  0 365 ASN DDD CB    1 ? 4 
ATOM   13946 C CG    . ASN D 1 365 ? 61.343  47.153  66.989  1.000 99.412  0 365 ASN DDD CG    1 ? 4 
ATOM   13947 O OD1   . ASN D 1 365 ? 60.949  47.042  68.152  1.000 98.342  0 365 ASN DDD OD1   1 ? 4 
ATOM   13948 N ND2   . ASN D 1 365 ? 62.318  47.982  66.634  1.000 105.281 0 365 ASN DDD ND2   1 ? 4 
ATOM   13949 N N     . GLU D 1 366 ? 61.839  42.683  66.095  1.000 83.144  0 366 GLU DDD N     1 ? 4 
ATOM   13950 C CA    . GLU D 1 366 ? 61.561  41.396  66.779  1.000 80.301  0 366 GLU DDD CA    1 ? 4 
ATOM   13951 C C     . GLU D 1 366 ? 62.721  41.096  67.724  1.000 75.129  0 366 GLU DDD C     1 ? 4 
ATOM   13952 O O     . GLU D 1 366 ? 63.892  41.188  67.295  1.000 72.588  0 366 GLU DDD O     1 ? 4 
ATOM   13953 C CB    . GLU D 1 366 ? 61.318  40.267  65.780  1.000 80.277  0 366 GLU DDD CB    1 ? 4 
ATOM   13954 C CG    . GLU D 1 366 ? 59.932  40.341  65.181  1.000 79.479  0 366 GLU DDD CG    1 ? 4 
ATOM   13955 C CD    . GLU D 1 366 ? 59.643  39.287  64.153  1.000 80.959  0 366 GLU DDD CD    1 ? 4 
ATOM   13956 O OE1   . GLU D 1 366 ? 59.848  39.572  62.954  1.000 87.309  0 366 GLU DDD OE1   1 ? 4 
ATOM   13957 O OE2   . GLU D 1 366 ? 59.183  38.201  64.555  1.000 81.016  0 366 GLU DDD OE2   1 ? 4 
ATOM   13958 N N     . PHE D 1 367 ? 62.363  40.789  68.971  1.000 72.836  0 367 PHE DDD N     1 ? 4 
ATOM   13959 C CA    . PHE D 1 367 ? 63.248  40.261  70.036  1.000 68.292  0 367 PHE DDD CA    1 ? 4 
ATOM   13960 C C     . PHE D 1 367 ? 62.800  38.831  70.363  1.000 65.209  0 367 PHE DDD C     1 ? 4 
ATOM   13961 O O     . PHE D 1 367 ? 61.654  38.447  70.043  1.000 69.283  0 367 PHE DDD O     1 ? 4 
ATOM   13962 C CB    . PHE D 1 367 ? 63.201  41.195  71.253  1.000 67.472  0 367 PHE DDD CB    1 ? 4 
ATOM   13963 C CG    . PHE D 1 367 ? 63.822  42.553  71.017  1.000 67.941  0 367 PHE DDD CG    1 ? 4 
ATOM   13964 C CD1   . PHE D 1 367 ? 63.101  43.568  70.401  1.000 66.863  0 367 PHE DDD CD1   1 ? 4 
ATOM   13965 C CD2   . PHE D 1 367 ? 65.143  42.806  71.382  1.000 67.140  0 367 PHE DDD CD2   1 ? 4 
ATOM   13966 C CE1   . PHE D 1 367 ? 63.676  44.815  70.184  1.000 65.701  0 367 PHE DDD CE1   1 ? 4 
ATOM   13967 C CE2   . PHE D 1 367 ? 65.720  44.052  71.164  1.000 66.999  0 367 PHE DDD CE2   1 ? 4 
ATOM   13968 C CZ    . PHE D 1 367 ? 64.987  45.048  70.552  1.000 67.555  0 367 PHE DDD CZ    1 ? 4 
ATOM   13969 N N     . ILE D 1 368 ? 63.696  38.049  70.969  1.000 60.884  0 368 ILE DDD N     1 ? 4 
ATOM   13970 C CA    . ILE D 1 368 ? 63.374  36.725  71.573  1.000 54.681  0 368 ILE DDD CA    1 ? 4 
ATOM   13971 C C     . ILE D 1 368 ? 62.339  36.927  72.685  1.000 53.385  0 368 ILE DDD C     1 ? 4 
ATOM   13972 O O     . ILE D 1 368 ? 62.412  37.970  73.400  1.000 52.032  0 368 ILE DDD O     1 ? 4 
ATOM   13973 C CB    . ILE D 1 368 ? 64.650  36.058  72.118  1.000 53.874  0 368 ILE DDD CB    1 ? 4 
ATOM   13974 C CG1   . ILE D 1 368 ? 65.630  35.702  71.001  1.000 51.303  0 368 ILE DDD CG1   1 ? 4 
ATOM   13975 C CG2   . ILE D 1 368 ? 64.298  34.864  73.014  1.000 55.429  0 368 ILE DDD CG2   1 ? 4 
ATOM   13976 C CD1   . ILE D 1 368 ? 66.980  35.256  71.483  1.000 50.133  0 368 ILE DDD CD1   1 ? 4 
ATOM   13977 N N     . ASP D 1 369 ? 61.437  35.957  72.837  1.000 51.644  0 369 ASP DDD N     1 ? 4 
ATOM   13978 C CA    . ASP D 1 369 ? 60.538  35.814  74.010  1.000 54.138  0 369 ASP DDD CA    1 ? 4 
ATOM   13979 C C     . ASP D 1 369 ? 61.276  34.936  75.031  1.000 55.269  0 369 ASP DDD C     1 ? 4 
ATOM   13980 O O     . ASP D 1 369 ? 61.292  33.690  74.855  1.000 59.608  0 369 ASP DDD O     1 ? 4 
ATOM   13981 C CB    . ASP D 1 369 ? 59.157  35.297  73.580  1.000 54.578  0 369 ASP DDD CB    1 ? 4 
ATOM   13982 C CG    . ASP D 1 369 ? 58.119  35.259  74.693  1.000 58.039  0 369 ASP DDD CG    1 ? 4 
ATOM   13983 O OD1   . ASP D 1 369 ? 58.508  35.432  75.880  1.000 60.791  0 369 ASP DDD OD1   1 ? 4 
ATOM   13984 O OD2   . ASP D 1 369 ? 56.914  35.047  74.375  1.000 59.186  0 369 ASP DDD OD2   1 ? 4 
ATOM   13985 N N     . TYR D 1 370 ? 61.888  35.552  76.048  1.000 55.210  0 370 TYR DDD N     1 ? 4 
ATOM   13986 C CA    . TYR D 1 370 ? 62.784  34.856  76.998  1.000 56.259  0 370 TYR DDD CA    1 ? 4 
ATOM   13987 C C     . TYR D 1 370 ? 61.964  34.026  77.987  1.000 57.268  0 370 TYR DDD C     1 ? 4 
ATOM   13988 O O     . TYR D 1 370 ? 62.577  33.317  78.790  1.000 61.232  0 370 TYR DDD O     1 ? 4 
ATOM   13989 C CB    . TYR D 1 370 ? 63.711  35.846  77.705  1.000 58.361  0 370 TYR DDD CB    1 ? 4 
ATOM   13990 C CG    . TYR D 1 370 ? 64.842  36.324  76.831  1.000 58.646  0 370 TYR DDD CG    1 ? 4 
ATOM   13991 C CD1   . TYR D 1 370 ? 65.920  35.500  76.543  1.000 59.217  0 370 TYR DDD CD1   1 ? 4 
ATOM   13992 C CD2   . TYR D 1 370 ? 64.831  37.591  76.272  1.000 58.002  0 370 TYR DDD CD2   1 ? 4 
ATOM   13993 C CE1   . TYR D 1 370 ? 66.958  35.918  75.718  1.000 60.882  0 370 TYR DDD CE1   1 ? 4 
ATOM   13994 C CE2   . TYR D 1 370 ? 65.859  38.030  75.452  1.000 59.538  0 370 TYR DDD CE2   1 ? 4 
ATOM   13995 C CZ    . TYR D 1 370 ? 66.922  37.189  75.162  1.000 62.108  0 370 TYR DDD CZ    1 ? 4 
ATOM   13996 O OH    . TYR D 1 370 ? 67.941  37.612  74.352  1.000 61.471  0 370 TYR DDD OH    1 ? 4 
ATOM   13997 N N     . ASP D 1 371 ? 60.636  34.076  77.910  1.000 54.680  0 371 ASP DDD N     1 ? 4 
ATOM   13998 C CA    . ASP D 1 371 ? 59.733  33.272  78.773  1.000 52.950  0 371 ASP DDD CA    1 ? 4 
ATOM   13999 C C     . ASP D 1 371 ? 59.693  31.817  78.290  1.000 47.453  0 371 ASP DDD C     1 ? 4 
ATOM   14000 O O     . ASP D 1 371 ? 59.291  30.973  79.080  1.000 45.718  0 371 ASP DDD O     1 ? 4 
ATOM   14001 C CB    . ASP D 1 371 ? 58.314  33.870  78.795  1.000 56.954  0 371 ASP DDD CB    1 ? 4 
ATOM   14002 C CG    . ASP D 1 371 ? 58.230  35.221  79.488  1.000 57.781  0 371 ASP DDD CG    1 ? 4 
ATOM   14003 O OD1   . ASP D 1 371 ? 58.969  35.387  80.476  1.000 59.587  0 371 ASP DDD OD1   1 ? 4 
ATOM   14004 O OD2   . ASP D 1 371 ? 57.427  36.089  79.041  1.000 60.079  0 371 ASP DDD OD2   1 ? 4 
ATOM   14005 N N     . PHE D 1 372 ? 60.038  31.540  77.032  1.000 45.871  0 372 PHE DDD N     1 ? 4 
ATOM   14006 C CA    . PHE D 1 372 ? 59.840  30.211  76.392  1.000 43.423  0 372 PHE DDD CA    1 ? 4 
ATOM   14007 C C     . PHE D 1 372 ? 61.136  29.750  75.721  1.000 41.342  0 372 PHE DDD C     1 ? 4 
ATOM   14008 O O     . PHE D 1 372 ? 61.168  29.593  74.495  1.000 42.168  0 372 PHE DDD O     1 ? 4 
ATOM   14009 C CB    . PHE D 1 372 ? 58.649  30.274  75.440  1.000 45.308  0 372 PHE DDD CB    1 ? 4 
ATOM   14010 C CG    . PHE D 1 372 ? 57.338  30.542  76.132  1.000 46.101  0 372 PHE DDD CG    1 ? 4 
ATOM   14011 C CD1   . PHE D 1 372 ? 56.739  29.566  76.911  1.000 46.768  0 372 PHE DDD CD1   1 ? 4 
ATOM   14012 C CD2   . PHE D 1 372 ? 56.735  31.785  76.039  1.000 47.450  0 372 PHE DDD CD2   1 ? 4 
ATOM   14013 C CE1   . PHE D 1 372 ? 55.533  29.814  77.553  1.000 49.861  0 372 PHE DDD CE1   1 ? 4 
ATOM   14014 C CE2   . PHE D 1 372 ? 55.538  32.049  76.699  1.000 48.701  0 372 PHE DDD CE2   1 ? 4 
ATOM   14015 C CZ    . PHE D 1 372 ? 54.935  31.061  77.450  1.000 48.716  0 372 PHE DDD CZ    1 ? 4 
ATOM   14016 N N     . VAL D 1 373 ? 62.163  29.540  76.543  1.000 37.815  0 373 VAL DDD N     1 ? 4 
ATOM   14017 C CA    . VAL D 1 373 ? 63.495  29.041  76.128  1.000 36.726  0 373 VAL DDD CA    1 ? 4 
ATOM   14018 C C     . VAL D 1 373 ? 63.662  27.638  76.692  1.000 33.545  0 373 VAL DDD C     1 ? 4 
ATOM   14019 O O     . VAL D 1 373 ? 63.922  27.477  77.870  1.000 31.801  0 373 VAL DDD O     1 ? 4 
ATOM   14020 C CB    . VAL D 1 373 ? 64.607  29.988  76.606  1.000 38.280  0 373 VAL DDD CB    1 ? 4 
ATOM   14021 C CG1   . VAL D 1 373 ? 66.006  29.408  76.324  1.000 39.510  0 373 VAL DDD CG1   1 ? 4 
ATOM   14022 C CG2   . VAL D 1 373 ? 64.441  31.373  75.984  1.000 38.660  0 373 VAL DDD CG2   1 ? 4 
ATOM   14023 N N     . PRO D 1 374 ? 63.519  26.580  75.876  1.000 33.595  0 374 PRO DDD N     1 ? 4 
ATOM   14024 C CA    . PRO D 1 374 ? 63.678  25.211  76.356  1.000 33.815  0 374 PRO DDD CA    1 ? 4 
ATOM   14025 C C     . PRO D 1 374 ? 65.175  24.867  76.474  1.000 34.886  0 374 PRO DDD C     1 ? 4 
ATOM   14026 O O     . PRO D 1 374 ? 66.004  25.521  75.875  1.000 34.718  0 374 PRO DDD O     1 ? 4 
ATOM   14027 C CB    . PRO D 1 374 ? 63.015  24.368  75.255  1.000 32.448  0 374 PRO DDD CB    1 ? 4 
ATOM   14028 C CG    . PRO D 1 374 ? 63.292  25.159  73.991  1.000 32.658  0 374 PRO DDD CG    1 ? 4 
ATOM   14029 C CD    . PRO D 1 374 ? 63.231  26.618  74.426  1.000 33.989  0 374 PRO DDD CD    1 ? 4 
ATOM   14030 N N     . THR D 1 375 ? 65.483  23.856  77.266  1.000 34.531  0 375 THR DDD N     1 ? 4 
ATOM   14031 C CA    . THR D 1 375 ? 66.853  23.401  77.517  1.000 37.420  0 375 THR DDD CA    1 ? 4 
ATOM   14032 C C     . THR D 1 375 ? 66.745  21.904  77.766  1.000 36.176  0 375 THR DDD C     1 ? 4 
ATOM   14033 O O     . THR D 1 375 ? 65.654  21.459  78.239  1.000 34.509  0 375 THR DDD O     1 ? 4 
ATOM   14034 C CB    . THR D 1 375 ? 67.495  24.175  78.680  1.000 41.921  0 375 THR DDD CB    1 ? 4 
ATOM   14035 O OG1   . THR D 1 375 ? 68.698  23.532  79.111  1.000 47.740  0 375 THR DDD OG1   1 ? 4 
ATOM   14036 C CG2   . THR D 1 375 ? 66.632  24.233  79.909  1.000 42.262  0 375 THR DDD CG2   1 ? 4 
ATOM   14037 N N     . THR D 1 376 ? 67.778  21.161  77.374  1.000 31.666  0 376 THR DDD N     1 ? 4 
ATOM   14038 C CA    . THR D 1 376 ? 67.920  19.752  77.782  1.000 32.256  0 376 THR DDD CA    1 ? 4 
ATOM   14039 C C     . THR D 1 376 ? 69.294  19.546  78.397  1.000 32.538  0 376 THR DDD C     1 ? 4 
ATOM   14040 O O     . THR D 1 376 ? 70.286  20.061  77.831  1.000 32.567  0 376 THR DDD O     1 ? 4 
ATOM   14041 C CB    . THR D 1 376 ? 67.693  18.779  76.627  1.000 31.919  0 376 THR DDD CB    1 ? 4 
ATOM   14042 O OG1   . THR D 1 376 ? 66.300  18.774  76.298  1.000 29.823  0 376 THR DDD OG1   1 ? 4 
ATOM   14043 C CG2   . THR D 1 376 ? 68.093  17.373  77.010  1.000 32.479  0 376 THR DDD CG2   1 ? 4 
ATOM   14044 N N     . VAL D 1 377 ? 69.324  18.835  79.521  1.000 31.556  0 377 VAL DDD N     1 ? 4 
ATOM   14045 C CA    . VAL D 1 377 ? 70.576  18.388  80.192  1.000 32.014  0 377 VAL DDD CA    1 ? 4 
ATOM   14046 C C     . VAL D 1 377 ? 70.834  16.951  79.750  1.000 31.546  0 377 VAL DDD C     1 ? 4 
ATOM   14047 O O     . VAL D 1 377 ? 69.921  16.129  79.895  1.000 31.464  0 377 VAL DDD O     1 ? 4 
ATOM   14048 C CB    . VAL D 1 377 ? 70.419  18.531  81.710  1.000 32.415  0 377 VAL DDD CB    1 ? 4 
ATOM   14049 C CG1   . VAL D 1 377 ? 71.572  17.914  82.470  1.000 33.268  0 377 VAL DDD CG1   1 ? 4 
ATOM   14050 C CG2   . VAL D 1 377 ? 70.242  20.002  82.073  1.000 33.529  0 377 VAL DDD CG2   1 ? 4 
ATOM   14051 N N     . PHE D 1 378 ? 71.984  16.677  79.154  1.000 32.185  0 378 PHE DDD N     1 ? 4 
ATOM   14052 C CA    . PHE D 1 378 ? 72.295  15.335  78.570  1.000 32.474  0 378 PHE DDD CA    1 ? 4 
ATOM   14053 C C     . PHE D 1 378 ? 72.997  14.448  79.604  1.000 31.189  0 378 PHE DDD C     1 ? 4 
ATOM   14054 O O     . PHE D 1 378 ? 74.093  13.936  79.345  1.000 33.305  0 378 PHE DDD O     1 ? 4 
ATOM   14055 C CB    . PHE D 1 378 ? 73.054  15.480  77.248  1.000 31.611  0 378 PHE DDD CB    1 ? 4 
ATOM   14056 C CG    . PHE D 1 378 ? 72.199  16.137  76.198  1.000 32.796  0 378 PHE DDD CG    1 ? 4 
ATOM   14057 C CD1   . PHE D 1 378 ? 71.314  15.383  75.436  1.000 33.240  0 378 PHE DDD CD1   1 ? 4 
ATOM   14058 C CD2   . PHE D 1 378 ? 72.230  17.512  76.022  1.000 33.434  0 378 PHE DDD CD2   1 ? 4 
ATOM   14059 C CE1   . PHE D 1 378 ? 70.531  15.992  74.469  1.000 33.528  0 378 PHE DDD CE1   1 ? 4 
ATOM   14060 C CE2   . PHE D 1 378 ? 71.432  18.130  75.077  1.000 33.261  0 378 PHE DDD CE2   1 ? 4 
ATOM   14061 C CZ    . PHE D 1 378 ? 70.581  17.370  74.308  1.000 34.322  0 378 PHE DDD CZ    1 ? 4 
ATOM   14062 N N     . THR D 1 379 ? 72.320  14.208  80.711  1.000 29.475  0 379 THR DDD N     1 ? 4 
ATOM   14063 C CA    . THR D 1 379 ? 72.747  13.275  81.768  1.000 29.712  0 379 THR DDD CA    1 ? 4 
ATOM   14064 C C     . THR D 1 379 ? 72.354  11.864  81.339  1.000 30.884  0 379 THR DDD C     1 ? 4 
ATOM   14065 O O     . THR D 1 379 ? 71.575  11.707  80.402  1.000 32.074  0 379 THR DDD O     1 ? 4 
ATOM   14066 C CB    . THR D 1 379 ? 72.183  13.755  83.107  1.000 30.627  0 379 THR DDD CB    1 ? 4 
ATOM   14067 O OG1   . THR D 1 379 ? 70.884  14.318  82.900  1.000 28.968  0 379 THR DDD OG1   1 ? 4 
ATOM   14068 C CG2   . THR D 1 379 ? 73.081  14.788  83.752  1.000 31.301  0 379 THR DDD CG2   1 ? 4 
ATOM   14069 N N     . PRO D 1 380 ? 72.883  10.801  81.995  1.000 32.314  0 380 PRO DDD N     1 ? 4 
ATOM   14070 C CA    . PRO D 1 380 ? 72.638  9.422   81.573  1.000 32.878  0 380 PRO DDD CA    1 ? 4 
ATOM   14071 C C     . PRO D 1 380 ? 71.155  9.105   81.324  1.000 33.307  0 380 PRO DDD C     1 ? 4 
ATOM   14072 O O     . PRO D 1 380 ? 70.875  8.418   80.390  1.000 34.122  0 380 PRO DDD O     1 ? 4 
ATOM   14073 C CB    . PRO D 1 380 ? 73.229  8.595   82.717  1.000 33.589  0 380 PRO DDD CB    1 ? 4 
ATOM   14074 C CG    . PRO D 1 380 ? 74.345  9.478   83.245  1.000 33.329  0 380 PRO DDD CG    1 ? 4 
ATOM   14075 C CD    . PRO D 1 380 ? 73.766  10.873  83.171  1.000 33.274  0 380 PRO DDD CD    1 ? 4 
ATOM   14076 N N     . ILE D 1 381 ? 70.255  9.635   82.149  1.000 32.788  0 381 ILE DDD N     1 ? 4 
ATOM   14077 C CA    . ILE D 1 381 ? 68.860  9.955   81.736  1.000 32.157  0 381 ILE DDD CA    1 ? 4 
ATOM   14078 C C     . ILE D 1 381 ? 68.825  11.465  81.553  1.000 30.260  0 381 ILE DDD C     1 ? 4 
ATOM   14079 O O     . ILE D 1 381 ? 69.375  12.153  82.396  1.000 32.228  0 381 ILE DDD O     1 ? 4 
ATOM   14080 C CB    . ILE D 1 381 ? 67.784  9.454   82.724  1.000 34.200  0 381 ILE DDD CB    1 ? 4 
ATOM   14081 C CG1   . ILE D 1 381 ? 68.039  9.940   84.141  1.000 35.251  0 381 ILE DDD CG1   1 ? 4 
ATOM   14082 C CG2   . ILE D 1 381 ? 67.624  7.942   82.680  1.000 35.029  0 381 ILE DDD CG2   1 ? 4 
ATOM   14083 C CD1   . ILE D 1 381 ? 67.011  9.429   85.140  1.000 38.651  0 381 ILE DDD CD1   1 ? 4 
ATOM   14084 N N     . GLU D 1 382 ? 68.225  11.929  80.469  1.000 29.931  0 382 GLU DDD N     1 ? 4 
ATOM   14085 C CA    . GLU D 1 382 ? 68.257  13.346  80.029  1.000 29.468  0 382 GLU DDD CA    1 ? 4 
ATOM   14086 C C     . GLU D 1 382 ? 67.124  14.090  80.728  1.000 28.352  0 382 GLU DDD C     1 ? 4 
ATOM   14087 O O     . GLU D 1 382 ? 66.162  13.428  81.198  1.000 30.000  0 382 GLU DDD O     1 ? 4 
ATOM   14088 C CB    . GLU D 1 382 ? 68.126  13.439  78.504  1.000 29.255  0 382 GLU DDD CB    1 ? 4 
ATOM   14089 C CG    . GLU D 1 382 ? 69.038  12.480  77.781  1.000 30.224  0 382 GLU DDD CG    1 ? 4 
ATOM   14090 C CD    . GLU D 1 382 ? 69.039  12.596  76.261  1.000 31.530  0 382 GLU DDD CD    1 ? 4 
ATOM   14091 O OE1   . GLU D 1 382 ? 68.045  13.185  75.685  1.000 30.244  0 382 GLU DDD OE1   1 ? 4 
ATOM   14092 O OE2   . GLU D 1 382 ? 70.047  12.079  75.633  1.000 32.419  0 382 GLU DDD OE2   1 ? 4 
ATOM   14093 N N     . TYR D 1 383 ? 67.203  15.410  80.758  1.000 27.944  0 383 TYR DDD N     1 ? 4 
ATOM   14094 C CA    . TYR D 1 383 ? 66.150  16.234  81.389  1.000 29.837  0 383 TYR DDD CA    1 ? 4 
ATOM   14095 C C     . TYR D 1 383 ? 65.871  17.427  80.486  1.000 29.210  0 383 TYR DDD C     1 ? 4 
ATOM   14096 O O     . TYR D 1 383 ? 66.772  18.262  80.265  1.000 28.291  0 383 TYR DDD O     1 ? 4 
ATOM   14097 C CB    . TYR D 1 383 ? 66.534  16.597  82.834  1.000 30.869  0 383 TYR DDD CB    1 ? 4 
ATOM   14098 C CG    . TYR D 1 383 ? 65.650  17.653  83.442  1.000 31.943  0 383 TYR DDD CG    1 ? 4 
ATOM   14099 C CD1   . TYR D 1 383 ? 64.275  17.610  83.258  1.000 31.886  0 383 TYR DDD CD1   1 ? 4 
ATOM   14100 C CD2   . TYR D 1 383 ? 66.178  18.697  84.174  1.000 32.619  0 383 TYR DDD CD2   1 ? 4 
ATOM   14101 C CE1   . TYR D 1 383 ? 63.447  18.596  83.754  1.000 33.217  0 383 TYR DDD CE1   1 ? 4 
ATOM   14102 C CE2   . TYR D 1 383 ? 65.357  19.709  84.665  1.000 33.752  0 383 TYR DDD CE2   1 ? 4 
ATOM   14103 C CZ    . TYR D 1 383 ? 63.987  19.644  84.470  1.000 33.973  0 383 TYR DDD CZ    1 ? 4 
ATOM   14104 O OH    . TYR D 1 383 ? 63.167  20.602  84.970  1.000 35.116  0 383 TYR DDD OH    1 ? 4 
ATOM   14105 N N     . GLY D 1 384 ? 64.664  17.453  79.946  1.000 28.805  0 384 GLY DDD N     1 ? 4 
ATOM   14106 C CA    . GLY D 1 384 ? 64.220  18.546  79.074  1.000 29.708  0 384 GLY DDD CA    1 ? 4 
ATOM   14107 C C     . GLY D 1 384 ? 63.083  19.289  79.729  1.000 30.734  0 384 GLY DDD C     1 ? 4 
ATOM   14108 O O     . GLY D 1 384 ? 62.217  18.607  80.353  1.000 30.766  0 384 GLY DDD O     1 ? 4 
ATOM   14109 N N     . HIS D 1 385 ? 63.080  20.615  79.624  1.000 31.730  0 385 HIS DDD N     1 ? 4 
ATOM   14110 C CA    . HIS D 1 385 ? 62.008  21.442  80.231  1.000 37.314  0 385 HIS DDD CA    1 ? 4 
ATOM   14111 C C     . HIS D 1 385 ? 61.857  22.747  79.458  1.000 38.047  0 385 HIS DDD C     1 ? 4 
ATOM   14112 O O     . HIS D 1 385 ? 62.827  23.144  78.754  1.000 37.265  0 385 HIS DDD O     1 ? 4 
ATOM   14113 C CB    . HIS D 1 385 ? 62.257  21.687  81.743  1.000 41.208  0 385 HIS DDD CB    1 ? 4 
ATOM   14114 C CG    . HIS D 1 385 ? 63.066  22.904  82.042  1.000 44.418  0 385 HIS DDD CG    1 ? 4 
ATOM   14115 N ND1   . HIS D 1 385 ? 62.495  24.138  82.361  1.000 49.586  0 385 HIS DDD ND1   1 ? 4 
ATOM   14116 C CD2   . HIS D 1 385 ? 64.415  23.088  82.070  1.000 44.846  0 385 HIS DDD CD2   1 ? 4 
ATOM   14117 C CE1   . HIS D 1 385 ? 63.462  25.029  82.553  1.000 49.463  0 385 HIS DDD CE1   1 ? 4 
ATOM   14118 N NE2   . HIS D 1 385 ? 64.654  24.400  82.371  1.000 44.604  0 385 HIS DDD NE2   1 ? 4 
ATOM   14119 N N     . VAL D 1 386 ? 60.675  23.357  79.582  1.000 35.993  0 386 VAL DDD N     1 ? 4 
ATOM   14120 C CA    . VAL D 1 386 ? 60.431  24.778  79.228  1.000 34.705  0 386 VAL DDD CA    1 ? 4 
ATOM   14121 C C     . VAL D 1 386 ? 59.460  25.353  80.261  1.000 38.276  0 386 VAL DDD C     1 ? 4 
ATOM   14122 O O     . VAL D 1 386 ? 58.612  24.588  80.818  1.000 40.399  0 386 VAL DDD O     1 ? 4 
ATOM   14123 C CB    . VAL D 1 386 ? 59.880  24.920  77.809  1.000 33.145  0 386 VAL DDD CB    1 ? 4 
ATOM   14124 C CG1   . VAL D 1 386 ? 58.462  24.366  77.705  1.000 33.330  0 386 VAL DDD CG1   1 ? 4 
ATOM   14125 C CG2   . VAL D 1 386 ? 59.947  26.360  77.350  1.000 32.141  0 386 VAL DDD CG2   1 ? 4 
ATOM   14126 N N     . GLY D 1 387 ? 59.573  26.658  80.491  1.000 38.813  0 387 GLY DDD N     1 ? 4 
ATOM   14127 C CA    . GLY D 1 387 ? 58.788  27.396  81.482  1.000 42.310  0 387 GLY DDD CA    1 ? 4 
ATOM   14128 C C     . GLY D 1 387 ? 59.283  27.114  82.877  1.000 44.308  0 387 GLY DDD C     1 ? 4 
ATOM   14129 O O     . GLY D 1 387 ? 60.483  26.898  83.050  1.000 44.355  0 387 GLY DDD O     1 ? 4 
ATOM   14130 N N     . LEU D 1 388 ? 58.366  27.092  83.839  1.000 48.362  0 388 LEU DDD N     1 ? 4 
ATOM   14131 C CA    . LEU D 1 388 ? 58.701  27.212  85.282  1.000 51.102  0 388 LEU DDD CA    1 ? 4 
ATOM   14132 C C     . LEU D 1 388 ? 58.814  25.826  85.908  1.000 50.196  0 388 LEU DDD C     1 ? 4 
ATOM   14133 O O     . LEU D 1 388 ? 58.007  24.933  85.564  1.000 45.714  0 388 LEU DDD O     1 ? 4 
ATOM   14134 C CB    . LEU D 1 388 ? 57.615  28.050  85.976  1.000 55.780  0 388 LEU DDD CB    1 ? 4 
ATOM   14135 C CG    . LEU D 1 388 ? 57.319  29.399  85.321  1.000 57.824  0 388 LEU DDD CG    1 ? 4 
ATOM   14136 C CD1   . LEU D 1 388 ? 56.076  30.044  85.943  1.000 58.503  0 388 LEU DDD CD1   1 ? 4 
ATOM   14137 C CD2   . LEU D 1 388 ? 58.568  30.299  85.386  1.000 57.058  0 388 LEU DDD CD2   1 ? 4 
ATOM   14138 N N     . SER D 1 389 ? 59.778  25.685  86.815  1.000 53.983  0 389 SER DDD N     1 ? 4 
ATOM   14139 C CA    . SER D 1 389 ? 59.826  24.610  87.832  1.000 53.184  0 389 SER DDD CA    1 ? 4 
ATOM   14140 C C     . SER D 1 389 ? 58.566  24.690  88.702  1.000 54.616  0 389 SER DDD C     1 ? 4 
ATOM   14141 O O     . SER D 1 389 ? 57.881  25.732  88.684  1.000 54.205  0 389 SER DDD O     1 ? 4 
ATOM   14142 C CB    . SER D 1 389 ? 61.067  24.743  88.652  1.000 55.618  0 389 SER DDD CB    1 ? 4 
ATOM   14143 O OG    . SER D 1 389 ? 61.086  26.011  89.298  1.000 57.247  0 389 SER DDD OG    1 ? 4 
ATOM   14144 N N     . SER D 1 390 ? 58.258  23.608  89.416  1.000 55.841  0 390 SER DDD N     1 ? 4 
ATOM   14145 C CA    . SER D 1 390 ? 57.268  23.571  90.517  1.000 57.117  0 390 SER DDD CA    1 ? 4 
ATOM   14146 C C     . SER D 1 390 ? 57.548  24.748  91.464  1.000 60.061  0 390 SER DDD C     1 ? 4 
ATOM   14147 O O     . SER D 1 390 ? 56.607  25.499  91.761  1.000 63.074  0 390 SER DDD O     1 ? 4 
ATOM   14148 C CB    . SER D 1 390 ? 57.312  22.242  91.225  1.000 56.586  0 390 SER DDD CB    1 ? 4 
ATOM   14149 O OG    . SER D 1 390 ? 57.020  21.180  90.330  1.000 55.835  0 390 SER DDD OG    1 ? 4 
ATOM   14150 N N     . GLU D 1 391 ? 58.815  24.959  91.840  1.000 60.785  0 391 GLU DDD N     1 ? 4 
ATOM   14151 C CA    . GLU D 1 391 ? 59.240  25.982  92.839  1.000 60.752  0 391 GLU DDD CA    1 ? 4 
ATOM   14152 C C     . GLU D 1 391 ? 58.913  27.382  92.300  1.000 63.046  0 391 GLU DDD C     1 ? 4 
ATOM   14153 O O     . GLU D 1 391 ? 58.237  28.154  93.032  1.000 66.263  0 391 GLU DDD O     1 ? 4 
ATOM   14154 C CB    . GLU D 1 391 ? 60.721  25.821  93.202  1.000 59.107  0 391 GLU DDD CB    1 ? 4 
ATOM   14155 C CG    . GLU D 1 391 ? 61.012  24.588  94.050  1.000 58.729  0 391 GLU DDD CG    1 ? 4 
ATOM   14156 C CD    . GLU D 1 391 ? 60.958  23.245  93.307  1.000 58.902  0 391 GLU DDD CD    1 ? 4 
ATOM   14157 O OE1   . GLU D 1 391 ? 61.412  23.164  92.118  1.000 51.679  0 391 GLU DDD OE1   1 ? 4 
ATOM   14158 O OE2   . GLU D 1 391 ? 60.446  22.274  93.901  1.000 54.470  0 391 GLU DDD OE2   1 ? 4 
ATOM   14159 N N     . ALA D 1 392 ? 59.352  27.717  91.082  1.000 61.837  0 392 ALA DDD N     1 ? 4 
ATOM   14160 C CA    . ALA D 1 392 ? 59.104  29.052  90.485  1.000 61.013  0 392 ALA DDD CA    1 ? 4 
ATOM   14161 C C     . ALA D 1 392 ? 57.594  29.241  90.258  1.000 61.024  0 392 ALA DDD C     1 ? 4 
ATOM   14162 O O     . ALA D 1 392 ? 57.138  30.391  90.309  1.000 60.808  0 392 ALA DDD O     1 ? 4 
ATOM   14163 C CB    . ALA D 1 392 ? 59.901  29.240  89.211  1.000 57.066  0 392 ALA DDD CB    1 ? 4 
ATOM   14164 N N     . ALA D 1 393 ? 56.843  28.160  90.011  1.000 61.457  0 393 ALA DDD N     1 ? 4 
ATOM   14165 C CA    . ALA D 1 393 ? 55.383  28.203  89.753  1.000 59.755  0 393 ALA DDD CA    1 ? 4 
ATOM   14166 C C     . ALA D 1 393 ? 54.644  28.514  91.059  1.000 59.957  0 393 ALA DDD C     1 ? 4 
ATOM   14167 O O     . ALA D 1 393 ? 53.789  29.416  91.052  1.000 56.071  0 393 ALA DDD O     1 ? 4 
ATOM   14168 C CB    . ALA D 1 393 ? 54.917  26.906  89.146  1.000 57.131  0 393 ALA DDD CB    1 ? 4 
ATOM   14169 N N     . ILE D 1 394 ? 54.987  27.790  92.128  1.000 61.737  0 394 ILE DDD N     1 ? 4 
ATOM   14170 C CA    . ILE D 1 394 ? 54.423  27.989  93.494  1.000 66.620  0 394 ILE DDD CA    1 ? 4 
ATOM   14171 C C     . ILE D 1 394 ? 54.736  29.427  93.971  1.000 67.534  0 394 ILE DDD C     1 ? 4 
ATOM   14172 O O     . ILE D 1 394 ? 53.791  30.124  94.361  1.000 60.386  0 394 ILE DDD O     1 ? 4 
ATOM   14173 C CB    . ILE D 1 394 ? 54.912  26.868  94.438  1.000 68.272  0 394 ILE DDD CB    1 ? 4 
ATOM   14174 C CG1   . ILE D 1 394 ? 54.208  25.547  94.109  1.000 67.173  0 394 ILE DDD CG1   1 ? 4 
ATOM   14175 C CG2   . ILE D 1 394 ? 54.728  27.266  95.900  1.000 70.951  0 394 ILE DDD CG2   1 ? 4 
ATOM   14176 C CD1   . ILE D 1 394 ? 54.712  24.343  94.882  1.000 66.856  0 394 ILE DDD CD1   1 ? 4 
ATOM   14177 N N     . ALA D 1 395 ? 55.987  29.887  93.843  1.000 72.494  0 395 ALA DDD N     1 ? 4 
ATOM   14178 C CA    . ALA D 1 395 ? 56.443  31.249  94.222  1.000 74.025  0 395 ALA DDD CA    1 ? 4 
ATOM   14179 C C     . ALA D 1 395 ? 55.626  32.324  93.481  1.000 75.921  0 395 ALA DDD C     1 ? 4 
ATOM   14180 O O     . ALA D 1 395 ? 55.246  33.316  94.137  1.000 83.928  0 395 ALA DDD O     1 ? 4 
ATOM   14181 C CB    . ALA D 1 395 ? 57.931  31.414  93.965  1.000 70.575  0 395 ALA DDD CB    1 ? 4 
ATOM   14182 N N     . LYS D 1 396 ? 55.361  32.154  92.181  1.000 71.640  0 396 LYS DDD N     1 ? 4 
ATOM   14183 C CA    . LYS D 1 396 ? 54.774  33.214  91.313  1.000 70.627  0 396 LYS DDD CA    1 ? 4 
ATOM   14184 C C     . LYS D 1 396 ? 53.246  33.276  91.472  1.000 69.105  0 396 LYS DDD C     1 ? 4 
ATOM   14185 O O     . LYS D 1 396 ? 52.731  34.408  91.503  1.000 70.043  0 396 LYS DDD O     1 ? 4 
ATOM   14186 C CB    . LYS D 1 396 ? 55.143  32.995  89.844  1.000 68.213  0 396 LYS DDD CB    1 ? 4 
ATOM   14187 C CG    . LYS D 1 396 ? 54.659  34.063  88.871  1.000 68.713  0 396 LYS DDD CG    1 ? 4 
ATOM   14188 C CD    . LYS D 1 396 ? 54.950  33.692  87.432  1.000 68.271  0 396 LYS DDD CD    1 ? 4 
ATOM   14189 C CE    . LYS D 1 396 ? 54.258  34.564  86.403  1.000 68.764  0 396 LYS DDD CE    1 ? 4 
ATOM   14190 N NZ    . LYS D 1 396 ? 54.807  35.936  86.385  1.000 67.855  0 396 LYS DDD NZ    1 ? 4 
ATOM   14191 N N     . TYR D 1 397 ? 52.548  32.134  91.545  1.000 66.411  0 397 TYR DDD N     1 ? 4 
ATOM   14192 C CA    . TYR D 1 397 ? 51.056  32.062  91.490  1.000 66.849  0 397 TYR DDD CA    1 ? 4 
ATOM   14193 C C     . TYR D 1 397 ? 50.455  31.683  92.853  1.000 66.761  0 397 TYR DDD C     1 ? 4 
ATOM   14194 O O     . TYR D 1 397 ? 49.247  31.871  93.005  1.000 67.524  0 397 TYR DDD O     1 ? 4 
ATOM   14195 C CB    . TYR D 1 397 ? 50.597  31.089  90.395  1.000 64.763  0 397 TYR DDD CB    1 ? 4 
ATOM   14196 C CG    . TYR D 1 397 ? 50.900  31.556  88.994  1.000 62.383  0 397 TYR DDD CG    1 ? 4 
ATOM   14197 C CD1   . TYR D 1 397 ? 50.170  32.568  88.395  1.000 63.072  0 397 TYR DDD CD1   1 ? 4 
ATOM   14198 C CD2   . TYR D 1 397 ? 51.937  31.000  88.267  1.000 59.201  0 397 TYR DDD CD2   1 ? 4 
ATOM   14199 C CE1   . TYR D 1 397 ? 50.466  33.016  87.115  1.000 61.411  0 397 TYR DDD CE1   1 ? 4 
ATOM   14200 C CE2   . TYR D 1 397 ? 52.253  31.442  86.998  1.000 57.211  0 397 TYR DDD CE2   1 ? 4 
ATOM   14201 C CZ    . TYR D 1 397 ? 51.517  32.448  86.414  1.000 60.035  0 397 TYR DDD CZ    1 ? 4 
ATOM   14202 O OH    . TYR D 1 397 ? 51.847  32.850  85.147  1.000 58.660  0 397 TYR DDD OH    1 ? 4 
ATOM   14203 N N     . GLY D 1 398 ? 51.264  31.166  93.785  1.000 68.307  0 398 GLY DDD N     1 ? 4 
ATOM   14204 C CA    . GLY D 1 398 ? 50.816  30.594  95.070  1.000 68.548  0 398 GLY DDD CA    1 ? 4 
ATOM   14205 C C     . GLY D 1 398 ? 50.467  29.116  94.968  1.000 68.396  0 398 GLY DDD C     1 ? 4 
ATOM   14206 O O     . GLY D 1 398 ? 49.925  28.725  93.957  1.000 67.107  0 398 GLY DDD O     1 ? 4 
ATOM   14207 N N     . GLU D 1 399 ? 50.729  28.356  96.032  1.000 77.648  0 399 GLU DDD N     1 ? 4 
ATOM   14208 C CA    . GLU D 1 399 ? 50.536  26.885  96.175  1.000 82.014  0 399 GLU DDD CA    1 ? 4 
ATOM   14209 C C     . GLU D 1 399 ? 49.138  26.464  95.711  1.000 81.111  0 399 GLU DDD C     1 ? 4 
ATOM   14210 O O     . GLU D 1 399 ? 49.028  25.366  95.144  1.000 81.871  0 399 GLU DDD O     1 ? 4 
ATOM   14211 C CB    . GLU D 1 399 ? 50.743  26.472  97.639  1.000 89.614  0 399 GLU DDD CB    1 ? 4 
ATOM   14212 C CG    . GLU D 1 399 ? 50.655  24.975  97.885  1.000 94.030  0 399 GLU DDD CG    1 ? 4 
ATOM   14213 C CD    . GLU D 1 399 ? 51.863  24.177  97.408  1.000 99.981  0 399 GLU DDD CD    1 ? 4 
ATOM   14214 O OE1   . GLU D 1 399 ? 52.987  24.563  97.765  1.000 103.484 0 399 GLU DDD OE1   1 ? 4 
ATOM   14215 O OE2   . GLU D 1 399 ? 51.682  23.170  96.683  1.000 103.001 0 399 GLU DDD OE2   1 ? 4 
ATOM   14216 N N     . ASP D 1 400 ? 48.099  27.265  95.974  1.000 79.833  0 400 ASP DDD N     1 ? 4 
ATOM   14217 C CA    . ASP D 1 400 ? 46.694  26.829  95.749  1.000 79.023  0 400 ASP DDD CA    1 ? 4 
ATOM   14218 C C     . ASP D 1 400 ? 46.247  27.074  94.308  1.000 73.657  0 400 ASP DDD C     1 ? 4 
ATOM   14219 O O     . ASP D 1 400 ? 45.241  26.460  93.900  1.000 74.171  0 400 ASP DDD O     1 ? 4 
ATOM   14220 C CB    . ASP D 1 400 ? 45.702  27.455  96.730  1.000 81.696  0 400 ASP DDD CB    1 ? 4 
ATOM   14221 C CG    . ASP D 1 400 ? 45.438  26.505  97.889  1.000 83.594  0 400 ASP DDD CG    1 ? 4 
ATOM   14222 O OD1   . ASP D 1 400 ? 46.431  25.920  98.376  1.000 84.049  0 400 ASP DDD OD1   1 ? 4 
ATOM   14223 O OD2   . ASP D 1 400 ? 44.243  26.297  98.241  1.000 82.352  0 400 ASP DDD OD2   1 ? 4 
ATOM   14224 N N     . ASP D 1 401 ? 46.941  27.941  93.586  1.000 68.736  0 401 ASP DDD N     1 ? 4 
ATOM   14225 C CA    . ASP D 1 401 ? 46.628  28.213  92.159  1.000 68.477  0 401 ASP DDD CA    1 ? 4 
ATOM   14226 C C     . ASP D 1 401 ? 47.495  27.303  91.256  1.000 65.452  0 401 ASP DDD C     1 ? 4 
ATOM   14227 O O     . ASP D 1 401 ? 47.421  27.468  90.040  1.000 64.713  0 401 ASP DDD O     1 ? 4 
ATOM   14228 C CB    . ASP D 1 401 ? 46.768  29.707  91.850  1.000 67.314  0 401 ASP DDD CB    1 ? 4 
ATOM   14229 C CG    . ASP D 1 401 ? 45.883  30.187  90.701  1.000 67.340  0 401 ASP DDD CG    1 ? 4 
ATOM   14230 O OD1   . ASP D 1 401 ? 44.885  29.490  90.373  1.000 65.312  0 401 ASP DDD OD1   1 ? 4 
ATOM   14231 O OD2   . ASP D 1 401 ? 46.203  31.255  90.132  1.000 66.539  0 401 ASP DDD OD2   1 ? 4 
ATOM   14232 N N     . ILE D 1 402 ? 48.206  26.319  91.830  1.000 61.402  0 402 ILE DDD N     1 ? 4 
ATOM   14233 C CA    . ILE D 1 402 ? 49.123  25.379  91.117  1.000 58.669  0 402 ILE DDD CA    1 ? 4 
ATOM   14234 C C     . ILE D 1 402 ? 48.626  23.932  91.227  1.000 56.329  0 402 ILE DDD C     1 ? 4 
ATOM   14235 O O     . ILE D 1 402 ? 48.378  23.453  92.346  1.000 52.869  0 402 ILE DDD O     1 ? 4 
ATOM   14236 C CB    . ILE D 1 402 ? 50.565  25.510  91.657  1.000 60.390  0 402 ILE DDD CB    1 ? 4 
ATOM   14237 C CG1   . ILE D 1 402 ? 51.204  26.843  91.257  1.000 61.166  0 402 ILE DDD CG1   1 ? 4 
ATOM   14238 C CG2   . ILE D 1 402 ? 51.424  24.330  91.231  1.000 58.660  0 402 ILE DDD CG2   1 ? 4 
ATOM   14239 C CD1   . ILE D 1 402 ? 51.040  27.198  89.789  1.000 61.010  0 402 ILE DDD CD1   1 ? 4 
ATOM   14240 N N     . GLU D 1 403 ? 48.545  23.236  90.095  1.000 55.601  0 403 GLU DDD N     1 ? 4 
ATOM   14241 C CA    . GLU D 1 403 ? 48.428  21.753  90.070  1.000 60.151  0 403 GLU DDD CA    1 ? 4 
ATOM   14242 C C     . GLU D 1 403 ? 49.669  21.186  89.370  1.000 56.339  0 403 GLU DDD C     1 ? 4 
ATOM   14243 O O     . GLU D 1 403 ? 50.084  21.741  88.328  1.000 55.186  0 403 GLU DDD O     1 ? 4 
ATOM   14244 C CB    . GLU D 1 403 ? 47.121  21.309  89.401  1.000 63.834  0 403 GLU DDD CB    1 ? 4 
ATOM   14245 C CG    . GLU D 1 403 ? 46.554  20.013  89.951  1.000 67.519  0 403 GLU DDD CG    1 ? 4 
ATOM   14246 C CD    . GLU D 1 403 ? 45.973  20.101  91.357  1.000 70.361  0 403 GLU DDD CD    1 ? 4 
ATOM   14247 O OE1   . GLU D 1 403 ? 44.996  20.811  91.518  1.000 73.456  0 403 GLU DDD OE1   1 ? 4 
ATOM   14248 O OE2   . GLU D 1 403 ? 46.474  19.414  92.268  1.000 70.793  0 403 GLU DDD OE2   1 ? 4 
ATOM   14249 N N     . GLU D 1 404 ? 50.242  20.122  89.923  1.000 55.404  0 404 GLU DDD N     1 ? 4 
ATOM   14250 C CA    . GLU D 1 404 ? 51.326  19.333  89.283  1.000 52.973  0 404 GLU DDD CA    1 ? 4 
ATOM   14251 C C     . GLU D 1 404 ? 50.781  17.945  88.963  1.000 49.923  0 404 GLU DDD C     1 ? 4 
ATOM   14252 O O     . GLU D 1 404 ? 50.461  17.201  89.885  1.000 47.465  0 404 GLU DDD O     1 ? 4 
ATOM   14253 C CB    . GLU D 1 404 ? 52.565  19.272  90.172  1.000 58.081  0 404 GLU DDD CB    1 ? 4 
ATOM   14254 C CG    . GLU D 1 404 ? 53.027  20.643  90.615  1.000 61.551  0 404 GLU DDD CG    1 ? 4 
ATOM   14255 C CD    . GLU D 1 404 ? 54.079  20.619  91.700  1.000 63.681  0 404 GLU DDD CD    1 ? 4 
ATOM   14256 O OE1   . GLU D 1 404 ? 54.979  19.739  91.646  1.000 60.284  0 404 GLU DDD OE1   1 ? 4 
ATOM   14257 O OE2   . GLU D 1 404 ? 53.982  21.487  92.594  1.000 68.175  0 404 GLU DDD OE2   1 ? 4 
ATOM   14258 N N     . TYR D 1 405 ? 50.670  17.641  87.670  1.000 49.291  0 405 TYR DDD N     1 ? 4 
ATOM   14259 C CA    . TYR D 1 405 ? 50.326  16.297  87.148  1.000 46.220  0 405 TYR DDD CA    1 ? 4 
ATOM   14260 C C     . TYR D 1 405 ? 51.628  15.603  86.742  1.000 44.608  0 405 TYR DDD C     1 ? 4 
ATOM   14261 O O     . TYR D 1 405 ? 52.473  16.245  86.131  1.000 42.663  0 405 TYR DDD O     1 ? 4 
ATOM   14262 C CB    . TYR D 1 405 ? 49.372  16.431  85.972  1.000 45.287  0 405 TYR DDD CB    1 ? 4 
ATOM   14263 C CG    . TYR D 1 405 ? 48.004  16.989  86.286  1.000 45.498  0 405 TYR DDD CG    1 ? 4 
ATOM   14264 C CD1   . TYR D 1 405 ? 46.948  16.140  86.564  1.000 45.559  0 405 TYR DDD CD1   1 ? 4 
ATOM   14265 C CD2   . TYR D 1 405 ? 47.743  18.345  86.225  1.000 45.530  0 405 TYR DDD CD2   1 ? 4 
ATOM   14266 C CE1   . TYR D 1 405 ? 45.673  16.613  86.801  1.000 46.832  0 405 TYR DDD CE1   1 ? 4 
ATOM   14267 C CE2   . TYR D 1 405 ? 46.470  18.842  86.473  1.000 48.484  0 405 TYR DDD CE2   1 ? 4 
ATOM   14268 C CZ    . TYR D 1 405 ? 45.431  17.971  86.767  1.000 48.252  0 405 TYR DDD CZ    1 ? 4 
ATOM   14269 O OH    . TYR D 1 405 ? 44.165  18.434  86.980  1.000 49.757  0 405 TYR DDD OH    1 ? 4 
ATOM   14270 N N     . LEU D 1 406 ? 51.801  14.350  87.125  1.000 42.946  0 406 LEU DDD N     1 ? 4 
ATOM   14271 C CA    . LEU D 1 406 ? 53.065  13.653  86.884  1.000 43.191  0 406 LEU DDD CA    1 ? 4 
ATOM   14272 C C     . LEU D 1 406 ? 52.862  12.141  86.863  1.000 43.661  0 406 LEU DDD C     1 ? 4 
ATOM   14273 O O     . LEU D 1 406 ? 51.809  11.630  87.297  1.000 41.748  0 406 LEU DDD O     1 ? 4 
ATOM   14274 C CB    . LEU D 1 406 ? 54.137  14.107  87.887  1.000 42.874  0 406 LEU DDD CB    1 ? 4 
ATOM   14275 C CG    . LEU D 1 406 ? 54.055  13.631  89.334  1.000 43.965  0 406 LEU DDD CG    1 ? 4 
ATOM   14276 C CD1   . LEU D 1 406 ? 55.316  14.041  90.075  1.000 43.256  0 406 LEU DDD CD1   1 ? 4 
ATOM   14277 C CD2   . LEU D 1 406 ? 52.839  14.200  90.066  1.000 44.671  0 406 LEU DDD CD2   1 ? 4 
ATOM   14278 N N     . SER D 1 407 ? 53.820  11.491  86.214  1.000 41.994  0 407 SER DDD N     1 ? 4 
ATOM   14279 C CA    . SER D 1 407 ? 53.896  10.024  86.077  1.000 42.855  0 407 SER DDD CA    1 ? 4 
ATOM   14280 C C     . SER D 1 407 ? 55.376  9.631   86.010  1.000 42.510  0 407 SER DDD C     1 ? 4 
ATOM   14281 O O     . SER D 1 407 ? 56.141  10.328  85.333  1.000 43.258  0 407 SER DDD O     1 ? 4 
ATOM   14282 C CB    . SER D 1 407 ? 53.110  9.572   84.881  1.000 41.108  0 407 SER DDD CB    1 ? 4 
ATOM   14283 O OG    . SER D 1 407 ? 53.205  8.167   84.728  1.000 41.101  0 407 SER DDD OG    1 ? 4 
ATOM   14284 N N     . GLU D 1 408 ? 55.773  8.614   86.768  1.000 42.653  0 408 GLU DDD N     1 ? 4 
ATOM   14285 C CA    . GLU D 1 408 ? 57.122  8.018   86.763  1.000 42.343  0 408 GLU DDD CA    1 ? 4 
ATOM   14286 C C     . GLU D 1 408 ? 56.964  6.605   86.238  1.000 41.153  0 408 GLU DDD C     1 ? 4 
ATOM   14287 O O     . GLU D 1 408 ? 56.127  5.877   86.764  1.000 39.605  0 408 GLU DDD O     1 ? 4 
ATOM   14288 C CB    . GLU D 1 408 ? 57.718  7.994   88.163  1.000 45.285  0 408 GLU DDD CB    1 ? 4 
ATOM   14289 C CG    . GLU D 1 408 ? 59.206  7.702   88.211  1.000 47.358  0 408 GLU DDD CG    1 ? 4 
ATOM   14290 C CD    . GLU D 1 408 ? 59.824  7.932   89.577  1.000 50.028  0 408 GLU DDD CD    1 ? 4 
ATOM   14291 O OE1   . GLU D 1 408 ? 59.089  7.822   90.573  1.000 55.659  0 408 GLU DDD OE1   1 ? 4 
ATOM   14292 O OE2   . GLU D 1 408 ? 61.029  8.264   89.646  1.000 54.636  0 408 GLU DDD OE2   1 ? 4 
ATOM   14293 N N     . PHE D 1 409 ? 57.746  6.239   85.229  1.000 39.555  0 409 PHE DDD N     1 ? 4 
ATOM   14294 C CA    . PHE D 1 409 ? 57.578  4.949   84.528  1.000 36.530  0 409 PHE DDD CA    1 ? 4 
ATOM   14295 C C     . PHE D 1 409 ? 58.862  4.606   83.790  1.000 35.909  0 409 PHE DDD C     1 ? 4 
ATOM   14296 O O     . PHE D 1 409 ? 59.808  5.415   83.715  1.000 33.139  0 409 PHE DDD O     1 ? 4 
ATOM   14297 C CB    . PHE D 1 409 ? 56.467  5.045   83.493  1.000 36.042  0 409 PHE DDD CB    1 ? 4 
ATOM   14298 C CG    . PHE D 1 409 ? 56.715  6.118   82.470  1.000 33.838  0 409 PHE DDD CG    1 ? 4 
ATOM   14299 C CD1   . PHE D 1 409 ? 56.515  7.448   82.791  1.000 32.879  0 409 PHE DDD CD1   1 ? 4 
ATOM   14300 C CD2   . PHE D 1 409 ? 57.170  5.791   81.199  1.000 33.334  0 409 PHE DDD CD2   1 ? 4 
ATOM   14301 C CE1   . PHE D 1 409 ? 56.731  8.439   81.850  1.000 33.592  0 409 PHE DDD CE1   1 ? 4 
ATOM   14302 C CE2   . PHE D 1 409 ? 57.426  6.779   80.263  1.000 32.482  0 409 PHE DDD CE2   1 ? 4 
ATOM   14303 C CZ    . PHE D 1 409 ? 57.179  8.103   80.581  1.000 34.357  0 409 PHE DDD CZ    1 ? 4 
ATOM   14304 N N     . SER D 1 410 ? 58.849  3.418   83.212  1.000 34.149  0 410 SER DDD N     1 ? 4 
ATOM   14305 C CA    . SER D 1 410 ? 59.969  2.909   82.411  1.000 32.814  0 410 SER DDD CA    1 ? 4 
ATOM   14306 C C     . SER D 1 410 ? 59.589  2.945   80.931  1.000 32.256  0 410 SER DDD C     1 ? 4 
ATOM   14307 O O     . SER D 1 410 ? 58.448  2.637   80.610  1.000 32.161  0 410 SER DDD O     1 ? 4 
ATOM   14308 C CB    . SER D 1 410 ? 60.324  1.558   82.848  1.000 32.775  0 410 SER DDD CB    1 ? 4 
ATOM   14309 O OG    . SER D 1 410 ? 61.299  1.049   81.965  1.000 32.844  0 410 SER DDD OG    1 ? 4 
ATOM   14310 N N     . THR D 1 411 ? 60.502  3.401   80.082  1.000 32.091  0 411 THR DDD N     1 ? 4 
ATOM   14311 C CA    . THR D 1 411 ? 60.510  3.080   78.634  1.000 31.024  0 411 THR DDD CA    1 ? 4 
ATOM   14312 C C     . THR D 1 411 ? 60.203  1.591   78.498  1.000 29.976  0 411 THR DDD C     1 ? 4 
ATOM   14313 O O     . THR D 1 411 ? 60.718  0.808   79.329  1.000 29.437  0 411 THR DDD O     1 ? 4 
ATOM   14314 C CB    . THR D 1 411 ? 61.861  3.452   77.996  1.000 31.641  0 411 THR DDD CB    1 ? 4 
ATOM   14315 O OG1   . THR D 1 411 ? 62.078  4.835   78.284  1.000 30.345  0 411 THR DDD OG1   1 ? 4 
ATOM   14316 C CG2   . THR D 1 411 ? 61.910  3.241   76.488  1.000 32.223  0 411 THR DDD CG2   1 ? 4 
ATOM   14317 N N     . LEU D 1 412 ? 59.376  1.238   77.514  1.000 30.957  0 412 LEU DDD N     1 ? 4 
ATOM   14318 C CA    . LEU D 1 412 ? 59.024  -0.159  77.150  1.000 32.875  0 412 LEU DDD CA    1 ? 4 
ATOM   14319 C C     . LEU D 1 412 ? 60.285  -1.016  76.976  1.000 33.179  0 412 LEU DDD C     1 ? 4 
ATOM   14320 O O     . LEU D 1 412 ? 60.379  -2.064  77.615  1.000 36.588  0 412 LEU DDD O     1 ? 4 
ATOM   14321 C CB    . LEU D 1 412 ? 58.239  -0.067  75.844  1.000 34.648  0 412 LEU DDD CB    1 ? 4 
ATOM   14322 C CG    . LEU D 1 412 ? 57.845  -1.395  75.196  1.000 35.488  0 412 LEU DDD CG    1 ? 4 
ATOM   14323 C CD1   . LEU D 1 412 ? 57.115  -2.265  76.193  1.000 36.797  0 412 LEU DDD CD1   1 ? 4 
ATOM   14324 C CD2   . LEU D 1 412 ? 56.957  -1.151  73.984  1.000 33.115  0 412 LEU DDD CD2   1 ? 4 
ATOM   14325 N N     . GLU D 1 413 ? 61.211  -0.587  76.118  1.000 33.038  0 413 GLU DDD N     1 ? 4 
ATOM   14326 C CA    . GLU D 1 413 ? 62.424  -1.351  75.721  1.000 33.079  0 413 GLU DDD CA    1 ? 4 
ATOM   14327 C C     . GLU D 1 413 ? 63.313  -1.554  76.949  1.000 31.952  0 413 GLU DDD C     1 ? 4 
ATOM   14328 O O     . GLU D 1 413 ? 63.833  -2.650  77.151  1.000 29.535  0 413 GLU DDD O     1 ? 4 
ATOM   14329 C CB    . GLU D 1 413 ? 63.240  -0.578  74.693  1.000 35.073  0 413 GLU DDD CB    1 ? 4 
ATOM   14330 C CG    . GLU D 1 413 ? 62.445  -0.230  73.434  1.000 38.457  0 413 GLU DDD CG    1 ? 4 
ATOM   14331 C CD    . GLU D 1 413 ? 61.811  1.147   73.411  1.000 39.113  0 413 GLU DDD CD    1 ? 4 
ATOM   14332 O OE1   . GLU D 1 413 ? 60.978  1.398   74.298  1.000 43.255  0 413 GLU DDD OE1   1 ? 4 
ATOM   14333 O OE2   . GLU D 1 413 ? 62.187  1.976   72.546  1.000 39.688  0 413 GLU DDD OE2   1 ? 4 
ATOM   14334 N N     . ILE D 1 414 ? 63.490  -0.494  77.734  1.000 30.812  0 414 ILE DDD N     1 ? 4 
ATOM   14335 C CA    . ILE D 1 414 ? 64.276  -0.557  78.988  1.000 30.895  0 414 ILE DDD CA    1 ? 4 
ATOM   14336 C C     . ILE D 1 414 ? 63.576  -1.496  79.976  1.000 30.110  0 414 ILE DDD C     1 ? 4 
ATOM   14337 O O     . ILE D 1 414 ? 64.255  -2.338  80.564  1.000 29.913  0 414 ILE DDD O     1 ? 4 
ATOM   14338 C CB    . ILE D 1 414 ? 64.500  0.844   79.568  1.000 32.362  0 414 ILE DDD CB    1 ? 4 
ATOM   14339 C CG1   . ILE D 1 414 ? 64.979  1.803   78.469  1.000 32.160  0 414 ILE DDD CG1   1 ? 4 
ATOM   14340 C CG2   . ILE D 1 414 ? 65.468  0.781   80.758  1.000 32.688  0 414 ILE DDD CG2   1 ? 4 
ATOM   14341 C CD1   . ILE D 1 414 ? 66.349  1.531   77.975  1.000 31.554  0 414 ILE DDD CD1   1 ? 4 
ATOM   14342 N N     . ALA D 1 415 ? 62.259  -1.402  80.121  1.000 31.031  0 415 ALA DDD N     1 ? 4 
ATOM   14343 C CA    . ALA D 1 415 ? 61.510  -2.280  81.034  1.000 31.676  0 415 ALA DDD CA    1 ? 4 
ATOM   14344 C C     . ALA D 1 415 ? 61.841  -3.735  80.683  1.000 33.571  0 415 ALA DDD C     1 ? 4 
ATOM   14345 O O     . ALA D 1 415 ? 62.135  -4.498  81.627  1.000 33.186  0 415 ALA DDD O     1 ? 4 
ATOM   14346 C CB    . ALA D 1 415 ? 60.027  -1.999  80.989  1.000 32.105  0 415 ALA DDD CB    1 ? 4 
ATOM   14347 N N     . ALA D 1 416 ? 61.803  -4.112  79.395  1.000 33.066  0 416 ALA DDD N     1 ? 4 
ATOM   14348 C CA    . ALA D 1 416 ? 61.989  -5.504  78.935  1.000 34.162  0 416 ALA DDD CA    1 ? 4 
ATOM   14349 C C     . ALA D 1 416 ? 63.456  -5.960  79.113  1.000 35.784  0 416 ALA DDD C     1 ? 4 
ATOM   14350 O O     . ALA D 1 416 ? 63.712  -7.200  79.197  1.000 38.283  0 416 ALA DDD O     1 ? 4 
ATOM   14351 C CB    . ALA D 1 416 ? 61.542  -5.596  77.498  1.000 34.303  0 416 ALA DDD CB    1 ? 4 
ATOM   14352 N N     . ALA D 1 417 ? 64.402  -5.023  79.196  1.000 35.075  0 417 ALA DDD N     1 ? 4 
ATOM   14353 C CA    . ALA D 1 417 ? 65.849  -5.317  79.368  1.000 35.950  0 417 ALA DDD CA    1 ? 4 
ATOM   14354 C C     . ALA D 1 417 ? 66.146  -5.750  80.807  1.000 38.165  0 417 ALA DDD C     1 ? 4 
ATOM   14355 O O     . ALA D 1 417 ? 67.123  -6.460  81.001  1.000 38.366  0 417 ALA DDD O     1 ? 4 
ATOM   14356 C CB    . ALA D 1 417 ? 66.684  -4.105  78.989  1.000 34.499  0 417 ALA DDD CB    1 ? 4 
ATOM   14357 N N     . HIS D 1 418 ? 65.356  -5.315  81.804  1.000 41.373  0 418 HIS DDD N     1 ? 4 
ATOM   14358 C CA    . HIS D 1 418 ? 65.580  -5.623  83.246  1.000 40.794  0 418 HIS DDD CA    1 ? 4 
ATOM   14359 C C     . HIS D 1 418 ? 66.975  -5.121  83.618  1.000 40.738  0 418 HIS DDD C     1 ? 4 
ATOM   14360 O O     . HIS D 1 418 ? 67.788  -5.928  84.069  1.000 41.600  0 418 HIS DDD O     1 ? 4 
ATOM   14361 C CB    . HIS D 1 418 ? 65.381  -7.122  83.544  1.000 42.035  0 418 HIS DDD CB    1 ? 4 
ATOM   14362 C CG    . HIS D 1 418 ? 63.959  -7.571  83.473  1.000 44.171  0 418 HIS DDD CG    1 ? 4 
ATOM   14363 N ND1   . HIS D 1 418 ? 63.046  -7.354  84.490  1.000 44.743  0 418 HIS DDD ND1   1 ? 4 
ATOM   14364 C CD2   . HIS D 1 418 ? 63.269  -8.206  82.499  1.000 45.754  0 418 HIS DDD CD2   1 ? 4 
ATOM   14365 C CE1   . HIS D 1 418 ? 61.859  -7.812  84.128  1.000 44.463  0 418 HIS DDD CE1   1 ? 4 
ATOM   14366 N NE2   . HIS D 1 418 ? 61.968  -8.355  82.938  1.000 43.283  0 418 HIS DDD NE2   1 ? 4 
ATOM   14367 N N     . ARG D 1 419 ? 67.231  -3.828  83.410  1.000 39.639  0 419 ARG DDD N     1 ? 4 
ATOM   14368 C CA    . ARG D 1 419 ? 68.497  -3.151  83.769  1.000 40.996  0 419 ARG DDD CA    1 ? 4 
ATOM   14369 C C     . ARG D 1 419 ? 68.717  -3.270  85.285  1.000 45.255  0 419 ARG DDD C     1 ? 4 
ATOM   14370 O O     . ARG D 1 419 ? 67.779  -2.902  86.056  1.000 48.742  0 419 ARG DDD O     1 ? 4 
ATOM   14371 C CB    . ARG D 1 419 ? 68.475  -1.674  83.355  1.000 38.507  0 419 ARG DDD CB    1 ? 4 
ATOM   14372 C CG    . ARG D 1 419 ? 68.486  -1.436  81.857  1.000 36.398  0 419 ARG DDD CG    1 ? 4 
ATOM   14373 C CD    . ARG D 1 419 ? 69.024  -0.074  81.486  1.000 35.711  0 419 ARG DDD CD    1 ? 4 
ATOM   14374 N NE    . ARG D 1 419 ? 69.351  -0.027  80.066  1.000 34.374  0 419 ARG DDD NE    1 ? 4 
ATOM   14375 C CZ    . ARG D 1 419 ? 69.825  1.036   79.431  1.000 34.800  0 419 ARG DDD CZ    1 ? 4 
ATOM   14376 N NH1   . ARG D 1 419 ? 69.973  2.184   80.073  1.000 34.081  0 419 ARG DDD NH1   1 ? 4 
ATOM   14377 N NH2   . ARG D 1 419 ? 70.104  0.958   78.135  1.000 35.792  0 419 ARG DDD NH2   1 ? 4 
ATOM   14378 N N     . GLU D 1 420 ? 69.909  -3.738  85.684  1.000 46.984  0 420 GLU DDD N     1 ? 4 
ATOM   14379 C CA    . GLU D 1 420 ? 70.281  -4.017  87.096  1.000 53.964  0 420 GLU DDD CA    1 ? 4 
ATOM   14380 C C     . GLU D 1 420 ? 71.363  -3.040  87.555  1.000 52.051  0 420 GLU DDD C     1 ? 4 
ATOM   14381 O O     . GLU D 1 420 ? 72.254  -2.690  86.730  1.000 49.528  0 420 GLU DDD O     1 ? 4 
ATOM   14382 C CB    . GLU D 1 420 ? 70.778  -5.462  87.239  1.000 58.818  0 420 GLU DDD CB    1 ? 4 
ATOM   14383 C CG    . GLU D 1 420 ? 69.677  -6.494  87.034  1.000 61.396  0 420 GLU DDD CG    1 ? 4 
ATOM   14384 C CD    . GLU D 1 420 ? 70.062  -7.770  86.285  1.000 64.102  0 420 GLU DDD CD    1 ? 4 
ATOM   14385 O OE1   . GLU D 1 420 ? 71.178  -8.281  86.522  1.000 65.531  0 420 GLU DDD OE1   1 ? 4 
ATOM   14386 O OE2   . GLU D 1 420 ? 69.254  -8.215  85.418  1.000 66.021  0 420 GLU DDD OE2   1 ? 4 
ATOM   14387 N N     . LYS D 1 421 ? 71.269  -2.646  88.829  1.000 53.269  0 421 LYS DDD N     1 ? 4 
ATOM   14388 C CA    . LYS D 1 421 ? 72.344  -1.967  89.589  1.000 54.271  0 421 LYS DDD CA    1 ? 4 
ATOM   14389 C C     . LYS D 1 421 ? 73.636  -2.767  89.456  1.000 54.249  0 421 LYS DDD C     1 ? 4 
ATOM   14390 O O     . LYS D 1 421 ? 73.594  -3.997  89.437  1.000 54.133  0 421 LYS DDD O     1 ? 4 
ATOM   14391 C CB    . LYS D 1 421 ? 71.998  -1.891  91.072  1.000 54.245  0 421 LYS DDD CB    1 ? 4 
ATOM   14392 C CG    . LYS D 1 421 ? 71.055  -0.788  91.501  1.000 56.619  0 421 LYS DDD CG    1 ? 4 
ATOM   14393 C CD    . LYS D 1 421 ? 71.067  -0.581  93.022  1.000 58.432  0 421 LYS DDD CD    1 ? 4 
ATOM   14394 C CE    . LYS D 1 421 ? 70.635  0.797   93.494  1.000 59.220  0 421 LYS DDD CE    1 ? 4 
ATOM   14395 N NZ    . LYS D 1 421 ? 69.292  0.778   94.128  1.000 60.470  0 421 LYS DDD NZ    1 ? 4 
ATOM   14396 N N     . PRO D 1 422 ? 74.820  -2.112  89.376  1.000 54.860  0 422 PRO DDD N     1 ? 4 
ATOM   14397 C CA    . PRO D 1 422 ? 76.089  -2.823  89.508  1.000 58.924  0 422 PRO DDD CA    1 ? 4 
ATOM   14398 C C     . PRO D 1 422 ? 76.104  -3.476  90.900  1.000 63.620  0 422 PRO DDD C     1 ? 4 
ATOM   14399 O O     . PRO D 1 422 ? 75.491  -2.900  91.818  1.000 60.260  0 422 PRO DDD O     1 ? 4 
ATOM   14400 C CB    . PRO D 1 422 ? 77.167  -1.739  89.384  1.000 58.029  0 422 PRO DDD CB    1 ? 4 
ATOM   14401 C CG    . PRO D 1 422 ? 76.449  -0.526  88.790  1.000 56.262  0 422 PRO DDD CG    1 ? 4 
ATOM   14402 C CD    . PRO D 1 422 ? 74.989  -0.671  89.171  1.000 54.575  0 422 PRO DDD CD    1 ? 4 
ATOM   14403 N N     . GLU D 1 423 ? 76.734  -4.653  91.049  1.000 67.835  0 423 GLU DDD N     1 ? 4 
ATOM   14404 C CA    . GLU D 1 423 ? 76.440  -5.508  92.234  1.000 71.160  0 423 GLU DDD CA    1 ? 4 
ATOM   14405 C C     . GLU D 1 423 ? 77.130  -4.906  93.466  1.000 69.974  0 423 GLU DDD C     1 ? 4 
ATOM   14406 O O     . GLU D 1 423 ? 76.669  -5.219  94.576  1.000 65.739  0 423 GLU DDD O     1 ? 4 
ATOM   14407 C CB    . GLU D 1 423 ? 76.611  -6.994  91.906  1.000 76.768  0 423 GLU DDD CB    1 ? 4 
ATOM   14408 C CG    . GLU D 1 423 ? 77.858  -7.685  92.420  1.000 81.306  0 423 GLU DDD CG    1 ? 4 
ATOM   14409 C CD    . GLU D 1 423 ? 77.773  -9.192  92.193  1.000 83.432  0 423 GLU DDD CD    1 ? 4 
ATOM   14410 O OE1   . GLU D 1 423 ? 78.550  -9.947  92.840  1.000 77.696  0 423 GLU DDD OE1   1 ? 4 
ATOM   14411 O OE2   . GLU D 1 423 ? 76.907  -9.611  91.362  1.000 82.102  0 423 GLU DDD OE2   1 ? 4 
ATOM   14412 N N     . HIS D 1 424 ? 78.069  -3.966  93.298  1.000 70.579  0 424 HIS DDD N     1 ? 4 
ATOM   14413 C CA    . HIS D 1 424 ? 78.714  -3.249  94.435  1.000 76.672  0 424 HIS DDD CA    1 ? 4 
ATOM   14414 C C     . HIS D 1 424 ? 77.756  -2.249  95.114  1.000 78.442  0 424 HIS DDD C     1 ? 4 
ATOM   14415 O O     . HIS D 1 424 ? 78.140  -1.767  96.189  1.000 77.517  0 424 HIS DDD O     1 ? 4 
ATOM   14416 C CB    . HIS D 1 424 ? 80.054  -2.609  94.031  1.000 76.875  0 424 HIS DDD CB    1 ? 4 
ATOM   14417 C CG    . HIS D 1 424 ? 79.980  -1.529  93.001  1.000 79.796  0 424 HIS DDD CG    1 ? 4 
ATOM   14418 N ND1   . HIS D 1 424 ? 79.690  -0.212  93.317  1.000 82.398  0 424 HIS DDD ND1   1 ? 4 
ATOM   14419 C CD2   . HIS D 1 424 ? 80.236  -1.545  91.671  1.000 79.299  0 424 HIS DDD CD2   1 ? 4 
ATOM   14420 C CE1   . HIS D 1 424 ? 79.713  0.524   92.221  1.000 78.365  0 424 HIS DDD CE1   1 ? 4 
ATOM   14421 N NE2   . HIS D 1 424 ? 80.071  -0.265  91.200  1.000 77.652  0 424 HIS DDD NE2   1 ? 4 
ATOM   14422 N N     . LEU D 1 425 ? 76.566  -1.963  94.561  1.000 74.274  0 425 LEU DDD N     1 ? 4 
ATOM   14423 C CA    . LEU D 1 425 ? 75.608  -0.979  95.147  1.000 76.942  0 425 LEU DDD CA    1 ? 4 
ATOM   14424 C C     . LEU D 1 425 ? 74.328  -1.667  95.630  1.000 78.423  0 425 LEU DDD C     1 ? 4 
ATOM   14425 O O     . LEU D 1 425 ? 73.389  -0.950  96.065  1.000 73.768  0 425 LEU DDD O     1 ? 4 
ATOM   14426 C CB    . LEU D 1 425 ? 75.267  0.082   94.097  1.000 77.436  0 425 LEU DDD CB    1 ? 4 
ATOM   14427 C CG    . LEU D 1 425 ? 76.388  1.060   93.781  1.000 78.988  0 425 LEU DDD CG    1 ? 4 
ATOM   14428 C CD1   . LEU D 1 425 ? 76.068  1.833   92.513  1.000 78.773  0 425 LEU DDD CD1   1 ? 4 
ATOM   14429 C CD2   . LEU D 1 425 ? 76.621  2.020   94.945  1.000 81.777  0 425 LEU DDD CD2   1 ? 4 
ATOM   14430 N N     . ARG D 1 426 ? 74.265  -2.994  95.532  1.000 81.969  0 426 ARG DDD N     1 ? 4 
ATOM   14431 C CA    . ARG D 1 426 ? 73.071  -3.792  95.918  1.000 86.031  0 426 ARG DDD CA    1 ? 4 
ATOM   14432 C C     . ARG D 1 426 ? 72.985  -3.841  97.449  1.000 92.206  0 426 ARG DDD C     1 ? 4 
ATOM   14433 O O     . ARG D 1 426 ? 74.035  -4.076  98.083  1.000 91.708  0 426 ARG DDD O     1 ? 4 
ATOM   14434 C CB    . ARG D 1 426 ? 73.176  -5.192  95.319  1.000 83.753  0 426 ARG DDD CB    1 ? 4 
ATOM   14435 C CG    . ARG D 1 426 ? 72.977  -5.244  93.814  1.000 80.624  0 426 ARG DDD CG    1 ? 4 
ATOM   14436 C CD    . ARG D 1 426 ? 71.530  -5.044  93.441  1.000 78.298  0 426 ARG DDD CD    1 ? 4 
ATOM   14437 N NE    . ARG D 1 426 ? 70.681  -6.036  94.070  1.000 76.660  0 426 ARG DDD NE    1 ? 4 
ATOM   14438 C CZ    . ARG D 1 426 ? 70.433  -7.258  93.598  1.000 76.403  0 426 ARG DDD CZ    1 ? 4 
ATOM   14439 N NH1   . ARG D 1 426 ? 70.945  -7.652  92.437  1.000 71.437  0 426 ARG DDD NH1   1 ? 4 
ATOM   14440 N NH2   . ARG D 1 426 ? 69.642  -8.071  94.290  1.000 78.648  0 426 ARG DDD NH2   1 ? 4 
ATOM   14441 N N     . GLU D 1 427 ? 71.778  -3.630  98.004  1.000 97.983  0 427 GLU DDD N     1 ? 4 
ATOM   14442 C CA    . GLU D 1 427 ? 71.498  -3.596  99.471  1.000 101.020 0 427 GLU DDD CA    1 ? 4 
ATOM   14443 C C     . GLU D 1 427 ? 70.750  -4.866  99.918  1.000 102.985 0 427 GLU DDD C     1 ? 4 
ATOM   14444 O O     . GLU D 1 427 ? 70.822  -5.169  101.115 1.000 108.328 0 427 GLU DDD O     1 ? 4 
ATOM   14445 C CB    . GLU D 1 427 ? 70.718  -2.327  99.852  1.000 103.071 0 427 GLU DDD CB    1 ? 4 
ATOM   14446 C CG    . GLU D 1 427 ? 71.560  -1.276  100.589 1.000 103.329 0 427 GLU DDD CG    1 ? 4 
ATOM   14447 C CD    . GLU D 1 427 ? 70.835  -0.040  101.119 1.000 102.496 0 427 GLU DDD CD    1 ? 4 
ATOM   14448 O OE1   . GLU D 1 427 ? 71.253  1.070   100.750 1.000 101.035 0 427 GLU DDD OE1   1 ? 4 
ATOM   14449 O OE2   . GLU D 1 427 ? 69.872  -0.177  101.922 1.000 94.577  0 427 GLU DDD OE2   1 ? 4 
ATOM   14450 N N     . ASN D 1 428 ? 70.081  -5.590  99.012  1.000 100.083 0 428 ASN DDD N     1 ? 4 
ATOM   14451 C CA    . ASN D 1 428 ? 69.304  -6.816  99.354  1.000 100.164 0 428 ASN DDD CA    1 ? 4 
ATOM   14452 C C     . ASN D 1 428 ? 68.952  -7.583  98.074  1.000 99.438  0 428 ASN DDD C     1 ? 4 
ATOM   14453 O O     . ASN D 1 428 ? 69.599  -7.328  97.045  1.000 100.699 0 428 ASN DDD O     1 ? 4 
ATOM   14454 C CB    . ASN D 1 428 ? 68.069  -6.465  100.182 1.000 102.539 0 428 ASN DDD CB    1 ? 4 
ATOM   14455 C CG    . ASN D 1 428 ? 67.218  -5.378  99.561  1.000 106.985 0 428 ASN DDD CG    1 ? 4 
ATOM   14456 O OD1   . ASN D 1 428 ? 66.785  -5.488  98.420  1.000 106.194 0 428 ASN DDD OD1   1 ? 4 
ATOM   14457 N ND2   . ASN D 1 428 ? 66.959  -4.316  100.307 1.000 109.881 0 428 ASN DDD ND2   1 ? 4 
ATOM   14458 N N     . GLU D 1 429 ? 67.966  -8.484  98.137  1.000 99.007  0 429 GLU DDD N     1 ? 4 
ATOM   14459 C CA    . GLU D 1 429 ? 67.538  -9.340  96.992  1.000 99.626  0 429 GLU DDD CA    1 ? 4 
ATOM   14460 C C     . GLU D 1 429 ? 66.355  -8.713  96.236  1.000 99.365  0 429 GLU DDD C     1 ? 4 
ATOM   14461 O O     . GLU D 1 429 ? 65.885  -9.338  95.278  1.000 98.950  0 429 GLU DDD O     1 ? 4 
ATOM   14462 C CB    . GLU D 1 429 ? 67.179  -10.750 97.464  1.000 101.113 0 429 GLU DDD CB    1 ? 4 
ATOM   14463 C CG    . GLU D 1 429 ? 68.232  -11.372 98.365  1.000 102.413 0 429 GLU DDD CG    1 ? 4 
ATOM   14464 C CD    . GLU D 1 429 ? 69.668  -11.166 97.910  1.000 100.430 0 429 GLU DDD CD    1 ? 4 
ATOM   14465 O OE1   . GLU D 1 429 ? 69.960  -11.463 96.736  1.000 96.887  0 429 GLU DDD OE1   1 ? 4 
ATOM   14466 O OE2   . GLU D 1 429 ? 70.488  -10.686 98.728  1.000 99.708  0 429 GLU DDD OE2   1 ? 4 
ATOM   14467 N N     . MET D 1 430 ? 65.894  -7.525  96.645  1.000 97.427  0 430 MET DDD N     1 ? 4 
ATOM   14468 C CA    . MET D 1 430 ? 64.730  -6.783  96.081  1.000 94.943  0 430 MET DDD CA    1 ? 4 
ATOM   14469 C C     . MET D 1 430 ? 65.164  -5.379  95.581  1.000 88.288  0 430 MET DDD C     1 ? 4 
ATOM   14470 O O     . MET D 1 430 ? 64.294  -4.607  95.154  1.000 88.630  0 430 MET DDD O     1 ? 4 
ATOM   14471 C CB    . MET D 1 430 ? 63.703  -6.656  97.219  1.000 95.732  0 430 MET DDD CB    1 ? 4 
ATOM   14472 C CG    . MET D 1 430 ? 62.235  -6.600  96.811  1.000 99.262  0 430 MET DDD CG    1 ? 4 
ATOM   14473 S SD    . MET D 1 430 ? 61.060  -6.697  98.226  1.000 98.741  0 430 MET DDD SD    1 ? 4 
ATOM   14474 C CE    . MET D 1 430 ? 60.001  -5.299  97.861  1.000 96.690  0 430 MET DDD CE    1 ? 4 
ATOM   14475 N N     . ASP D 1 431 ? 66.467  -5.068  95.616  1.000 78.440  0 431 ASP DDD N     1 ? 4 
ATOM   14476 C CA    . ASP D 1 431 ? 67.069  -3.766  95.226  1.000 72.005  0 431 ASP DDD CA    1 ? 4 
ATOM   14477 C C     . ASP D 1 431 ? 67.773  -3.897  93.852  1.000 67.999  0 431 ASP DDD C     1 ? 4 
ATOM   14478 O O     . ASP D 1 431 ? 68.714  -3.124  93.582  1.000 65.317  0 431 ASP DDD O     1 ? 4 
ATOM   14479 C CB    . ASP D 1 431 ? 68.003  -3.364  96.369  1.000 71.318  0 431 ASP DDD CB    1 ? 4 
ATOM   14480 C CG    . ASP D 1 431 ? 68.963  -2.236  96.099  1.000 68.172  0 431 ASP DDD CG    1 ? 4 
ATOM   14481 O OD1   . ASP D 1 431 ? 68.509  -1.228  95.507  1.000 71.749  0 431 ASP DDD OD1   1 ? 4 
ATOM   14482 O OD2   . ASP D 1 431 ? 70.152  -2.387  96.465  1.000 60.217  0 431 ASP DDD OD2   1 ? 4 
ATOM   14483 N N     . PHE D 1 432 ? 67.345  -4.840  93.003  1.000 60.286  0 432 PHE DDD N     1 ? 4 
ATOM   14484 C CA    . PHE D 1 432 ? 68.090  -5.301  91.805  1.000 57.020  0 432 PHE DDD CA    1 ? 4 
ATOM   14485 C C     . PHE D 1 432 ? 68.060  -4.257  90.688  1.000 54.299  0 432 PHE DDD C     1 ? 4 
ATOM   14486 O O     . PHE D 1 432 ? 69.102  -4.037  90.038  1.000 49.939  0 432 PHE DDD O     1 ? 4 
ATOM   14487 C CB    . PHE D 1 432 ? 67.578  -6.672  91.348  1.000 58.133  0 432 PHE DDD CB    1 ? 4 
ATOM   14488 C CG    . PHE D 1 432 ? 66.080  -6.809  91.192  1.000 58.836  0 432 PHE DDD CG    1 ? 4 
ATOM   14489 C CD1   . PHE D 1 432 ? 65.454  -6.473  89.996  1.000 57.076  0 432 PHE DDD CD1   1 ? 4 
ATOM   14490 C CD2   . PHE D 1 432 ? 65.287  -7.288  92.236  1.000 61.725  0 432 PHE DDD CD2   1 ? 4 
ATOM   14491 C CE1   . PHE D 1 432 ? 64.079  -6.610  89.841  1.000 56.481  0 432 PHE DDD CE1   1 ? 4 
ATOM   14492 C CE2   . PHE D 1 432 ? 63.910  -7.421  92.083  1.000 62.285  0 432 PHE DDD CE2   1 ? 4 
ATOM   14493 C CZ    . PHE D 1 432 ? 63.307  -7.080  90.883  1.000 60.324  0 432 PHE DDD CZ    1 ? 4 
ATOM   14494 N N     . ALA D 1 433 ? 66.902  -3.615  90.511  1.000 51.333  0 433 ALA DDD N     1 ? 4 
ATOM   14495 C CA    . ALA D 1 433 ? 66.546  -2.724  89.395  1.000 47.063  0 433 ALA DDD CA    1 ? 4 
ATOM   14496 C C     . ALA D 1 433 ? 67.265  -1.375  89.509  1.000 45.890  0 433 ALA DDD C     1 ? 4 
ATOM   14497 O O     . ALA D 1 433 ? 67.426  -0.854  90.618  1.000 44.795  0 433 ALA DDD O     1 ? 4 
ATOM   14498 C CB    . ALA D 1 433 ? 65.047  -2.512  89.390  1.000 46.677  0 433 ALA DDD CB    1 ? 4 
ATOM   14499 N N     . LEU D 1 434 ? 67.599  -0.792  88.363  1.000 43.418  0 434 LEU DDD N     1 ? 4 
ATOM   14500 C CA    . LEU D 1 434 ? 67.780  0.681   88.215  1.000 40.754  0 434 LEU DDD CA    1 ? 4 
ATOM   14501 C C     . LEU D 1 434 ? 66.467  1.391   88.524  1.000 39.875  0 434 LEU DDD C     1 ? 4 
ATOM   14502 O O     . LEU D 1 434 ? 65.389  0.830   88.384  1.000 41.004  0 434 LEU DDD O     1 ? 4 
ATOM   14503 C CB    . LEU D 1 434 ? 68.231  0.976   86.792  1.000 38.870  0 434 LEU DDD CB    1 ? 4 
ATOM   14504 C CG    . LEU D 1 434 ? 69.623  0.448   86.448  1.000 38.897  0 434 LEU DDD CG    1 ? 4 
ATOM   14505 C CD1   . LEU D 1 434 ? 70.097  1.023   85.120  1.000 39.160  0 434 LEU DDD CD1   1 ? 4 
ATOM   14506 C CD2   . LEU D 1 434 ? 70.622  0.802   87.530  1.000 40.278  0 434 LEU DDD CD2   1 ? 4 
ATOM   14507 N N     . PRO D 1 435 ? 66.488  2.654   88.979  1.000 39.375  0 435 PRO DDD N     1 ? 4 
ATOM   14508 C CA    . PRO D 1 435 ? 65.259  3.428   89.080  1.000 39.412  0 435 PRO DDD CA    1 ? 4 
ATOM   14509 C C     . PRO D 1 435 ? 64.520  3.462   87.728  1.000 40.612  0 435 PRO DDD C     1 ? 4 
ATOM   14510 O O     . PRO D 1 435 ? 65.144  3.369   86.666  1.000 39.361  0 435 PRO DDD O     1 ? 4 
ATOM   14511 C CB    . PRO D 1 435 ? 65.745  4.836   89.461  1.000 38.561  0 435 PRO DDD CB    1 ? 4 
ATOM   14512 C CG    . PRO D 1 435 ? 67.035  4.586   90.178  1.000 38.950  0 435 PRO DDD CG    1 ? 4 
ATOM   14513 C CD    . PRO D 1 435 ? 67.666  3.412   89.434  1.000 40.434  0 435 PRO DDD CD    1 ? 4 
ATOM   14514 N N     . LEU D 1 436 ? 63.203  3.635   87.784  1.000 40.751  0 436 LEU DDD N     1 ? 4 
ATOM   14515 C CA    . LEU D 1 436 ? 62.399  3.940   86.583  1.000 39.438  0 436 LEU DDD CA    1 ? 4 
ATOM   14516 C C     . LEU D 1 436 ? 63.103  5.075   85.828  1.000 37.948  0 436 LEU DDD C     1 ? 4 
ATOM   14517 O O     . LEU D 1 436 ? 63.547  6.027   86.490  1.000 37.467  0 436 LEU DDD O     1 ? 4 
ATOM   14518 C CB    . LEU D 1 436 ? 60.983  4.319   87.026  1.000 40.167  0 436 LEU DDD CB    1 ? 4 
ATOM   14519 C CG    . LEU D 1 436 ? 60.225  3.243   87.804  1.000 40.409  0 436 LEU DDD CG    1 ? 4 
ATOM   14520 C CD1   . LEU D 1 436 ? 58.999  3.828   88.457  1.000 40.439  0 436 LEU DDD CD1   1 ? 4 
ATOM   14521 C CD2   . LEU D 1 436 ? 59.842  2.072   86.906  1.000 40.384  0 436 LEU DDD CD2   1 ? 4 
ATOM   14522 N N     . ASN D 1 437 ? 63.251  4.963   84.496  1.000 35.049  0 437 ASN DDD N     1 ? 4 
ATOM   14523 C CA    . ASN D 1 437 ? 64.137  5.881   83.744  1.000 32.741  0 437 ASN DDD CA    1 ? 4 
ATOM   14524 C C     . ASN D 1 437 ? 63.422  7.194   83.447  1.000 30.522  0 437 ASN DDD C     1 ? 4 
ATOM   14525 O O     . ASN D 1 437 ? 64.138  8.151   83.143  1.000 29.272  0 437 ASN DDD O     1 ? 4 
ATOM   14526 C CB    . ASN D 1 437 ? 64.744  5.206   82.515  1.000 33.136  0 437 ASN DDD CB    1 ? 4 
ATOM   14527 C CG    . ASN D 1 437 ? 63.736  4.865   81.441  1.000 33.275  0 437 ASN DDD CG    1 ? 4 
ATOM   14528 O OD1   . ASN D 1 437 ? 62.573  4.537   81.724  1.000 31.251  0 437 ASN DDD OD1   1 ? 4 
ATOM   14529 N ND2   . ASN D 1 437 ? 64.180  4.958   80.193  1.000 34.630  0 437 ASN DDD ND2   1 ? 4 
ATOM   14530 N N     . CYS D 1 438 ? 62.080  7.251   83.509  1.000 30.903  0 438 CYS DDD N     1 ? 4 
ATOM   14531 C CA    . CYS D 1 438 ? 61.279  8.403   83.026  1.000 31.572  0 438 CYS DDD CA    1 ? 4 
ATOM   14532 C C     . CYS D 1 438 ? 60.460  9.058   84.129  1.000 32.865  0 438 CYS DDD C     1 ? 4 
ATOM   14533 O O     . CYS D 1 438 ? 59.939  8.355   85.004  1.000 32.842  0 438 CYS DDD O     1 ? 4 
ATOM   14534 C CB    . CYS D 1 438 ? 60.308  8.018   81.923  1.000 32.306  0 438 CYS DDD CB    1 ? 4 
ATOM   14535 S SG    . CYS D 1 438 ? 61.147  7.404   80.437  1.000 32.199  0 438 CYS DDD SG    1 ? 4 
ATOM   14536 N N     . LEU D 1 439 ? 60.293  10.372  83.981  1.000 33.481  0 439 LEU DDD N     1 ? 4 
ATOM   14537 C CA    . LEU D 1 439 ? 59.411  11.208  84.813  1.000 33.321  0 439 LEU DDD CA    1 ? 4 
ATOM   14538 C C     . LEU D 1 439 ? 58.846  12.325  83.955  1.000 32.585  0 439 LEU DDD C     1 ? 4 
ATOM   14539 O O     . LEU D 1 439 ? 59.619  13.161  83.476  1.000 31.379  0 439 LEU DDD O     1 ? 4 
ATOM   14540 C CB    . LEU D 1 439 ? 60.163  11.809  86.005  1.000 34.449  0 439 LEU DDD CB    1 ? 4 
ATOM   14541 C CG    . LEU D 1 439 ? 59.287  12.716  86.869  1.000 34.634  0 439 LEU DDD CG    1 ? 4 
ATOM   14542 C CD1   . LEU D 1 439 ? 58.271  11.886  87.614  1.000 34.985  0 439 LEU DDD CD1   1 ? 4 
ATOM   14543 C CD2   . LEU D 1 439 ? 60.122  13.539  87.806  1.000 36.341  0 439 LEU DDD CD2   1 ? 4 
ATOM   14544 N N     . ALA D 1 440 ? 57.522  12.354  83.838  1.000 32.764  0 440 ALA DDD N     1 ? 4 
ATOM   14545 C CA    . ALA D 1 440 ? 56.774  13.384  83.095  1.000 33.793  0 440 ALA DDD CA    1 ? 4 
ATOM   14546 C C     . ALA D 1 440 ? 56.027  14.260  84.105  1.000 35.942  0 440 ALA DDD C     1 ? 4 
ATOM   14547 O O     . ALA D 1 440 ? 55.374  13.696  85.005  1.000 35.325  0 440 ALA DDD O     1 ? 4 
ATOM   14548 C CB    . ALA D 1 440 ? 55.840  12.708  82.140  1.000 32.574  0 440 ALA DDD CB    1 ? 4 
ATOM   14549 N N     . LYS D 1 441 ? 56.136  15.574  83.953  1.000 37.191  0 441 LYS DDD N     1 ? 4 
ATOM   14550 C CA    . LYS D 1 441 ? 55.427  16.532  84.819  1.000 39.241  0 441 LYS DDD CA    1 ? 4 
ATOM   14551 C C     . LYS D 1 441 ? 54.966  17.759  84.032  1.000 39.204  0 441 LYS DDD C     1 ? 4 
ATOM   14552 O O     . LYS D 1 441 ? 55.787  18.380  83.340  1.000 39.771  0 441 LYS DDD O     1 ? 4 
ATOM   14553 C CB    . LYS D 1 441 ? 56.344  16.948  85.959  1.000 40.940  0 441 LYS DDD CB    1 ? 4 
ATOM   14554 C CG    . LYS D 1 441 ? 55.757  18.016  86.858  1.000 41.414  0 441 LYS DDD CG    1 ? 4 
ATOM   14555 C CD    . LYS D 1 441 ? 56.336  17.961  88.229  1.000 43.849  0 441 LYS DDD CD    1 ? 4 
ATOM   14556 C CE    . LYS D 1 441 ? 57.741  18.506  88.257  1.000 44.565  0 441 LYS DDD CE    1 ? 4 
ATOM   14557 N NZ    . LYS D 1 441 ? 58.280  18.542  89.633  1.000 44.571  0 441 LYS DDD NZ    1 ? 4 
ATOM   14558 N N     . LEU D 1 442 ? 53.689  18.091  84.186  1.000 40.299  0 442 LEU DDD N     1 ? 4 
ATOM   14559 C CA    . LEU D 1 442 ? 53.074  19.386  83.798  1.000 41.416  0 442 LEU DDD CA    1 ? 4 
ATOM   14560 C C     . LEU D 1 442 ? 52.781  20.209  85.053  1.000 43.866  0 442 LEU DDD C     1 ? 4 
ATOM   14561 O O     . LEU D 1 442 ? 52.212  19.678  86.027  1.000 45.894  0 442 LEU DDD O     1 ? 4 
ATOM   14562 C CB    . LEU D 1 442 ? 51.779  19.113  83.025  1.000 41.456  0 442 LEU DDD CB    1 ? 4 
ATOM   14563 C CG    . LEU D 1 442 ? 51.966  18.379  81.697  1.000 41.131  0 442 LEU DDD CG    1 ? 4 
ATOM   14564 C CD1   . LEU D 1 442 ? 50.644  18.028  81.078  1.000 40.709  0 442 LEU DDD CD1   1 ? 4 
ATOM   14565 C CD2   . LEU D 1 442 ? 52.816  19.189  80.706  1.000 39.548  0 442 LEU DDD CD2   1 ? 4 
ATOM   14566 N N     . VAL D 1 443 ? 53.114  21.489  84.994  1.000 45.347  0 443 VAL DDD N     1 ? 4 
ATOM   14567 C CA    . VAL D 1 443 ? 52.759  22.492  86.034  1.000 45.313  0 443 VAL DDD CA    1 ? 4 
ATOM   14568 C C     . VAL D 1 443 ? 51.731  23.429  85.400  1.000 45.605  0 443 VAL DDD C     1 ? 4 
ATOM   14569 O O     . VAL D 1 443 ? 52.067  24.029  84.359  1.000 43.589  0 443 VAL DDD O     1 ? 4 
ATOM   14570 C CB    . VAL D 1 443 ? 54.032  23.193  86.534  1.000 44.117  0 443 VAL DDD CB    1 ? 4 
ATOM   14571 C CG1   . VAL D 1 443 ? 53.726  24.126  87.683  1.000 44.929  0 443 VAL DDD CG1   1 ? 4 
ATOM   14572 C CG2   . VAL D 1 443 ? 55.090  22.185  86.932  1.000 42.563  0 443 VAL DDD CG2   1 ? 4 
ATOM   14573 N N     . VAL D 1 444 ? 50.524  23.493  85.976  1.000 45.993  0 444 VAL DDD N     1 ? 4 
ATOM   14574 C CA    . VAL D 1 444 ? 49.361  24.258  85.435  1.000 45.585  0 444 VAL DDD CA    1 ? 4 
ATOM   14575 C C     . VAL D 1 444 ? 48.812  25.263  86.460  1.000 46.633  0 444 VAL DDD C     1 ? 4 
ATOM   14576 O O     . VAL D 1 444 ? 48.887  25.008  87.688  1.000 45.259  0 444 VAL DDD O     1 ? 4 
ATOM   14577 C CB    . VAL D 1 444 ? 48.271  23.291  84.948  1.000 47.078  0 444 VAL DDD CB    1 ? 4 
ATOM   14578 C CG1   . VAL D 1 444 ? 48.873  22.210  84.058  1.000 47.249  0 444 VAL DDD CG1   1 ? 4 
ATOM   14579 C CG2   . VAL D 1 444 ? 47.480  22.658  86.084  1.000 46.131  0 444 VAL DDD CG2   1 ? 4 
ATOM   14580 N N     . VAL D 1 445 ? 48.257  26.372  85.960  1.000 49.119  0 445 VAL DDD N     1 ? 4 
ATOM   14581 C CA    . VAL D 1 445 ? 47.557  27.416  86.771  1.000 51.142  0 445 VAL DDD CA    1 ? 4 
ATOM   14582 C C     . VAL D 1 445 ? 46.040  27.165  86.715  1.000 53.136  0 445 VAL DDD C     1 ? 4 
ATOM   14583 O O     . VAL D 1 445 ? 45.443  27.211  85.623  1.000 53.460  0 445 VAL DDD O     1 ? 4 
ATOM   14584 C CB    . VAL D 1 445 ? 47.940  28.836  86.316  1.000 51.459  0 445 VAL DDD CB    1 ? 4 
ATOM   14585 C CG1   . VAL D 1 445 ? 47.226  29.898  87.147  1.000 53.688  0 445 VAL DDD CG1   1 ? 4 
ATOM   14586 C CG2   . VAL D 1 445 ? 49.452  29.043  86.386  1.000 50.807  0 445 VAL DDD CG2   1 ? 4 
ATOM   14587 N N     . LYS D 1 446 ? 45.448  26.908  87.876  1.000 56.335  0 446 LYS DDD N     1 ? 4 
ATOM   14588 C CA    . LYS D 1 446 ? 44.009  26.557  88.007  1.000 61.729  0 446 LYS DDD CA    1 ? 4 
ATOM   14589 C C     . LYS D 1 446 ? 43.132  27.723  87.538  1.000 63.634  0 446 LYS DDD C     1 ? 4 
ATOM   14590 O O     . LYS D 1 446 ? 42.189  27.468  86.772  1.000 64.337  0 446 LYS DDD O     1 ? 4 
ATOM   14591 C CB    . LYS D 1 446 ? 43.716  26.152  89.451  1.000 60.226  0 446 LYS DDD CB    1 ? 4 
ATOM   14592 C CG    . LYS D 1 446 ? 44.528  24.947  89.894  1.000 60.186  0 446 LYS DDD CG    1 ? 4 
ATOM   14593 C CD    . LYS D 1 446 ? 43.701  23.866  90.513  1.000 59.472  0 446 LYS DDD CD    1 ? 4 
ATOM   14594 C CE    . LYS D 1 446 ? 43.470  24.107  91.982  1.000 59.589  0 446 LYS DDD CE    1 ? 4 
ATOM   14595 N NZ    . LYS D 1 446 ? 42.819  22.923  92.585  1.000 58.713  0 446 LYS DDD NZ    1 ? 4 
ATOM   14596 N N     . SER D 1 447 ? 43.471  28.955  87.923  1.000 65.173  0 447 SER DDD N     1 ? 4 
ATOM   14597 C CA    . SER D 1 447 ? 42.649  30.157  87.639  1.000 67.458  0 447 SER DDD CA    1 ? 4 
ATOM   14598 C C     . SER D 1 447 ? 42.695  30.517  86.147  1.000 67.955  0 447 SER DDD C     1 ? 4 
ATOM   14599 O O     . SER D 1 447 ? 42.091  31.528  85.784  1.000 66.437  0 447 SER DDD O     1 ? 4 
ATOM   14600 C CB    . SER D 1 447 ? 43.065  31.314  88.505  1.000 69.450  0 447 SER DDD CB    1 ? 4 
ATOM   14601 O OG    . SER D 1 447 ? 44.418  31.658  88.263  1.000 73.017  0 447 SER DDD OG    1 ? 4 
ATOM   14602 N N     . GLN D 1 448 ? 43.376  29.730  85.306  1.000 69.419  0 448 GLN DDD N     1 ? 4 
ATOM   14603 C CA    . GLN D 1 448 ? 43.447  29.978  83.838  1.000 69.494  0 448 GLN DDD CA    1 ? 4 
ATOM   14604 C C     . GLN D 1 448 ? 43.064  28.706  83.073  1.000 67.389  0 448 GLN DDD C     1 ? 4 
ATOM   14605 O O     . GLN D 1 448 ? 43.651  28.466  82.002  1.000 68.419  0 448 GLN DDD O     1 ? 4 
ATOM   14606 C CB    . GLN D 1 448 ? 44.835  30.496  83.454  1.000 68.421  0 448 GLN DDD CB    1 ? 4 
ATOM   14607 C CG    . GLN D 1 448 ? 45.210  31.767  84.191  1.000 71.120  0 448 GLN DDD CG    1 ? 4 
ATOM   14608 C CD    . GLN D 1 448 ? 46.614  32.223  83.871  1.000 72.483  0 448 GLN DDD CD    1 ? 4 
ATOM   14609 O OE1   . GLN D 1 448 ? 47.429  31.500  83.290  1.000 75.645  0 448 GLN DDD OE1   1 ? 4 
ATOM   14610 N NE2   . GLN D 1 448 ? 46.936  33.418  84.322  1.000 70.252  0 448 GLN DDD NE2   1 ? 4 
ATOM   14611 N N     . GLY D 1 449 ? 42.082  27.961  83.591  1.000 66.787  0 449 GLY DDD N     1 ? 4 
ATOM   14612 C CA    . GLY D 1 449 ? 41.587  26.700  83.005  1.000 63.953  0 449 GLY DDD CA    1 ? 4 
ATOM   14613 C C     . GLY D 1 449 ? 42.710  25.685  82.869  1.000 61.752  0 449 GLY DDD C     1 ? 4 
ATOM   14614 O O     . GLY D 1 449 ? 42.779  25.034  81.807  1.000 59.370  0 449 GLY DDD O     1 ? 4 
ATOM   14615 N N     . GLU D 1 450 ? 43.567  25.589  83.898  1.000 58.839  0 450 GLU DDD N     1 ? 4 
ATOM   14616 C CA    . GLU D 1 450 ? 44.769  24.720  83.970  1.000 57.278  0 450 GLU DDD CA    1 ? 4 
ATOM   14617 C C     . GLU D 1 450 ? 45.717  24.990  82.791  1.000 54.079  0 450 GLU DDD C     1 ? 4 
ATOM   14618 O O     . GLU D 1 450 ? 46.129  24.027  82.152  1.000 54.131  0 450 GLU DDD O     1 ? 4 
ATOM   14619 C CB    . GLU D 1 450 ? 44.339  23.256  84.046  1.000 56.860  0 450 GLU DDD CB    1 ? 4 
ATOM   14620 C CG    . GLU D 1 450 ? 43.626  22.921  85.342  1.000 58.287  0 450 GLU DDD CG    1 ? 4 
ATOM   14621 C CD    . GLU D 1 450 ? 43.568  21.441  85.652  1.000 57.758  0 450 GLU DDD CD    1 ? 4 
ATOM   14622 O OE1   . GLU D 1 450 ? 43.105  20.644  84.791  1.000 56.209  0 450 GLU DDD OE1   1 ? 4 
ATOM   14623 O OE2   . GLU D 1 450 ? 43.988  21.083  86.753  1.000 57.384  0 450 GLU DDD OE2   1 ? 4 
ATOM   14624 N N     . LYS D 1 451 ? 46.073  26.248  82.519  1.000 52.554  0 451 LYS DDD N     1 ? 4 
ATOM   14625 C CA    . LYS D 1 451 ? 47.081  26.581  81.474  1.000 54.122  0 451 LYS DDD CA    1 ? 4 
ATOM   14626 C C     . LYS D 1 451 ? 48.427  25.951  81.866  1.000 50.811  0 451 LYS DDD C     1 ? 4 
ATOM   14627 O O     . LYS D 1 451 ? 48.779  26.010  83.051  1.000 47.264  0 451 LYS DDD O     1 ? 4 
ATOM   14628 C CB    . LYS D 1 451 ? 47.264  28.095  81.315  1.000 58.205  0 451 LYS DDD CB    1 ? 4 
ATOM   14629 C CG    . LYS D 1 451 ? 48.115  28.524  80.120  1.000 58.762  0 451 LYS DDD CG    1 ? 4 
ATOM   14630 C CD    . LYS D 1 451 ? 48.273  30.028  80.044  1.000 61.820  0 451 LYS DDD CD    1 ? 4 
ATOM   14631 C CE    . LYS D 1 451 ? 48.091  30.600  78.654  1.000 64.361  0 451 LYS DDD CE    1 ? 4 
ATOM   14632 N NZ    . LYS D 1 451 ? 47.916  32.065  78.734  1.000 64.680  0 451 LYS DDD NZ    1 ? 4 
ATOM   14633 N N     . VAL D 1 452 ? 49.149  25.367  80.916  1.000 46.869  0 452 VAL DDD N     1 ? 4 
ATOM   14634 C CA    . VAL D 1 452 ? 50.487  24.774  81.203  1.000 47.221  0 452 VAL DDD CA    1 ? 4 
ATOM   14635 C C     . VAL D 1 452 ? 51.532  25.899  81.233  1.000 45.954  0 452 VAL DDD C     1 ? 4 
ATOM   14636 O O     . VAL D 1 452 ? 51.675  26.635  80.237  1.000 48.414  0 452 VAL DDD O     1 ? 4 
ATOM   14637 C CB    . VAL D 1 452 ? 50.840  23.671  80.196  1.000 47.416  0 452 VAL DDD CB    1 ? 4 
ATOM   14638 C CG1   . VAL D 1 452 ? 52.211  23.060  80.465  1.000 47.845  0 452 VAL DDD CG1   1 ? 4 
ATOM   14639 C CG2   . VAL D 1 452 ? 49.776  22.595  80.169  1.000 46.742  0 452 VAL DDD CG2   1 ? 4 
ATOM   14640 N N     . VAL D 1 453 ? 52.202  26.074  82.367  1.000 46.105  0 453 VAL DDD N     1 ? 4 
ATOM   14641 C CA    . VAL D 1 453 ? 53.247  27.127  82.541  1.000 46.138  0 453 VAL DDD CA    1 ? 4 
ATOM   14642 C C     . VAL D 1 453 ? 54.609  26.450  82.722  1.000 44.195  0 453 VAL DDD C     1 ? 4 
ATOM   14643 O O     . VAL D 1 453 ? 55.624  27.163  82.649  1.000 47.348  0 453 VAL DDD O     1 ? 4 
ATOM   14644 C CB    . VAL D 1 453 ? 52.914  28.078  83.711  1.000 46.306  0 453 VAL DDD CB    1 ? 4 
ATOM   14645 C CG1   . VAL D 1 453 ? 51.649  28.890  83.452  1.000 44.739  0 453 VAL DDD CG1   1 ? 4 
ATOM   14646 C CG2   . VAL D 1 453 ? 52.823  27.357  85.043  1.000 47.614  0 453 VAL DDD CG2   1 ? 4 
ATOM   14647 N N     . GLY D 1 454 ? 54.625  25.140  82.963  1.000 41.187  0 454 GLY DDD N     1 ? 4 
ATOM   14648 C CA    . GLY D 1 454 ? 55.858  24.351  83.162  1.000 42.677  0 454 GLY DDD CA    1 ? 4 
ATOM   14649 C C     . GLY D 1 454 ? 55.714  22.955  82.588  1.000 42.315  0 454 GLY DDD C     1 ? 4 
ATOM   14650 O O     . GLY D 1 454 ? 54.725  22.287  82.941  1.000 47.743  0 454 GLY DDD O     1 ? 4 
ATOM   14651 N N     . PHE D 1 455 ? 56.631  22.566  81.695  1.000 39.019  0 455 PHE DDD N     1 ? 4 
ATOM   14652 C CA    . PHE D 1 455 ? 56.732  21.219  81.079  1.000 35.465  0 455 PHE DDD CA    1 ? 4 
ATOM   14653 C C     . PHE D 1 455 ? 58.113  20.629  81.396  1.000 34.872  0 455 PHE DDD C     1 ? 4 
ATOM   14654 O O     . PHE D 1 455 ? 59.115  21.332  81.193  1.000 35.114  0 455 PHE DDD O     1 ? 4 
ATOM   14655 C CB    . PHE D 1 455 ? 56.485  21.326  79.574  1.000 33.932  0 455 PHE DDD CB    1 ? 4 
ATOM   14656 C CG    . PHE D 1 455 ? 56.777  20.055  78.825  1.000 33.098  0 455 PHE DDD CG    1 ? 4 
ATOM   14657 C CD1   . PHE D 1 455 ? 58.096  19.680  78.568  1.000 32.333  0 455 PHE DDD CD1   1 ? 4 
ATOM   14658 C CD2   . PHE D 1 455 ? 55.747  19.237  78.375  1.000 32.136  0 455 PHE DDD CD2   1 ? 4 
ATOM   14659 C CE1   . PHE D 1 455 ? 58.377  18.502  77.899  1.000 31.383  0 455 PHE DDD CE1   1 ? 4 
ATOM   14660 C CE2   . PHE D 1 455 ? 56.029  18.055  77.706  1.000 32.804  0 455 PHE DDD CE2   1 ? 4 
ATOM   14661 C CZ    . PHE D 1 455 ? 57.347  17.692  77.470  1.000 33.185  0 455 PHE DDD CZ    1 ? 4 
ATOM   14662 N N     . HIS D 1 456 ? 58.168  19.375  81.848  1.000 32.755  0 456 HIS DDD N     1 ? 4 
ATOM   14663 C CA    . HIS D 1 456 ? 59.373  18.734  82.416  1.000 32.427  0 456 HIS DDD CA    1 ? 4 
ATOM   14664 C C     . HIS D 1 456 ? 59.398  17.262  82.030  1.000 31.529  0 456 HIS DDD C     1 ? 4 
ATOM   14665 O O     . HIS D 1 456 ? 58.395  16.565  82.259  1.000 31.980  0 456 HIS DDD O     1 ? 4 
ATOM   14666 C CB    . HIS D 1 456 ? 59.364  18.830  83.944  1.000 34.799  0 456 HIS DDD CB    1 ? 4 
ATOM   14667 C CG    . HIS D 1 456 ? 59.391  20.232  84.434  1.000 36.292  0 456 HIS DDD CG    1 ? 4 
ATOM   14668 N ND1   . HIS D 1 456 ? 60.575  20.896  84.676  1.000 36.835  0 456 HIS DDD ND1   1 ? 4 
ATOM   14669 C CD2   . HIS D 1 456 ? 58.402  21.115  84.640  1.000 37.775  0 456 HIS DDD CD2   1 ? 4 
ATOM   14670 C CE1   . HIS D 1 456 ? 60.327  22.126  85.024  1.000 36.011  0 456 HIS DDD CE1   1 ? 4 
ATOM   14671 N NE2   . HIS D 1 456 ? 59.004  22.288  85.017  1.000 37.685  0 456 HIS DDD NE2   1 ? 4 
ATOM   14672 N N     . PHE D 1 457 ? 60.495  16.783  81.486  1.000 30.334  0 457 PHE DDD N     1 ? 4 
ATOM   14673 C CA    . PHE D 1 457 ? 60.561  15.366  81.066  1.000 30.867  0 457 PHE DDD CA    1 ? 4 
ATOM   14674 C C     . PHE D 1 457 ? 61.966  14.869  81.322  1.000 30.773  0 457 PHE DDD C     1 ? 4 
ATOM   14675 O O     . PHE D 1 457 ? 62.926  15.431  80.749  1.000 32.316  0 457 PHE DDD O     1 ? 4 
ATOM   14676 C CB    . PHE D 1 457 ? 60.173  15.133  79.598  1.000 29.736  0 457 PHE DDD CB    1 ? 4 
ATOM   14677 C CG    . PHE D 1 457 ? 60.257  13.673  79.253  1.000 29.061  0 457 PHE DDD CG    1 ? 4 
ATOM   14678 C CD1   . PHE D 1 457 ? 59.247  12.801  79.652  1.000 28.765  0 457 PHE DDD CD1   1 ? 4 
ATOM   14679 C CD2   . PHE D 1 457 ? 61.389  13.155  78.639  1.000 28.286  0 457 PHE DDD CD2   1 ? 4 
ATOM   14680 C CE1   . PHE D 1 457 ? 59.330  11.449  79.361  1.000 28.820  0 457 PHE DDD CE1   1 ? 4 
ATOM   14681 C CE2   . PHE D 1 457 ? 61.473  11.793  78.378  1.000 28.780  0 457 PHE DDD CE2   1 ? 4 
ATOM   14682 C CZ    . PHE D 1 457 ? 60.452  10.941  78.732  1.000 27.747  0 457 PHE DDD CZ    1 ? 4 
ATOM   14683 N N     . VAL D 1 458 ? 62.064  13.895  82.225  1.000 30.376  0 458 VAL DDD N     1 ? 4 
ATOM   14684 C CA    . VAL D 1 458 ? 63.295  13.131  82.500  1.000 29.766  0 458 VAL DDD CA    1 ? 4 
ATOM   14685 C C     . VAL D 1 458 ? 63.140  11.803  81.773  1.000 28.410  0 458 VAL DDD C     1 ? 4 
ATOM   14686 O O     . VAL D 1 458 ? 62.082  11.172  81.960  1.000 25.918  0 458 VAL DDD O     1 ? 4 
ATOM   14687 C CB    . VAL D 1 458 ? 63.499  12.947  84.015  1.000 30.893  0 458 VAL DDD CB    1 ? 4 
ATOM   14688 C CG1   . VAL D 1 458 ? 64.745  12.113  84.313  1.000 31.394  0 458 VAL DDD CG1   1 ? 4 
ATOM   14689 C CG2   . VAL D 1 458 ? 63.610  14.294  84.696  1.000 31.777  0 458 VAL DDD CG2   1 ? 4 
ATOM   14690 N N     . GLY D 1 459 ? 64.178  11.400  81.035  1.000 29.140  0 459 GLY DDD N     1 ? 4 
ATOM   14691 C CA    . GLY D 1 459 ? 64.177  10.119  80.294  1.000 30.627  0 459 GLY DDD CA    1 ? 4 
ATOM   14692 C C     . GLY D 1 459 ? 64.971  10.193  78.995  1.000 28.604  0 459 GLY DDD C     1 ? 4 
ATOM   14693 O O     . GLY D 1 459 ? 65.657  11.173  78.766  1.000 28.337  0 459 GLY DDD O     1 ? 4 
ATOM   14694 N N     . PRO D 1 460 ? 64.943  9.142   78.153  1.000 27.596  0 460 PRO DDD N     1 ? 4 
ATOM   14695 C CA    . PRO D 1 460 ? 65.696  9.137   76.896  1.000 26.737  0 460 PRO DDD CA    1 ? 4 
ATOM   14696 C C     . PRO D 1 460 ? 65.183  10.173  75.905  1.000 26.839  0 460 PRO DDD C     1 ? 4 
ATOM   14697 O O     . PRO D 1 460 ? 64.013  10.459  75.916  1.000 26.697  0 460 PRO DDD O     1 ? 4 
ATOM   14698 C CB    . PRO D 1 460 ? 65.506  7.741   76.294  1.000 27.219  0 460 PRO DDD CB    1 ? 4 
ATOM   14699 C CG    . PRO D 1 460 ? 65.001  6.901   77.504  1.000 28.768  0 460 PRO DDD CG    1 ? 4 
ATOM   14700 C CD    . PRO D 1 460 ? 64.231  7.877   78.384  1.000 28.649  0 460 PRO DDD CD    1 ? 4 
ATOM   14701 N N     . ASN D 1 461 ? 66.073  10.719  75.078  1.000 28.476  0 461 ASN DDD N     1 ? 4 
ATOM   14702 C CA    . ASN D 1 461 ? 65.672  11.618  73.966  1.000 28.697  0 461 ASN DDD CA    1 ? 4 
ATOM   14703 C C     . ASN D 1 461 ? 64.781  12.747  74.532  1.000 29.767  0 461 ASN DDD C     1 ? 4 
ATOM   14704 O O     . ASN D 1 461 ? 63.717  13.082  73.910  1.000 28.460  0 461 ASN DDD O     1 ? 4 
ATOM   14705 C CB    . ASN D 1 461 ? 64.939  10.786  72.916  1.000 28.016  0 461 ASN DDD CB    1 ? 4 
ATOM   14706 C CG    . ASN D 1 461 ? 65.669  9.497   72.644  1.000 29.019  0 461 ASN DDD CG    1 ? 4 
ATOM   14707 O OD1   . ASN D 1 461 ? 66.868  9.533   72.308  1.000 32.015  0 461 ASN DDD OD1   1 ? 4 
ATOM   14708 N ND2   . ASN D 1 461 ? 64.971  8.381   72.806  1.000 28.039  0 461 ASN DDD ND2   1 ? 4 
ATOM   14709 N N     . ALA D 1 462 ? 65.175  13.335  75.655  1.000 28.614  0 462 ALA DDD N     1 ? 4 
ATOM   14710 C CA    . ALA D 1 462 ? 64.326  14.336  76.331  1.000 30.323  0 462 ALA DDD CA    1 ? 4 
ATOM   14711 C C     . ALA D 1 462 ? 64.260  15.604  75.486  1.000 29.229  0 462 ALA DDD C     1 ? 4 
ATOM   14712 O O     . ALA D 1 462 ? 63.215  16.258  75.512  1.000 29.892  0 462 ALA DDD O     1 ? 4 
ATOM   14713 C CB    . ALA D 1 462 ? 64.836  14.618  77.732  1.000 30.902  0 462 ALA DDD CB    1 ? 4 
ATOM   14714 N N     . GLY D 1 463 ? 65.359  15.997  74.851  1.000 29.196  0 463 GLY DDD N     1 ? 4 
ATOM   14715 C CA    . GLY D 1 463 ? 65.353  17.165  73.957  1.000 30.221  0 463 GLY DDD CA    1 ? 4 
ATOM   14716 C C     . GLY D 1 463 ? 64.487  16.931  72.733  1.000 31.454  0 463 GLY DDD C     1 ? 4 
ATOM   14717 O O     . GLY D 1 463 ? 63.729  17.821  72.373  1.000 32.204  0 463 GLY DDD O     1 ? 4 
ATOM   14718 N N     . GLU D 1 464 ? 64.550  15.743  72.154  1.000 32.721  0 464 GLU DDD N     1 ? 4 
ATOM   14719 C CA    . GLU D 1 464 ? 63.694  15.369  71.005  1.000 32.841  0 464 GLU DDD CA    1 ? 4 
ATOM   14720 C C     . GLU D 1 464 ? 62.228  15.502  71.433  1.000 31.296  0 464 GLU DDD C     1 ? 4 
ATOM   14721 O O     . GLU D 1 464 ? 61.396  15.964  70.605  1.000 31.397  0 464 GLU DDD O     1 ? 4 
ATOM   14722 C CB    . GLU D 1 464 ? 64.063  13.980  70.449  1.000 32.491  0 464 GLU DDD CB    1 ? 4 
ATOM   14723 C CG    . GLU D 1 464 ? 65.525  13.803  70.049  1.000 31.900  0 464 GLU DDD CG    1 ? 4 
ATOM   14724 C CD    . GLU D 1 464 ? 66.086  14.682  68.927  1.000 34.432  0 464 GLU DDD CD    1 ? 4 
ATOM   14725 O OE1   . GLU D 1 464 ? 65.260  15.396  68.250  1.000 36.354  0 464 GLU DDD OE1   1 ? 4 
ATOM   14726 O OE2   . GLU D 1 464 ? 67.375  14.678  68.706  1.000 31.636  0 464 GLU DDD OE2   1 ? 4 
ATOM   14727 N N     . ILE D 1 465 ? 61.896  15.140  72.665  1.000 30.943  0 465 ILE DDD N     1 ? 4 
ATOM   14728 C CA    . ILE D 1 465 ? 60.483  15.117  73.141  1.000 29.175  0 465 ILE DDD CA    1 ? 4 
ATOM   14729 C C     . ILE D 1 465 ? 60.055  16.553  73.433  1.000 28.623  0 465 ILE DDD C     1 ? 4 
ATOM   14730 O O     . ILE D 1 465 ? 58.877  16.896  73.134  1.000 27.784  0 465 ILE DDD O     1 ? 4 
ATOM   14731 C CB    . ILE D 1 465 ? 60.331  14.184  74.361  1.000 29.765  0 465 ILE DDD CB    1 ? 4 
ATOM   14732 C CG1   . ILE D 1 465 ? 60.410  12.729  73.889  1.000 30.144  0 465 ILE DDD CG1   1 ? 4 
ATOM   14733 C CG2   . ILE D 1 465 ? 59.052  14.470  75.141  1.000 30.340  0 465 ILE DDD CG2   1 ? 4 
ATOM   14734 C CD1   . ILE D 1 465 ? 60.622  11.712  74.992  1.000 29.864  0 465 ILE DDD CD1   1 ? 4 
ATOM   14735 N N     . THR D 1 466 ? 60.969  17.374  73.941  1.000 27.212  0 466 THR DDD N     1 ? 4 
ATOM   14736 C CA    . THR D 1 466 ? 60.584  18.646  74.575  1.000 28.630  0 466 THR DDD CA    1 ? 4 
ATOM   14737 C C     . THR D 1 466 ? 60.391  19.705  73.511  1.000 29.859  0 466 THR DDD C     1 ? 4 
ATOM   14738 O O     . THR D 1 466 ? 59.617  20.653  73.768  1.000 32.597  0 466 THR DDD O     1 ? 4 
ATOM   14739 C CB    . THR D 1 466 ? 61.636  19.115  75.584  1.000 28.316  0 466 THR DDD CB    1 ? 4 
ATOM   14740 O OG1   . THR D 1 466 ? 61.617  18.209  76.679  1.000 28.301  0 466 THR DDD OG1   1 ? 4 
ATOM   14741 C CG2   . THR D 1 466 ? 61.387  20.521  76.075  1.000 27.733  0 466 THR DDD CG2   1 ? 4 
ATOM   14742 N N     . GLN D 1 467 ? 61.136  19.611  72.411  1.000 29.265  0 467 GLN DDD N     1 ? 4 
ATOM   14743 C CA    . GLN D 1 467 ? 61.132  20.675  71.378  1.000 29.460  0 467 GLN DDD CA    1 ? 4 
ATOM   14744 C C     . GLN D 1 467 ? 59.685  21.017  71.015  1.000 28.767  0 467 GLN DDD C     1 ? 4 
ATOM   14745 O O     . GLN D 1 467 ? 59.291  22.170  71.155  1.000 28.016  0 467 GLN DDD O     1 ? 4 
ATOM   14746 C CB    . GLN D 1 467 ? 61.880  20.227  70.132  1.000 29.075  0 467 GLN DDD CB    1 ? 4 
ATOM   14747 C CG    . GLN D 1 467 ? 62.096  21.351  69.127  1.000 29.369  0 467 GLN DDD CG    1 ? 4 
ATOM   14748 C CD    . GLN D 1 467 ? 63.006  22.427  69.659  1.000 29.214  0 467 GLN DDD CD    1 ? 4 
ATOM   14749 O OE1   . GLN D 1 467 ? 64.246  22.300  69.635  1.000 30.505  0 467 GLN DDD OE1   1 ? 4 
ATOM   14750 N NE2   . GLN D 1 467 ? 62.396  23.505  70.128  1.000 29.589  0 467 GLN DDD NE2   1 ? 4 
ATOM   14751 N N     . GLY D 1 468 ? 58.910  20.021  70.618  1.000 29.418  0 468 GLY DDD N     1 ? 4 
ATOM   14752 C CA    . GLY D 1 468 ? 57.542  20.229  70.118  1.000 30.632  0 468 GLY DDD CA    1 ? 4 
ATOM   14753 C C     . GLY D 1 468 ? 56.619  20.743  71.195  1.000 31.896  0 468 GLY DDD C     1 ? 4 
ATOM   14754 O O     . GLY D 1 468 ? 55.827  21.657  70.953  1.000 33.382  0 468 GLY DDD O     1 ? 4 
ATOM   14755 N N     . PHE D 1 469 ? 56.680  20.120  72.347  1.000 33.359  0 469 PHE DDD N     1 ? 4 
ATOM   14756 C CA    . PHE D 1 469 ? 55.841  20.470  73.507  1.000 32.578  0 469 PHE DDD CA    1 ? 4 
ATOM   14757 C C     . PHE D 1 469 ? 56.160  21.907  73.909  1.000 35.099  0 469 PHE DDD C     1 ? 4 
ATOM   14758 O O     . PHE D 1 469 ? 55.206  22.630  74.223  1.000 35.162  0 469 PHE DDD O     1 ? 4 
ATOM   14759 C CB    . PHE D 1 469 ? 56.097  19.468  74.628  1.000 30.819  0 469 PHE DDD CB    1 ? 4 
ATOM   14760 C CG    . PHE D 1 469 ? 55.299  18.212  74.467  1.000 29.019  0 469 PHE DDD CG    1 ? 4 
ATOM   14761 C CD1   . PHE D 1 469 ? 53.909  18.266  74.424  1.000 28.094  0 469 PHE DDD CD1   1 ? 4 
ATOM   14762 C CD2   . PHE D 1 469 ? 55.924  16.986  74.389  1.000 27.582  0 469 PHE DDD CD2   1 ? 4 
ATOM   14763 C CE1   . PHE D 1 469 ? 53.174  17.104  74.327  1.000 27.491  0 469 PHE DDD CE1   1 ? 4 
ATOM   14764 C CE2   . PHE D 1 469 ? 55.180  15.820  74.311  1.000 27.330  0 469 PHE DDD CE2   1 ? 4 
ATOM   14765 C CZ    . PHE D 1 469 ? 53.809  15.888  74.262  1.000 28.097  0 469 PHE DDD CZ    1 ? 4 
ATOM   14766 N N     . SER D 1 470 ? 57.429  22.320  73.829  1.000 35.834  0 470 SER DDD N     1 ? 4 
ATOM   14767 C CA    . SER D 1 470 ? 57.825  23.718  74.112  1.000 36.591  0 470 SER DDD CA    1 ? 4 
ATOM   14768 C C     . SER D 1 470 ? 57.025  24.698  73.246  1.000 36.461  0 470 SER DDD C     1 ? 4 
ATOM   14769 O O     . SER D 1 470 ? 56.522  25.681  73.790  1.000 37.915  0 470 SER DDD O     1 ? 4 
ATOM   14770 C CB    . SER D 1 470 ? 59.329  23.932  74.007  1.000 34.780  0 470 SER DDD CB    1 ? 4 
ATOM   14771 O OG    . SER D 1 470 ? 59.749  24.082  72.679  1.000 35.006  0 470 SER DDD OG    1 ? 4 
ATOM   14772 N N     . LEU D 1 471 ? 56.920  24.442  71.947  1.000 38.166  0 471 LEU DDD N     1 ? 4 
ATOM   14773 C CA    . LEU D 1 471 ? 56.113  25.279  71.026  1.000 38.049  0 471 LEU DDD CA    1 ? 4 
ATOM   14774 C C     . LEU D 1 471 ? 54.643  25.261  71.466  1.000 39.500  0 471 LEU DDD C     1 ? 4 
ATOM   14775 O O     . LEU D 1 471 ? 54.030  26.341  71.477  1.000 38.930  0 471 LEU DDD O     1 ? 4 
ATOM   14776 C CB    . LEU D 1 471 ? 56.236  24.746  69.602  1.000 37.787  0 471 LEU DDD CB    1 ? 4 
ATOM   14777 C CG    . LEU D 1 471 ? 55.385  25.496  68.577  1.000 37.222  0 471 LEU DDD CG    1 ? 4 
ATOM   14778 C CD1   . LEU D 1 471 ? 55.695  26.968  68.613  1.000 37.443  0 471 LEU DDD CD1   1 ? 4 
ATOM   14779 C CD2   . LEU D 1 471 ? 55.615  24.967  67.180  1.000 36.749  0 471 LEU DDD CD2   1 ? 4 
ATOM   14780 N N     . ALA D 1 472 ? 54.080  24.079  71.742  1.000 40.870  0 472 ALA DDD N     1 ? 4 
ATOM   14781 C CA    . ALA D 1 472 ? 52.666  23.913  72.159  1.000 40.874  0 472 ALA DDD CA    1 ? 4 
ATOM   14782 C C     . ALA D 1 472 ? 52.449  24.717  73.435  1.000 41.642  0 472 ALA DDD C     1 ? 4 
ATOM   14783 O O     . ALA D 1 472 ? 51.400  25.397  73.556  1.000 40.916  0 472 ALA DDD O     1 ? 4 
ATOM   14784 C CB    . ALA D 1 472 ? 52.324  22.459  72.370  1.000 40.368  0 472 ALA DDD CB    1 ? 4 
ATOM   14785 N N     . VAL D 1 473 ? 53.400  24.649  74.364  1.000 40.978  0 473 VAL DDD N     1 ? 4 
ATOM   14786 C CA    . VAL D 1 473 ? 53.228  25.347  75.666  1.000 43.706  0 473 VAL DDD CA    1 ? 4 
ATOM   14787 C C     . VAL D 1 473 ? 53.260  26.854  75.386  1.000 45.469  0 473 VAL DDD C     1 ? 4 
ATOM   14788 O O     . VAL D 1 473 ? 52.435  27.580  75.980  1.000 45.239  0 473 VAL DDD O     1 ? 4 
ATOM   14789 C CB    . VAL D 1 473 ? 54.251  24.891  76.715  1.000 44.834  0 473 VAL DDD CB    1 ? 4 
ATOM   14790 C CG1   . VAL D 1 473 ? 54.350  25.841  77.906  1.000 46.961  0 473 VAL DDD CG1   1 ? 4 
ATOM   14791 C CG2   . VAL D 1 473 ? 53.937  23.474  77.186  1.000 46.451  0 473 VAL DDD CG2   1 ? 4 
ATOM   14792 N N     . LYS D 1 474 ? 54.116  27.296  74.457  1.000 46.672  0 474 LYS DDD N     1 ? 4 
ATOM   14793 C CA    . LYS D 1 474 ? 54.245  28.734  74.086  1.000 48.277  0 474 LYS DDD CA    1 ? 4 
ATOM   14794 C C     . LYS D 1 474 ? 52.927  29.252  73.481  1.000 47.669  0 474 LYS DDD C     1 ? 4 
ATOM   14795 O O     . LYS D 1 474 ? 52.579  30.426  73.747  1.000 47.481  0 474 LYS DDD O     1 ? 4 
ATOM   14796 C CB    . LYS D 1 474 ? 55.431  28.920  73.141  1.000 47.520  0 474 LYS DDD CB    1 ? 4 
ATOM   14797 C CG    . LYS D 1 474 ? 55.685  30.356  72.714  1.000 48.995  0 474 LYS DDD CG    1 ? 4 
ATOM   14798 C CD    . LYS D 1 474 ? 56.502  30.507  71.454  1.000 47.081  0 474 LYS DDD CD    1 ? 4 
ATOM   14799 C CE    . LYS D 1 474 ? 57.227  31.833  71.410  1.000 46.296  0 474 LYS DDD CE    1 ? 4 
ATOM   14800 N NZ    . LYS D 1 474 ? 58.446  31.732  70.586  1.000 47.051  0 474 LYS DDD NZ    1 ? 4 
ATOM   14801 N N     . LEU D 1 475 ? 52.211  28.395  72.744  1.000 46.614  0 475 LEU DDD N     1 ? 4 
ATOM   14802 C CA    . LEU D 1 475 ? 50.940  28.742  72.055  1.000 47.552  0 475 LEU DDD CA    1 ? 4 
ATOM   14803 C C     . LEU D 1 475 ? 49.749  28.687  73.027  1.000 47.319  0 475 LEU DDD C     1 ? 4 
ATOM   14804 O O     . LEU D 1 475 ? 48.622  28.971  72.572  1.000 47.826  0 475 LEU DDD O     1 ? 4 
ATOM   14805 C CB    . LEU D 1 475 ? 50.718  27.806  70.858  1.000 48.141  0 475 LEU DDD CB    1 ? 4 
ATOM   14806 C CG    . LEU D 1 475 ? 51.648  27.998  69.653  1.000 48.407  0 475 LEU DDD CG    1 ? 4 
ATOM   14807 C CD1   . LEU D 1 475 ? 51.315  26.998  68.564  1.000 48.146  0 475 LEU DDD CD1   1 ? 4 
ATOM   14808 C CD2   . LEU D 1 475 ? 51.634  29.411  69.092  1.000 47.821  0 475 LEU DDD CD2   1 ? 4 
ATOM   14809 N N     . GLY D 1 476 ? 49.955  28.288  74.286  1.000 47.595  0 476 GLY DDD N     1 ? 4 
ATOM   14810 C CA    . GLY D 1 476 ? 48.964  28.430  75.372  1.000 49.019  0 476 GLY DDD CA    1 ? 4 
ATOM   14811 C C     . GLY D 1 476 ? 48.179  27.158  75.633  1.000 48.563  0 476 GLY DDD C     1 ? 4 
ATOM   14812 O O     . GLY D 1 476 ? 46.953  27.245  75.945  1.000 48.696  0 476 GLY DDD O     1 ? 4 
ATOM   14813 N N     . ALA D 1 477 ? 48.840  26.008  75.505  1.000 46.252  0 477 ALA DDD N     1 ? 4 
ATOM   14814 C CA    . ALA D 1 477 ? 48.226  24.674  75.682  1.000 43.119  0 477 ALA DDD CA    1 ? 4 
ATOM   14815 C C     . ALA D 1 477 ? 47.728  24.536  77.131  1.000 41.041  0 477 ALA DDD C     1 ? 4 
ATOM   14816 O O     . ALA D 1 477 ? 48.454  24.922  78.039  1.000 40.251  0 477 ALA DDD O     1 ? 4 
ATOM   14817 C CB    . ALA D 1 477 ? 49.230  23.606  75.314  1.000 42.376  0 477 ALA DDD CB    1 ? 4 
ATOM   14818 N N     . THR D 1 478 ? 46.535  23.981  77.320  1.000 39.056  0 478 THR DDD N     1 ? 4 
ATOM   14819 C CA    . THR D 1 478 ? 45.927  23.723  78.652  1.000 39.780  0 478 THR DDD CA    1 ? 4 
ATOM   14820 C C     . THR D 1 478 ? 46.051  22.238  78.995  1.000 41.008  0 478 THR DDD C     1 ? 4 
ATOM   14821 O O     . THR D 1 478 ? 46.249  21.412  78.069  1.000 43.617  0 478 THR DDD O     1 ? 4 
ATOM   14822 C CB    . THR D 1 478 ? 44.438  24.112  78.666  1.000 38.087  0 478 THR DDD CB    1 ? 4 
ATOM   14823 O OG1   . THR D 1 478 ? 43.788  23.258  77.730  1.000 35.249  0 478 THR DDD OG1   1 ? 4 
ATOM   14824 C CG2   . THR D 1 478 ? 44.177  25.546  78.270  1.000 37.227  0 478 THR DDD CG2   1 ? 4 
ATOM   14825 N N     . LYS D 1 479 ? 45.850  21.882  80.258  1.000 42.269  0 479 LYS DDD N     1 ? 4 
ATOM   14826 C CA    . LYS D 1 479 ? 45.793  20.454  80.662  1.000 42.470  0 479 LYS DDD CA    1 ? 4 
ATOM   14827 C C     . LYS D 1 479 ? 44.741  19.729  79.816  1.000 43.099  0 479 LYS DDD C     1 ? 4 
ATOM   14828 O O     . LYS D 1 479 ? 44.996  18.563  79.471  1.000 43.896  0 479 LYS DDD O     1 ? 4 
ATOM   14829 C CB    . LYS D 1 479 ? 45.551  20.305  82.168  1.000 42.261  0 479 LYS DDD CB    1 ? 4 
ATOM   14830 C CG    . LYS D 1 479 ? 45.561  18.868  82.655  1.000 43.166  0 479 LYS DDD CG    1 ? 4 
ATOM   14831 C CD    . LYS D 1 479 ? 46.753  18.060  82.165  1.000 44.553  0 479 LYS DDD CD    1 ? 4 
ATOM   14832 C CE    . LYS D 1 479 ? 46.965  16.787  82.947  1.000 46.837  0 479 LYS DDD CE    1 ? 4 
ATOM   14833 N NZ    . LYS D 1 479 ? 45.761  15.917  82.968  1.000 47.354  0 479 LYS DDD NZ    1 ? 4 
ATOM   14834 N N     . LYS D 1 480 ? 43.611  20.379  79.478  1.000 45.596  0 480 LYS DDD N     1 ? 4 
ATOM   14835 C CA    . LYS D 1 480 ? 42.529  19.753  78.657  1.000 45.399  0 480 LYS DDD CA    1 ? 4 
ATOM   14836 C C     . LYS D 1 480 ? 43.108  19.399  77.279  1.000 43.561  0 480 LYS DDD C     1 ? 4 
ATOM   14837 O O     . LYS D 1 480 ? 42.900  18.280  76.821  1.000 43.445  0 480 LYS DDD O     1 ? 4 
ATOM   14838 C CB    . LYS D 1 480 ? 41.301  20.677  78.593  1.000 46.454  0 480 LYS DDD CB    1 ? 4 
ATOM   14839 C CG    . LYS D 1 480 ? 40.239  20.322  77.555  1.000 47.836  0 480 LYS DDD CG    1 ? 4 
ATOM   14840 C CD    . LYS D 1 480 ? 38.811  20.659  77.980  1.000 49.793  0 480 LYS DDD CD    1 ? 4 
ATOM   14841 C CE    . LYS D 1 480 ? 37.797  20.622  76.855  1.000 48.838  0 480 LYS DDD CE    1 ? 4 
ATOM   14842 N NZ    . LYS D 1 480 ? 37.852  19.370  76.063  1.000 46.724  0 480 LYS DDD NZ    1 ? 4 
ATOM   14843 N N     . ASP D 1 481 ? 43.835  20.327  76.651  1.000 44.524  0 481 ASP DDD N     1 ? 4 
ATOM   14844 C CA    . ASP D 1 481 ? 44.520  20.112  75.341  1.000 43.525  0 481 ASP DDD CA    1 ? 4 
ATOM   14845 C C     . ASP D 1 481 ? 45.416  18.882  75.406  1.000 40.498  0 481 ASP DDD C     1 ? 4 
ATOM   14846 O O     . ASP D 1 481 ? 45.396  18.129  74.445  1.000 38.977  0 481 ASP DDD O     1 ? 4 
ATOM   14847 C CB    . ASP D 1 481 ? 45.397  21.312  74.960  1.000 44.773  0 481 ASP DDD CB    1 ? 4 
ATOM   14848 C CG    . ASP D 1 481 ? 44.592  22.545  74.645  1.000 45.256  0 481 ASP DDD CG    1 ? 4 
ATOM   14849 O OD1   . ASP D 1 481 ? 43.481  22.351  74.137  1.000 46.776  0 481 ASP DDD OD1   1 ? 4 
ATOM   14850 O OD2   . ASP D 1 481 ? 45.085  23.665  74.921  1.000 46.050  0 481 ASP DDD OD2   1 ? 4 
ATOM   14851 N N     . PHE D 1 482 ? 46.146  18.707  76.511  1.000 38.913  0 482 PHE DDD N     1 ? 4 
ATOM   14852 C CA    . PHE D 1 482 ? 47.051  17.550  76.737  1.000 37.510  0 482 PHE DDD CA    1 ? 4 
ATOM   14853 C C     . PHE D 1 482 ? 46.239  16.256  76.855  1.000 37.796  0 482 PHE DDD C     1 ? 4 
ATOM   14854 O O     . PHE D 1 482 ? 46.626  15.277  76.247  1.000 37.099  0 482 PHE DDD O     1 ? 4 
ATOM   14855 C CB    . PHE D 1 482 ? 47.949  17.819  77.936  1.000 35.604  0 482 PHE DDD CB    1 ? 4 
ATOM   14856 C CG    . PHE D 1 482 ? 49.215  18.572  77.611  1.000 34.979  0 482 PHE DDD CG    1 ? 4 
ATOM   14857 C CD1   . PHE D 1 482 ? 49.222  19.946  77.500  1.000 34.559  0 482 PHE DDD CD1   1 ? 4 
ATOM   14858 C CD2   . PHE D 1 482 ? 50.415  17.901  77.447  1.000 34.276  0 482 PHE DDD CD2   1 ? 4 
ATOM   14859 C CE1   . PHE D 1 482 ? 50.398  20.628  77.239  1.000 35.118  0 482 PHE DDD CE1   1 ? 4 
ATOM   14860 C CE2   . PHE D 1 482 ? 51.590  18.589  77.201  1.000 33.260  0 482 PHE DDD CE2   1 ? 4 
ATOM   14861 C CZ    . PHE D 1 482 ? 51.580  19.947  77.072  1.000 32.582  0 482 PHE DDD CZ    1 ? 4 
ATOM   14862 N N     . ASP D 1 483 ? 45.117  16.272  77.564  1.000 39.120  0 483 ASP DDD N     1 ? 4 
ATOM   14863 C CA    . ASP D 1 483 ? 44.256  15.070  77.757  1.000 40.229  0 483 ASP DDD CA    1 ? 4 
ATOM   14864 C C     . ASP D 1 483 ? 43.563  14.677  76.446  1.000 39.156  0 483 ASP DDD C     1 ? 4 
ATOM   14865 O O     . ASP D 1 483 ? 43.281  13.487  76.296  1.000 38.769  0 483 ASP DDD O     1 ? 4 
ATOM   14866 C CB    . ASP D 1 483 ? 43.171  15.301  78.811  1.000 43.207  0 483 ASP DDD CB    1 ? 4 
ATOM   14867 C CG    . ASP D 1 483 ? 43.685  15.442  80.224  1.000 44.635  0 483 ASP DDD CG    1 ? 4 
ATOM   14868 O OD1   . ASP D 1 483 ? 44.826  15.065  80.464  1.000 45.972  0 483 ASP DDD OD1   1 ? 4 
ATOM   14869 O OD2   . ASP D 1 483 ? 42.931  15.966  81.070  1.000 50.135  0 483 ASP DDD OD2   1 ? 4 
ATOM   14870 N N     . ASP D 1 484 ? 43.247  15.630  75.568  1.000 37.073  0 484 ASP DDD N     1 ? 4 
ATOM   14871 C CA    . ASP D 1 484 ? 42.508  15.367  74.307  1.000 37.006  0 484 ASP DDD CA    1 ? 4 
ATOM   14872 C C     . ASP D 1 484 ? 43.506  15.125  73.158  1.000 36.274  0 484 ASP DDD C     1 ? 4 
ATOM   14873 O O     . ASP D 1 484 ? 43.062  15.012  71.969  1.000 36.645  0 484 ASP DDD O     1 ? 4 
ATOM   14874 C CB    . ASP D 1 484 ? 41.582  16.533  73.943  1.000 38.132  0 484 ASP DDD CB    1 ? 4 
ATOM   14875 C CG    . ASP D 1 484 ? 40.530  16.909  74.977  1.000 38.429  0 484 ASP DDD CG    1 ? 4 
ATOM   14876 O OD1   . ASP D 1 484 ? 40.387  16.180  76.003  1.000 34.426  0 484 ASP DDD OD1   1 ? 4 
ATOM   14877 O OD2   . ASP D 1 484 ? 39.899  17.970  74.746  1.000 39.609  0 484 ASP DDD OD2   1 ? 4 
ATOM   14878 N N     . MET D 1 485 ? 44.816  15.195  73.437  1.000 35.277  0 485 MET DDD N     1 ? 4 
ATOM   14879 C CA    . MET D 1 485 ? 45.909  14.945  72.446  1.000 34.956  0 485 MET DDD CA    1 ? 4 
ATOM   14880 C C     . MET D 1 485 ? 45.974  13.440  72.185  1.000 33.727  0 485 MET DDD C     1 ? 4 
ATOM   14881 O O     . MET D 1 485 ? 46.117  12.646  73.176  1.000 34.463  0 485 MET DDD O     1 ? 4 
ATOM   14882 C CB    . MET D 1 485 ? 47.259  15.443  72.968  1.000 36.437  0 485 MET DDD CB    1 ? 4 
ATOM   14883 C CG    . MET D 1 485 ? 48.458  14.944  72.168  1.000 38.424  0 485 MET DDD CG    1 ? 4 
ATOM   14884 S SD    . MET D 1 485 ? 50.086  15.323  72.866  1.000 40.314  0 485 MET DDD SD    1 ? 4 
ATOM   14885 C CE    . MET D 1 485 ? 49.892  14.808  74.575  1.000 42.001  0 485 MET DDD CE    1 ? 4 
ATOM   14886 N N     . ILE D 1 486 ? 45.878  13.024  70.926  1.000 32.614  0 486 ILE DDD N     1 ? 4 
ATOM   14887 C CA    . ILE D 1 486 ? 46.036  11.587  70.576  1.000 33.189  0 486 ILE DDD CA    1 ? 4 
ATOM   14888 C C     . ILE D 1 486 ? 47.519  11.234  70.652  1.000 34.370  0 486 ILE DDD C     1 ? 4 
ATOM   14889 O O     . ILE D 1 486 ? 48.386  12.011  70.132  1.000 33.098  0 486 ILE DDD O     1 ? 4 
ATOM   14890 C CB    . ILE D 1 486 ? 45.426  11.244  69.210  1.000 32.990  0 486 ILE DDD CB    1 ? 4 
ATOM   14891 C CG1   . ILE D 1 486 ? 43.948  11.666  69.138  1.000 34.003  0 486 ILE DDD CG1   1 ? 4 
ATOM   14892 C CG2   . ILE D 1 486 ? 45.617  9.761   68.900  1.000 32.612  0 486 ILE DDD CG2   1 ? 4 
ATOM   14893 C CD1   . ILE D 1 486 ? 43.006  10.797  69.902  1.000 33.378  0 486 ILE DDD CD1   1 ? 4 
ATOM   14894 N N     . GLY D 1 487 ? 47.770  10.106  71.320  1.000 35.135  0 487 GLY DDD N     1 ? 4 
ATOM   14895 C CA    . GLY D 1 487 ? 49.104  9.562   71.597  1.000 33.088  0 487 GLY DDD CA    1 ? 4 
ATOM   14896 C C     . GLY D 1 487 ? 49.605  8.796   70.385  1.000 33.355  0 487 GLY DDD C     1 ? 4 
ATOM   14897 O O     . GLY D 1 487 ? 48.766  8.299   69.578  1.000 32.715  0 487 GLY DDD O     1 ? 4 
ATOM   14898 N N     . ILE D 1 488 ? 50.927  8.801   70.215  1.000 30.675  0 488 ILE DDD N     1 ? 4 
ATOM   14899 C CA    . ILE D 1 488 ? 51.683  7.867   69.337  1.000 31.603  0 488 ILE DDD CA    1 ? 4 
ATOM   14900 C C     . ILE D 1 488 ? 52.200  6.762   70.242  1.000 29.920  0 488 ILE DDD C     1 ? 4 
ATOM   14901 O O     . ILE D 1 488 ? 52.856  7.080   71.242  1.000 29.488  0 488 ILE DDD O     1 ? 4 
ATOM   14902 C CB    . ILE D 1 488 ? 52.858  8.564   68.606  1.000 31.151  0 488 ILE DDD CB    1 ? 4 
ATOM   14903 C CG1   . ILE D 1 488 ? 52.403  9.845   67.892  1.000 30.690  0 488 ILE DDD CG1   1 ? 4 
ATOM   14904 C CG2   . ILE D 1 488 ? 53.510  7.597   67.663  1.000 29.860  0 488 ILE DDD CG2   1 ? 4 
ATOM   14905 C CD1   . ILE D 1 488 ? 53.520  10.648  67.294  1.000 30.285  0 488 ILE DDD CD1   1 ? 4 
ATOM   14906 N N     . HIS D 1 489 ? 51.864  5.524   69.915  1.000 29.655  0 489 HIS DDD N     1 ? 4 
ATOM   14907 C CA    . HIS D 1 489 ? 52.209  4.315   70.694  1.000 29.945  0 489 HIS DDD CA    1 ? 4 
ATOM   14908 C C     . HIS D 1 489 ? 53.092  3.411   69.845  1.000 30.019  0 489 HIS DDD C     1 ? 4 
ATOM   14909 O O     . HIS D 1 489 ? 52.859  3.269   68.653  1.000 29.870  0 489 HIS DDD O     1 ? 4 
ATOM   14910 C CB    . HIS D 1 489 ? 50.936  3.602   71.063  1.000 32.464  0 489 HIS DDD CB    1 ? 4 
ATOM   14911 C CG    . HIS D 1 489 ? 51.139  2.460   71.986  1.000 35.509  0 489 HIS DDD CG    1 ? 4 
ATOM   14912 N ND1   . HIS D 1 489 ? 51.749  2.590   73.218  1.000 37.202  0 489 HIS DDD ND1   1 ? 4 
ATOM   14913 C CD2   . HIS D 1 489 ? 50.740  1.188   71.901  1.000 37.207  0 489 HIS DDD CD2   1 ? 4 
ATOM   14914 C CE1   . HIS D 1 489 ? 51.732  1.428   73.837  1.000 39.643  0 489 HIS DDD CE1   1 ? 4 
ATOM   14915 N NE2   . HIS D 1 489 ? 51.096  0.556   73.070  1.000 38.180  0 489 HIS DDD NE2   1 ? 4 
ATOM   14916 N N     . PRO D 1 490 ? 54.136  2.766   70.397  1.000 29.954  0 490 PRO DDD N     1 ? 4 
ATOM   14917 C CA    . PRO D 1 490 ? 54.609  3.014   71.754  1.000 32.122  0 490 PRO DDD CA    1 ? 4 
ATOM   14918 C C     . PRO D 1 490 ? 55.685  4.107   71.759  1.000 32.117  0 490 PRO DDD C     1 ? 4 
ATOM   14919 O O     . PRO D 1 490 ? 56.682  3.962   71.045  1.000 33.358  0 490 PRO DDD O     1 ? 4 
ATOM   14920 C CB    . PRO D 1 490 ? 55.207  1.662   72.175  1.000 31.230  0 490 PRO DDD CB    1 ? 4 
ATOM   14921 C CG    . PRO D 1 490 ? 55.081  0.793   70.930  1.000 31.095  0 490 PRO DDD CG    1 ? 4 
ATOM   14922 C CD    . PRO D 1 490 ? 54.927  1.725   69.755  1.000 29.727  0 490 PRO DDD CD    1 ? 4 
ATOM   14923 N N     . THR D 1 491 ? 55.457  5.159   72.542  1.000 29.779  0 491 THR DDD N     1 ? 4 
ATOM   14924 C CA    . THR D 1 491 ? 56.474  6.191   72.840  1.000 29.422  0 491 THR DDD CA    1 ? 4 
ATOM   14925 C C     . THR D 1 491 ? 56.503  6.425   74.348  1.000 29.185  0 491 THR DDD C     1 ? 4 
ATOM   14926 O O     . THR D 1 491 ? 55.619  5.967   75.036  1.000 28.813  0 491 THR DDD O     1 ? 4 
ATOM   14927 C CB    . THR D 1 491 ? 56.205  7.485   72.070  1.000 29.630  0 491 THR DDD CB    1 ? 4 
ATOM   14928 O OG1   . THR D 1 491 ? 54.989  8.071   72.535  1.000 29.373  0 491 THR DDD OG1   1 ? 4 
ATOM   14929 C CG2   . THR D 1 491 ? 56.087  7.288   70.575  1.000 30.171  0 491 THR DDD CG2   1 ? 4 
ATOM   14930 N N     . ASP D 1 492 ? 57.495  7.136   74.819  1.000 29.991  0 492 ASP DDD N     1 ? 4 
ATOM   14931 C CA    . ASP D 1 492 ? 57.506  7.752   76.172  1.000 31.148  0 492 ASP DDD CA    1 ? 4 
ATOM   14932 C C     . ASP D 1 492 ? 56.655  9.032   76.115  1.000 31.703  0 492 ASP DDD C     1 ? 4 
ATOM   14933 O O     . ASP D 1 492 ? 55.996  9.336   77.113  1.000 33.917  0 492 ASP DDD O     1 ? 4 
ATOM   14934 C CB    . ASP D 1 492 ? 58.952  7.978   76.624  1.000 30.738  0 492 ASP DDD CB    1 ? 4 
ATOM   14935 C CG    . ASP D 1 492 ? 59.711  6.669   76.810  1.000 33.398  0 492 ASP DDD CG    1 ? 4 
ATOM   14936 O OD1   . ASP D 1 492 ? 59.053  5.626   77.062  1.000 35.535  0 492 ASP DDD OD1   1 ? 4 
ATOM   14937 O OD2   . ASP D 1 492 ? 60.965  6.673   76.740  1.000 37.421  0 492 ASP DDD OD2   1 ? 4 
ATOM   14938 N N     . ALA D 1 493 ? 56.650  9.780   75.007  1.000 30.378  0 493 ALA DDD N     1 ? 4 
ATOM   14939 C CA    . ALA D 1 493 ? 56.038  11.130  74.973  1.000 31.120  0 493 ALA DDD CA    1 ? 4 
ATOM   14940 C C     . ALA D 1 493 ? 54.505  11.034  75.001  1.000 32.581  0 493 ALA DDD C     1 ? 4 
ATOM   14941 O O     . ALA D 1 493 ? 53.864  12.066  75.318  1.000 33.326  0 493 ALA DDD O     1 ? 4 
ATOM   14942 C CB    . ALA D 1 493 ? 56.489  11.914  73.785  1.000 30.300  0 493 ALA DDD CB    1 ? 4 
ATOM   14943 N N     . GLU D 1 494 ? 53.917  9.874   74.693  1.000 33.001  0 494 GLU DDD N     1 ? 4 
ATOM   14944 C CA    . GLU D 1 494 ? 52.430  9.698   74.772  1.000 34.215  0 494 GLU DDD CA    1 ? 4 
ATOM   14945 C C     . GLU D 1 494 ? 51.978  9.797   76.235  1.000 33.051  0 494 GLU DDD C     1 ? 4 
ATOM   14946 O O     . GLU D 1 494 ? 50.803  10.100  76.475  1.000 31.726  0 494 GLU DDD O     1 ? 4 
ATOM   14947 C CB    . GLU D 1 494 ? 51.970  8.396   74.125  1.000 34.503  0 494 GLU DDD CB    1 ? 4 
ATOM   14948 C CG    . GLU D 1 494 ? 52.415  7.133   74.867  1.000 37.135  0 494 GLU DDD CG    1 ? 4 
ATOM   14949 C CD    . GLU D 1 494 ? 51.837  5.858   74.275  1.000 37.353  0 494 GLU DDD CD    1 ? 4 
ATOM   14950 O OE1   . GLU D 1 494 ? 50.646  5.880   73.925  1.000 38.981  0 494 GLU DDD OE1   1 ? 4 
ATOM   14951 O OE2   . GLU D 1 494 ? 52.577  4.854   74.150  1.000 41.477  0 494 GLU DDD OE2   1 ? 4 
ATOM   14952 N N     . VAL D 1 495 ? 52.886  9.617   77.193  1.000 33.115  0 495 VAL DDD N     1 ? 4 
ATOM   14953 C CA    . VAL D 1 495 ? 52.523  9.747   78.634  1.000 33.550  0 495 VAL DDD CA    1 ? 4 
ATOM   14954 C C     . VAL D 1 495 ? 51.868  11.119  78.885  1.000 33.829  0 495 VAL DDD C     1 ? 4 
ATOM   14955 O O     . VAL D 1 495 ? 50.899  11.148  79.633  1.000 33.494  0 495 VAL DDD O     1 ? 4 
ATOM   14956 C CB    . VAL D 1 495 ? 53.712  9.510   79.559  1.000 34.414  0 495 VAL DDD CB    1 ? 4 
ATOM   14957 C CG1   . VAL D 1 495 ? 54.619  10.735  79.622  1.000 35.097  0 495 VAL DDD CG1   1 ? 4 
ATOM   14958 C CG2   . VAL D 1 495 ? 53.244  9.106   80.947  1.000 36.118  0 495 VAL DDD CG2   1 ? 4 
ATOM   14959 N N     . PHE D 1 496 ? 52.291  12.178  78.187  1.000 33.065  0 496 PHE DDD N     1 ? 4 
ATOM   14960 C CA    . PHE D 1 496 ? 51.762  13.555  78.359  1.000 33.408  0 496 PHE DDD CA    1 ? 4 
ATOM   14961 C C     . PHE D 1 496 ? 50.282  13.677  78.005  1.000 34.246  0 496 PHE DDD C     1 ? 4 
ATOM   14962 O O     . PHE D 1 496 ? 49.742  14.754  78.308  1.000 35.717  0 496 PHE DDD O     1 ? 4 
ATOM   14963 C CB    . PHE D 1 496 ? 52.584  14.576  77.577  1.000 31.978  0 496 PHE DDD CB    1 ? 4 
ATOM   14964 C CG    . PHE D 1 496 ? 53.862  14.855  78.308  1.000 31.964  0 496 PHE DDD CG    1 ? 4 
ATOM   14965 C CD1   . PHE D 1 496 ? 53.841  15.624  79.461  1.000 31.773  0 496 PHE DDD CD1   1 ? 4 
ATOM   14966 C CD2   . PHE D 1 496 ? 55.051  14.277  77.908  1.000 30.581  0 496 PHE DDD CD2   1 ? 4 
ATOM   14967 C CE1   . PHE D 1 496 ? 55.010  15.869  80.165  1.000 31.923  0 496 PHE DDD CE1   1 ? 4 
ATOM   14968 C CE2   . PHE D 1 496 ? 56.211  14.528  78.619  1.000 30.988  0 496 PHE DDD CE2   1 ? 4 
ATOM   14969 C CZ    . PHE D 1 496 ? 56.187  15.318  79.750  1.000 31.076  0 496 PHE DDD CZ    1 ? 4 
ATOM   14970 N N     . GLY D 1 497 ? 49.650  12.628  77.490  1.000 34.811  0 497 GLY DDD N     1 ? 4 
ATOM   14971 C CA    . GLY D 1 497 ? 48.214  12.616  77.159  1.000 35.575  0 497 GLY DDD CA    1 ? 4 
ATOM   14972 C C     . GLY D 1 497 ? 47.354  11.949  78.221  1.000 37.151  0 497 GLY DDD C     1 ? 4 
ATOM   14973 O O     . GLY D 1 497 ? 46.154  11.981  78.080  1.000 42.014  0 497 GLY DDD O     1 ? 4 
ATOM   14974 N N     . ILE D 1 498 ? 47.928  11.340  79.249  1.000 38.734  0 498 ILE DDD N     1 ? 4 
ATOM   14975 C CA    . ILE D 1 498 ? 47.172  10.496  80.228  1.000 39.656  0 498 ILE DDD CA    1 ? 4 
ATOM   14976 C C     . ILE D 1 498 ? 47.706  10.761  81.638  1.000 37.637  0 498 ILE DDD C     1 ? 4 
ATOM   14977 O O     . ILE D 1 498 ? 47.660  9.858   82.468  1.000 35.317  0 498 ILE DDD O     1 ? 4 
ATOM   14978 C CB    . ILE D 1 498 ? 47.276  9.001   79.860  1.000 40.770  0 498 ILE DDD CB    1 ? 4 
ATOM   14979 C CG1   . ILE D 1 498 ? 48.738  8.548   79.808  1.000 42.213  0 498 ILE DDD CG1   1 ? 4 
ATOM   14980 C CG2   . ILE D 1 498 ? 46.559  8.716   78.550  1.000 40.850  0 498 ILE DDD CG2   1 ? 4 
ATOM   14981 C CD1   . ILE D 1 498 ? 48.946  7.041   79.991  1.000 43.481  0 498 ILE DDD CD1   1 ? 4 
ATOM   14982 N N     . LEU D 1 499 ? 48.207  11.958  81.891  1.000 38.354  0 499 LEU DDD N     1 ? 4 
ATOM   14983 C CA    . LEU D 1 499 ? 48.663  12.324  83.246  1.000 43.845  0 499 LEU DDD CA    1 ? 4 
ATOM   14984 C C     . LEU D 1 499 ? 47.413  12.609  84.079  1.000 49.294  0 499 LEU DDD C     1 ? 4 
ATOM   14985 O O     . LEU D 1 499 ? 46.529  13.341  83.570  1.000 54.092  0 499 LEU DDD O     1 ? 4 
ATOM   14986 C CB    . LEU D 1 499 ? 49.591  13.535  83.153  1.000 42.699  0 499 LEU DDD CB    1 ? 4 
ATOM   14987 C CG    . LEU D 1 499 ? 50.961  13.285  82.507  1.000 40.778  0 499 LEU DDD CG    1 ? 4 
ATOM   14988 C CD1   . LEU D 1 499 ? 51.665  14.596  82.279  1.000 40.215  0 499 LEU DDD CD1   1 ? 4 
ATOM   14989 C CD2   . LEU D 1 499 ? 51.844  12.381  83.335  1.000 40.439  0 499 LEU DDD CD2   1 ? 4 
ATOM   14990 N N     . GLU D 1 500 ? 47.296  12.020  85.272  1.000 53.053  0 500 GLU DDD N     1 ? 4 
ATOM   14991 C CA    . GLU D 1 500 ? 46.079  12.204  86.122  1.000 56.035  0 500 GLU DDD CA    1 ? 4 
ATOM   14992 C C     . GLU D 1 500 ? 46.427  12.369  87.602  1.000 57.071  0 500 GLU DDD C     1 ? 4 
ATOM   14993 O O     . GLU D 1 500 ? 45.604  12.975  88.296  1.000 65.320  0 500 GLU DDD O     1 ? 4 
ATOM   14994 C CB    . GLU D 1 500 ? 45.079  11.068  85.925  1.000 56.892  0 500 GLU DDD CB    1 ? 4 
ATOM   14995 C CG    . GLU D 1 500 ? 45.663  9.677   86.096  1.000 58.497  0 500 GLU DDD CG    1 ? 4 
ATOM   14996 C CD    . GLU D 1 500 ? 44.650  8.601   85.748  1.000 63.856  0 500 GLU DDD CD    1 ? 4 
ATOM   14997 O OE1   . GLU D 1 500 ? 43.737  8.893   84.909  1.000 58.721  0 500 GLU DDD OE1   1 ? 4 
ATOM   14998 O OE2   . GLU D 1 500 ? 44.757  7.482   86.328  1.000 70.893  0 500 GLU DDD OE2   1 ? 4 
ATOM   14999 N N     . VAL D 1 501 ? 47.572  11.871  88.070  1.000 54.674  0 501 VAL DDD N     1 ? 4 
ATOM   15000 C CA    . VAL D 1 501 ? 47.944  11.923  89.513  1.000 55.170  0 501 VAL DDD CA    1 ? 4 
ATOM   15001 C C     . VAL D 1 501 ? 48.535  13.301  89.782  1.000 53.418  0 501 VAL DDD C     1 ? 4 
ATOM   15002 O O     . VAL D 1 501 ? 49.336  13.762  88.976  1.000 51.838  0 501 VAL DDD O     1 ? 4 
ATOM   15003 C CB    . VAL D 1 501 ? 48.931  10.808  89.882  1.000 57.144  0 501 VAL DDD CB    1 ? 4 
ATOM   15004 C CG1   . VAL D 1 501 ? 49.342  10.901  91.343  1.000 57.865  0 501 VAL DDD CG1   1 ? 4 
ATOM   15005 C CG2   . VAL D 1 501 ? 48.380  9.428   89.523  1.000 56.930  0 501 VAL DDD CG2   1 ? 4 
ATOM   15006 N N     . THR D 1 502 ? 48.100  13.968  90.844  1.000 53.808  0 502 THR DDD N     1 ? 4 
ATOM   15007 C CA    . THR D 1 502 ? 48.599  15.314  91.230  1.000 53.621  0 502 THR DDD CA    1 ? 4 
ATOM   15008 C C     . THR D 1 502 ? 49.533  15.138  92.428  1.000 53.828  0 502 THR DDD C     1 ? 4 
ATOM   15009 O O     . THR D 1 502 ? 49.356  14.154  93.163  1.000 54.237  0 502 THR DDD O     1 ? 4 
ATOM   15010 C CB    . THR D 1 502 ? 47.434  16.283  91.462  1.000 53.452  0 502 THR DDD CB    1 ? 4 
ATOM   15011 O OG1   . THR D 1 502 ? 46.848  15.931  92.713  1.000 56.951  0 502 THR DDD OG1   1 ? 4 
ATOM   15012 C CG2   . THR D 1 502 ? 46.402  16.243  90.347  1.000 51.206  0 502 THR DDD CG2   1 ? 4 
ATOM   15013 N N     . LYS D 1 503 ? 50.522  16.016  92.582  1.000 55.001  0 503 LYS DDD N     1 ? 4 
ATOM   15014 C CA    . LYS D 1 503 ? 51.348  16.070  93.810  1.000 58.755  0 503 LYS DDD CA    1 ? 4 
ATOM   15015 C C     . LYS D 1 503 ? 50.400  16.252  94.995  1.000 59.114  0 503 LYS DDD C     1 ? 4 
ATOM   15016 O O     . LYS D 1 503 ? 50.415  15.385  95.894  1.000 59.877  0 503 LYS DDD O     1 ? 4 
ATOM   15017 C CB    . LYS D 1 503 ? 52.380  17.197  93.725  1.000 61.446  0 503 LYS DDD CB    1 ? 4 
ATOM   15018 C CG    . LYS D 1 503 ? 53.337  17.270  94.906  1.000 62.328  0 503 LYS DDD CG    1 ? 4 
ATOM   15019 C CD    . LYS D 1 503 ? 54.089  18.578  94.996  1.000 62.265  0 503 LYS DDD CD    1 ? 4 
ATOM   15020 C CE    . LYS D 1 503 ? 54.485  18.953  96.410  1.000 64.235  0 503 LYS DDD CE    1 ? 4 
ATOM   15021 N NZ    . LYS D 1 503 ? 55.825  18.423  96.758  1.000 62.004  0 503 LYS DDD NZ    1 ? 4 
ATOM   15022 N N     . ARG D 1 504 ? 49.549  17.286  94.931  1.000 62.165  0 504 ARG DDD N     1 ? 4 
ATOM   15023 C CA    . ARG D 1 504 ? 48.544  17.630  95.981  1.000 63.514  0 504 ARG DDD CA    1 ? 4 
ATOM   15024 C C     . ARG D 1 504 ? 47.814  16.358  96.441  1.000 62.316  0 504 ARG DDD C     1 ? 4 
ATOM   15025 O O     . ARG D 1 504 ? 47.720  16.172  97.671  1.000 60.932  0 504 ARG DDD O     1 ? 4 
ATOM   15026 C CB    . ARG D 1 504 ? 47.545  18.691  95.497  1.000 64.650  0 504 ARG DDD CB    1 ? 4 
ATOM   15027 C CG    . ARG D 1 504 ? 46.336  18.845  96.415  1.000 65.829  0 504 ARG DDD CG    1 ? 4 
ATOM   15028 C CD    . ARG D 1 504 ? 45.409  20.008  96.117  1.000 66.044  0 504 ARG DDD CD    1 ? 4 
ATOM   15029 N NE    . ARG D 1 504 ? 46.111  21.283  96.173  1.000 64.509  0 504 ARG DDD NE    1 ? 4 
ATOM   15030 C CZ    . ARG D 1 504 ? 46.215  22.139  95.161  1.000 64.073  0 504 ARG DDD CZ    1 ? 4 
ATOM   15031 N NH1   . ARG D 1 504 ? 45.634  21.875  94.003  1.000 64.014  0 504 ARG DDD NH1   1 ? 4 
ATOM   15032 N NH2   . ARG D 1 504 ? 46.926  23.243  95.297  1.000 64.750  0 504 ARG DDD NH2   1 ? 4 
ATOM   15033 N N     . SER D 1 505 ? 47.329  15.521  95.510  1.000 60.334  0 505 SER DDD N     1 ? 4 
ATOM   15034 C CA    . SER D 1 505 ? 46.545  14.295  95.822  1.000 59.415  0 505 SER DDD CA    1 ? 4 
ATOM   15035 C C     . SER D 1 505 ? 47.331  13.375  96.762  1.000 61.582  0 505 SER DDD C     1 ? 4 
ATOM   15036 O O     . SER D 1 505 ? 46.654  12.564  97.433  1.000 66.889  0 505 SER DDD O     1 ? 4 
ATOM   15037 C CB    . SER D 1 505 ? 46.131  13.533  94.583  1.000 60.512  0 505 SER DDD CB    1 ? 4 
ATOM   15038 O OG    . SER D 1 505 ? 47.199  12.715  94.119  1.000 56.718  0 505 SER DDD OG    1 ? 4 
ATOM   15039 N N     . GLY D 1 506 ? 48.680  13.449  96.787  1.000 59.842  0 506 GLY DDD N     1 ? 4 
ATOM   15040 C CA    . GLY D 1 506 ? 49.546  12.579  97.613  1.000 59.437  0 506 GLY DDD CA    1 ? 4 
ATOM   15041 C C     . GLY D 1 506 ? 49.459  11.092  97.240  1.000 58.874  0 506 GLY DDD C     1 ? 4 
ATOM   15042 O O     . GLY D 1 506 ? 50.155  10.275  97.872  1.000 58.141  0 506 GLY DDD O     1 ? 4 
ATOM   15043 N N     . GLU D 1 507 ? 48.685  10.743  96.208  1.000 58.409  0 507 GLU DDD N     1 ? 4 
ATOM   15044 C CA    . GLU D 1 507 ? 48.608  9.370   95.650  1.000 59.811  0 507 GLU DDD CA    1 ? 4 
ATOM   15045 C C     . GLU D 1 507 ? 49.927  9.032   94.921  1.000 56.651  0 507 GLU DDD C     1 ? 4 
ATOM   15046 O O     . GLU D 1 507 ? 50.732  9.963   94.613  1.000 50.375  0 507 GLU DDD O     1 ? 4 
ATOM   15047 C CB    . GLU D 1 507 ? 47.387  9.251   94.734  1.000 63.469  0 507 GLU DDD CB    1 ? 4 
ATOM   15048 C CG    . GLU D 1 507 ? 46.049  9.259   95.459  1.000 67.742  0 507 GLU DDD CG    1 ? 4 
ATOM   15049 C CD    . GLU D 1 507 ? 44.830  9.349   94.545  1.000 71.340  0 507 GLU DDD CD    1 ? 4 
ATOM   15050 O OE1   . GLU D 1 507 ? 44.861  10.080  93.501  1.000 74.737  0 507 GLU DDD OE1   1 ? 4 
ATOM   15051 O OE2   . GLU D 1 507 ? 43.834  8.690   94.876  1.000 73.347  0 507 GLU DDD OE2   1 ? 4 
ATOM   15052 N N     . SER D 1 508 ? 50.161  7.732   94.700  1.000 57.405  0 508 SER DDD N     1 ? 4 
ATOM   15053 C CA    . SER D 1 508 ? 51.359  7.178   94.003  1.000 58.450  0 508 SER DDD CA    1 ? 4 
ATOM   15054 C C     . SER D 1 508 ? 51.344  7.596   92.526  1.000 57.979  0 508 SER DDD C     1 ? 4 
ATOM   15055 O O     . SER D 1 508 ? 50.329  7.363   91.872  1.000 54.761  0 508 SER DDD O     1 ? 4 
ATOM   15056 C CB    . SER D 1 508 ? 51.442  5.671   94.134  1.000 57.932  0 508 SER DDD CB    1 ? 4 
ATOM   15057 O OG    . SER D 1 508 ? 52.557  5.167   93.416  1.000 54.661  0 508 SER DDD OG    1 ? 4 
ATOM   15058 N N     . PHE D 1 509 ? 52.427  8.206   92.039  1.000 60.524  0 509 PHE DDD N     1 ? 4 
ATOM   15059 C CA    . PHE D 1 509 ? 52.590  8.618   90.616  1.000 62.618  0 509 PHE DDD CA    1 ? 4 
ATOM   15060 C C     . PHE D 1 509 ? 53.468  7.593   89.877  1.000 58.001  0 509 PHE DDD C     1 ? 4 
ATOM   15061 O O     . PHE D 1 509 ? 53.687  7.731   88.673  1.000 48.966  0 509 PHE DDD O     1 ? 4 
ATOM   15062 C CB    . PHE D 1 509 ? 53.089  10.065  90.500  1.000 65.778  0 509 PHE DDD CB    1 ? 4 
ATOM   15063 C CG    . PHE D 1 509 ? 54.332  10.385  91.288  1.000 67.962  0 509 PHE DDD CG    1 ? 4 
ATOM   15064 C CD1   . PHE D 1 509 ? 55.590  10.048  90.807  1.000 69.959  0 509 PHE DDD CD1   1 ? 4 
ATOM   15065 C CD2   . PHE D 1 509 ? 54.235  11.036  92.510  1.000 68.658  0 509 PHE DDD CD2   1 ? 4 
ATOM   15066 C CE1   . PHE D 1 509 ? 56.726  10.328  91.555  1.000 70.687  0 509 PHE DDD CE1   1 ? 4 
ATOM   15067 C CE2   . PHE D 1 509 ? 55.370  11.333  93.244  1.000 70.898  0 509 PHE DDD CE2   1 ? 4 
ATOM   15068 C CZ    . PHE D 1 509 ? 56.615  10.979  92.765  1.000 72.597  0 509 PHE DDD CZ    1 ? 4 
ATOM   15069 N N     . VAL D 1 510 ? 53.905  6.546   90.571  1.000 60.826  0 510 VAL DDD N     1 ? 4 
ATOM   15070 C CA    . VAL D 1 510 ? 54.625  5.405   89.937  1.000 63.796  0 510 VAL DDD CA    1 ? 4 
ATOM   15071 C C     . VAL D 1 510 ? 53.614  4.551   89.157  1.000 65.903  0 510 VAL DDD C     1 ? 4 
ATOM   15072 O O     . VAL D 1 510 ? 52.489  4.365   89.648  1.000 68.460  0 510 VAL DDD O     1 ? 4 
ATOM   15073 C CB    . VAL D 1 510 ? 55.386  4.593   91.002  1.000 64.139  0 510 VAL DDD CB    1 ? 4 
ATOM   15074 C CG1   . VAL D 1 510 ? 55.912  3.272   90.462  1.000 63.382  0 510 VAL DDD CG1   1 ? 4 
ATOM   15075 C CG2   . VAL D 1 510 ? 56.521  5.414   91.595  1.000 64.835  0 510 VAL DDD CG2   1 ? 4 
ATOM   15076 N N     . SER D 1 511 ? 53.993  4.082   87.971  1.000 69.203  0 511 SER DDD N     1 ? 4 
ATOM   15077 C CA    . SER D 1 511 ? 53.321  2.970   87.244  1.000 74.327  0 511 SER DDD CA    1 ? 4 
ATOM   15078 C C     . SER D 1 511 ? 54.356  1.860   87.016  1.000 82.633  0 511 SER DDD C     1 ? 4 
ATOM   15079 O O     . SER D 1 511 ? 55.448  2.175   86.479  1.000 76.532  0 511 SER DDD O     1 ? 4 
ATOM   15080 C CB    . SER D 1 511 ? 52.699  3.457   85.962  1.000 74.275  0 511 SER DDD CB    1 ? 4 
ATOM   15081 O OG    . SER D 1 511 ? 51.797  4.527   86.233  1.000 72.304  0 511 SER DDD OG    1 ? 4 
ATOM   15082 N N     . SER D 1 512 ? 54.061  0.627   87.457  1.000 94.984  0 512 SER DDD N     1 ? 4 
ATOM   15083 C CA    . SER D 1 512 ? 55.016  -0.521  87.519  1.000 99.061  0 512 SER DDD CA    1 ? 4 
ATOM   15084 C C     . SER D 1 512 ? 54.931  -1.401  86.257  1.000 98.558  0 512 SER DDD C     1 ? 4 
ATOM   15085 O O     . SER D 1 512 ? 55.976  -1.968  85.870  1.000 96.762  0 512 SER DDD O     1 ? 4 
ATOM   15086 C CB    . SER D 1 512 ? 54.810  -1.343  88.779  1.000 102.380 0 512 SER DDD CB    1 ? 4 
ATOM   15087 O OG    . SER D 1 512 ? 55.255  -0.628  89.925  1.000 104.295 0 512 SER DDD OG    1 ? 4 
ATOM   15088 N N     . GLY D 1 513 ? 53.740  -1.546  85.665  1.000 98.497  0 513 GLY DDD N     1 ? 4 
ATOM   15089 C CA    . GLY D 1 513 ? 53.533  -2.227  84.370  1.000 95.376  0 513 GLY DDD CA    1 ? 4 
ATOM   15090 C C     . GLY D 1 513 ? 54.345  -1.577  83.258  1.000 91.729  0 513 GLY DDD C     1 ? 4 
ATOM   15091 O O     . GLY D 1 513 ? 54.503  -0.337  83.299  1.000 93.326  0 513 GLY DDD O     1 ? 4 
ATOM   15092 N N     . GLY D 1 514 ? 54.828  -2.367  82.292  1.000 85.983  0 514 GLY DDD N     1 ? 4 
ATOM   15093 C CA    . GLY D 1 514 ? 55.774  -1.922  81.246  1.000 82.803  0 514 GLY DDD CA    1 ? 4 
ATOM   15094 C C     . GLY D 1 514 ? 55.133  -1.766  79.869  1.000 76.010  0 514 GLY DDD C     1 ? 4 
ATOM   15095 O O     . GLY D 1 514 ? 55.637  -2.367  78.921  1.000 69.485  0 514 GLY DDD O     1 ? 4 
ATOM   15096 N N     . CYS D 1 515 ? 54.070  -0.968  79.761  1.000 72.756  0 515 CYS DDD N     1 ? 4 
ATOM   15097 C CA    . CYS D 1 515 ? 53.415  -0.519  78.496  1.000 72.032  0 515 CYS DDD CA    1 ? 4 
ATOM   15098 C C     . CYS D 1 515 ? 54.148  0.732   77.958  1.000 65.605  0 515 CYS DDD C     1 ? 4 
ATOM   15099 O O     . CYS D 1 515 ? 53.692  1.309   76.949  1.000 66.786  0 515 CYS DDD O     1 ? 4 
ATOM   15100 C CB    . CYS D 1 515 ? 51.915  -0.233  78.687  1.000 70.946  0 515 CYS DDD CB    1 ? 4 
ATOM   15101 S SG    . CYS D 1 515 ? 51.161  -0.849  80.230  1.000 80.579  0 515 CYS DDD SG    1 ? 4 
ATOM   15102 N N     . GLY D 1 516 ? 55.235  1.141   78.622  1.000 63.218  0 516 GLY DDD N     1 ? 4 
ATOM   15103 C CA    . GLY D 1 516 ? 55.990  2.370   78.322  1.000 61.281  0 516 GLY DDD CA    1 ? 4 
ATOM   15104 C C     . GLY D 1 516 ? 55.246  3.602   78.805  1.000 58.953  0 516 GLY DDD C     1 ? 4 
ATOM   15105 O O     . GLY D 1 516 ? 54.713  3.579   79.923  1.000 55.033  0 516 GLY DDD O     1 ? 4 
ATOM   15106 N N     . GLY D 1 517 ? 55.189  4.637   77.969  1.000 60.526  0 517 GLY DDD N     1 ? 4 
ATOM   15107 C CA    . GLY D 1 517 ? 54.498  5.911   78.269  1.000 64.202  0 517 GLY DDD CA    1 ? 4 
ATOM   15108 C C     . GLY D 1 517 ? 52.972  5.813   78.277  1.000 62.037  0 517 GLY DDD C     1 ? 4 
ATOM   15109 O O     . GLY D 1 517 ? 52.353  6.758   78.772  1.000 61.064  0 517 GLY DDD O     1 ? 4 
ATOM   15110 N N     . GLY D 1 518 ? 52.368  4.778   77.683  1.000 64.773  0 518 GLY DDD N     1 ? 4 
ATOM   15111 C CA    . GLY D 1 518 ? 50.950  4.834   77.258  1.000 69.204  0 518 GLY DDD CA    1 ? 4 
ATOM   15112 C C     . GLY D 1 518 ? 50.064  3.860   78.003  1.000 66.888  0 518 GLY DDD C     1 ? 4 
ATOM   15113 O O     . GLY D 1 518 ? 50.295  3.670   79.223  1.000 75.206  0 518 GLY DDD O     1 ? 4 
ATOM   15114 N N     . LYS D 1 519 ? 49.090  3.286   77.282  0.500 58.680  0 519 LYS DDD N     1 ? 4 
ATOM   15115 C CA    . LYS D 1 519 ? 48.288  2.091   77.656  0.500 54.157  0 519 LYS DDD CA    1 ? 4 
ATOM   15116 C C     . LYS D 1 519 ? 48.023  1.286   76.373  0.500 52.196  0 519 LYS DDD C     1 ? 4 
ATOM   15117 O O     . LYS D 1 519 ? 48.008  1.806   75.241  0.500 45.527  0 519 LYS DDD O     1 ? 4 
ATOM   15118 C CB    . LYS D 1 519 ? 46.994  2.514   78.364  0.500 53.601  0 519 LYS DDD CB    1 ? 4 
ATOM   15119 C CG    . LYS D 1 519 ? 47.126  2.892   79.841  0.500 51.879  0 519 LYS DDD CG    1 ? 4 
ATOM   15120 C CD    . LYS D 1 519 ? 46.577  1.856   80.807  0.500 51.099  0 519 LYS DDD CD    1 ? 4 
ATOM   15121 C CE    . LYS D 1 519 ? 46.770  2.228   82.265  0.500 50.743  0 519 LYS DDD CE    1 ? 4 
ATOM   15122 N NZ    . LYS D 1 519 ? 46.942  1.031   83.123  0.500 49.770  0 519 LYS DDD NZ    1 ? 4 
HETATM 15123 P PA    . FAD E 2 .   ? 6.171   8.980   26.034  1.000 32.319  0 601 FAD AAA PA    1 ? ? 
HETATM 15124 O O1A   . FAD E 2 .   ? 6.510   9.676   27.318  1.000 30.419  0 601 FAD AAA O1A   1 ? ? 
HETATM 15125 O O2A   . FAD E 2 .   ? 7.243   8.275   25.259  1.000 32.348  0 601 FAD AAA O2A   1 ? ? 
HETATM 15126 O O5B   . FAD E 2 .   ? 5.434   10.034  25.097  1.000 29.357  0 601 FAD AAA O5B   1 ? ? 
HETATM 15127 C C5B   . FAD E 2 .   ? 4.234   10.737  25.477  1.000 27.244  0 601 FAD AAA C5B   1 ? ? 
HETATM 15128 C C4B   . FAD E 2 .   ? 4.204   12.011  24.671  1.000 28.197  0 601 FAD AAA C4B   1 ? ? 
HETATM 15129 O O4B   . FAD E 2 .   ? 2.914   12.672  24.808  1.000 28.922  0 601 FAD AAA O4B   1 ? ? 
HETATM 15130 C C3B   . FAD E 2 .   ? 5.251   13.056  25.084  1.000 28.595  0 601 FAD AAA C3B   1 ? ? 
HETATM 15131 O O3B   . FAD E 2 .   ? 5.777   13.781  23.977  1.000 28.781  0 601 FAD AAA O3B   1 ? ? 
HETATM 15132 C C2B   . FAD E 2 .   ? 4.418   14.009  25.946  1.000 30.367  0 601 FAD AAA C2B   1 ? ? 
HETATM 15133 O O2B   . FAD E 2 .   ? 5.114   15.226  26.059  1.000 29.051  0 601 FAD AAA O2B   1 ? ? 
HETATM 15134 C C1B   . FAD E 2 .   ? 3.134   14.036  25.114  1.000 31.709  0 601 FAD AAA C1B   1 ? ? 
HETATM 15135 N N9A   . FAD E 2 .   ? 1.881   14.528  25.701  1.000 33.426  0 601 FAD AAA N9A   1 ? ? 
HETATM 15136 C C8A   . FAD E 2 .   ? 1.465   14.469  27.016  1.000 34.481  0 601 FAD AAA C8A   1 ? ? 
HETATM 15137 N N7A   . FAD E 2 .   ? 0.245   14.934  27.179  1.000 35.738  0 601 FAD AAA N7A   1 ? ? 
HETATM 15138 C C5A   . FAD E 2 .   ? -0.176  15.295  25.903  1.000 35.771  0 601 FAD AAA C5A   1 ? ? 
HETATM 15139 C C6A   . FAD E 2 .   ? -1.381  15.851  25.406  1.000 35.145  0 601 FAD AAA C6A   1 ? ? 
HETATM 15140 N N6A   . FAD E 2 .   ? -2.435  16.107  26.169  1.000 31.625  0 601 FAD AAA N6A   1 ? ? 
HETATM 15141 N N1A   . FAD E 2 .   ? -1.474  16.076  24.065  1.000 32.773  0 601 FAD AAA N1A   1 ? ? 
HETATM 15142 C C2A   . FAD E 2 .   ? -0.393  15.810  23.314  1.000 34.251  0 601 FAD AAA C2A   1 ? ? 
HETATM 15143 N N3A   . FAD E 2 .   ? 0.783   15.280  23.669  1.000 32.287  0 601 FAD AAA N3A   1 ? ? 
HETATM 15144 C C4A   . FAD E 2 .   ? 0.830   15.046  24.989  1.000 32.550  0 601 FAD AAA C4A   1 ? ? 
HETATM 15145 N N1    . FAD E 2 .   ? 12.598  2.432   28.460  1.000 17.168  0 601 FAD AAA N1    1 ? ? 
HETATM 15146 C C2    . FAD E 2 .   ? 13.289  1.457   27.880  1.000 17.163  0 601 FAD AAA C2    1 ? ? 
HETATM 15147 O O2    . FAD E 2 .   ? 12.714  0.521   27.312  1.000 17.404  0 601 FAD AAA O2    1 ? ? 
HETATM 15148 N N3    . FAD E 2 .   ? 14.640  1.392   27.967  1.000 17.364  0 601 FAD AAA N3    1 ? ? 
HETATM 15149 C C4    . FAD E 2 .   ? 15.374  2.363   28.580  1.000 17.768  0 601 FAD AAA C4    1 ? ? 
HETATM 15150 O O4    . FAD E 2 .   ? 16.589  2.282   28.574  1.000 17.912  0 601 FAD AAA O4    1 ? ? 
HETATM 15151 C C4X   . FAD E 2 .   ? 14.682  3.456   29.147  1.000 17.412  0 601 FAD AAA C4X   1 ? ? 
HETATM 15152 N N5    . FAD E 2 .   ? 15.360  4.408   29.737  1.000 18.515  0 601 FAD AAA N5    1 ? ? 
HETATM 15153 C C5X   . FAD E 2 .   ? 14.645  5.477   30.237  1.000 17.918  0 601 FAD AAA C5X   1 ? ? 
HETATM 15154 C C6    . FAD E 2 .   ? 15.354  6.539   30.845  1.000 15.909  0 601 FAD AAA C6    1 ? ? 
HETATM 15155 C C7    . FAD E 2 .   ? 14.708  7.639   31.353  1.000 14.467  0 601 FAD AAA C7    1 ? ? 
HETATM 15156 C C7M   . FAD E 2 .   ? 15.511  8.733   31.991  1.000 13.831  0 601 FAD AAA C7M   1 ? ? 
HETATM 15157 C C8    . FAD E 2 .   ? 13.275  7.705   31.277  1.000 14.955  0 601 FAD AAA C8    1 ? ? 
HETATM 15158 C C8M   . FAD E 2 .   ? 12.514  8.905   31.781  1.000 14.084  0 601 FAD AAA C8M   1 ? ? 
HETATM 15159 C C9    . FAD E 2 .   ? 12.572  6.647   30.715  1.000 14.873  0 601 FAD AAA C9    1 ? ? 
HETATM 15160 C C9A   . FAD E 2 .   ? 13.236  5.538   30.176  1.000 16.132  0 601 FAD AAA C9A   1 ? ? 
HETATM 15161 N N10   . FAD E 2 .   ? 12.570  4.480   29.569  1.000 17.188  0 601 FAD AAA N10   1 ? ? 
HETATM 15162 C C10   . FAD E 2 .   ? 13.258  3.415   29.036  1.000 17.243  0 601 FAD AAA C10   1 ? ? 
HETATM 15163 C "C1'" . FAD E 2 .   ? 11.101  4.473   29.500  1.000 17.453  0 601 FAD AAA "C1'" 1 ? ? 
HETATM 15164 C "C2'" . FAD E 2 .   ? 10.575  5.030   28.213  1.000 18.336  0 601 FAD AAA "C2'" 1 ? ? 
HETATM 15165 O "O2'" . FAD E 2 .   ? 11.104  6.323   28.009  1.000 19.121  0 601 FAD AAA "O2'" 1 ? ? 
HETATM 15166 C "C3'" . FAD E 2 .   ? 9.048   5.087   28.328  1.000 19.243  0 601 FAD AAA "C3'" 1 ? ? 
HETATM 15167 O "O3'" . FAD E 2 .   ? 8.562   3.843   28.881  1.000 17.599  0 601 FAD AAA "O3'" 1 ? ? 
HETATM 15168 C "C4'" . FAD E 2 .   ? 8.348   5.348   26.999  1.000 21.156  0 601 FAD AAA "C4'" 1 ? ? 
HETATM 15169 O "O4'" . FAD E 2 .   ? 8.966   6.435   26.313  1.000 21.481  0 601 FAD AAA "O4'" 1 ? ? 
HETATM 15170 C "C5'" . FAD E 2 .   ? 6.901   5.693   27.218  1.000 24.041  0 601 FAD AAA "C5'" 1 ? ? 
HETATM 15171 O "O5'" . FAD E 2 .   ? 6.223   5.796   25.949  1.000 25.849  0 601 FAD AAA "O5'" 1 ? ? 
HETATM 15172 P P     . FAD E 2 .   ? 4.741   6.372   25.975  1.000 29.692  0 601 FAD AAA P     1 ? ? 
HETATM 15173 O O1P   . FAD E 2 .   ? 4.105   6.181   24.627  1.000 31.676  0 601 FAD AAA O1P   1 ? ? 
HETATM 15174 O O2P   . FAD E 2 .   ? 4.001   5.902   27.200  1.000 31.998  0 601 FAD AAA O2P   1 ? ? 
HETATM 15175 O O3P   . FAD E 2 .   ? 5.013   7.915   26.276  1.000 27.759  0 601 FAD AAA O3P   1 ? ? 
HETATM 15176 C C1    . PEG F 3 .   ? 8.179   -28.225 28.837  1.000 71.894  0 602 PEG AAA C1    1 ? ? 
HETATM 15177 O O1    . PEG F 3 .   ? 8.955   -27.376 29.667  1.000 65.425  0 602 PEG AAA O1    1 ? ? 
HETATM 15178 C C2    . PEG F 3 .   ? 7.066   -27.499 28.133  1.000 74.068  0 602 PEG AAA C2    1 ? ? 
HETATM 15179 O O2    . PEG F 3 .   ? 7.448   -26.151 27.866  1.000 80.637  0 602 PEG AAA O2    1 ? ? 
HETATM 15180 C C3    . PEG F 3 .   ? 6.366   -25.222 27.923  1.000 76.870  0 602 PEG AAA C3    1 ? ? 
HETATM 15181 C C4    . PEG F 3 .   ? 6.898   -23.815 27.908  1.000 74.830  0 602 PEG AAA C4    1 ? ? 
HETATM 15182 O O4    . PEG F 3 .   ? 5.888   -22.832 28.057  1.000 73.878  0 602 PEG AAA O4    1 ? ? 
HETATM 15183 P PA    . FAD G 2 .   ? 44.511  -28.115 21.425  1.000 18.435  0 601 FAD BBB PA    1 ? ? 
HETATM 15184 O O1A   . FAD G 2 .   ? 45.026  -27.576 20.134  1.000 20.130  0 601 FAD BBB O1A   1 ? ? 
HETATM 15185 O O2A   . FAD G 2 .   ? 43.861  -27.041 22.244  1.000 20.139  0 601 FAD BBB O2A   1 ? ? 
HETATM 15186 O O5B   . FAD G 2 .   ? 45.670  -28.783 22.294  1.000 17.904  0 601 FAD BBB O5B   1 ? ? 
HETATM 15187 C C5B   . FAD G 2 .   ? 46.291  -30.039 22.014  1.000 18.129  0 601 FAD BBB C5B   1 ? ? 
HETATM 15188 C C4B   . FAD G 2 .   ? 47.583  -30.062 22.785  1.000 18.219  0 601 FAD BBB C4B   1 ? ? 
HETATM 15189 O O4B   . FAD G 2 .   ? 48.337  -31.264 22.499  1.000 19.197  0 601 FAD BBB O4B   1 ? ? 
HETATM 15190 C C3B   . FAD G 2 .   ? 48.555  -28.918 22.479  1.000 18.387  0 601 FAD BBB C3B   1 ? ? 
HETATM 15191 O O3B   . FAD G 2 .   ? 48.920  -28.391 23.745  1.000 21.808  0 601 FAD BBB O3B   1 ? ? 
HETATM 15192 C C2B   . FAD G 2 .   ? 49.755  -29.599 21.812  1.000 18.458  0 601 FAD BBB C2B   1 ? ? 
HETATM 15193 O O2B   . FAD G 2 .   ? 51.008  -28.988 22.054  1.000 18.994  0 601 FAD BBB O2B   1 ? ? 
HETATM 15194 C C1B   . FAD G 2 .   ? 49.710  -30.931 22.525  1.000 18.139  0 601 FAD BBB C1B   1 ? ? 
HETATM 15195 N N9A   . FAD G 2 .   ? 50.362  -32.036 21.923  1.000 19.786  0 601 FAD BBB N9A   1 ? ? 
HETATM 15196 C C8A   . FAD G 2 .   ? 50.358  -32.387 20.573  1.000 20.233  0 601 FAD BBB C8A   1 ? ? 
HETATM 15197 N N7A   . FAD G 2 .   ? 50.921  -33.552 20.365  1.000 20.763  0 601 FAD BBB N7A   1 ? ? 
HETATM 15198 C C5A   . FAD G 2 .   ? 51.246  -34.010 21.639  1.000 20.904  0 601 FAD BBB C5A   1 ? ? 
HETATM 15199 C C6A   . FAD G 2 .   ? 51.848  -35.192 22.093  1.000 21.243  0 601 FAD BBB C6A   1 ? ? 
HETATM 15200 N N6A   . FAD G 2 .   ? 52.164  -36.183 21.276  1.000 20.237  0 601 FAD BBB N6A   1 ? ? 
HETATM 15201 N N1A   . FAD G 2 .   ? 52.018  -35.353 23.436  1.000 22.717  0 601 FAD BBB N1A   1 ? ? 
HETATM 15202 C C2A   . FAD G 2 .   ? 51.678  -34.341 24.245  1.000 21.823  0 601 FAD BBB C2A   1 ? ? 
HETATM 15203 N N3A   . FAD G 2 .   ? 51.074  -33.196 23.931  1.000 22.419  0 601 FAD BBB N3A   1 ? ? 
HETATM 15204 C C4A   . FAD G 2 .   ? 50.896  -33.092 22.602  1.000 20.154  0 601 FAD BBB C4A   1 ? ? 
HETATM 15205 N N1    . FAD G 2 .   ? 37.690  -21.660 18.907  1.000 19.252  0 601 FAD BBB N1    1 ? ? 
HETATM 15206 C C2    . FAD G 2 .   ? 36.612  -21.013 19.419  1.000 19.316  0 601 FAD BBB C2    1 ? ? 
HETATM 15207 O O2    . FAD G 2 .   ? 35.610  -21.632 19.867  1.000 19.324  0 601 FAD BBB O2    1 ? ? 
HETATM 15208 N N3    . FAD G 2 .   ? 36.562  -19.668 19.441  1.000 18.142  0 601 FAD BBB N3    1 ? ? 
HETATM 15209 C C4    . FAD G 2 .   ? 37.573  -18.882 18.959  1.000 18.286  0 601 FAD BBB C4    1 ? ? 
HETATM 15210 O O4    . FAD G 2 .   ? 37.479  -17.666 19.029  1.000 17.786  0 601 FAD BBB O4    1 ? ? 
HETATM 15211 C C4X   . FAD G 2 .   ? 38.712  -19.506 18.453  1.000 19.547  0 601 FAD BBB C4X   1 ? ? 
HETATM 15212 N N5    . FAD G 2 .   ? 39.704  -18.759 18.009  1.000 22.113  0 601 FAD BBB N5    1 ? ? 
HETATM 15213 C C5X   . FAD G 2 .   ? 40.809  -19.389 17.498  1.000 19.700  0 601 FAD BBB C5X   1 ? ? 
HETATM 15214 C C6    . FAD G 2 .   ? 41.875  -18.599 17.027  1.000 18.915  0 601 FAD BBB C6    1 ? ? 
HETATM 15215 C C7    . FAD G 2 .   ? 43.032  -19.170 16.541  1.000 19.751  0 601 FAD BBB C7    1 ? ? 
HETATM 15216 C C7M   . FAD G 2 .   ? 44.168  -18.307 16.027  1.000 19.317  0 601 FAD BBB C7M   1 ? ? 
HETATM 15217 C C8    . FAD G 2 .   ? 43.126  -20.568 16.502  1.000 19.890  0 601 FAD BBB C8    1 ? ? 
HETATM 15218 C C8M   . FAD G 2 .   ? 44.362  -21.228 15.954  1.000 21.812  0 601 FAD BBB C8M   1 ? ? 
HETATM 15219 C C9    . FAD G 2 .   ? 42.077  -21.353 16.932  1.000 19.594  0 601 FAD BBB C9    1 ? ? 
HETATM 15220 C C9A   . FAD G 2 .   ? 40.901  -20.790 17.446  1.000 19.290  0 601 FAD BBB C9A   1 ? ? 
HETATM 15221 N N10   . FAD G 2 .   ? 39.825  -21.548 17.932  1.000 20.866  0 601 FAD BBB N10   1 ? ? 
HETATM 15222 C C10   . FAD G 2 .   ? 38.696  -20.937 18.449  1.000 19.318  0 601 FAD BBB C10   1 ? ? 
HETATM 15223 C "C1'" . FAD G 2 .   ? 39.855  -23.028 17.889  1.000 20.300  0 601 FAD BBB "C1'" 1 ? ? 
HETATM 15224 C "C2'" . FAD G 2 .   ? 40.511  -23.621 19.104  1.000 21.197  0 601 FAD BBB "C2'" 1 ? ? 
HETATM 15225 O "O2'" . FAD G 2 .   ? 41.841  -23.048 19.305  1.000 22.437  0 601 FAD BBB "O2'" 1 ? ? 
HETATM 15226 C "C3'" . FAD G 2 .   ? 40.618  -25.140 18.948  1.000 20.753  0 601 FAD BBB "C3'" 1 ? ? 
HETATM 15227 O "O3'" . FAD G 2 .   ? 39.450  -25.657 18.304  1.000 21.468  0 601 FAD BBB "O3'" 1 ? ? 
HETATM 15228 C "C4'" . FAD G 2 .   ? 40.774  -25.882 20.273  1.000 20.909  0 601 FAD BBB "C4'" 1 ? ? 
HETATM 15229 O "O4'" . FAD G 2 .   ? 41.894  -25.365 21.007  1.000 21.454  0 601 FAD BBB "O4'" 1 ? ? 
HETATM 15230 C "C5'" . FAD G 2 .   ? 40.945  -27.359 20.023  1.000 20.155  0 601 FAD BBB "C5'" 1 ? ? 
HETATM 15231 O "O5'" . FAD G 2 .   ? 41.453  -27.952 21.202  1.000 17.665  0 601 FAD BBB "O5'" 1 ? ? 
HETATM 15232 P P     . FAD G 2 .   ? 41.900  -29.462 21.159  1.000 21.556  0 601 FAD BBB P     1 ? ? 
HETATM 15233 O O1P   . FAD G 2 .   ? 41.522  -30.036 22.486  1.000 22.118  0 601 FAD BBB O1P   1 ? ? 
HETATM 15234 O O2P   . FAD G 2 .   ? 41.460  -30.081 19.852  1.000 19.030  0 601 FAD BBB O2P   1 ? ? 
HETATM 15235 O O3P   . FAD G 2 .   ? 43.512  -29.358 21.192  1.000 18.564  0 601 FAD BBB O3P   1 ? ? 
HETATM 15236 C C1    . PEG H 3 .   ? 11.331  -28.715 17.760  1.000 68.491  0 602 PEG BBB C1    1 ? ? 
HETATM 15237 O O1    . PEG H 3 .   ? 10.414  -28.115 16.859  1.000 60.412  0 602 PEG BBB O1    1 ? ? 
HETATM 15238 C C2    . PEG H 3 .   ? 12.353  -29.578 17.062  1.000 69.339  0 602 PEG BBB C2    1 ? ? 
HETATM 15239 O O2    . PEG H 3 .   ? 12.984  -28.842 16.015  1.000 75.512  0 602 PEG BBB O2    1 ? ? 
HETATM 15240 C C3    . PEG H 3 .   ? 14.323  -28.450 16.314  1.000 75.302  0 602 PEG BBB C3    1 ? ? 
HETATM 15241 C C4    . PEG H 3 .   ? 14.850  -27.522 15.246  1.000 76.092  0 602 PEG BBB C4    1 ? ? 
HETATM 15242 O O4    . PEG H 3 .   ? 15.293  -28.211 14.081  1.000 70.952  0 602 PEG BBB O4    1 ? ? 
HETATM 15243 C C1    . PEG I 3 .   ? 56.724  -16.405 25.008  1.000 67.360  0 603 PEG BBB C1    1 ? ? 
HETATM 15244 O O1    . PEG I 3 .   ? 57.867  -17.072 24.505  1.000 65.279  0 603 PEG BBB O1    1 ? ? 
HETATM 15245 C C2    . PEG I 3 .   ? 55.434  -17.109 24.690  1.000 65.740  0 603 PEG BBB C2    1 ? ? 
HETATM 15246 O O2    . PEG I 3 .   ? 54.401  -16.683 25.581  1.000 67.094  0 603 PEG BBB O2    1 ? ? 
HETATM 15247 C C3    . PEG I 3 .   ? 54.267  -17.519 26.729  1.000 66.270  0 603 PEG BBB C3    1 ? ? 
HETATM 15248 C C4    . PEG I 3 .   ? 53.448  -16.848 27.806  1.000 63.578  0 603 PEG BBB C4    1 ? ? 
HETATM 15249 O O4    . PEG I 3 .   ? 54.188  -16.605 28.998  1.000 59.311  0 603 PEG BBB O4    1 ? ? 
HETATM 15250 P PA    . FAD J 2 .   ? 42.606  -5.730  69.423  1.000 30.790  0 601 FAD CCC PA    1 ? ? 
HETATM 15251 O O1A   . FAD J 2 .   ? 42.999  -6.437  68.163  1.000 29.191  0 601 FAD CCC O1A   1 ? ? 
HETATM 15252 O O2A   . FAD J 2 .   ? 43.636  -4.986  70.206  1.000 30.343  0 601 FAD CCC O2A   1 ? ? 
HETATM 15253 O O5B   . FAD J 2 .   ? 41.917  -6.802  70.375  1.000 31.106  0 601 FAD CCC O5B   1 ? ? 
HETATM 15254 C C5B   . FAD J 2 .   ? 40.776  -7.588  69.940  1.000 30.149  0 601 FAD CCC C5B   1 ? ? 
HETATM 15255 C C4B   . FAD J 2 .   ? 40.670  -8.776  70.864  1.000 30.086  0 601 FAD CCC C4B   1 ? ? 
HETATM 15256 O O4B   . FAD J 2 .   ? 39.358  -9.395  70.737  1.000 30.338  0 601 FAD CCC O4B   1 ? ? 
HETATM 15257 C C3B   . FAD J 2 .   ? 41.688  -9.894  70.604  1.000 29.652  0 601 FAD CCC C3B   1 ? ? 
HETATM 15258 O O3B   . FAD J 2 .   ? 42.265  -10.318 71.835  1.000 32.280  0 601 FAD CCC O3B   1 ? ? 
HETATM 15259 C C2B   . FAD J 2 .   ? 40.835  -10.982 69.934  1.000 32.356  0 601 FAD CCC C2B   1 ? ? 
HETATM 15260 O O2B   . FAD J 2 .   ? 41.396  -12.274 70.054  1.000 31.835  0 601 FAD CCC O2B   1 ? ? 
HETATM 15261 C C1B   . FAD J 2 .   ? 39.523  -10.792 70.696  1.000 31.387  0 601 FAD CCC C1B   1 ? ? 
HETATM 15262 N N9A   . FAD J 2 .   ? 38.294  -11.335 70.141  1.000 34.227  0 601 FAD CCC N9A   1 ? ? 
HETATM 15263 C C8A   . FAD J 2 .   ? 37.930  -11.395 68.816  1.000 36.430  0 601 FAD CCC C8A   1 ? ? 
HETATM 15264 N N7A   . FAD J 2 .   ? 36.730  -11.902 68.652  1.000 35.472  0 601 FAD CCC N7A   1 ? ? 
HETATM 15265 C C5A   . FAD J 2 .   ? 36.264  -12.150 69.936  1.000 35.170  0 601 FAD CCC C5A   1 ? ? 
HETATM 15266 C C6A   . FAD J 2 .   ? 35.045  -12.661 70.427  1.000 34.761  0 601 FAD CCC C6A   1 ? ? 
HETATM 15267 N N6A   . FAD J 2 .   ? 34.029  -13.007 69.645  1.000 31.040  0 601 FAD CCC N6A   1 ? ? 
HETATM 15268 N N1A   . FAD J 2 .   ? 34.908  -12.776 71.775  1.000 39.553  0 601 FAD CCC N1A   1 ? ? 
HETATM 15269 C C2A   . FAD J 2 .   ? 35.936  -12.412 72.558  1.000 38.345  0 601 FAD CCC C2A   1 ? ? 
HETATM 15270 N N3A   . FAD J 2 .   ? 37.120  -11.912 72.204  1.000 38.905  0 601 FAD CCC N3A   1 ? ? 
HETATM 15271 C C4A   . FAD J 2 .   ? 37.225  -11.808 70.864  1.000 36.861  0 601 FAD CCC C4A   1 ? ? 
HETATM 15272 N N1    . FAD J 2 .   ? 49.151  0.739   66.608  1.000 20.466  0 601 FAD CCC N1    1 ? ? 
HETATM 15273 C C2    . FAD J 2 .   ? 49.806  1.794   67.032  1.000 20.869  0 601 FAD CCC C2    1 ? ? 
HETATM 15274 O O2    . FAD J 2 .   ? 49.183  2.735   67.489  1.000 24.395  0 601 FAD CCC O2    1 ? ? 
HETATM 15275 N N3    . FAD J 2 .   ? 51.169  1.885   67.035  1.000 21.472  0 601 FAD CCC N3    1 ? ? 
HETATM 15276 C C4    . FAD J 2 .   ? 51.959  0.874   66.543  1.000 23.883  0 601 FAD CCC C4    1 ? ? 
HETATM 15277 O O4    . FAD J 2 .   ? 53.188  0.997   66.565  1.000 23.254  0 601 FAD CCC O4    1 ? ? 
HETATM 15278 C C4X   . FAD J 2 .   ? 51.276  -0.303  66.052  1.000 22.565  0 601 FAD CCC C4X   1 ? ? 
HETATM 15279 N N5    . FAD J 2 .   ? 51.976  -1.314  65.578  1.000 22.972  0 601 FAD CCC N5    1 ? ? 
HETATM 15280 C C5X   . FAD J 2 .   ? 51.268  -2.415  65.149  1.000 21.891  0 601 FAD CCC C5X   1 ? ? 
HETATM 15281 C C6    . FAD J 2 .   ? 51.980  -3.513  64.634  1.000 20.691  0 601 FAD CCC C6    1 ? ? 
HETATM 15282 C C7    . FAD J 2 .   ? 51.331  -4.640  64.180  1.000 22.131  0 601 FAD CCC C7    1 ? ? 
HETATM 15283 C C7M   . FAD J 2 .   ? 52.126  -5.825  63.693  1.000 22.235  0 601 FAD CCC C7M   1 ? ? 
HETATM 15284 C C8    . FAD J 2 .   ? 49.912  -4.708  64.251  1.000 21.917  0 601 FAD CCC C8    1 ? ? 
HETATM 15285 C C8M   . FAD J 2 .   ? 49.157  -5.935  63.802  1.000 22.994  0 601 FAD CCC C8M   1 ? ? 
HETATM 15286 C C9    . FAD J 2 .   ? 49.205  -3.626  64.727  1.000 21.499  0 601 FAD CCC C9    1 ? ? 
HETATM 15287 C C9A   . FAD J 2 .   ? 49.854  -2.471  65.177  1.000 21.085  0 601 FAD CCC C9A   1 ? ? 
HETATM 15288 N N10   . FAD J 2 .   ? 49.153  -1.381  65.669  1.000 20.392  0 601 FAD CCC N10   1 ? ? 
HETATM 15289 C C10   . FAD J 2 .   ? 49.833  -0.274  66.128  1.000 21.153  0 601 FAD CCC C10   1 ? ? 
HETATM 15290 C "C1'" . FAD J 2 .   ? 47.678  -1.407  65.700  1.000 23.063  0 601 FAD CCC "C1'" 1 ? ? 
HETATM 15291 C "C2'" . FAD J 2 .   ? 47.067  -1.886  67.019  1.000 26.030  0 601 FAD CCC "C2'" 1 ? ? 
HETATM 15292 O "O2'" . FAD J 2 .   ? 47.433  -3.208  67.385  1.000 29.584  0 601 FAD CCC "O2'" 1 ? ? 
HETATM 15293 C "C3'" . FAD J 2 .   ? 45.543  -1.931  66.888  1.000 26.327  0 601 FAD CCC "C3'" 1 ? ? 
HETATM 15294 O "O3'" . FAD J 2 .   ? 45.077  -0.729  66.295  1.000 24.986  0 601 FAD CCC "O3'" 1 ? ? 
HETATM 15295 C "C4'" . FAD J 2 .   ? 44.815  -2.091  68.222  1.000 27.007  0 601 FAD CCC "C4'" 1 ? ? 
HETATM 15296 O "O4'" . FAD J 2 .   ? 45.388  -3.157  68.991  1.000 24.915  0 601 FAD CCC "O4'" 1 ? ? 
HETATM 15297 C "C5'" . FAD J 2 .   ? 43.347  -2.341  67.983  1.000 26.839  0 601 FAD CCC "C5'" 1 ? ? 
HETATM 15298 O "O5'" . FAD J 2 .   ? 42.736  -2.701  69.241  1.000 26.722  0 601 FAD CCC "O5'" 1 ? ? 
HETATM 15299 P P     . FAD J 2 .   ? 41.197  -3.169  69.279  1.000 25.966  0 601 FAD CCC P     1 ? ? 
HETATM 15300 O O1P   . FAD J 2 .   ? 40.685  -2.769  70.635  1.000 27.123  0 601 FAD CCC O1P   1 ? ? 
HETATM 15301 O O2P   . FAD J 2 .   ? 40.469  -2.624  68.081  1.000 24.550  0 601 FAD CCC O2P   1 ? ? 
HETATM 15302 O O3P   . FAD J 2 .   ? 41.364  -4.749  69.151  1.000 25.347  0 601 FAD CCC O3P   1 ? ? 
HETATM 15303 C C1    . PEG K 3 .   ? 44.948  29.703  64.970  1.000 66.575  0 602 PEG CCC C1    1 ? ? 
HETATM 15304 O O1    . PEG K 3 .   ? 44.910  30.988  65.562  1.000 58.388  0 602 PEG CCC O1    1 ? ? 
HETATM 15305 C C2    . PEG K 3 .   ? 44.080  28.715  65.696  1.000 70.692  0 602 PEG CCC C2    1 ? ? 
HETATM 15306 O O2    . PEG K 3 .   ? 43.584  27.733  64.787  1.000 75.147  0 602 PEG CCC O2    1 ? ? 
HETATM 15307 C C3    . PEG K 3 .   ? 42.655  26.823  65.377  1.000 75.848  0 602 PEG CCC C3    1 ? ? 
HETATM 15308 C C4    . PEG K 3 .   ? 43.369  25.618  65.938  1.000 75.949  0 602 PEG CCC C4    1 ? ? 
HETATM 15309 O O4    . PEG K 3 .   ? 43.314  24.483  65.081  1.000 72.922  0 602 PEG CCC O4    1 ? ? 
HETATM 15310 P PA    . FAD L 2 .   ? 81.253  31.288  72.153  1.000 34.740  0 601 FAD DDD PA    1 ? ? 
HETATM 15311 O O1A   . FAD L 2 .   ? 82.105  30.941  73.314  1.000 35.234  0 601 FAD DDD O1A   1 ? ? 
HETATM 15312 O O2A   . FAD L 2 .   ? 80.547  30.167  71.460  1.000 37.366  0 601 FAD DDD O2A   1 ? ? 
HETATM 15313 O O5B   . FAD L 2 .   ? 82.096  32.155  71.103  1.000 32.523  0 601 FAD DDD O5B   1 ? ? 
HETATM 15314 C C5B   . FAD L 2 .   ? 83.078  33.102  71.602  1.000 35.181  0 601 FAD DDD C5B   1 ? ? 
HETATM 15315 C C4B   . FAD L 2 .   ? 84.334  33.087  70.756  1.000 35.495  0 601 FAD DDD C4B   1 ? ? 
HETATM 15316 O O4B   . FAD L 2 .   ? 85.032  34.354  70.898  1.000 39.376  0 601 FAD DDD O4B   1 ? ? 
HETATM 15317 C C3B   . FAD L 2 .   ? 85.391  32.026  71.097  1.000 36.300  0 601 FAD DDD C3B   1 ? ? 
HETATM 15318 O O3B   . FAD L 2 .   ? 85.750  31.342  69.902  1.000 33.867  0 601 FAD DDD O3B   1 ? ? 
HETATM 15319 C C2B   . FAD L 2 .   ? 86.580  32.832  71.649  1.000 39.233  0 601 FAD DDD C2B   1 ? ? 
HETATM 15320 O O2B   . FAD L 2 .   ? 87.806  32.177  71.393  1.000 38.964  0 601 FAD DDD O2B   1 ? ? 
HETATM 15321 C C1B   . FAD L 2 .   ? 86.426  34.133  70.867  1.000 38.000  0 601 FAD DDD C1B   1 ? ? 
HETATM 15322 N N9A   . FAD L 2 .   ? 87.057  35.365  71.380  1.000 41.181  0 601 FAD DDD N9A   1 ? ? 
HETATM 15323 C C8A   . FAD L 2 .   ? 87.083  35.805  72.696  1.000 37.928  0 601 FAD DDD C8A   1 ? ? 
HETATM 15324 N N7A   . FAD L 2 .   ? 87.648  36.984  72.817  1.000 37.245  0 601 FAD DDD N7A   1 ? ? 
HETATM 15325 C C5A   . FAD L 2 .   ? 88.009  37.350  71.522  1.000 41.949  0 601 FAD DDD C5A   1 ? ? 
HETATM 15326 C C6A   . FAD L 2 .   ? 88.662  38.489  70.994  1.000 45.420  0 601 FAD DDD C6A   1 ? ? 
HETATM 15327 N N6A   . FAD L 2 .   ? 89.048  39.521  71.737  1.000 46.158  0 601 FAD DDD N6A   1 ? ? 
HETATM 15328 N N1A   . FAD L 2 .   ? 88.875  38.543  69.654  1.000 43.686  0 601 FAD DDD N1A   1 ? ? 
HETATM 15329 C C2A   . FAD L 2 .   ? 88.480  37.495  68.918  1.000 48.012  0 601 FAD DDD C2A   1 ? ? 
HETATM 15330 N N3A   . FAD L 2 .   ? 87.850  36.381  69.304  1.000 48.292  0 601 FAD DDD N3A   1 ? ? 
HETATM 15331 C C4A   . FAD L 2 .   ? 87.645  36.361  70.633  1.000 41.387  0 601 FAD DDD C4A   1 ? ? 
HETATM 15332 N N1    . FAD L 2 .   ? 74.341  25.161  74.917  1.000 37.454  0 601 FAD DDD N1    1 ? ? 
HETATM 15333 C C2    . FAD L 2 .   ? 73.197  24.551  74.497  1.000 34.455  0 601 FAD DDD C2    1 ? ? 
HETATM 15334 O O2    . FAD L 2 .   ? 72.244  25.207  74.024  1.000 38.204  0 601 FAD DDD O2    1 ? ? 
HETATM 15335 N N3    . FAD L 2 .   ? 73.036  23.216  74.588  1.000 32.174  0 601 FAD DDD N3    1 ? ? 
HETATM 15336 C C4    . FAD L 2 .   ? 74.015  22.389  75.062  1.000 34.159  0 601 FAD DDD C4    1 ? ? 
HETATM 15337 O O4    . FAD L 2 .   ? 73.810  21.182  75.116  1.000 36.861  0 601 FAD DDD O4    1 ? ? 
HETATM 15338 C C4X   . FAD L 2 .   ? 75.202  22.974  75.521  1.000 33.604  0 601 FAD DDD C4X   1 ? ? 
HETATM 15339 N N5    . FAD L 2 .   ? 76.132  22.195  76.001  1.000 34.507  0 601 FAD DDD N5    1 ? ? 
HETATM 15340 C C5X   . FAD L 2 .   ? 77.275  22.788  76.460  1.000 32.721  0 601 FAD DDD C5X   1 ? ? 
HETATM 15341 C C6    . FAD L 2 .   ? 78.271  21.964  77.006  1.000 31.820  0 601 FAD DDD C6    1 ? ? 
HETATM 15342 C C7    . FAD L 2 .   ? 79.439  22.481  77.509  1.000 32.431  0 601 FAD DDD C7    1 ? ? 
HETATM 15343 C C7M   . FAD L 2 .   ? 80.475  21.548  78.084  1.000 32.672  0 601 FAD DDD C7M   1 ? ? 
HETATM 15344 C C8    . FAD L 2 .   ? 79.647  23.885  77.468  1.000 33.396  0 601 FAD DDD C8    1 ? ? 
HETATM 15345 C C8M   . FAD L 2 .   ? 80.923  24.506  77.984  1.000 33.826  0 601 FAD DDD C8M   1 ? ? 
HETATM 15346 C C9    . FAD L 2 .   ? 78.681  24.698  76.920  1.000 33.507  0 601 FAD DDD C9    1 ? ? 
HETATM 15347 C C9A   . FAD L 2 .   ? 77.477  24.179  76.418  1.000 32.695  0 601 FAD DDD C9A   1 ? ? 
HETATM 15348 N N10   . FAD L 2 .   ? 76.471  24.978  75.870  1.000 34.202  0 601 FAD DDD N10   1 ? ? 
HETATM 15349 C C10   . FAD L 2 .   ? 75.295  24.406  75.424  1.000 35.161  0 601 FAD DDD C10   1 ? ? 
HETATM 15350 C "C1'" . FAD L 2 .   ? 76.619  26.450  75.841  1.000 34.153  0 601 FAD DDD "C1'" 1 ? ? 
HETATM 15351 C "C2'" . FAD L 2 .   ? 77.275  26.973  74.581  1.000 35.891  0 601 FAD DDD "C2'" 1 ? ? 
HETATM 15352 O "O2'" . FAD L 2 .   ? 78.637  26.581  74.442  1.000 35.029  0 601 FAD DDD "O2'" 1 ? ? 
HETATM 15353 C "C3'" . FAD L 2 .   ? 77.244  28.498  74.605  1.000 36.814  0 601 FAD DDD "C3'" 1 ? ? 
HETATM 15354 O "O3'" . FAD L 2 .   ? 76.014  28.939  75.130  1.000 36.061  0 601 FAD DDD "O3'" 1 ? ? 
HETATM 15355 C "C4'" . FAD L 2 .   ? 77.435  29.125  73.231  1.000 38.840  0 601 FAD DDD "C4'" 1 ? ? 
HETATM 15356 O "O4'" . FAD L 2 .   ? 78.620  28.591  72.637  1.000 42.534  0 601 FAD DDD "O4'" 1 ? ? 
HETATM 15357 C "C5'" . FAD L 2 .   ? 77.546  30.625  73.333  1.000 40.513  0 601 FAD DDD "C5'" 1 ? ? 
HETATM 15358 O "O5'" . FAD L 2 .   ? 78.041  31.162  72.096  1.000 38.492  0 601 FAD DDD "O5'" 1 ? ? 
HETATM 15359 P P     . FAD L 2 .   ? 78.650  32.631  72.100  1.000 39.653  0 601 FAD DDD P     1 ? ? 
HETATM 15360 O O1P   . FAD L 2 .   ? 78.677  33.095  70.677  1.000 35.749  0 601 FAD DDD O1P   1 ? ? 
HETATM 15361 O O2P   . FAD L 2 .   ? 77.975  33.444  73.154  1.000 43.583  0 601 FAD DDD O2P   1 ? ? 
HETATM 15362 O O3P   . FAD L 2 .   ? 80.129  32.328  72.637  1.000 39.705  0 601 FAD DDD O3P   1 ? ? 
HETATM 15363 C C1    . PEG M 3 .   ? 47.936  31.831  74.150  1.000 80.959  0 602 PEG DDD C1    1 ? ? 
HETATM 15364 O O1    . PEG M 3 .   ? 46.914  31.480  75.075  1.000 82.325  0 602 PEG DDD O1    1 ? ? 
HETATM 15365 C C2    . PEG M 3 .   ? 48.571  33.162  74.459  1.000 79.282  0 602 PEG DDD C2    1 ? ? 
HETATM 15366 O O2    . PEG M 3 .   ? 49.263  33.101  75.705  1.000 77.138  0 602 PEG DDD O2    1 ? ? 
HETATM 15367 C C3    . PEG M 3 .   ? 50.682  33.200  75.589  1.000 72.965  0 602 PEG DDD C3    1 ? ? 
HETATM 15368 C C4    . PEG M 3 .   ? 51.346  32.370  76.662  1.000 68.789  0 602 PEG DDD C4    1 ? ? 
HETATM 15369 O O4    . PEG M 3 .   ? 51.929  33.153  77.694  1.000 59.459  0 602 PEG DDD O4    1 ? ? 
HETATM 15370 O O     . HOH N 4 .   ? 35.321  6.557   34.263  1.000 26.081  0 701 HOH AAA O     1 ? ? 
HETATM 15371 O O     . HOH N 4 .   ? 5.342   5.911   8.560   1.000 40.756  0 702 HOH AAA O     1 ? ? 
HETATM 15372 O O     . HOH N 4 .   ? 32.409  4.786   46.972  1.000 19.185  0 703 HOH AAA O     1 ? ? 
HETATM 15373 O O     . HOH N 4 .   ? 37.242  16.525  25.403  1.000 27.680  0 704 HOH AAA O     1 ? ? 
HETATM 15374 O O     . HOH N 4 .   ? 20.604  -27.370 24.535  1.000 20.751  0 705 HOH AAA O     1 ? ? 
HETATM 15375 O O     . HOH N 4 .   ? 11.079  -9.669  43.140  1.000 36.163  0 706 HOH AAA O     1 ? ? 
HETATM 15376 O O     . HOH N 4 .   ? -10.267 -2.215  8.470   1.000 34.602  0 707 HOH AAA O     1 ? ? 
HETATM 15377 O O     . HOH N 4 .   ? 14.415  12.538  37.212  1.000 18.881  0 708 HOH AAA O     1 ? ? 
HETATM 15378 O O     . HOH N 4 .   ? 5.870   17.198  19.288  1.000 27.483  0 709 HOH AAA O     1 ? ? 
HETATM 15379 O O     . HOH N 4 .   ? 6.146   7.656   32.715  1.000 29.989  0 710 HOH AAA O     1 ? ? 
HETATM 15380 O O     . HOH N 4 .   ? 21.313  -17.172 44.554  1.000 30.692  0 711 HOH AAA O     1 ? ? 
HETATM 15381 O O     . HOH N 4 .   ? 11.985  10.492  34.834  1.000 17.047  0 712 HOH AAA O     1 ? ? 
HETATM 15382 O O     . HOH N 4 .   ? -1.911  14.444  28.881  1.000 25.351  0 713 HOH AAA O     1 ? ? 
HETATM 15383 O O     . HOH N 4 .   ? 14.729  -1.541  33.791  1.000 28.368  0 714 HOH AAA O     1 ? ? 
HETATM 15384 O O     . HOH N 4 .   ? -10.341 -5.285  13.685  1.000 35.343  0 715 HOH AAA O     1 ? ? 
HETATM 15385 O O     . HOH N 4 .   ? 43.948  -0.952  34.737  1.000 16.806  0 716 HOH AAA O     1 ? ? 
HETATM 15386 O O     . HOH N 4 .   ? 4.769   15.155  10.375  1.000 31.401  0 717 HOH AAA O     1 ? ? 
HETATM 15387 O O     . HOH N 4 .   ? 29.954  -5.873  42.204  1.000 24.060  0 718 HOH AAA O     1 ? ? 
HETATM 15388 O O     . HOH N 4 .   ? 23.773  -4.425  26.649  1.000 20.115  0 719 HOH AAA O     1 ? ? 
HETATM 15389 O O     . HOH N 4 .   ? 1.024   6.276   28.004  1.000 30.123  0 720 HOH AAA O     1 ? ? 
HETATM 15390 O O     . HOH N 4 .   ? 9.926   -28.424 31.758  1.000 27.420  0 721 HOH AAA O     1 ? ? 
HETATM 15391 O O     . HOH N 4 .   ? -18.595 2.237   14.490  1.000 38.115  0 722 HOH AAA O     1 ? ? 
HETATM 15392 O O     . HOH N 4 .   ? 12.593  18.958  35.444  1.000 25.915  0 723 HOH AAA O     1 ? ? 
HETATM 15393 O O     . HOH N 4 .   ? 9.591   13.534  30.515  1.000 35.943  0 724 HOH AAA O     1 ? ? 
HETATM 15394 O O     . HOH N 4 .   ? 22.661  -14.104 24.362  1.000 26.332  0 725 HOH AAA O     1 ? ? 
HETATM 15395 O O     . HOH N 4 .   ? 12.066  -4.148  27.457  1.000 13.561  0 726 HOH AAA O     1 ? ? 
HETATM 15396 O O     . HOH N 4 .   ? 34.729  -13.153 28.686  1.000 29.262  0 727 HOH AAA O     1 ? ? 
HETATM 15397 O O     . HOH N 4 .   ? 20.774  18.664  13.580  1.000 35.170  0 728 HOH AAA O     1 ? ? 
HETATM 15398 O O     . HOH N 4 .   ? 5.524   2.286   28.534  1.000 27.743  0 729 HOH AAA O     1 ? ? 
HETATM 15399 O O     . HOH N 4 .   ? 24.895  -9.663  45.679  1.000 17.191  0 730 HOH AAA O     1 ? ? 
HETATM 15400 O O     . HOH N 4 .   ? 18.021  -12.345 45.115  1.000 24.837  0 731 HOH AAA O     1 ? ? 
HETATM 15401 O O     . HOH N 4 .   ? 9.096   -11.627 25.182  1.000 21.169  0 732 HOH AAA O     1 ? ? 
HETATM 15402 O O     . HOH N 4 .   ? 31.377  -22.448 19.418  1.000 14.924  0 733 HOH AAA O     1 ? ? 
HETATM 15403 O O     . HOH N 4 .   ? 33.737  15.435  34.463  1.000 40.922  0 734 HOH AAA O     1 ? ? 
HETATM 15404 O O     . HOH N 4 .   ? 29.587  3.974   40.318  1.000 19.675  0 735 HOH AAA O     1 ? ? 
HETATM 15405 O O     . HOH N 4 .   ? 33.218  1.002   35.474  1.000 18.621  0 736 HOH AAA O     1 ? ? 
HETATM 15406 O O     . HOH N 4 .   ? 28.542  14.217  45.602  1.000 29.181  0 737 HOH AAA O     1 ? ? 
HETATM 15407 O O     . HOH N 4 .   ? 27.508  4.554   32.659  1.000 27.896  0 738 HOH AAA O     1 ? ? 
HETATM 15408 O O     . HOH N 4 .   ? 11.205  18.960  55.501  1.000 30.010  0 739 HOH AAA O     1 ? ? 
HETATM 15409 O O     . HOH N 4 .   ? 7.993   14.300  25.392  1.000 22.853  0 740 HOH AAA O     1 ? ? 
HETATM 15410 O O     . HOH N 4 .   ? 10.177  -14.241 48.569  1.000 24.327  0 741 HOH AAA O     1 ? ? 
HETATM 15411 O O     . HOH N 4 .   ? 1.487   17.229  34.303  1.000 29.490  0 742 HOH AAA O     1 ? ? 
HETATM 15412 O O     . HOH N 4 .   ? -0.977  -6.337  24.751  1.000 24.513  0 743 HOH AAA O     1 ? ? 
HETATM 15413 O O     . HOH N 4 .   ? 1.894   -0.636  27.005  1.000 26.157  0 744 HOH AAA O     1 ? ? 
HETATM 15414 O O     . HOH N 4 .   ? 20.656  -12.261 22.572  1.000 19.632  0 745 HOH AAA O     1 ? ? 
HETATM 15415 O O     . HOH N 4 .   ? 14.926  -8.748  38.636  1.000 22.572  0 746 HOH AAA O     1 ? ? 
HETATM 15416 O O     . HOH N 4 .   ? -12.832 2.220   11.365  1.000 31.613  0 747 HOH AAA O     1 ? ? 
HETATM 15417 O O     . HOH N 4 .   ? -5.010  -1.522  34.013  1.000 24.830  0 748 HOH AAA O     1 ? ? 
HETATM 15418 O O     . HOH N 4 .   ? 4.030   -10.680 24.158  1.000 29.037  0 749 HOH AAA O     1 ? ? 
HETATM 15419 O O     . HOH N 4 .   ? 11.704  9.442   8.145   1.000 43.445  0 750 HOH AAA O     1 ? ? 
HETATM 15420 O O     . HOH N 4 .   ? 25.205  4.133   34.302  1.000 29.266  0 751 HOH AAA O     1 ? ? 
HETATM 15421 O O     . HOH N 4 .   ? 30.232  5.079   38.090  1.000 28.244  0 752 HOH AAA O     1 ? ? 
HETATM 15422 O O     . HOH N 4 .   ? 34.505  0.334   29.219  1.000 24.997  0 753 HOH AAA O     1 ? ? 
HETATM 15423 O O     . HOH N 4 .   ? 3.901   1.396   13.805  1.000 27.008  0 754 HOH AAA O     1 ? ? 
HETATM 15424 O O     . HOH N 4 .   ? 13.387  -9.000  44.862  1.000 28.874  0 755 HOH AAA O     1 ? ? 
HETATM 15425 O O     . HOH N 4 .   ? 5.530   -7.371  32.546  1.000 22.131  0 756 HOH AAA O     1 ? ? 
HETATM 15426 O O     . HOH N 4 .   ? 44.812  3.688   30.541  1.000 18.646  0 757 HOH AAA O     1 ? ? 
HETATM 15427 O O     . HOH N 4 .   ? 13.309  13.473  7.971   1.000 34.873  0 758 HOH AAA O     1 ? ? 
HETATM 15428 O O     . HOH N 4 .   ? 28.265  -2.612  28.832  1.000 20.768  0 759 HOH AAA O     1 ? ? 
HETATM 15429 O O     . HOH N 4 .   ? 15.047  -2.252  29.698  1.000 17.326  0 760 HOH AAA O     1 ? ? 
HETATM 15430 O O     . HOH N 4 .   ? 29.461  -2.633  31.526  1.000 22.044  0 761 HOH AAA O     1 ? ? 
HETATM 15431 O O     . HOH N 4 .   ? 24.207  -23.915 32.800  1.000 23.173  0 762 HOH AAA O     1 ? ? 
HETATM 15432 O O     . HOH N 4 .   ? 36.348  -8.315  36.826  1.000 31.658  0 763 HOH AAA O     1 ? ? 
HETATM 15433 O O     . HOH N 4 .   ? 45.557  4.941   48.030  1.000 36.902  0 764 HOH AAA O     1 ? ? 
HETATM 15434 O O     . HOH N 4 .   ? 17.337  15.614  29.395  1.000 38.555  0 765 HOH AAA O     1 ? ? 
HETATM 15435 O O     . HOH N 4 .   ? 10.263  3.829   33.300  1.000 21.874  0 766 HOH AAA O     1 ? ? 
HETATM 15436 O O     . HOH N 4 .   ? 17.060  -5.799  34.446  1.000 28.722  0 767 HOH AAA O     1 ? ? 
HETATM 15437 O O     . HOH N 4 .   ? 13.606  -2.204  27.259  1.000 26.486  0 768 HOH AAA O     1 ? ? 
HETATM 15438 O O     . HOH N 4 .   ? 3.594   -14.870 23.416  1.000 31.705  0 769 HOH AAA O     1 ? ? 
HETATM 15439 O O     . HOH N 4 .   ? -17.964 15.419  13.816  1.000 38.074  0 770 HOH AAA O     1 ? ? 
HETATM 15440 O O     . HOH N 4 .   ? 43.148  9.429   24.829  1.000 50.476  0 771 HOH AAA O     1 ? ? 
HETATM 15441 O O     . HOH N 4 .   ? 29.671  -9.003  27.636  1.000 28.018  0 772 HOH AAA O     1 ? ? 
HETATM 15442 O O     . HOH N 4 .   ? 2.150   14.770  9.460   1.000 32.329  0 773 HOH AAA O     1 ? ? 
HETATM 15443 O O     . HOH N 4 .   ? 14.227  -31.675 39.549  1.000 33.412  0 774 HOH AAA O     1 ? ? 
HETATM 15444 O O     . HOH N 4 .   ? 27.991  19.972  16.056  1.000 28.040  0 775 HOH AAA O     1 ? ? 
HETATM 15445 O O     . HOH N 4 .   ? 33.294  -0.732  31.361  1.000 21.836  0 776 HOH AAA O     1 ? ? 
HETATM 15446 O O     . HOH N 4 .   ? -2.463  -9.342  27.950  1.000 22.849  0 777 HOH AAA O     1 ? ? 
HETATM 15447 O O     . HOH N 4 .   ? 10.399  23.834  46.158  1.000 26.309  0 778 HOH AAA O     1 ? ? 
HETATM 15448 O O     . HOH N 4 .   ? 13.725  0.885   39.393  1.000 20.170  0 779 HOH AAA O     1 ? ? 
HETATM 15449 O O     . HOH N 4 .   ? -1.890  17.342  30.624  1.000 41.002  0 780 HOH AAA O     1 ? ? 
HETATM 15450 O O     . HOH N 4 .   ? 49.437  9.887   24.310  1.000 29.486  0 781 HOH AAA O     1 ? ? 
HETATM 15451 O O     . HOH N 4 .   ? 7.934   -0.568  35.419  1.000 29.321  0 782 HOH AAA O     1 ? ? 
HETATM 15452 O O     . HOH N 4 .   ? 7.169   8.857   41.811  1.000 51.547  0 783 HOH AAA O     1 ? ? 
HETATM 15453 O O     . HOH N 4 .   ? 36.026  -28.196 31.793  1.000 32.239  0 784 HOH AAA O     1 ? ? 
HETATM 15454 O O     . HOH N 4 .   ? 19.279  22.402  21.622  1.000 40.704  0 785 HOH AAA O     1 ? ? 
HETATM 15455 O O     . HOH N 4 .   ? -13.962 4.749   7.009   1.000 36.155  0 786 HOH AAA O     1 ? ? 
HETATM 15456 O O     . HOH N 4 .   ? 47.132  -1.080  55.259  1.000 19.113  0 787 HOH AAA O     1 ? ? 
HETATM 15457 O O     . HOH N 4 .   ? 37.338  -20.589 39.159  1.000 39.012  0 788 HOH AAA O     1 ? ? 
HETATM 15458 O O     . HOH N 4 .   ? -15.181 7.751   7.111   1.000 42.557  0 789 HOH AAA O     1 ? ? 
HETATM 15459 O O     . HOH O 4 .   ? 40.449  -29.054 39.079  1.000 32.484  0 701 HOH BBB O     1 ? ? 
HETATM 15460 O O     . HOH O 4 .   ? 27.526  -45.151 27.943  1.000 33.992  0 702 HOH BBB O     1 ? ? 
HETATM 15461 O O     . HOH O 4 .   ? 31.191  -10.956 20.533  1.000 28.274  0 703 HOH BBB O     1 ? ? 
HETATM 15462 O O     . HOH O 4 .   ? 48.605  -28.811 18.462  1.000 16.351  0 704 HOH BBB O     1 ? ? 
HETATM 15463 O O     . HOH O 4 .   ? 34.410  -0.452  16.274  1.000 18.258  0 705 HOH BBB O     1 ? ? 
HETATM 15464 O O     . HOH O 4 .   ? 33.452  -43.543 16.396  1.000 28.216  0 706 HOH BBB O     1 ? ? 
HETATM 15465 O O     . HOH O 4 .   ? 35.864  -21.192 6.099   1.000 19.769  0 707 HOH BBB O     1 ? ? 
HETATM 15466 O O     . HOH O 4 .   ? 19.226  -25.411 11.456  1.000 22.574  0 708 HOH BBB O     1 ? ? 
HETATM 15467 O O     . HOH O 4 .   ? 22.141  -27.850 2.709   1.000 31.470  0 709 HOH BBB O     1 ? ? 
HETATM 15468 O O     . HOH O 4 .   ? 48.665  -26.215 19.745  1.000 17.686  0 710 HOH BBB O     1 ? ? 
HETATM 15469 O O     . HOH O 4 .   ? 64.854  -4.559  21.891  1.000 24.948  0 711 HOH BBB O     1 ? ? 
HETATM 15470 O O     . HOH O 4 .   ? 33.237  -20.841 19.663  1.000 10.740  0 712 HOH BBB O     1 ? ? 
HETATM 15471 O O     . HOH O 4 .   ? 29.690  1.871   10.602  1.000 27.689  0 713 HOH BBB O     1 ? ? 
HETATM 15472 O O     . HOH O 4 .   ? 44.342  -27.029 17.533  1.000 13.334  0 714 HOH BBB O     1 ? ? 
HETATM 15473 O O     . HOH O 4 .   ? 8.040   -15.071 21.539  1.000 26.588  0 715 HOH BBB O     1 ? ? 
HETATM 15474 O O     . HOH O 4 .   ? 39.540  -23.277 14.215  1.000 21.939  0 716 HOH BBB O     1 ? ? 
HETATM 15475 O O     . HOH O 4 .   ? 51.042  -35.409 18.584  1.000 24.354  0 717 HOH BBB O     1 ? ? 
HETATM 15476 O O     . HOH O 4 .   ? 50.982  -20.285 -4.859  1.000 38.697  0 718 HOH BBB O     1 ? ? 
HETATM 15477 O O     . HOH O 4 .   ? 36.234  -17.178 16.383  1.000 39.533  0 719 HOH BBB O     1 ? ? 
HETATM 15478 O O     . HOH O 4 .   ? 21.935  -26.699 11.415  1.000 21.755  0 720 HOH BBB O     1 ? ? 
HETATM 15479 O O     . HOH O 4 .   ? 52.388  -27.884 28.683  1.000 30.023  0 721 HOH BBB O     1 ? ? 
HETATM 15480 O O     . HOH O 4 .   ? 53.351  -30.159 20.741  1.000 14.421  0 722 HOH BBB O     1 ? ? 
HETATM 15481 O O     . HOH O 4 .   ? 59.379  -47.062 27.418  1.000 32.468  0 723 HOH BBB O     1 ? ? 
HETATM 15482 O O     . HOH O 4 .   ? 43.240  -24.738 24.217  1.000 31.757  0 724 HOH BBB O     1 ? ? 
HETATM 15483 O O     . HOH O 4 .   ? 39.779  -3.815  8.139   1.000 28.052  0 725 HOH BBB O     1 ? ? 
HETATM 15484 O O     . HOH O 4 .   ? 23.964  -15.706 1.763   1.000 36.893  0 726 HOH BBB O     1 ? ? 
HETATM 15485 O O     . HOH O 4 .   ? 61.146  -8.311  7.057   1.000 31.988  0 727 HOH BBB O     1 ? ? 
HETATM 15486 O O     . HOH O 4 .   ? 47.785  -20.865 16.469  1.000 19.153  0 728 HOH BBB O     1 ? ? 
HETATM 15487 O O     . HOH O 4 .   ? 39.616  -8.709  13.692  1.000 17.584  0 729 HOH BBB O     1 ? ? 
HETATM 15488 O O     . HOH O 4 .   ? 46.389  -21.542 12.827  1.000 22.184  0 730 HOH BBB O     1 ? ? 
HETATM 15489 O O     . HOH O 4 .   ? 22.351  -40.657 28.611  1.000 29.339  0 731 HOH BBB O     1 ? ? 
HETATM 15490 O O     . HOH O 4 .   ? 32.411  18.118  -2.085  1.000 36.418  0 732 HOH BBB O     1 ? ? 
HETATM 15491 O O     . HOH O 4 .   ? 41.244  -19.950 35.219  1.000 49.192  0 733 HOH BBB O     1 ? ? 
HETATM 15492 O O     . HOH O 4 .   ? 30.087  -16.440 12.087  1.000 37.191  0 734 HOH BBB O     1 ? ? 
HETATM 15493 O O     . HOH O 4 .   ? 23.844  -26.140 20.993  1.000 20.755  0 735 HOH BBB O     1 ? ? 
HETATM 15494 O O     . HOH O 4 .   ? 58.824  -35.099 25.791  1.000 20.740  0 736 HOH BBB O     1 ? ? 
HETATM 15495 O O     . HOH O 4 .   ? 5.308   -20.817 19.982  1.000 31.151  0 737 HOH BBB O     1 ? ? 
HETATM 15496 O O     . HOH O 4 .   ? 37.661  -18.771 2.302   1.000 34.565  0 738 HOH BBB O     1 ? ? 
HETATM 15497 O O     . HOH O 4 .   ? 49.748  -26.136 25.959  1.000 23.106  0 739 HOH BBB O     1 ? ? 
HETATM 15498 O O     . HOH O 4 .   ? 11.664  -11.178 25.064  1.000 22.557  0 740 HOH BBB O     1 ? ? 
HETATM 15499 O O     . HOH O 4 .   ? 50.461  -4.459  3.671   1.000 23.937  0 741 HOH BBB O     1 ? ? 
HETATM 15500 O O     . HOH O 4 .   ? 32.307  12.688  11.708  1.000 30.199  0 742 HOH BBB O     1 ? ? 
HETATM 15501 O O     . HOH O 4 .   ? 48.396  -21.313 7.881   1.000 16.689  0 743 HOH BBB O     1 ? ? 
HETATM 15502 O O     . HOH O 4 .   ? 56.461  -15.024 18.501  1.000 27.220  0 744 HOH BBB O     1 ? ? 
HETATM 15503 O O     . HOH O 4 .   ? 54.247  -26.265 27.810  1.000 32.614  0 745 HOH BBB O     1 ? ? 
HETATM 15504 O O     . HOH O 4 .   ? 23.848  -28.344 19.909  1.000 22.425  0 746 HOH BBB O     1 ? ? 
HETATM 15505 O O     . HOH O 4 .   ? 49.632  -7.456  32.911  1.000 36.918  0 747 HOH BBB O     1 ? ? 
HETATM 15506 O O     . HOH O 4 .   ? 35.278  -38.887 12.236  1.000 28.829  0 748 HOH BBB O     1 ? ? 
HETATM 15507 O O     . HOH O 4 .   ? 52.492  -35.653 16.250  1.000 25.456  0 749 HOH BBB O     1 ? ? 
HETATM 15508 O O     . HOH O 4 .   ? 13.746  -23.830 14.821  1.000 37.219  0 750 HOH BBB O     1 ? ? 
HETATM 15509 O O     . HOH O 4 .   ? 23.664  12.575  14.720  1.000 39.879  0 751 HOH BBB O     1 ? ? 
HETATM 15510 O O     . HOH O 4 .   ? 35.389  11.189  18.004  1.000 26.422  0 752 HOH BBB O     1 ? ? 
HETATM 15511 O O     . HOH O 4 .   ? 37.734  10.442  18.662  1.000 19.477  0 753 HOH BBB O     1 ? ? 
HETATM 15512 O O     . HOH O 4 .   ? 50.328  -30.543 12.394  1.000 23.602  0 754 HOH BBB O     1 ? ? 
HETATM 15513 O O     . HOH O 4 .   ? 42.400  -32.865 19.051  1.000 22.977  0 755 HOH BBB O     1 ? ? 
HETATM 15514 O O     . HOH O 4 .   ? 28.459  6.426   12.167  1.000 21.507  0 756 HOH BBB O     1 ? ? 
HETATM 15515 O O     . HOH O 4 .   ? 26.879  2.254   11.259  1.000 35.485  0 757 HOH BBB O     1 ? ? 
HETATM 15516 O O     . HOH O 4 .   ? 51.284  -29.428 18.823  1.000 30.808  0 758 HOH BBB O     1 ? ? 
HETATM 15517 O O     . HOH O 4 .   ? 43.370  -31.188 24.254  1.000 27.687  0 759 HOH BBB O     1 ? ? 
HETATM 15518 O O     . HOH O 4 .   ? 56.046  -28.006 26.603  1.000 20.239  0 760 HOH BBB O     1 ? ? 
HETATM 15519 O O     . HOH O 4 .   ? 52.751  -24.330 32.066  1.000 17.297  0 761 HOH BBB O     1 ? ? 
HETATM 15520 O O     . HOH O 4 .   ? 13.304  -14.049 0.959   1.000 27.185  0 762 HOH BBB O     1 ? ? 
HETATM 15521 O O     . HOH O 4 .   ? 37.841  -28.734 18.765  1.000 15.492  0 763 HOH BBB O     1 ? ? 
HETATM 15522 O O     . HOH O 4 .   ? 36.110  -30.447 17.604  1.000 30.125  0 764 HOH BBB O     1 ? ? 
HETATM 15523 O O     . HOH O 4 .   ? 52.493  -0.542  8.955   1.000 22.684  0 765 HOH BBB O     1 ? ? 
HETATM 15524 O O     . HOH O 4 .   ? 57.469  -12.852 8.595   1.000 22.764  0 766 HOH BBB O     1 ? ? 
HETATM 15525 O O     . HOH O 4 .   ? 11.221  -10.584 13.559  1.000 32.487  0 767 HOH BBB O     1 ? ? 
HETATM 15526 O O     . HOH O 4 .   ? 51.248  -16.309 18.788  1.000 28.173  0 768 HOH BBB O     1 ? ? 
HETATM 15527 O O     . HOH O 4 .   ? 60.429  -11.108 -8.079  1.000 33.791  0 769 HOH BBB O     1 ? ? 
HETATM 15528 O O     . HOH O 4 .   ? 61.100  -21.846 3.114   1.000 33.857  0 770 HOH BBB O     1 ? ? 
HETATM 15529 O O     . HOH O 4 .   ? 21.852  -10.587 -1.723  1.000 37.584  0 771 HOH BBB O     1 ? ? 
HETATM 15530 O O     . HOH O 4 .   ? 40.650  -21.218 -3.550  1.000 27.169  0 772 HOH BBB O     1 ? ? 
HETATM 15531 O O     . HOH O 4 .   ? 24.076  -7.591  1.571   1.000 26.650  0 773 HOH BBB O     1 ? ? 
HETATM 15532 O O     . HOH O 4 .   ? 30.776  -20.953 0.689   1.000 32.363  0 774 HOH BBB O     1 ? ? 
HETATM 15533 O O     . HOH O 4 .   ? 53.884  -20.266 37.401  1.000 28.229  0 775 HOH BBB O     1 ? ? 
HETATM 15534 O O     . HOH O 4 .   ? 30.859  -1.119  14.684  1.000 25.693  0 776 HOH BBB O     1 ? ? 
HETATM 15535 O O     . HOH O 4 .   ? 59.526  -9.799  16.134  1.000 29.786  0 777 HOH BBB O     1 ? ? 
HETATM 15536 O O     . HOH O 4 .   ? 8.333   -26.155 17.981  1.000 37.250  0 778 HOH BBB O     1 ? ? 
HETATM 15537 O O     . HOH O 4 .   ? 27.264  -19.379 8.037   1.000 30.016  0 779 HOH BBB O     1 ? ? 
HETATM 15538 O O     . HOH O 4 .   ? 43.676  -14.263 15.218  1.000 36.320  0 780 HOH BBB O     1 ? ? 
HETATM 15539 O O     . HOH O 4 .   ? 53.831  -30.381 14.366  1.000 30.862  0 781 HOH BBB O     1 ? ? 
HETATM 15540 O O     . HOH O 4 .   ? 54.249  -23.804 13.848  1.000 20.768  0 782 HOH BBB O     1 ? ? 
HETATM 15541 O O     . HOH O 4 .   ? 51.424  -2.813  34.001  1.000 30.602  0 783 HOH BBB O     1 ? ? 
HETATM 15542 O O     . HOH O 4 .   ? 59.523  -12.361 17.382  1.000 35.584  0 784 HOH BBB O     1 ? ? 
HETATM 15543 O O     . HOH O 4 .   ? 43.449  -21.242 9.029   1.000 17.412  0 785 HOH BBB O     1 ? ? 
HETATM 15544 O O     . HOH O 4 .   ? 51.176  -32.408 10.864  1.000 26.708  0 786 HOH BBB O     1 ? ? 
HETATM 15545 O O     . HOH O 4 .   ? 65.537  -22.828 5.765   1.000 44.936  0 787 HOH BBB O     1 ? ? 
HETATM 15546 O O     . HOH O 4 .   ? 6.726   -10.524 9.025   1.000 28.930  0 788 HOH BBB O     1 ? ? 
HETATM 15547 O O     . HOH O 4 .   ? 59.727  -15.318 -8.744  1.000 26.526  0 789 HOH BBB O     1 ? ? 
HETATM 15548 O O     . HOH O 4 .   ? 26.691  -36.960 16.232  1.000 34.410  0 790 HOH BBB O     1 ? ? 
HETATM 15549 O O     . HOH O 4 .   ? 34.668  -21.841 12.477  1.000 30.765  0 791 HOH BBB O     1 ? ? 
HETATM 15550 O O     . HOH O 4 .   ? 58.457  -14.675 16.816  1.000 30.319  0 792 HOH BBB O     1 ? ? 
HETATM 15551 O O     . HOH O 4 .   ? 25.795  15.754  0.702   1.000 19.152  0 793 HOH BBB O     1 ? ? 
HETATM 15552 O O     . HOH O 4 .   ? 49.140  -0.936  -4.641  1.000 38.478  0 794 HOH BBB O     1 ? ? 
HETATM 15553 O O     . HOH P 4 .   ? 47.522  -1.115  62.340  1.000 24.256  0 701 HOH CCC O     1 ? ? 
HETATM 15554 O O     . HOH P 4 .   ? 68.417  21.537  54.476  1.000 24.915  0 702 HOH CCC O     1 ? ? 
HETATM 15555 O O     . HOH P 4 .   ? 24.367  -13.239 61.815  1.000 39.700  0 703 HOH CCC O     1 ? ? 
HETATM 15556 O O     . HOH P 4 .   ? 38.184  -3.312  67.571  1.000 31.119  0 704 HOH CCC O     1 ? ? 
HETATM 15557 O O     . HOH P 4 .   ? 32.240  -2.085  47.051  1.000 31.380  0 705 HOH CCC O     1 ? ? 
HETATM 15558 O O     . HOH P 4 .   ? 62.955  6.226   69.978  1.000 26.526  0 706 HOH CCC O     1 ? ? 
HETATM 15559 O O     . HOH P 4 .   ? 63.878  28.452  65.507  1.000 35.287  0 707 HOH CCC O     1 ? ? 
HETATM 15560 O O     . HOH P 4 .   ? 40.706  -9.973  84.903  1.000 44.743  0 708 HOH CCC O     1 ? ? 
HETATM 15561 O O     . HOH P 4 .   ? 31.606  3.876   60.845  1.000 21.959  0 709 HOH CCC O     1 ? ? 
HETATM 15562 O O     . HOH P 4 .   ? 88.332  0.933   44.609  1.000 35.550  0 710 HOH CCC O     1 ? ? 
HETATM 15563 O O     . HOH P 4 .   ? 64.221  -1.825  62.637  1.000 28.557  0 711 HOH CCC O     1 ? ? 
HETATM 15564 O O     . HOH P 4 .   ? 51.647  -3.463  82.942  1.000 46.253  0 712 HOH CCC O     1 ? ? 
HETATM 15565 O O     . HOH P 4 .   ? 40.102  19.249  68.748  1.000 36.682  0 713 HOH CCC O     1 ? ? 
HETATM 15566 O O     . HOH P 4 .   ? 48.645  -8.013  60.718  1.000 22.947  0 714 HOH CCC O     1 ? ? 
HETATM 15567 O O     . HOH P 4 .   ? 36.043  -9.989  58.229  1.000 30.332  0 715 HOH CCC O     1 ? ? 
HETATM 15568 O O     . HOH P 4 .   ? 39.362  0.868   61.633  1.000 29.771  0 716 HOH CCC O     1 ? ? 
HETATM 15569 O O     . HOH P 4 .   ? 53.535  -13.164 66.614  1.000 24.375  0 717 HOH CCC O     1 ? ? 
HETATM 15570 O O     . HOH P 4 .   ? 63.212  22.954  46.561  1.000 40.698  0 718 HOH CCC O     1 ? ? 
HETATM 15571 O O     . HOH P 4 .   ? 43.274  -5.586  65.685  1.000 16.523  0 719 HOH CCC O     1 ? ? 
HETATM 15572 O O     . HOH P 4 .   ? 44.013  -10.946 74.156  1.000 16.235  0 720 HOH CCC O     1 ? ? 
HETATM 15573 O O     . HOH P 4 .   ? 39.303  -4.160  72.379  1.000 20.982  0 721 HOH CCC O     1 ? ? 
HETATM 15574 O O     . HOH P 4 .   ? 50.872  1.282   56.242  1.000 29.127  0 722 HOH CCC O     1 ? ? 
HETATM 15575 O O     . HOH P 4 .   ? 61.831  -1.551  61.206  1.000 31.597  0 723 HOH CCC O     1 ? ? 
HETATM 15576 O O     . HOH P 4 .   ? 65.750  -13.357 78.269  1.000 22.580  0 724 HOH CCC O     1 ? ? 
HETATM 15577 O O     . HOH P 4 .   ? 40.551  14.197  69.801  1.000 29.310  0 725 HOH CCC O     1 ? ? 
HETATM 15578 O O     . HOH P 4 .   ? 60.983  5.682   74.017  1.000 22.727  0 726 HOH CCC O     1 ? ? 
HETATM 15579 O O     . HOH P 4 .   ? 40.672  -12.677 66.663  1.000 24.201  0 727 HOH CCC O     1 ? ? 
HETATM 15580 O O     . HOH P 4 .   ? 65.349  24.729  55.034  1.000 29.176  0 728 HOH CCC O     1 ? ? 
HETATM 15581 O O     . HOH P 4 .   ? 71.424  15.783  65.745  1.000 25.551  0 729 HOH CCC O     1 ? ? 
HETATM 15582 O O     . HOH P 4 .   ? 51.203  -10.055 58.895  1.000 26.339  0 730 HOH CCC O     1 ? ? 
HETATM 15583 O O     . HOH P 4 .   ? 51.804  11.148  55.398  1.000 21.563  0 731 HOH CCC O     1 ? ? 
HETATM 15584 O O     . HOH P 4 .   ? 18.791  -1.699  71.174  1.000 37.016  0 732 HOH CCC O     1 ? ? 
HETATM 15585 O O     . HOH P 4 .   ? 45.837  -4.351  72.177  1.000 29.647  0 733 HOH CCC O     1 ? ? 
HETATM 15586 O O     . HOH P 4 .   ? 29.950  -17.045 71.485  1.000 31.826  0 734 HOH CCC O     1 ? ? 
HETATM 15587 O O     . HOH P 4 .   ? 55.682  33.362  65.874  1.000 43.159  0 735 HOH CCC O     1 ? ? 
HETATM 15588 O O     . HOH P 4 .   ? 72.221  -3.780  60.963  1.000 36.786  0 736 HOH CCC O     1 ? ? 
HETATM 15589 O O     . HOH P 4 .   ? 48.521  -10.048 56.092  1.000 21.762  0 737 HOH CCC O     1 ? ? 
HETATM 15590 O O     . HOH P 4 .   ? 40.689  2.828   65.947  1.000 24.946  0 738 HOH CCC O     1 ? ? 
HETATM 15591 O O     . HOH P 4 .   ? 46.192  -9.915  65.102  1.000 20.224  0 739 HOH CCC O     1 ? ? 
HETATM 15592 O O     . HOH P 4 .   ? 42.060  0.837   66.768  1.000 30.820  0 740 HOH CCC O     1 ? ? 
HETATM 15593 O O     . HOH P 4 .   ? 81.250  0.272   52.191  1.000 31.820  0 741 HOH CCC O     1 ? ? 
HETATM 15594 O O     . HOH P 4 .   ? 46.699  26.373  42.553  1.000 40.601  0 742 HOH CCC O     1 ? ? 
HETATM 15595 O O     . HOH P 4 .   ? 43.680  -16.139 75.544  1.000 27.596  0 743 HOH CCC O     1 ? ? 
HETATM 15596 O O     . HOH P 4 .   ? 53.783  8.159   59.945  1.000 41.146  0 744 HOH CCC O     1 ? ? 
HETATM 15597 O O     . HOH P 4 .   ? 68.412  -0.838  58.158  1.000 18.119  0 745 HOH CCC O     1 ? ? 
HETATM 15598 O O     . HOH P 4 .   ? 28.176  -24.251 74.461  1.000 37.691  0 746 HOH CCC O     1 ? ? 
HETATM 15599 O O     . HOH P 4 .   ? 69.746  22.674  57.805  1.000 38.457  0 747 HOH CCC O     1 ? ? 
HETATM 15600 O O     . HOH P 4 .   ? 47.311  13.083  54.587  1.000 26.723  0 748 HOH CCC O     1 ? ? 
HETATM 15601 O O     . HOH P 4 .   ? 27.569  7.811   72.499  1.000 30.084  0 749 HOH CCC O     1 ? ? 
HETATM 15602 O O     . HOH P 4 .   ? 69.358  -15.073 56.126  1.000 20.184  0 750 HOH CCC O     1 ? ? 
HETATM 15603 O O     . HOH P 4 .   ? 38.749  3.535   67.600  1.000 31.462  0 751 HOH CCC O     1 ? ? 
HETATM 15604 O O     . HOH P 4 .   ? 69.815  24.668  51.787  1.000 29.720  0 752 HOH CCC O     1 ? ? 
HETATM 15605 O O     . HOH P 4 .   ? 49.041  -8.109  57.985  1.000 23.398  0 753 HOH CCC O     1 ? ? 
HETATM 15606 O O     . HOH P 4 .   ? 46.525  -27.289 53.222  1.000 36.300  0 754 HOH CCC O     1 ? ? 
HETATM 15607 O O     . HOH P 4 .   ? 46.622  -14.085 79.906  1.000 25.666  0 755 HOH CCC O     1 ? ? 
HETATM 15608 O O     . HOH P 4 .   ? 42.748  -18.204 61.993  1.000 31.239  0 756 HOH CCC O     1 ? ? 
HETATM 15609 O O     . HOH P 4 .   ? 37.497  -12.027 59.125  1.000 33.174  0 757 HOH CCC O     1 ? ? 
HETATM 15610 O O     . HOH P 4 .   ? 10.645  -4.583  82.837  1.000 36.986  0 758 HOH CCC O     1 ? ? 
HETATM 15611 O O     . HOH P 4 .   ? 22.104  4.710   67.337  1.000 29.631  0 759 HOH CCC O     1 ? ? 
HETATM 15612 O O     . HOH P 4 .   ? 41.828  -13.446 86.427  1.000 44.979  0 760 HOH CCC O     1 ? ? 
HETATM 15613 O O     . HOH P 4 .   ? 42.411  23.850  43.853  1.000 38.140  0 761 HOH CCC O     1 ? ? 
HETATM 15614 O O     . HOH P 4 .   ? 45.948  20.996  42.391  1.000 33.902  0 762 HOH CCC O     1 ? ? 
HETATM 15615 O O     . HOH P 4 .   ? 45.230  -27.966 51.032  1.000 37.992  0 763 HOH CCC O     1 ? ? 
HETATM 15616 O O     . HOH P 4 .   ? 40.451  -15.984 62.808  1.000 31.084  0 764 HOH CCC O     1 ? ? 
HETATM 15617 O O     . HOH Q 4 .   ? 68.047  3.291   82.468  1.000 18.649  0 701 HOH DDD O     1 ? ? 
HETATM 15618 O O     . HOH Q 4 .   ? 60.643  20.638  91.829  1.000 36.303  0 702 HOH DDD O     1 ? ? 
HETATM 15619 O O     . HOH Q 4 .   ? 57.354  15.675  71.482  1.000 27.810  0 703 HOH DDD O     1 ? ? 
HETATM 15620 O O     . HOH Q 4 .   ? 67.438  14.338  73.411  1.000 30.157  0 704 HOH DDD O     1 ? ? 
HETATM 15621 O O     . HOH Q 4 .   ? 71.627  -4.674  83.615  1.000 29.299  0 705 HOH DDD O     1 ? ? 
HETATM 15622 O O     . HOH Q 4 .   ? 73.089  54.028  76.661  1.000 42.461  0 706 HOH DDD O     1 ? ? 
HETATM 15623 O O     . HOH Q 4 .   ? 60.410  29.154  71.969  1.000 24.548  0 707 HOH DDD O     1 ? ? 
HETATM 15624 O O     . HOH Q 4 .   ? 75.906  12.395  81.004  1.000 20.357  0 708 HOH DDD O     1 ? ? 
HETATM 15625 O O     . HOH Q 4 .   ? 74.441  31.945  74.581  1.000 19.340  0 709 HOH DDD O     1 ? ? 
HETATM 15626 O O     . HOH Q 4 .   ? 90.065  33.399  73.003  1.000 32.416  0 710 HOH DDD O     1 ? ? 
HETATM 15627 O O     . HOH Q 4 .   ? 87.559  7.461   64.020  1.000 22.053  0 711 HOH DDD O     1 ? ? 
HETATM 15628 O O     . HOH Q 4 .   ? 77.411  2.289   80.850  1.000 27.887  0 712 HOH DDD O     1 ? ? 
HETATM 15629 O O     . HOH Q 4 .   ? 70.143  50.406  63.224  1.000 41.161  0 713 HOH DDD O     1 ? ? 
HETATM 15630 O O     . HOH Q 4 .   ? 85.029  27.481  76.818  1.000 35.947  0 714 HOH DDD O     1 ? ? 
HETATM 15631 O O     . HOH Q 4 .   ? 87.657  19.752  75.387  1.000 29.295  0 715 HOH DDD O     1 ? ? 
HETATM 15632 O O     . HOH Q 4 .   ? 83.144  1.825   78.406  1.000 37.205  0 716 HOH DDD O     1 ? ? 
HETATM 15633 O O     . HOH Q 4 .   ? 99.538  10.806  75.406  1.000 43.440  0 717 HOH DDD O     1 ? ? 
HETATM 15634 O O     . HOH Q 4 .   ? 90.928  27.292  80.454  1.000 36.236  0 718 HOH DDD O     1 ? ? 
HETATM 15635 O O     . HOH Q 4 .   ? 57.678  22.793  94.255  1.000 33.302  0 719 HOH DDD O     1 ? ? 
HETATM 15636 O O     . HOH Q 4 .   ? 65.947  8.091   89.209  1.000 28.798  0 720 HOH DDD O     1 ? ? 
HETATM 15637 O O     . HOH Q 4 .   ? 88.701  4.359   86.395  1.000 17.861  0 721 HOH DDD O     1 ? ? 
HETATM 15638 O O     . HOH Q 4 .   ? 49.419  10.163  86.334  1.000 30.470  0 722 HOH DDD O     1 ? ? 
HETATM 15639 O O     . HOH Q 4 .   ? 71.359  4.640   67.561  1.000 37.984  0 723 HOH DDD O     1 ? ? 
HETATM 15640 O O     . HOH Q 4 .   ? 97.804  25.676  91.103  1.000 51.432  0 724 HOH DDD O     1 ? ? 
HETATM 15641 O O     . HOH Q 4 .   ? 72.704  34.114  75.449  1.000 36.785  0 725 HOH DDD O     1 ? ? 
HETATM 15642 O O     . HOH Q 4 .   ? 78.197  57.487  57.949  1.000 35.567  0 726 HOH DDD O     1 ? ? 
HETATM 15643 O O     . HOH Q 4 .   ? 71.114  4.569   78.568  1.000 15.646  0 727 HOH DDD O     1 ? ? 
HETATM 15644 O O     . HOH Q 4 .   ? 63.771  23.589  85.414  1.000 30.731  0 728 HOH DDD O     1 ? ? 
HETATM 15645 O O     . HOH Q 4 .   ? 75.585  11.155  98.834  1.000 30.791  0 729 HOH DDD O     1 ? ? 
HETATM 15646 O O     . HOH Q 4 .   ? 93.992  7.016   68.885  1.000 36.008  0 730 HOH DDD O     1 ? ? 
HETATM 15647 O O     . HOH Q 4 .   ? 89.502  26.621  61.660  1.000 20.631  0 731 HOH DDD O     1 ? ? 
HETATM 15648 O O     . HOH Q 4 .   ? 75.930  34.314  53.623  1.000 41.534  0 732 HOH DDD O     1 ? ? 
HETATM 15649 O O     . HOH Q 4 .   ? 45.707  27.279  72.764  1.000 39.705  0 733 HOH DDD O     1 ? ? 
HETATM 15650 O O     . HOH Q 4 .   ? 39.953  17.799  79.047  1.000 44.086  0 734 HOH DDD O     1 ? ? 
HETATM 15651 O O     . HOH Q 4 .   ? 74.559  5.569   83.316  1.000 40.144  0 735 HOH DDD O     1 ? ? 
HETATM 15652 O O     . HOH Q 4 .   ? 63.448  12.104  93.217  1.000 27.422  0 736 HOH DDD O     1 ? ? 
HETATM 15653 O O     . HOH Q 4 .   ? 43.775  15.950  95.494  1.000 26.336  0 737 HOH DDD O     1 ? ? 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . LEU A 24  ? 0.957 1.288 0.781 0.248  -0.040 -0.111 24  LEU AAA N   
2     C CA  . LEU A 24  ? 0.950 1.270 0.766 0.252  -0.037 -0.103 24  LEU AAA CA  
3     C C   . LEU A 24  ? 0.929 1.244 0.755 0.241  -0.038 -0.105 24  LEU AAA C   
4     O O   . LEU A 24  ? 0.939 1.239 0.761 0.239  -0.034 -0.097 24  LEU AAA O   
5     C CB  . LEU A 24  ? 0.978 1.314 0.785 0.267  -0.039 -0.105 24  LEU AAA CB  
6     C CG  . LEU A 24  ? 1.006 1.345 0.800 0.281  -0.037 -0.100 24  LEU AAA CG  
7     C CD1 . LEU A 24  ? 1.002 1.366 0.792 0.294  -0.041 -0.108 24  LEU AAA CD1 
8     C CD2 . LEU A 24  ? 1.007 1.327 0.788 0.287  -0.030 -0.086 24  LEU AAA CD2 
9     N N   . THR A 25  ? 0.903 1.231 0.742 0.233  -0.042 -0.116 25  THR AAA N   
10    C CA  . THR A 25  ? 0.868 1.192 0.719 0.221  -0.043 -0.119 25  THR AAA CA  
11    C C   . THR A 25  ? 0.852 1.153 0.702 0.212  -0.038 -0.109 25  THR AAA C   
12    O O   . THR A 25  ? 0.868 1.160 0.718 0.209  -0.036 -0.106 25  THR AAA O   
13    C CB  . THR A 25  ? 0.837 1.174 0.704 0.213  -0.046 -0.131 25  THR AAA CB  
14    O OG1 . THR A 25  ? 0.750 1.085 0.627 0.203  -0.047 -0.134 25  THR AAA OG1 
15    C CG2 . THR A 25  ? 0.826 1.157 0.698 0.206  -0.045 -0.130 25  THR AAA CG2 
16    N N   . PHE A 26  ? 0.757 1.047 0.604 0.210  -0.035 -0.104 26  PHE AAA N   
17    C CA  . PHE A 26  ? 0.700 0.968 0.545 0.203  -0.031 -0.094 26  PHE AAA CA  
18    C C   . PHE A 26  ? 0.648 0.909 0.482 0.211  -0.028 -0.086 26  PHE AAA C   
19    O O   . PHE A 26  ? 0.620 0.890 0.454 0.215  -0.029 -0.090 26  PHE AAA O   
20    C CB  . PHE A 26  ? 0.686 0.950 0.544 0.189  -0.032 -0.096 26  PHE AAA CB  
21    C CG  . PHE A 26  ? 0.672 0.943 0.542 0.181  -0.034 -0.103 26  PHE AAA CG  
22    C CD1 . PHE A 26  ? 0.652 0.917 0.522 0.178  -0.033 -0.100 26  PHE AAA CD1 
23    C CD2 . PHE A 26  ? 0.687 0.972 0.569 0.177  -0.038 -0.113 26  PHE AAA CD2 
24    C CE1 . PHE A 26  ? 0.651 0.923 0.532 0.171  -0.035 -0.107 26  PHE AAA CE1 
25    C CE2 . PHE A 26  ? 0.658 0.949 0.552 0.169  -0.039 -0.119 26  PHE AAA CE2 
26    C CZ  . PHE A 26  ? 0.630 0.914 0.523 0.167  -0.038 -0.116 26  PHE AAA CZ  
27    N N   . MET A 27  ? 0.660 0.905 0.485 0.213  -0.023 -0.076 27  MET AAA N   
28    C CA  . MET A 27  ? 0.661 0.896 0.476 0.220  -0.018 -0.067 27  MET AAA CA  
29    C C   . MET A 27  ? 0.636 0.866 0.457 0.211  -0.018 -0.068 27  MET AAA C   
30    O O   . MET A 27  ? 0.670 0.904 0.486 0.218  -0.018 -0.067 27  MET AAA O   
31    C CB  . MET A 27  ? 0.700 0.917 0.509 0.220  -0.013 -0.057 27  MET AAA CB  
32    C CG  . MET A 27  ? 0.744 0.963 0.545 0.230  -0.012 -0.055 27  MET AAA CG  
33    S SD  . MET A 27  ? 0.828 1.027 0.625 0.228  -0.005 -0.045 27  MET AAA SD  
34    C CE  . MET A 27  ? 0.817 1.001 0.603 0.235  0.002  -0.035 27  MET AAA CE  
35    N N   . TYR A 28  ? 0.604 0.827 0.435 0.198  -0.019 -0.069 28  TYR AAA N   
36    C CA  . TYR A 28  ? 0.588 0.804 0.425 0.190  -0.018 -0.068 28  TYR AAA CA  
37    C C   . TYR A 28  ? 0.575 0.801 0.426 0.180  -0.022 -0.077 28  TYR AAA C   
38    O O   . TYR A 28  ? 0.572 0.805 0.428 0.178  -0.025 -0.083 28  TYR AAA O   
39    C CB  . TYR A 28  ? 0.579 0.776 0.416 0.183  -0.013 -0.060 28  TYR AAA CB  
40    C CG  . TYR A 28  ? 0.580 0.765 0.405 0.190  -0.008 -0.051 28  TYR AAA CG  
41    C CD1 . TYR A 28  ? 0.592 0.773 0.410 0.196  -0.006 -0.047 28  TYR AAA CD1 
42    C CD2 . TYR A 28  ? 0.582 0.758 0.402 0.192  -0.005 -0.046 28  TYR AAA CD2 
43    C CE1 . TYR A 28  ? 0.610 0.779 0.417 0.203  0.000  -0.038 28  TYR AAA CE1 
44    C CE2 . TYR A 28  ? 0.599 0.765 0.409 0.199  0.001  -0.037 28  TYR AAA CE2 
45    C CZ  . TYR A 28  ? 0.624 0.786 0.428 0.205  0.003  -0.033 28  TYR AAA CZ  
46    O OH  . TYR A 28  ? 0.654 0.804 0.448 0.212  0.009  -0.025 28  TYR AAA OH  
47    N N   . ASP A 29  ? 0.584 0.810 0.439 0.176  -0.023 -0.079 29  ASP AAA N   
48    C CA  . ASP A 29  ? 0.563 0.795 0.433 0.166  -0.026 -0.087 29  ASP AAA CA  
49    C C   . ASP A 29  ? 0.564 0.782 0.440 0.154  -0.024 -0.082 29  ASP AAA C   
50    O O   . ASP A 29  ? 0.507 0.728 0.393 0.146  -0.025 -0.086 29  ASP AAA O   
51    C CB  . ASP A 29  ? 0.566 0.805 0.439 0.166  -0.027 -0.091 29  ASP AAA CB  
52    C CG  . ASP A 29  ? 0.604 0.860 0.473 0.178  -0.030 -0.097 29  ASP AAA CG  
53    O OD1 . ASP A 29  ? 0.623 0.894 0.499 0.178  -0.034 -0.106 29  ASP AAA OD1 
54    O OD2 . ASP A 29  ? 0.600 0.855 0.458 0.186  -0.029 -0.093 29  ASP AAA OD2 
55    N N   . LEU A 30  ? 0.555 0.757 0.424 0.154  -0.020 -0.073 30  LEU AAA N   
56    C CA  . LEU A 30  ? 0.571 0.759 0.444 0.143  -0.017 -0.068 30  LEU AAA CA  
57    C C   . LEU A 30  ? 0.581 0.754 0.445 0.146  -0.012 -0.059 30  LEU AAA C   
58    O O   . LEU A 30  ? 0.583 0.752 0.438 0.153  -0.010 -0.055 30  LEU AAA O   
59    C CB  . LEU A 30  ? 0.574 0.760 0.453 0.137  -0.017 -0.069 30  LEU AAA CB  
60    C CG  . LEU A 30  ? 0.597 0.768 0.480 0.127  -0.015 -0.064 30  LEU AAA CG  
61    C CD1 . LEU A 30  ? 0.601 0.775 0.494 0.119  -0.016 -0.067 30  LEU AAA CD1 
62    C CD2 . LEU A 30  ? 0.620 0.788 0.507 0.123  -0.014 -0.063 30  LEU AAA CD2 
63    N N   . VAL A 31  ? 0.542 0.709 0.408 0.141  -0.011 -0.057 31  VAL AAA N   
64    C CA  . VAL A 31  ? 0.562 0.713 0.421 0.141  -0.006 -0.049 31  VAL AAA CA  
65    C C   . VAL A 31  ? 0.538 0.680 0.404 0.129  -0.005 -0.047 31  VAL AAA C   
66    O O   . VAL A 31  ? 0.532 0.679 0.407 0.122  -0.008 -0.051 31  VAL AAA O   
67    C CB  . VAL A 31  ? 0.557 0.708 0.411 0.146  -0.005 -0.048 31  VAL AAA CB  
68    C CG1 . VAL A 31  ? 0.585 0.722 0.437 0.144  -0.000 -0.041 31  VAL AAA CG1 
69    C CG2 . VAL A 31  ? 0.568 0.728 0.414 0.158  -0.006 -0.048 31  VAL AAA CG2 
70    N N   . VAL A 32  ? 0.516 0.646 0.380 0.128  -0.002 -0.041 32  VAL AAA N   
71    C CA  . VAL A 32  ? 0.509 0.631 0.379 0.117  -0.000 -0.039 32  VAL AAA CA  
72    C C   . VAL A 32  ? 0.506 0.616 0.372 0.117  0.004  -0.034 32  VAL AAA C   
73    O O   . VAL A 32  ? 0.535 0.638 0.393 0.123  0.008  -0.029 32  VAL AAA O   
74    C CB  . VAL A 32  ? 0.506 0.624 0.377 0.115  0.000  -0.038 32  VAL AAA CB  
75    C CG1 . VAL A 32  ? 0.501 0.611 0.378 0.105  0.002  -0.036 32  VAL AAA CG1 
76    C CG2 . VAL A 32  ? 0.485 0.615 0.360 0.117  -0.004 -0.044 32  VAL AAA CG2 
77    N N   . ILE A 33  ? 0.504 0.612 0.375 0.110  0.004  -0.034 33  ILE AAA N   
78    C CA  . ILE A 33  ? 0.520 0.617 0.389 0.108  0.008  -0.030 33  ILE AAA CA  
79    C C   . ILE A 33  ? 0.489 0.579 0.363 0.100  0.010  -0.028 33  ILE AAA C   
80    O O   . ILE A 33  ? 0.452 0.546 0.334 0.092  0.008  -0.030 33  ILE AAA O   
81    C CB  . ILE A 33  ? 0.534 0.635 0.406 0.107  0.007  -0.032 33  ILE AAA CB  
82    C CG1 . ILE A 33  ? 0.559 0.669 0.426 0.115  0.005  -0.034 33  ILE AAA CG1 
83    C CG2 . ILE A 33  ? 0.568 0.658 0.437 0.106  0.012  -0.028 33  ILE AAA CG2 
84    C CD1 . ILE A 33  ? 0.545 0.659 0.415 0.114  0.004  -0.037 33  ILE AAA CD1 
85    N N   . GLY A 34  ? 0.467 0.547 0.337 0.101  0.014  -0.024 34  GLY AAA N   
86    C CA  . GLY A 34  ? 0.452 0.526 0.326 0.094  0.015  -0.022 34  GLY AAA CA  
87    C C   . GLY A 34  ? 0.417 0.489 0.289 0.096  0.016  -0.021 34  GLY AAA C   
88    O O   . GLY A 34  ? 0.391 0.472 0.266 0.097  0.012  -0.024 34  GLY AAA O   
89    N N   . GLY A 35  ? 0.436 0.498 0.305 0.097  0.020  -0.017 35  GLY AAA N   
90    C CA  . GLY A 35  ? 0.464 0.523 0.330 0.099  0.021  -0.015 35  GLY AAA CA  
91    C C   . GLY A 35  ? 0.483 0.537 0.355 0.091  0.022  -0.015 35  GLY AAA C   
92    O O   . GLY A 35  ? 0.482 0.527 0.351 0.092  0.026  -0.011 35  GLY AAA O   
93    N N   . GLY A 36  ? 0.465 0.524 0.345 0.083  0.019  -0.017 36  GLY AAA N   
94    C CA  . GLY A 36  ? 0.446 0.503 0.332 0.076  0.018  -0.017 36  GLY AAA CA  
95    C C   . GLY A 36  ? 0.453 0.517 0.342 0.075  0.014  -0.020 36  GLY AAA C   
96    O O   . GLY A 36  ? 0.407 0.476 0.293 0.080  0.013  -0.021 36  GLY AAA O   
97    N N   . SER A 37  ? 0.455 0.520 0.352 0.067  0.013  -0.021 37  SER AAA N   
98    C CA  . SER A 37  ? 0.461 0.532 0.363 0.065  0.010  -0.023 37  SER AAA CA  
99    C C   . SER A 37  ? 0.444 0.524 0.347 0.068  0.006  -0.027 37  SER AAA C   
100   O O   . SER A 37  ? 0.462 0.547 0.365 0.071  0.005  -0.029 37  SER AAA O   
101   C CB  . SER A 37  ? 0.441 0.510 0.350 0.058  0.010  -0.022 37  SER AAA CB  
102   O OG  . SER A 37  ? 0.453 0.513 0.359 0.056  0.013  -0.019 37  SER AAA OG  
103   N N   . GLY A 38  ? 0.421 0.507 0.328 0.066  0.005  -0.028 38  GLY AAA N   
104   C CA  . GLY A 38  ? 0.405 0.501 0.315 0.068  0.001  -0.033 38  GLY AAA CA  
105   C C   . GLY A 38  ? 0.397 0.496 0.300 0.076  0.001  -0.034 38  GLY AAA C   
106   O O   . GLY A 38  ? 0.415 0.522 0.319 0.079  -0.001 -0.038 38  GLY AAA O   
107   N N   . GLY A 39  ? 0.406 0.500 0.301 0.081  0.004  -0.032 39  GLY AAA N   
108   C CA  . GLY A 39  ? 0.423 0.520 0.311 0.090  0.004  -0.032 39  GLY AAA CA  
109   C C   . GLY A 39  ? 0.441 0.538 0.324 0.096  0.004  -0.032 39  GLY AAA C   
110   O O   . GLY A 39  ? 0.433 0.540 0.315 0.101  0.002  -0.035 39  GLY AAA O   
111   N N   . MET A 40  ? 0.455 0.543 0.335 0.095  0.007  -0.028 40  MET AAA N   
112   C CA  . MET A 40  ? 0.477 0.565 0.352 0.101  0.009  -0.027 40  MET AAA CA  
113   C C   . MET A 40  ? 0.462 0.559 0.343 0.099  0.005  -0.032 40  MET AAA C   
114   O O   . MET A 40  ? 0.472 0.575 0.348 0.106  0.003  -0.034 40  MET AAA O   
115   C CB  . MET A 40  ? 0.512 0.587 0.384 0.099  0.013  -0.021 40  MET AAA CB  
116   C CG  . MET A 40  ? 0.546 0.612 0.410 0.103  0.018  -0.017 40  MET AAA CG  
117   S SD  . MET A 40  ? 0.627 0.680 0.487 0.104  0.024  -0.011 40  MET AAA SD  
118   C CE  . MET A 40  ? 0.614 0.664 0.483 0.092  0.022  -0.013 40  MET AAA CE  
119   N N   . ALA A 41  ? 0.434 0.533 0.324 0.091  0.003  -0.034 41  ALA AAA N   
120   C CA  . ALA A 41  ? 0.419 0.526 0.316 0.088  -0.001 -0.039 41  ALA AAA CA  
121   C C   . ALA A 41  ? 0.418 0.538 0.317 0.093  -0.004 -0.045 41  ALA AAA C   
122   O O   . ALA A 41  ? 0.398 0.525 0.297 0.097  -0.006 -0.049 41  ALA AAA O   
123   C CB  . ALA A 41  ? 0.399 0.504 0.306 0.079  -0.001 -0.039 41  ALA AAA CB  
124   N N   . ALA A 42  ? 0.412 0.534 0.313 0.091  -0.005 -0.046 42  ALA AAA N   
125   C CA  . ALA A 42  ? 0.422 0.557 0.325 0.095  -0.008 -0.052 42  ALA AAA CA  
126   C C   . ALA A 42  ? 0.448 0.588 0.342 0.106  -0.008 -0.052 42  ALA AAA C   
127   O O   . ALA A 42  ? 0.414 0.565 0.310 0.109  -0.011 -0.058 42  ALA AAA O   
128   C CB  . ALA A 42  ? 0.415 0.550 0.320 0.092  -0.008 -0.052 42  ALA AAA CB  
129   N N   . ALA A 43  ? 0.482 0.613 0.366 0.110  -0.005 -0.046 43  ALA AAA N   
130   C CA  . ALA A 43  ? 0.509 0.642 0.382 0.121  -0.004 -0.045 43  ALA AAA CA  
131   C C   . ALA A 43  ? 0.547 0.685 0.418 0.126  -0.004 -0.046 43  ALA AAA C   
132   O O   . ALA A 43  ? 0.591 0.740 0.459 0.134  -0.007 -0.050 43  ALA AAA O   
133   C CB  . ALA A 43  ? 0.523 0.643 0.388 0.123  0.001  -0.037 43  ALA AAA CB  
134   N N   . LYS A 44  ? 0.532 0.661 0.402 0.123  -0.002 -0.043 44  LYS AAA N   
135   C CA  . LYS A 44  ? 0.545 0.677 0.413 0.127  -0.003 -0.044 44  LYS AAA CA  
136   C C   . LYS A 44  ? 0.523 0.670 0.401 0.125  -0.007 -0.053 44  LYS AAA C   
137   O O   . LYS A 44  ? 0.530 0.685 0.404 0.132  -0.009 -0.056 44  LYS AAA O   
138   C CB  . LYS A 44  ? 0.577 0.698 0.447 0.121  0.000  -0.040 44  LYS AAA CB  
139   C CG  . LYS A 44  ? 0.633 0.741 0.493 0.124  0.006  -0.032 44  LYS AAA CG  
140   C CD  . LYS A 44  ? 0.676 0.774 0.538 0.119  0.008  -0.028 44  LYS AAA CD  
141   C CE  . LYS A 44  ? 0.691 0.778 0.558 0.110  0.010  -0.025 44  LYS AAA CE  
142   N NZ  . LYS A 44  ? 0.696 0.772 0.560 0.108  0.014  -0.021 44  LYS AAA NZ  
143   N N   . GLU A 45  ? 0.505 0.654 0.394 0.116  -0.009 -0.056 45  GLU AAA N   
144   C CA  . GLU A 45  ? 0.496 0.658 0.395 0.114  -0.013 -0.065 45  GLU AAA CA  
145   C C   . GLU A 45  ? 0.520 0.695 0.418 0.120  -0.016 -0.071 45  GLU AAA C   
146   O O   . GLU A 45  ? 0.542 0.730 0.443 0.124  -0.019 -0.078 45  GLU AAA O   
147   C CB  . GLU A 45  ? 0.479 0.638 0.390 0.103  -0.014 -0.066 45  GLU AAA CB  
148   C CG  . GLU A 45  ? 0.489 0.659 0.412 0.100  -0.017 -0.074 45  GLU AAA CG  
149   C CD  . GLU A 45  ? 0.484 0.651 0.409 0.098  -0.016 -0.074 45  GLU AAA CD  
150   O OE1 . GLU A 45  ? 0.502 0.660 0.418 0.100  -0.014 -0.068 45  GLU AAA OE1 
151   O OE2 . GLU A 45  ? 0.452 0.626 0.387 0.094  -0.018 -0.080 45  GLU AAA OE2 
152   N N   . ALA A 46  ? 0.511 0.685 0.405 0.122  -0.016 -0.069 46  ALA AAA N   
153   C CA  . ALA A 46  ? 0.561 0.748 0.453 0.129  -0.018 -0.074 46  ALA AAA CA  
154   C C   . ALA A 46  ? 0.618 0.811 0.500 0.141  -0.018 -0.074 46  ALA AAA C   
155   O O   . ALA A 46  ? 0.662 0.870 0.546 0.145  -0.022 -0.082 46  ALA AAA O   
156   C CB  . ALA A 46  ? 0.573 0.756 0.462 0.130  -0.017 -0.071 46  ALA AAA CB  
157   N N   . ALA A 47  ? 0.647 0.829 0.518 0.145  -0.014 -0.066 47  ALA AAA N   
158   C CA  . ALA A 47  ? 0.675 0.859 0.534 0.157  -0.013 -0.063 47  ALA AAA CA  
159   C C   . ALA A 47  ? 0.675 0.869 0.538 0.158  -0.015 -0.068 47  ALA AAA C   
160   O O   . ALA A 47  ? 0.674 0.879 0.530 0.169  -0.016 -0.071 47  ALA AAA O   
161   C CB  . ALA A 47  ? 0.715 0.883 0.565 0.158  -0.008 -0.053 47  ALA AAA CB  
162   N N   . LYS A 48  ? 0.691 0.881 0.563 0.149  -0.016 -0.070 48  LYS AAA N   
163   C CA  . LYS A 48  ? 0.720 0.919 0.597 0.149  -0.018 -0.076 48  LYS AAA CA  
164   C C   . LYS A 48  ? 0.700 0.919 0.583 0.153  -0.023 -0.087 48  LYS AAA C   
165   O O   . LYS A 48  ? 0.694 0.923 0.576 0.158  -0.024 -0.091 48  LYS AAA O   
166   C CB  . LYS A 48  ? 0.753 0.946 0.642 0.137  -0.018 -0.078 48  LYS AAA CB  
167   C CG  . LYS A 48  ? 0.815 0.996 0.702 0.134  -0.015 -0.072 48  LYS AAA CG  
168   C CD  . LYS A 48  ? 0.865 1.046 0.765 0.124  -0.017 -0.076 48  LYS AAA CD  
169   C CE  . LYS A 48  ? 0.906 1.104 0.814 0.126  -0.020 -0.086 48  LYS AAA CE  
170   N NZ  . LYS A 48  ? 0.912 1.106 0.826 0.121  -0.020 -0.087 48  LYS AAA NZ  
171   N N   . TYR A 49  ? 0.661 0.886 0.548 0.152  -0.025 -0.091 49  TYR AAA N   
172   C CA  . TYR A 49  ? 0.666 0.911 0.561 0.154  -0.029 -0.102 49  TYR AAA CA  
173   C C   . TYR A 49  ? 0.666 0.920 0.550 0.166  -0.030 -0.103 49  TYR AAA C   
174   O O   . TYR A 49  ? 0.649 0.919 0.539 0.169  -0.033 -0.112 49  TYR AAA O   
175   C CB  . TYR A 49  ? 0.635 0.880 0.544 0.144  -0.030 -0.107 49  TYR AAA CB  
176   C CG  . TYR A 49  ? 0.627 0.864 0.547 0.133  -0.029 -0.107 49  TYR AAA CG  
177   C CD1 . TYR A 49  ? 0.634 0.878 0.560 0.132  -0.031 -0.112 49  TYR AAA CD1 
178   C CD2 . TYR A 49  ? 0.642 0.865 0.565 0.124  -0.027 -0.100 49  TYR AAA CD2 
179   C CE1 . TYR A 49  ? 0.640 0.876 0.576 0.122  -0.030 -0.112 49  TYR AAA CE1 
180   C CE2 . TYR A 49  ? 0.627 0.842 0.558 0.115  -0.026 -0.100 49  TYR AAA CE2 
181   C CZ  . TYR A 49  ? 0.632 0.854 0.570 0.114  -0.027 -0.105 49  TYR AAA CZ  
182   O OH  . TYR A 49  ? 0.628 0.843 0.576 0.105  -0.026 -0.105 49  TYR AAA OH  
183   N N   . GLY A 50  ? 0.658 0.905 0.528 0.174  -0.027 -0.094 50  GLY AAA N   
184   C CA  . GLY A 50  ? 0.672 0.928 0.530 0.187  -0.027 -0.093 50  GLY AAA CA  
185   C C   . GLY A 50  ? 0.640 0.891 0.495 0.188  -0.027 -0.091 50  GLY AAA C   
186   O O   . GLY A 50  ? 0.660 0.921 0.508 0.198  -0.027 -0.092 50  GLY AAA O   
187   N N   . LYS A 51  ? 0.613 0.852 0.474 0.177  -0.025 -0.087 51  LYS AAA N   
188   C CA  . LYS A 51  ? 0.623 0.859 0.484 0.176  -0.025 -0.086 51  LYS AAA CA  
189   C C   . LYS A 51  ? 0.607 0.828 0.455 0.182  -0.020 -0.075 51  LYS AAA C   
190   O O   . LYS A 51  ? 0.577 0.786 0.420 0.181  -0.016 -0.068 51  LYS AAA O   
191   C CB  . LYS A 51  ? 0.626 0.856 0.500 0.163  -0.025 -0.088 51  LYS AAA CB  
192   C CG  . LYS A 51  ? 0.622 0.866 0.510 0.158  -0.029 -0.098 51  LYS AAA CG  
193   C CD  . LYS A 51  ? 0.630 0.894 0.519 0.166  -0.033 -0.108 51  LYS AAA CD  
194   C CE  . LYS A 51  ? 0.628 0.903 0.532 0.159  -0.036 -0.118 51  LYS AAA CE  
195   N NZ  . LYS A 51  ? 0.648 0.942 0.554 0.166  -0.040 -0.128 51  LYS AAA NZ  
196   N N   . LYS A 52  ? 0.601 0.825 0.444 0.187  -0.020 -0.074 52  LYS AAA N   
197   C CA  . LYS A 52  ? 0.630 0.841 0.462 0.192  -0.015 -0.064 52  LYS AAA CA  
198   C C   . LYS A 52  ? 0.565 0.761 0.402 0.181  -0.013 -0.060 52  LYS AAA C   
199   O O   . LYS A 52  ? 0.509 0.710 0.355 0.175  -0.016 -0.065 52  LYS AAA O   
200   C CB  . LYS A 52  ? 0.708 0.928 0.532 0.203  -0.016 -0.065 52  LYS AAA CB  
201   C CG  . LYS A 52  ? 0.784 0.993 0.594 0.213  -0.011 -0.055 52  LYS AAA CG  
202   C CD  . LYS A 52  ? 0.833 1.048 0.638 0.221  -0.010 -0.054 52  LYS AAA CD  
203   C CE  . LYS A 52  ? 0.878 1.077 0.671 0.227  -0.004 -0.043 52  LYS AAA CE  
204   N NZ  . LYS A 52  ? 0.902 1.103 0.690 0.234  -0.003 -0.041 52  LYS AAA NZ  
205   N N   . VAL A 53  ? 0.519 0.698 0.352 0.178  -0.008 -0.052 53  VAL AAA N   
206   C CA  . VAL A 53  ? 0.520 0.686 0.360 0.167  -0.006 -0.048 53  VAL AAA CA  
207   C C   . VAL A 53  ? 0.504 0.655 0.335 0.170  -0.000 -0.039 53  VAL AAA C   
208   O O   . VAL A 53  ? 0.495 0.642 0.317 0.177  0.003  -0.034 53  VAL AAA O   
209   C CB  . VAL A 53  ? 0.516 0.677 0.362 0.158  -0.006 -0.049 53  VAL AAA CB  
210   C CG1 . VAL A 53  ? 0.516 0.666 0.370 0.147  -0.005 -0.046 53  VAL AAA CG1 
211   C CG2 . VAL A 53  ? 0.527 0.702 0.381 0.157  -0.011 -0.057 53  VAL AAA CG2 
212   N N   . ALA A 54  ? 0.482 0.627 0.316 0.165  0.001  -0.038 54  ALA AAA N   
213   C CA  . ALA A 54  ? 0.505 0.634 0.333 0.165  0.006  -0.030 54  ALA AAA CA  
214   C C   . ALA A 54  ? 0.513 0.632 0.349 0.153  0.007  -0.029 54  ALA AAA C   
215   O O   . ALA A 54  ? 0.510 0.636 0.355 0.146  0.003  -0.034 54  ALA AAA O   
216   C CB  . ALA A 54  ? 0.511 0.641 0.335 0.171  0.007  -0.029 54  ALA AAA CB  
217   N N   . LEU A 55  ? 0.518 0.623 0.352 0.151  0.012  -0.023 55  LEU AAA N   
218   C CA  . LEU A 55  ? 0.503 0.599 0.344 0.140  0.014  -0.022 55  LEU AAA CA  
219   C C   . LEU A 55  ? 0.513 0.596 0.350 0.141  0.019  -0.016 55  LEU AAA C   
220   O O   . LEU A 55  ? 0.540 0.616 0.369 0.148  0.024  -0.011 55  LEU AAA O   
221   C CB  . LEU A 55  ? 0.496 0.588 0.340 0.135  0.014  -0.021 55  LEU AAA CB  
222   C CG  . LEU A 55  ? 0.499 0.583 0.350 0.124  0.015  -0.020 55  LEU AAA CG  
223   C CD1 . LEU A 55  ? 0.495 0.582 0.352 0.118  0.012  -0.023 55  LEU AAA CD1 
224   C CD2 . LEU A 55  ? 0.508 0.578 0.356 0.123  0.021  -0.014 55  LEU AAA CD2 
225   N N   . PHE A 56  ? 0.518 0.599 0.360 0.134  0.019  -0.018 56  PHE AAA N   
226   C CA  . PHE A 56  ? 0.540 0.610 0.382 0.132  0.024  -0.014 56  PHE AAA CA  
227   C C   . PHE A 56  ? 0.509 0.571 0.357 0.123  0.025  -0.013 56  PHE AAA C   
228   O O   . PHE A 56  ? 0.506 0.573 0.361 0.115  0.022  -0.016 56  PHE AAA O   
229   C CB  . PHE A 56  ? 0.535 0.610 0.379 0.132  0.022  -0.016 56  PHE AAA CB  
230   C CG  . PHE A 56  ? 0.566 0.648 0.403 0.143  0.021  -0.017 56  PHE AAA CG  
231   C CD1 . PHE A 56  ? 0.599 0.674 0.428 0.151  0.026  -0.012 56  PHE AAA CD1 
232   C CD2 . PHE A 56  ? 0.575 0.671 0.414 0.145  0.015  -0.022 56  PHE AAA CD2 
233   C CE1 . PHE A 56  ? 0.599 0.681 0.422 0.161  0.025  -0.012 56  PHE AAA CE1 
234   C CE2 . PHE A 56  ? 0.611 0.714 0.443 0.155  0.014  -0.023 56  PHE AAA CE2 
235   C CZ  . PHE A 56  ? 0.606 0.703 0.430 0.163  0.019  -0.018 56  PHE AAA CZ  
236   N N   . ASP A 57  ? 0.511 0.561 0.356 0.123  0.031  -0.008 57  ASP AAA N   
237   C CA  . ASP A 57  ? 0.506 0.547 0.357 0.114  0.034  -0.007 57  ASP AAA CA  
238   C C   . ASP A 57  ? 0.515 0.545 0.364 0.116  0.041  -0.004 57  ASP AAA C   
239   O O   . ASP A 57  ? 0.525 0.549 0.367 0.124  0.045  0.000  57  ASP AAA O   
240   C CB  . ASP A 57  ? 0.496 0.534 0.348 0.111  0.035  -0.006 57  ASP AAA CB  
241   C CG  . ASP A 57  ? 0.481 0.514 0.340 0.102  0.036  -0.007 57  ASP AAA CG  
242   O OD1 . ASP A 57  ? 0.470 0.509 0.335 0.095  0.031  -0.010 57  ASP AAA OD1 
243   O OD2 . ASP A 57  ? 0.458 0.480 0.317 0.100  0.041  -0.004 57  ASP AAA OD2 
244   N N   . PHE A 58  ? 0.511 0.538 0.365 0.110  0.041  -0.005 58  PHE AAA N   
245   C CA  . PHE A 58  ? 0.528 0.544 0.382 0.110  0.048  -0.003 58  PHE AAA CA  
246   C C   . PHE A 58  ? 0.518 0.532 0.380 0.100  0.048  -0.005 58  PHE AAA C   
247   O O   . PHE A 58  ? 0.507 0.529 0.374 0.094  0.043  -0.009 58  PHE AAA O   
248   C CB  . PHE A 58  ? 0.528 0.543 0.379 0.116  0.050  -0.002 58  PHE AAA CB  
249   C CG  . PHE A 58  ? 0.539 0.543 0.391 0.116  0.057  -0.000 58  PHE AAA CG  
250   C CD1 . PHE A 58  ? 0.550 0.553 0.409 0.108  0.057  -0.003 58  PHE AAA CD1 
251   C CD2 . PHE A 58  ? 0.564 0.558 0.411 0.123  0.064  0.005  58  PHE AAA CD2 
252   C CE1 . PHE A 58  ? 0.566 0.559 0.427 0.108  0.064  -0.002 58  PHE AAA CE1 
253   C CE2 . PHE A 58  ? 0.562 0.545 0.411 0.123  0.071  0.007  58  PHE AAA CE2 
254   C CZ  . PHE A 58  ? 0.595 0.577 0.451 0.115  0.071  0.003  58  PHE AAA CZ  
255   N N   . VAL A 59  ? 0.528 0.532 0.392 0.097  0.054  -0.003 59  VAL AAA N   
256   C CA  . VAL A 59  ? 0.543 0.545 0.415 0.088  0.054  -0.006 59  VAL AAA CA  
257   C C   . VAL A 59  ? 0.540 0.539 0.416 0.086  0.058  -0.007 59  VAL AAA C   
258   O O   . VAL A 59  ? 0.534 0.523 0.409 0.089  0.065  -0.005 59  VAL AAA O   
259   C CB  . VAL A 59  ? 0.536 0.531 0.410 0.085  0.058  -0.004 59  VAL AAA CB  
260   C CG1 . VAL A 59  ? 0.530 0.525 0.411 0.076  0.058  -0.007 59  VAL AAA CG1 
261   C CG2 . VAL A 59  ? 0.545 0.544 0.415 0.087  0.054  -0.003 59  VAL AAA CG2 
262   N N   . LYS A 60  ? 0.553 0.560 0.433 0.082  0.054  -0.011 60  LYS AAA N   
263   C CA  . LYS A 60  ? 0.562 0.566 0.446 0.079  0.057  -0.014 60  LYS AAA CA  
264   C C   . LYS A 60  ? 0.585 0.585 0.476 0.072  0.060  -0.015 60  LYS AAA C   
265   O O   . LYS A 60  ? 0.598 0.603 0.492 0.067  0.056  -0.016 60  LYS AAA O   
266   C CB  . LYS A 60  ? 0.555 0.571 0.443 0.076  0.051  -0.017 60  LYS AAA CB  
267   C CG  . LYS A 60  ? 0.567 0.587 0.449 0.083  0.049  -0.016 60  LYS AAA CG  
268   C CD  . LYS A 60  ? 0.547 0.578 0.431 0.081  0.044  -0.020 60  LYS AAA CD  
269   C CE  . LYS A 60  ? 0.531 0.571 0.419 0.075  0.038  -0.022 60  LYS AAA CE  
270   N NZ  . LYS A 60  ? 0.522 0.565 0.405 0.080  0.035  -0.020 60  LYS AAA NZ  
271   N N   . PRO A 61  ? 0.607 0.598 0.500 0.072  0.067  -0.015 61  PRO AAA N   
272   C CA  . PRO A 61  ? 0.593 0.580 0.493 0.066  0.070  -0.017 61  PRO AAA CA  
273   C C   . PRO A 61  ? 0.578 0.575 0.484 0.058  0.065  -0.022 61  PRO AAA C   
274   O O   . PRO A 61  ? 0.528 0.533 0.436 0.057  0.062  -0.024 61  PRO AAA O   
275   C CB  . PRO A 61  ? 0.606 0.582 0.508 0.067  0.078  -0.017 61  PRO AAA CB  
276   C CG  . PRO A 61  ? 0.632 0.604 0.526 0.076  0.080  -0.013 61  PRO AAA CG  
277   C CD  . PRO A 61  ? 0.621 0.604 0.511 0.078  0.072  -0.014 61  PRO AAA CD  
278   N N   . SER A 62  ? 0.572 0.570 0.483 0.052  0.065  -0.024 62  SER AAA N   
279   C CA  . SER A 62  ? 0.570 0.577 0.487 0.045  0.061  -0.028 62  SER AAA CA  
280   C C   . SER A 62  ? 0.558 0.567 0.481 0.043  0.064  -0.032 62  SER AAA C   
281   O O   . SER A 62  ? 0.594 0.594 0.516 0.046  0.070  -0.032 62  SER AAA O   
282   C CB  . SER A 62  ? 0.555 0.562 0.476 0.040  0.062  -0.028 62  SER AAA CB  
283   O OG  . SER A 62  ? 0.530 0.528 0.455 0.039  0.069  -0.030 62  SER AAA OG  
284   N N   . THR A 63  ? 0.534 0.552 0.462 0.037  0.061  -0.036 63  THR AAA N   
285   C CA  . THR A 63  ? 0.554 0.575 0.488 0.034  0.063  -0.042 63  THR AAA CA  
286   C C   . THR A 63  ? 0.543 0.554 0.482 0.033  0.071  -0.044 63  THR AAA C   
287   O O   . THR A 63  ? 0.541 0.552 0.485 0.032  0.074  -0.048 63  THR AAA O   
288   C CB  . THR A 63  ? 0.539 0.573 0.477 0.029  0.058  -0.045 63  THR AAA CB  
289   O OG1 . THR A 63  ? 0.476 0.512 0.416 0.025  0.057  -0.045 63  THR AAA OG1 
290   C CG2 . THR A 63  ? 0.530 0.573 0.464 0.030  0.051  -0.043 63  THR AAA CG2 
291   N N   . GLN A 64  ? 0.548 0.553 0.486 0.033  0.073  -0.041 64  GLN AAA N   
292   C CA  . GLN A 64  ? 0.577 0.572 0.520 0.031  0.081  -0.044 64  GLN AAA CA  
293   C C   . GLN A 64  ? 0.603 0.584 0.542 0.037  0.087  -0.038 64  GLN AAA C   
294   O O   . GLN A 64  ? 0.636 0.608 0.578 0.036  0.093  -0.039 64  GLN AAA O   
295   C CB  . GLN A 64  ? 0.559 0.559 0.507 0.026  0.079  -0.046 64  GLN AAA CB  
296   C CG  . GLN A 64  ? 0.533 0.545 0.487 0.020  0.075  -0.052 64  GLN AAA CG  
297   C CD  . GLN A 64  ? 0.550 0.564 0.512 0.018  0.080  -0.058 64  GLN AAA CD  
298   O OE1 . GLN A 64  ? 0.566 0.569 0.531 0.019  0.087  -0.060 64  GLN AAA OE1 
299   N NE2 . GLN A 64  ? 0.541 0.566 0.505 0.015  0.076  -0.062 64  GLN AAA NE2 
300   N N   . GLY A 65  ? 0.595 0.574 0.526 0.043  0.085  -0.034 65  GLY AAA N   
301   C CA  . GLY A 65  ? 0.584 0.551 0.509 0.050  0.091  -0.028 65  GLY AAA CA  
302   C C   . GLY A 65  ? 0.573 0.536 0.493 0.052  0.090  -0.023 65  GLY AAA C   
303   O O   . GLY A 65  ? 0.591 0.543 0.506 0.058  0.095  -0.019 65  GLY AAA O   
304   N N   . THR A 66  ? 0.539 0.510 0.459 0.049  0.084  -0.024 66  THR AAA N   
305   C CA  . THR A 66  ? 0.518 0.486 0.432 0.050  0.083  -0.020 66  THR AAA CA  
306   C C   . THR A 66  ? 0.518 0.488 0.424 0.057  0.079  -0.016 66  THR AAA C   
307   O O   . THR A 66  ? 0.508 0.488 0.414 0.057  0.073  -0.017 66  THR AAA O   
308   C CB  . THR A 66  ? 0.498 0.473 0.416 0.044  0.078  -0.022 66  THR AAA CB  
309   O OG1 . THR A 66  ? 0.450 0.426 0.377 0.038  0.081  -0.027 66  THR AAA OG1 
310   C CG2 . THR A 66  ? 0.513 0.484 0.428 0.046  0.079  -0.018 66  THR AAA CG2 
311   N N   . LYS A 67  ? 0.559 0.523 0.459 0.063  0.082  -0.011 67  LYS AAA N   
312   C CA  . LYS A 67  ? 0.581 0.547 0.472 0.070  0.078  -0.007 67  LYS AAA CA  
313   C C   . LYS A 67  ? 0.547 0.509 0.434 0.072  0.079  -0.003 67  LYS AAA C   
314   O O   . LYS A 67  ? 0.555 0.511 0.446 0.068  0.083  -0.003 67  LYS AAA O   
315   C CB  . LYS A 67  ? 0.634 0.595 0.521 0.077  0.082  -0.004 67  LYS AAA CB  
316   C CG  . LYS A 67  ? 0.700 0.647 0.584 0.082  0.091  -0.000 67  LYS AAA CG  
317   C CD  . LYS A 67  ? 0.753 0.697 0.634 0.089  0.095  0.002  67  LYS AAA CD  
318   C CE  . LYS A 67  ? 0.788 0.719 0.667 0.095  0.104  0.007  67  LYS AAA CE  
319   N NZ  . LYS A 67  ? 0.827 0.756 0.698 0.105  0.105  0.011  67  LYS AAA NZ  
320   N N   . TRP A 68  ? 0.527 0.494 0.408 0.077  0.074  -0.001 68  TRP AAA N   
321   C CA  . TRP A 68  ? 0.503 0.470 0.381 0.078  0.073  0.002  68  TRP AAA CA  
322   C C   . TRP A 68  ? 0.534 0.505 0.403 0.087  0.070  0.004  68  TRP AAA C   
323   O O   . TRP A 68  ? 0.559 0.534 0.426 0.091  0.069  0.004  68  TRP AAA O   
324   C CB  . TRP A 68  ? 0.463 0.438 0.346 0.071  0.067  -0.002 68  TRP AAA CB  
325   C CG  . TRP A 68  ? 0.432 0.418 0.317 0.068  0.060  -0.005 68  TRP AAA CG  
326   C CD1 . TRP A 68  ? 0.415 0.409 0.297 0.070  0.054  -0.005 68  TRP AAA CD1 
327   C CD2 . TRP A 68  ? 0.414 0.404 0.305 0.061  0.059  -0.009 68  TRP AAA CD2 
328   N NE1 . TRP A 68  ? 0.387 0.390 0.274 0.066  0.050  -0.008 68  TRP AAA NE1 
329   C CE2 . TRP A 68  ? 0.390 0.391 0.282 0.061  0.052  -0.010 68  TRP AAA CE2 
330   C CE3 . TRP A 68  ? 0.403 0.390 0.301 0.056  0.063  -0.011 68  TRP AAA CE3 
331   C CZ2 . TRP A 68  ? 0.393 0.401 0.291 0.056  0.049  -0.014 68  TRP AAA CZ2 
332   C CZ3 . TRP A 68  ? 0.396 0.390 0.299 0.052  0.060  -0.015 68  TRP AAA CZ3 
333   C CH2 . TRP A 68  ? 0.385 0.389 0.287 0.051  0.053  -0.016 68  TRP AAA CH2 
334   N N   . GLY A 69  ? 0.519 0.491 0.385 0.089  0.069  0.007  69  GLY AAA N   
335   C CA  . GLY A 69  ? 0.532 0.508 0.390 0.098  0.067  0.009  69  GLY AAA CA  
336   C C   . GLY A 69  ? 0.528 0.517 0.387 0.096  0.058  0.006  69  GLY AAA C   
337   O O   . GLY A 69  ? 0.533 0.527 0.398 0.089  0.054  0.002  69  GLY AAA O   
338   N N   . LEU A 70  ? 0.560 0.554 0.413 0.102  0.056  0.007  70  LEU AAA N   
339   C CA  . LEU A 70  ? 0.566 0.572 0.419 0.103  0.048  0.003  70  LEU AAA CA  
340   C C   . LEU A 70  ? 0.552 0.562 0.411 0.095  0.045  0.001  70  LEU AAA C   
341   O O   . LEU A 70  ? 0.597 0.601 0.458 0.092  0.048  0.002  70  LEU AAA O   
342   C CB  . LEU A 70  ? 0.578 0.588 0.423 0.112  0.048  0.006  70  LEU AAA CB  
343   C CG  . LEU A 70  ? 0.584 0.607 0.430 0.113  0.041  0.002  70  LEU AAA CG  
344   C CD1 . LEU A 70  ? 0.569 0.601 0.417 0.113  0.037  -0.002 70  LEU AAA CD1 
345   C CD2 . LEU A 70  ? 0.585 0.611 0.423 0.123  0.042  0.004  70  LEU AAA CD2 
346   N N   . GLY A 71  ? 0.541 0.562 0.406 0.091  0.038  -0.003 71  GLY AAA N   
347   C CA  . GLY A 71  ? 0.523 0.549 0.394 0.085  0.034  -0.006 71  GLY AAA CA  
348   C C   . GLY A 71  ? 0.492 0.522 0.370 0.077  0.031  -0.008 71  GLY AAA C   
349   O O   . GLY A 71  ? 0.495 0.530 0.378 0.072  0.027  -0.011 71  GLY AAA O   
350   N N   . GLY A 72  ? 0.480 0.506 0.358 0.076  0.033  -0.008 72  GLY AAA N   
351   C CA  . GLY A 72  ? 0.469 0.501 0.354 0.070  0.031  -0.011 72  GLY AAA CA  
352   C C   . GLY A 72  ? 0.455 0.485 0.346 0.062  0.031  -0.011 72  GLY AAA C   
353   O O   . GLY A 72  ? 0.430 0.452 0.320 0.062  0.035  -0.009 72  GLY AAA O   
354   N N   . THR A 73  ? 0.449 0.485 0.346 0.056  0.028  -0.013 73  THR AAA N   
355   C CA  . THR A 73  ? 0.441 0.476 0.343 0.050  0.029  -0.014 73  THR AAA CA  
356   C C   . THR A 73  ? 0.423 0.455 0.326 0.047  0.029  -0.013 73  THR AAA C   
357   O O   . THR A 73  ? 0.395 0.421 0.300 0.044  0.032  -0.012 73  THR AAA O   
358   C CB  . THR A 73  ? 0.428 0.471 0.335 0.045  0.025  -0.016 73  THR AAA CB  
359   O OG1 . THR A 73  ? 0.419 0.465 0.325 0.048  0.025  -0.017 73  THR AAA OG1 
360   C CG2 . THR A 73  ? 0.415 0.459 0.328 0.039  0.026  -0.016 73  THR AAA CG2 
361   N N   . CYS A 74  ? 0.414 0.451 0.318 0.048  0.026  -0.013 74  CYS AAA N   
362   C CA  . CYS A 74  ? 0.444 0.479 0.350 0.045  0.025  -0.012 74  CYS AAA CA  
363   C C   . CYS A 74  ? 0.446 0.473 0.349 0.048  0.030  -0.010 74  CYS AAA C   
364   O O   . CYS A 74  ? 0.415 0.438 0.321 0.044  0.032  -0.010 74  CYS AAA O   
365   C CB  . CYS A 74  ? 0.473 0.515 0.382 0.046  0.021  -0.014 74  CYS AAA CB  
366   S SG  . CYS A 74  ? 0.567 0.608 0.481 0.041  0.021  -0.013 74  CYS AAA SG  
367   N N   . VAL A 75  ? 0.429 0.452 0.325 0.054  0.032  -0.009 75  VAL AAA N   
368   C CA  . VAL A 75  ? 0.426 0.440 0.317 0.058  0.037  -0.007 75  VAL AAA CA  
369   C C   . VAL A 75  ? 0.406 0.412 0.298 0.056  0.042  -0.006 75  VAL AAA C   
370   O O   . VAL A 75  ? 0.388 0.387 0.280 0.054  0.045  -0.005 75  VAL AAA O   
371   C CB  . VAL A 75  ? 0.434 0.448 0.318 0.066  0.037  -0.005 75  VAL AAA CB  
372   C CG1 . VAL A 75  ? 0.451 0.455 0.329 0.071  0.043  -0.002 75  VAL AAA CG1 
373   C CG2 . VAL A 75  ? 0.434 0.456 0.317 0.069  0.033  -0.007 75  VAL AAA CG2 
374   N N   . ASN A 76  ? 0.394 0.401 0.287 0.055  0.043  -0.007 76  ASN AAA N   
375   C CA  . ASN A 76  ? 0.398 0.396 0.290 0.055  0.048  -0.006 76  ASN AAA CA  
376   C C   . ASN A 76  ? 0.399 0.399 0.299 0.048  0.048  -0.009 76  ASN AAA C   
377   O O   . ASN A 76  ? 0.411 0.405 0.313 0.046  0.053  -0.009 76  ASN AAA O   
378   C CB  . ASN A 76  ? 0.393 0.391 0.282 0.061  0.050  -0.006 76  ASN AAA CB  
379   C CG  . ASN A 76  ? 0.401 0.395 0.282 0.069  0.051  -0.003 76  ASN AAA CG  
380   O OD1 . ASN A 76  ? 0.393 0.379 0.271 0.072  0.057  0.000  76  ASN AAA OD1 
381   N ND2 . ASN A 76  ? 0.396 0.399 0.275 0.072  0.046  -0.003 76  ASN AAA ND2 
382   N N   . VAL A 77  ? 0.392 0.401 0.296 0.044  0.044  -0.011 77  VAL AAA N   
383   C CA  . VAL A 77  ? 0.381 0.393 0.291 0.038  0.044  -0.014 77  VAL AAA CA  
384   C C   . VAL A 77  ? 0.370 0.391 0.284 0.034  0.038  -0.015 77  VAL AAA C   
385   O O   . VAL A 77  ? 0.352 0.379 0.270 0.030  0.037  -0.017 77  VAL AAA O   
386   C CB  . VAL A 77  ? 0.391 0.403 0.300 0.040  0.045  -0.015 77  VAL AAA CB  
387   C CG1 . VAL A 77  ? 0.404 0.406 0.311 0.042  0.052  -0.015 77  VAL AAA CG1 
388   C CG2 . VAL A 77  ? 0.401 0.419 0.308 0.043  0.041  -0.015 77  VAL AAA CG2 
389   N N   . GLY A 78  ? 0.376 0.399 0.290 0.034  0.035  -0.014 78  GLY AAA N   
390   C CA  . GLY A 78  ? 0.365 0.397 0.284 0.030  0.031  -0.014 78  GLY AAA CA  
391   C C   . GLY A 78  ? 0.380 0.409 0.299 0.029  0.030  -0.013 78  GLY AAA C   
392   O O   . GLY A 78  ? 0.384 0.409 0.305 0.027  0.033  -0.013 78  GLY AAA O   
393   N N   . CYS A 79  ? 0.374 0.408 0.294 0.030  0.027  -0.013 79  CYS AAA N   
394   C CA  . CYS A 79  ? 0.395 0.429 0.317 0.028  0.025  -0.012 79  CYS AAA CA  
395   C C   . CYS A 79  ? 0.392 0.418 0.312 0.029  0.029  -0.011 79  CYS AAA C   
396   O O   . CYS A 79  ? 0.381 0.406 0.304 0.025  0.030  -0.011 79  CYS AAA O   
397   C CB  . CYS A 79  ? 0.417 0.456 0.340 0.030  0.022  -0.012 79  CYS AAA CB  
398   S SG  . CYS A 79  ? 0.451 0.496 0.373 0.032  0.019  -0.013 79  CYS AAA SG  
399   N N   . VAL A 80  ? 0.383 0.403 0.297 0.034  0.032  -0.010 80  VAL AAA N   
400   C CA  . VAL A 80  ? 0.386 0.399 0.297 0.036  0.036  -0.009 80  VAL AAA CA  
401   C C   . VAL A 80  ? 0.372 0.380 0.285 0.032  0.040  -0.009 80  VAL AAA C   
402   O O   . VAL A 80  ? 0.360 0.366 0.276 0.029  0.040  -0.009 80  VAL AAA O   
403   C CB  . VAL A 80  ? 0.399 0.407 0.302 0.043  0.038  -0.007 80  VAL AAA CB  
404   C CG1 . VAL A 80  ? 0.390 0.390 0.291 0.045  0.043  -0.005 80  VAL AAA CG1 
405   C CG2 . VAL A 80  ? 0.402 0.417 0.304 0.047  0.034  -0.007 80  VAL AAA CG2 
406   N N   . PRO A 81  ? 0.378 0.383 0.291 0.033  0.043  -0.010 81  PRO AAA N   
407   C CA  . PRO A 81  ? 0.389 0.389 0.305 0.029  0.047  -0.011 81  PRO AAA CA  
408   C C   . PRO A 81  ? 0.393 0.400 0.316 0.023  0.044  -0.013 81  PRO AAA C   
409   O O   . PRO A 81  ? 0.424 0.429 0.350 0.020  0.047  -0.014 81  PRO AAA O   
410   C CB  . PRO A 81  ? 0.388 0.386 0.304 0.031  0.050  -0.012 81  PRO AAA CB  
411   C CG  . PRO A 81  ? 0.393 0.396 0.305 0.034  0.047  -0.011 81  PRO AAA CG  
412   C CD  . PRO A 81  ? 0.391 0.397 0.301 0.037  0.043  -0.010 81  PRO AAA CD  
413   N N   . LYS A 82  ? 0.379 0.395 0.304 0.021  0.039  -0.014 82  LYS AAA N   
414   C CA  . LYS A 82  ? 0.388 0.410 0.318 0.016  0.037  -0.015 82  LYS AAA CA  
415   C C   . LYS A 82  ? 0.372 0.394 0.304 0.015  0.036  -0.014 82  LYS AAA C   
416   O O   . LYS A 82  ? 0.363 0.385 0.299 0.011  0.037  -0.016 82  LYS AAA O   
417   C CB  . LYS A 82  ? 0.412 0.443 0.344 0.016  0.032  -0.015 82  LYS AAA CB  
418   C CG  . LYS A 82  ? 0.435 0.474 0.372 0.012  0.029  -0.015 82  LYS AAA CG  
419   C CD  . LYS A 82  ? 0.450 0.491 0.389 0.011  0.026  -0.014 82  LYS AAA CD  
420   C CE  . LYS A 82  ? 0.476 0.519 0.413 0.014  0.023  -0.012 82  LYS AAA CE  
421   N NZ  . LYS A 82  ? 0.456 0.507 0.396 0.013  0.021  -0.012 82  LYS AAA NZ  
422   N N   . LYS A 83  ? 0.360 0.380 0.289 0.018  0.034  -0.013 83  LYS AAA N   
423   C CA  . LYS A 83  ? 0.363 0.383 0.294 0.016  0.033  -0.012 83  LYS AAA CA  
424   C C   . LYS A 83  ? 0.376 0.389 0.306 0.016  0.038  -0.012 83  LYS AAA C   
425   O O   . LYS A 83  ? 0.362 0.375 0.296 0.013  0.037  -0.012 83  LYS AAA O   
426   C CB  . LYS A 83  ? 0.362 0.384 0.291 0.020  0.030  -0.010 83  LYS AAA CB  
427   C CG  . LYS A 83  ? 0.381 0.403 0.311 0.019  0.029  -0.010 83  LYS AAA CG  
428   C CD  . LYS A 83  ? 0.378 0.407 0.315 0.015  0.025  -0.010 83  LYS AAA CD  
429   C CE  . LYS A 83  ? 0.371 0.399 0.310 0.013  0.025  -0.010 83  LYS AAA CE  
430   N NZ  . LYS A 83  ? 0.352 0.384 0.294 0.014  0.021  -0.009 83  LYS AAA NZ  
431   N N   . LEU A 84  ? 0.372 0.377 0.298 0.019  0.042  -0.012 84  LEU AAA N   
432   C CA  . LEU A 84  ? 0.383 0.381 0.309 0.019  0.047  -0.012 84  LEU AAA CA  
433   C C   . LEU A 84  ? 0.394 0.393 0.325 0.014  0.049  -0.015 84  LEU AAA C   
434   O O   . LEU A 84  ? 0.396 0.393 0.330 0.012  0.051  -0.016 84  LEU AAA O   
435   C CB  . LEU A 84  ? 0.385 0.375 0.305 0.024  0.052  -0.010 84  LEU AAA CB  
436   C CG  . LEU A 84  ? 0.389 0.378 0.303 0.030  0.050  -0.007 84  LEU AAA CG  
437   C CD1 . LEU A 84  ? 0.399 0.380 0.307 0.035  0.055  -0.005 84  LEU AAA CD1 
438   C CD2 . LEU A 84  ? 0.377 0.364 0.290 0.030  0.050  -0.007 84  LEU AAA CD2 
439   N N   . MET A 85  ? 0.386 0.390 0.320 0.013  0.049  -0.017 85  MET AAA N   
440   C CA  . MET A 85  ? 0.399 0.406 0.338 0.008  0.050  -0.020 85  MET AAA CA  
441   C C   . MET A 85  ? 0.356 0.370 0.299 0.005  0.046  -0.021 85  MET AAA C   
442   O O   . MET A 85  ? 0.361 0.376 0.309 0.002  0.048  -0.023 85  MET AAA O   
443   C CB  . MET A 85  ? 0.447 0.458 0.387 0.008  0.049  -0.022 85  MET AAA CB  
444   C CG  . MET A 85  ? 0.496 0.499 0.433 0.011  0.054  -0.022 85  MET AAA CG  
445   S SD  . MET A 85  ? 0.580 0.581 0.522 0.008  0.060  -0.027 85  MET AAA SD  
446   C CE  . MET A 85  ? 0.573 0.562 0.511 0.013  0.066  -0.025 85  MET AAA CE  
447   N N   . HIS A 86  ? 0.319 0.338 0.261 0.005  0.041  -0.018 86  HIS AAA N   
448   C CA  . HIS A 86  ? 0.297 0.324 0.243 0.003  0.037  -0.018 86  HIS AAA CA  
449   C C   . HIS A 86  ? 0.299 0.321 0.246 0.002  0.039  -0.018 86  HIS AAA C   
450   O O   . HIS A 86  ? 0.292 0.318 0.243 -0.001 0.038  -0.019 86  HIS AAA O   
451   C CB  . HIS A 86  ? 0.279 0.311 0.225 0.004  0.032  -0.015 86  HIS AAA CB  
452   C CG  . HIS A 86  ? 0.264 0.302 0.214 0.002  0.029  -0.014 86  HIS AAA CG  
453   N ND1 . HIS A 86  ? 0.254 0.299 0.207 -0.001 0.028  -0.015 86  HIS AAA ND1 
454   C CD2 . HIS A 86  ? 0.258 0.296 0.208 0.003  0.027  -0.012 86  HIS AAA CD2 
455   C CE1 . HIS A 86  ? 0.239 0.287 0.195 -0.002 0.025  -0.013 86  HIS AAA CE1 
456   N NE2 . HIS A 86  ? 0.246 0.291 0.201 0.000  0.024  -0.011 86  HIS AAA NE2 
457   N N   . TYR A 87  ? 0.299 0.313 0.241 0.005  0.040  -0.016 87  TYR AAA N   
458   C CA  . TYR A 87  ? 0.319 0.328 0.261 0.005  0.042  -0.015 87  TYR AAA CA  
459   C C   . TYR A 87  ? 0.309 0.315 0.254 0.003  0.047  -0.018 87  TYR AAA C   
460   O O   . TYR A 87  ? 0.290 0.298 0.239 -0.000 0.046  -0.019 87  TYR AAA O   
461   C CB  . TYR A 87  ? 0.345 0.348 0.282 0.010  0.043  -0.013 87  TYR AAA CB  
462   C CG  . TYR A 87  ? 0.387 0.388 0.324 0.010  0.044  -0.012 87  TYR AAA CG  
463   C CD1 . TYR A 87  ? 0.414 0.419 0.354 0.008  0.040  -0.012 87  TYR AAA CD1 
464   C CD2 . TYR A 87  ? 0.431 0.423 0.365 0.011  0.049  -0.012 87  TYR AAA CD2 
465   C CE1 . TYR A 87  ? 0.451 0.453 0.390 0.008  0.040  -0.012 87  TYR AAA CE1 
466   C CE2 . TYR A 87  ? 0.426 0.415 0.360 0.011  0.049  -0.011 87  TYR AAA CE2 
467   C CZ  . TYR A 87  ? 0.464 0.459 0.401 0.010  0.045  -0.011 87  TYR AAA CZ  
468   O OH  . TYR A 87  ? 0.495 0.487 0.432 0.010  0.046  -0.011 87  TYR AAA OH  
469   N N   . SER A 88  ? 0.303 0.305 0.248 0.003  0.051  -0.020 88  SER AAA N   
470   C CA  . SER A 88  ? 0.320 0.320 0.269 0.000  0.056  -0.023 88  SER AAA CA  
471   C C   . SER A 88  ? 0.320 0.329 0.275 -0.004 0.053  -0.027 88  SER AAA C   
472   O O   . SER A 88  ? 0.325 0.334 0.283 -0.007 0.055  -0.029 88  SER AAA O   
473   C CB  . SER A 88  ? 0.334 0.329 0.282 0.001  0.060  -0.025 88  SER AAA CB  
474   O OG  . SER A 88  ? 0.332 0.324 0.285 -0.001 0.066  -0.029 88  SER AAA OG  
475   N N   . ALA A 89  ? 0.316 0.334 0.271 -0.004 0.049  -0.026 89  ALA AAA N   
476   C CA  . ALA A 89  ? 0.314 0.342 0.274 -0.008 0.046  -0.029 89  ALA AAA CA  
477   C C   . ALA A 89  ? 0.302 0.333 0.264 -0.009 0.043  -0.027 89  ALA AAA C   
478   O O   . ALA A 89  ? 0.304 0.340 0.271 -0.011 0.044  -0.030 89  ALA AAA O   
479   C CB  . ALA A 89  ? 0.309 0.345 0.269 -0.007 0.042  -0.028 89  ALA AAA CB  
480   N N   . LEU A 90  ? 0.311 0.339 0.270 -0.007 0.041  -0.023 90  LEU AAA N   
481   C CA  . LEU A 90  ? 0.322 0.353 0.283 -0.007 0.038  -0.022 90  LEU AAA CA  
482   C C   . LEU A 90  ? 0.330 0.356 0.292 -0.009 0.042  -0.024 90  LEU AAA C   
483   O O   . LEU A 90  ? 0.333 0.362 0.298 -0.011 0.041  -0.025 90  LEU AAA O   
484   C CB  . LEU A 90  ? 0.336 0.364 0.293 -0.005 0.035  -0.018 90  LEU AAA CB  
485   C CG  . LEU A 90  ? 0.352 0.387 0.310 -0.004 0.031  -0.016 90  LEU AAA CG  
486   C CD1 . LEU A 90  ? 0.352 0.384 0.307 -0.001 0.029  -0.013 90  LEU AAA CD1 
487   C CD2 . LEU A 90  ? 0.337 0.381 0.299 -0.006 0.029  -0.015 90  LEU AAA CD2 
488   N N   . ILE A 91  ? 0.337 0.354 0.296 -0.007 0.046  -0.024 91  ILE AAA N   
489   C CA  . ILE A 91  ? 0.346 0.356 0.307 -0.008 0.051  -0.026 91  ILE AAA CA  
490   C C   . ILE A 91  ? 0.347 0.362 0.313 -0.012 0.053  -0.031 91  ILE AAA C   
491   O O   . ILE A 91  ? 0.343 0.360 0.313 -0.014 0.053  -0.033 91  ILE AAA O   
492   C CB  . ILE A 91  ? 0.346 0.345 0.302 -0.006 0.056  -0.025 91  ILE AAA CB  
493   C CG1 . ILE A 91  ? 0.335 0.331 0.285 -0.002 0.054  -0.021 91  ILE AAA CG1 
494   C CG2 . ILE A 91  ? 0.348 0.341 0.306 -0.007 0.062  -0.028 91  ILE AAA CG2 
495   C CD1 . ILE A 91  ? 0.345 0.330 0.290 0.002  0.059  -0.019 91  ILE AAA CD1 
496   N N   . ALA A 92  ? 0.339 0.357 0.307 -0.013 0.054  -0.034 92  ALA AAA N   
497   C CA  . ALA A 92  ? 0.348 0.373 0.322 -0.016 0.055  -0.040 92  ALA AAA CA  
498   C C   . ALA A 92  ? 0.351 0.387 0.329 -0.018 0.051  -0.040 92  ALA AAA C   
499   O O   . ALA A 92  ? 0.334 0.373 0.316 -0.020 0.052  -0.044 92  ALA AAA O   
500   C CB  . ALA A 92  ? 0.348 0.377 0.323 -0.016 0.055  -0.042 92  ALA AAA CB  
501   N N   . SER A 93  ? 0.355 0.397 0.331 -0.016 0.045  -0.036 93  SER AAA N   
502   C CA  . SER A 93  ? 0.354 0.406 0.332 -0.017 0.041  -0.035 93  SER AAA CA  
503   C C   . SER A 93  ? 0.350 0.400 0.329 -0.018 0.041  -0.035 93  SER AAA C   
504   O O   . SER A 93  ? 0.365 0.421 0.348 -0.019 0.040  -0.037 93  SER AAA O   
505   C CB  . SER A 93  ? 0.353 0.409 0.329 -0.015 0.037  -0.030 93  SER AAA CB  
506   O OG  . SER A 93  ? 0.375 0.439 0.351 -0.015 0.035  -0.032 93  SER AAA OG  
507   N N   A SER A 94  ? 0.363 0.404 0.339 -0.016 0.041  -0.031 94  SER AAA N   
508   N N   B SER A 94  ? 0.363 0.404 0.339 -0.016 0.041  -0.031 94  SER AAA N   
509   C CA  A SER A 94  ? 0.368 0.405 0.344 -0.016 0.042  -0.030 94  SER AAA CA  
510   C CA  B SER A 94  ? 0.368 0.405 0.344 -0.016 0.042  -0.030 94  SER AAA CA  
511   C C   A SER A 94  ? 0.380 0.415 0.360 -0.019 0.046  -0.035 94  SER AAA C   
512   C C   B SER A 94  ? 0.380 0.415 0.360 -0.019 0.046  -0.035 94  SER AAA C   
513   O O   A SER A 94  ? 0.387 0.425 0.369 -0.020 0.045  -0.036 94  SER AAA O   
514   O O   B SER A 94  ? 0.387 0.425 0.369 -0.020 0.045  -0.036 94  SER AAA O   
515   C CB  A SER A 94  ? 0.369 0.396 0.340 -0.014 0.042  -0.026 94  SER AAA CB  
516   C CB  B SER A 94  ? 0.369 0.396 0.340 -0.014 0.042  -0.026 94  SER AAA CB  
517   O OG  A SER A 94  ? 0.385 0.406 0.356 -0.014 0.045  -0.027 94  SER AAA OG  
518   O OG  B SER A 94  ? 0.385 0.406 0.356 -0.014 0.045  -0.027 94  SER AAA OG  
519   N N   . ILE A 95  ? 0.397 0.427 0.376 -0.019 0.051  -0.038 95  ILE AAA N   
520   C CA  . ILE A 95  ? 0.410 0.438 0.394 -0.022 0.056  -0.043 95  ILE AAA CA  
521   C C   . ILE A 95  ? 0.412 0.452 0.402 -0.024 0.054  -0.048 95  ILE AAA C   
522   O O   . ILE A 95  ? 0.397 0.439 0.392 -0.026 0.055  -0.052 95  ILE AAA O   
523   C CB  . ILE A 95  ? 0.432 0.450 0.415 -0.021 0.062  -0.045 95  ILE AAA CB  
524   C CG1 . ILE A 95  ? 0.457 0.464 0.434 -0.018 0.064  -0.040 95  ILE AAA CG1 
525   C CG2 . ILE A 95  ? 0.436 0.453 0.425 -0.025 0.067  -0.051 95  ILE AAA CG2 
526   C CD1 . ILE A 95  ? 0.470 0.467 0.445 -0.017 0.070  -0.040 95  ILE AAA CD1 
527   N N   . HIS A 96  ? 0.414 0.461 0.404 -0.024 0.052  -0.050 96  HIS AAA N   
528   C CA  . HIS A 96  ? 0.398 0.458 0.394 -0.026 0.051  -0.055 96  HIS AAA CA  
529   C C   . HIS A 96  ? 0.372 0.441 0.369 -0.026 0.046  -0.053 96  HIS AAA C   
530   O O   . HIS A 96  ? 0.340 0.415 0.342 -0.028 0.047  -0.057 96  HIS AAA O   
531   C CB  . HIS A 96  ? 0.425 0.493 0.421 -0.026 0.049  -0.056 96  HIS AAA CB  
532   C CG  . HIS A 96  ? 0.454 0.537 0.456 -0.027 0.048  -0.061 96  HIS AAA CG  
533   N ND1 . HIS A 96  ? 0.502 0.597 0.503 -0.026 0.042  -0.059 96  HIS AAA ND1 
534   C CD2 . HIS A 96  ? 0.497 0.585 0.505 -0.030 0.051  -0.069 96  HIS AAA CD2 
535   C CE1 . HIS A 96  ? 0.515 0.622 0.521 -0.027 0.042  -0.065 96  HIS AAA CE1 
536   N NE2 . HIS A 96  ? 0.535 0.639 0.546 -0.029 0.047  -0.072 96  HIS AAA NE2 
537   N N   . HIS A 97  ? 0.348 0.417 0.341 -0.023 0.042  -0.046 97  HIS AAA N   
538   C CA  . HIS A 97  ? 0.342 0.421 0.336 -0.023 0.037  -0.043 97  HIS AAA CA  
539   C C   . HIS A 97  ? 0.317 0.391 0.312 -0.023 0.037  -0.041 97  HIS AAA C   
540   O O   . HIS A 97  ? 0.304 0.386 0.301 -0.023 0.035  -0.041 97  HIS AAA O   
541   C CB  . HIS A 97  ? 0.325 0.406 0.316 -0.020 0.033  -0.037 97  HIS AAA CB  
542   C CG  . HIS A 97  ? 0.338 0.428 0.329 -0.020 0.033  -0.039 97  HIS AAA CG  
543   N ND1 . HIS A 97  ? 0.350 0.452 0.345 -0.020 0.031  -0.043 97  HIS AAA ND1 
544   C CD2 . HIS A 97  ? 0.345 0.432 0.334 -0.019 0.033  -0.038 97  HIS AAA CD2 
545   C CE1 . HIS A 97  ? 0.342 0.450 0.336 -0.020 0.031  -0.044 97  HIS AAA CE1 
546   N NE2 . HIS A 97  ? 0.344 0.443 0.335 -0.019 0.032  -0.041 97  HIS AAA NE2 
547   N N   . ASP A 98  ? 0.306 0.368 0.297 -0.022 0.039  -0.039 98  ASP AAA N   
548   C CA  . ASP A 98  ? 0.312 0.369 0.302 -0.021 0.037  -0.035 98  ASP AAA CA  
549   C C   . ASP A 98  ? 0.318 0.367 0.308 -0.022 0.041  -0.037 98  ASP AAA C   
550   O O   . ASP A 98  ? 0.330 0.380 0.322 -0.023 0.040  -0.036 98  ASP AAA O   
551   C CB  . ASP A 98  ? 0.316 0.367 0.301 -0.019 0.036  -0.029 98  ASP AAA CB  
552   C CG  . ASP A 98  ? 0.316 0.374 0.301 -0.017 0.032  -0.026 98  ASP AAA CG  
553   O OD1 . ASP A 98  ? 0.310 0.377 0.297 -0.018 0.030  -0.027 98  ASP AAA OD1 
554   O OD2 . ASP A 98  ? 0.337 0.389 0.318 -0.016 0.031  -0.023 98  ASP AAA OD2 
555   N N   . ALA A 99  ? 0.321 0.363 0.311 -0.023 0.046  -0.040 99  ALA AAA N   
556   C CA  . ALA A 99  ? 0.355 0.388 0.344 -0.024 0.050  -0.041 99  ALA AAA CA  
557   C C   . ALA A 99  ? 0.358 0.395 0.352 -0.026 0.051  -0.045 99  ALA AAA C   
558   O O   . ALA A 99  ? 0.368 0.401 0.361 -0.026 0.051  -0.043 99  ALA AAA O   
559   C CB  . ALA A 99  ? 0.356 0.381 0.344 -0.024 0.056  -0.043 99  ALA AAA CB  
560   N N   . GLN A 100 ? 0.372 0.418 0.371 -0.028 0.051  -0.050 100 GLN AAA N   
561   C CA  . GLN A 100 ? 0.419 0.470 0.423 -0.030 0.052  -0.055 100 GLN AAA CA  
562   C C   . GLN A 100 ? 0.395 0.452 0.400 -0.029 0.047  -0.051 100 GLN AAA C   
563   O O   . GLN A 100 ? 0.414 0.468 0.420 -0.030 0.048  -0.052 100 GLN AAA O   
564   C CB  . GLN A 100 ? 0.476 0.537 0.486 -0.032 0.053  -0.061 100 GLN AAA CB  
565   C CG  . GLN A 100 ? 0.563 0.634 0.579 -0.034 0.053  -0.067 100 GLN AAA CG  
566   C CD  . GLN A 100 ? 0.628 0.694 0.649 -0.037 0.059  -0.073 100 GLN AAA CD  
567   O OE1 . GLN A 100 ? 0.673 0.743 0.699 -0.039 0.062  -0.079 100 GLN AAA OE1 
568   N NE2 . GLN A 100 ? 0.692 0.751 0.713 -0.037 0.061  -0.072 100 GLN AAA NE2 
569   N N   . MET A 101 ? 0.368 0.432 0.371 -0.027 0.042  -0.047 101 MET AAA N   
570   C CA  . MET A 101 ? 0.351 0.420 0.355 -0.025 0.038  -0.043 101 MET AAA CA  
571   C C   . MET A 101 ? 0.332 0.391 0.333 -0.025 0.038  -0.039 101 MET AAA C   
572   O O   . MET A 101 ? 0.330 0.391 0.332 -0.024 0.036  -0.038 101 MET AAA O   
573   C CB  . MET A 101 ? 0.350 0.425 0.351 -0.023 0.034  -0.039 101 MET AAA CB  
574   C CG  . MET A 101 ? 0.370 0.459 0.375 -0.023 0.033  -0.042 101 MET AAA CG  
575   S SD  . MET A 101 ? 0.386 0.487 0.396 -0.024 0.031  -0.046 101 MET AAA SD  
576   C CE  . MET A 101 ? 0.373 0.476 0.382 -0.021 0.027  -0.038 101 MET AAA CE  
577   N N   . PHE A 102 ? 0.311 0.359 0.307 -0.024 0.040  -0.037 102 PHE AAA N   
578   C CA  . PHE A 102 ? 0.319 0.359 0.313 -0.023 0.040  -0.034 102 PHE AAA CA  
579   C C   . PHE A 102 ? 0.301 0.333 0.294 -0.024 0.044  -0.037 102 PHE AAA C   
580   O O   . PHE A 102 ? 0.292 0.316 0.282 -0.022 0.045  -0.034 102 PHE AAA O   
581   C CB  . PHE A 102 ? 0.314 0.350 0.303 -0.020 0.038  -0.029 102 PHE AAA CB  
582   C CG  . PHE A 102 ? 0.305 0.347 0.295 -0.019 0.033  -0.026 102 PHE AAA CG  
583   C CD1 . PHE A 102 ? 0.301 0.351 0.292 -0.019 0.032  -0.026 102 PHE AAA CD1 
584   C CD2 . PHE A 102 ? 0.300 0.342 0.291 -0.018 0.031  -0.022 102 PHE AAA CD2 
585   C CE1 . PHE A 102 ? 0.294 0.350 0.285 -0.018 0.028  -0.022 102 PHE AAA CE1 
586   C CE2 . PHE A 102 ? 0.296 0.344 0.289 -0.017 0.027  -0.019 102 PHE AAA CE2 
587   C CZ  . PHE A 102 ? 0.294 0.349 0.287 -0.017 0.026  -0.019 102 PHE AAA CZ  
588   N N   . GLY A 103 ? 0.305 0.341 0.303 -0.026 0.047  -0.042 103 GLY AAA N   
589   C CA  . GLY A 103 ? 0.328 0.358 0.327 -0.028 0.052  -0.045 103 GLY AAA CA  
590   C C   . GLY A 103 ? 0.336 0.357 0.334 -0.029 0.058  -0.047 103 GLY AAA C   
591   O O   . GLY A 103 ? 0.346 0.362 0.346 -0.030 0.062  -0.050 103 GLY AAA O   
592   N N   . HIS A 104 ? 0.356 0.376 0.351 -0.028 0.058  -0.046 104 HIS AAA N   
593   C CA  . HIS A 104 ? 0.385 0.397 0.379 -0.028 0.064  -0.047 104 HIS AAA CA  
594   C C   . HIS A 104 ? 0.425 0.442 0.424 -0.030 0.066  -0.053 104 HIS AAA C   
595   O O   . HIS A 104 ? 0.412 0.434 0.410 -0.030 0.064  -0.053 104 HIS AAA O   
596   C CB  . HIS A 104 ? 0.387 0.393 0.374 -0.024 0.062  -0.042 104 HIS AAA CB  
597   C CG  . HIS A 104 ? 0.381 0.382 0.363 -0.022 0.060  -0.037 104 HIS AAA CG  
598   N ND1 . HIS A 104 ? 0.390 0.382 0.370 -0.020 0.065  -0.036 104 HIS AAA ND1 
599   C CD2 . HIS A 104 ? 0.386 0.392 0.367 -0.020 0.055  -0.033 104 HIS AAA CD2 
600   C CE1 . HIS A 104 ? 0.393 0.384 0.368 -0.018 0.061  -0.032 104 HIS AAA CE1 
601   N NE2 . HIS A 104 ? 0.396 0.395 0.373 -0.018 0.055  -0.031 104 HIS AAA NE2 
602   N N   . LYS A 105 ? 0.467 0.484 0.472 -0.033 0.071  -0.059 105 LYS AAA N   
603   C CA  . LYS A 105 ? 0.515 0.536 0.526 -0.036 0.075  -0.066 105 LYS AAA CA  
604   C C   . LYS A 105 ? 0.515 0.524 0.523 -0.035 0.080  -0.065 105 LYS AAA C   
605   O O   . LYS A 105 ? 0.545 0.543 0.550 -0.034 0.085  -0.062 105 LYS AAA O   
606   C CB  . LYS A 105 ? 0.551 0.574 0.569 -0.039 0.078  -0.072 105 LYS AAA CB  
607   C CG  . LYS A 105 ? 0.609 0.637 0.635 -0.042 0.083  -0.080 105 LYS AAA CG  
608   C CD  . LYS A 105 ? 0.658 0.701 0.687 -0.043 0.078  -0.084 105 LYS AAA CD  
609   C CE  . LYS A 105 ? 0.699 0.750 0.738 -0.047 0.081  -0.094 105 LYS AAA CE  
610   N NZ  . LYS A 105 ? 0.706 0.762 0.749 -0.048 0.080  -0.097 105 LYS AAA NZ  
611   N N   . THR A 106 ? 0.520 0.533 0.529 -0.035 0.080  -0.066 106 THR AAA N   
612   C CA  . THR A 106 ? 0.538 0.541 0.543 -0.033 0.084  -0.064 106 THR AAA CA  
613   C C   . THR A 106 ? 0.529 0.536 0.541 -0.036 0.088  -0.071 106 THR AAA C   
614   O O   . THR A 106 ? 0.523 0.542 0.539 -0.038 0.084  -0.075 106 THR AAA O   
615   C CB  . THR A 106 ? 0.532 0.535 0.530 -0.030 0.079  -0.057 106 THR AAA CB  
616   O OG1 . THR A 106 ? 0.542 0.557 0.543 -0.031 0.075  -0.060 106 THR AAA OG1 
617   C CG2 . THR A 106 ? 0.529 0.532 0.522 -0.027 0.074  -0.051 106 THR AAA CG2 
618   N N   . SER A 107 ? 0.538 0.534 0.551 -0.036 0.095  -0.071 107 SER AAA N   
619   C CA  . SER A 107 ? 0.527 0.525 0.545 -0.037 0.099  -0.076 107 SER AAA CA  
620   C C   . SER A 107 ? 0.519 0.508 0.529 -0.033 0.099  -0.070 107 SER AAA C   
621   O O   . SER A 107 ? 0.517 0.495 0.521 -0.031 0.101  -0.064 107 SER AAA O   
622   C CB  . SER A 107 ? 0.551 0.545 0.577 -0.041 0.107  -0.083 107 SER AAA CB  
623   O OG  . SER A 107 ? 0.543 0.523 0.568 -0.040 0.114  -0.080 107 SER AAA OG  
624   N N   . SER A 108 ? 0.513 0.508 0.524 -0.033 0.098  -0.071 108 SER AAA N   
625   C CA  . SER A 108 ? 0.563 0.552 0.567 -0.029 0.097  -0.066 108 SER AAA CA  
626   C C   . SER A 108 ? 0.574 0.565 0.582 -0.031 0.099  -0.071 108 SER AAA C   
627   O O   . SER A 108 ? 0.580 0.582 0.595 -0.034 0.098  -0.077 108 SER AAA O   
628   C CB  . SER A 108 ? 0.567 0.563 0.564 -0.027 0.088  -0.061 108 SER AAA CB  
629   O OG  . SER A 108 ? 0.549 0.540 0.539 -0.023 0.087  -0.055 108 SER AAA OG  
630   N N   . SER A 109 ? 0.558 0.539 0.563 -0.028 0.103  -0.067 109 SER AAA N   
631   C CA  . SER A 109 ? 0.532 0.516 0.540 -0.028 0.104  -0.071 109 SER AAA CA  
632   C C   . SER A 109 ? 0.522 0.500 0.521 -0.024 0.103  -0.063 109 SER AAA C   
633   O O   . SER A 109 ? 0.534 0.501 0.526 -0.020 0.105  -0.057 109 SER AAA O   
634   C CB  . SER A 109 ? 0.522 0.500 0.538 -0.031 0.114  -0.077 109 SER AAA CB  
635   O OG  . SER A 109 ? 0.521 0.484 0.535 -0.029 0.121  -0.073 109 SER AAA OG  
636   N N   . PHE A 110 ? 0.498 0.484 0.497 -0.023 0.099  -0.065 110 PHE AAA N   
637   C CA  . PHE A 110 ? 0.488 0.471 0.478 -0.019 0.096  -0.058 110 PHE AAA CA  
638   C C   . PHE A 110 ? 0.470 0.443 0.461 -0.017 0.103  -0.059 110 PHE AAA C   
639   O O   . PHE A 110 ? 0.477 0.454 0.476 -0.021 0.106  -0.066 110 PHE AAA O   
640   C CB  . PHE A 110 ? 0.476 0.472 0.465 -0.019 0.088  -0.059 110 PHE AAA CB  
641   C CG  . PHE A 110 ? 0.470 0.463 0.452 -0.015 0.086  -0.053 110 PHE AAA CG  
642   C CD1 . PHE A 110 ? 0.459 0.446 0.433 -0.011 0.084  -0.046 110 PHE AAA CD1 
643   C CD2 . PHE A 110 ? 0.472 0.468 0.455 -0.015 0.085  -0.056 110 PHE AAA CD2 
644   C CE1 . PHE A 110 ? 0.471 0.456 0.438 -0.007 0.081  -0.042 110 PHE AAA CE1 
645   C CE2 . PHE A 110 ? 0.474 0.468 0.450 -0.011 0.083  -0.051 110 PHE AAA CE2 
646   C CZ  . PHE A 110 ? 0.478 0.467 0.447 -0.007 0.081  -0.044 110 PHE AAA CZ  
647   N N   . GLU A 111 ? 0.451 0.414 0.434 -0.013 0.105  -0.052 111 GLU AAA N   
648   C CA  . GLU A 111 ? 0.464 0.418 0.447 -0.010 0.111  -0.052 111 GLU AAA CA  
649   C C   . GLU A 111 ? 0.448 0.403 0.423 -0.005 0.106  -0.046 111 GLU AAA C   
650   O O   . GLU A 111 ? 0.444 0.394 0.411 -0.001 0.105  -0.040 111 GLU AAA O   
651   C CB  . GLU A 111 ? 0.484 0.424 0.467 -0.008 0.120  -0.049 111 GLU AAA CB  
652   C CG  . GLU A 111 ? 0.510 0.449 0.503 -0.014 0.125  -0.056 111 GLU AAA CG  
653   C CD  . GLU A 111 ? 0.534 0.476 0.538 -0.018 0.130  -0.064 111 GLU AAA CD  
654   O OE1 . GLU A 111 ? 0.518 0.463 0.532 -0.023 0.133  -0.071 111 GLU AAA OE1 
655   O OE2 . GLU A 111 ? 0.511 0.454 0.515 -0.016 0.130  -0.065 111 GLU AAA OE2 
656   N N   . TRP A 112 ? 0.445 0.406 0.422 -0.006 0.104  -0.050 112 TRP AAA N   
657   C CA  . TRP A 112 ? 0.439 0.404 0.410 -0.003 0.099  -0.046 112 TRP AAA CA  
658   C C   . TRP A 112 ? 0.438 0.391 0.401 0.003  0.103  -0.039 112 TRP AAA C   
659   O O   . TRP A 112 ? 0.423 0.377 0.379 0.007  0.098  -0.034 112 TRP AAA O   
660   C CB  . TRP A 112 ? 0.431 0.404 0.407 -0.005 0.098  -0.051 112 TRP AAA CB  
661   C CG  . TRP A 112 ? 0.440 0.414 0.410 -0.001 0.095  -0.048 112 TRP AAA CG  
662   C CD1 . TRP A 112 ? 0.445 0.412 0.413 0.002  0.099  -0.046 112 TRP AAA CD1 
663   C CD2 . TRP A 112 ? 0.426 0.410 0.392 -0.001 0.086  -0.045 112 TRP AAA CD2 
664   N NE1 . TRP A 112 ? 0.438 0.409 0.400 0.005  0.093  -0.043 112 TRP AAA NE1 
665   C CE2 . TRP A 112 ? 0.421 0.404 0.382 0.003  0.085  -0.043 112 TRP AAA CE2 
666   C CE3 . TRP A 112 ? 0.421 0.415 0.386 -0.003 0.079  -0.045 112 TRP AAA CE3 
667   C CZ2 . TRP A 112 ? 0.416 0.406 0.373 0.005  0.078  -0.040 112 TRP AAA CZ2 
668   C CZ3 . TRP A 112 ? 0.419 0.420 0.380 -0.001 0.073  -0.042 112 TRP AAA CZ3 
669   C CH2 . TRP A 112 ? 0.424 0.424 0.381 0.003  0.072  -0.040 112 TRP AAA CH2 
670   N N   . GLY A 113 ? 0.460 0.402 0.426 0.004  0.112  -0.040 113 GLY AAA N   
671   C CA  . GLY A 113 ? 0.480 0.410 0.439 0.010  0.116  -0.034 113 GLY AAA CA  
672   C C   . GLY A 113 ? 0.476 0.401 0.427 0.015  0.116  -0.027 113 GLY AAA C   
673   O O   . GLY A 113 ? 0.494 0.415 0.438 0.021  0.116  -0.021 113 GLY AAA O   
674   N N   . LYS A 114 ? 0.472 0.399 0.425 0.012  0.115  -0.028 114 LYS AAA N   
675   C CA  . LYS A 114 ? 0.479 0.402 0.425 0.015  0.114  -0.023 114 LYS AAA CA  
676   C C   . LYS A 114 ? 0.464 0.396 0.404 0.017  0.105  -0.020 114 LYS AAA C   
677   O O   . LYS A 114 ? 0.451 0.380 0.383 0.023  0.104  -0.014 114 LYS AAA O   
678   C CB  . LYS A 114 ? 0.485 0.408 0.437 0.010  0.116  -0.026 114 LYS AAA CB  
679   C CG  . LYS A 114 ? 0.514 0.433 0.460 0.014  0.115  -0.020 114 LYS AAA CG  
680   C CD  . LYS A 114 ? 0.550 0.459 0.488 0.021  0.120  -0.014 114 LYS AAA CD  
681   C CE  . LYS A 114 ? 0.581 0.488 0.513 0.023  0.119  -0.010 114 LYS AAA CE  
682   N NZ  . LYS A 114 ? 0.627 0.523 0.553 0.030  0.126  -0.004 114 LYS AAA NZ  
683   N N   . LEU A 115 ? 0.433 0.376 0.376 0.013  0.098  -0.023 115 LEU AAA N   
684   C CA  . LEU A 115 ? 0.425 0.377 0.364 0.015  0.089  -0.021 115 LEU AAA CA  
685   C C   . LEU A 115 ? 0.424 0.375 0.357 0.020  0.088  -0.018 115 LEU AAA C   
686   O O   . LEU A 115 ? 0.401 0.353 0.327 0.024  0.085  -0.014 115 LEU AAA O   
687   C CB  . LEU A 115 ? 0.403 0.367 0.347 0.009  0.083  -0.026 115 LEU AAA CB  
688   C CG  . LEU A 115 ? 0.392 0.365 0.334 0.010  0.075  -0.024 115 LEU AAA CG  
689   C CD1 . LEU A 115 ? 0.388 0.361 0.325 0.012  0.072  -0.020 115 LEU AAA CD1 
690   C CD2 . LEU A 115 ? 0.384 0.369 0.332 0.005  0.071  -0.028 115 LEU AAA CD2 
691   N N   . VAL A 116 ? 0.451 0.401 0.387 0.019  0.091  -0.021 116 VAL AAA N   
692   C CA  . VAL A 116 ? 0.469 0.416 0.400 0.024  0.092  -0.018 116 VAL AAA CA  
693   C C   . VAL A 116 ? 0.478 0.416 0.402 0.031  0.096  -0.012 116 VAL AAA C   
694   O O   . VAL A 116 ? 0.468 0.408 0.385 0.035  0.092  -0.009 116 VAL AAA O   
695   C CB  . VAL A 116 ? 0.486 0.431 0.423 0.022  0.097  -0.022 116 VAL AAA CB  
696   C CG1 . VAL A 116 ? 0.507 0.447 0.439 0.028  0.100  -0.019 116 VAL AAA CG1 
697   C CG2 . VAL A 116 ? 0.484 0.440 0.426 0.017  0.092  -0.027 116 VAL AAA CG2 
698   N N   . GLU A 117 ? 0.527 0.455 0.452 0.031  0.103  -0.011 117 GLU AAA N   
699   C CA  . GLU A 117 ? 0.580 0.499 0.498 0.038  0.108  -0.005 117 GLU AAA CA  
700   C C   . GLU A 117 ? 0.543 0.467 0.454 0.041  0.102  -0.002 117 GLU AAA C   
701   O O   . GLU A 117 ? 0.526 0.449 0.429 0.048  0.101  0.002  117 GLU AAA O   
702   C CB  . GLU A 117 ? 0.628 0.537 0.550 0.037  0.118  -0.006 117 GLU AAA CB  
703   C CG  . GLU A 117 ? 0.665 0.563 0.580 0.043  0.123  0.001  117 GLU AAA CG  
704   C CD  . GLU A 117 ? 0.736 0.626 0.658 0.040  0.132  -0.001 117 GLU AAA CD  
705   O OE1 . GLU A 117 ? 0.721 0.611 0.643 0.038  0.131  -0.001 117 GLU AAA OE1 
706   O OE2 . GLU A 117 ? 0.795 0.677 0.721 0.040  0.140  -0.002 117 GLU AAA OE2 
707   N N   . THR A 118 ? 0.538 0.467 0.452 0.036  0.097  -0.004 118 THR AAA N   
708   C CA  . THR A 118 ? 0.534 0.470 0.443 0.038  0.091  -0.002 118 THR AAA CA  
709   C C   . THR A 118 ? 0.510 0.454 0.416 0.041  0.084  -0.001 118 THR AAA C   
710   O O   . THR A 118 ? 0.475 0.421 0.374 0.046  0.082  0.002  118 THR AAA O   
711   C CB  . THR A 118 ? 0.528 0.468 0.443 0.032  0.088  -0.005 118 THR AAA CB  
712   O OG1 . THR A 118 ? 0.518 0.448 0.433 0.032  0.095  -0.004 118 THR AAA OG1 
713   C CG2 . THR A 118 ? 0.518 0.465 0.429 0.033  0.081  -0.004 118 THR AAA CG2 
714   N N   . LEU A 119 ? 0.510 0.460 0.420 0.037  0.081  -0.005 119 LEU AAA N   
715   C CA  . LEU A 119 ? 0.526 0.484 0.433 0.039  0.075  -0.005 119 LEU AAA CA  
716   C C   . LEU A 119 ? 0.522 0.474 0.421 0.047  0.078  -0.001 119 LEU AAA C   
717   O O   . LEU A 119 ? 0.518 0.474 0.412 0.051  0.074  0.001  119 LEU AAA O   
718   C CB  . LEU A 119 ? 0.524 0.487 0.436 0.034  0.073  -0.009 119 LEU AAA CB  
719   C CG  . LEU A 119 ? 0.512 0.486 0.430 0.029  0.066  -0.011 119 LEU AAA CG  
720   C CD1 . LEU A 119 ? 0.498 0.470 0.419 0.025  0.068  -0.012 119 LEU AAA CD1 
721   C CD2 . LEU A 119 ? 0.511 0.491 0.433 0.025  0.064  -0.015 119 LEU AAA CD2 
722   N N   . ARG A 120 ? 0.570 0.515 0.471 0.048  0.085  -0.001 120 ARG AAA N   
723   C CA  . ARG A 120 ? 0.663 0.603 0.558 0.055  0.089  0.002  120 ARG AAA CA  
724   C C   . ARG A 120 ? 0.642 0.578 0.529 0.062  0.090  0.007  120 ARG AAA C   
725   O O   . ARG A 120 ? 0.612 0.552 0.493 0.068  0.087  0.010  120 ARG AAA O   
726   C CB  . ARG A 120 ? 0.748 0.678 0.647 0.054  0.097  0.002  120 ARG AAA CB  
727   C CG  . ARG A 120 ? 0.823 0.756 0.726 0.052  0.097  -0.001 120 ARG AAA CG  
728   C CD  . ARG A 120 ? 0.934 0.856 0.840 0.054  0.106  -0.001 120 ARG AAA CD  
729   N NE  . ARG A 120 ? 1.022 0.940 0.937 0.047  0.111  -0.005 120 ARG AAA NE  
730   C CZ  . ARG A 120 ? 1.009 0.918 0.925 0.046  0.118  -0.005 120 ARG AAA CZ  
731   N NH1 . ARG A 120 ? 0.977 0.880 0.887 0.052  0.121  0.001  120 ARG AAA NH1 
732   N NH2 . ARG A 120 ? 1.013 0.921 0.939 0.040  0.121  -0.010 120 ARG AAA NH2 
733   N N   . ASN A 121 ? 0.608 0.539 0.496 0.061  0.093  0.009  121 ASN AAA N   
734   C CA  . ASN A 121 ? 0.611 0.539 0.490 0.068  0.095  0.013  121 ASN AAA CA  
735   C C   . ASN A 121 ? 0.564 0.503 0.440 0.070  0.086  0.013  121 ASN AAA C   
736   O O   . ASN A 121 ? 0.554 0.494 0.423 0.077  0.086  0.016  121 ASN AAA O   
737   C CB  . ASN A 121 ? 0.627 0.548 0.508 0.066  0.099  0.014  121 ASN AAA CB  
738   C CG  . ASN A 121 ? 0.657 0.567 0.542 0.065  0.109  0.015  121 ASN AAA CG  
739   O OD1 . ASN A 121 ? 0.690 0.595 0.575 0.067  0.113  0.016  121 ASN AAA OD1 
740   N ND2 . ASN A 121 ? 0.642 0.546 0.530 0.062  0.114  0.015  121 ASN AAA ND2 
741   N N   . HIS A 122 ? 0.544 0.490 0.425 0.063  0.080  0.009  122 HIS AAA N   
742   C CA  . HIS A 122 ? 0.517 0.473 0.396 0.064  0.072  0.008  122 HIS AAA CA  
743   C C   . HIS A 122 ? 0.520 0.483 0.396 0.068  0.068  0.008  122 HIS AAA C   
744   O O   . HIS A 122 ? 0.505 0.472 0.376 0.074  0.065  0.009  122 HIS AAA O   
745   C CB  . HIS A 122 ? 0.497 0.459 0.383 0.057  0.068  0.005  122 HIS AAA CB  
746   C CG  . HIS A 122 ? 0.493 0.463 0.378 0.058  0.061  0.004  122 HIS AAA CG  
747   N ND1 . HIS A 122 ? 0.509 0.489 0.397 0.056  0.055  0.002  122 HIS AAA ND1 
748   C CD2 . HIS A 122 ? 0.492 0.463 0.374 0.060  0.061  0.006  122 HIS AAA CD2 
749   C CE1 . HIS A 122 ? 0.483 0.469 0.370 0.058  0.051  0.002  122 HIS AAA CE1 
750   N NE2 . HIS A 122 ? 0.479 0.460 0.363 0.060  0.054  0.003  122 HIS AAA NE2 
751   N N   . ILE A 123 ? 0.524 0.488 0.405 0.065  0.068  0.006  123 ILE AAA N   
752   C CA  . ILE A 123 ? 0.532 0.501 0.410 0.068  0.065  0.005  123 ILE AAA CA  
753   C C   . ILE A 123 ? 0.563 0.527 0.433 0.077  0.069  0.009  123 ILE AAA C   
754   O O   . ILE A 123 ? 0.591 0.562 0.457 0.082  0.065  0.009  123 ILE AAA O   
755   C CB  . ILE A 123 ? 0.509 0.479 0.394 0.062  0.065  0.003  123 ILE AAA CB  
756   C CG1 . ILE A 123 ? 0.508 0.485 0.399 0.055  0.060  -0.001 123 ILE AAA CG1 
757   C CG2 . ILE A 123 ? 0.494 0.466 0.375 0.066  0.064  0.002  123 ILE AAA CG2 
758   C CD1 . ILE A 123 ? 0.516 0.494 0.413 0.049  0.061  -0.004 123 ILE AAA CD1 
759   N N   . ARG A 124 ? 0.612 0.566 0.480 0.079  0.077  0.012  124 ARG AAA N   
760   C CA  . ARG A 124 ? 0.662 0.611 0.522 0.089  0.082  0.017  124 ARG AAA CA  
761   C C   . ARG A 124 ? 0.608 0.562 0.462 0.095  0.079  0.019  124 ARG AAA C   
762   O O   . ARG A 124 ? 0.560 0.520 0.408 0.102  0.076  0.020  124 ARG AAA O   
763   C CB  . ARG A 124 ? 0.735 0.670 0.595 0.090  0.091  0.020  124 ARG AAA CB  
764   C CG  . ARG A 124 ? 0.807 0.736 0.661 0.099  0.097  0.025  124 ARG AAA CG  
765   C CD  . ARG A 124 ? 0.871 0.786 0.727 0.099  0.108  0.028  124 ARG AAA CD  
766   N NE  . ARG A 124 ? 0.890 0.802 0.756 0.090  0.110  0.023  124 ARG AAA NE  
767   C CZ  . ARG A 124 ? 0.927 0.835 0.799 0.084  0.113  0.022  124 ARG AAA CZ  
768   N NH1 . ARG A 124 ? 0.922 0.828 0.790 0.086  0.114  0.024  124 ARG AAA NH1 
769   N NH2 . ARG A 124 ? 0.935 0.841 0.816 0.076  0.114  0.017  124 ARG AAA NH2 
770   N N   . MET A 125 ? 0.599 0.553 0.454 0.092  0.078  0.019  125 MET AAA N   
771   C CA  . MET A 125 ? 0.595 0.555 0.444 0.098  0.075  0.020  125 MET AAA CA  
772   C C   . MET A 125 ? 0.582 0.554 0.431 0.098  0.066  0.016  125 MET AAA C   
773   O O   . MET A 125 ? 0.583 0.562 0.426 0.106  0.065  0.017  125 MET AAA O   
774   C CB  . MET A 125 ? 0.584 0.543 0.437 0.093  0.074  0.019  125 MET AAA CB  
775   C CG  . MET A 125 ? 0.616 0.581 0.464 0.097  0.071  0.019  125 MET AAA CG  
776   S SD  . MET A 125 ? 0.674 0.654 0.526 0.095  0.061  0.014  125 MET AAA SD  
777   C CE  . MET A 125 ? 0.651 0.631 0.514 0.083  0.058  0.010  125 MET AAA CE  
778   N N   . LEU A 126 ? 0.532 0.510 0.389 0.091  0.062  0.012  126 LEU AAA N   
779   C CA  . LEU A 126 ? 0.494 0.483 0.352 0.090  0.054  0.008  126 LEU AAA CA  
780   C C   . LEU A 126 ? 0.485 0.477 0.339 0.096  0.054  0.009  126 LEU AAA C   
781   O O   . LEU A 126 ? 0.464 0.465 0.315 0.101  0.050  0.008  126 LEU AAA O   
782   C CB  . LEU A 126 ? 0.466 0.459 0.333 0.081  0.050  0.005  126 LEU AAA CB  
783   C CG  . LEU A 126 ? 0.450 0.445 0.322 0.075  0.048  0.003  126 LEU AAA CG  
784   C CD1 . LEU A 126 ? 0.443 0.440 0.323 0.066  0.045  0.000  126 LEU AAA CD1 
785   C CD2 . LEU A 126 ? 0.435 0.439 0.306 0.078  0.042  0.001  126 LEU AAA CD2 
786   N N   . ASN A 127 ? 0.507 0.491 0.360 0.096  0.059  0.011  127 ASN AAA N   
787   C CA  . ASN A 127 ? 0.527 0.512 0.376 0.103  0.060  0.012  127 ASN AAA CA  
788   C C   . ASN A 127 ? 0.554 0.541 0.393 0.113  0.061  0.015  127 ASN AAA C   
789   O O   . ASN A 127 ? 0.543 0.540 0.380 0.118  0.057  0.014  127 ASN AAA O   
790   C CB  . ASN A 127 ? 0.538 0.513 0.388 0.103  0.067  0.014  127 ASN AAA CB  
791   C CG  . ASN A 127 ? 0.531 0.505 0.389 0.093  0.066  0.011  127 ASN AAA CG  
792   O OD1 . ASN A 127 ? 0.529 0.493 0.390 0.090  0.072  0.012  127 ASN AAA OD1 
793   N ND2 . ASN A 127 ? 0.513 0.496 0.376 0.088  0.060  0.007  127 ASN AAA ND2 
794   N N   . PHE A 128 ? 0.595 0.574 0.430 0.116  0.066  0.019  128 PHE AAA N   
795   C CA  . PHE A 128 ? 0.633 0.613 0.459 0.127  0.069  0.023  128 PHE AAA CA  
796   C C   . PHE A 128 ? 0.620 0.613 0.445 0.129  0.062  0.020  128 PHE AAA C   
797   O O   . PHE A 128 ? 0.577 0.579 0.397 0.137  0.059  0.019  128 PHE AAA O   
798   C CB  . PHE A 128 ? 0.656 0.624 0.480 0.128  0.077  0.028  128 PHE AAA CB  
799   C CG  . PHE A 128 ? 0.712 0.679 0.527 0.138  0.080  0.033  128 PHE AAA CG  
800   C CD1 . PHE A 128 ? 0.732 0.705 0.539 0.149  0.080  0.035  128 PHE AAA CD1 
801   C CD2 . PHE A 128 ? 0.724 0.686 0.539 0.138  0.084  0.036  128 PHE AAA CD2 
802   C CE1 . PHE A 128 ? 0.706 0.679 0.504 0.159  0.083  0.040  128 PHE AAA CE1 
803   C CE2 . PHE A 128 ? 0.698 0.658 0.504 0.147  0.088  0.040  128 PHE AAA CE2 
804   C CZ  . PHE A 128 ? 0.699 0.666 0.497 0.158  0.087  0.043  128 PHE AAA CZ  
805   N N   . SER A 129 ? 0.595 0.591 0.427 0.121  0.058  0.017  129 SER AAA N   
806   C CA  . SER A 129 ? 0.626 0.634 0.459 0.121  0.052  0.013  129 SER AAA CA  
807   C C   . SER A 129 ? 0.621 0.640 0.455 0.123  0.045  0.008  129 SER AAA C   
808   O O   . SER A 129 ? 0.602 0.631 0.433 0.128  0.042  0.006  129 SER AAA O   
809   C CB  . SER A 129 ? 0.625 0.631 0.466 0.112  0.050  0.010  129 SER AAA CB  
810   O OG  . SER A 129 ? 0.613 0.630 0.457 0.110  0.043  0.006  129 SER AAA OG  
811   N N   . TYR A 130 ? 0.665 0.683 0.504 0.118  0.044  0.007  130 TYR AAA N   
812   C CA  . TYR A 130 ? 0.678 0.707 0.519 0.118  0.039  0.002  130 TYR AAA CA  
813   C C   . TYR A 130 ? 0.677 0.708 0.509 0.129  0.040  0.004  130 TYR AAA C   
814   O O   . TYR A 130 ? 0.656 0.699 0.488 0.133  0.036  0.001  130 TYR AAA O   
815   C CB  . TYR A 130 ? 0.712 0.739 0.560 0.109  0.037  0.000  130 TYR AAA CB  
816   C CG  . TYR A 130 ? 0.724 0.754 0.581 0.100  0.034  -0.003 130 TYR AAA CG  
817   C CD1 . TYR A 130 ? 0.763 0.804 0.623 0.100  0.028  -0.007 130 TYR AAA CD1 
818   C CD2 . TYR A 130 ? 0.735 0.758 0.598 0.092  0.036  -0.002 130 TYR AAA CD2 
819   C CE1 . TYR A 130 ? 0.801 0.844 0.669 0.092  0.025  -0.010 130 TYR AAA CE1 
820   C CE2 . TYR A 130 ? 0.769 0.794 0.639 0.085  0.033  -0.005 130 TYR AAA CE2 
821   C CZ  . TYR A 130 ? 0.801 0.836 0.674 0.084  0.027  -0.008 130 TYR AAA CZ  
822   O OH  . TYR A 130 ? 0.827 0.864 0.707 0.077  0.025  -0.010 130 TYR AAA OH  
823   N N   . ARG A 131 ? 0.745 0.767 0.572 0.133  0.047  0.010  131 ARG AAA N   
824   C CA  . ARG A 131 ? 0.811 0.834 0.630 0.144  0.049  0.013  131 ARG AAA CA  
825   C C   . ARG A 131 ? 0.765 0.797 0.577 0.152  0.047  0.012  131 ARG AAA C   
826   O O   . ARG A 131 ? 0.727 0.771 0.536 0.159  0.043  0.010  131 ARG AAA O   
827   C CB  . ARG A 131 ? 0.857 0.866 0.670 0.148  0.058  0.019  131 ARG AAA CB  
828   C CG  . ARG A 131 ? 0.913 0.917 0.728 0.147  0.060  0.020  131 ARG AAA CG  
829   C CD  . ARG A 131 ? 0.997 0.986 0.809 0.149  0.069  0.026  131 ARG AAA CD  
830   N NE  . ARG A 131 ? 1.098 1.084 0.901 0.160  0.074  0.032  131 ARG AAA NE  
831   C CZ  . ARG A 131 ? 1.116 1.089 0.916 0.163  0.083  0.038  131 ARG AAA CZ  
832   N NH1 . ARG A 131 ? 1.117 1.079 0.924 0.155  0.087  0.038  131 ARG AAA NH1 
833   N NH2 . ARG A 131 ? 1.130 1.102 0.921 0.174  0.087  0.043  131 ARG AAA NH2 
834   N N   . THR A 132 ? 0.730 0.759 0.541 0.152  0.049  0.014  132 THR AAA N   
835   C CA  . THR A 132 ? 0.753 0.790 0.558 0.160  0.047  0.014  132 THR AAA CA  
836   C C   . THR A 132 ? 0.752 0.805 0.563 0.157  0.039  0.006  132 THR AAA C   
837   O O   . THR A 132 ? 0.744 0.808 0.549 0.166  0.036  0.004  132 THR AAA O   
838   C CB  . THR A 132 ? 0.764 0.793 0.569 0.158  0.052  0.018  132 THR AAA CB  
839   O OG1 . THR A 132 ? 0.783 0.798 0.582 0.162  0.060  0.025  132 THR AAA OG1 
840   C CG2 . THR A 132 ? 0.800 0.838 0.599 0.165  0.050  0.017  132 THR AAA CG2 
841   N N   . GLY A 133 ? 0.731 0.784 0.551 0.146  0.036  0.002  133 GLY AAA N   
842   C CA  . GLY A 133 ? 0.711 0.777 0.539 0.142  0.028  -0.005 133 GLY AAA CA  
843   C C   . GLY A 133 ? 0.710 0.787 0.537 0.146  0.024  -0.009 133 GLY AAA C   
844   O O   . GLY A 133 ? 0.746 0.836 0.575 0.149  0.019  -0.015 133 GLY AAA O   
845   N N   . LEU A 134 ? 0.680 0.751 0.505 0.147  0.027  -0.006 134 LEU AAA N   
846   C CA  . LEU A 134 ? 0.669 0.750 0.493 0.152  0.023  -0.010 134 LEU AAA CA  
847   C C   . LEU A 134 ? 0.682 0.770 0.496 0.165  0.024  -0.008 134 LEU AAA C   
848   O O   . LEU A 134 ? 0.705 0.807 0.519 0.169  0.019  -0.014 134 LEU AAA O   
849   C CB  . LEU A 134 ? 0.657 0.729 0.482 0.149  0.026  -0.007 134 LEU AAA CB  
850   C CG  . LEU A 134 ? 0.655 0.726 0.490 0.137  0.024  -0.010 134 LEU AAA CG  
851   C CD1 . LEU A 134 ? 0.651 0.715 0.486 0.136  0.026  -0.008 134 LEU AAA CD1 
852   C CD2 . LEU A 134 ? 0.630 0.714 0.473 0.133  0.017  -0.017 134 LEU AAA CD2 
853   N N   . ARG A 135 ? 0.701 0.780 0.507 0.171  0.030  -0.001 135 ARG AAA N   
854   C CA  . ARG A 135 ? 0.751 0.835 0.545 0.185  0.032  0.002  135 ARG AAA CA  
855   C C   . ARG A 135 ? 0.690 0.787 0.484 0.188  0.028  -0.003 135 ARG AAA C   
856   O O   . ARG A 135 ? 0.640 0.752 0.432 0.196  0.024  -0.007 135 ARG AAA O   
857   C CB  . ARG A 135 ? 0.827 0.897 0.613 0.190  0.040  0.011  135 ARG AAA CB  
858   C CG  . ARG A 135 ? 0.887 0.961 0.662 0.205  0.043  0.015  135 ARG AAA CG  
859   C CD  . ARG A 135 ? 0.933 0.991 0.701 0.209  0.053  0.025  135 ARG AAA CD  
860   N NE  . ARG A 135 ? 0.943 0.994 0.709 0.209  0.056  0.028  135 ARG AAA NE  
861   C CZ  . ARG A 135 ? 0.990 1.028 0.763 0.199  0.060  0.030  135 ARG AAA CZ  
862   N NH1 . ARG A 135 ? 0.955 0.985 0.735 0.190  0.060  0.029  135 ARG AAA NH1 
863   N NH2 . ARG A 135 ? 1.001 1.034 0.771 0.199  0.063  0.033  135 ARG AAA NH2 
864   N N   . VAL A 136 ? 0.678 0.772 0.476 0.183  0.028  -0.003 136 VAL AAA N   
865   C CA  . VAL A 136 ? 0.664 0.769 0.463 0.185  0.024  -0.008 136 VAL AAA CA  
866   C C   . VAL A 136 ? 0.631 0.751 0.439 0.181  0.017  -0.017 136 VAL AAA C   
867   O O   . VAL A 136 ? 0.646 0.781 0.452 0.187  0.013  -0.022 136 VAL AAA O   
868   C CB  . VAL A 136 ? 0.683 0.779 0.485 0.177  0.026  -0.006 136 VAL AAA CB  
869   C CG1 . VAL A 136 ? 0.661 0.769 0.470 0.175  0.021  -0.013 136 VAL AAA CG1 
870   C CG2 . VAL A 136 ? 0.674 0.760 0.467 0.184  0.034  0.002  136 VAL AAA CG2 
871   N N   . GLY A 137 ? 0.644 0.761 0.461 0.171  0.015  -0.020 137 GLY AAA N   
872   C CA  . GLY A 137 ? 0.630 0.760 0.456 0.166  0.008  -0.029 137 GLY AAA CA  
873   C C   . GLY A 137 ? 0.641 0.780 0.464 0.172  0.006  -0.032 137 GLY AAA C   
874   O O   . GLY A 137 ? 0.651 0.800 0.483 0.167  0.001  -0.039 137 GLY AAA O   
875   N N   . ASN A 138 ? 0.644 0.782 0.456 0.182  0.009  -0.026 138 ASN AAA N   
876   C CA  . ASN A 138 ? 0.684 0.832 0.492 0.191  0.007  -0.029 138 ASN AAA CA  
877   C C   . ASN A 138 ? 0.663 0.807 0.477 0.184  0.006  -0.030 138 ASN AAA C   
878   O O   . ASN A 138 ? 0.667 0.824 0.485 0.185  0.002  -0.036 138 ASN AAA O   
879   C CB  . ASN A 138 ? 0.708 0.876 0.518 0.196  0.002  -0.038 138 ASN AAA CB  
880   C CG  . ASN A 138 ? 0.749 0.929 0.554 0.206  -0.000 -0.040 138 ASN AAA CG  
881   O OD1 . ASN A 138 ? 0.784 0.960 0.579 0.214  0.004  -0.033 138 ASN AAA OD1 
882   N ND2 . ASN A 138 ? 0.765 0.962 0.577 0.205  -0.006 -0.050 138 ASN AAA ND2 
883   N N   . VAL A 139 ? 0.632 0.761 0.448 0.177  0.010  -0.025 139 VAL AAA N   
884   C CA  . VAL A 139 ? 0.608 0.732 0.428 0.171  0.010  -0.024 139 VAL AAA CA  
885   C C   . VAL A 139 ? 0.608 0.721 0.419 0.177  0.016  -0.017 139 VAL AAA C   
886   O O   . VAL A 139 ? 0.622 0.724 0.428 0.179  0.022  -0.010 139 VAL AAA O   
887   C CB  . VAL A 139 ? 0.601 0.716 0.430 0.158  0.010  -0.025 139 VAL AAA CB  
888   C CG1 . VAL A 139 ? 0.608 0.718 0.441 0.152  0.011  -0.024 139 VAL AAA CG1 
889   C CG2 . VAL A 139 ? 0.592 0.716 0.431 0.151  0.005  -0.032 139 VAL AAA CG2 
890   N N   . GLU A 140 ? 0.597 0.714 0.405 0.181  0.015  -0.018 140 GLU AAA N   
891   C CA  . GLU A 140 ? 0.642 0.748 0.443 0.187  0.021  -0.011 140 GLU AAA CA  
892   C C   . GLU A 140 ? 0.621 0.715 0.429 0.176  0.024  -0.009 140 GLU AAA C   
893   O O   . GLU A 140 ? 0.626 0.723 0.440 0.170  0.020  -0.013 140 GLU AAA O   
894   C CB  . GLU A 140 ? 0.702 0.819 0.499 0.195  0.019  -0.013 140 GLU AAA CB  
895   C CG  . GLU A 140 ? 0.755 0.862 0.544 0.204  0.025  -0.005 140 GLU AAA CG  
896   C CD  . GLU A 140 ? 0.818 0.934 0.602 0.212  0.024  -0.007 140 GLU AAA CD  
897   O OE1 . GLU A 140 ? 0.821 0.953 0.607 0.213  0.017  -0.014 140 GLU AAA OE1 
898   O OE2 . GLU A 140 ? 0.820 0.927 0.599 0.217  0.029  -0.001 140 GLU AAA OE2 
899   N N   . TYR A 141 ? 0.605 0.684 0.411 0.174  0.029  -0.003 141 TYR AAA N   
900   C CA  . TYR A 141 ? 0.616 0.682 0.427 0.165  0.033  -0.000 141 TYR AAA CA  
901   C C   . TYR A 141 ? 0.614 0.672 0.421 0.170  0.038  0.004  141 TYR AAA C   
902   O O   . TYR A 141 ? 0.594 0.648 0.393 0.179  0.043  0.009  141 TYR AAA O   
903   C CB  . TYR A 141 ? 0.595 0.650 0.407 0.161  0.037  0.003  141 TYR AAA CB  
904   C CG  . TYR A 141 ? 0.594 0.635 0.410 0.153  0.042  0.006  141 TYR AAA CG  
905   C CD1 . TYR A 141 ? 0.588 0.630 0.413 0.144  0.039  0.003  141 TYR AAA CD1 
906   C CD2 . TYR A 141 ? 0.610 0.637 0.423 0.155  0.049  0.012  141 TYR AAA CD2 
907   C CE1 . TYR A 141 ? 0.582 0.613 0.411 0.138  0.043  0.004  141 TYR AAA CE1 
908   C CE2 . TYR A 141 ? 0.600 0.616 0.418 0.148  0.053  0.014  141 TYR AAA CE2 
909   C CZ  . TYR A 141 ? 0.595 0.613 0.421 0.139  0.050  0.010  141 TYR AAA CZ  
910   O OH  . TYR A 141 ? 0.576 0.583 0.406 0.133  0.055  0.011  141 TYR AAA OH  
911   N N   . ILE A 142 ? 0.624 0.681 0.436 0.164  0.037  0.002  142 ILE AAA N   
912   C CA  . ILE A 142 ? 0.657 0.705 0.466 0.167  0.042  0.006  142 ILE AAA CA  
913   C C   . ILE A 142 ? 0.672 0.710 0.489 0.157  0.044  0.006  142 ILE AAA C   
914   O O   . ILE A 142 ? 0.630 0.674 0.455 0.148  0.040  0.001  142 ILE AAA O   
915   C CB  . ILE A 142 ? 0.678 0.737 0.486 0.172  0.038  0.002  142 ILE AAA CB  
916   C CG1 . ILE A 142 ? 0.694 0.765 0.495 0.183  0.035  0.001  142 ILE AAA CG1 
917   C CG2 . ILE A 142 ? 0.669 0.721 0.476 0.174  0.042  0.005  142 ILE AAA CG2 
918   C CD1 . ILE A 142 ? 0.713 0.798 0.515 0.185  0.029  -0.004 142 ILE AAA CD1 
919   N N   . ASN A 143 ? 0.702 0.726 0.518 0.157  0.052  0.011  143 ASN AAA N   
920   C CA  . ASN A 143 ? 0.680 0.694 0.502 0.148  0.055  0.011  143 ASN AAA CA  
921   C C   . ASN A 143 ? 0.680 0.693 0.504 0.148  0.056  0.010  143 ASN AAA C   
922   O O   . ASN A 143 ? 0.679 0.682 0.501 0.152  0.063  0.014  143 ASN AAA O   
923   C CB  . ASN A 143 ? 0.689 0.689 0.510 0.149  0.063  0.016  143 ASN AAA CB  
924   C CG  . ASN A 143 ? 0.705 0.696 0.534 0.138  0.066  0.015  143 ASN AAA CG  
925   O OD1 . ASN A 143 ? 0.685 0.681 0.522 0.130  0.062  0.010  143 ASN AAA OD1 
926   N ND2 . ASN A 143 ? 0.693 0.671 0.521 0.139  0.074  0.019  143 ASN AAA ND2 
927   N N   . ALA A 144 ? 0.691 0.715 0.519 0.145  0.050  0.005  144 ALA AAA N   
928   C CA  . ALA A 144 ? 0.680 0.704 0.510 0.144  0.050  0.003  144 ALA AAA CA  
929   C C   . ALA A 144 ? 0.645 0.680 0.483 0.135  0.043  -0.003 144 ALA AAA C   
930   O O   . ALA A 144 ? 0.686 0.729 0.526 0.132  0.038  -0.006 144 ALA AAA O   
931   C CB  . ALA A 144 ? 0.691 0.720 0.514 0.155  0.050  0.004  144 ALA AAA CB  
932   N N   . LEU A 145 ? 0.616 0.649 0.459 0.131  0.044  -0.005 145 LEU AAA N   
933   C CA  . LEU A 145 ? 0.629 0.672 0.478 0.124  0.038  -0.010 145 LEU AAA CA  
934   C C   . LEU A 145 ? 0.640 0.694 0.486 0.130  0.033  -0.013 145 LEU AAA C   
935   O O   . LEU A 145 ? 0.662 0.715 0.503 0.138  0.036  -0.011 145 LEU AAA O   
936   C CB  . LEU A 145 ? 0.623 0.661 0.477 0.119  0.041  -0.011 145 LEU AAA CB  
937   C CG  . LEU A 145 ? 0.594 0.625 0.454 0.110  0.044  -0.011 145 LEU AAA CG  
938   C CD1 . LEU A 145 ? 0.610 0.637 0.474 0.107  0.046  -0.013 145 LEU AAA CD1 
939   C CD2 . LEU A 145 ? 0.571 0.609 0.436 0.103  0.039  -0.014 145 LEU AAA CD2 
940   N N   . ALA A 146 ? 0.622 0.688 0.472 0.126  0.027  -0.017 146 ALA AAA N   
941   C CA  . ALA A 146 ? 0.626 0.705 0.475 0.130  0.022  -0.021 146 ALA AAA CA  
942   C C   . ALA A 146 ? 0.616 0.700 0.472 0.123  0.019  -0.025 146 ALA AAA C   
943   O O   . ALA A 146 ? 0.591 0.672 0.453 0.114  0.019  -0.025 146 ALA AAA O   
944   C CB  . ALA A 146 ? 0.633 0.719 0.482 0.131  0.018  -0.023 146 ALA AAA CB  
945   N N   . LYS A 147 ? 0.662 0.755 0.517 0.126  0.016  -0.028 147 LYS AAA N   
946   C CA  . LYS A 147 ? 0.688 0.790 0.551 0.120  0.012  -0.032 147 LYS AAA CA  
947   C C   . LYS A 147 ? 0.646 0.761 0.508 0.124  0.007  -0.037 147 LYS AAA C   
948   O O   . LYS A 147 ? 0.628 0.746 0.484 0.133  0.007  -0.037 147 LYS AAA O   
949   C CB  . LYS A 147 ? 0.736 0.833 0.599 0.119  0.015  -0.032 147 LYS AAA CB  
950   C CG  . LYS A 147 ? 0.795 0.891 0.651 0.129  0.017  -0.031 147 LYS AAA CG  
951   C CD  . LYS A 147 ? 0.829 0.925 0.688 0.127  0.018  -0.032 147 LYS AAA CD  
952   C CE  . LYS A 147 ? 0.878 0.961 0.736 0.126  0.024  -0.029 147 LYS AAA CE  
953   N NZ  . LYS A 147 ? 0.935 1.019 0.794 0.127  0.025  -0.030 147 LYS AAA NZ  
954   N N   . LEU A 148 ? 0.599 0.723 0.469 0.118  0.003  -0.041 148 LEU AAA N   
955   C CA  . LEU A 148 ? 0.607 0.745 0.479 0.120  -0.001 -0.047 148 LEU AAA CA  
956   C C   . LEU A 148 ? 0.576 0.718 0.445 0.126  -0.002 -0.048 148 LEU AAA C   
957   O O   . LEU A 148 ? 0.574 0.711 0.444 0.123  0.000  -0.047 148 LEU AAA O   
958   C CB  . LEU A 148 ? 0.605 0.750 0.487 0.111  -0.005 -0.050 148 LEU AAA CB  
959   C CG  . LEU A 148 ? 0.602 0.743 0.487 0.106  -0.005 -0.049 148 LEU AAA CG  
960   C CD1 . LEU A 148 ? 0.592 0.738 0.487 0.096  -0.007 -0.052 148 LEU AAA CD1 
961   C CD2 . LEU A 148 ? 0.595 0.741 0.478 0.111  -0.006 -0.051 148 LEU AAA CD2 
962   N N   . ILE A 149 ? 0.642 0.792 0.506 0.134  -0.004 -0.051 149 ILE AAA N   
963   C CA  . ILE A 149 ? 0.646 0.802 0.507 0.140  -0.005 -0.053 149 ILE AAA CA  
964   C C   . ILE A 149 ? 0.645 0.816 0.514 0.137  -0.010 -0.060 149 ILE AAA C   
965   O O   . ILE A 149 ? 0.663 0.837 0.535 0.135  -0.010 -0.062 149 ILE AAA O   
966   C CB  . ILE A 149 ? 0.686 0.842 0.538 0.152  -0.003 -0.051 149 ILE AAA CB  
967   C CG1 . ILE A 149 ? 0.700 0.841 0.546 0.155  0.003  -0.044 149 ILE AAA CG1 
968   C CG2 . ILE A 149 ? 0.689 0.856 0.539 0.159  -0.006 -0.055 149 ILE AAA CG2 
969   C CD1 . ILE A 149 ? 0.688 0.823 0.536 0.152  0.006  -0.042 149 ILE AAA CD1 
970   N N   . ASP A 150 ? 0.639 0.817 0.511 0.136  -0.013 -0.064 150 ASP AAA N   
971   C CA  . ASP A 150 ? 0.646 0.838 0.527 0.132  -0.017 -0.071 150 ASP AAA CA  
972   C C   . ASP A 150 ? 0.611 0.806 0.497 0.128  -0.018 -0.073 150 ASP AAA C   
973   O O   . ASP A 150 ? 0.571 0.758 0.454 0.129  -0.016 -0.069 150 ASP AAA O   
974   C CB  . ASP A 150 ? 0.661 0.865 0.540 0.140  -0.019 -0.076 150 ASP AAA CB  
975   C CG  . ASP A 150 ? 0.679 0.889 0.551 0.150  -0.020 -0.077 150 ASP AAA CG  
976   O OD1 . ASP A 150 ? 0.698 0.908 0.571 0.150  -0.021 -0.077 150 ASP AAA OD1 
977   O OD2 . ASP A 150 ? 0.740 0.954 0.605 0.159  -0.021 -0.077 150 ASP AAA OD2 
978   N N   . PRO A 151 ? 0.603 0.809 0.498 0.124  -0.022 -0.079 151 PRO AAA N   
979   C CA  . PRO A 151 ? 0.600 0.809 0.501 0.120  -0.023 -0.082 151 PRO AAA CA  
980   C C   . PRO A 151 ? 0.573 0.783 0.468 0.127  -0.023 -0.081 151 PRO AAA C   
981   O O   . PRO A 151 ? 0.571 0.781 0.471 0.124  -0.023 -0.083 151 PRO AAA O   
982   C CB  . PRO A 151 ? 0.600 0.824 0.511 0.118  -0.026 -0.090 151 PRO AAA CB  
983   C CG  . PRO A 151 ? 0.590 0.815 0.503 0.115  -0.026 -0.090 151 PRO AAA CG  
984   C CD  . PRO A 151 ? 0.594 0.811 0.496 0.122  -0.024 -0.085 151 PRO AAA CD  
985   N N   . HIS A 152 ? 0.585 0.796 0.471 0.138  -0.022 -0.080 152 HIS AAA N   
986   C CA  . HIS A 152 ? 0.598 0.811 0.477 0.146  -0.023 -0.080 152 HIS AAA CA  
987   C C   . HIS A 152 ? 0.610 0.812 0.477 0.153  -0.019 -0.072 152 HIS AAA C   
988   O O   . HIS A 152 ? 0.615 0.820 0.475 0.162  -0.019 -0.071 152 HIS AAA O   
989   C CB  . HIS A 152 ? 0.588 0.818 0.467 0.153  -0.026 -0.088 152 HIS AAA CB  
990   C CG  . HIS A 152 ? 0.602 0.844 0.494 0.146  -0.030 -0.096 152 HIS AAA CG  
991   N ND1 . HIS A 152 ? 0.592 0.833 0.489 0.142  -0.030 -0.097 152 HIS AAA ND1 
992   C CD2 . HIS A 152 ? 0.643 0.894 0.543 0.143  -0.032 -0.102 152 HIS AAA CD2 
993   C CE1 . HIS A 152 ? 0.614 0.866 0.523 0.137  -0.032 -0.105 152 HIS AAA CE1 
994   N NE2 . HIS A 152 ? 0.639 0.897 0.550 0.137  -0.034 -0.108 152 HIS AAA NE2 
995   N N   . SER A 153 ? 0.591 0.781 0.455 0.151  -0.016 -0.066 153 SER AAA N   
996   C CA  . SER A 153 ? 0.606 0.786 0.460 0.158  -0.011 -0.059 153 SER AAA CA  
997   C C   . SER A 153 ? 0.582 0.745 0.436 0.152  -0.007 -0.053 153 SER AAA C   
998   O O   . SER A 153 ? 0.552 0.714 0.413 0.143  -0.007 -0.054 153 SER AAA O   
999   C CB  . SER A 153 ? 0.586 0.770 0.436 0.165  -0.012 -0.060 153 SER AAA CB  
1000  O OG  . SER A 153 ? 0.638 0.839 0.489 0.170  -0.016 -0.067 153 SER AAA OG  
1001  N N   . VAL A 154 ? 0.580 0.733 0.426 0.156  -0.003 -0.047 154 VAL AAA N   
1002  C CA  . VAL A 154 ? 0.626 0.764 0.473 0.151  0.002  -0.041 154 VAL AAA CA  
1003  C C   . VAL A 154 ? 0.651 0.780 0.489 0.159  0.007  -0.035 154 VAL AAA C   
1004  O O   . VAL A 154 ? 0.696 0.828 0.526 0.169  0.007  -0.034 154 VAL AAA O   
1005  C CB  . VAL A 154 ? 0.598 0.731 0.447 0.146  0.002  -0.040 154 VAL AAA CB  
1006  C CG1 . VAL A 154 ? 0.632 0.764 0.473 0.155  0.004  -0.037 154 VAL AAA CG1 
1007  C CG2 . VAL A 154 ? 0.621 0.741 0.473 0.138  0.006  -0.036 154 VAL AAA CG2 
1008  N N   . GLU A 155 ? 0.678 0.794 0.516 0.155  0.011  -0.031 155 GLU AAA N   
1009  C CA  . GLU A 155 ? 0.723 0.829 0.554 0.162  0.017  -0.026 155 GLU AAA CA  
1010  C C   . GLU A 155 ? 0.710 0.801 0.541 0.159  0.022  -0.020 155 GLU AAA C   
1011  O O   . GLU A 155 ? 0.723 0.811 0.561 0.149  0.022  -0.021 155 GLU AAA O   
1012  C CB  . GLU A 155 ? 0.780 0.885 0.614 0.160  0.017  -0.027 155 GLU AAA CB  
1013  C CG  . GLU A 155 ? 0.812 0.908 0.640 0.168  0.023  -0.022 155 GLU AAA CG  
1014  C CD  . GLU A 155 ? 0.819 0.916 0.649 0.167  0.023  -0.024 155 GLU AAA CD  
1015  O OE1 . GLU A 155 ? 0.751 0.847 0.589 0.157  0.022  -0.027 155 GLU AAA OE1 
1016  O OE2 . GLU A 155 ? 0.826 0.923 0.650 0.176  0.025  -0.023 155 GLU AAA OE2 
1017  N N   . TYR A 156 ? 0.711 0.794 0.534 0.167  0.027  -0.015 156 TYR AAA N   
1018  C CA  . TYR A 156 ? 0.755 0.823 0.578 0.165  0.034  -0.009 156 TYR AAA CA  
1019  C C   . TYR A 156 ? 0.843 0.901 0.659 0.174  0.041  -0.004 156 TYR AAA C   
1020  O O   . TYR A 156 ? 0.862 0.925 0.670 0.184  0.040  -0.002 156 TYR AAA O   
1021  C CB  . TYR A 156 ? 0.721 0.788 0.543 0.164  0.034  -0.008 156 TYR AAA CB  
1022  C CG  . TYR A 156 ? 0.701 0.772 0.514 0.175  0.034  -0.005 156 TYR AAA CG  
1023  C CD1 . TYR A 156 ? 0.689 0.775 0.500 0.180  0.028  -0.010 156 TYR AAA CD1 
1024  C CD2 . TYR A 156 ? 0.679 0.739 0.485 0.182  0.040  0.001  156 TYR AAA CD2 
1025  C CE1 . TYR A 156 ? 0.703 0.795 0.506 0.191  0.028  -0.008 156 TYR AAA CE1 
1026  C CE2 . TYR A 156 ? 0.691 0.756 0.489 0.193  0.041  0.004  156 TYR AAA CE2 
1027  C CZ  . TYR A 156 ? 0.703 0.784 0.498 0.197  0.034  -0.001 156 TYR AAA CZ  
1028  O OH  . TYR A 156 ? 0.700 0.787 0.487 0.209  0.035  0.001  156 TYR AAA OH  
1029  N N   . GLU A 157 ? 0.924 0.967 0.741 0.171  0.047  0.000  157 GLU AAA N   
1030  C CA  . GLU A 157 ? 0.973 1.005 0.785 0.179  0.055  0.006  157 GLU AAA CA  
1031  C C   . GLU A 157 ? 1.049 1.076 0.855 0.184  0.059  0.012  157 GLU AAA C   
1032  O O   . GLU A 157 ? 1.066 1.093 0.875 0.178  0.057  0.011  157 GLU AAA O   
1033  C CB  . GLU A 157 ? 1.038 1.059 0.856 0.173  0.060  0.007  157 GLU AAA CB  
1034  C CG  . GLU A 157 ? 1.102 1.110 0.923 0.167  0.066  0.010  157 GLU AAA CG  
1035  C CD  . GLU A 157 ? 1.166 1.166 0.996 0.159  0.070  0.008  157 GLU AAA CD  
1036  O OE1 . GLU A 157 ? 1.161 1.167 0.995 0.154  0.066  0.003  157 GLU AAA OE1 
1037  O OE2 . GLU A 157 ? 1.174 1.162 1.006 0.157  0.077  0.011  157 GLU AAA OE2 
1038  N N   . ASP A 158 ? 1.105 1.126 0.903 0.196  0.064  0.018  158 ASP AAA N   
1039  C CA  . ASP A 158 ? 1.145 1.161 0.935 0.204  0.069  0.024  158 ASP AAA CA  
1040  C C   . ASP A 158 ? 1.189 1.195 0.973 0.214  0.077  0.031  158 ASP AAA C   
1041  O O   . ASP A 158 ? 1.187 1.199 0.966 0.223  0.076  0.031  158 ASP AAA O   
1042  C CB  . ASP A 158 ? 1.124 1.156 0.909 0.210  0.062  0.021  158 ASP AAA CB  
1043  C CG  . ASP A 158 ? 1.148 1.178 0.924 0.220  0.066  0.028  158 ASP AAA CG  
1044  O OD1 . ASP A 158 ? 1.166 1.183 0.942 0.218  0.072  0.032  158 ASP AAA OD1 
1045  O OD2 . ASP A 158 ? 1.150 1.189 0.917 0.231  0.064  0.028  158 ASP AAA OD2 
1046  N N   . ASN A 159 ? 1.218 1.207 1.004 0.212  0.086  0.035  159 ASN AAA N   
1047  C CA  . ASN A 159 ? 1.286 1.262 1.069 0.219  0.095  0.042  159 ASN AAA CA  
1048  C C   . ASN A 159 ? 1.321 1.300 1.110 0.217  0.094  0.038  159 ASN AAA C   
1049  O O   . ASN A 159 ? 1.378 1.356 1.161 0.227  0.097  0.042  159 ASN AAA O   
1050  C CB  . ASN A 159 ? 1.293 1.271 1.065 0.235  0.099  0.049  159 ASN AAA CB  
1051  C CG  . ASN A 159 ? 1.329 1.302 1.097 0.237  0.102  0.054  159 ASN AAA CG  
1052  O OD1 . ASN A 159 ? 1.288 1.245 1.056 0.238  0.111  0.060  159 ASN AAA OD1 
1053  N ND2 . ASN A 159 ? 1.360 1.346 1.124 0.238  0.095  0.051  159 ASN AAA ND2 
1054  N N   . GLY A 160 ? 1.383 1.365 1.181 0.205  0.089  0.031  160 GLY AAA N   
1055  C CA  . GLY A 160 ? 1.355 1.339 1.158 0.201  0.088  0.027  160 GLY AAA CA  
1056  C C   . GLY A 160 ? 1.332 1.329 1.130 0.209  0.082  0.025  160 GLY AAA C   
1057  O O   . GLY A 160 ? 1.270 1.266 1.068 0.212  0.084  0.025  160 GLY AAA O   
1058  N N   . GLN A 161 ? 1.344 1.354 1.137 0.212  0.075  0.023  161 GLN AAA N   
1059  C CA  . GLN A 161 ? 1.330 1.355 1.118 0.220  0.069  0.021  161 GLN AAA CA  
1060  C C   . GLN A 161 ? 1.293 1.333 1.085 0.212  0.059  0.013  161 GLN AAA C   
1061  O O   . GLN A 161 ? 1.287 1.331 1.076 0.213  0.057  0.014  161 GLN AAA O   
1062  C CB  . GLN A 161 ? 1.354 1.381 1.131 0.234  0.072  0.027  161 GLN AAA CB  
1063  C CG  . GLN A 161 ? 1.403 1.416 1.175 0.243  0.081  0.034  161 GLN AAA CG  
1064  C CD  . GLN A 161 ? 1.467 1.486 1.227 0.259  0.082  0.039  161 GLN AAA CD  
1065  O OE1 . GLN A 161 ? 1.444 1.475 1.199 0.264  0.077  0.038  161 GLN AAA OE1 
1066  N NE2 . GLN A 161 ? 1.499 1.512 1.257 0.267  0.088  0.043  161 GLN AAA NE2 
1067  N N   . LYS A 162 ? 1.246 1.292 1.044 0.205  0.055  0.007  162 LYS AAA N   
1068  C CA  . LYS A 162 ? 1.186 1.247 0.988 0.199  0.046  -0.000 162 LYS AAA CA  
1069  C C   . LYS A 162 ? 1.078 1.152 0.873 0.208  0.041  -0.001 162 LYS AAA C   
1070  O O   . LYS A 162 ? 1.064 1.141 0.852 0.219  0.043  0.001  162 LYS AAA O   
1071  C CB  . LYS A 162 ? 1.234 1.302 1.041 0.195  0.042  -0.005 162 LYS AAA CB  
1072  C CG  . LYS A 162 ? 1.282 1.341 1.097 0.186  0.045  -0.006 162 LYS AAA CG  
1073  C CD  . LYS A 162 ? 1.256 1.313 1.078 0.174  0.043  -0.008 162 LYS AAA CD  
1074  C CE  . LYS A 162 ? 1.202 1.257 1.033 0.163  0.043  -0.012 162 LYS AAA CE  
1075  N NZ  . LYS A 162 ? 1.188 1.248 1.026 0.153  0.038  -0.015 162 LYS AAA NZ  
1076  N N   . LYS A 163 ? 0.987 1.067 0.784 0.203  0.037  -0.004 163 LYS AAA N   
1077  C CA  . LYS A 163 ? 0.929 1.024 0.722 0.210  0.032  -0.007 163 LYS AAA CA  
1078  C C   . LYS A 163 ? 0.834 0.941 0.636 0.201  0.024  -0.015 163 LYS AAA C   
1079  O O   . LYS A 163 ? 0.808 0.910 0.618 0.189  0.024  -0.016 163 LYS AAA O   
1080  C CB  . LYS A 163 ? 0.933 1.024 0.721 0.214  0.034  -0.002 163 LYS AAA CB  
1081  C CG  . LYS A 163 ? 0.975 1.056 0.754 0.225  0.042  0.006  163 LYS AAA CG  
1082  C CD  . LYS A 163 ? 0.994 1.076 0.765 0.233  0.043  0.010  163 LYS AAA CD  
1083  C CE  . LYS A 163 ? 1.050 1.123 0.811 0.245  0.051  0.018  163 LYS AAA CE  
1084  N NZ  . LYS A 163 ? 1.042 1.122 0.796 0.254  0.051  0.021  163 LYS AAA NZ  
1085  N N   . THR A 164 ? 0.810 0.933 0.611 0.205  0.018  -0.020 164 THR AAA N   
1086  C CA  . THR A 164 ? 0.815 0.951 0.624 0.198  0.011  -0.028 164 THR AAA CA  
1087  C C   . THR A 164 ? 0.778 0.925 0.585 0.202  0.008  -0.031 164 THR AAA C   
1088  O O   . THR A 164 ? 0.784 0.935 0.582 0.214  0.009  -0.029 164 THR AAA O   
1089  C CB  . THR A 164 ? 0.869 1.014 0.680 0.198  0.008  -0.033 164 THR AAA CB  
1090  O OG1 . THR A 164 ? 0.867 1.002 0.681 0.193  0.011  -0.031 164 THR AAA OG1 
1091  C CG2 . THR A 164 ? 0.886 1.046 0.707 0.191  0.001  -0.042 164 THR AAA CG2 
1092  N N   . ILE A 165 ? 0.712 0.863 0.526 0.194  0.005  -0.035 165 ILE AAA N   
1093  C CA  . ILE A 165 ? 0.688 0.851 0.502 0.197  0.001  -0.039 165 ILE AAA CA  
1094  C C   . ILE A 165 ? 0.636 0.810 0.461 0.188  -0.005 -0.048 165 ILE AAA C   
1095  O O   . ILE A 165 ? 0.597 0.766 0.429 0.178  -0.005 -0.049 165 ILE AAA O   
1096  C CB  . ILE A 165 ? 0.697 0.850 0.509 0.196  0.004  -0.034 165 ILE AAA CB  
1097  C CG1 . ILE A 165 ? 0.678 0.822 0.498 0.182  0.005  -0.034 165 ILE AAA CG1 
1098  C CG2 . ILE A 165 ? 0.716 0.857 0.517 0.205  0.011  -0.026 165 ILE AAA CG2 
1099  C CD1 . ILE A 165 ? 0.703 0.842 0.523 0.180  0.006  -0.032 165 ILE AAA CD1 
1100  N N   . THR A 166 ? 0.610 0.800 0.436 0.192  -0.009 -0.054 166 THR AAA N   
1101  C CA  . THR A 166 ? 0.601 0.804 0.437 0.186  -0.015 -0.063 166 THR AAA CA  
1102  C C   . THR A 166 ? 0.583 0.789 0.425 0.181  -0.017 -0.066 166 THR AAA C   
1103  O O   . THR A 166 ? 0.574 0.781 0.409 0.188  -0.016 -0.064 166 THR AAA O   
1104  C CB  . THR A 166 ? 0.600 0.819 0.435 0.194  -0.018 -0.069 166 THR AAA CB  
1105  O OG1 . THR A 166 ? 0.612 0.838 0.439 0.205  -0.019 -0.069 166 THR AAA OG1 
1106  C CG2 . THR A 166 ? 0.603 0.819 0.434 0.198  -0.017 -0.067 166 THR AAA CG2 
1107  N N   . SER A 167 ? 0.554 0.764 0.408 0.171  -0.019 -0.071 167 SER AAA N   
1108  C CA  . SER A 167 ? 0.550 0.762 0.411 0.165  -0.021 -0.075 167 SER AAA CA  
1109  C C   . SER A 167 ? 0.539 0.764 0.412 0.158  -0.025 -0.084 167 SER AAA C   
1110  O O   . SER A 167 ? 0.546 0.771 0.424 0.153  -0.026 -0.085 167 SER AAA O   
1111  C CB  . SER A 167 ? 0.548 0.745 0.410 0.157  -0.018 -0.068 167 SER AAA CB  
1112  O OG  . SER A 167 ? 0.544 0.742 0.408 0.156  -0.018 -0.069 167 SER AAA OG  
1113  N N   . ARG A 168 ? 0.576 0.811 0.455 0.158  -0.028 -0.090 168 ARG AAA N   
1114  C CA  . ARG A 168 ? 0.594 0.840 0.487 0.150  -0.031 -0.099 168 ARG AAA CA  
1115  C C   . ARG A 168 ? 0.532 0.766 0.432 0.138  -0.029 -0.095 168 ARG AAA C   
1116  O O   . ARG A 168 ? 0.508 0.745 0.416 0.132  -0.030 -0.098 168 ARG AAA O   
1117  C CB  . ARG A 168 ? 0.689 0.945 0.585 0.153  -0.033 -0.105 168 ARG AAA CB  
1118  C CG  . ARG A 168 ? 0.792 1.061 0.702 0.147  -0.036 -0.115 168 ARG AAA CG  
1119  C CD  . ARG A 168 ? 0.923 1.201 0.841 0.144  -0.038 -0.121 168 ARG AAA CD  
1120  N NE  . ARG A 168 ? 1.005 1.291 0.938 0.136  -0.039 -0.130 168 ARG AAA NE  
1121  C CZ  . ARG A 168 ? 0.987 1.274 0.929 0.129  -0.039 -0.132 168 ARG AAA CZ  
1122  N NH1 . ARG A 168 ? 0.959 1.240 0.896 0.129  -0.038 -0.127 168 ARG AAA NH1 
1123  N NH2 . ARG A 168 ? 0.985 1.280 0.942 0.122  -0.040 -0.140 168 ARG AAA NH2 
1124  N N   . TYR A 169 ? 0.538 0.758 0.434 0.135  -0.026 -0.088 169 TYR AAA N   
1125  C CA  . TYR A 169 ? 0.513 0.723 0.417 0.124  -0.024 -0.084 169 TYR AAA CA  
1126  C C   . TYR A 169 ? 0.512 0.705 0.406 0.124  -0.020 -0.075 169 TYR AAA C   
1127  O O   . TYR A 169 ? 0.516 0.705 0.401 0.132  -0.018 -0.071 169 TYR AAA O   
1128  C CB  . TYR A 169 ? 0.507 0.718 0.418 0.120  -0.025 -0.087 169 TYR AAA CB  
1129  C CG  . TYR A 169 ? 0.513 0.739 0.435 0.118  -0.028 -0.097 169 TYR AAA CG  
1130  C CD1 . TYR A 169 ? 0.529 0.760 0.460 0.112  -0.029 -0.101 169 TYR AAA CD1 
1131  C CD2 . TYR A 169 ? 0.526 0.761 0.447 0.123  -0.030 -0.102 169 TYR AAA CD2 
1132  C CE1 . TYR A 169 ? 0.532 0.777 0.474 0.111  -0.032 -0.111 169 TYR AAA CE1 
1133  C CE2 . TYR A 169 ? 0.524 0.774 0.457 0.122  -0.033 -0.112 169 TYR AAA CE2 
1134  C CZ  . TYR A 169 ? 0.530 0.785 0.473 0.116  -0.033 -0.116 169 TYR AAA CZ  
1135  O OH  . TYR A 169 ? 0.520 0.788 0.475 0.114  -0.036 -0.127 169 TYR AAA OH  
1136  N N   . ILE A 170 ? 0.526 0.712 0.425 0.117  -0.019 -0.072 170 ILE AAA N   
1137  C CA  . ILE A 170 ? 0.531 0.701 0.423 0.115  -0.015 -0.064 170 ILE AAA CA  
1138  C C   . ILE A 170 ? 0.509 0.673 0.409 0.105  -0.014 -0.062 170 ILE AAA C   
1139  O O   . ILE A 170 ? 0.502 0.671 0.411 0.098  -0.016 -0.066 170 ILE AAA O   
1140  C CB  . ILE A 170 ? 0.532 0.700 0.421 0.116  -0.014 -0.062 170 ILE AAA CB  
1141  C CG1 . ILE A 170 ? 0.555 0.730 0.437 0.127  -0.014 -0.063 170 ILE AAA CG1 
1142  C CG2 . ILE A 170 ? 0.539 0.692 0.424 0.114  -0.010 -0.054 170 ILE AAA CG2 
1143  C CD1 . ILE A 170 ? 0.557 0.732 0.437 0.128  -0.014 -0.063 170 ILE AAA CD1 
1144  N N   . LEU A 171 ? 0.480 0.633 0.376 0.104  -0.011 -0.056 171 LEU AAA N   
1145  C CA  . LEU A 171 ? 0.466 0.612 0.368 0.095  -0.010 -0.054 171 LEU AAA CA  
1146  C C   . LEU A 171 ? 0.457 0.591 0.355 0.093  -0.006 -0.048 171 LEU AAA C   
1147  O O   . LEU A 171 ? 0.460 0.587 0.349 0.098  -0.004 -0.044 171 LEU AAA O   
1148  C CB  . LEU A 171 ? 0.480 0.624 0.382 0.095  -0.010 -0.054 171 LEU AAA CB  
1149  C CG  . LEU A 171 ? 0.488 0.623 0.394 0.087  -0.008 -0.050 171 LEU AAA CG  
1150  C CD1 . LEU A 171 ? 0.491 0.631 0.408 0.079  -0.010 -0.052 171 LEU AAA CD1 
1151  C CD2 . LEU A 171 ? 0.494 0.629 0.400 0.088  -0.008 -0.050 171 LEU AAA CD2 
1152  N N   . LEU A 172 ? 0.431 0.564 0.335 0.086  -0.006 -0.047 172 LEU AAA N   
1153  C CA  . LEU A 172 ? 0.426 0.548 0.328 0.082  -0.003 -0.042 172 LEU AAA CA  
1154  C C   . LEU A 172 ? 0.409 0.525 0.314 0.076  -0.002 -0.040 172 LEU AAA C   
1155  O O   . LEU A 172 ? 0.388 0.509 0.301 0.071  -0.004 -0.042 172 LEU AAA O   
1156  C CB  . LEU A 172 ? 0.424 0.550 0.330 0.078  -0.004 -0.043 172 LEU AAA CB  
1157  C CG  . LEU A 172 ? 0.424 0.558 0.328 0.083  -0.005 -0.047 172 LEU AAA CG  
1158  C CD1 . LEU A 172 ? 0.447 0.585 0.357 0.078  -0.006 -0.048 172 LEU AAA CD1 
1159  C CD2 . LEU A 172 ? 0.412 0.540 0.307 0.091  -0.003 -0.044 172 LEU AAA CD2 
1160  N N   . ALA A 173 ? 0.413 0.519 0.312 0.078  0.001  -0.036 173 ALA AAA N   
1161  C CA  . ALA A 173 ? 0.418 0.517 0.320 0.072  0.003  -0.033 173 ALA AAA CA  
1162  C C   . ALA A 173 ? 0.425 0.514 0.322 0.073  0.007  -0.029 173 ALA AAA C   
1163  O O   . ALA A 173 ? 0.412 0.494 0.305 0.075  0.009  -0.026 173 ALA AAA O   
1164  C CB  . ALA A 173 ? 0.441 0.541 0.342 0.074  0.002  -0.033 173 ALA AAA CB  
1165  N N   . THR A 174 ? 0.430 0.519 0.328 0.071  0.008  -0.029 174 THR AAA N   
1166  C CA  . THR A 174 ? 0.437 0.516 0.331 0.072  0.012  -0.026 174 THR AAA CA  
1167  C C   . THR A 174 ? 0.417 0.492 0.316 0.065  0.014  -0.024 174 THR AAA C   
1168  O O   . THR A 174 ? 0.396 0.463 0.292 0.065  0.018  -0.023 174 THR AAA O   
1169  C CB  . THR A 174 ? 0.440 0.523 0.333 0.074  0.012  -0.027 174 THR AAA CB  
1170  O OG1 . THR A 174 ? 0.416 0.507 0.316 0.068  0.009  -0.030 174 THR AAA OG1 
1171  C CG2 . THR A 174 ? 0.472 0.557 0.359 0.082  0.011  -0.028 174 THR AAA CG2 
1172  N N   . GLY A 175 ? 0.427 0.506 0.331 0.059  0.011  -0.025 175 GLY AAA N   
1173  C CA  . GLY A 175 ? 0.405 0.481 0.313 0.053  0.012  -0.024 175 GLY AAA CA  
1174  C C   . GLY A 175 ? 0.415 0.493 0.326 0.049  0.013  -0.024 175 GLY AAA C   
1175  O O   . GLY A 175 ? 0.409 0.490 0.319 0.051  0.013  -0.026 175 GLY AAA O   
1176  N N   . GLY A 176 ? 0.423 0.498 0.337 0.044  0.015  -0.023 176 GLY AAA N   
1177  C CA  . GLY A 176 ? 0.415 0.490 0.331 0.041  0.016  -0.024 176 GLY AAA CA  
1178  C C   . GLY A 176 ? 0.427 0.493 0.340 0.042  0.021  -0.023 176 GLY AAA C   
1179  O O   . GLY A 176 ? 0.413 0.472 0.323 0.045  0.023  -0.022 176 GLY AAA O   
1180  N N   . ARG A 177 ? 0.428 0.495 0.344 0.039  0.022  -0.025 177 ARG AAA N   
1181  C CA  . ARG A 177 ? 0.436 0.496 0.352 0.037  0.026  -0.025 177 ARG AAA CA  
1182  C C   . ARG A 177 ? 0.434 0.501 0.357 0.031  0.026  -0.027 177 ARG AAA C   
1183  O O   . ARG A 177 ? 0.407 0.482 0.332 0.029  0.023  -0.027 177 ARG AAA O   
1184  C CB  . ARG A 177 ? 0.435 0.491 0.349 0.042  0.030  -0.026 177 ARG AAA CB  
1185  C CG  . ARG A 177 ? 0.456 0.506 0.364 0.048  0.031  -0.024 177 ARG AAA CG  
1186  C CD  . ARG A 177 ? 0.459 0.501 0.364 0.049  0.033  -0.021 177 ARG AAA CD  
1187  N NE  . ARG A 177 ? 0.463 0.497 0.369 0.049  0.039  -0.022 177 ARG AAA NE  
1188  C CZ  . ARG A 177 ? 0.443 0.469 0.346 0.053  0.043  -0.021 177 ARG AAA CZ  
1189  N NH1 . ARG A 177 ? 0.458 0.484 0.355 0.059  0.043  -0.019 177 ARG AAA NH1 
1190  N NH2 . ARG A 177 ? 0.445 0.463 0.350 0.052  0.049  -0.021 177 ARG AAA NH2 
1191  N N   . PRO A 178 ? 0.433 0.495 0.358 0.029  0.029  -0.027 178 PRO AAA N   
1192  C CA  . PRO A 178 ? 0.458 0.527 0.388 0.024  0.028  -0.029 178 PRO AAA CA  
1193  C C   . PRO A 178 ? 0.494 0.569 0.425 0.023  0.028  -0.032 178 PRO AAA C   
1194  O O   . PRO A 178 ? 0.422 0.494 0.352 0.026  0.030  -0.033 178 PRO AAA O   
1195  C CB  . PRO A 178 ? 0.466 0.527 0.397 0.023  0.033  -0.031 178 PRO AAA CB  
1196  C CG  . PRO A 178 ? 0.456 0.507 0.383 0.026  0.035  -0.028 178 PRO AAA CG  
1197  C CD  . PRO A 178 ? 0.442 0.493 0.364 0.031  0.033  -0.026 178 PRO AAA CD  
1198  N N   . SER A 179 ? 0.520 0.605 0.455 0.020  0.025  -0.032 179 SER AAA N   
1199  C CA  . SER A 179 ? 0.571 0.664 0.508 0.019  0.024  -0.035 179 SER AAA CA  
1200  C C   . SER A 179 ? 0.571 0.667 0.513 0.015  0.026  -0.039 179 SER AAA C   
1201  O O   . SER A 179 ? 0.480 0.578 0.424 0.013  0.026  -0.038 179 SER AAA O   
1202  C CB  . SER A 179 ? 0.586 0.689 0.525 0.018  0.020  -0.034 179 SER AAA CB  
1203  O OG  . SER A 179 ? 0.607 0.716 0.546 0.018  0.020  -0.036 179 SER AAA OG  
1204  N N   . ILE A 180 ? 0.596 0.692 0.538 0.016  0.029  -0.042 180 ILE AAA N   
1205  C CA  . ILE A 180 ? 0.613 0.714 0.560 0.013  0.031  -0.047 180 ILE AAA CA  
1206  C C   . ILE A 180 ? 0.608 0.719 0.557 0.012  0.029  -0.049 180 ILE AAA C   
1207  O O   . ILE A 180 ? 0.612 0.722 0.559 0.015  0.029  -0.050 180 ILE AAA O   
1208  C CB  . ILE A 180 ? 0.638 0.728 0.586 0.014  0.036  -0.050 180 ILE AAA CB  
1209  C CG1 . ILE A 180 ? 0.606 0.685 0.552 0.015  0.039  -0.047 180 ILE AAA CG1 
1210  C CG2 . ILE A 180 ? 0.663 0.760 0.618 0.010  0.038  -0.056 180 ILE AAA CG2 
1211  C CD1 . ILE A 180 ? 0.606 0.675 0.554 0.016  0.045  -0.050 180 ILE AAA CD1 
1212  N N   . PRO A 181 ? 0.622 0.745 0.575 0.009  0.027  -0.051 181 PRO AAA N   
1213  C CA  . PRO A 181 ? 0.609 0.743 0.563 0.009  0.025  -0.054 181 PRO AAA CA  
1214  C C   . PRO A 181 ? 0.594 0.727 0.551 0.009  0.029  -0.059 181 PRO AAA C   
1215  O O   . PRO A 181 ? 0.560 0.692 0.521 0.008  0.032  -0.063 181 PRO AAA O   
1216  C CB  . PRO A 181 ? 0.597 0.743 0.555 0.006  0.024  -0.054 181 PRO AAA CB  
1217  C CG  . PRO A 181 ? 0.606 0.746 0.566 0.004  0.026  -0.055 181 PRO AAA CG  
1218  C CD  . PRO A 181 ? 0.621 0.748 0.576 0.007  0.027  -0.051 181 PRO AAA CD  
1219  N N   . GLU A 182 ? 0.624 0.757 0.579 0.012  0.028  -0.059 182 GLU AAA N   
1220  C CA  . GLU A 182 ? 0.680 0.812 0.637 0.013  0.030  -0.064 182 GLU AAA CA  
1221  C C   . GLU A 182 ? 0.661 0.806 0.622 0.010  0.030  -0.069 182 GLU AAA C   
1222  O O   . GLU A 182 ? 0.685 0.830 0.650 0.009  0.033  -0.075 182 GLU AAA O   
1223  C CB  . GLU A 182 ? 0.742 0.872 0.694 0.016  0.029  -0.062 182 GLU AAA CB  
1224  C CG  . GLU A 182 ? 0.880 0.998 0.827 0.019  0.030  -0.057 182 GLU AAA CG  
1225  C CD  . GLU A 182 ? 0.972 1.081 0.916 0.024  0.032  -0.058 182 GLU AAA CD  
1226  O OE1 . GLU A 182 ? 0.917 1.030 0.864 0.024  0.033  -0.062 182 GLU AAA OE1 
1227  O OE2 . GLU A 182 ? 0.994 1.094 0.934 0.027  0.033  -0.054 182 GLU AAA OE2 
1228  N N   . THR A 183 ? 0.584 0.741 0.546 0.008  0.026  -0.067 183 THR AAA N   
1229  C CA  . THR A 183 ? 0.641 0.814 0.607 0.006  0.025  -0.071 183 THR AAA CA  
1230  C C   . THR A 183 ? 0.649 0.824 0.620 0.004  0.027  -0.077 183 THR AAA C   
1231  O O   . THR A 183 ? 0.701 0.885 0.676 0.003  0.028  -0.083 183 THR AAA O   
1232  C CB  . THR A 183 ? 0.660 0.843 0.624 0.006  0.021  -0.067 183 THR AAA CB  
1233  O OG1 . THR A 183 ? 0.651 0.831 0.613 0.005  0.020  -0.063 183 THR AAA OG1 
1234  C CG2 . THR A 183 ? 0.650 0.830 0.609 0.008  0.019  -0.062 183 THR AAA CG2 
1235  N N   . VAL A 184 ? 0.576 0.743 0.546 0.003  0.029  -0.075 184 VAL AAA N   
1236  C CA  . VAL A 184 ? 0.534 0.704 0.510 0.000  0.031  -0.080 184 VAL AAA CA  
1237  C C   . VAL A 184 ? 0.521 0.681 0.501 0.000  0.036  -0.085 184 VAL AAA C   
1238  O O   . VAL A 184 ? 0.559 0.704 0.536 0.002  0.039  -0.083 184 VAL AAA O   
1239  C CB  . VAL A 184 ? 0.491 0.658 0.466 -0.000 0.030  -0.076 184 VAL AAA CB  
1240  C CG1 . VAL A 184 ? 0.478 0.645 0.458 -0.003 0.033  -0.082 184 VAL AAA CG1 
1241  C CG2 . VAL A 184 ? 0.468 0.646 0.441 -0.000 0.026  -0.071 184 VAL AAA CG2 
1242  N N   . PRO A 185 ? 0.535 0.702 0.520 -0.001 0.038  -0.093 185 PRO AAA N   
1243  C CA  . PRO A 185 ? 0.523 0.680 0.513 -0.002 0.044  -0.099 185 PRO AAA CA  
1244  C C   . PRO A 185 ? 0.489 0.636 0.482 -0.003 0.048  -0.100 185 PRO AAA C   
1245  O O   . PRO A 185 ? 0.463 0.617 0.459 -0.005 0.047  -0.101 185 PRO AAA O   
1246  C CB  . PRO A 185 ? 0.527 0.697 0.524 -0.003 0.045  -0.108 185 PRO AAA CB  
1247  C CG  . PRO A 185 ? 0.538 0.725 0.533 -0.003 0.039  -0.106 185 PRO AAA CG  
1248  C CD  . PRO A 185 ? 0.533 0.718 0.522 -0.003 0.036  -0.098 185 PRO AAA CD  
1249  N N   . GLY A 186 ? 0.472 0.603 0.465 -0.001 0.053  -0.099 186 GLY AAA N   
1250  C CA  . GLY A 186 ? 0.490 0.608 0.484 -0.002 0.058  -0.099 186 GLY AAA CA  
1251  C C   . GLY A 186 ? 0.492 0.602 0.480 -0.000 0.056  -0.090 186 GLY AAA C   
1252  O O   . GLY A 186 ? 0.497 0.594 0.485 -0.000 0.060  -0.089 186 GLY AAA O   
1253  N N   . ALA A 187 ? 0.490 0.605 0.471 0.001  0.050  -0.085 187 ALA AAA N   
1254  C CA  . ALA A 187 ? 0.485 0.594 0.460 0.002  0.048  -0.077 187 ALA AAA CA  
1255  C C   . ALA A 187 ? 0.505 0.599 0.476 0.005  0.051  -0.073 187 ALA AAA C   
1256  O O   . ALA A 187 ? 0.503 0.587 0.473 0.005  0.053  -0.071 187 ALA AAA O   
1257  C CB  . ALA A 187 ? 0.476 0.595 0.447 0.003  0.041  -0.073 187 ALA AAA CB  
1258  N N   . ILE A 188 ? 0.523 0.613 0.490 0.009  0.051  -0.072 188 ILE AAA N   
1259  C CA  . ILE A 188 ? 0.545 0.622 0.507 0.013  0.053  -0.067 188 ILE AAA CA  
1260  C C   . ILE A 188 ? 0.549 0.614 0.516 0.013  0.061  -0.069 188 ILE AAA C   
1261  O O   . ILE A 188 ? 0.591 0.644 0.553 0.016  0.063  -0.065 188 ILE AAA O   
1262  C CB  . ILE A 188 ? 0.554 0.633 0.514 0.016  0.052  -0.066 188 ILE AAA CB  
1263  C CG1 . ILE A 188 ? 0.548 0.633 0.502 0.017  0.046  -0.062 188 ILE AAA CG1 
1264  C CG2 . ILE A 188 ? 0.538 0.603 0.495 0.020  0.057  -0.065 188 ILE AAA CG2 
1265  C CD1 . ILE A 188 ? 0.558 0.649 0.510 0.019  0.043  -0.062 188 ILE AAA CD1 
1266  N N   . GLN A 189 ? 0.578 0.645 0.551 0.010  0.064  -0.076 189 GLN AAA N   
1267  C CA  . GLN A 189 ? 0.602 0.658 0.580 0.010  0.072  -0.080 189 GLN AAA CA  
1268  C C   . GLN A 189 ? 0.581 0.633 0.562 0.008  0.074  -0.080 189 GLN AAA C   
1269  O O   . GLN A 189 ? 0.545 0.583 0.526 0.010  0.080  -0.077 189 GLN AAA O   
1270  C CB  . GLN A 189 ? 0.604 0.666 0.591 0.008  0.075  -0.088 189 GLN AAA CB  
1271  C CG  . GLN A 189 ? 0.625 0.674 0.617 0.009  0.084  -0.090 189 GLN AAA CG  
1272  C CD  . GLN A 189 ? 0.626 0.680 0.629 0.006  0.087  -0.100 189 GLN AAA CD  
1273  O OE1 . GLN A 189 ? 0.558 0.625 0.563 0.004  0.084  -0.105 189 GLN AAA OE1 
1274  N NE2 . GLN A 189 ? 0.633 0.677 0.643 0.004  0.095  -0.104 189 GLN AAA NE2 
1275  N N   . TYR A 190 ? 0.565 0.628 0.549 0.004  0.071  -0.082 190 TYR AAA N   
1276  C CA  . TYR A 190 ? 0.566 0.628 0.555 0.000  0.073  -0.085 190 TYR AAA CA  
1277  C C   . TYR A 190 ? 0.520 0.582 0.504 0.001  0.069  -0.079 190 TYR AAA C   
1278  O O   . TYR A 190 ? 0.522 0.578 0.508 -0.001 0.073  -0.080 190 TYR AAA O   
1279  C CB  . TYR A 190 ? 0.589 0.665 0.587 -0.004 0.073  -0.094 190 TYR AAA CB  
1280  C CG  . TYR A 190 ? 0.634 0.709 0.639 -0.005 0.078  -0.101 190 TYR AAA CG  
1281  C CD1 . TYR A 190 ? 0.651 0.711 0.660 -0.005 0.086  -0.103 190 TYR AAA CD1 
1282  C CD2 . TYR A 190 ? 0.657 0.745 0.666 -0.006 0.076  -0.107 190 TYR AAA CD2 
1283  C CE1 . TYR A 190 ? 0.657 0.717 0.675 -0.005 0.092  -0.110 190 TYR AAA CE1 
1284  C CE2 . TYR A 190 ? 0.651 0.739 0.668 -0.007 0.081  -0.114 190 TYR AAA CE2 
1285  C CZ  . TYR A 190 ? 0.679 0.753 0.701 -0.007 0.089  -0.116 190 TYR AAA CZ  
1286  O OH  . TYR A 190 ? 0.735 0.807 0.765 -0.008 0.094  -0.123 190 TYR AAA OH  
1287  N N   . SER A 191 ? 0.490 0.557 0.467 0.002  0.063  -0.074 191 SER AAA N   
1288  C CA  . SER A 191 ? 0.461 0.529 0.433 0.002  0.059  -0.068 191 SER AAA CA  
1289  C C   . SER A 191 ? 0.432 0.488 0.398 0.006  0.060  -0.062 191 SER AAA C   
1290  O O   . SER A 191 ? 0.428 0.478 0.390 0.010  0.061  -0.060 191 SER AAA O   
1291  C CB  . SER A 191 ? 0.457 0.538 0.427 0.002  0.052  -0.066 191 SER AAA CB  
1292  O OG  . SER A 191 ? 0.508 0.587 0.472 0.005  0.050  -0.062 191 SER AAA OG  
1293  N N   . ILE A 192 ? 0.434 0.486 0.397 0.006  0.059  -0.059 192 ILE AAA N   
1294  C CA  . ILE A 192 ? 0.429 0.471 0.386 0.009  0.059  -0.052 192 ILE AAA CA  
1295  C C   . ILE A 192 ? 0.413 0.463 0.366 0.010  0.052  -0.048 192 ILE AAA C   
1296  O O   . ILE A 192 ? 0.391 0.453 0.346 0.007  0.048  -0.049 192 ILE AAA O   
1297  C CB  . ILE A 192 ? 0.448 0.482 0.406 0.008  0.063  -0.052 192 ILE AAA CB  
1298  C CG1 . ILE A 192 ? 0.448 0.489 0.410 0.004  0.061  -0.053 192 ILE AAA CG1 
1299  C CG2 . ILE A 192 ? 0.478 0.503 0.441 0.008  0.071  -0.056 192 ILE AAA CG2 
1300  C CD1 . ILE A 192 ? 0.440 0.473 0.402 0.004  0.064  -0.051 192 ILE AAA CD1 
1301  N N   . THR A 193 ? 0.402 0.446 0.349 0.013  0.051  -0.042 193 THR AAA N   
1302  C CA  . THR A 193 ? 0.379 0.427 0.322 0.014  0.046  -0.038 193 THR AAA CA  
1303  C C   . THR A 193 ? 0.379 0.420 0.319 0.015  0.046  -0.035 193 THR AAA C   
1304  O O   . THR A 193 ? 0.372 0.404 0.313 0.015  0.051  -0.035 193 THR AAA O   
1305  C CB  . THR A 193 ? 0.378 0.428 0.316 0.018  0.043  -0.036 193 THR AAA CB  
1306  O OG1 . THR A 193 ? 0.364 0.403 0.298 0.022  0.046  -0.034 193 THR AAA OG1 
1307  C CG2 . THR A 193 ? 0.377 0.434 0.318 0.016  0.043  -0.040 193 THR AAA CG2 
1308  N N   . SER A 194 ? 0.387 0.430 0.324 0.016  0.042  -0.031 194 SER AAA N   
1309  C CA  . SER A 194 ? 0.369 0.406 0.303 0.018  0.042  -0.028 194 SER AAA CA  
1310  C C   . SER A 194 ? 0.361 0.388 0.289 0.023  0.046  -0.026 194 SER AAA C   
1311  O O   . SER A 194 ? 0.356 0.376 0.282 0.025  0.048  -0.024 194 SER AAA O   
1312  C CB  . SER A 194 ? 0.362 0.406 0.295 0.018  0.036  -0.025 194 SER AAA CB  
1313  O OG  . SER A 194 ? 0.368 0.416 0.298 0.020  0.034  -0.025 194 SER AAA OG  
1314  N N   . ASP A 195 ? 0.337 0.363 0.264 0.026  0.047  -0.026 195 ASP AAA N   
1315  C CA  . ASP A 195 ? 0.348 0.364 0.269 0.031  0.051  -0.024 195 ASP AAA CA  
1316  C C   . ASP A 195 ? 0.368 0.374 0.292 0.031  0.058  -0.025 195 ASP AAA C   
1317  O O   . ASP A 195 ? 0.390 0.387 0.310 0.035  0.062  -0.022 195 ASP AAA O   
1318  C CB  . ASP A 195 ? 0.346 0.364 0.266 0.034  0.051  -0.025 195 ASP AAA CB  
1319  C CG  . ASP A 195 ? 0.339 0.364 0.255 0.037  0.045  -0.023 195 ASP AAA CG  
1320  O OD1 . ASP A 195 ? 0.322 0.351 0.239 0.036  0.041  -0.022 195 ASP AAA OD1 
1321  O OD2 . ASP A 195 ? 0.378 0.404 0.293 0.039  0.045  -0.024 195 ASP AAA OD2 
1322  N N   . ASP A 196 ? 0.375 0.384 0.306 0.026  0.059  -0.029 196 ASP AAA N   
1323  C CA  . ASP A 196 ? 0.407 0.407 0.341 0.025  0.067  -0.031 196 ASP AAA CA  
1324  C C   . ASP A 196 ? 0.408 0.407 0.345 0.021  0.067  -0.032 196 ASP AAA C   
1325  O O   . ASP A 196 ? 0.397 0.386 0.335 0.021  0.074  -0.032 196 ASP AAA O   
1326  C CB  . ASP A 196 ? 0.415 0.419 0.355 0.022  0.069  -0.036 196 ASP AAA CB  
1327  C CG  . ASP A 196 ? 0.444 0.451 0.382 0.025  0.067  -0.036 196 ASP AAA CG  
1328  O OD1 . ASP A 196 ? 0.451 0.450 0.384 0.030  0.070  -0.033 196 ASP AAA OD1 
1329  O OD2 . ASP A 196 ? 0.430 0.447 0.370 0.022  0.062  -0.039 196 ASP AAA OD2 
1330  N N   . ILE A 197 ? 0.389 0.398 0.328 0.017  0.062  -0.033 197 ILE AAA N   
1331  C CA  . ILE A 197 ? 0.401 0.411 0.345 0.013  0.062  -0.035 197 ILE AAA CA  
1332  C C   . ILE A 197 ? 0.394 0.395 0.335 0.015  0.065  -0.031 197 ILE AAA C   
1333  O O   . ILE A 197 ? 0.384 0.382 0.329 0.012  0.069  -0.034 197 ILE AAA O   
1334  C CB  . ILE A 197 ? 0.392 0.414 0.337 0.010  0.056  -0.035 197 ILE AAA CB  
1335  C CG1 . ILE A 197 ? 0.368 0.393 0.318 0.006  0.056  -0.037 197 ILE AAA CG1 
1336  C CG2 . ILE A 197 ? 0.390 0.414 0.330 0.013  0.051  -0.030 197 ILE AAA CG2 
1337  C CD1 . ILE A 197 ? 0.366 0.391 0.323 0.003  0.061  -0.043 197 ILE AAA CD1 
1338  N N   . PHE A 198 ? 0.412 0.409 0.346 0.019  0.064  -0.027 198 PHE AAA N   
1339  C CA  . PHE A 198 ? 0.428 0.417 0.359 0.021  0.066  -0.023 198 PHE AAA CA  
1340  C C   . PHE A 198 ? 0.467 0.445 0.398 0.024  0.074  -0.023 198 PHE AAA C   
1341  O O   . PHE A 198 ? 0.517 0.488 0.445 0.025  0.076  -0.021 198 PHE AAA O   
1342  C CB  . PHE A 198 ? 0.417 0.408 0.342 0.025  0.061  -0.019 198 PHE AAA CB  
1343  C CG  . PHE A 198 ? 0.394 0.397 0.321 0.022  0.054  -0.020 198 PHE AAA CG  
1344  C CD1 . PHE A 198 ? 0.384 0.391 0.315 0.018  0.052  -0.021 198 PHE AAA CD1 
1345  C CD2 . PHE A 198 ? 0.379 0.387 0.303 0.024  0.050  -0.019 198 PHE AAA CD2 
1346  C CE1 . PHE A 198 ? 0.371 0.387 0.303 0.016  0.046  -0.021 198 PHE AAA CE1 
1347  C CE2 . PHE A 198 ? 0.363 0.381 0.289 0.022  0.044  -0.020 198 PHE AAA CE2 
1348  C CZ  . PHE A 198 ? 0.358 0.380 0.288 0.018  0.043  -0.020 198 PHE AAA CZ  
1349  N N   . PHE A 199 ? 0.491 0.465 0.422 0.025  0.078  -0.024 199 PHE AAA N   
1350  C CA  . PHE A 199 ? 0.509 0.471 0.439 0.029  0.086  -0.023 199 PHE AAA CA  
1351  C C   . PHE A 199 ? 0.499 0.458 0.437 0.025  0.091  -0.028 199 PHE AAA C   
1352  O O   . PHE A 199 ? 0.485 0.434 0.423 0.028  0.099  -0.027 199 PHE AAA O   
1353  C CB  . PHE A 199 ? 0.522 0.482 0.445 0.036  0.086  -0.019 199 PHE AAA CB  
1354  C CG  . PHE A 199 ? 0.547 0.511 0.463 0.039  0.079  -0.015 199 PHE AAA CG  
1355  C CD1 . PHE A 199 ? 0.571 0.531 0.484 0.041  0.080  -0.012 199 PHE AAA CD1 
1356  C CD2 . PHE A 199 ? 0.588 0.560 0.501 0.040  0.073  -0.015 199 PHE AAA CD2 
1357  C CE1 . PHE A 199 ? 0.587 0.551 0.494 0.044  0.075  -0.009 199 PHE AAA CE1 
1358  C CE2 . PHE A 199 ? 0.603 0.580 0.511 0.043  0.068  -0.012 199 PHE AAA CE2 
1359  C CZ  . PHE A 199 ? 0.608 0.580 0.513 0.046  0.069  -0.009 199 PHE AAA CZ  
1360  N N   . LEU A 200 ? 0.492 0.460 0.437 0.019  0.089  -0.033 200 LEU AAA N   
1361  C CA  . LEU A 200 ? 0.524 0.491 0.478 0.016  0.094  -0.039 200 LEU AAA CA  
1362  C C   . LEU A 200 ? 0.557 0.512 0.514 0.016  0.103  -0.039 200 LEU AAA C   
1363  O O   . LEU A 200 ? 0.572 0.526 0.528 0.015  0.103  -0.038 200 LEU AAA O   
1364  C CB  . LEU A 200 ? 0.527 0.506 0.487 0.009  0.090  -0.045 200 LEU AAA CB  
1365  C CG  . LEU A 200 ? 0.508 0.499 0.467 0.008  0.083  -0.047 200 LEU AAA CG  
1366  C CD1 . LEU A 200 ? 0.505 0.508 0.472 0.003  0.081  -0.052 200 LEU AAA CD1 
1367  C CD2 . LEU A 200 ? 0.507 0.497 0.467 0.011  0.086  -0.048 200 LEU AAA CD2 
1368  N N   . SER A 201 ? 0.598 0.544 0.558 0.017  0.111  -0.040 201 SER AAA N   
1369  C CA  A SER A 201 ? 0.609 0.543 0.573 0.017  0.120  -0.040 201 SER AAA CA  
1370  C CA  B SER A 201 ? 0.607 0.541 0.570 0.017  0.120  -0.040 201 SER AAA CA  
1371  C C   . SER A 201 ? 0.608 0.547 0.581 0.010  0.121  -0.048 201 SER AAA C   
1372  O O   . SER A 201 ? 0.638 0.571 0.615 0.009  0.126  -0.048 201 SER AAA O   
1373  C CB  A SER A 201 ? 0.617 0.540 0.582 0.020  0.128  -0.040 201 SER AAA CB  
1374  C CB  B SER A 201 ? 0.611 0.535 0.577 0.020  0.128  -0.040 201 SER AAA CB  
1375  O OG  A SER A 201 ? 0.615 0.545 0.587 0.017  0.128  -0.046 201 SER AAA OG  
1376  O OG  B SER A 201 ? 0.609 0.530 0.566 0.027  0.127  -0.034 201 SER AAA OG  
1377  N N   . LYS A 202 ? 0.636 0.587 0.615 0.006  0.116  -0.054 202 LYS AAA N   
1378  C CA  . LYS A 202 ? 0.645 0.605 0.634 -0.001 0.116  -0.062 202 LYS AAA CA  
1379  C C   . LYS A 202 ? 0.609 0.582 0.596 -0.003 0.107  -0.062 202 LYS AAA C   
1380  O O   . LYS A 202 ? 0.553 0.532 0.533 -0.001 0.100  -0.059 202 LYS AAA O   
1381  C CB  . LYS A 202 ? 0.681 0.645 0.679 -0.004 0.119  -0.070 202 LYS AAA CB  
1382  C CG  . LYS A 202 ? 0.717 0.688 0.726 -0.010 0.121  -0.079 202 LYS AAA CG  
1383  C CD  . LYS A 202 ? 0.754 0.738 0.770 -0.013 0.119  -0.087 202 LYS AAA CD  
1384  C CE  . LYS A 202 ? 0.780 0.776 0.789 -0.012 0.109  -0.084 202 LYS AAA CE  
1385  N NZ  . LYS A 202 ? 0.795 0.807 0.810 -0.016 0.104  -0.091 202 LYS AAA NZ  
1386  N N   . SER A 203 ? 0.576 0.553 0.567 -0.007 0.107  -0.065 203 SER AAA N   
1387  C CA  . SER A 203 ? 0.568 0.558 0.558 -0.010 0.098  -0.066 203 SER AAA CA  
1388  C C   . SER A 203 ? 0.572 0.576 0.565 -0.012 0.094  -0.071 203 SER AAA C   
1389  O O   . SER A 203 ? 0.563 0.568 0.564 -0.014 0.098  -0.077 203 SER AAA O   
1390  C CB  . SER A 203 ? 0.559 0.552 0.554 -0.013 0.099  -0.069 203 SER AAA CB  
1391  O OG  . SER A 203 ? 0.586 0.582 0.591 -0.018 0.104  -0.078 203 SER AAA OG  
1392  N N   . PRO A 204 ? 0.557 0.571 0.546 -0.011 0.086  -0.068 204 PRO AAA N   
1393  C CA  . PRO A 204 ? 0.517 0.543 0.507 -0.012 0.082  -0.071 204 PRO AAA CA  
1394  C C   . PRO A 204 ? 0.464 0.503 0.463 -0.016 0.081  -0.080 204 PRO AAA C   
1395  O O   . PRO A 204 ? 0.436 0.485 0.437 -0.017 0.079  -0.083 204 PRO AAA O   
1396  C CB  . PRO A 204 ? 0.535 0.567 0.518 -0.010 0.074  -0.065 204 PRO AAA CB  
1397  C CG  . PRO A 204 ? 0.544 0.572 0.524 -0.010 0.073  -0.062 204 PRO AAA CG  
1398  C CD  . PRO A 204 ? 0.540 0.554 0.522 -0.009 0.081  -0.062 204 PRO AAA CD  
1399  N N   . GLY A 205 ? 0.421 0.462 0.425 -0.019 0.083  -0.083 205 GLY AAA N   
1400  C CA  . GLY A 205 ? 0.387 0.441 0.399 -0.023 0.082  -0.091 205 GLY AAA CA  
1401  C C   . GLY A 205 ? 0.373 0.442 0.382 -0.023 0.074  -0.090 205 GLY AAA C   
1402  O O   . GLY A 205 ? 0.366 0.435 0.368 -0.020 0.069  -0.082 205 GLY AAA O   
1403  N N   . LYS A 206 ? 0.350 0.433 0.366 -0.025 0.073  -0.098 206 LYS AAA N   
1404  C CA  . LYS A 206 ? 0.355 0.455 0.370 -0.025 0.066  -0.097 206 LYS AAA CA  
1405  C C   . LYS A 206 ? 0.354 0.452 0.361 -0.022 0.063  -0.091 206 LYS AAA C   
1406  O O   . LYS A 206 ? 0.364 0.457 0.372 -0.021 0.066  -0.093 206 LYS AAA O   
1407  C CB  . LYS A 206 ? 0.377 0.491 0.400 -0.028 0.067  -0.108 206 LYS AAA CB  
1408  C CG  . LYS A 206 ? 0.393 0.525 0.415 -0.027 0.060  -0.108 206 LYS AAA CG  
1409  C CD  . LYS A 206 ? 0.404 0.553 0.434 -0.029 0.060  -0.118 206 LYS AAA CD  
1410  C CE  . LYS A 206 ? 0.405 0.572 0.433 -0.027 0.054  -0.117 206 LYS AAA CE  
1411  N NZ  . LYS A 206 ? 0.423 0.607 0.459 -0.029 0.054  -0.127 206 LYS AAA NZ  
1412  N N   . THR A 207 ? 0.335 0.436 0.336 -0.020 0.057  -0.084 207 THR AAA N   
1413  C CA  . THR A 207 ? 0.327 0.424 0.320 -0.017 0.054  -0.077 207 THR AAA CA  
1414  C C   . THR A 207 ? 0.320 0.432 0.311 -0.016 0.048  -0.076 207 THR AAA C   
1415  O O   . THR A 207 ? 0.350 0.470 0.341 -0.016 0.045  -0.075 207 THR AAA O   
1416  C CB  . THR A 207 ? 0.326 0.410 0.312 -0.014 0.054  -0.070 207 THR AAA CB  
1417  O OG1 . THR A 207 ? 0.343 0.414 0.331 -0.015 0.060  -0.071 207 THR AAA OG1 
1418  C CG2 . THR A 207 ? 0.327 0.408 0.306 -0.011 0.051  -0.064 207 THR AAA CG2 
1419  N N   . LEU A 208 ? 0.314 0.428 0.303 -0.014 0.047  -0.075 208 LEU AAA N   
1420  C CA  . LEU A 208 ? 0.304 0.429 0.290 -0.013 0.041  -0.071 208 LEU AAA CA  
1421  C C   . LEU A 208 ? 0.302 0.417 0.281 -0.010 0.040  -0.064 208 LEU AAA C   
1422  O O   . LEU A 208 ? 0.301 0.407 0.278 -0.009 0.043  -0.064 208 LEU AAA O   
1423  C CB  . LEU A 208 ? 0.310 0.446 0.300 -0.013 0.041  -0.077 208 LEU AAA CB  
1424  C CG  . LEU A 208 ? 0.299 0.446 0.285 -0.012 0.037  -0.074 208 LEU AAA CG  
1425  C CD1 . LEU A 208 ? 0.291 0.450 0.277 -0.012 0.033  -0.072 208 LEU AAA CD1 
1426  C CD2 . LEU A 208 ? 0.307 0.462 0.297 -0.012 0.037  -0.079 208 LEU AAA CD2 
1427  N N   . VAL A 209 ? 0.292 0.412 0.268 -0.009 0.035  -0.058 209 VAL AAA N   
1428  C CA  . VAL A 209 ? 0.310 0.424 0.279 -0.007 0.033  -0.051 209 VAL AAA CA  
1429  C C   . VAL A 209 ? 0.321 0.447 0.290 -0.006 0.029  -0.050 209 VAL AAA C   
1430  O O   . VAL A 209 ? 0.328 0.465 0.299 -0.007 0.027  -0.049 209 VAL AAA O   
1431  C CB  . VAL A 209 ? 0.295 0.402 0.262 -0.006 0.032  -0.046 209 VAL AAA CB  
1432  C CG1 . VAL A 209 ? 0.294 0.398 0.256 -0.004 0.029  -0.040 209 VAL AAA CG1 
1433  C CG2 . VAL A 209 ? 0.300 0.395 0.267 -0.007 0.036  -0.047 209 VAL AAA CG2 
1434  N N   . ILE A 210 ? 0.349 0.474 0.316 -0.005 0.029  -0.049 210 ILE AAA N   
1435  C CA  . ILE A 210 ? 0.359 0.495 0.325 -0.004 0.025  -0.046 210 ILE AAA CA  
1436  C C   . ILE A 210 ? 0.338 0.468 0.300 -0.002 0.023  -0.040 210 ILE AAA C   
1437  O O   . ILE A 210 ? 0.339 0.459 0.298 -0.001 0.024  -0.039 210 ILE AAA O   
1438  C CB  . ILE A 210 ? 0.387 0.526 0.353 -0.003 0.026  -0.051 210 ILE AAA CB  
1439  C CG1 . ILE A 210 ? 0.398 0.541 0.370 -0.005 0.029  -0.058 210 ILE AAA CG1 
1440  C CG2 . ILE A 210 ? 0.383 0.534 0.349 -0.003 0.023  -0.048 210 ILE AAA CG2 
1441  C CD1 . ILE A 210 ? 0.406 0.536 0.378 -0.005 0.034  -0.062 210 ILE AAA CD1 
1442  N N   . GLY A 211 ? 0.334 0.472 0.296 -0.002 0.020  -0.036 211 GLY AAA N   
1443  C CA  . GLY A 211 ? 0.335 0.470 0.295 -0.001 0.018  -0.030 211 GLY AAA CA  
1444  C C   . GLY A 211 ? 0.354 0.488 0.315 -0.002 0.017  -0.027 211 GLY AAA C   
1445  O O   . GLY A 211 ? 0.372 0.497 0.333 -0.002 0.019  -0.028 211 GLY AAA O   
1446  N N   . ALA A 212 ? 0.346 0.486 0.308 -0.002 0.015  -0.022 212 ALA AAA N   
1447  C CA  . ALA A 212 ? 0.329 0.468 0.292 -0.002 0.014  -0.018 212 ALA AAA CA  
1448  C C   . ALA A 212 ? 0.337 0.469 0.298 -0.001 0.013  -0.014 212 ALA AAA C   
1449  O O   . ALA A 212 ? 0.360 0.493 0.323 -0.001 0.012  -0.010 212 ALA AAA O   
1450  C CB  . ALA A 212 ? 0.330 0.481 0.295 -0.002 0.013  -0.017 212 ALA AAA CB  
1451  N N   . SER A 213 ? 0.352 0.478 0.311 -0.000 0.014  -0.015 213 SER AAA N   
1452  C CA  . SER A 213 ? 0.352 0.469 0.310 0.001  0.013  -0.013 213 SER AAA CA  
1453  C C   . SER A 213 ? 0.323 0.432 0.280 0.001  0.014  -0.013 213 SER AAA C   
1454  O O   . SER A 213 ? 0.306 0.414 0.263 -0.000 0.016  -0.016 213 SER AAA O   
1455  C CB  . SER A 213 ? 0.351 0.464 0.306 0.003  0.014  -0.016 213 SER AAA CB  
1456  O OG  . SER A 213 ? 0.370 0.478 0.324 0.003  0.016  -0.020 213 SER AAA OG  
1457  N N   . TYR A 214 ? 0.324 0.427 0.281 0.002  0.013  -0.011 214 TYR AAA N   
1458  C CA  . TYR A 214 ? 0.349 0.444 0.305 0.002  0.014  -0.011 214 TYR AAA CA  
1459  C C   . TYR A 214 ? 0.360 0.448 0.313 0.003  0.017  -0.014 214 TYR AAA C   
1460  O O   . TYR A 214 ? 0.374 0.458 0.327 0.002  0.018  -0.015 214 TYR AAA O   
1461  C CB  . TYR A 214 ? 0.372 0.464 0.329 0.003  0.013  -0.009 214 TYR AAA CB  
1462  C CG  . TYR A 214 ? 0.388 0.475 0.342 0.006  0.013  -0.010 214 TYR AAA CG  
1463  C CD1 . TYR A 214 ? 0.396 0.474 0.346 0.007  0.014  -0.011 214 TYR AAA CD1 
1464  C CD2 . TYR A 214 ? 0.389 0.478 0.341 0.007  0.012  -0.010 214 TYR AAA CD2 
1465  C CE1 . TYR A 214 ? 0.407 0.480 0.353 0.010  0.015  -0.012 214 TYR AAA CE1 
1466  C CE2 . TYR A 214 ? 0.395 0.480 0.344 0.010  0.012  -0.012 214 TYR AAA CE2 
1467  C CZ  . TYR A 214 ? 0.396 0.472 0.341 0.012  0.013  -0.012 214 TYR AAA CZ  
1468  O OH  . TYR A 214 ? 0.422 0.495 0.364 0.015  0.013  -0.013 214 TYR AAA OH  
1469  N N   . ILE A 215 ? 0.357 0.443 0.307 0.004  0.018  -0.016 215 ILE AAA N   
1470  C CA  . ILE A 215 ? 0.357 0.436 0.304 0.005  0.021  -0.019 215 ILE AAA CA  
1471  C C   . ILE A 215 ? 0.343 0.424 0.293 0.003  0.023  -0.022 215 ILE AAA C   
1472  O O   . ILE A 215 ? 0.360 0.435 0.310 0.003  0.025  -0.023 215 ILE AAA O   
1473  C CB  . ILE A 215 ? 0.357 0.434 0.302 0.008  0.021  -0.020 215 ILE AAA CB  
1474  C CG1 . ILE A 215 ? 0.352 0.425 0.293 0.011  0.020  -0.018 215 ILE AAA CG1 
1475  C CG2 . ILE A 215 ? 0.369 0.439 0.311 0.009  0.025  -0.023 215 ILE AAA CG2 
1476  C CD1 . ILE A 215 ? 0.366 0.440 0.305 0.013  0.019  -0.018 215 ILE AAA CD1 
1477  N N   . GLY A 216 ? 0.353 0.444 0.306 0.002  0.021  -0.023 216 GLY AAA N   
1478  C CA  . GLY A 216 ? 0.330 0.427 0.286 -0.000 0.023  -0.026 216 GLY AAA CA  
1479  C C   . GLY A 216 ? 0.319 0.416 0.277 -0.002 0.023  -0.026 216 GLY AAA C   
1480  O O   . GLY A 216 ? 0.327 0.421 0.286 -0.003 0.025  -0.029 216 GLY AAA O   
1481  N N   . LEU A 217 ? 0.306 0.407 0.265 -0.002 0.020  -0.022 217 LEU AAA N   
1482  C CA  . LEU A 217 ? 0.303 0.406 0.264 -0.004 0.020  -0.021 217 LEU AAA CA  
1483  C C   . LEU A 217 ? 0.317 0.408 0.277 -0.004 0.022  -0.021 217 LEU AAA C   
1484  O O   . LEU A 217 ? 0.332 0.423 0.294 -0.005 0.024  -0.023 217 LEU AAA O   
1485  C CB  . LEU A 217 ? 0.289 0.397 0.251 -0.003 0.017  -0.016 217 LEU AAA CB  
1486  C CG  . LEU A 217 ? 0.298 0.418 0.262 -0.004 0.016  -0.015 217 LEU AAA CG  
1487  C CD1 . LEU A 217 ? 0.303 0.428 0.270 -0.003 0.014  -0.010 217 LEU AAA CD1 
1488  C CD2 . LEU A 217 ? 0.297 0.425 0.263 -0.005 0.016  -0.019 217 LEU AAA CD2 
1489  N N   . GLU A 218 ? 0.314 0.397 0.271 -0.002 0.022  -0.019 218 GLU AAA N   
1490  C CA  . GLU A 218 ? 0.329 0.402 0.284 -0.001 0.024  -0.019 218 GLU AAA CA  
1491  C C   . GLU A 218 ? 0.329 0.398 0.284 -0.002 0.028  -0.023 218 GLU AAA C   
1492  O O   . GLU A 218 ? 0.333 0.398 0.289 -0.003 0.030  -0.024 218 GLU AAA O   
1493  C CB  . GLU A 218 ? 0.349 0.416 0.300 0.002  0.023  -0.017 218 GLU AAA CB  
1494  C CG  . GLU A 218 ? 0.348 0.418 0.300 0.002  0.020  -0.014 218 GLU AAA CG  
1495  C CD  . GLU A 218 ? 0.356 0.420 0.305 0.005  0.020  -0.013 218 GLU AAA CD  
1496  O OE1 . GLU A 218 ? 0.359 0.420 0.304 0.007  0.021  -0.014 218 GLU AAA OE1 
1497  O OE2 . GLU A 218 ? 0.390 0.455 0.340 0.005  0.018  -0.011 218 GLU AAA OE2 
1498  N N   . THR A 219 ? 0.328 0.398 0.282 -0.001 0.029  -0.025 219 THR AAA N   
1499  C CA  . THR A 219 ? 0.308 0.372 0.262 -0.001 0.033  -0.029 219 THR AAA CA  
1500  C C   . THR A 219 ? 0.308 0.378 0.267 -0.004 0.035  -0.033 219 THR AAA C   
1501  O O   . THR A 219 ? 0.278 0.342 0.239 -0.005 0.038  -0.036 219 THR AAA O   
1502  C CB  . THR A 219 ? 0.298 0.363 0.251 0.000  0.034  -0.031 219 THR AAA CB  
1503  O OG1 . THR A 219 ? 0.291 0.352 0.239 0.003  0.032  -0.027 219 THR AAA OG1 
1504  C CG2 . THR A 219 ? 0.317 0.375 0.271 0.000  0.039  -0.034 219 THR AAA CG2 
1505  N N   . ALA A 220 ? 0.306 0.388 0.268 -0.006 0.032  -0.034 220 ALA AAA N   
1506  C CA  . ALA A 220 ? 0.311 0.401 0.278 -0.008 0.032  -0.038 220 ALA AAA CA  
1507  C C   . ALA A 220 ? 0.293 0.381 0.261 -0.009 0.032  -0.037 220 ALA AAA C   
1508  O O   . ALA A 220 ? 0.275 0.363 0.247 -0.011 0.035  -0.041 220 ALA AAA O   
1509  C CB  . ALA A 220 ? 0.315 0.418 0.283 -0.008 0.029  -0.038 220 ALA AAA CB  
1510  N N   . GLY A 221 ? 0.289 0.375 0.254 -0.008 0.030  -0.032 221 GLY AAA N   
1511  C CA  . GLY A 221 ? 0.296 0.381 0.263 -0.009 0.029  -0.030 221 GLY AAA CA  
1512  C C   . GLY A 221 ? 0.304 0.378 0.270 -0.009 0.033  -0.032 221 GLY AAA C   
1513  O O   . GLY A 221 ? 0.309 0.384 0.278 -0.011 0.034  -0.034 221 GLY AAA O   
1514  N N   . PHE A 222 ? 0.306 0.370 0.269 -0.007 0.035  -0.031 222 PHE AAA N   
1515  C CA  . PHE A 222 ? 0.343 0.396 0.304 -0.007 0.039  -0.032 222 PHE AAA CA  
1516  C C   . PHE A 222 ? 0.339 0.392 0.305 -0.009 0.044  -0.038 222 PHE AAA C   
1517  O O   . PHE A 222 ? 0.351 0.400 0.319 -0.010 0.047  -0.040 222 PHE AAA O   
1518  C CB  . PHE A 222 ? 0.356 0.399 0.312 -0.004 0.040  -0.028 222 PHE AAA CB  
1519  C CG  . PHE A 222 ? 0.372 0.412 0.325 -0.001 0.041  -0.028 222 PHE AAA CG  
1520  C CD1 . PHE A 222 ? 0.395 0.429 0.349 -0.002 0.046  -0.032 222 PHE AAA CD1 
1521  C CD2 . PHE A 222 ? 0.377 0.418 0.327 0.001  0.038  -0.025 222 PHE AAA CD2 
1522  C CE1 . PHE A 222 ? 0.406 0.437 0.358 0.001  0.048  -0.032 222 PHE AAA CE1 
1523  C CE2 . PHE A 222 ? 0.390 0.428 0.337 0.003  0.040  -0.025 222 PHE AAA CE2 
1524  C CZ  . PHE A 222 ? 0.396 0.430 0.344 0.003  0.044  -0.029 222 PHE AAA CZ  
1525  N N   . LEU A 223 ? 0.345 0.402 0.312 -0.009 0.044  -0.041 223 LEU AAA N   
1526  C CA  . LEU A 223 ? 0.360 0.418 0.332 -0.011 0.049  -0.047 223 LEU AAA CA  
1527  C C   . LEU A 223 ? 0.364 0.431 0.341 -0.014 0.048  -0.051 223 LEU AAA C   
1528  O O   . LEU A 223 ? 0.378 0.441 0.360 -0.016 0.052  -0.055 223 LEU AAA O   
1529  C CB  . LEU A 223 ? 0.360 0.422 0.332 -0.011 0.049  -0.049 223 LEU AAA CB  
1530  C CG  . LEU A 223 ? 0.375 0.428 0.343 -0.008 0.051  -0.047 223 LEU AAA CG  
1531  C CD1 . LEU A 223 ? 0.381 0.439 0.350 -0.008 0.051  -0.050 223 LEU AAA CD1 
1532  C CD2 . LEU A 223 ? 0.386 0.425 0.353 -0.007 0.057  -0.047 223 LEU AAA CD2 
1533  N N   . ASN A 224 ? 0.357 0.435 0.335 -0.015 0.043  -0.049 224 ASN AAA N   
1534  C CA  . ASN A 224 ? 0.374 0.462 0.357 -0.017 0.042  -0.052 224 ASN AAA CA  
1535  C C   . ASN A 224 ? 0.394 0.474 0.377 -0.017 0.043  -0.051 224 ASN AAA C   
1536  O O   . ASN A 224 ? 0.394 0.476 0.381 -0.020 0.046  -0.056 224 ASN AAA O   
1537  C CB  . ASN A 224 ? 0.366 0.466 0.348 -0.016 0.037  -0.050 224 ASN AAA CB  
1538  C CG  . ASN A 224 ? 0.350 0.461 0.337 -0.017 0.036  -0.053 224 ASN AAA CG  
1539  O OD1 . ASN A 224 ? 0.350 0.470 0.340 -0.019 0.037  -0.059 224 ASN AAA OD1 
1540  N ND2 . ASN A 224 ? 0.354 0.465 0.339 -0.017 0.033  -0.049 224 ASN AAA ND2 
1541  N N   . GLU A 225 ? 0.409 0.482 0.387 -0.016 0.042  -0.045 225 GLU AAA N   
1542  C CA  . GLU A 225 ? 0.417 0.483 0.394 -0.016 0.043  -0.043 225 GLU AAA CA  
1543  C C   . GLU A 225 ? 0.418 0.475 0.397 -0.017 0.049  -0.047 225 GLU AAA C   
1544  O O   . GLU A 225 ? 0.395 0.449 0.377 -0.018 0.051  -0.049 225 GLU AAA O   
1545  C CB  . GLU A 225 ? 0.455 0.515 0.427 -0.013 0.040  -0.037 225 GLU AAA CB  
1546  C CG  . GLU A 225 ? 0.472 0.539 0.445 -0.013 0.036  -0.033 225 GLU AAA CG  
1547  C CD  . GLU A 225 ? 0.489 0.552 0.459 -0.011 0.033  -0.028 225 GLU AAA CD  
1548  O OE1 . GLU A 225 ? 0.511 0.573 0.477 -0.010 0.032  -0.025 225 GLU AAA OE1 
1549  O OE2 . GLU A 225 ? 0.521 0.581 0.491 -0.012 0.033  -0.026 225 GLU AAA OE2 
1550  N N   . LEU A 226 ? 0.418 0.469 0.396 -0.016 0.052  -0.048 226 LEU AAA N   
1551  C CA  . LEU A 226 ? 0.441 0.480 0.419 -0.016 0.058  -0.051 226 LEU AAA CA  
1552  C C   . LEU A 226 ? 0.457 0.501 0.444 -0.020 0.062  -0.059 226 LEU AAA C   
1553  O O   . LEU A 226 ? 0.422 0.457 0.411 -0.020 0.068  -0.061 226 LEU AAA O   
1554  C CB  . LEU A 226 ? 0.431 0.462 0.405 -0.013 0.060  -0.048 226 LEU AAA CB  
1555  C CG  . LEU A 226 ? 0.431 0.454 0.398 -0.010 0.059  -0.041 226 LEU AAA CG  
1556  C CD1 . LEU A 226 ? 0.432 0.449 0.394 -0.006 0.060  -0.039 226 LEU AAA CD1 
1557  C CD2 . LEU A 226 ? 0.412 0.426 0.378 -0.010 0.062  -0.040 226 LEU AAA CD2 
1558  N N   . GLY A 227 ? 0.459 0.518 0.450 -0.021 0.059  -0.062 227 GLY AAA N   
1559  C CA  . GLY A 227 ? 0.469 0.536 0.468 -0.024 0.061  -0.070 227 GLY AAA CA  
1560  C C   . GLY A 227 ? 0.479 0.550 0.480 -0.025 0.062  -0.075 227 GLY AAA C   
1561  O O   . GLY A 227 ? 0.512 0.590 0.521 -0.028 0.065  -0.083 227 GLY AAA O   
1562  N N   . PHE A 228 ? 0.478 0.548 0.475 -0.023 0.060  -0.071 228 PHE AAA N   
1563  C CA  . PHE A 228 ? 0.447 0.522 0.446 -0.023 0.061  -0.076 228 PHE AAA CA  
1564  C C   . PHE A 228 ? 0.421 0.513 0.421 -0.023 0.056  -0.078 228 PHE AAA C   
1565  O O   . PHE A 228 ? 0.424 0.521 0.420 -0.022 0.051  -0.072 228 PHE AAA O   
1566  C CB  . PHE A 228 ? 0.433 0.499 0.427 -0.020 0.062  -0.071 228 PHE AAA CB  
1567  C CG  . PHE A 228 ? 0.435 0.484 0.427 -0.019 0.068  -0.069 228 PHE AAA CG  
1568  C CD1 . PHE A 228 ? 0.438 0.482 0.437 -0.021 0.075  -0.075 228 PHE AAA CD1 
1569  C CD2 . PHE A 228 ? 0.445 0.485 0.430 -0.016 0.067  -0.062 228 PHE AAA CD2 
1570  C CE1 . PHE A 228 ? 0.457 0.486 0.454 -0.020 0.081  -0.073 228 PHE AAA CE1 
1571  C CE2 . PHE A 228 ? 0.434 0.459 0.417 -0.015 0.073  -0.060 228 PHE AAA CE2 
1572  C CZ  . PHE A 228 ? 0.454 0.473 0.443 -0.016 0.080  -0.065 228 PHE AAA CZ  
1573  N N   . ASP A 229 ? 0.415 0.517 0.422 -0.025 0.057  -0.085 229 ASP AAA N   
1574  C CA  . ASP A 229 ? 0.390 0.509 0.398 -0.025 0.053  -0.088 229 ASP AAA CA  
1575  C C   . ASP A 229 ? 0.377 0.497 0.379 -0.022 0.049  -0.082 229 ASP AAA C   
1576  O O   . ASP A 229 ? 0.375 0.489 0.377 -0.022 0.052  -0.083 229 ASP AAA O   
1577  C CB  . ASP A 229 ? 0.402 0.530 0.420 -0.027 0.056  -0.098 229 ASP AAA CB  
1578  C CG  . ASP A 229 ? 0.416 0.564 0.436 -0.027 0.052  -0.102 229 ASP AAA CG  
1579  O OD1 . ASP A 229 ? 0.387 0.541 0.401 -0.025 0.047  -0.096 229 ASP AAA OD1 
1580  O OD2 . ASP A 229 ? 0.448 0.606 0.475 -0.029 0.054  -0.112 229 ASP AAA OD2 
1581  N N   . THR A 230 ? 0.350 0.476 0.348 -0.020 0.044  -0.076 230 THR AAA N   
1582  C CA  . THR A 230 ? 0.350 0.473 0.342 -0.018 0.041  -0.069 230 THR AAA CA  
1583  C C   . THR A 230 ? 0.318 0.457 0.309 -0.017 0.036  -0.068 230 THR AAA C   
1584  O O   . THR A 230 ? 0.293 0.442 0.286 -0.017 0.034  -0.068 230 THR AAA O   
1585  C CB  . THR A 230 ? 0.371 0.484 0.357 -0.016 0.040  -0.061 230 THR AAA CB  
1586  O OG1 . THR A 230 ? 0.403 0.501 0.389 -0.017 0.045  -0.062 230 THR AAA OG1 
1587  C CG2 . THR A 230 ? 0.381 0.492 0.361 -0.014 0.037  -0.055 230 THR AAA CG2 
1588  N N   . THR A 231 ? 0.312 0.452 0.301 -0.015 0.035  -0.067 231 THR AAA N   
1589  C CA  . THR A 231 ? 0.313 0.468 0.301 -0.014 0.031  -0.066 231 THR AAA CA  
1590  C C   . THR A 231 ? 0.320 0.470 0.302 -0.012 0.029  -0.059 231 THR AAA C   
1591  O O   . THR A 231 ? 0.337 0.476 0.318 -0.012 0.032  -0.059 231 THR AAA O   
1592  C CB  . THR A 231 ? 0.321 0.487 0.314 -0.015 0.033  -0.074 231 THR AAA CB  
1593  O OG1 . THR A 231 ? 0.311 0.482 0.309 -0.017 0.035  -0.080 231 THR AAA OG1 
1594  C CG2 . THR A 231 ? 0.320 0.503 0.313 -0.014 0.029  -0.073 231 THR AAA CG2 
1595  N N   . VAL A 232 ? 0.306 0.462 0.285 -0.011 0.026  -0.053 232 VAL AAA N   
1596  C CA  . VAL A 232 ? 0.317 0.471 0.292 -0.009 0.024  -0.048 232 VAL AAA CA  
1597  C C   . VAL A 232 ? 0.341 0.509 0.317 -0.008 0.021  -0.048 232 VAL AAA C   
1598  O O   . VAL A 232 ? 0.376 0.557 0.354 -0.007 0.020  -0.048 232 VAL AAA O   
1599  C CB  . VAL A 232 ? 0.319 0.468 0.291 -0.008 0.021  -0.040 232 VAL AAA CB  
1600  C CG1 . VAL A 232 ? 0.295 0.445 0.265 -0.006 0.019  -0.035 232 VAL AAA CG1 
1601  C CG2 . VAL A 232 ? 0.314 0.449 0.285 -0.008 0.023  -0.039 232 VAL AAA CG2 
1602  N N   . ALA A 233 ? 0.332 0.500 0.307 -0.007 0.022  -0.050 233 ALA AAA N   
1603  C CA  . ALA A 233 ? 0.345 0.525 0.320 -0.006 0.020  -0.050 233 ALA AAA CA  
1604  C C   . ALA A 233 ? 0.357 0.534 0.328 -0.005 0.017  -0.042 233 ALA AAA C   
1605  O O   . ALA A 233 ? 0.334 0.501 0.303 -0.004 0.018  -0.040 233 ALA AAA O   
1606  C CB  . ALA A 233 ? 0.344 0.524 0.320 -0.007 0.022  -0.056 233 ALA AAA CB  
1607  N N   . MET A 234 ? 0.361 0.547 0.332 -0.004 0.015  -0.037 234 MET AAA N   
1608  C CA  . MET A 234 ? 0.374 0.560 0.343 -0.002 0.013  -0.030 234 MET AAA CA  
1609  C C   . MET A 234 ? 0.396 0.594 0.364 -0.001 0.012  -0.029 234 MET AAA C   
1610  O O   . MET A 234 ? 0.401 0.613 0.371 -0.000 0.011  -0.030 234 MET AAA O   
1611  C CB  . MET A 234 ? 0.391 0.578 0.360 -0.002 0.013  -0.025 234 MET AAA CB  
1612  C CG  . MET A 234 ? 0.397 0.585 0.366 -0.001 0.011  -0.018 234 MET AAA CG  
1613  S SD  . MET A 234 ? 0.404 0.586 0.374 -0.001 0.011  -0.013 234 MET AAA SD  
1614  C CE  . MET A 234 ? 0.451 0.648 0.423 0.000  0.011  -0.015 234 MET AAA CE  
1615  N N   . ARG A 235 ? 0.419 0.613 0.386 -0.000 0.012  -0.027 235 ARG AAA N   
1616  C CA  . ARG A 235 ? 0.442 0.647 0.408 0.001  0.011  -0.026 235 ARG AAA CA  
1617  C C   . ARG A 235 ? 0.450 0.664 0.417 0.002  0.010  -0.020 235 ARG AAA C   
1618  O O   . ARG A 235 ? 0.502 0.731 0.470 0.004  0.009  -0.020 235 ARG AAA O   
1619  C CB  . ARG A 235 ? 0.465 0.663 0.430 0.001  0.011  -0.025 235 ARG AAA CB  
1620  C CG  . ARG A 235 ? 0.511 0.721 0.476 0.002  0.010  -0.026 235 ARG AAA CG  
1621  C CD  . ARG A 235 ? 0.542 0.745 0.505 0.002  0.010  -0.028 235 ARG AAA CD  
1622  N NE  . ARG A 235 ? 0.562 0.777 0.525 0.003  0.010  -0.031 235 ARG AAA NE  
1623  C CZ  . ARG A 235 ? 0.585 0.812 0.549 0.004  0.009  -0.027 235 ARG AAA CZ  
1624  N NH1 . ARG A 235 ? 0.580 0.806 0.544 0.005  0.008  -0.020 235 ARG AAA NH1 
1625  N NH2 . ARG A 235 ? 0.587 0.824 0.550 0.004  0.008  -0.030 235 ARG AAA NH2 
1626  N N   . SER A 236 ? 0.402 0.610 0.369 0.002  0.009  -0.014 236 SER AAA N   
1627  C CA  . SER A 236 ? 0.371 0.585 0.338 0.004  0.009  -0.007 236 SER AAA CA  
1628  C C   . SER A 236 ? 0.365 0.572 0.334 0.003  0.009  -0.004 236 SER AAA C   
1629  O O   . SER A 236 ? 0.349 0.562 0.319 0.004  0.009  -0.004 236 SER AAA O   
1630  C CB  . SER A 236 ? 0.352 0.566 0.320 0.005  0.009  -0.002 236 SER AAA CB  
1631  O OG  . SER A 236 ? 0.333 0.534 0.301 0.003  0.009  -0.003 236 SER AAA OG  
1632  N N   . ILE A 237 ? 0.364 0.559 0.333 0.003  0.009  -0.001 237 ILE AAA N   
1633  C CA  . ILE A 237 ? 0.354 0.543 0.325 0.002  0.010  0.003  237 ILE AAA CA  
1634  C C   . ILE A 237 ? 0.331 0.506 0.301 0.001  0.010  0.000  237 ILE AAA C   
1635  O O   . ILE A 237 ? 0.355 0.524 0.323 0.001  0.010  -0.003 237 ILE AAA O   
1636  C CB  . ILE A 237 ? 0.345 0.534 0.318 0.003  0.010  0.010  237 ILE AAA CB  
1637  C CG1 . ILE A 237 ? 0.355 0.537 0.327 0.003  0.010  0.010  237 ILE AAA CG1 
1638  C CG2 . ILE A 237 ? 0.345 0.548 0.318 0.005  0.010  0.014  237 ILE AAA CG2 
1639  C CD1 . ILE A 237 ? 0.373 0.555 0.349 0.003  0.011  0.016  237 ILE AAA CD1 
1640  N N   . PRO A 238 ? 0.332 0.502 0.303 0.000  0.010  0.001  238 PRO AAA N   
1641  C CA  . PRO A 238 ? 0.322 0.479 0.292 -0.001 0.011  -0.001 238 PRO AAA CA  
1642  C C   . PRO A 238 ? 0.309 0.458 0.280 -0.001 0.010  0.003  238 PRO AAA C   
1643  O O   . PRO A 238 ? 0.318 0.470 0.291 -0.000 0.010  0.008  238 PRO AAA O   
1644  C CB  . PRO A 238 ? 0.310 0.466 0.281 -0.001 0.011  -0.000 238 PRO AAA CB  
1645  C CG  . PRO A 238 ? 0.310 0.477 0.284 0.000  0.010  0.005  238 PRO AAA CG  
1646  C CD  . PRO A 238 ? 0.327 0.503 0.300 0.001  0.010  0.005  238 PRO AAA CD  
1647  N N   . LEU A 239 ? 0.301 0.441 0.270 -0.001 0.011  -0.000 239 LEU AAA N   
1648  C CA  . LEU A 239 ? 0.306 0.439 0.276 -0.000 0.010  0.002  239 LEU AAA CA  
1649  C C   . LEU A 239 ? 0.318 0.456 0.290 -0.000 0.010  0.005  239 LEU AAA C   
1650  O O   . LEU A 239 ? 0.313 0.451 0.289 -0.000 0.010  0.009  239 LEU AAA O   
1651  C CB  . LEU A 239 ? 0.318 0.446 0.289 -0.001 0.010  0.004  239 LEU AAA CB  
1652  C CG  . LEU A 239 ? 0.324 0.446 0.293 -0.001 0.011  0.000  239 LEU AAA CG  
1653  C CD1 . LEU A 239 ? 0.319 0.436 0.290 -0.002 0.011  0.003  239 LEU AAA CD1 
1654  C CD2 . LEU A 239 ? 0.343 0.458 0.309 -0.001 0.012  -0.003 239 LEU AAA CD2 
1655  N N   . ARG A 240 ? 0.323 0.467 0.294 0.000  0.010  0.004  240 ARG AAA N   
1656  C CA  . ARG A 240 ? 0.332 0.481 0.305 0.001  0.010  0.007  240 ARG AAA CA  
1657  C C   . ARG A 240 ? 0.335 0.477 0.311 0.001  0.010  0.008  240 ARG AAA C   
1658  O O   . ARG A 240 ? 0.319 0.455 0.293 0.001  0.009  0.005  240 ARG AAA O   
1659  C CB  . ARG A 240 ? 0.344 0.498 0.315 0.001  0.009  0.004  240 ARG AAA CB  
1660  C CG  . ARG A 240 ? 0.374 0.535 0.347 0.002  0.010  0.007  240 ARG AAA CG  
1661  C CD  . ARG A 240 ? 0.377 0.544 0.348 0.002  0.009  0.004  240 ARG AAA CD  
1662  N NE  . ARG A 240 ? 0.384 0.558 0.353 0.002  0.009  0.004  240 ARG AAA NE  
1663  C CZ  . ARG A 240 ? 0.386 0.571 0.357 0.003  0.010  0.007  240 ARG AAA CZ  
1664  N NH1 . ARG A 240 ? 0.406 0.593 0.380 0.003  0.010  0.012  240 ARG AAA NH1 
1665  N NH2 . ARG A 240 ? 0.379 0.572 0.348 0.004  0.009  0.006  240 ARG AAA NH2 
1666  N N   . GLY A 241 ? 0.365 0.510 0.347 0.000  0.010  0.012  241 GLY AAA N   
1667  C CA  . GLY A 241 ? 0.376 0.516 0.361 -0.000 0.011  0.013  241 GLY AAA CA  
1668  C C   . GLY A 241 ? 0.377 0.512 0.365 -0.001 0.011  0.015  241 GLY AAA C   
1669  O O   . GLY A 241 ? 0.388 0.522 0.383 -0.001 0.012  0.017  241 GLY AAA O   
1670  N N   . PHE A 242 ? 0.362 0.495 0.348 -0.001 0.011  0.014  242 PHE AAA N   
1671  C CA  . PHE A 242 ? 0.341 0.469 0.329 -0.001 0.011  0.016  242 PHE AAA CA  
1672  C C   . PHE A 242 ? 0.323 0.457 0.315 -0.001 0.012  0.021  242 PHE AAA C   
1673  O O   . PHE A 242 ? 0.289 0.430 0.279 -0.001 0.013  0.023  242 PHE AAA O   
1674  C CB  . PHE A 242 ? 0.361 0.484 0.344 -0.001 0.010  0.012  242 PHE AAA CB  
1675  C CG  . PHE A 242 ? 0.383 0.499 0.362 -0.001 0.010  0.008  242 PHE AAA CG  
1676  C CD1 . PHE A 242 ? 0.403 0.521 0.380 0.000  0.009  0.005  242 PHE AAA CD1 
1677  C CD2 . PHE A 242 ? 0.399 0.508 0.378 -0.001 0.010  0.006  242 PHE AAA CD2 
1678  C CE1 . PHE A 242 ? 0.429 0.540 0.401 0.001  0.009  0.001  242 PHE AAA CE1 
1679  C CE2 . PHE A 242 ? 0.398 0.502 0.373 0.000  0.009  0.003  242 PHE AAA CE2 
1680  C CZ  . PHE A 242 ? 0.402 0.506 0.374 0.002  0.009  0.000  242 PHE AAA CZ  
1681  N N   . ASP A 243 ? 0.311 0.440 0.307 -0.002 0.013  0.023  243 ASP AAA N   
1682  C CA  . ASP A 243 ? 0.313 0.447 0.312 -0.001 0.015  0.029  243 ASP AAA CA  
1683  C C   . ASP A 243 ? 0.304 0.444 0.299 -0.000 0.014  0.029  243 ASP AAA C   
1684  O O   . ASP A 243 ? 0.275 0.413 0.266 -0.001 0.013  0.026  243 ASP AAA O   
1685  C CB  . ASP A 243 ? 0.314 0.442 0.318 -0.002 0.015  0.030  243 ASP AAA CB  
1686  C CG  . ASP A 243 ? 0.336 0.466 0.343 -0.001 0.017  0.036  243 ASP AAA CG  
1687  O OD1 . ASP A 243 ? 0.328 0.461 0.341 -0.001 0.019  0.040  243 ASP AAA OD1 
1688  O OD2 . ASP A 243 ? 0.351 0.483 0.357 -0.001 0.016  0.036  243 ASP AAA OD2 
1689  N N   . ARG A 244 ? 0.305 0.454 0.301 0.001  0.015  0.034  244 ARG AAA N   
1690  C CA  . ARG A 244 ? 0.322 0.480 0.315 0.003  0.015  0.034  244 ARG AAA CA  
1691  C C   . ARG A 244 ? 0.311 0.468 0.304 0.003  0.014  0.034  244 ARG AAA C   
1692  O O   . ARG A 244 ? 0.337 0.496 0.326 0.003  0.013  0.030  244 ARG AAA O   
1693  C CB  . ARG A 244 ? 0.340 0.509 0.334 0.005  0.016  0.039  244 ARG AAA CB  
1694  C CG  . ARG A 244 ? 0.346 0.518 0.339 0.004  0.016  0.039  244 ARG AAA CG  
1695  C CD  . ARG A 244 ? 0.350 0.524 0.337 0.004  0.014  0.033  244 ARG AAA CD  
1696  N NE  . ARG A 244 ? 0.360 0.524 0.346 0.002  0.013  0.027  244 ARG AAA NE  
1697  C CZ  . ARG A 244 ? 0.368 0.531 0.350 0.002  0.012  0.022  244 ARG AAA CZ  
1698  N NH1 . ARG A 244 ? 0.353 0.522 0.332 0.002  0.011  0.019  244 ARG AAA NH1 
1699  N NH2 . ARG A 244 ? 0.385 0.538 0.365 0.001  0.011  0.018  244 ARG AAA NH2 
1700  N N   . GLN A 245 ? 0.291 0.445 0.287 0.003  0.016  0.039  245 GLN AAA N   
1701  C CA  . GLN A 245 ? 0.282 0.436 0.279 0.004  0.016  0.040  245 GLN AAA CA  
1702  C C   . GLN A 245 ? 0.282 0.429 0.276 0.002  0.014  0.033  245 GLN AAA C   
1703  O O   . GLN A 245 ? 0.290 0.441 0.282 0.002  0.013  0.031  245 GLN AAA O   
1704  C CB  . GLN A 245 ? 0.292 0.442 0.295 0.004  0.018  0.045  245 GLN AAA CB  
1705  C CG  . GLN A 245 ? 0.314 0.466 0.318 0.005  0.018  0.047  245 GLN AAA CG  
1706  C CD  . GLN A 245 ? 0.342 0.489 0.353 0.006  0.020  0.052  245 GLN AAA CD  
1707  O OE1 . GLN A 245 ? 0.363 0.504 0.378 0.005  0.021  0.054  245 GLN AAA OE1 
1708  N NE2 . GLN A 245 ? 0.337 0.486 0.348 0.007  0.020  0.055  245 GLN AAA NE2 
1709  N N   . CYS A 246 ? 0.273 0.411 0.268 0.000  0.014  0.031  246 CYS AAA N   
1710  C CA  . CYS A 246 ? 0.269 0.399 0.261 -0.001 0.013  0.025  246 CYS AAA CA  
1711  C C   . CYS A 246 ? 0.265 0.398 0.252 -0.001 0.012  0.020  246 CYS AAA C   
1712  O O   . CYS A 246 ? 0.265 0.396 0.249 -0.002 0.012  0.017  246 CYS AAA O   
1713  C CB  . CYS A 246 ? 0.268 0.389 0.261 -0.002 0.013  0.023  246 CYS AAA CB  
1714  S SG  . CYS A 246 ? 0.295 0.412 0.296 -0.002 0.014  0.027  246 CYS AAA SG  
1715  N N   . SER A 247 ? 0.252 0.388 0.238 -0.001 0.012  0.020  247 SER AAA N   
1716  C CA  . SER A 247 ? 0.270 0.408 0.251 -0.001 0.011  0.015  247 SER AAA CA  
1717  C C   . SER A 247 ? 0.270 0.416 0.250 -0.001 0.011  0.014  247 SER AAA C   
1718  O O   . SER A 247 ? 0.251 0.396 0.228 -0.001 0.011  0.009  247 SER AAA O   
1719  C CB  . SER A 247 ? 0.279 0.421 0.259 -0.001 0.011  0.015  247 SER AAA CB  
1720  O OG  . SER A 247 ? 0.287 0.422 0.268 -0.001 0.011  0.015  247 SER AAA OG  
1721  N N   . GLU A 248 ? 0.283 0.438 0.265 0.001  0.011  0.018  248 GLU AAA N   
1722  C CA  . GLU A 248 ? 0.296 0.461 0.277 0.002  0.011  0.017  248 GLU AAA CA  
1723  C C   . GLU A 248 ? 0.281 0.443 0.263 0.001  0.011  0.016  248 GLU AAA C   
1724  O O   . GLU A 248 ? 0.247 0.414 0.228 0.001  0.011  0.011  248 GLU AAA O   
1725  C CB  . GLU A 248 ? 0.314 0.490 0.297 0.004  0.011  0.023  248 GLU AAA CB  
1726  C CG  . GLU A 248 ? 0.348 0.530 0.329 0.005  0.011  0.024  248 GLU AAA CG  
1727  C CD  . GLU A 248 ? 0.391 0.581 0.374 0.008  0.013  0.031  248 GLU AAA CD  
1728  O OE1 . GLU A 248 ? 0.420 0.614 0.405 0.009  0.013  0.035  248 GLU AAA OE1 
1729  O OE2 . GLU A 248 ? 0.368 0.560 0.352 0.008  0.013  0.033  248 GLU AAA OE2 
1730  N N   . LYS A 249 ? 0.282 0.436 0.266 0.001  0.011  0.019  249 LYS AAA N   
1731  C CA  . LYS A 249 ? 0.283 0.432 0.268 0.000  0.011  0.017  249 LYS AAA CA  
1732  C C   . LYS A 249 ? 0.263 0.406 0.244 -0.002 0.012  0.010  249 LYS AAA C   
1733  O O   . LYS A 249 ? 0.255 0.401 0.237 -0.002 0.012  0.006  249 LYS AAA O   
1734  C CB  . LYS A 249 ? 0.285 0.426 0.273 -0.000 0.012  0.020  249 LYS AAA CB  
1735  C CG  . LYS A 249 ? 0.296 0.433 0.284 -0.001 0.012  0.018  249 LYS AAA CG  
1736  C CD  . LYS A 249 ? 0.312 0.442 0.304 -0.001 0.012  0.021  249 LYS AAA CD  
1737  C CE  . LYS A 249 ? 0.310 0.437 0.302 -0.002 0.012  0.020  249 LYS AAA CE  
1738  N NZ  . LYS A 249 ? 0.338 0.476 0.330 -0.000 0.012  0.019  249 LYS AAA NZ  
1739  N N   . ILE A 250 ? 0.240 0.376 0.220 -0.003 0.012  0.008  250 ILE AAA N   
1740  C CA  . ILE A 250 ? 0.260 0.390 0.238 -0.004 0.012  0.002  250 ILE AAA CA  
1741  C C   . ILE A 250 ? 0.265 0.404 0.242 -0.004 0.013  -0.002 250 ILE AAA C   
1742  O O   . ILE A 250 ? 0.249 0.386 0.226 -0.005 0.014  -0.006 250 ILE AAA O   
1743  C CB  . ILE A 250 ? 0.272 0.395 0.247 -0.004 0.012  0.002  250 ILE AAA CB  
1744  C CG1 . ILE A 250 ? 0.294 0.408 0.270 -0.004 0.012  0.004  250 ILE AAA CG1 
1745  C CG2 . ILE A 250 ? 0.273 0.390 0.245 -0.005 0.014  -0.004 250 ILE AAA CG2 
1746  C CD1 . ILE A 250 ? 0.309 0.420 0.285 -0.003 0.012  0.005  250 ILE AAA CD1 
1747  N N   . VAL A 251 ? 0.261 0.409 0.238 -0.003 0.012  -0.002 251 VAL AAA N   
1748  C CA  . VAL A 251 ? 0.272 0.429 0.248 -0.003 0.012  -0.006 251 VAL AAA CA  
1749  C C   . VAL A 251 ? 0.286 0.451 0.264 -0.003 0.012  -0.008 251 VAL AAA C   
1750  O O   . VAL A 251 ? 0.294 0.460 0.272 -0.004 0.013  -0.014 251 VAL AAA O   
1751  C CB  . VAL A 251 ? 0.269 0.434 0.244 -0.002 0.012  -0.005 251 VAL AAA CB  
1752  C CG1 . VAL A 251 ? 0.262 0.441 0.238 -0.001 0.011  -0.009 251 VAL AAA CG1 
1753  C CG2 . VAL A 251 ? 0.260 0.417 0.233 -0.002 0.012  -0.006 251 VAL AAA CG2 
1754  N N   . GLU A 252 ? 0.309 0.478 0.288 -0.001 0.011  -0.002 252 GLU AAA N   
1755  C CA  . GLU A 252 ? 0.318 0.494 0.299 -0.000 0.011  -0.003 252 GLU AAA CA  
1756  C C   . GLU A 252 ? 0.298 0.466 0.280 -0.003 0.012  -0.007 252 GLU AAA C   
1757  O O   . GLU A 252 ? 0.307 0.481 0.290 -0.003 0.012  -0.013 252 GLU AAA O   
1758  C CB  . GLU A 252 ? 0.360 0.539 0.342 0.002  0.011  0.005  252 GLU AAA CB  
1759  C CG  . GLU A 252 ? 0.413 0.601 0.397 0.003  0.010  0.006  252 GLU AAA CG  
1760  C CD  . GLU A 252 ? 0.438 0.622 0.424 0.005  0.010  0.012  252 GLU AAA CD  
1761  O OE1 . GLU A 252 ? 0.485 0.679 0.472 0.008  0.010  0.016  252 GLU AAA OE1 
1762  O OE2 . GLU A 252 ? 0.452 0.623 0.439 0.003  0.011  0.012  252 GLU AAA OE2 
1763  N N   . TYR A 253 ? 0.290 0.444 0.271 -0.004 0.013  -0.006 253 TYR AAA N   
1764  C CA  . TYR A 253 ? 0.277 0.422 0.259 -0.006 0.014  -0.010 253 TYR AAA CA  
1765  C C   . TYR A 253 ? 0.269 0.413 0.250 -0.007 0.016  -0.017 253 TYR AAA C   
1766  O O   . TYR A 253 ? 0.278 0.422 0.260 -0.009 0.017  -0.022 253 TYR AAA O   
1767  C CB  . TYR A 253 ? 0.286 0.419 0.267 -0.006 0.014  -0.006 253 TYR AAA CB  
1768  C CG  . TYR A 253 ? 0.289 0.412 0.269 -0.008 0.016  -0.009 253 TYR AAA CG  
1769  C CD1 . TYR A 253 ? 0.282 0.397 0.261 -0.009 0.017  -0.014 253 TYR AAA CD1 
1770  C CD2 . TYR A 253 ? 0.293 0.417 0.276 -0.008 0.015  -0.008 253 TYR AAA CD2 
1771  C CE1 . TYR A 253 ? 0.291 0.399 0.270 -0.010 0.019  -0.016 253 TYR AAA CE1 
1772  C CE2 . TYR A 253 ? 0.298 0.414 0.281 -0.009 0.017  -0.011 253 TYR AAA CE2 
1773  C CZ  . TYR A 253 ? 0.302 0.410 0.283 -0.010 0.019  -0.015 253 TYR AAA CZ  
1774  O OH  . TYR A 253 ? 0.312 0.412 0.293 -0.012 0.021  -0.018 253 TYR AAA OH  
1775  N N   . MET A 254 ? 0.262 0.402 0.240 -0.007 0.016  -0.017 254 MET AAA N   
1776  C CA  . MET A 254 ? 0.262 0.400 0.240 -0.009 0.018  -0.024 254 MET AAA CA  
1777  C C   . MET A 254 ? 0.264 0.414 0.245 -0.009 0.018  -0.029 254 MET AAA C   
1778  O O   . MET A 254 ? 0.248 0.396 0.231 -0.011 0.021  -0.035 254 MET AAA O   
1779  C CB  . MET A 254 ? 0.264 0.398 0.239 -0.008 0.018  -0.023 254 MET AAA CB  
1780  C CG  . MET A 254 ? 0.261 0.384 0.234 -0.008 0.018  -0.019 254 MET AAA CG  
1781  S SD  . MET A 254 ? 0.237 0.355 0.207 -0.007 0.018  -0.019 254 MET AAA SD  
1782  C CE  . MET A 254 ? 0.246 0.362 0.216 -0.008 0.021  -0.026 254 MET AAA CE  
1783  N N   . LYS A 255 ? 0.282 0.445 0.263 -0.008 0.016  -0.027 255 LYS AAA N   
1784  C CA  . LYS A 255 ? 0.307 0.485 0.291 -0.007 0.016  -0.032 255 LYS AAA CA  
1785  C C   . LYS A 255 ? 0.312 0.492 0.299 -0.008 0.017  -0.035 255 LYS AAA C   
1786  O O   . LYS A 255 ? 0.303 0.487 0.293 -0.010 0.018  -0.043 255 LYS AAA O   
1787  C CB  . LYS A 255 ? 0.341 0.533 0.324 -0.005 0.014  -0.028 255 LYS AAA CB  
1788  C CG  . LYS A 255 ? 0.392 0.590 0.374 -0.004 0.013  -0.029 255 LYS AAA CG  
1789  C CD  . LYS A 255 ? 0.412 0.623 0.393 -0.001 0.011  -0.023 255 LYS AAA CD  
1790  C CE  . LYS A 255 ? 0.454 0.673 0.434 0.000  0.011  -0.025 255 LYS AAA CE  
1791  N NZ  . LYS A 255 ? 0.478 0.700 0.456 0.002  0.010  -0.018 255 LYS AAA NZ  
1792  N N   . ALA A 256 ? 0.296 0.472 0.282 -0.007 0.016  -0.030 256 ALA AAA N   
1793  C CA  . ALA A 256 ? 0.277 0.455 0.266 -0.008 0.016  -0.032 256 ALA AAA CA  
1794  C C   . ALA A 256 ? 0.271 0.438 0.262 -0.011 0.019  -0.037 256 ALA AAA C   
1795  O O   . ALA A 256 ? 0.270 0.440 0.264 -0.012 0.020  -0.042 256 ALA AAA O   
1796  C CB  . ALA A 256 ? 0.274 0.450 0.263 -0.006 0.014  -0.025 256 ALA AAA CB  
1797  N N   . THR A 257 ? 0.266 0.420 0.254 -0.012 0.021  -0.037 257 THR AAA N   
1798  C CA  . THR A 257 ? 0.259 0.402 0.249 -0.014 0.024  -0.042 257 THR AAA CA  
1799  C C   . THR A 257 ? 0.253 0.396 0.244 -0.016 0.027  -0.049 257 THR AAA C   
1800  O O   . THR A 257 ? 0.258 0.390 0.249 -0.018 0.030  -0.052 257 THR AAA O   
1801  C CB  . THR A 257 ? 0.264 0.391 0.250 -0.014 0.024  -0.037 257 THR AAA CB  
1802  O OG1 . THR A 257 ? 0.272 0.396 0.254 -0.013 0.024  -0.033 257 THR AAA OG1 
1803  C CG2 . THR A 257 ? 0.265 0.390 0.250 -0.013 0.023  -0.032 257 THR AAA CG2 
1804  N N   . GLY A 258 ? 0.251 0.405 0.243 -0.015 0.026  -0.051 258 GLY AAA N   
1805  C CA  . GLY A 258 ? 0.256 0.413 0.251 -0.017 0.028  -0.059 258 GLY AAA CA  
1806  C C   . GLY A 258 ? 0.259 0.414 0.251 -0.016 0.028  -0.058 258 GLY AAA C   
1807  O O   . GLY A 258 ? 0.241 0.399 0.237 -0.018 0.031  -0.065 258 GLY AAA O   
1808  N N   . THR A 259 ? 0.270 0.421 0.258 -0.014 0.026  -0.051 259 THR AAA N   
1809  C CA  . THR A 259 ? 0.282 0.432 0.267 -0.014 0.026  -0.051 259 THR AAA CA  
1810  C C   . THR A 259 ? 0.306 0.473 0.293 -0.013 0.024  -0.052 259 THR AAA C   
1811  O O   . THR A 259 ? 0.314 0.490 0.300 -0.011 0.021  -0.048 259 THR AAA O   
1812  C CB  . THR A 259 ? 0.273 0.413 0.254 -0.012 0.025  -0.043 259 THR AAA CB  
1813  O OG1 . THR A 259 ? 0.266 0.392 0.246 -0.013 0.027  -0.043 259 THR AAA OG1 
1814  C CG2 . THR A 259 ? 0.278 0.417 0.257 -0.012 0.025  -0.044 259 THR AAA CG2 
1815  N N   . LYS A 260 ? 0.321 0.494 0.310 -0.013 0.025  -0.058 260 LYS AAA N   
1816  C CA  . LYS A 260 ? 0.337 0.527 0.327 -0.012 0.023  -0.060 260 LYS AAA CA  
1817  C C   . LYS A 260 ? 0.336 0.524 0.322 -0.010 0.021  -0.054 260 LYS AAA C   
1818  O O   . LYS A 260 ? 0.373 0.548 0.357 -0.011 0.023  -0.054 260 LYS AAA O   
1819  C CB  . LYS A 260 ? 0.342 0.540 0.338 -0.013 0.025  -0.070 260 LYS AAA CB  
1820  C CG  . LYS A 260 ? 0.359 0.564 0.360 -0.015 0.026  -0.075 260 LYS AAA CG  
1821  C CD  . LYS A 260 ? 0.360 0.566 0.367 -0.018 0.030  -0.086 260 LYS AAA CD  
1822  C CE  . LYS A 260 ? 0.372 0.559 0.379 -0.020 0.034  -0.087 260 LYS AAA CE  
1823  N NZ  . LYS A 260 ? 0.378 0.568 0.392 -0.022 0.038  -0.097 260 LYS AAA NZ  
1824  N N   . PHE A 261 ? 0.337 0.536 0.321 -0.008 0.018  -0.050 261 PHE AAA N   
1825  C CA  . PHE A 261 ? 0.358 0.559 0.339 -0.006 0.017  -0.045 261 PHE AAA CA  
1826  C C   . PHE A 261 ? 0.356 0.574 0.339 -0.005 0.015  -0.049 261 PHE AAA C   
1827  O O   . PHE A 261 ? 0.342 0.573 0.326 -0.004 0.014  -0.049 261 PHE AAA O   
1828  C CB  . PHE A 261 ? 0.352 0.551 0.330 -0.005 0.015  -0.036 261 PHE AAA CB  
1829  C CG  . PHE A 261 ? 0.352 0.535 0.329 -0.005 0.015  -0.032 261 PHE AAA CG  
1830  C CD1 . PHE A 261 ? 0.368 0.546 0.346 -0.006 0.016  -0.033 261 PHE AAA CD1 
1831  C CD2 . PHE A 261 ? 0.354 0.528 0.328 -0.005 0.015  -0.029 261 PHE AAA CD2 
1832  C CE1 . PHE A 261 ? 0.338 0.502 0.315 -0.007 0.017  -0.030 261 PHE AAA CE1 
1833  C CE2 . PHE A 261 ? 0.350 0.511 0.323 -0.006 0.016  -0.026 261 PHE AAA CE2 
1834  C CZ  . PHE A 261 ? 0.344 0.499 0.318 -0.006 0.016  -0.026 261 PHE AAA CZ  
1835  N N   . LEU A 262 ? 0.381 0.598 0.363 -0.006 0.016  -0.052 262 LEU AAA N   
1836  C CA  . LEU A 262 ? 0.410 0.641 0.392 -0.004 0.015  -0.053 262 LEU AAA CA  
1837  C C   . LEU A 262 ? 0.420 0.649 0.398 -0.002 0.013  -0.045 262 LEU AAA C   
1838  O O   . LEU A 262 ? 0.393 0.611 0.369 -0.003 0.014  -0.043 262 LEU AAA O   
1839  C CB  . LEU A 262 ? 0.427 0.654 0.411 -0.006 0.017  -0.061 262 LEU AAA CB  
1840  C CG  . LEU A 262 ? 0.438 0.662 0.427 -0.008 0.020  -0.069 262 LEU AAA CG  
1841  C CD1 . LEU A 262 ? 0.442 0.663 0.434 -0.010 0.023  -0.076 262 LEU AAA CD1 
1842  C CD2 . LEU A 262 ? 0.437 0.678 0.430 -0.008 0.019  -0.074 262 LEU AAA CD2 
1843  N N   . VAL A 263 ? 0.459 0.700 0.436 0.000  0.011  -0.040 263 VAL AAA N   
1844  C CA  . VAL A 263 ? 0.485 0.726 0.460 0.002  0.010  -0.031 263 VAL AAA CA  
1845  C C   . VAL A 263 ? 0.469 0.721 0.442 0.004  0.009  -0.032 263 VAL AAA C   
1846  O O   . VAL A 263 ? 0.440 0.707 0.414 0.005  0.009  -0.037 263 VAL AAA O   
1847  C CB  . VAL A 263 ? 0.516 0.763 0.490 0.004  0.009  -0.025 263 VAL AAA CB  
1848  C CG1 . VAL A 263 ? 0.536 0.779 0.508 0.006  0.008  -0.016 263 VAL AAA CG1 
1849  C CG2 . VAL A 263 ? 0.518 0.757 0.493 0.003  0.010  -0.025 263 VAL AAA CG2 
1850  N N   . GLY A 264 ? 0.463 0.709 0.435 0.003  0.009  -0.030 264 GLY AAA N   
1851  C CA  . GLY A 264 ? 0.470 0.724 0.440 0.004  0.009  -0.030 264 GLY AAA CA  
1852  C C   . GLY A 264 ? 0.482 0.739 0.455 0.003  0.010  -0.040 264 GLY AAA C   
1853  O O   . GLY A 264 ? 0.471 0.741 0.444 0.004  0.009  -0.042 264 GLY AAA O   
1854  N N   . VAL A 265 ? 0.515 0.762 0.489 0.001  0.011  -0.045 265 VAL AAA N   
1855  C CA  . VAL A 265 ? 0.516 0.764 0.494 -0.001 0.013  -0.054 265 VAL AAA CA  
1856  C C   . VAL A 265 ? 0.515 0.745 0.491 -0.002 0.015  -0.055 265 VAL AAA C   
1857  O O   . VAL A 265 ? 0.557 0.774 0.532 -0.003 0.015  -0.051 265 VAL AAA O   
1858  C CB  . VAL A 265 ? 0.560 0.815 0.542 -0.002 0.014  -0.061 265 VAL AAA CB  
1859  C CG1 . VAL A 265 ? 0.583 0.835 0.569 -0.004 0.016  -0.071 265 VAL AAA CG1 
1860  C CG2 . VAL A 265 ? 0.555 0.829 0.537 0.001  0.012  -0.061 265 VAL AAA CG2 
1861  N N   . VAL A 266 ? 0.527 0.755 0.504 -0.003 0.016  -0.059 266 VAL AAA N   
1862  C CA  . VAL A 266 ? 0.495 0.706 0.471 -0.004 0.018  -0.061 266 VAL AAA CA  
1863  C C   . VAL A 266 ? 0.469 0.683 0.449 -0.005 0.021  -0.070 266 VAL AAA C   
1864  O O   . VAL A 266 ? 0.465 0.694 0.448 -0.005 0.020  -0.074 266 VAL AAA O   
1865  C CB  . VAL A 266 ? 0.544 0.750 0.516 -0.002 0.017  -0.055 266 VAL AAA CB  
1866  C CG1 . VAL A 266 ? 0.607 0.810 0.577 -0.001 0.015  -0.046 266 VAL AAA CG1 
1867  C CG2 . VAL A 266 ? 0.516 0.734 0.488 -0.001 0.015  -0.056 266 VAL AAA CG2 
1868  N N   . PRO A 267 ? 0.427 0.627 0.408 -0.006 0.024  -0.072 267 PRO AAA N   
1869  C CA  . PRO A 267 ? 0.403 0.603 0.388 -0.007 0.027  -0.080 267 PRO AAA CA  
1870  C C   . PRO A 267 ? 0.384 0.590 0.368 -0.006 0.025  -0.081 267 PRO AAA C   
1871  O O   . PRO A 267 ? 0.370 0.572 0.349 -0.004 0.024  -0.075 267 PRO AAA O   
1872  C CB  . PRO A 267 ? 0.409 0.589 0.393 -0.007 0.030  -0.080 267 PRO AAA CB  
1873  C CG  . PRO A 267 ? 0.424 0.598 0.405 -0.007 0.029  -0.074 267 PRO AAA CG  
1874  C CD  . PRO A 267 ? 0.422 0.605 0.400 -0.006 0.025  -0.068 267 PRO AAA CD  
1875  N N   . ILE A 268 ? 0.385 0.601 0.374 -0.007 0.027  -0.089 268 ILE AAA N   
1876  C CA  . ILE A 268 ? 0.382 0.602 0.370 -0.006 0.026  -0.091 268 ILE AAA CA  
1877  C C   . ILE A 268 ? 0.378 0.590 0.372 -0.007 0.031  -0.099 268 ILE AAA C   
1878  O O   . ILE A 268 ? 0.363 0.576 0.357 -0.006 0.031  -0.100 268 ILE AAA O   
1879  C CB  . ILE A 268 ? 0.392 0.634 0.383 -0.005 0.024  -0.094 268 ILE AAA CB  
1880  C CG1 . ILE A 268 ? 0.386 0.638 0.383 -0.007 0.025  -0.103 268 ILE AAA CG1 
1881  C CG2 . ILE A 268 ? 0.382 0.629 0.367 -0.003 0.020  -0.085 268 ILE AAA CG2 
1882  C CD1 . ILE A 268 ? 0.382 0.656 0.381 -0.006 0.022  -0.106 268 ILE AAA CD1 
1883  N N   . ASN A 269 ? 0.381 0.587 0.379 -0.009 0.034  -0.103 269 ASN AAA N   
1884  C CA  . ASN A 269 ? 0.408 0.604 0.411 -0.010 0.040  -0.110 269 ASN AAA CA  
1885  C C   . ASN A 269 ? 0.407 0.590 0.412 -0.011 0.044  -0.110 269 ASN AAA C   
1886  O O   . ASN A 269 ? 0.422 0.610 0.428 -0.013 0.043  -0.110 269 ASN AAA O   
1887  C CB  . ASN A 269 ? 0.396 0.606 0.407 -0.011 0.041  -0.120 269 ASN AAA CB  
1888  C CG  . ASN A 269 ? 0.406 0.606 0.423 -0.012 0.047  -0.127 269 ASN AAA CG  
1889  O OD1 . ASN A 269 ? 0.455 0.655 0.480 -0.015 0.051  -0.134 269 ASN AAA OD1 
1890  N ND2 . ASN A 269 ? 0.417 0.609 0.431 -0.010 0.047  -0.124 269 ASN AAA ND2 
1891  N N   . ILE A 270 ? 0.430 0.598 0.436 -0.011 0.048  -0.110 270 ILE AAA N   
1892  C CA  . ILE A 270 ? 0.478 0.631 0.486 -0.012 0.053  -0.110 270 ILE AAA CA  
1893  C C   . ILE A 270 ? 0.516 0.660 0.530 -0.013 0.060  -0.117 270 ILE AAA C   
1894  O O   . ILE A 270 ? 0.522 0.659 0.534 -0.010 0.061  -0.115 270 ILE AAA O   
1895  C CB  . ILE A 270 ? 0.499 0.638 0.498 -0.009 0.051  -0.099 270 ILE AAA CB  
1896  C CG1 . ILE A 270 ? 0.505 0.653 0.499 -0.009 0.046  -0.094 270 ILE AAA CG1 
1897  C CG2 . ILE A 270 ? 0.508 0.630 0.507 -0.009 0.057  -0.098 270 ILE AAA CG2 
1898  C CD1 . ILE A 270 ? 0.522 0.659 0.508 -0.006 0.043  -0.084 270 ILE AAA CD1 
1899  N N   . GLU A 271 ? 0.543 0.689 0.566 -0.016 0.064  -0.124 271 GLU AAA N   
1900  C CA  . GLU A 271 ? 0.608 0.747 0.639 -0.017 0.071  -0.132 271 GLU AAA CA  
1901  C C   . GLU A 271 ? 0.620 0.748 0.656 -0.019 0.077  -0.134 271 GLU AAA C   
1902  O O   . GLU A 271 ? 0.562 0.694 0.597 -0.020 0.074  -0.133 271 GLU AAA O   
1903  C CB  . GLU A 271 ? 0.631 0.787 0.672 -0.019 0.071  -0.143 271 GLU AAA CB  
1904  C CG  . GLU A 271 ? 0.662 0.837 0.703 -0.021 0.065  -0.146 271 GLU AAA CG  
1905  C CD  . GLU A 271 ? 0.649 0.843 0.698 -0.023 0.065  -0.157 271 GLU AAA CD  
1906  O OE1 . GLU A 271 ? 0.665 0.857 0.723 -0.024 0.070  -0.165 271 GLU AAA OE1 
1907  O OE2 . GLU A 271 ? 0.607 0.818 0.654 -0.022 0.059  -0.157 271 GLU AAA OE2 
1908  N N   . LYS A 272 ? 0.695 0.808 0.736 -0.019 0.084  -0.136 272 LYS AAA N   
1909  C CA  . LYS A 272 ? 0.745 0.847 0.792 -0.021 0.091  -0.139 272 LYS AAA CA  
1910  C C   . LYS A 272 ? 0.778 0.890 0.838 -0.025 0.095  -0.152 272 LYS AAA C   
1911  O O   . LYS A 272 ? 0.836 0.950 0.903 -0.026 0.098  -0.158 272 LYS AAA O   
1912  C CB  . LYS A 272 ? 0.792 0.874 0.838 -0.018 0.098  -0.134 272 LYS AAA CB  
1913  C CG  . LYS A 272 ? 0.857 0.924 0.905 -0.019 0.104  -0.133 272 LYS AAA CG  
1914  C CD  . LYS A 272 ? 0.919 0.967 0.959 -0.014 0.107  -0.123 272 LYS AAA CD  
1915  C CE  . LYS A 272 ? 0.976 1.009 1.020 -0.015 0.115  -0.123 272 LYS AAA CE  
1916  N NZ  . LYS A 272 ? 1.049 1.064 1.088 -0.010 0.121  -0.116 272 LYS AAA NZ  
1917  N N   . VAL A 273 ? 0.789 0.909 0.853 -0.028 0.094  -0.156 273 VAL AAA N   
1918  C CA  . VAL A 273 ? 0.844 0.973 0.922 -0.032 0.098  -0.169 273 VAL AAA CA  
1919  C C   . VAL A 273 ? 0.881 0.994 0.964 -0.034 0.106  -0.169 273 VAL AAA C   
1920  O O   . VAL A 273 ? 0.964 1.078 1.044 -0.035 0.103  -0.166 273 VAL AAA O   
1921  C CB  . VAL A 273 ? 0.847 0.998 0.926 -0.034 0.092  -0.174 273 VAL AAA CB  
1922  C CG1 . VAL A 273 ? 0.821 0.982 0.915 -0.038 0.096  -0.187 273 VAL AAA CG1 
1923  C CG2 . VAL A 273 ? 0.814 0.981 0.890 -0.032 0.085  -0.174 273 VAL AAA CG2 
1924  N N   . ASN A 274 ? 0.885 0.984 0.975 -0.035 0.114  -0.172 274 ASN AAA N   
1925  C CA  . ASN A 274 ? 0.866 0.948 0.960 -0.036 0.123  -0.171 274 ASN AAA CA  
1926  C C   . ASN A 274 ? 0.847 0.914 0.927 -0.031 0.121  -0.157 274 ASN AAA C   
1927  O O   . ASN A 274 ? 0.773 0.833 0.846 -0.027 0.120  -0.150 274 ASN AAA O   
1928  C CB  . ASN A 274 ? 0.902 0.991 1.005 -0.040 0.125  -0.180 274 ASN AAA CB  
1929  C CG  . ASN A 274 ? 0.922 1.025 1.041 -0.044 0.128  -0.195 274 ASN AAA CG  
1930  O OD1 . ASN A 274 ? 0.890 1.012 1.011 -0.046 0.122  -0.201 274 ASN AAA OD1 
1931  N ND2 . ASN A 274 ? 0.919 1.013 1.047 -0.045 0.136  -0.200 274 ASN AAA ND2 
1932  N N   . GLU A 275 ? 0.827 0.890 0.905 -0.032 0.120  -0.154 275 GLU AAA N   
1933  C CA  . GLU A 275 ? 0.836 0.887 0.902 -0.029 0.119  -0.141 275 GLU AAA CA  
1934  C C   . GLU A 275 ? 0.752 0.814 0.808 -0.028 0.109  -0.136 275 GLU AAA C   
1935  O O   . GLU A 275 ? 0.747 0.801 0.792 -0.024 0.106  -0.126 275 GLU AAA O   
1936  C CB  . GLU A 275 ? 0.894 0.930 0.963 -0.030 0.126  -0.140 275 GLU AAA CB  
1937  C CG  . GLU A 275 ? 0.939 0.986 1.015 -0.034 0.125  -0.147 275 GLU AAA CG  
1938  C CD  . GLU A 275 ? 0.972 1.027 1.064 -0.039 0.130  -0.161 275 GLU AAA CD  
1939  O OE1 . GLU A 275 ? 0.985 1.035 1.084 -0.040 0.137  -0.166 275 GLU AAA OE1 
1940  O OE2 . GLU A 275 ? 1.024 1.091 1.122 -0.043 0.128  -0.167 275 GLU AAA OE2 
1941  N N   . ASN A 276 ? 0.675 0.756 0.734 -0.030 0.103  -0.142 276 ASN AAA N   
1942  C CA  . ASN A 276 ? 0.637 0.731 0.688 -0.029 0.094  -0.137 276 ASN AAA CA  
1943  C C   . ASN A 276 ? 0.609 0.710 0.654 -0.026 0.089  -0.134 276 ASN AAA C   
1944  O O   . ASN A 276 ? 0.581 0.679 0.630 -0.025 0.092  -0.137 276 ASN AAA O   
1945  C CB  . ASN A 276 ? 0.628 0.741 0.686 -0.032 0.091  -0.145 276 ASN AAA CB  
1946  C CG  . ASN A 276 ? 0.654 0.762 0.716 -0.035 0.094  -0.147 276 ASN AAA CG  
1947  O OD1 . ASN A 276 ? 0.615 0.708 0.671 -0.033 0.096  -0.139 276 ASN AAA OD1 
1948  N ND2 . ASN A 276 ? 0.644 0.764 0.716 -0.038 0.095  -0.157 276 ASN AAA ND2 
1949  N N   . ILE A 277 ? 0.563 0.671 0.600 -0.024 0.081  -0.127 277 ILE AAA N   
1950  C CA  . ILE A 277 ? 0.528 0.644 0.558 -0.022 0.075  -0.124 277 ILE AAA CA  
1951  C C   . ILE A 277 ? 0.505 0.643 0.538 -0.023 0.069  -0.127 277 ILE AAA C   
1952  O O   . ILE A 277 ? 0.488 0.631 0.517 -0.023 0.065  -0.124 277 ILE AAA O   
1953  C CB  . ILE A 277 ? 0.505 0.612 0.524 -0.018 0.072  -0.112 277 ILE AAA CB  
1954  C CG1 . ILE A 277 ? 0.516 0.603 0.533 -0.016 0.078  -0.108 277 ILE AAA CG1 
1955  C CG2 . ILE A 277 ? 0.470 0.586 0.483 -0.016 0.066  -0.109 277 ILE AAA CG2 
1956  C CD1 . ILE A 277 ? 0.511 0.587 0.518 -0.012 0.075  -0.098 277 ILE AAA CD1 
1957  N N   . LYS A 278 ? 0.513 0.663 0.551 -0.024 0.069  -0.135 278 LYS AAA N   
1958  C CA  . LYS A 278 ? 0.489 0.661 0.529 -0.024 0.064  -0.139 278 LYS AAA CA  
1959  C C   . LYS A 278 ? 0.470 0.645 0.499 -0.021 0.057  -0.130 278 LYS AAA C   
1960  O O   . LYS A 278 ? 0.483 0.653 0.510 -0.020 0.058  -0.129 278 LYS AAA O   
1961  C CB  . LYS A 278 ? 0.498 0.681 0.548 -0.026 0.066  -0.151 278 LYS AAA CB  
1962  C CG  . LYS A 278 ? 0.511 0.717 0.563 -0.027 0.062  -0.157 278 LYS AAA CG  
1963  C CD  . LYS A 278 ? 0.520 0.737 0.582 -0.028 0.064  -0.169 278 LYS AAA CD  
1964  C CE  . LYS A 278 ? 0.527 0.769 0.594 -0.029 0.060  -0.176 278 LYS AAA CE  
1965  N NZ  . LYS A 278 ? 0.515 0.771 0.588 -0.029 0.061  -0.186 278 LYS AAA NZ  
1966  N N   . VAL A 279 ? 0.415 0.598 0.440 -0.020 0.052  -0.125 279 VAL AAA N   
1967  C CA  . VAL A 279 ? 0.407 0.594 0.423 -0.017 0.047  -0.116 279 VAL AAA CA  
1968  C C   . VAL A 279 ? 0.413 0.622 0.430 -0.017 0.042  -0.120 279 VAL AAA C   
1969  O O   . VAL A 279 ? 0.433 0.653 0.454 -0.018 0.041  -0.123 279 VAL AAA O   
1970  C CB  . VAL A 279 ? 0.384 0.561 0.392 -0.016 0.044  -0.106 279 VAL AAA CB  
1971  C CG1 . VAL A 279 ? 0.384 0.568 0.385 -0.014 0.039  -0.098 279 VAL AAA CG1 
1972  C CG2 . VAL A 279 ? 0.364 0.521 0.369 -0.015 0.048  -0.102 279 VAL AAA CG2 
1973  N N   . SER A 280 ? 0.410 0.625 0.425 -0.015 0.040  -0.119 280 SER AAA N   
1974  C CA  . SER A 280 ? 0.404 0.640 0.419 -0.014 0.036  -0.121 280 SER AAA CA  
1975  C C   . SER A 280 ? 0.392 0.630 0.399 -0.012 0.031  -0.110 280 SER AAA C   
1976  O O   . SER A 280 ? 0.397 0.623 0.398 -0.011 0.031  -0.104 280 SER AAA O   
1977  C CB  . SER A 280 ? 0.432 0.676 0.451 -0.015 0.037  -0.128 280 SER AAA CB  
1978  O OG  . SER A 280 ? 0.422 0.668 0.451 -0.017 0.041  -0.139 280 SER AAA OG  
1979  N N   . PHE A 281 ? 0.413 0.663 0.418 -0.011 0.028  -0.108 281 PHE AAA N   
1980  C CA  . PHE A 281 ? 0.423 0.674 0.421 -0.009 0.024  -0.097 281 PHE AAA CA  
1981  C C   . PHE A 281 ? 0.431 0.699 0.427 -0.006 0.021  -0.096 281 PHE AAA C   
1982  O O   . PHE A 281 ? 0.430 0.713 0.431 -0.007 0.021  -0.104 281 PHE AAA O   
1983  C CB  . PHE A 281 ? 0.420 0.673 0.418 -0.009 0.023  -0.094 281 PHE AAA CB  
1984  C CG  . PHE A 281 ? 0.411 0.646 0.409 -0.010 0.026  -0.093 281 PHE AAA CG  
1985  C CD1 . PHE A 281 ? 0.384 0.605 0.376 -0.009 0.025  -0.084 281 PHE AAA CD1 
1986  C CD2 . PHE A 281 ? 0.402 0.636 0.406 -0.013 0.029  -0.100 281 PHE AAA CD2 
1987  C CE1 . PHE A 281 ? 0.394 0.599 0.386 -0.011 0.027  -0.083 281 PHE AAA CE1 
1988  C CE2 . PHE A 281 ? 0.396 0.613 0.399 -0.014 0.031  -0.099 281 PHE AAA CE2 
1989  C CZ  . PHE A 281 ? 0.400 0.604 0.398 -0.013 0.031  -0.090 281 PHE AAA CZ  
1990  N N   . SER A 282 ? 0.427 0.693 0.417 -0.004 0.018  -0.087 282 SER AAA N   
1991  C CA  . SER A 282 ? 0.423 0.701 0.410 -0.002 0.015  -0.083 282 SER AAA CA  
1992  C C   . SER A 282 ? 0.450 0.749 0.439 -0.000 0.013  -0.085 282 SER AAA C   
1993  O O   . SER A 282 ? 0.428 0.740 0.415 0.002  0.012  -0.084 282 SER AAA O   
1994  C CB  . SER A 282 ? 0.404 0.673 0.385 -0.001 0.014  -0.072 282 SER AAA CB  
1995  O OG  . SER A 282 ? 0.411 0.680 0.390 -0.000 0.013  -0.066 282 SER AAA OG  
1996  N N   . ASP A 283 ? 0.447 0.748 0.438 -0.001 0.014  -0.087 283 ASP AAA N   
1997  C CA  . ASP A 283 ? 0.457 0.779 0.449 0.001  0.012  -0.089 283 ASP AAA CA  
1998  C C   . ASP A 283 ? 0.435 0.769 0.434 -0.000 0.013  -0.101 283 ASP AAA C   
1999  O O   . ASP A 283 ? 0.414 0.765 0.416 0.001  0.012  -0.105 283 ASP AAA O   
2000  C CB  . ASP A 283 ? 0.466 0.785 0.456 0.002  0.011  -0.083 283 ASP AAA CB  
2001  C CG  . ASP A 283 ? 0.460 0.770 0.455 -0.001 0.013  -0.088 283 ASP AAA CG  
2002  O OD1 . ASP A 283 ? 0.427 0.726 0.425 -0.004 0.016  -0.094 283 ASP AAA OD1 
2003  O OD2 . ASP A 283 ? 0.456 0.768 0.450 -0.000 0.012  -0.085 283 ASP AAA OD2 
2004  N N   . GLY A 284 ? 0.419 0.744 0.422 -0.003 0.016  -0.108 284 GLY AAA N   
2005  C CA  . GLY A 284 ? 0.421 0.756 0.432 -0.005 0.018  -0.121 284 GLY AAA CA  
2006  C C   . GLY A 284 ? 0.440 0.770 0.457 -0.007 0.020  -0.127 284 GLY AAA C   
2007  O O   . GLY A 284 ? 0.460 0.798 0.484 -0.009 0.022  -0.139 284 GLY AAA O   
2008  N N   . SER A 285 ? 0.445 0.761 0.458 -0.008 0.021  -0.120 285 SER AAA N   
2009  C CA  . SER A 285 ? 0.419 0.728 0.437 -0.010 0.023  -0.125 285 SER AAA CA  
2010  C C   . SER A 285 ? 0.412 0.701 0.433 -0.013 0.028  -0.128 285 SER AAA C   
2011  O O   . SER A 285 ? 0.407 0.685 0.424 -0.013 0.028  -0.122 285 SER AAA O   
2012  C CB  . SER A 285 ? 0.395 0.700 0.409 -0.009 0.022  -0.117 285 SER AAA CB  
2013  O OG  . SER A 285 ? 0.416 0.703 0.424 -0.009 0.022  -0.107 285 SER AAA OG  
2014  N N   . VAL A 286 ? 0.420 0.705 0.448 -0.016 0.032  -0.136 286 VAL AAA N   
2015  C CA  . VAL A 286 ? 0.477 0.743 0.509 -0.019 0.037  -0.139 286 VAL AAA CA  
2016  C C   . VAL A 286 ? 0.497 0.752 0.531 -0.021 0.039  -0.139 286 VAL AAA C   
2017  O O   . VAL A 286 ? 0.537 0.804 0.573 -0.021 0.038  -0.141 286 VAL AAA O   
2018  C CB  . VAL A 286 ? 0.477 0.751 0.518 -0.021 0.040  -0.152 286 VAL AAA CB  
2019  C CG1 . VAL A 286 ? 0.485 0.742 0.532 -0.024 0.047  -0.157 286 VAL AAA CG1 
2020  C CG2 . VAL A 286 ? 0.471 0.754 0.510 -0.019 0.038  -0.152 286 VAL AAA CG2 
2021  N N   . GLU A 287 ? 0.492 0.727 0.525 -0.022 0.043  -0.135 287 GLU AAA N   
2022  C CA  . GLU A 287 ? 0.505 0.728 0.539 -0.024 0.046  -0.134 287 GLU AAA CA  
2023  C C   . GLU A 287 ? 0.469 0.670 0.503 -0.025 0.051  -0.133 287 GLU AAA C   
2024  O O   . GLU A 287 ? 0.416 0.609 0.445 -0.023 0.051  -0.128 287 GLU AAA O   
2025  C CB  . GLU A 287 ? 0.514 0.735 0.540 -0.022 0.042  -0.124 287 GLU AAA CB  
2026  C CG  . GLU A 287 ? 0.538 0.755 0.567 -0.023 0.043  -0.125 287 GLU AAA CG  
2027  C CD  . GLU A 287 ? 0.559 0.777 0.581 -0.021 0.039  -0.116 287 GLU AAA CD  
2028  O OE1 . GLU A 287 ? 0.578 0.803 0.594 -0.019 0.035  -0.109 287 GLU AAA OE1 
2029  O OE2 . GLU A 287 ? 0.536 0.746 0.558 -0.023 0.041  -0.115 287 GLU AAA OE2 
2030  N N   . GLU A 288 ? 0.483 0.677 0.524 -0.027 0.056  -0.138 288 GLU AAA N   
2031  C CA  . GLU A 288 ? 0.507 0.679 0.548 -0.028 0.063  -0.137 288 GLU AAA CA  
2032  C C   . GLU A 288 ? 0.475 0.633 0.509 -0.027 0.062  -0.128 288 GLU AAA C   
2033  O O   . GLU A 288 ? 0.459 0.623 0.493 -0.027 0.059  -0.126 288 GLU AAA O   
2034  C CB  . GLU A 288 ? 0.538 0.710 0.591 -0.032 0.069  -0.149 288 GLU AAA CB  
2035  C CG  . GLU A 288 ? 0.586 0.770 0.647 -0.033 0.070  -0.159 288 GLU AAA CG  
2036  C CD  . GLU A 288 ? 0.647 0.825 0.720 -0.036 0.078  -0.169 288 GLU AAA CD  
2037  O OE1 . GLU A 288 ? 0.712 0.873 0.786 -0.037 0.084  -0.167 288 GLU AAA OE1 
2038  O OE2 . GLU A 288 ? 0.737 0.928 0.818 -0.038 0.079  -0.179 288 GLU AAA OE2 
2039  N N   . PHE A 289 ? 0.453 0.595 0.482 -0.025 0.064  -0.121 289 PHE AAA N   
2040  C CA  . PHE A 289 ? 0.474 0.601 0.497 -0.024 0.065  -0.113 289 PHE AAA CA  
2041  C C   . PHE A 289 ? 0.470 0.578 0.494 -0.024 0.072  -0.113 289 PHE AAA C   
2042  O O   . PHE A 289 ? 0.501 0.608 0.528 -0.024 0.075  -0.117 289 PHE AAA O   
2043  C CB  . PHE A 289 ? 0.462 0.587 0.474 -0.021 0.059  -0.102 289 PHE AAA CB  
2044  C CG  . PHE A 289 ? 0.462 0.605 0.473 -0.020 0.053  -0.101 289 PHE AAA CG  
2045  C CD1 . PHE A 289 ? 0.449 0.605 0.461 -0.020 0.050  -0.104 289 PHE AAA CD1 
2046  C CD2 . PHE A 289 ? 0.446 0.592 0.454 -0.020 0.049  -0.098 289 PHE AAA CD2 
2047  C CE1 . PHE A 289 ? 0.460 0.632 0.470 -0.019 0.045  -0.103 289 PHE AAA CE1 
2048  C CE2 . PHE A 289 ? 0.449 0.611 0.456 -0.019 0.044  -0.096 289 PHE AAA CE2 
2049  C CZ  . PHE A 289 ? 0.440 0.615 0.447 -0.019 0.042  -0.098 289 PHE AAA CZ  
2050  N N   . GLU A 290 ? 0.462 0.557 0.483 -0.024 0.075  -0.108 290 GLU AAA N   
2051  C CA  . GLU A 290 ? 0.491 0.568 0.512 -0.022 0.081  -0.106 290 GLU AAA CA  
2052  C C   . GLU A 290 ? 0.488 0.557 0.500 -0.018 0.079  -0.097 290 GLU AAA C   
2053  O O   . GLU A 290 ? 0.484 0.541 0.495 -0.016 0.084  -0.096 290 GLU AAA O   
2054  C CB  . GLU A 290 ? 0.527 0.596 0.550 -0.024 0.085  -0.105 290 GLU AAA CB  
2055  C CG  . GLU A 290 ? 0.597 0.648 0.622 -0.023 0.093  -0.105 290 GLU AAA CG  
2056  C CD  . GLU A 290 ? 0.628 0.674 0.657 -0.026 0.097  -0.107 290 GLU AAA CD  
2057  O OE1 . GLU A 290 ? 0.671 0.702 0.698 -0.024 0.102  -0.102 290 GLU AAA OE1 
2058  O OE2 . GLU A 290 ? 0.591 0.650 0.626 -0.029 0.095  -0.113 290 GLU AAA OE2 
2059  N N   . THR A 291 ? 0.447 0.521 0.451 -0.016 0.072  -0.091 291 THR AAA N   
2060  C CA  . THR A 291 ? 0.430 0.497 0.424 -0.012 0.069  -0.082 291 THR AAA CA  
2061  C C   . THR A 291 ? 0.413 0.494 0.404 -0.012 0.062  -0.080 291 THR AAA C   
2062  O O   . THR A 291 ? 0.398 0.489 0.391 -0.013 0.058  -0.080 291 THR AAA O   
2063  C CB  . THR A 291 ? 0.436 0.492 0.425 -0.011 0.070  -0.075 291 THR AAA CB  
2064  O OG1 . THR A 291 ? 0.429 0.473 0.422 -0.011 0.077  -0.077 291 THR AAA OG1 
2065  C CG2 . THR A 291 ? 0.445 0.495 0.425 -0.006 0.067  -0.068 291 THR AAA CG2 
2066  N N   . VAL A 292 ? 0.408 0.488 0.395 -0.009 0.060  -0.077 292 VAL AAA N   
2067  C CA  . VAL A 292 ? 0.393 0.484 0.376 -0.008 0.054  -0.074 292 VAL AAA CA  
2068  C C   . VAL A 292 ? 0.376 0.458 0.350 -0.004 0.052  -0.066 292 VAL AAA C   
2069  O O   . VAL A 292 ? 0.372 0.445 0.345 -0.002 0.055  -0.065 292 VAL AAA O   
2070  C CB  . VAL A 292 ? 0.387 0.489 0.373 -0.009 0.053  -0.079 292 VAL AAA CB  
2071  C CG1 . VAL A 292 ? 0.381 0.493 0.363 -0.007 0.047  -0.075 292 VAL AAA CG1 
2072  C CG2 . VAL A 292 ? 0.371 0.484 0.365 -0.012 0.054  -0.087 292 VAL AAA CG2 
2073  N N   . LEU A 293 ? 0.365 0.451 0.336 -0.004 0.047  -0.061 293 LEU AAA N   
2074  C CA  . LEU A 293 ? 0.356 0.434 0.320 -0.001 0.045  -0.054 293 LEU AAA CA  
2075  C C   . LEU A 293 ? 0.336 0.425 0.298 -0.000 0.039  -0.051 293 LEU AAA C   
2076  O O   . LEU A 293 ? 0.324 0.422 0.287 -0.002 0.036  -0.051 293 LEU AAA O   
2077  C CB  . LEU A 293 ? 0.362 0.434 0.324 -0.001 0.045  -0.050 293 LEU AAA CB  
2078  C CG  . LEU A 293 ? 0.381 0.444 0.337 0.003  0.044  -0.044 293 LEU AAA CG  
2079  C CD1 . LEU A 293 ? 0.398 0.452 0.353 0.003  0.047  -0.042 293 LEU AAA CD1 
2080  C CD2 . LEU A 293 ? 0.381 0.452 0.334 0.003  0.038  -0.040 293 LEU AAA CD2 
2081  N N   . TYR A 294 ? 0.338 0.425 0.296 0.002  0.038  -0.049 294 TYR AAA N   
2082  C CA  . TYR A 294 ? 0.350 0.446 0.306 0.003  0.034  -0.046 294 TYR AAA CA  
2083  C C   . TYR A 294 ? 0.347 0.437 0.298 0.005  0.031  -0.040 294 TYR AAA C   
2084  O O   . TYR A 294 ? 0.358 0.439 0.306 0.008  0.033  -0.038 294 TYR AAA O   
2085  C CB  . TYR A 294 ? 0.351 0.448 0.306 0.005  0.034  -0.047 294 TYR AAA CB  
2086  C CG  . TYR A 294 ? 0.358 0.466 0.317 0.003  0.033  -0.052 294 TYR AAA CG  
2087  C CD1 . TYR A 294 ? 0.359 0.480 0.319 0.002  0.029  -0.051 294 TYR AAA CD1 
2088  C CD2 . TYR A 294 ? 0.365 0.472 0.328 0.002  0.037  -0.058 294 TYR AAA CD2 
2089  C CE1 . TYR A 294 ? 0.356 0.489 0.320 0.000  0.029  -0.055 294 TYR AAA CE1 
2090  C CE2 . TYR A 294 ? 0.366 0.485 0.334 -0.000 0.037  -0.063 294 TYR AAA CE2 
2091  C CZ  . TYR A 294 ? 0.370 0.503 0.338 -0.001 0.032  -0.062 294 TYR AAA CZ  
2092  O OH  . TYR A 294 ? 0.384 0.530 0.356 -0.002 0.032  -0.067 294 TYR AAA OH  
2093  N N   . ALA A 295 ? 0.347 0.445 0.300 0.004  0.028  -0.037 295 ALA AAA N   
2094  C CA  . ALA A 295 ? 0.354 0.450 0.304 0.005  0.025  -0.032 295 ALA AAA CA  
2095  C C   . ALA A 295 ? 0.368 0.474 0.319 0.004  0.022  -0.030 295 ALA AAA C   
2096  O O   . ALA A 295 ? 0.355 0.465 0.307 0.003  0.019  -0.027 295 ALA AAA O   
2097  C CB  . ALA A 295 ? 0.354 0.447 0.305 0.003  0.025  -0.031 295 ALA AAA CB  
2098  N N   . THR A 296 ? 0.404 0.513 0.354 0.005  0.021  -0.032 296 THR AAA N   
2099  C CA  . THR A 296 ? 0.453 0.573 0.404 0.005  0.018  -0.030 296 THR AAA CA  
2100  C C   . THR A 296 ? 0.493 0.611 0.442 0.007  0.016  -0.027 296 THR AAA C   
2101  O O   . THR A 296 ? 0.551 0.677 0.502 0.006  0.014  -0.024 296 THR AAA O   
2102  C CB  . THR A 296 ? 0.443 0.570 0.396 0.005  0.019  -0.034 296 THR AAA CB  
2103  O OG1 . THR A 296 ? 0.402 0.521 0.353 0.006  0.021  -0.037 296 THR AAA OG1 
2104  C CG2 . THR A 296 ? 0.452 0.586 0.408 0.002  0.020  -0.038 296 THR AAA CG2 
2105  N N   . GLY A 297 ? 0.465 0.573 0.411 0.009  0.017  -0.027 297 GLY AAA N   
2106  C CA  . GLY A 297 ? 0.454 0.559 0.398 0.011  0.016  -0.024 297 GLY AAA CA  
2107  C C   . GLY A 297 ? 0.426 0.524 0.366 0.015  0.017  -0.025 297 GLY AAA C   
2108  O O   . GLY A 297 ? 0.381 0.473 0.320 0.015  0.020  -0.028 297 GLY AAA O   
2109  N N   . ARG A 298 ? 0.383 0.482 0.321 0.017  0.015  -0.024 298 ARG AAA N   
2110  C CA  . ARG A 298 ? 0.372 0.464 0.306 0.021  0.016  -0.025 298 ARG AAA CA  
2111  C C   . ARG A 298 ? 0.382 0.480 0.316 0.023  0.014  -0.025 298 ARG AAA C   
2112  O O   . ARG A 298 ? 0.362 0.466 0.298 0.021  0.011  -0.024 298 ARG AAA O   
2113  C CB  . ARG A 298 ? 0.344 0.430 0.276 0.023  0.016  -0.023 298 ARG AAA CB  
2114  C CG  . ARG A 298 ? 0.336 0.415 0.268 0.022  0.019  -0.023 298 ARG AAA CG  
2115  C CD  . ARG A 298 ? 0.323 0.398 0.254 0.023  0.018  -0.021 298 ARG AAA CD  
2116  N NE  . ARG A 298 ? 0.315 0.384 0.240 0.028  0.019  -0.021 298 ARG AAA NE  
2117  C CZ  . ARG A 298 ? 0.330 0.390 0.252 0.031  0.022  -0.021 298 ARG AAA CZ  
2118  N NH1 . ARG A 298 ? 0.326 0.382 0.248 0.029  0.026  -0.021 298 ARG AAA NH1 
2119  N NH2 . ARG A 298 ? 0.350 0.407 0.268 0.036  0.023  -0.020 298 ARG AAA NH2 
2120  N N   . ASN A 299 ? 0.393 0.488 0.324 0.026  0.015  -0.027 299 ASN AAA N   
2121  C CA  . ASN A 299 ? 0.399 0.499 0.328 0.029  0.013  -0.028 299 ASN AAA CA  
2122  C C   . ASN A 299 ? 0.424 0.519 0.349 0.033  0.013  -0.028 299 ASN AAA C   
2123  O O   . ASN A 299 ? 0.385 0.472 0.307 0.036  0.016  -0.027 299 ASN AAA O   
2124  C CB  . ASN A 299 ? 0.387 0.488 0.315 0.030  0.015  -0.030 299 ASN AAA CB  
2125  C CG  . ASN A 299 ? 0.370 0.478 0.303 0.025  0.015  -0.032 299 ASN AAA CG  
2126  O OD1 . ASN A 299 ? 0.360 0.466 0.293 0.025  0.017  -0.034 299 ASN AAA OD1 
2127  N ND2 . ASN A 299 ? 0.352 0.467 0.287 0.023  0.012  -0.030 299 ASN AAA ND2 
2128  N N   . PRO A 300 ? 0.449 0.549 0.374 0.035  0.010  -0.028 300 PRO AAA N   
2129  C CA  . PRO A 300 ? 0.423 0.521 0.345 0.040  0.010  -0.028 300 PRO AAA CA  
2130  C C   . PRO A 300 ? 0.430 0.523 0.346 0.045  0.012  -0.029 300 PRO AAA C   
2131  O O   . PRO A 300 ? 0.395 0.492 0.312 0.045  0.012  -0.031 300 PRO AAA O   
2132  C CB  . PRO A 300 ? 0.419 0.525 0.344 0.040  0.006  -0.030 300 PRO AAA CB  
2133  C CG  . PRO A 300 ? 0.440 0.552 0.369 0.035  0.006  -0.030 300 PRO AAA CG  
2134  C CD  . PRO A 300 ? 0.439 0.548 0.369 0.032  0.008  -0.028 300 PRO AAA CD  
2135  N N   . ASP A 301 ? 0.468 0.554 0.380 0.049  0.014  -0.028 301 ASP AAA N   
2136  C CA  . ASP A 301 ? 0.498 0.578 0.404 0.055  0.016  -0.028 301 ASP AAA CA  
2137  C C   . ASP A 301 ? 0.491 0.577 0.395 0.060  0.014  -0.030 301 ASP AAA C   
2138  O O   . ASP A 301 ? 0.476 0.560 0.375 0.065  0.014  -0.029 301 ASP AAA O   
2139  C CB  . ASP A 301 ? 0.518 0.589 0.421 0.058  0.020  -0.026 301 ASP AAA CB  
2140  C CG  . ASP A 301 ? 0.565 0.629 0.462 0.063  0.024  -0.025 301 ASP AAA CG  
2141  O OD1 . ASP A 301 ? 0.579 0.645 0.478 0.063  0.025  -0.027 301 ASP AAA OD1 
2142  O OD2 . ASP A 301 ? 0.573 0.630 0.465 0.069  0.026  -0.023 301 ASP AAA OD2 
2143  N N   . VAL A 302 ? 0.531 0.624 0.437 0.059  0.012  -0.032 302 VAL AAA N   
2144  C CA  . VAL A 302 ? 0.545 0.645 0.450 0.063  0.009  -0.034 302 VAL AAA CA  
2145  C C   . VAL A 302 ? 0.595 0.697 0.498 0.065  0.010  -0.035 302 VAL AAA C   
2146  O O   . VAL A 302 ? 0.671 0.778 0.572 0.070  0.008  -0.037 302 VAL AAA O   
2147  C CB  . VAL A 302 ? 0.512 0.622 0.424 0.058  0.005  -0.036 302 VAL AAA CB  
2148  C CG1 . VAL A 302 ? 0.506 0.615 0.419 0.057  0.004  -0.035 302 VAL AAA CG1 
2149  C CG2 . VAL A 302 ? 0.485 0.599 0.402 0.052  0.005  -0.036 302 VAL AAA CG2 
2150  N N   . LYS A 303 ? 0.632 0.728 0.535 0.064  0.013  -0.035 303 LYS AAA N   
2151  C CA  . LYS A 303 ? 0.631 0.729 0.533 0.065  0.014  -0.036 303 LYS AAA CA  
2152  C C   . LYS A 303 ? 0.624 0.718 0.521 0.073  0.015  -0.036 303 LYS AAA C   
2153  O O   . LYS A 303 ? 0.714 0.812 0.609 0.076  0.014  -0.038 303 LYS AAA O   
2154  C CB  . LYS A 303 ? 0.653 0.748 0.559 0.061  0.017  -0.037 303 LYS AAA CB  
2155  C CG  . LYS A 303 ? 0.665 0.767 0.577 0.054  0.014  -0.037 303 LYS AAA CG  
2156  C CD  . LYS A 303 ? 0.694 0.795 0.609 0.049  0.017  -0.038 303 LYS AAA CD  
2157  C CE  . LYS A 303 ? 0.694 0.805 0.614 0.044  0.014  -0.040 303 LYS AAA CE  
2158  N NZ  . LYS A 303 ? 0.683 0.796 0.606 0.040  0.016  -0.042 303 LYS AAA NZ  
2159  N N   . GLY A 304 ? 0.643 0.729 0.535 0.077  0.018  -0.033 304 GLY AAA N   
2160  C CA  . GLY A 304 ? 0.643 0.725 0.528 0.086  0.020  -0.032 304 GLY AAA CA  
2161  C C   . GLY A 304 ? 0.623 0.713 0.505 0.091  0.016  -0.033 304 GLY AAA C   
2162  O O   . GLY A 304 ? 0.674 0.762 0.551 0.099  0.017  -0.032 304 GLY AAA O   
2163  N N   . LEU A 305 ? 0.585 0.684 0.472 0.087  0.012  -0.035 305 LEU AAA N   
2164  C CA  . LEU A 305 ? 0.598 0.704 0.484 0.091  0.008  -0.037 305 LEU AAA CA  
2165  C C   . LEU A 305 ? 0.572 0.688 0.458 0.094  0.005  -0.041 305 LEU AAA C   
2166  O O   . LEU A 305 ? 0.562 0.684 0.446 0.099  0.003  -0.043 305 LEU AAA O   
2167  C CB  . LEU A 305 ? 0.569 0.679 0.460 0.085  0.005  -0.038 305 LEU AAA CB  
2168  C CG  . LEU A 305 ? 0.550 0.653 0.440 0.084  0.007  -0.035 305 LEU AAA CG  
2169  C CD1 . LEU A 305 ? 0.514 0.621 0.410 0.078  0.005  -0.036 305 LEU AAA CD1 
2170  C CD2 . LEU A 305 ? 0.556 0.656 0.439 0.092  0.008  -0.034 305 LEU AAA CD2 
2171  N N   . ASN A 306 ? 0.578 0.695 0.467 0.091  0.006  -0.042 306 ASN AAA N   
2172  C CA  . ASN A 306 ? 0.616 0.742 0.505 0.093  0.003  -0.045 306 ASN AAA CA  
2173  C C   . ASN A 306 ? 0.632 0.770 0.528 0.089  -0.001 -0.049 306 ASN AAA C   
2174  O O   . ASN A 306 ? 0.657 0.803 0.552 0.093  -0.004 -0.052 306 ASN AAA O   
2175  C CB  . ASN A 306 ? 0.669 0.796 0.552 0.103  0.004  -0.045 306 ASN AAA CB  
2176  C CG  . ASN A 306 ? 0.708 0.840 0.590 0.105  0.002  -0.048 306 ASN AAA CG  
2177  O OD1 . ASN A 306 ? 0.764 0.898 0.650 0.100  0.002  -0.049 306 ASN AAA OD1 
2178  N ND2 . ASN A 306 ? 0.738 0.876 0.615 0.114  0.001  -0.049 306 ASN AAA ND2 
2179  N N   . LEU A 307 ? 0.646 0.783 0.547 0.081  -0.002 -0.048 307 LEU AAA N   
2180  C CA  . LEU A 307 ? 0.668 0.815 0.577 0.077  -0.005 -0.051 307 LEU AAA CA  
2181  C C   . LEU A 307 ? 0.669 0.825 0.582 0.075  -0.007 -0.054 307 LEU AAA C   
2182  O O   . LEU A 307 ? 0.691 0.855 0.607 0.076  -0.009 -0.058 307 LEU AAA O   
2183  C CB  . LEU A 307 ? 0.660 0.803 0.574 0.070  -0.004 -0.049 307 LEU AAA CB  
2184  C CG  . LEU A 307 ? 0.702 0.837 0.613 0.070  -0.002 -0.046 307 LEU AAA CG  
2185  C CD1 . LEU A 307 ? 0.706 0.839 0.622 0.063  -0.002 -0.044 307 LEU AAA CD1 
2186  C CD2 . LEU A 307 ? 0.681 0.818 0.589 0.075  -0.004 -0.047 307 LEU AAA CD2 
2187  N N   . ASN A 308 ? 0.668 0.822 0.581 0.073  -0.005 -0.054 308 ASN AAA N   
2188  C CA  . ASN A 308 ? 0.668 0.831 0.585 0.070  -0.007 -0.056 308 ASN AAA CA  
2189  C C   . ASN A 308 ? 0.616 0.786 0.532 0.076  -0.009 -0.060 308 ASN AAA C   
2190  O O   . ASN A 308 ? 0.553 0.732 0.474 0.074  -0.011 -0.064 308 ASN AAA O   
2191  C CB  . ASN A 308 ? 0.687 0.846 0.603 0.068  -0.005 -0.055 308 ASN AAA CB  
2192  C CG  . ASN A 308 ? 0.742 0.910 0.664 0.064  -0.006 -0.057 308 ASN AAA CG  
2193  O OD1 . ASN A 308 ? 0.712 0.889 0.638 0.064  -0.009 -0.060 308 ASN AAA OD1 
2194  N ND2 . ASN A 308 ? 0.832 0.999 0.755 0.060  -0.005 -0.056 308 ASN AAA ND2 
2195  N N   . ALA A 309 ? 0.606 0.771 0.514 0.084  -0.008 -0.060 309 ALA AAA N   
2196  C CA  . ALA A 309 ? 0.616 0.788 0.521 0.091  -0.010 -0.063 309 ALA AAA CA  
2197  C C   . ALA A 309 ? 0.596 0.775 0.502 0.093  -0.012 -0.066 309 ALA AAA C   
2198  O O   . ALA A 309 ? 0.531 0.720 0.438 0.097  -0.015 -0.071 309 ALA AAA O   
2199  C CB  . ALA A 309 ? 0.641 0.804 0.537 0.098  -0.007 -0.060 309 ALA AAA CB  
2200  N N   . ILE A 310 ? 0.598 0.774 0.506 0.092  -0.012 -0.065 310 ILE AAA N   
2201  C CA  . ILE A 310 ? 0.587 0.770 0.496 0.095  -0.015 -0.068 310 ILE AAA CA  
2202  C C   . ILE A 310 ? 0.560 0.751 0.479 0.088  -0.017 -0.072 310 ILE AAA C   
2203  O O   . ILE A 310 ? 0.562 0.762 0.485 0.090  -0.019 -0.077 310 ILE AAA O   
2204  C CB  . ILE A 310 ? 0.642 0.818 0.546 0.097  -0.013 -0.065 310 ILE AAA CB  
2205  C CG1 . ILE A 310 ? 0.682 0.849 0.577 0.104  -0.011 -0.061 310 ILE AAA CG1 
2206  C CG2 . ILE A 310 ? 0.642 0.826 0.549 0.100  -0.016 -0.069 310 ILE AAA CG2 
2207  C CD1 . ILE A 310 ? 0.709 0.881 0.599 0.112  -0.011 -0.063 310 ILE AAA CD1 
2208  N N   . GLY A 311 ? 0.542 0.730 0.466 0.080  -0.015 -0.070 311 GLY AAA N   
2209  C CA  . GLY A 311 ? 0.522 0.717 0.456 0.073  -0.016 -0.072 311 GLY AAA CA  
2210  C C   . GLY A 311 ? 0.508 0.698 0.446 0.068  -0.016 -0.069 311 GLY AAA C   
2211  O O   . GLY A 311 ? 0.530 0.726 0.476 0.064  -0.016 -0.072 311 GLY AAA O   
2212  N N   . VAL A 312 ? 0.494 0.674 0.427 0.069  -0.014 -0.065 312 VAL AAA N   
2213  C CA  . VAL A 312 ? 0.471 0.646 0.407 0.064  -0.013 -0.062 312 VAL AAA CA  
2214  C C   . VAL A 312 ? 0.443 0.616 0.383 0.057  -0.011 -0.059 312 VAL AAA C   
2215  O O   . VAL A 312 ? 0.412 0.579 0.347 0.057  -0.010 -0.055 312 VAL AAA O   
2216  C CB  . VAL A 312 ? 0.461 0.627 0.389 0.068  -0.011 -0.059 312 VAL AAA CB  
2217  C CG1 . VAL A 312 ? 0.456 0.616 0.387 0.063  -0.010 -0.056 312 VAL AAA CG1 
2218  C CG2 . VAL A 312 ? 0.470 0.639 0.394 0.076  -0.013 -0.062 312 VAL AAA CG2 
2219  N N   . GLU A 313 ? 0.438 0.615 0.387 0.052  -0.012 -0.059 313 GLU AAA N   
2220  C CA  . GLU A 313 ? 0.463 0.641 0.417 0.045  -0.010 -0.056 313 GLU AAA CA  
2221  C C   . GLU A 313 ? 0.467 0.636 0.418 0.043  -0.008 -0.051 313 GLU AAA C   
2222  O O   . GLU A 313 ? 0.447 0.612 0.398 0.043  -0.008 -0.051 313 GLU AAA O   
2223  C CB  . GLU A 313 ? 0.483 0.668 0.446 0.041  -0.010 -0.058 313 GLU AAA CB  
2224  C CG  . GLU A 313 ? 0.514 0.709 0.481 0.042  -0.012 -0.064 313 GLU AAA CG  
2225  C CD  . GLU A 313 ? 0.544 0.741 0.508 0.044  -0.012 -0.065 313 GLU AAA CD  
2226  O OE1 . GLU A 313 ? 0.578 0.775 0.542 0.041  -0.011 -0.062 313 GLU AAA OE1 
2227  O OE2 . GLU A 313 ? 0.549 0.751 0.511 0.049  -0.014 -0.069 313 GLU AAA OE2 
2228  N N   . VAL A 314 ? 0.458 0.625 0.409 0.040  -0.007 -0.048 314 VAL AAA N   
2229  C CA  . VAL A 314 ? 0.462 0.622 0.411 0.037  -0.005 -0.044 314 VAL AAA CA  
2230  C C   . VAL A 314 ? 0.458 0.621 0.412 0.031  -0.004 -0.042 314 VAL AAA C   
2231  O O   . VAL A 314 ? 0.503 0.673 0.461 0.030  -0.005 -0.043 314 VAL AAA O   
2232  C CB  . VAL A 314 ? 0.472 0.625 0.413 0.040  -0.004 -0.043 314 VAL AAA CB  
2233  C CG1 . VAL A 314 ? 0.460 0.608 0.395 0.046  -0.004 -0.044 314 VAL AAA CG1 
2234  C CG2 . VAL A 314 ? 0.465 0.622 0.405 0.040  -0.004 -0.044 314 VAL AAA CG2 
2235  N N   . SER A 315 ? 0.431 0.591 0.387 0.028  -0.003 -0.038 315 SER AAA N   
2236  C CA  . SER A 315 ? 0.438 0.602 0.399 0.023  -0.002 -0.035 315 SER AAA CA  
2237  C C   . SER A 315 ? 0.446 0.610 0.403 0.023  -0.001 -0.034 315 SER AAA C   
2238  O O   . SER A 315 ? 0.410 0.570 0.361 0.026  -0.001 -0.035 315 SER AAA O   
2239  C CB  . SER A 315 ? 0.440 0.600 0.404 0.021  -0.001 -0.032 315 SER AAA CB  
2240  O OG  . SER A 315 ? 0.433 0.585 0.391 0.022  -0.001 -0.030 315 SER AAA OG  
2241  N N   . ASP A 316 ? 0.496 0.663 0.456 0.020  -0.000 -0.031 316 ASP AAA N   
2242  C CA  . ASP A 316 ? 0.524 0.693 0.481 0.019  0.000  -0.030 316 ASP AAA CA  
2243  C C   . ASP A 316 ? 0.513 0.675 0.466 0.020  0.001  -0.030 316 ASP AAA C   
2244  O O   . ASP A 316 ? 0.534 0.695 0.483 0.020  0.002  -0.031 316 ASP AAA O   
2245  C CB  . ASP A 316 ? 0.536 0.712 0.498 0.015  0.001  -0.027 316 ASP AAA CB  
2246  C CG  . ASP A 316 ? 0.540 0.724 0.506 0.015  0.001  -0.028 316 ASP AAA CG  
2247  O OD1 . ASP A 316 ? 0.569 0.755 0.534 0.017  0.000  -0.031 316 ASP AAA OD1 
2248  O OD2 . ASP A 316 ? 0.523 0.712 0.495 0.012  0.002  -0.025 316 ASP AAA OD2 
2249  N N   . SER A 317 ? 0.519 0.675 0.473 0.019  0.001  -0.028 317 SER AAA N   
2250  C CA  . SER A 317 ? 0.487 0.635 0.436 0.020  0.003  -0.028 317 SER AAA CA  
2251  C C   . SER A 317 ? 0.450 0.591 0.394 0.024  0.003  -0.030 317 SER AAA C   
2252  O O   . SER A 317 ? 0.452 0.586 0.393 0.025  0.004  -0.030 317 SER AAA O   
2253  C CB  . SER A 317 ? 0.501 0.646 0.453 0.018  0.003  -0.025 317 SER AAA CB  
2254  O OG  . SER A 317 ? 0.505 0.648 0.458 0.020  0.002  -0.026 317 SER AAA OG  
2255  N N   . GLY A 318 ? 0.406 0.549 0.349 0.027  0.001  -0.032 318 GLY AAA N   
2256  C CA  . GLY A 318 ? 0.395 0.533 0.333 0.032  0.002  -0.034 318 GLY AAA CA  
2257  C C   . GLY A 318 ? 0.371 0.505 0.308 0.034  0.001  -0.034 318 GLY AAA C   
2258  O O   . GLY A 318 ? 0.367 0.497 0.299 0.038  0.001  -0.035 318 GLY AAA O   
2259  N N   . LYS A 319 ? 0.373 0.509 0.316 0.031  0.000  -0.033 319 LYS AAA N   
2260  C CA  . LYS A 319 ? 0.394 0.528 0.337 0.032  -0.001 -0.033 319 LYS AAA CA  
2261  C C   . LYS A 319 ? 0.416 0.556 0.361 0.034  -0.002 -0.036 319 LYS AAA C   
2262  O O   . LYS A 319 ? 0.418 0.565 0.368 0.033  -0.003 -0.037 319 LYS AAA O   
2263  C CB  . LYS A 319 ? 0.369 0.502 0.317 0.028  -0.000 -0.030 319 LYS AAA CB  
2264  C CG  . LYS A 319 ? 0.369 0.495 0.314 0.027  0.002  -0.028 319 LYS AAA CG  
2265  C CD  . LYS A 319 ? 0.360 0.484 0.308 0.024  0.002  -0.026 319 LYS AAA CD  
2266  C CE  . LYS A 319 ? 0.349 0.467 0.295 0.023  0.003  -0.024 319 LYS AAA CE  
2267  N NZ  . LYS A 319 ? 0.336 0.452 0.286 0.021  0.003  -0.022 319 LYS AAA NZ  
2268  N N   . ILE A 320 ? 0.436 0.574 0.379 0.038  -0.003 -0.038 320 ILE AAA N   
2269  C CA  . ILE A 320 ? 0.447 0.591 0.392 0.041  -0.005 -0.042 320 ILE AAA CA  
2270  C C   . ILE A 320 ? 0.450 0.599 0.404 0.037  -0.006 -0.043 320 ILE AAA C   
2271  O O   . ILE A 320 ? 0.437 0.583 0.394 0.034  -0.005 -0.041 320 ILE AAA O   
2272  C CB  . ILE A 320 ? 0.467 0.608 0.406 0.047  -0.006 -0.044 320 ILE AAA CB  
2273  C CG1 . ILE A 320 ? 0.498 0.634 0.429 0.052  -0.005 -0.043 320 ILE AAA CG1 
2274  C CG2 . ILE A 320 ? 0.474 0.624 0.417 0.050  -0.008 -0.049 320 ILE AAA CG2 
2275  C CD1 . ILE A 320 ? 0.532 0.665 0.457 0.058  -0.004 -0.043 320 ILE AAA CD1 
2276  N N   . ILE A 321 ? 0.439 0.596 0.398 0.036  -0.007 -0.046 321 ILE AAA N   
2277  C CA  . ILE A 321 ? 0.448 0.610 0.417 0.032  -0.007 -0.047 321 ILE AAA CA  
2278  C C   . ILE A 321 ? 0.440 0.605 0.410 0.035  -0.008 -0.052 321 ILE AAA C   
2279  O O   . ILE A 321 ? 0.413 0.582 0.381 0.040  -0.010 -0.056 321 ILE AAA O   
2280  C CB  . ILE A 321 ? 0.477 0.647 0.452 0.029  -0.007 -0.048 321 ILE AAA CB  
2281  C CG1 . ILE A 321 ? 0.480 0.649 0.455 0.026  -0.005 -0.043 321 ILE AAA CG1 
2282  C CG2 . ILE A 321 ? 0.497 0.672 0.482 0.026  -0.006 -0.051 321 ILE AAA CG2 
2283  C CD1 . ILE A 321 ? 0.487 0.662 0.464 0.025  -0.005 -0.044 321 ILE AAA CD1 
2284  N N   . ALA A 322 ? 0.411 0.573 0.385 0.034  -0.008 -0.051 322 ALA AAA N   
2285  C CA  . ALA A 322 ? 0.393 0.557 0.368 0.037  -0.009 -0.055 322 ALA AAA CA  
2286  C C   . ALA A 322 ? 0.370 0.532 0.353 0.032  -0.008 -0.054 322 ALA AAA C   
2287  O O   . ALA A 322 ? 0.310 0.467 0.290 0.034  -0.008 -0.053 322 ALA AAA O   
2288  C CB  . ALA A 322 ? 0.381 0.541 0.346 0.043  -0.010 -0.055 322 ALA AAA CB  
2289  N N   . PRO A 323 ? 0.383 0.549 0.376 0.027  -0.007 -0.054 323 PRO AAA N   
2290  C CA  . PRO A 323 ? 0.391 0.555 0.392 0.023  -0.005 -0.052 323 PRO AAA CA  
2291  C C   . PRO A 323 ? 0.391 0.556 0.395 0.025  -0.007 -0.057 323 PRO AAA C   
2292  O O   . PRO A 323 ? 0.375 0.535 0.381 0.023  -0.005 -0.055 323 PRO AAA O   
2293  C CB  . PRO A 323 ? 0.378 0.547 0.390 0.018  -0.004 -0.053 323 PRO AAA CB  
2294  C CG  . PRO A 323 ? 0.362 0.538 0.373 0.021  -0.005 -0.057 323 PRO AAA CG  
2295  C CD  . PRO A 323 ? 0.369 0.542 0.367 0.026  -0.007 -0.056 323 PRO AAA CD  
2296  N N   . LYS A 324 ? 0.419 0.590 0.422 0.029  -0.009 -0.063 324 LYS AAA N   
2297  C CA  . LYS A 324 ? 0.404 0.577 0.408 0.032  -0.010 -0.069 324 LYS AAA CA  
2298  C C   . LYS A 324 ? 0.377 0.550 0.370 0.039  -0.012 -0.070 324 LYS AAA C   
2299  O O   . LYS A 324 ? 0.410 0.589 0.403 0.043  -0.014 -0.076 324 LYS AAA O   
2300  C CB  . LYS A 324 ? 0.435 0.619 0.451 0.031  -0.010 -0.076 324 LYS AAA CB  
2301  C CG  . LYS A 324 ? 0.494 0.678 0.523 0.025  -0.008 -0.076 324 LYS AAA CG  
2302  C CD  . LYS A 324 ? 0.542 0.734 0.579 0.022  -0.007 -0.079 324 LYS AAA CD  
2303  C CE  . LYS A 324 ? 0.597 0.788 0.648 0.016  -0.003 -0.077 324 LYS AAA CE  
2304  N NZ  . LYS A 324 ? 0.614 0.814 0.677 0.014  -0.002 -0.084 324 LYS AAA NZ  
2305  N N   . ASP A 325 ? 0.352 0.518 0.335 0.041  -0.012 -0.064 325 ASP AAA N   
2306  C CA  . ASP A 325 ? 0.367 0.531 0.338 0.048  -0.013 -0.064 325 ASP AAA CA  
2307  C C   . ASP A 325 ? 0.378 0.548 0.345 0.052  -0.014 -0.067 325 ASP AAA C   
2308  O O   . ASP A 325 ? 0.380 0.547 0.337 0.057  -0.014 -0.065 325 ASP AAA O   
2309  C CB  . ASP A 325 ? 0.393 0.557 0.362 0.051  -0.013 -0.066 325 ASP AAA CB  
2310  C CG  . ASP A 325 ? 0.392 0.550 0.365 0.047  -0.012 -0.063 325 ASP AAA CG  
2311  O OD1 . ASP A 325 ? 0.361 0.512 0.334 0.043  -0.010 -0.057 325 ASP AAA OD1 
2312  O OD2 . ASP A 325 ? 0.430 0.591 0.406 0.048  -0.013 -0.067 325 ASP AAA OD2 
2313  N N   . ALA A 326 ? 0.390 0.570 0.366 0.051  -0.015 -0.073 326 ALA AAA N   
2314  C CA  . ALA A 326 ? 0.404 0.592 0.378 0.055  -0.017 -0.077 326 ALA AAA CA  
2315  C C   . ALA A 326 ? 0.394 0.578 0.366 0.052  -0.015 -0.073 326 ALA AAA C   
2316  O O   . ALA A 326 ? 0.391 0.576 0.371 0.045  -0.014 -0.071 326 ALA AAA O   
2317  C CB  . ALA A 326 ? 0.390 0.589 0.375 0.054  -0.018 -0.085 326 ALA AAA CB  
2318  N N   . THR A 327 ? 0.402 0.585 0.365 0.056  -0.016 -0.071 327 THR AAA N   
2319  C CA  . THR A 327 ? 0.425 0.607 0.386 0.055  -0.015 -0.069 327 THR AAA CA  
2320  C C   . THR A 327 ? 0.430 0.622 0.398 0.054  -0.016 -0.074 327 THR AAA C   
2321  O O   . THR A 327 ? 0.436 0.636 0.410 0.055  -0.017 -0.080 327 THR AAA O   
2322  C CB  . THR A 327 ? 0.427 0.603 0.376 0.061  -0.015 -0.066 327 THR AAA CB  
2323  O OG1 . THR A 327 ? 0.462 0.645 0.408 0.067  -0.017 -0.071 327 THR AAA OG1 
2324  C CG2 . THR A 327 ? 0.429 0.596 0.372 0.062  -0.013 -0.061 327 THR AAA CG2 
2325  N N   . SER A 328 ? 0.430 0.623 0.396 0.053  -0.016 -0.073 328 SER AAA N   
2326  C CA  . SER A 328 ? 0.426 0.629 0.398 0.053  -0.017 -0.077 328 SER AAA CA  
2327  C C   . SER A 328 ? 0.426 0.635 0.393 0.061  -0.019 -0.083 328 SER AAA C   
2328  O O   . SER A 328 ? 0.370 0.589 0.343 0.061  -0.020 -0.089 328 SER AAA O   
2329  C CB  . SER A 328 ? 0.433 0.634 0.403 0.051  -0.015 -0.074 328 SER AAA CB  
2330  O OG  . SER A 328 ? 0.453 0.647 0.412 0.054  -0.015 -0.070 328 SER AAA OG  
2331  N N   . VAL A 329 ? 0.434 0.638 0.391 0.067  -0.019 -0.081 329 VAL AAA N   
2332  C CA  . VAL A 329 ? 0.439 0.649 0.390 0.075  -0.022 -0.086 329 VAL AAA CA  
2333  C C   . VAL A 329 ? 0.471 0.684 0.424 0.077  -0.023 -0.088 329 VAL AAA C   
2334  O O   . VAL A 329 ? 0.479 0.683 0.427 0.078  -0.021 -0.084 329 VAL AAA O   
2335  C CB  . VAL A 329 ? 0.449 0.653 0.389 0.081  -0.021 -0.081 329 VAL AAA CB  
2336  C CG1 . VAL A 329 ? 0.452 0.661 0.384 0.091  -0.023 -0.084 329 VAL AAA CG1 
2337  C CG2 . VAL A 329 ? 0.457 0.661 0.396 0.079  -0.020 -0.080 329 VAL AAA CG2 
2338  N N   . PRO A 330 ? 0.468 0.693 0.428 0.079  -0.025 -0.096 330 PRO AAA N   
2339  C CA  . PRO A 330 ? 0.469 0.697 0.434 0.078  -0.025 -0.100 330 PRO AAA CA  
2340  C C   . PRO A 330 ? 0.487 0.714 0.443 0.086  -0.026 -0.099 330 PRO AAA C   
2341  O O   . PRO A 330 ? 0.540 0.767 0.499 0.085  -0.026 -0.101 330 PRO AAA O   
2342  C CB  . PRO A 330 ? 0.477 0.719 0.453 0.078  -0.027 -0.109 330 PRO AAA CB  
2343  C CG  . PRO A 330 ? 0.484 0.732 0.457 0.081  -0.028 -0.111 330 PRO AAA CG  
2344  C CD  . PRO A 330 ? 0.461 0.697 0.424 0.081  -0.026 -0.102 330 PRO AAA CD  
2345  N N   . SER A 331 ? 0.455 0.680 0.400 0.094  -0.026 -0.096 331 SER AAA N   
2346  C CA  . SER A 331 ? 0.445 0.667 0.379 0.102  -0.026 -0.094 331 SER AAA CA  
2347  C C   . SER A 331 ? 0.455 0.662 0.382 0.100  -0.023 -0.086 331 SER AAA C   
2348  O O   . SER A 331 ? 0.464 0.667 0.383 0.106  -0.023 -0.083 331 SER AAA O   
2349  C CB  . SER A 331 ? 0.422 0.649 0.347 0.111  -0.028 -0.096 331 SER AAA CB  
2350  O OG  . SER A 331 ? 0.424 0.644 0.344 0.110  -0.026 -0.091 331 SER AAA OG  
2351  N N   . ILE A 332 ? 0.440 0.639 0.370 0.092  -0.022 -0.081 332 ILE AAA N   
2352  C CA  . ILE A 332 ? 0.437 0.622 0.362 0.090  -0.019 -0.074 332 ILE AAA CA  
2353  C C   . ILE A 332 ? 0.412 0.592 0.345 0.081  -0.018 -0.072 332 ILE AAA C   
2354  O O   . ILE A 332 ? 0.410 0.594 0.352 0.075  -0.018 -0.073 332 ILE AAA O   
2355  C CB  . ILE A 332 ? 0.450 0.630 0.371 0.090  -0.017 -0.070 332 ILE AAA CB  
2356  C CG1 . ILE A 332 ? 0.441 0.624 0.353 0.099  -0.018 -0.071 332 ILE AAA CG1 
2357  C CG2 . ILE A 332 ? 0.449 0.616 0.367 0.086  -0.014 -0.063 332 ILE AAA CG2 
2358  C CD1 . ILE A 332 ? 0.459 0.636 0.366 0.099  -0.016 -0.067 332 ILE AAA CD1 
2359  N N   . PHE A 333 ? 0.435 0.608 0.365 0.082  -0.017 -0.069 333 PHE AAA N   
2360  C CA  . PHE A 333 ? 0.416 0.585 0.352 0.075  -0.016 -0.067 333 PHE AAA CA  
2361  C C   . PHE A 333 ? 0.406 0.563 0.337 0.073  -0.013 -0.059 333 PHE AAA C   
2362  O O   . PHE A 333 ? 0.416 0.567 0.337 0.077  -0.011 -0.056 333 PHE AAA O   
2363  C CB  . PHE A 333 ? 0.416 0.589 0.354 0.077  -0.017 -0.070 333 PHE AAA CB  
2364  C CG  . PHE A 333 ? 0.438 0.624 0.383 0.078  -0.019 -0.078 333 PHE AAA CG  
2365  C CD1 . PHE A 333 ? 0.441 0.635 0.381 0.086  -0.021 -0.082 333 PHE AAA CD1 
2366  C CD2 . PHE A 333 ? 0.434 0.624 0.392 0.072  -0.020 -0.081 333 PHE AAA CD2 
2367  C CE1 . PHE A 333 ? 0.440 0.647 0.387 0.088  -0.024 -0.090 333 PHE AAA CE1 
2368  C CE2 . PHE A 333 ? 0.424 0.626 0.389 0.072  -0.022 -0.090 333 PHE AAA CE2 
2369  C CZ  . PHE A 333 ? 0.429 0.641 0.390 0.080  -0.024 -0.094 333 PHE AAA CZ  
2370  N N   . ALA A 334 ? 0.385 0.536 0.321 0.066  -0.012 -0.057 334 ALA AAA N   
2371  C CA  . ALA A 334 ? 0.372 0.513 0.304 0.063  -0.009 -0.051 334 ALA AAA CA  
2372  C C   . ALA A 334 ? 0.339 0.477 0.277 0.058  -0.009 -0.049 334 ALA AAA C   
2373  O O   . ALA A 334 ? 0.319 0.462 0.265 0.054  -0.010 -0.052 334 ALA AAA O   
2374  C CB  . ALA A 334 ? 0.371 0.511 0.304 0.059  -0.008 -0.049 334 ALA AAA CB  
2375  N N   . VAL A 335 ? 0.340 0.468 0.272 0.058  -0.007 -0.045 335 VAL AAA N   
2376  C CA  . VAL A 335 ? 0.337 0.461 0.273 0.054  -0.006 -0.043 335 VAL AAA CA  
2377  C C   . VAL A 335 ? 0.323 0.437 0.254 0.052  -0.003 -0.038 335 VAL AAA C   
2378  O O   . VAL A 335 ? 0.307 0.418 0.232 0.055  -0.002 -0.036 335 VAL AAA O   
2379  C CB  . VAL A 335 ? 0.350 0.474 0.285 0.057  -0.006 -0.045 335 VAL AAA CB  
2380  C CG1 . VAL A 335 ? 0.363 0.498 0.303 0.059  -0.009 -0.051 335 VAL AAA CG1 
2381  C CG2 . VAL A 335 ? 0.351 0.469 0.275 0.064  -0.005 -0.042 335 VAL AAA CG2 
2382  N N   . GLY A 336 ? 0.324 0.434 0.259 0.047  -0.002 -0.035 336 GLY AAA N   
2383  C CA  . GLY A 336 ? 0.334 0.435 0.266 0.045  0.000  -0.031 336 GLY AAA CA  
2384  C C   . GLY A 336 ? 0.336 0.439 0.271 0.040  0.001  -0.029 336 GLY AAA C   
2385  O O   . GLY A 336 ? 0.327 0.437 0.268 0.038  -0.000 -0.031 336 GLY AAA O   
2386  N N   . ASP A 337 ? 0.352 0.448 0.282 0.040  0.003  -0.027 337 ASP AAA N   
2387  C CA  . ASP A 337 ? 0.367 0.464 0.300 0.036  0.004  -0.025 337 ASP AAA CA  
2388  C C   . ASP A 337 ? 0.383 0.485 0.316 0.036  0.003  -0.027 337 ASP AAA C   
2389  O O   . ASP A 337 ? 0.367 0.472 0.304 0.032  0.003  -0.026 337 ASP AAA O   
2390  C CB  . ASP A 337 ? 0.385 0.474 0.313 0.036  0.007  -0.023 337 ASP AAA CB  
2391  C CG  . ASP A 337 ? 0.391 0.475 0.320 0.034  0.008  -0.021 337 ASP AAA CG  
2392  O OD1 . ASP A 337 ? 0.389 0.474 0.321 0.033  0.007  -0.021 337 ASP AAA OD1 
2393  O OD2 . ASP A 337 ? 0.401 0.479 0.327 0.034  0.011  -0.020 337 ASP AAA OD2 
2394  N N   . ILE A 338 ? 0.372 0.476 0.302 0.041  0.002  -0.029 338 ILE AAA N   
2395  C CA  . ILE A 338 ? 0.378 0.487 0.308 0.042  0.002  -0.031 338 ILE AAA CA  
2396  C C   . ILE A 338 ? 0.386 0.504 0.323 0.039  -0.001 -0.033 338 ILE AAA C   
2397  O O   . ILE A 338 ? 0.405 0.529 0.343 0.038  -0.001 -0.034 338 ILE AAA O   
2398  C CB  . ILE A 338 ? 0.377 0.485 0.300 0.048  0.002  -0.032 338 ILE AAA CB  
2399  C CG1 . ILE A 338 ? 0.374 0.487 0.298 0.052  -0.000 -0.035 338 ILE AAA CG1 
2400  C CG2 . ILE A 338 ? 0.382 0.481 0.298 0.051  0.005  -0.030 338 ILE AAA CG2 
2401  C CD1 . ILE A 338 ? 0.387 0.499 0.303 0.060  -0.000 -0.036 338 ILE AAA CD1 
2402  N N   . VAL A 339 ? 0.399 0.519 0.341 0.037  -0.001 -0.033 339 VAL AAA N   
2403  C CA  . VAL A 339 ? 0.412 0.541 0.362 0.035  -0.003 -0.035 339 VAL AAA CA  
2404  C C   . VAL A 339 ? 0.418 0.547 0.374 0.029  -0.002 -0.032 339 VAL AAA C   
2405  O O   . VAL A 339 ? 0.398 0.523 0.354 0.026  -0.001 -0.029 339 VAL AAA O   
2406  C CB  . VAL A 339 ? 0.421 0.552 0.374 0.036  -0.004 -0.038 339 VAL AAA CB  
2407  C CG1 . VAL A 339 ? 0.429 0.568 0.392 0.033  -0.005 -0.041 339 VAL AAA CG1 
2408  C CG2 . VAL A 339 ? 0.408 0.539 0.355 0.043  -0.005 -0.041 339 VAL AAA CG2 
2409  N N   . GLU A 340 ? 0.458 0.594 0.418 0.027  -0.002 -0.033 340 GLU AAA N   
2410  C CA  . GLU A 340 ? 0.479 0.617 0.444 0.022  -0.001 -0.030 340 GLU AAA CA  
2411  C C   . GLU A 340 ? 0.460 0.600 0.434 0.019  -0.001 -0.029 340 GLU AAA C   
2412  O O   . GLU A 340 ? 0.399 0.542 0.377 0.020  -0.002 -0.033 340 GLU AAA O   
2413  C CB  . GLU A 340 ? 0.572 0.718 0.540 0.021  -0.002 -0.031 340 GLU AAA CB  
2414  C CG  . GLU A 340 ? 0.659 0.809 0.634 0.016  -0.000 -0.028 340 GLU AAA CG  
2415  C CD  . GLU A 340 ? 0.725 0.879 0.700 0.015  0.000  -0.026 340 GLU AAA CD  
2416  O OE1 . GLU A 340 ? 0.820 0.980 0.800 0.014  0.001  -0.027 340 GLU AAA OE1 
2417  O OE2 . GLU A 340 ? 0.760 0.911 0.729 0.015  0.001  -0.024 340 GLU AAA OE2 
2418  N N   . GLY A 341 ? 0.425 0.563 0.401 0.016  0.000  -0.025 341 GLY AAA N   
2419  C CA  . GLY A 341 ? 0.404 0.542 0.388 0.012  0.001  -0.023 341 GLY AAA CA  
2420  C C   . GLY A 341 ? 0.396 0.529 0.380 0.013  0.001  -0.024 341 GLY AAA C   
2421  O O   . GLY A 341 ? 0.391 0.526 0.384 0.011  0.002  -0.024 341 GLY AAA O   
2422  N N   . ARG A 342 ? 0.385 0.514 0.363 0.016  0.000  -0.024 342 ARG AAA N   
2423  C CA  . ARG A 342 ? 0.397 0.520 0.374 0.016  0.000  -0.024 342 ARG AAA CA  
2424  C C   . ARG A 342 ? 0.371 0.488 0.342 0.016  0.001  -0.021 342 ARG AAA C   
2425  O O   . ARG A 342 ? 0.330 0.445 0.295 0.018  0.002  -0.021 342 ARG AAA O   
2426  C CB  . ARG A 342 ? 0.396 0.520 0.371 0.020  -0.001 -0.029 342 ARG AAA CB  
2427  C CG  . ARG A 342 ? 0.404 0.525 0.370 0.025  -0.002 -0.030 342 ARG AAA CG  
2428  C CD  . ARG A 342 ? 0.404 0.526 0.367 0.029  -0.003 -0.035 342 ARG AAA CD  
2429  N NE  . ARG A 342 ? 0.400 0.531 0.370 0.030  -0.004 -0.039 342 ARG AAA NE  
2430  C CZ  . ARG A 342 ? 0.393 0.528 0.362 0.034  -0.006 -0.044 342 ARG AAA CZ  
2431  N NH1 . ARG A 342 ? 0.401 0.533 0.364 0.038  -0.006 -0.044 342 ARG AAA NH1 
2432  N NH2 . ARG A 342 ? 0.382 0.525 0.357 0.034  -0.007 -0.048 342 ARG AAA NH2 
2433  N N   . PRO A 343 ? 0.371 0.484 0.343 0.015  0.002  -0.020 343 PRO AAA N   
2434  C CA  . PRO A 343 ? 0.381 0.488 0.348 0.015  0.003  -0.017 343 PRO AAA CA  
2435  C C   . PRO A 343 ? 0.389 0.492 0.348 0.019  0.003  -0.019 343 PRO AAA C   
2436  O O   . PRO A 343 ? 0.386 0.489 0.344 0.022  0.002  -0.022 343 PRO AAA O   
2437  C CB  . PRO A 343 ? 0.368 0.473 0.340 0.013  0.003  -0.016 343 PRO AAA CB  
2438  C CG  . PRO A 343 ? 0.369 0.479 0.350 0.011  0.003  -0.017 343 PRO AAA CG  
2439  C CD  . PRO A 343 ? 0.364 0.479 0.345 0.013  0.002  -0.020 343 PRO AAA CD  
2440  N N   . GLU A 344 ? 0.397 0.496 0.351 0.019  0.004  -0.018 344 GLU AAA N   
2441  C CA  . GLU A 344 ? 0.412 0.505 0.359 0.022  0.005  -0.019 344 GLU AAA CA  
2442  C C   . GLU A 344 ? 0.395 0.483 0.341 0.022  0.006  -0.018 344 GLU AAA C   
2443  O O   . GLU A 344 ? 0.404 0.487 0.347 0.021  0.008  -0.016 344 GLU AAA O   
2444  C CB  . GLU A 344 ? 0.450 0.543 0.394 0.022  0.007  -0.018 344 GLU AAA CB  
2445  C CG  . GLU A 344 ? 0.464 0.563 0.409 0.021  0.006  -0.019 344 GLU AAA CG  
2446  C CD  . GLU A 344 ? 0.508 0.608 0.452 0.020  0.007  -0.019 344 GLU AAA CD  
2447  O OE1 . GLU A 344 ? 0.536 0.630 0.477 0.020  0.009  -0.018 344 GLU AAA OE1 
2448  O OE2 . GLU A 344 ? 0.517 0.622 0.462 0.020  0.006  -0.019 344 GLU AAA OE2 
2449  N N   . LEU A 345 ? 0.369 0.456 0.316 0.024  0.005  -0.019 345 LEU AAA N   
2450  C CA  . LEU A 345 ? 0.340 0.422 0.286 0.024  0.006  -0.018 345 LEU AAA CA  
2451  C C   . LEU A 345 ? 0.329 0.409 0.270 0.029  0.005  -0.020 345 LEU AAA C   
2452  O O   . LEU A 345 ? 0.302 0.387 0.244 0.032  0.004  -0.023 345 LEU AAA O   
2453  C CB  . LEU A 345 ? 0.345 0.430 0.299 0.021  0.005  -0.017 345 LEU AAA CB  
2454  C CG  . LEU A 345 ? 0.354 0.441 0.312 0.016  0.005  -0.015 345 LEU AAA CG  
2455  C CD1 . LEU A 345 ? 0.345 0.435 0.311 0.014  0.005  -0.014 345 LEU AAA CD1 
2456  C CD2 . LEU A 345 ? 0.357 0.438 0.312 0.015  0.007  -0.013 345 LEU AAA CD2 
2457  N N   . THR A 346 ? 0.310 0.384 0.247 0.031  0.007  -0.019 346 THR AAA N   
2458  C CA  . THR A 346 ? 0.315 0.387 0.246 0.037  0.007  -0.021 346 THR AAA CA  
2459  C C   . THR A 346 ? 0.311 0.389 0.247 0.038  0.005  -0.024 346 THR AAA C   
2460  O O   . THR A 346 ? 0.317 0.399 0.251 0.042  0.003  -0.026 346 THR AAA O   
2461  C CB  . THR A 346 ? 0.320 0.383 0.246 0.038  0.010  -0.019 346 THR AAA CB  
2462  O OG1 . THR A 346 ? 0.330 0.390 0.251 0.040  0.012  -0.017 346 THR AAA OG1 
2463  C CG2 . THR A 346 ? 0.318 0.381 0.240 0.043  0.010  -0.020 346 THR AAA CG2 
2464  N N   . PRO A 347 ? 0.307 0.386 0.249 0.034  0.004  -0.024 347 PRO AAA N   
2465  C CA  . PRO A 347 ? 0.298 0.382 0.244 0.035  0.002  -0.027 347 PRO AAA CA  
2466  C C   . PRO A 347 ? 0.303 0.396 0.254 0.035  -0.000 -0.030 347 PRO AAA C   
2467  O O   . PRO A 347 ? 0.326 0.424 0.279 0.038  -0.002 -0.034 347 PRO AAA O   
2468  C CB  . PRO A 347 ? 0.289 0.372 0.243 0.031  0.002  -0.026 347 PRO AAA CB  
2469  C CG  . PRO A 347 ? 0.296 0.371 0.244 0.030  0.004  -0.022 347 PRO AAA CG  
2470  C CD  . PRO A 347 ? 0.293 0.368 0.237 0.030  0.005  -0.021 347 PRO AAA CD  
2471  N N   . VAL A 348 ? 0.320 0.413 0.273 0.032  0.000  -0.029 348 VAL AAA N   
2472  C CA  . VAL A 348 ? 0.329 0.430 0.287 0.032  -0.001 -0.031 348 VAL AAA CA  
2473  C C   . VAL A 348 ? 0.335 0.438 0.286 0.037  -0.002 -0.034 348 VAL AAA C   
2474  O O   . VAL A 348 ? 0.370 0.481 0.325 0.039  -0.004 -0.038 348 VAL AAA O   
2475  C CB  . VAL A 348 ? 0.328 0.430 0.290 0.027  -0.000 -0.028 348 VAL AAA CB  
2476  C CG1 . VAL A 348 ? 0.327 0.436 0.293 0.027  -0.002 -0.031 348 VAL AAA CG1 
2477  C CG2 . VAL A 348 ? 0.339 0.439 0.307 0.022  0.000  -0.026 348 VAL AAA CG2 
2478  N N   . ALA A 349 ? 0.326 0.424 0.269 0.040  -0.001 -0.031 349 ALA AAA N   
2479  C CA  . ALA A 349 ? 0.336 0.435 0.272 0.046  -0.001 -0.032 349 ALA AAA CA  
2480  C C   . ALA A 349 ? 0.347 0.449 0.281 0.051  -0.002 -0.036 349 ALA AAA C   
2481  O O   . ALA A 349 ? 0.356 0.465 0.290 0.055  -0.004 -0.039 349 ALA AAA O   
2482  C CB  . ALA A 349 ? 0.330 0.420 0.258 0.047  0.002  -0.029 349 ALA AAA CB  
2483  N N   . VAL A 350 ? 0.357 0.454 0.289 0.052  -0.001 -0.034 350 VAL AAA N   
2484  C CA  . VAL A 350 ? 0.365 0.464 0.294 0.057  -0.002 -0.037 350 VAL AAA CA  
2485  C C   . VAL A 350 ? 0.356 0.466 0.294 0.056  -0.005 -0.042 350 VAL AAA C   
2486  O O   . VAL A 350 ? 0.326 0.442 0.261 0.061  -0.006 -0.046 350 VAL AAA O   
2487  C CB  . VAL A 350 ? 0.366 0.458 0.294 0.056  -0.000 -0.034 350 VAL AAA CB  
2488  C CG1 . VAL A 350 ? 0.362 0.459 0.290 0.060  -0.001 -0.037 350 VAL AAA CG1 
2489  C CG2 . VAL A 350 ? 0.379 0.462 0.299 0.057  0.003  -0.029 350 VAL AAA CG2 
2490  N N   . LYS A 351 ? 0.360 0.471 0.307 0.050  -0.005 -0.043 351 LYS AAA N   
2491  C CA  . LYS A 351 ? 0.371 0.490 0.327 0.049  -0.007 -0.049 351 LYS AAA CA  
2492  C C   . LYS A 351 ? 0.361 0.489 0.320 0.050  -0.009 -0.052 351 LYS AAA C   
2493  O O   . LYS A 351 ? 0.389 0.525 0.351 0.053  -0.010 -0.058 351 LYS AAA O   
2494  C CB  . LYS A 351 ? 0.375 0.494 0.341 0.042  -0.007 -0.048 351 LYS AAA CB  
2495  C CG  . LYS A 351 ? 0.413 0.540 0.390 0.041  -0.008 -0.055 351 LYS AAA CG  
2496  C CD  . LYS A 351 ? 0.450 0.575 0.437 0.035  -0.007 -0.054 351 LYS AAA CD  
2497  C CE  . LYS A 351 ? 0.457 0.577 0.442 0.036  -0.007 -0.053 351 LYS AAA CE  
2498  N NZ  . LYS A 351 ? 0.468 0.595 0.452 0.040  -0.008 -0.058 351 LYS AAA NZ  
2499  N N   . ALA A 352 ? 0.376 0.501 0.333 0.048  -0.008 -0.049 352 ALA AAA N   
2500  C CA  . ALA A 352 ? 0.387 0.520 0.346 0.049  -0.009 -0.053 352 ALA AAA CA  
2501  C C   . ALA A 352 ? 0.392 0.529 0.342 0.057  -0.010 -0.055 352 ALA AAA C   
2502  O O   . ALA A 352 ? 0.367 0.513 0.321 0.060  -0.012 -0.061 352 ALA AAA O   
2503  C CB  . ALA A 352 ? 0.380 0.510 0.338 0.046  -0.008 -0.049 352 ALA AAA CB  
2504  N N   . GLY A 353 ? 0.400 0.529 0.340 0.061  -0.009 -0.051 353 GLY AAA N   
2505  C CA  . GLY A 353 ? 0.420 0.552 0.351 0.070  -0.009 -0.052 353 GLY AAA CA  
2506  C C   . GLY A 353 ? 0.437 0.577 0.369 0.074  -0.011 -0.058 353 GLY AAA C   
2507  O O   . GLY A 353 ? 0.466 0.616 0.397 0.080  -0.013 -0.062 353 GLY AAA O   
2508  N N   . ILE A 354 ? 0.423 0.561 0.359 0.071  -0.011 -0.058 354 ILE AAA N   
2509  C CA  . ILE A 354 ? 0.414 0.560 0.353 0.075  -0.013 -0.064 354 ILE AAA CA  
2510  C C   . ILE A 354 ? 0.387 0.545 0.337 0.072  -0.015 -0.071 354 ILE AAA C   
2511  O O   . ILE A 354 ? 0.355 0.523 0.304 0.078  -0.017 -0.077 354 ILE AAA O   
2512  C CB  . ILE A 354 ? 0.434 0.574 0.375 0.072  -0.012 -0.061 354 ILE AAA CB  
2513  C CG1 . ILE A 354 ? 0.440 0.570 0.370 0.075  -0.009 -0.055 354 ILE AAA CG1 
2514  C CG2 . ILE A 354 ? 0.437 0.587 0.383 0.074  -0.014 -0.068 354 ILE AAA CG2 
2515  C CD1 . ILE A 354 ? 0.439 0.563 0.371 0.071  -0.008 -0.052 354 ILE AAA CD1 
2516  N N   . LEU A 355 ? 0.382 0.539 0.342 0.065  -0.015 -0.071 355 LEU AAA N   
2517  C CA  . LEU A 355 ? 0.390 0.556 0.362 0.062  -0.016 -0.078 355 LEU AAA CA  
2518  C C   . LEU A 355 ? 0.412 0.587 0.383 0.066  -0.018 -0.081 355 LEU AAA C   
2519  O O   . LEU A 355 ? 0.433 0.619 0.409 0.068  -0.020 -0.089 355 LEU AAA O   
2520  C CB  . LEU A 355 ? 0.387 0.549 0.369 0.053  -0.015 -0.076 355 LEU AAA CB  
2521  C CG  . LEU A 355 ? 0.405 0.561 0.392 0.048  -0.013 -0.073 355 LEU AAA CG  
2522  C CD1 . LEU A 355 ? 0.390 0.545 0.389 0.041  -0.012 -0.072 355 LEU AAA CD1 
2523  C CD2 . LEU A 355 ? 0.392 0.554 0.383 0.051  -0.015 -0.079 355 LEU AAA CD2 
2524  N N   . LEU A 356 ? 0.406 0.575 0.368 0.067  -0.017 -0.076 356 LEU AAA N   
2525  C CA  . LEU A 356 ? 0.427 0.603 0.385 0.072  -0.018 -0.079 356 LEU AAA CA  
2526  C C   . LEU A 356 ? 0.430 0.615 0.383 0.081  -0.020 -0.084 356 LEU AAA C   
2527  O O   . LEU A 356 ? 0.442 0.639 0.400 0.083  -0.022 -0.091 356 LEU AAA O   
2528  C CB  . LEU A 356 ? 0.431 0.598 0.382 0.072  -0.017 -0.072 356 LEU AAA CB  
2529  C CG  . LEU A 356 ? 0.454 0.627 0.399 0.077  -0.018 -0.074 356 LEU AAA CG  
2530  C CD1 . LEU A 356 ? 0.444 0.627 0.398 0.074  -0.019 -0.080 356 LEU AAA CD1 
2531  C CD2 . LEU A 356 ? 0.478 0.641 0.415 0.077  -0.016 -0.067 356 LEU AAA CD2 
2532  N N   . ALA A 357 ? 0.445 0.623 0.387 0.086  -0.019 -0.079 357 ALA AAA N   
2533  C CA  . ALA A 357 ? 0.471 0.656 0.406 0.095  -0.021 -0.082 357 ALA AAA CA  
2534  C C   . ALA A 357 ? 0.468 0.666 0.412 0.095  -0.023 -0.091 357 ALA AAA C   
2535  O O   . ALA A 357 ? 0.486 0.696 0.429 0.101  -0.026 -0.098 357 ALA AAA O   
2536  C CB  . ALA A 357 ? 0.476 0.652 0.401 0.098  -0.018 -0.076 357 ALA AAA CB  
2537  N N   . ARG A 358 ? 0.467 0.664 0.421 0.088  -0.023 -0.093 358 ARG AAA N   
2538  C CA  . ARG A 358 ? 0.484 0.693 0.449 0.088  -0.025 -0.102 358 ARG AAA CA  
2539  C C   . ARG A 358 ? 0.502 0.721 0.477 0.085  -0.026 -0.110 358 ARG AAA C   
2540  O O   . ARG A 358 ? 0.534 0.767 0.513 0.089  -0.029 -0.118 358 ARG AAA O   
2541  C CB  . ARG A 358 ? 0.478 0.681 0.452 0.080  -0.024 -0.101 358 ARG AAA CB  
2542  C CG  . ARG A 358 ? 0.497 0.694 0.463 0.083  -0.023 -0.097 358 ARG AAA CG  
2543  C CD  . ARG A 358 ? 0.486 0.676 0.460 0.076  -0.021 -0.096 358 ARG AAA CD  
2544  N NE  . ARG A 358 ? 0.517 0.699 0.481 0.079  -0.020 -0.090 358 ARG AAA NE  
2545  C CZ  . ARG A 358 ? 0.512 0.685 0.479 0.074  -0.018 -0.086 358 ARG AAA CZ  
2546  N NH1 . ARG A 358 ? 0.492 0.663 0.471 0.066  -0.018 -0.087 358 ARG AAA NH1 
2547  N NH2 . ARG A 358 ? 0.500 0.666 0.458 0.077  -0.017 -0.081 358 ARG AAA NH2 
2548  N N   . ARG A 359 ? 0.494 0.709 0.474 0.079  -0.025 -0.107 359 ARG AAA N   
2549  C CA  . ARG A 359 ? 0.467 0.691 0.458 0.076  -0.026 -0.113 359 ARG AAA CA  
2550  C C   . ARG A 359 ? 0.482 0.716 0.465 0.084  -0.028 -0.117 359 ARG AAA C   
2551  O O   . ARG A 359 ? 0.471 0.719 0.463 0.085  -0.030 -0.127 359 ARG AAA O   
2552  C CB  . ARG A 359 ? 0.451 0.667 0.446 0.068  -0.024 -0.108 359 ARG AAA CB  
2553  C CG  . ARG A 359 ? 0.433 0.641 0.438 0.060  -0.021 -0.105 359 ARG AAA CG  
2554  C CD  . ARG A 359 ? 0.419 0.624 0.431 0.053  -0.019 -0.103 359 ARG AAA CD  
2555  N NE  . ARG A 359 ? 0.406 0.604 0.408 0.054  -0.019 -0.096 359 ARG AAA NE  
2556  C CZ  . ARG A 359 ? 0.376 0.562 0.370 0.053  -0.017 -0.087 359 ARG AAA CZ  
2557  N NH1 . ARG A 359 ? 0.369 0.548 0.363 0.051  -0.016 -0.084 359 ARG AAA NH1 
2558  N NH2 . ARG A 359 ? 0.390 0.572 0.376 0.054  -0.017 -0.082 359 ARG AAA NH2 
2559  N N   . LEU A 360 ? 0.474 0.701 0.443 0.090  -0.028 -0.111 360 LEU AAA N   
2560  C CA  . LEU A 360 ? 0.500 0.736 0.461 0.099  -0.030 -0.113 360 LEU AAA CA  
2561  C C   . LEU A 360 ? 0.514 0.763 0.472 0.107  -0.032 -0.120 360 LEU AAA C   
2562  O O   . LEU A 360 ? 0.535 0.798 0.495 0.112  -0.035 -0.127 360 LEU AAA O   
2563  C CB  . LEU A 360 ? 0.488 0.712 0.434 0.102  -0.028 -0.104 360 LEU AAA CB  
2564  C CG  . LEU A 360 ? 0.479 0.693 0.427 0.096  -0.026 -0.098 360 LEU AAA CG  
2565  C CD1 . LEU A 360 ? 0.460 0.663 0.394 0.100  -0.024 -0.089 360 LEU AAA CD1 
2566  C CD2 . LEU A 360 ? 0.474 0.697 0.430 0.093  -0.027 -0.103 360 LEU AAA CD2 
2567  N N   . PHE A 361 ? 0.489 0.735 0.445 0.109  -0.032 -0.118 361 PHE AAA N   
2568  C CA  . PHE A 361 ? 0.490 0.745 0.438 0.119  -0.034 -0.122 361 PHE AAA CA  
2569  C C   . PHE A 361 ? 0.500 0.762 0.456 0.117  -0.035 -0.128 361 PHE AAA C   
2570  O O   . PHE A 361 ? 0.497 0.770 0.448 0.126  -0.037 -0.133 361 PHE AAA O   
2571  C CB  . PHE A 361 ? 0.497 0.741 0.428 0.125  -0.032 -0.112 361 PHE AAA CB  
2572  C CG  . PHE A 361 ? 0.505 0.743 0.428 0.128  -0.030 -0.106 361 PHE AAA CG  
2573  C CD1 . PHE A 361 ? 0.498 0.748 0.419 0.134  -0.032 -0.111 361 PHE AAA CD1 
2574  C CD2 . PHE A 361 ? 0.493 0.715 0.410 0.124  -0.027 -0.096 361 PHE AAA CD2 
2575  C CE1 . PHE A 361 ? 0.493 0.737 0.406 0.136  -0.031 -0.106 361 PHE AAA CE1 
2576  C CE2 . PHE A 361 ? 0.498 0.714 0.407 0.127  -0.026 -0.091 361 PHE AAA CE2 
2577  C CZ  . PHE A 361 ? 0.514 0.741 0.421 0.133  -0.028 -0.096 361 PHE AAA CZ  
2578  N N   . ALA A 362 ? 0.497 0.754 0.465 0.108  -0.033 -0.129 362 ALA AAA N   
2579  C CA  . ALA A 362 ? 0.490 0.753 0.467 0.105  -0.034 -0.135 362 ALA AAA CA  
2580  C C   . ALA A 362 ? 0.480 0.747 0.475 0.096  -0.034 -0.142 362 ALA AAA C   
2581  O O   . ALA A 362 ? 0.428 0.695 0.433 0.092  -0.033 -0.145 362 ALA AAA O   
2582  C CB  . ALA A 362 ? 0.523 0.772 0.495 0.103  -0.032 -0.127 362 ALA AAA CB  
2583  N N   . GLY A 363 ? 0.532 0.803 0.533 0.094  -0.034 -0.146 363 GLY AAA N   
2584  C CA  . GLY A 363 ? 0.542 0.821 0.562 0.087  -0.034 -0.153 363 GLY AAA CA  
2585  C C   . GLY A 363 ? 0.598 0.864 0.627 0.077  -0.031 -0.149 363 GLY AAA C   
2586  O O   . GLY A 363 ? 0.602 0.873 0.646 0.071  -0.030 -0.156 363 GLY AAA O   
2587  N N   . SER A 364 ? 0.636 0.886 0.656 0.075  -0.029 -0.137 364 SER AAA N   
2588  C CA  . SER A 364 ? 0.610 0.848 0.637 0.066  -0.026 -0.131 364 SER AAA CA  
2589  C C   . SER A 364 ? 0.600 0.835 0.634 0.060  -0.024 -0.129 364 SER AAA C   
2590  O O   . SER A 364 ? 0.556 0.795 0.584 0.063  -0.025 -0.130 364 SER AAA O   
2591  C CB  . SER A 364 ? 0.626 0.849 0.640 0.066  -0.025 -0.121 364 SER AAA CB  
2592  O OG  . SER A 364 ? 0.571 0.782 0.590 0.058  -0.022 -0.114 364 SER AAA OG  
2593  N N   . ASN A 365 ? 0.613 0.843 0.659 0.051  -0.021 -0.128 365 ASN AAA N   
2594  C CA  . ASN A 365 ? 0.646 0.871 0.696 0.046  -0.019 -0.124 365 ASN AAA CA  
2595  C C   . ASN A 365 ? 0.613 0.824 0.664 0.040  -0.016 -0.114 365 ASN AAA C   
2596  O O   . ASN A 365 ? 0.590 0.798 0.649 0.033  -0.014 -0.112 365 ASN AAA O   
2597  C CB  . ASN A 365 ? 0.688 0.924 0.755 0.042  -0.018 -0.133 365 ASN AAA CB  
2598  C CG  . ASN A 365 ? 0.747 0.983 0.813 0.041  -0.018 -0.131 365 ASN AAA CG  
2599  O OD1 . ASN A 365 ? 0.736 0.965 0.807 0.034  -0.015 -0.126 365 ASN AAA OD1 
2600  N ND2 . ASN A 365 ? 0.767 1.011 0.825 0.047  -0.021 -0.134 365 ASN AAA ND2 
2601  N N   . GLU A 366 ? 0.621 0.824 0.662 0.042  -0.016 -0.109 366 GLU AAA N   
2602  C CA  . GLU A 366 ? 0.603 0.793 0.643 0.037  -0.014 -0.100 366 GLU AAA CA  
2603  C C   . GLU A 366 ? 0.523 0.705 0.552 0.037  -0.013 -0.091 366 GLU AAA C   
2604  O O   . GLU A 366 ? 0.463 0.644 0.479 0.043  -0.015 -0.090 366 GLU AAA O   
2605  C CB  . GLU A 366 ? 0.637 0.824 0.673 0.039  -0.015 -0.099 366 GLU AAA CB  
2606  C CG  . GLU A 366 ? 0.677 0.870 0.726 0.037  -0.014 -0.107 366 GLU AAA CG  
2607  C CD  . GLU A 366 ? 0.732 0.918 0.780 0.035  -0.014 -0.104 366 GLU AAA CD  
2608  O OE1 . GLU A 366 ? 0.742 0.933 0.787 0.040  -0.015 -0.108 366 GLU AAA OE1 
2609  O OE2 . GLU A 366 ? 0.743 0.920 0.795 0.030  -0.011 -0.097 366 GLU AAA OE2 
2610  N N   . PHE A 367 ? 0.501 0.677 0.535 0.031  -0.011 -0.086 367 PHE AAA N   
2611  C CA  . PHE A 367 ? 0.477 0.644 0.503 0.029  -0.010 -0.077 367 PHE AAA CA  
2612  C C   . PHE A 367 ? 0.436 0.594 0.462 0.026  -0.008 -0.071 367 PHE AAA C   
2613  O O   . PHE A 367 ? 0.412 0.570 0.448 0.023  -0.007 -0.073 367 PHE AAA O   
2614  C CB  . PHE A 367 ? 0.473 0.643 0.504 0.026  -0.008 -0.077 367 PHE AAA CB  
2615  C CG  . PHE A 367 ? 0.487 0.665 0.516 0.030  -0.010 -0.082 367 PHE AAA CG  
2616  C CD1 . PHE A 367 ? 0.463 0.652 0.502 0.031  -0.011 -0.091 367 PHE AAA CD1 
2617  C CD2 . PHE A 367 ? 0.506 0.683 0.524 0.034  -0.011 -0.079 367 PHE AAA CD2 
2618  C CE1 . PHE A 367 ? 0.449 0.647 0.486 0.035  -0.013 -0.097 367 PHE AAA CE1 
2619  C CE2 . PHE A 367 ? 0.508 0.693 0.524 0.038  -0.013 -0.084 367 PHE AAA CE2 
2620  C CZ  . PHE A 367 ? 0.448 0.644 0.474 0.038  -0.014 -0.093 367 PHE AAA CZ  
2621  N N   . ILE A 368 ? 0.470 0.620 0.487 0.026  -0.007 -0.064 368 ILE AAA N   
2622  C CA  . ILE A 368 ? 0.438 0.579 0.454 0.022  -0.005 -0.057 368 ILE AAA CA  
2623  C C   . ILE A 368 ? 0.416 0.557 0.444 0.016  -0.003 -0.055 368 ILE AAA C   
2624  O O   . ILE A 368 ? 0.347 0.493 0.378 0.015  -0.002 -0.056 368 ILE AAA O   
2625  C CB  . ILE A 368 ? 0.432 0.565 0.436 0.023  -0.005 -0.050 368 ILE AAA CB  
2626  C CG1 . ILE A 368 ? 0.429 0.561 0.423 0.029  -0.006 -0.051 368 ILE AAA CG1 
2627  C CG2 . ILE A 368 ? 0.442 0.569 0.448 0.019  -0.003 -0.044 368 ILE AAA CG2 
2628  C CD1 . ILE A 368 ? 0.416 0.541 0.398 0.031  -0.006 -0.046 368 ILE AAA CD1 
2629  N N   . ASP A 369 ? 0.424 0.561 0.458 0.013  -0.001 -0.052 369 ASP AAA N   
2630  C CA  . ASP A 369 ? 0.432 0.567 0.475 0.008  0.002  -0.048 369 ASP AAA CA  
2631  C C   . ASP A 369 ? 0.421 0.550 0.455 0.007  0.003  -0.040 369 ASP AAA C   
2632  O O   . ASP A 369 ? 0.422 0.545 0.452 0.007  0.003  -0.037 369 ASP AAA O   
2633  C CB  . ASP A 369 ? 0.451 0.585 0.505 0.005  0.003  -0.049 369 ASP AAA CB  
2634  C CG  . ASP A 369 ? 0.476 0.609 0.540 0.000  0.007  -0.045 369 ASP AAA CG  
2635  O OD1 . ASP A 369 ? 0.551 0.683 0.613 -0.001 0.008  -0.040 369 ASP AAA OD1 
2636  O OD2 . ASP A 369 ? 0.448 0.581 0.523 -0.002 0.009  -0.047 369 ASP AAA OD2 
2637  N N   . TYR A 370 ? 0.420 0.551 0.452 0.006  0.003  -0.037 370 TYR AAA N   
2638  C CA  . TYR A 370 ? 0.425 0.551 0.448 0.006  0.003  -0.031 370 TYR AAA CA  
2639  C C   . TYR A 370 ? 0.437 0.560 0.465 0.003  0.006  -0.025 370 TYR AAA C   
2640  O O   . TYR A 370 ? 0.433 0.554 0.456 0.002  0.006  -0.020 370 TYR AAA O   
2641  C CB  . TYR A 370 ? 0.399 0.529 0.418 0.007  0.003  -0.031 370 TYR AAA CB  
2642  C CG  . TYR A 370 ? 0.417 0.548 0.427 0.012  0.000  -0.035 370 TYR AAA CG  
2643  C CD1 . TYR A 370 ? 0.400 0.526 0.400 0.014  -0.000 -0.033 370 TYR AAA CD1 
2644  C CD2 . TYR A 370 ? 0.398 0.535 0.411 0.014  -0.001 -0.041 370 TYR AAA CD2 
2645  C CE1 . TYR A 370 ? 0.416 0.542 0.408 0.019  -0.002 -0.036 370 TYR AAA CE1 
2646  C CE2 . TYR A 370 ? 0.404 0.542 0.408 0.019  -0.003 -0.044 370 TYR AAA CE2 
2647  C CZ  . TYR A 370 ? 0.425 0.557 0.418 0.022  -0.004 -0.042 370 TYR AAA CZ  
2648  O OH  . TYR A 370 ? 0.448 0.581 0.433 0.027  -0.005 -0.044 370 TYR AAA OH  
2649  N N   . ASP A 371 ? 0.469 0.593 0.509 -0.000 0.008  -0.026 371 ASP AAA N   
2650  C CA  . ASP A 371 ? 0.478 0.600 0.524 -0.003 0.011  -0.020 371 ASP AAA CA  
2651  C C   . ASP A 371 ? 0.431 0.547 0.472 -0.003 0.010  -0.018 371 ASP AAA C   
2652  O O   . ASP A 371 ? 0.433 0.546 0.475 -0.004 0.012  -0.012 371 ASP AAA O   
2653  C CB  . ASP A 371 ? 0.507 0.631 0.566 -0.006 0.013  -0.021 371 ASP AAA CB  
2654  C CG  . ASP A 371 ? 0.543 0.673 0.609 -0.007 0.015  -0.023 371 ASP AAA CG  
2655  O OD1 . ASP A 371 ? 0.559 0.690 0.619 -0.007 0.015  -0.020 371 ASP AAA OD1 
2656  O OD2 . ASP A 371 ? 0.574 0.706 0.651 -0.008 0.016  -0.027 371 ASP AAA OD2 
2657  N N   . PHE A 372 ? 0.409 0.523 0.446 -0.000 0.008  -0.022 372 PHE AAA N   
2658  C CA  . PHE A 372 ? 0.400 0.510 0.434 0.000  0.007  -0.021 372 PHE AAA CA  
2659  C C   . PHE A 372 ? 0.400 0.506 0.421 0.004  0.005  -0.022 372 PHE AAA C   
2660  O O   . PHE A 372 ? 0.407 0.513 0.426 0.006  0.004  -0.026 372 PHE AAA O   
2661  C CB  . PHE A 372 ? 0.415 0.525 0.458 -0.001 0.008  -0.025 372 PHE AAA CB  
2662  C CG  . PHE A 372 ? 0.420 0.531 0.476 -0.004 0.011  -0.024 372 PHE AAA CG  
2663  C CD1 . PHE A 372 ? 0.420 0.528 0.479 -0.006 0.013  -0.017 372 PHE AAA CD1 
2664  C CD2 . PHE A 372 ? 0.419 0.535 0.484 -0.005 0.012  -0.028 372 PHE AAA CD2 
2665  C CE1 . PHE A 372 ? 0.422 0.530 0.492 -0.009 0.016  -0.015 372 PHE AAA CE1 
2666  C CE2 . PHE A 372 ? 0.424 0.540 0.502 -0.008 0.015  -0.026 372 PHE AAA CE2 
2667  C CZ  . PHE A 372 ? 0.432 0.544 0.512 -0.010 0.018  -0.019 372 PHE AAA CZ  
2668  N N   . VAL A 373 ? 0.410 0.515 0.424 0.004  0.005  -0.019 373 VAL AAA N   
2669  C CA  . VAL A 373 ? 0.413 0.515 0.415 0.007  0.004  -0.019 373 VAL AAA CA  
2670  C C   . VAL A 373 ? 0.389 0.486 0.388 0.006  0.005  -0.014 373 VAL AAA C   
2671  O O   . VAL A 373 ? 0.433 0.531 0.431 0.004  0.006  -0.010 373 VAL AAA O   
2672  C CB  . VAL A 373 ? 0.413 0.517 0.410 0.009  0.003  -0.019 373 VAL AAA CB  
2673  C CG1 . VAL A 373 ? 0.425 0.526 0.412 0.011  0.003  -0.019 373 VAL AAA CG1 
2674  C CG2 . VAL A 373 ? 0.417 0.527 0.417 0.010  0.002  -0.024 373 VAL AAA CG2 
2675  N N   . PRO A 374 ? 0.372 0.464 0.369 0.006  0.005  -0.014 374 PRO AAA N   
2676  C CA  . PRO A 374 ? 0.356 0.445 0.351 0.005  0.006  -0.010 374 PRO AAA CA  
2677  C C   . PRO A 374 ? 0.372 0.458 0.357 0.007  0.005  -0.010 374 PRO AAA C   
2678  O O   . PRO A 374 ? 0.395 0.481 0.375 0.009  0.005  -0.013 374 PRO AAA O   
2679  C CB  . PRO A 374 ? 0.343 0.429 0.340 0.005  0.005  -0.012 374 PRO AAA CB  
2680  C CG  . PRO A 374 ? 0.351 0.438 0.346 0.008  0.004  -0.017 374 PRO AAA CG  
2681  C CD  . PRO A 374 ? 0.357 0.449 0.355 0.008  0.004  -0.018 374 PRO AAA CD  
2682  N N   . THR A 375 ? 0.382 0.467 0.365 0.005  0.006  -0.007 375 THR AAA N   
2683  C CA  . THR A 375 ? 0.387 0.470 0.363 0.006  0.007  -0.007 375 THR AAA CA  
2684  C C   . THR A 375 ? 0.346 0.425 0.321 0.005  0.008  -0.004 375 THR AAA C   
2685  O O   . THR A 375 ? 0.337 0.419 0.318 0.003  0.008  -0.002 375 THR AAA O   
2686  C CB  . THR A 375 ? 0.467 0.554 0.441 0.006  0.007  -0.006 375 THR AAA CB  
2687  O OG1 . THR A 375 ? 0.545 0.629 0.513 0.007  0.008  -0.006 375 THR AAA OG1 
2688  C CG2 . THR A 375 ? 0.497 0.589 0.478 0.003  0.007  -0.003 375 THR AAA CG2 
2689  N N   . THR A 376 ? 0.315 0.390 0.284 0.006  0.009  -0.005 376 THR AAA N   
2690  C CA  . THR A 376 ? 0.303 0.376 0.272 0.004  0.010  -0.004 376 THR AAA CA  
2691  C C   . THR A 376 ? 0.286 0.359 0.249 0.004  0.011  -0.005 376 THR AAA C   
2692  O O   . THR A 376 ? 0.291 0.361 0.250 0.006  0.012  -0.007 376 THR AAA O   
2693  C CB  . THR A 376 ? 0.312 0.379 0.278 0.005  0.010  -0.005 376 THR AAA CB  
2694  O OG1 . THR A 376 ? 0.354 0.422 0.327 0.004  0.010  -0.004 376 THR AAA OG1 
2695  C CG2 . THR A 376 ? 0.307 0.372 0.272 0.003  0.012  -0.004 376 THR AAA CG2 
2696  N N   . VAL A 377 ? 0.256 0.332 0.221 0.002  0.012  -0.003 377 VAL AAA N   
2697  C CA  . VAL A 377 ? 0.245 0.322 0.207 0.002  0.013  -0.005 377 VAL AAA CA  
2698  C C   . VAL A 377 ? 0.252 0.324 0.212 0.001  0.014  -0.006 377 VAL AAA C   
2699  O O   . VAL A 377 ? 0.250 0.324 0.214 -0.000 0.014  -0.004 377 VAL AAA O   
2700  C CB  . VAL A 377 ? 0.238 0.323 0.203 0.000  0.012  -0.003 377 VAL AAA CB  
2701  C CG1 . VAL A 377 ? 0.239 0.327 0.202 -0.000 0.014  -0.005 377 VAL AAA CG1 
2702  C CG2 . VAL A 377 ? 0.231 0.320 0.197 0.001  0.011  -0.002 377 VAL AAA CG2 
2703  N N   . PHE A 378 ? 0.252 0.319 0.209 0.002  0.016  -0.008 378 PHE AAA N   
2704  C CA  . PHE A 378 ? 0.267 0.328 0.223 0.002  0.018  -0.009 378 PHE AAA CA  
2705  C C   . PHE A 378 ? 0.266 0.331 0.223 -0.000 0.020  -0.011 378 PHE AAA C   
2706  O O   . PHE A 378 ? 0.275 0.335 0.230 -0.000 0.023  -0.013 378 PHE AAA O   
2707  C CB  . PHE A 378 ? 0.277 0.330 0.228 0.004  0.020  -0.010 378 PHE AAA CB  
2708  C CG  . PHE A 378 ? 0.270 0.321 0.220 0.006  0.019  -0.009 378 PHE AAA CG  
2709  C CD1 . PHE A 378 ? 0.269 0.318 0.221 0.006  0.018  -0.008 378 PHE AAA CD1 
2710  C CD2 . PHE A 378 ? 0.275 0.328 0.224 0.008  0.017  -0.009 378 PHE AAA CD2 
2711  C CE1 . PHE A 378 ? 0.280 0.328 0.232 0.008  0.017  -0.008 378 PHE AAA CE1 
2712  C CE2 . PHE A 378 ? 0.279 0.332 0.228 0.010  0.016  -0.009 378 PHE AAA CE2 
2713  C CZ  . PHE A 378 ? 0.279 0.329 0.230 0.010  0.015  -0.008 378 PHE AAA CZ  
2714  N N   . THR A 379 ? 0.268 0.341 0.229 -0.002 0.018  -0.010 379 THR AAA N   
2715  C CA  . THR A 379 ? 0.274 0.353 0.237 -0.004 0.019  -0.011 379 THR AAA CA  
2716  C C   . THR A 379 ? 0.282 0.358 0.246 -0.005 0.020  -0.012 379 THR AAA C   
2717  O O   . THR A 379 ? 0.276 0.347 0.240 -0.005 0.020  -0.010 379 THR AAA O   
2718  C CB  . THR A 379 ? 0.282 0.370 0.247 -0.004 0.017  -0.009 379 THR AAA CB  
2719  O OG1 . THR A 379 ? 0.272 0.361 0.239 -0.004 0.015  -0.005 379 THR AAA OG1 
2720  C CG2 . THR A 379 ? 0.280 0.372 0.244 -0.004 0.017  -0.011 379 THR AAA CG2 
2721  N N   . PRO A 380 ? 0.283 0.362 0.249 -0.007 0.021  -0.015 380 PRO AAA N   
2722  C CA  . PRO A 380 ? 0.280 0.357 0.248 -0.008 0.023  -0.016 380 PRO AAA CA  
2723  C C   . PRO A 380 ? 0.275 0.353 0.245 -0.008 0.020  -0.012 380 PRO AAA C   
2724  O O   . PRO A 380 ? 0.321 0.393 0.291 -0.008 0.021  -0.012 380 PRO AAA O   
2725  C CB  . PRO A 380 ? 0.276 0.361 0.247 -0.009 0.023  -0.019 380 PRO AAA CB  
2726  C CG  . PRO A 380 ? 0.279 0.366 0.248 -0.009 0.024  -0.022 380 PRO AAA CG  
2727  C CD  . PRO A 380 ? 0.276 0.362 0.242 -0.007 0.022  -0.018 380 PRO AAA CD  
2728  N N   . ILE A 381 ? 0.272 0.357 0.244 -0.007 0.018  -0.009 381 ILE AAA N   
2729  C CA  . ILE A 381 ? 0.262 0.345 0.235 -0.007 0.016  -0.005 381 ILE AAA CA  
2730  C C   . ILE A 381 ? 0.268 0.351 0.240 -0.005 0.015  -0.003 381 ILE AAA C   
2731  O O   . ILE A 381 ? 0.247 0.334 0.218 -0.005 0.015  -0.003 381 ILE AAA O   
2732  C CB  . ILE A 381 ? 0.263 0.355 0.241 -0.007 0.015  -0.002 381 ILE AAA CB  
2733  C CG1 . ILE A 381 ? 0.259 0.361 0.237 -0.006 0.014  -0.001 381 ILE AAA CG1 
2734  C CG2 . ILE A 381 ? 0.261 0.354 0.240 -0.008 0.016  -0.003 381 ILE AAA CG2 
2735  C CD1 . ILE A 381 ? 0.257 0.367 0.238 -0.006 0.013  0.002  381 ILE AAA CD1 
2736  N N   . GLU A 382 ? 0.272 0.349 0.244 -0.005 0.015  -0.002 382 GLU AAA N   
2737  C CA  . GLU A 382 ? 0.268 0.343 0.239 -0.003 0.014  -0.002 382 GLU AAA CA  
2738  C C   . GLU A 382 ? 0.258 0.338 0.233 -0.003 0.013  0.002  382 GLU AAA C   
2739  O O   . GLU A 382 ? 0.254 0.338 0.233 -0.004 0.012  0.004  382 GLU AAA O   
2740  C CB  . GLU A 382 ? 0.286 0.353 0.255 -0.002 0.015  -0.003 382 GLU AAA CB  
2741  C CG  . GLU A 382 ? 0.313 0.373 0.278 -0.002 0.017  -0.005 382 GLU AAA CG  
2742  C CD  . GLU A 382 ? 0.339 0.393 0.302 -0.000 0.017  -0.006 382 GLU AAA CD  
2743  O OE1 . GLU A 382 ? 0.326 0.380 0.291 0.001  0.016  -0.005 382 GLU AAA OE1 
2744  O OE2 . GLU A 382 ? 0.392 0.440 0.351 0.001  0.020  -0.008 382 GLU AAA OE2 
2745  N N   . TYR A 383 ? 0.241 0.322 0.215 -0.003 0.012  0.002  383 TYR AAA N   
2746  C CA  . TYR A 383 ? 0.234 0.320 0.213 -0.003 0.011  0.005  383 TYR AAA CA  
2747  C C   . TYR A 383 ? 0.222 0.305 0.202 -0.002 0.011  0.004  383 TYR AAA C   
2748  O O   . TYR A 383 ? 0.211 0.294 0.187 -0.001 0.010  0.002  383 TYR AAA O   
2749  C CB  . TYR A 383 ? 0.239 0.333 0.218 -0.003 0.011  0.006  383 TYR AAA CB  
2750  C CG  . TYR A 383 ? 0.249 0.348 0.232 -0.003 0.011  0.010  383 TYR AAA CG  
2751  C CD1 . TYR A 383 ? 0.258 0.356 0.247 -0.003 0.011  0.013  383 TYR AAA CD1 
2752  C CD2 . TYR A 383 ? 0.259 0.362 0.241 -0.002 0.011  0.010  383 TYR AAA CD2 
2753  C CE1 . TYR A 383 ? 0.268 0.369 0.261 -0.003 0.011  0.015  383 TYR AAA CE1 
2754  C CE2 . TYR A 383 ? 0.267 0.374 0.253 -0.002 0.011  0.012  383 TYR AAA CE2 
2755  C CZ  . TYR A 383 ? 0.261 0.367 0.254 -0.003 0.011  0.015  383 TYR AAA CZ  
2756  O OH  . TYR A 383 ? 0.240 0.349 0.237 -0.003 0.012  0.018  383 TYR AAA OH  
2757  N N   . GLY A 384 ? 0.215 0.296 0.199 -0.002 0.010  0.005  384 GLY AAA N   
2758  C CA  . GLY A 384 ? 0.216 0.296 0.203 -0.001 0.010  0.004  384 GLY AAA CA  
2759  C C   . GLY A 384 ? 0.215 0.299 0.208 -0.002 0.010  0.006  384 GLY AAA C   
2760  O O   . GLY A 384 ? 0.217 0.304 0.215 -0.003 0.011  0.010  384 GLY AAA O   
2761  N N   . HIS A 385 ? 0.219 0.305 0.214 -0.002 0.009  0.005  385 HIS AAA N   
2762  C CA  . HIS A 385 ? 0.226 0.316 0.229 -0.003 0.010  0.007  385 HIS AAA CA  
2763  C C   . HIS A 385 ? 0.238 0.329 0.243 -0.002 0.009  0.004  385 HIS AAA C   
2764  O O   . HIS A 385 ? 0.253 0.342 0.252 -0.000 0.008  0.000  385 HIS AAA O   
2765  C CB  . HIS A 385 ? 0.225 0.321 0.228 -0.003 0.011  0.011  385 HIS AAA CB  
2766  C CG  . HIS A 385 ? 0.229 0.329 0.229 -0.002 0.010  0.009  385 HIS AAA CG  
2767  N ND1 . HIS A 385 ? 0.237 0.336 0.229 -0.001 0.009  0.007  385 HIS AAA ND1 
2768  C CD2 . HIS A 385 ? 0.229 0.332 0.234 -0.003 0.011  0.009  385 HIS AAA CD2 
2769  C CE1 . HIS A 385 ? 0.232 0.335 0.225 -0.001 0.009  0.006  385 HIS AAA CE1 
2770  N NE2 . HIS A 385 ? 0.235 0.340 0.235 -0.002 0.010  0.008  385 HIS AAA NE2 
2771  N N   . VAL A 386 ? 0.242 0.334 0.255 -0.003 0.010  0.004  386 VAL AAA N   
2772  C CA  . VAL A 386 ? 0.244 0.339 0.262 -0.003 0.010  0.001  386 VAL AAA CA  
2773  C C   . VAL A 386 ? 0.257 0.356 0.284 -0.005 0.012  0.005  386 VAL AAA C   
2774  O O   . VAL A 386 ? 0.245 0.344 0.276 -0.006 0.014  0.009  386 VAL AAA O   
2775  C CB  . VAL A 386 ? 0.246 0.339 0.268 -0.003 0.010  -0.004 386 VAL AAA CB  
2776  C CG1 . VAL A 386 ? 0.244 0.335 0.274 -0.004 0.011  -0.002 386 VAL AAA CG1 
2777  C CG2 . VAL A 386 ? 0.240 0.337 0.265 -0.002 0.009  -0.008 386 VAL AAA CG2 
2778  N N   . GLY A 387 ? 0.266 0.369 0.295 -0.005 0.013  0.003  387 GLY AAA N   
2779  C CA  . GLY A 387 ? 0.269 0.376 0.306 -0.006 0.015  0.006  387 GLY AAA CA  
2780  C C   . GLY A 387 ? 0.286 0.396 0.319 -0.006 0.016  0.011  387 GLY AAA C   
2781  O O   . GLY A 387 ? 0.313 0.423 0.337 -0.005 0.014  0.011  387 GLY AAA O   
2782  N N   . LEU A 388 ? 0.305 0.417 0.344 -0.007 0.019  0.017  388 LEU AAA N   
2783  C CA  . LEU A 388 ? 0.307 0.424 0.344 -0.007 0.020  0.022  388 LEU AAA CA  
2784  C C   . LEU A 388 ? 0.301 0.418 0.334 -0.006 0.020  0.026  388 LEU AAA C   
2785  O O   . LEU A 388 ? 0.305 0.419 0.341 -0.006 0.021  0.028  388 LEU AAA O   
2786  C CB  . LEU A 388 ? 0.325 0.444 0.372 -0.008 0.024  0.025  388 LEU AAA CB  
2787  C CG  . LEU A 388 ? 0.340 0.459 0.393 -0.009 0.024  0.020  388 LEU AAA CG  
2788  C CD1 . LEU A 388 ? 0.343 0.464 0.408 -0.011 0.028  0.024  388 LEU AAA CD1 
2789  C CD2 . LEU A 388 ? 0.327 0.450 0.374 -0.008 0.022  0.016  388 LEU AAA CD2 
2790  N N   . SER A 389 ? 0.311 0.432 0.336 -0.005 0.019  0.028  389 SER AAA N   
2791  C CA  . SER A 389 ? 0.315 0.440 0.338 -0.004 0.020  0.033  389 SER AAA CA  
2792  C C   . SER A 389 ? 0.325 0.453 0.355 -0.004 0.023  0.039  389 SER AAA C   
2793  O O   . SER A 389 ? 0.338 0.465 0.375 -0.005 0.025  0.040  389 SER AAA O   
2794  C CB  . SER A 389 ? 0.315 0.446 0.331 -0.003 0.018  0.032  389 SER AAA CB  
2795  O OG  . SER A 389 ? 0.305 0.440 0.323 -0.003 0.019  0.033  389 SER AAA OG  
2796  N N   . SER A 390 ? 0.324 0.454 0.353 -0.002 0.024  0.044  390 SER AAA N   
2797  C CA  . SER A 390 ? 0.338 0.473 0.372 -0.001 0.027  0.052  390 SER AAA CA  
2798  C C   . SER A 390 ? 0.339 0.480 0.373 -0.001 0.029  0.054  390 SER AAA C   
2799  O O   . SER A 390 ? 0.349 0.490 0.391 -0.001 0.032  0.057  390 SER AAA O   
2800  C CB  . SER A 390 ? 0.329 0.468 0.359 0.001  0.027  0.056  390 SER AAA CB  
2801  O OG  . SER A 390 ? 0.312 0.445 0.342 0.000  0.026  0.054  390 SER AAA OG  
2802  N N   . GLU A 391 ? 0.325 0.470 0.352 -0.000 0.026  0.050  391 GLU AAA N   
2803  C CA  . GLU A 391 ? 0.328 0.480 0.354 0.000  0.027  0.052  391 GLU AAA CA  
2804  C C   . GLU A 391 ? 0.340 0.489 0.372 -0.002 0.028  0.049  391 GLU AAA C   
2805  O O   . GLU A 391 ? 0.338 0.489 0.375 -0.002 0.032  0.054  391 GLU AAA O   
2806  C CB  . GLU A 391 ? 0.316 0.473 0.332 0.001  0.024  0.048  391 GLU AAA CB  
2807  C CG  . GLU A 391 ? 0.327 0.490 0.338 0.003  0.023  0.051  391 GLU AAA CG  
2808  C CD  . GLU A 391 ? 0.331 0.489 0.340 0.003  0.022  0.049  391 GLU AAA CD  
2809  O OE1 . GLU A 391 ? 0.304 0.456 0.312 0.001  0.020  0.043  391 GLU AAA OE1 
2810  O OE2 . GLU A 391 ? 0.326 0.488 0.336 0.005  0.023  0.053  391 GLU AAA OE2 
2811  N N   . ALA A 392 ? 0.360 0.503 0.391 -0.003 0.026  0.042  392 ALA AAA N   
2812  C CA  . ALA A 392 ? 0.381 0.522 0.418 -0.005 0.027  0.039  392 ALA AAA CA  
2813  C C   . ALA A 392 ? 0.431 0.568 0.478 -0.006 0.031  0.042  392 ALA AAA C   
2814  O O   . ALA A 392 ? 0.527 0.665 0.582 -0.007 0.033  0.041  392 ALA AAA O   
2815  C CB  . ALA A 392 ? 0.356 0.492 0.389 -0.005 0.023  0.031  392 ALA AAA CB  
2816  N N   . ALA A 393 ? 0.430 0.564 0.480 -0.006 0.031  0.045  393 ALA AAA N   
2817  C CA  . ALA A 393 ? 0.425 0.555 0.487 -0.007 0.035  0.048  393 ALA AAA CA  
2818  C C   . ALA A 393 ? 0.430 0.564 0.496 -0.006 0.040  0.056  393 ALA AAA C   
2819  O O   . ALA A 393 ? 0.420 0.553 0.496 -0.007 0.044  0.056  393 ALA AAA O   
2820  C CB  . ALA A 393 ? 0.437 0.562 0.498 -0.007 0.035  0.048  393 ALA AAA CB  
2821  N N   . ILE A 394 ? 0.417 0.557 0.477 -0.003 0.040  0.061  394 ILE AAA N   
2822  C CA  . ILE A 394 ? 0.432 0.578 0.494 -0.001 0.044  0.070  394 ILE AAA CA  
2823  C C   . ILE A 394 ? 0.439 0.588 0.503 -0.002 0.045  0.068  394 ILE AAA C   
2824  O O   . ILE A 394 ? 0.454 0.603 0.527 -0.003 0.051  0.073  394 ILE AAA O   
2825  C CB  . ILE A 394 ? 0.429 0.581 0.482 0.002  0.043  0.074  394 ILE AAA CB  
2826  C CG1 . ILE A 394 ? 0.415 0.563 0.470 0.003  0.043  0.077  394 ILE AAA CG1 
2827  C CG2 . ILE A 394 ? 0.418 0.578 0.471 0.004  0.046  0.081  394 ILE AAA CG2 
2828  C CD1 . ILE A 394 ? 0.407 0.562 0.453 0.006  0.041  0.080  394 ILE AAA CD1 
2829  N N   . ALA A 395 ? 0.470 0.622 0.527 -0.003 0.041  0.063  395 ALA AAA N   
2830  C CA  . ALA A 395 ? 0.484 0.640 0.542 -0.004 0.042  0.061  395 ALA AAA CA  
2831  C C   . ALA A 395 ? 0.511 0.662 0.580 -0.006 0.045  0.058  395 ALA AAA C   
2832  O O   . ALA A 395 ? 0.509 0.663 0.584 -0.007 0.049  0.060  395 ALA AAA O   
2833  C CB  . ALA A 395 ? 0.475 0.633 0.523 -0.004 0.037  0.054  395 ALA AAA CB  
2834  N N   . LYS A 396 ? 0.545 0.690 0.618 -0.008 0.043  0.052  396 LYS AAA N   
2835  C CA  . LYS A 396 ? 0.521 0.662 0.604 -0.011 0.045  0.047  396 LYS AAA CA  
2836  C C   . LYS A 396 ? 0.493 0.631 0.588 -0.012 0.051  0.052  396 LYS AAA C   
2837  O O   . LYS A 396 ? 0.485 0.623 0.590 -0.014 0.054  0.050  396 LYS AAA O   
2838  C CB  . LYS A 396 ? 0.561 0.697 0.642 -0.012 0.041  0.038  396 LYS AAA CB  
2839  C CG  . LYS A 396 ? 0.587 0.721 0.677 -0.014 0.042  0.032  396 LYS AAA CG  
2840  C CD  . LYS A 396 ? 0.609 0.740 0.698 -0.014 0.038  0.024  396 LYS AAA CD  
2841  C CE  . LYS A 396 ? 0.660 0.790 0.760 -0.016 0.039  0.017  396 LYS AAA CE  
2842  N NZ  . LYS A 396 ? 0.700 0.834 0.802 -0.017 0.039  0.013  396 LYS AAA NZ  
2843  N N   . TYR A 397 ? 0.472 0.607 0.568 -0.011 0.052  0.057  397 TYR AAA N   
2844  C CA  . TYR A 397 ? 0.479 0.609 0.588 -0.012 0.058  0.061  397 TYR AAA CA  
2845  C C   . TYR A 397 ? 0.478 0.611 0.589 -0.009 0.063  0.072  397 TYR AAA C   
2846  O O   . TYR A 397 ? 0.468 0.597 0.590 -0.010 0.069  0.076  397 TYR AAA O   
2847  C CB  . TYR A 397 ? 0.483 0.607 0.594 -0.012 0.057  0.058  397 TYR AAA CB  
2848  C CG  . TYR A 397 ? 0.468 0.589 0.580 -0.015 0.053  0.047  397 TYR AAA CG  
2849  C CD1 . TYR A 397 ? 0.468 0.588 0.594 -0.017 0.056  0.043  397 TYR AAA CD1 
2850  C CD2 . TYR A 397 ? 0.470 0.591 0.572 -0.014 0.047  0.042  397 TYR AAA CD2 
2851  C CE1 . TYR A 397 ? 0.469 0.587 0.596 -0.019 0.052  0.033  397 TYR AAA CE1 
2852  C CE2 . TYR A 397 ? 0.475 0.594 0.578 -0.015 0.044  0.033  397 TYR AAA CE2 
2853  C CZ  . TYR A 397 ? 0.475 0.594 0.590 -0.018 0.046  0.028  397 TYR AAA CZ  
2854  O OH  . TYR A 397 ? 0.481 0.600 0.597 -0.018 0.043  0.019  397 TYR AAA OH  
2855  N N   . GLY A 398 ? 0.501 0.640 0.600 -0.006 0.061  0.076  398 GLY AAA N   
2856  C CA  . GLY A 398 ? 0.520 0.663 0.618 -0.003 0.065  0.087  398 GLY AAA CA  
2857  C C   . GLY A 398 ? 0.539 0.680 0.633 -0.001 0.064  0.090  398 GLY AAA C   
2858  O O   . GLY A 398 ? 0.516 0.650 0.616 -0.002 0.063  0.087  398 GLY AAA O   
2859  N N   . GLU A 399 ? 0.572 0.720 0.659 0.003  0.064  0.097  399 GLU AAA N   
2860  C CA  . GLU A 399 ? 0.622 0.770 0.704 0.006  0.062  0.101  399 GLU AAA CA  
2861  C C   . GLU A 399 ? 0.642 0.782 0.734 0.006  0.067  0.104  399 GLU AAA C   
2862  O O   . GLU A 399 ? 0.611 0.749 0.702 0.006  0.065  0.103  399 GLU AAA O   
2863  C CB  . GLU A 399 ? 0.685 0.843 0.760 0.011  0.064  0.109  399 GLU AAA CB  
2864  C CG  . GLU A 399 ? 0.714 0.875 0.784 0.014  0.062  0.113  399 GLU AAA CG  
2865  C CD  . GLU A 399 ? 0.759 0.922 0.818 0.014  0.055  0.105  399 GLU AAA CD  
2866  O OE1 . GLU A 399 ? 0.770 0.939 0.822 0.014  0.052  0.102  399 GLU AAA OE1 
2867  O OE2 . GLU A 399 ? 0.733 0.892 0.792 0.014  0.053  0.103  399 GLU AAA OE2 
2868  N N   . ASP A 400 ? 0.652 0.790 0.756 0.005  0.073  0.109  400 ASP AAA N   
2869  C CA  . ASP A 400 ? 0.633 0.764 0.748 0.006  0.079  0.114  400 ASP AAA CA  
2870  C C   . ASP A 400 ? 0.565 0.687 0.688 0.001  0.078  0.106  400 ASP AAA C   
2871  O O   . ASP A 400 ? 0.577 0.694 0.709 0.001  0.081  0.108  400 ASP AAA O   
2872  C CB  . ASP A 400 ? 0.687 0.818 0.812 0.007  0.087  0.123  400 ASP AAA CB  
2873  C CG  . ASP A 400 ? 0.696 0.836 0.813 0.012  0.089  0.133  400 ASP AAA CG  
2874  O OD1 . ASP A 400 ? 0.717 0.862 0.824 0.015  0.085  0.134  400 ASP AAA OD1 
2875  O OD2 . ASP A 400 ? 0.704 0.846 0.825 0.013  0.094  0.138  400 ASP AAA OD2 
2876  N N   . ASP A 401 ? 0.498 0.619 0.621 -0.002 0.075  0.097  401 ASP AAA N   
2877  C CA  . ASP A 401 ? 0.488 0.603 0.619 -0.006 0.074  0.088  401 ASP AAA CA  
2878  C C   . ASP A 401 ? 0.460 0.573 0.581 -0.007 0.066  0.081  401 ASP AAA C   
2879  O O   . ASP A 401 ? 0.453 0.563 0.578 -0.009 0.064  0.073  401 ASP AAA O   
2880  C CB  . ASP A 401 ? 0.469 0.584 0.607 -0.010 0.074  0.081  401 ASP AAA CB  
2881  C CG  . ASP A 401 ? 0.475 0.584 0.626 -0.013 0.076  0.074  401 ASP AAA CG  
2882  O OD1 . ASP A 401 ? 0.501 0.604 0.659 -0.014 0.079  0.076  401 ASP AAA OD1 
2883  O OD2 . ASP A 401 ? 0.444 0.554 0.598 -0.016 0.075  0.067  401 ASP AAA OD2 
2884  N N   . ILE A 402 ? 0.451 0.570 0.560 -0.004 0.063  0.085  402 ILE AAA N   
2885  C CA  . ILE A 402 ? 0.469 0.587 0.568 -0.003 0.056  0.079  402 ILE AAA CA  
2886  C C   . ILE A 402 ? 0.491 0.608 0.588 -0.001 0.056  0.084  402 ILE AAA C   
2887  O O   . ILE A 402 ? 0.531 0.652 0.625 0.002  0.059  0.092  402 ILE AAA O   
2888  C CB  . ILE A 402 ? 0.458 0.583 0.544 -0.002 0.052  0.077  402 ILE AAA CB  
2889  C CG1 . ILE A 402 ? 0.443 0.569 0.530 -0.005 0.051  0.071  402 ILE AAA CG1 
2890  C CG2 . ILE A 402 ? 0.435 0.560 0.511 -0.002 0.047  0.073  402 ILE AAA CG2 
2891  C CD1 . ILE A 402 ? 0.446 0.565 0.539 -0.008 0.049  0.062  402 ILE AAA CD1 
2892  N N   . GLU A 403 ? 0.506 0.617 0.603 -0.003 0.054  0.079  403 GLU AAA N   
2893  C CA  . GLU A 403 ? 0.490 0.601 0.583 -0.001 0.052  0.081  403 GLU AAA CA  
2894  C C   . GLU A 403 ? 0.466 0.577 0.548 -0.001 0.046  0.074  403 GLU AAA C   
2895  O O   . GLU A 403 ? 0.457 0.565 0.539 -0.004 0.043  0.066  403 GLU AAA O   
2896  C CB  . GLU A 403 ? 0.512 0.616 0.615 -0.001 0.055  0.082  403 GLU AAA CB  
2897  C CG  . GLU A 403 ? 0.528 0.632 0.630 0.002  0.057  0.089  403 GLU AAA CG  
2898  C CD  . GLU A 403 ? 0.533 0.642 0.639 0.005  0.062  0.099  403 GLU AAA CD  
2899  O OE1 . GLU A 403 ? 0.538 0.643 0.654 0.005  0.068  0.103  403 GLU AAA OE1 
2900  O OE2 . GLU A 403 ? 0.525 0.641 0.622 0.009  0.061  0.104  403 GLU AAA OE2 
2901  N N   . GLU A 404 ? 0.457 0.572 0.530 0.001  0.044  0.076  404 GLU AAA N   
2902  C CA  . GLU A 404 ? 0.466 0.582 0.530 0.001  0.038  0.070  404 GLU AAA CA  
2903  C C   . GLU A 404 ? 0.408 0.521 0.473 0.002  0.038  0.072  404 GLU AAA C   
2904  O O   . GLU A 404 ? 0.389 0.507 0.453 0.005  0.040  0.078  404 GLU AAA O   
2905  C CB  . GLU A 404 ? 0.514 0.638 0.568 0.003  0.036  0.071  404 GLU AAA CB  
2906  C CG  . GLU A 404 ? 0.541 0.669 0.595 0.002  0.037  0.071  404 GLU AAA CG  
2907  C CD  . GLU A 404 ? 0.569 0.705 0.614 0.004  0.035  0.071  404 GLU AAA CD  
2908  O OE1 . GLU A 404 ? 0.584 0.722 0.621 0.004  0.031  0.068  404 GLU AAA OE1 
2909  O OE2 . GLU A 404 ? 0.616 0.757 0.662 0.005  0.037  0.075  404 GLU AAA OE2 
2910  N N   . TYR A 405 ? 0.374 0.481 0.440 -0.000 0.036  0.066  405 TYR AAA N   
2911  C CA  . TYR A 405 ? 0.335 0.438 0.401 0.000  0.035  0.066  405 TYR AAA CA  
2912  C C   . TYR A 405 ? 0.317 0.422 0.373 -0.000 0.031  0.060  405 TYR AAA C   
2913  O O   . TYR A 405 ? 0.306 0.409 0.359 -0.002 0.028  0.054  405 TYR AAA O   
2914  C CB  . TYR A 405 ? 0.325 0.421 0.400 -0.002 0.037  0.063  405 TYR AAA CB  
2915  C CG  . TYR A 405 ? 0.323 0.417 0.410 -0.002 0.042  0.068  405 TYR AAA CG  
2916  C CD1 . TYR A 405 ? 0.306 0.398 0.400 -0.004 0.044  0.066  405 TYR AAA CD1 
2917  C CD2 . TYR A 405 ? 0.333 0.425 0.425 -0.000 0.045  0.073  405 TYR AAA CD2 
2918  C CE1 . TYR A 405 ? 0.328 0.418 0.434 -0.004 0.049  0.070  405 TYR AAA CE1 
2919  C CE2 . TYR A 405 ? 0.352 0.441 0.456 -0.000 0.050  0.078  405 TYR AAA CE2 
2920  C CZ  . TYR A 405 ? 0.349 0.437 0.461 -0.002 0.053  0.077  405 TYR AAA CZ  
2921  O OH  . TYR A 405 ? 0.369 0.454 0.493 -0.003 0.059  0.081  405 TYR AAA OH  
2922  N N   . LEU A 406 ? 0.309 0.417 0.360 0.002  0.029  0.062  406 LEU AAA N   
2923  C CA  . LEU A 406 ? 0.307 0.416 0.349 0.001  0.026  0.057  406 LEU AAA CA  
2924  C C   . LEU A 406 ? 0.296 0.407 0.337 0.003  0.025  0.058  406 LEU AAA C   
2925  O O   . LEU A 406 ? 0.267 0.378 0.312 0.004  0.027  0.063  406 LEU AAA O   
2926  C CB  . LEU A 406 ? 0.322 0.439 0.357 0.002  0.025  0.057  406 LEU AAA CB  
2927  C CG  . LEU A 406 ? 0.319 0.445 0.352 0.006  0.026  0.063  406 LEU AAA CG  
2928  C CD1 . LEU A 406 ? 0.316 0.449 0.341 0.006  0.024  0.061  406 LEU AAA CD1 
2929  C CD2 . LEU A 406 ? 0.342 0.470 0.382 0.007  0.030  0.071  406 LEU AAA CD2 
2930  N N   . SER A 407 ? 0.285 0.394 0.319 0.002  0.022  0.052  407 SER AAA N   
2931  C CA  . SER A 407 ? 0.293 0.402 0.324 0.002  0.021  0.051  407 SER AAA CA  
2932  C C   . SER A 407 ? 0.298 0.410 0.322 0.002  0.018  0.046  407 SER AAA C   
2933  O O   . SER A 407 ? 0.323 0.431 0.343 -0.000 0.017  0.041  407 SER AAA O   
2934  C CB  . SER A 407 ? 0.286 0.388 0.322 0.001  0.021  0.049  407 SER AAA CB  
2935  O OG  . SER A 407 ? 0.298 0.401 0.332 0.001  0.020  0.048  407 SER AAA OG  
2936  N N   . GLU A 408 ? 0.301 0.420 0.321 0.003  0.018  0.046  408 GLU AAA N   
2937  C CA  . GLU A 408 ? 0.298 0.419 0.311 0.002  0.016  0.040  408 GLU AAA CA  
2938  C C   . GLU A 408 ? 0.279 0.399 0.292 0.002  0.015  0.038  408 GLU AAA C   
2939  O O   . GLU A 408 ? 0.276 0.400 0.292 0.004  0.016  0.042  408 GLU AAA O   
2940  C CB  . GLU A 408 ? 0.313 0.446 0.322 0.004  0.015  0.042  408 GLU AAA CB  
2941  C CG  . GLU A 408 ? 0.321 0.457 0.324 0.003  0.014  0.035  408 GLU AAA CG  
2942  C CD  . GLU A 408 ? 0.350 0.498 0.351 0.005  0.013  0.036  408 GLU AAA CD  
2943  O OE1 . GLU A 408 ? 0.378 0.534 0.381 0.008  0.014  0.042  408 GLU AAA OE1 
2944  O OE2 . GLU A 408 ? 0.360 0.510 0.357 0.004  0.013  0.031  408 GLU AAA OE2 
2945  N N   . PHE A 409 ? 0.281 0.395 0.292 0.000  0.014  0.032  409 PHE AAA N   
2946  C CA  . PHE A 409 ? 0.274 0.385 0.285 -0.001 0.014  0.030  409 PHE AAA CA  
2947  C C   . PHE A 409 ? 0.265 0.372 0.271 -0.003 0.013  0.023  409 PHE AAA C   
2948  O O   . PHE A 409 ? 0.264 0.370 0.266 -0.003 0.013  0.021  409 PHE AAA O   
2949  C CB  . PHE A 409 ? 0.296 0.399 0.312 -0.001 0.014  0.031  409 PHE AAA CB  
2950  C CG  . PHE A 409 ? 0.297 0.392 0.312 -0.003 0.014  0.029  409 PHE AAA CG  
2951  C CD1 . PHE A 409 ? 0.295 0.391 0.312 -0.003 0.015  0.031  409 PHE AAA CD1 
2952  C CD2 . PHE A 409 ? 0.299 0.387 0.312 -0.005 0.014  0.024  409 PHE AAA CD2 
2953  C CE1 . PHE A 409 ? 0.316 0.406 0.333 -0.004 0.015  0.028  409 PHE AAA CE1 
2954  C CE2 . PHE A 409 ? 0.311 0.393 0.324 -0.006 0.013  0.022  409 PHE AAA CE2 
2955  C CZ  . PHE A 409 ? 0.305 0.388 0.320 -0.005 0.014  0.023  409 PHE AAA CZ  
2956  N N   . SER A 410 ? 0.260 0.365 0.266 -0.003 0.013  0.021  410 SER AAA N   
2957  C CA  . SER A 410 ? 0.259 0.359 0.261 -0.005 0.013  0.015  410 SER AAA CA  
2958  C C   . SER A 410 ? 0.257 0.346 0.260 -0.006 0.013  0.014  410 SER AAA C   
2959  O O   . SER A 410 ? 0.254 0.343 0.262 -0.006 0.013  0.016  410 SER AAA O   
2960  C CB  . SER A 410 ? 0.262 0.368 0.263 -0.005 0.013  0.012  410 SER AAA CB  
2961  O OG  . SER A 410 ? 0.275 0.375 0.274 -0.007 0.014  0.007  410 SER AAA OG  
2962  N N   . THR A 411 ? 0.251 0.334 0.250 -0.007 0.014  0.010  411 THR AAA N   
2963  C CA  . THR A 411 ? 0.259 0.334 0.258 -0.008 0.014  0.007  411 THR AAA CA  
2964  C C   . THR A 411 ? 0.263 0.339 0.264 -0.009 0.014  0.006  411 THR AAA C   
2965  O O   . THR A 411 ? 0.238 0.320 0.238 -0.009 0.014  0.005  411 THR AAA O   
2966  C CB  . THR A 411 ? 0.264 0.334 0.258 -0.009 0.015  0.003  411 THR AAA CB  
2967  O OG1 . THR A 411 ? 0.267 0.337 0.259 -0.008 0.014  0.005  411 THR AAA OG1 
2968  C CG2 . THR A 411 ? 0.277 0.338 0.269 -0.009 0.015  0.001  411 THR AAA CG2 
2969  N N   . LEU A 412 ? 0.261 0.331 0.264 -0.009 0.014  0.007  412 LEU AAA N   
2970  C CA  . LEU A 412 ? 0.274 0.345 0.279 -0.009 0.015  0.005  412 LEU AAA CA  
2971  C C   . LEU A 412 ? 0.292 0.362 0.293 -0.010 0.016  0.001  412 LEU AAA C   
2972  O O   . LEU A 412 ? 0.300 0.375 0.302 -0.011 0.016  -0.000 412 LEU AAA O   
2973  C CB  . LEU A 412 ? 0.289 0.353 0.296 -0.009 0.014  0.005  412 LEU AAA CB  
2974  C CG  . LEU A 412 ? 0.295 0.356 0.303 -0.010 0.015  0.004  412 LEU AAA CG  
2975  C CD1 . LEU A 412 ? 0.311 0.379 0.323 -0.009 0.014  0.006  412 LEU AAA CD1 
2976  C CD2 . LEU A 412 ? 0.306 0.361 0.316 -0.010 0.015  0.004  412 LEU AAA CD2 
2977  N N   . GLU A 413 ? 0.309 0.373 0.306 -0.011 0.017  -0.002 413 GLU AAA N   
2978  C CA  . GLU A 413 ? 0.328 0.388 0.322 -0.012 0.019  -0.006 413 GLU AAA CA  
2979  C C   . GLU A 413 ? 0.336 0.403 0.329 -0.013 0.019  -0.008 413 GLU AAA C   
2980  O O   . GLU A 413 ? 0.337 0.406 0.330 -0.014 0.021  -0.012 413 GLU AAA O   
2981  C CB  . GLU A 413 ? 0.362 0.414 0.351 -0.012 0.020  -0.008 413 GLU AAA CB  
2982  C CG  . GLU A 413 ? 0.397 0.444 0.386 -0.011 0.020  -0.007 413 GLU AAA CG  
2983  C CD  . GLU A 413 ? 0.403 0.450 0.393 -0.010 0.018  -0.004 413 GLU AAA CD  
2984  O OE1 . GLU A 413 ? 0.415 0.467 0.409 -0.010 0.016  -0.001 413 GLU AAA OE1 
2985  O OE2 . GLU A 413 ? 0.466 0.507 0.453 -0.009 0.018  -0.005 413 GLU AAA OE2 
2986  N N   . ILE A 414 ? 0.313 0.384 0.305 -0.012 0.018  -0.006 414 ILE AAA N   
2987  C CA  . ILE A 414 ? 0.320 0.399 0.312 -0.012 0.019  -0.008 414 ILE AAA CA  
2988  C C   . ILE A 414 ? 0.302 0.390 0.297 -0.012 0.017  -0.007 414 ILE AAA C   
2989  O O   . ILE A 414 ? 0.319 0.413 0.314 -0.012 0.018  -0.011 414 ILE AAA O   
2990  C CB  . ILE A 414 ? 0.318 0.399 0.308 -0.011 0.018  -0.006 414 ILE AAA CB  
2991  C CG1 . ILE A 414 ? 0.328 0.399 0.314 -0.011 0.019  -0.006 414 ILE AAA CG1 
2992  C CG2 . ILE A 414 ? 0.307 0.396 0.296 -0.012 0.018  -0.009 414 ILE AAA CG2 
2993  C CD1 . ILE A 414 ? 0.350 0.416 0.333 -0.012 0.021  -0.011 414 ILE AAA CD1 
2994  N N   . ALA A 415 ? 0.285 0.375 0.283 -0.010 0.016  -0.003 415 ALA AAA N   
2995  C CA  . ALA A 415 ? 0.267 0.367 0.268 -0.009 0.015  -0.001 415 ALA AAA CA  
2996  C C   . ALA A 415 ? 0.277 0.377 0.279 -0.010 0.016  -0.005 415 ALA AAA C   
2997  O O   . ALA A 415 ? 0.283 0.393 0.286 -0.010 0.016  -0.008 415 ALA AAA O   
2998  C CB  . ALA A 415 ? 0.250 0.349 0.255 -0.007 0.014  0.005  415 ALA AAA CB  
2999  N N   . ALA A 416 ? 0.288 0.379 0.290 -0.012 0.017  -0.007 416 ALA AAA N   
3000  C CA  . ALA A 416 ? 0.290 0.380 0.293 -0.013 0.018  -0.011 416 ALA AAA CA  
3001  C C   . ALA A 416 ? 0.300 0.391 0.301 -0.015 0.020  -0.017 416 ALA AAA C   
3002  O O   . ALA A 416 ? 0.297 0.392 0.301 -0.016 0.021  -0.021 416 ALA AAA O   
3003  C CB  . ALA A 416 ? 0.288 0.368 0.291 -0.014 0.019  -0.010 416 ALA AAA CB  
3004  N N   . ALA A 417 ? 0.313 0.402 0.312 -0.015 0.021  -0.018 417 ALA AAA N   
3005  C CA  . ALA A 417 ? 0.336 0.425 0.334 -0.017 0.024  -0.024 417 ALA AAA CA  
3006  C C   . ALA A 417 ? 0.361 0.464 0.362 -0.017 0.023  -0.027 417 ALA AAA C   
3007  O O   . ALA A 417 ? 0.433 0.537 0.435 -0.018 0.025  -0.033 417 ALA AAA O   
3008  C CB  . ALA A 417 ? 0.338 0.419 0.332 -0.017 0.025  -0.023 417 ALA AAA CB  
3009  N N   . HIS A 418 ? 0.380 0.491 0.380 -0.014 0.020  -0.023 418 HIS AAA N   
3010  C CA  . HIS A 418 ? 0.381 0.507 0.384 -0.013 0.019  -0.025 418 HIS AAA CA  
3011  C C   . HIS A 418 ? 0.376 0.503 0.377 -0.015 0.021  -0.029 418 HIS AAA C   
3012  O O   . HIS A 418 ? 0.408 0.541 0.412 -0.016 0.022  -0.036 418 HIS AAA O   
3013  C CB  . HIS A 418 ? 0.400 0.534 0.407 -0.013 0.019  -0.029 418 HIS AAA CB  
3014  C CG  . HIS A 418 ? 0.428 0.563 0.435 -0.011 0.017  -0.024 418 HIS AAA CG  
3015  N ND1 . HIS A 418 ? 0.474 0.619 0.482 -0.008 0.015  -0.019 418 HIS AAA ND1 
3016  C CD2 . HIS A 418 ? 0.462 0.590 0.470 -0.012 0.017  -0.022 418 HIS AAA CD2 
3017  C CE1 . HIS A 418 ? 0.469 0.613 0.479 -0.007 0.014  -0.015 418 HIS AAA CE1 
3018  N NE2 . HIS A 418 ? 0.452 0.585 0.463 -0.009 0.015  -0.017 418 HIS AAA NE2 
3019  N N   . ARG A 419 ? 0.381 0.501 0.379 -0.014 0.021  -0.027 419 ARG AAA N   
3020  C CA  . ARG A 419 ? 0.368 0.489 0.365 -0.015 0.022  -0.030 419 ARG AAA CA  
3021  C C   . ARG A 419 ? 0.379 0.516 0.378 -0.014 0.021  -0.032 419 ARG AAA C   
3022  O O   . ARG A 419 ? 0.398 0.543 0.396 -0.012 0.018  -0.027 419 ARG AAA O   
3023  C CB  . ARG A 419 ? 0.386 0.499 0.379 -0.015 0.022  -0.025 419 ARG AAA CB  
3024  C CG  . ARG A 419 ? 0.385 0.484 0.376 -0.015 0.023  -0.024 419 ARG AAA CG  
3025  C CD  . ARG A 419 ? 0.396 0.488 0.383 -0.015 0.024  -0.023 419 ARG AAA CD  
3026  N NE  . ARG A 419 ? 0.405 0.485 0.390 -0.015 0.026  -0.023 419 ARG AAA NE  
3027  C CZ  . ARG A 419 ? 0.407 0.479 0.389 -0.015 0.027  -0.022 419 ARG AAA CZ  
3028  N NH1 . ARG A 419 ? 0.410 0.485 0.390 -0.014 0.026  -0.021 419 ARG AAA NH1 
3029  N NH2 . ARG A 419 ? 0.412 0.474 0.392 -0.015 0.029  -0.022 419 ARG AAA NH2 
3030  N N   . GLU A 420 ? 0.402 0.543 0.403 -0.016 0.023  -0.040 420 GLU AAA N   
3031  C CA  . GLU A 420 ? 0.417 0.574 0.420 -0.015 0.022  -0.044 420 GLU AAA CA  
3032  C C   . GLU A 420 ? 0.415 0.573 0.417 -0.016 0.023  -0.046 420 GLU AAA C   
3033  O O   . GLU A 420 ? 0.396 0.542 0.398 -0.018 0.025  -0.048 420 GLU AAA O   
3034  C CB  . GLU A 420 ? 0.450 0.613 0.458 -0.017 0.023  -0.052 420 GLU AAA CB  
3035  C CG  . GLU A 420 ? 0.494 0.659 0.503 -0.016 0.022  -0.050 420 GLU AAA CG  
3036  C CD  . GLU A 420 ? 0.491 0.668 0.506 -0.017 0.023  -0.058 420 GLU AAA CD  
3037  O OE1 . GLU A 420 ? 0.468 0.658 0.484 -0.016 0.022  -0.063 420 GLU AAA OE1 
3038  O OE2 . GLU A 420 ? 0.547 0.719 0.563 -0.018 0.024  -0.059 420 GLU AAA OE2 
3039  N N   . LYS A 421 ? 0.382 0.554 0.384 -0.013 0.020  -0.046 421 LYS AAA N   
3040  C CA  . LYS A 421 ? 0.404 0.581 0.406 -0.014 0.021  -0.050 421 LYS AAA CA  
3041  C C   . LYS A 421 ? 0.395 0.572 0.402 -0.017 0.024  -0.060 421 LYS AAA C   
3042  O O   . LYS A 421 ? 0.380 0.561 0.391 -0.018 0.025  -0.064 421 LYS AAA O   
3043  C CB  . LYS A 421 ? 0.397 0.592 0.399 -0.011 0.018  -0.050 421 LYS AAA CB  
3044  C CG  . LYS A 421 ? 0.419 0.615 0.417 -0.008 0.016  -0.040 421 LYS AAA CG  
3045  C CD  . LYS A 421 ? 0.437 0.650 0.435 -0.004 0.013  -0.039 421 LYS AAA CD  
3046  C CE  . LYS A 421 ? 0.452 0.662 0.447 -0.002 0.012  -0.029 421 LYS AAA CE  
3047  N NZ  . LYS A 421 ? 0.458 0.685 0.452 0.002  0.010  -0.025 421 LYS AAA NZ  
3048  N N   . PRO A 422 ? 0.451 0.624 0.458 -0.019 0.027  -0.064 422 PRO AAA N   
3049  C CA  . PRO A 422 ? 0.498 0.673 0.511 -0.021 0.030  -0.074 422 PRO AAA CA  
3050  C C   . PRO A 422 ? 0.580 0.775 0.596 -0.020 0.028  -0.080 422 PRO AAA C   
3051  O O   . PRO A 422 ? 0.599 0.805 0.613 -0.017 0.025  -0.076 422 PRO AAA O   
3052  C CB  . PRO A 422 ? 0.479 0.647 0.490 -0.022 0.032  -0.075 422 PRO AAA CB  
3053  C CG  . PRO A 422 ? 0.476 0.634 0.480 -0.020 0.030  -0.065 422 PRO AAA CG  
3054  C CD  . PRO A 422 ? 0.452 0.618 0.454 -0.018 0.026  -0.059 422 PRO AAA CD  
3055  N N   . GLU A 423 ? 0.658 0.858 0.680 -0.023 0.031  -0.089 423 GLU AAA N   
3056  C CA  . GLU A 423 ? 0.689 0.910 0.717 -0.022 0.029  -0.095 423 GLU AAA CA  
3057  C C   . GLU A 423 ? 0.640 0.874 0.668 -0.020 0.028  -0.099 423 GLU AAA C   
3058  O O   . GLU A 423 ? 0.601 0.854 0.630 -0.017 0.025  -0.100 423 GLU AAA O   
3059  C CB  . GLU A 423 ? 0.772 0.992 0.807 -0.025 0.033  -0.105 423 GLU AAA CB  
3060  C CG  . GLU A 423 ? 0.834 1.047 0.874 -0.029 0.038  -0.113 423 GLU AAA CG  
3061  C CD  . GLU A 423 ? 0.887 1.104 0.936 -0.032 0.042  -0.124 423 GLU AAA CD  
3062  O OE1 . GLU A 423 ? 0.816 1.052 0.869 -0.031 0.040  -0.131 423 GLU AAA OE1 
3063  O OE2 . GLU A 423 ? 0.906 1.109 0.958 -0.036 0.047  -0.127 423 GLU AAA OE2 
3064  N N   . HIS A 424 ? 0.630 0.857 0.657 -0.022 0.030  -0.099 424 HIS AAA N   
3065  C CA  . HIS A 424 ? 0.643 0.882 0.671 -0.020 0.028  -0.103 424 HIS AAA CA  
3066  C C   . HIS A 424 ? 0.612 0.859 0.633 -0.016 0.024  -0.093 424 HIS AAA C   
3067  O O   . HIS A 424 ? 0.596 0.856 0.618 -0.014 0.022  -0.096 424 HIS AAA O   
3068  C CB  . HIS A 424 ? 0.677 0.905 0.706 -0.023 0.032  -0.106 424 HIS AAA CB  
3069  C CG  . HIS A 424 ? 0.683 0.893 0.706 -0.023 0.033  -0.098 424 HIS AAA CG  
3070  N ND1 . HIS A 424 ? 0.645 0.856 0.662 -0.020 0.030  -0.091 424 HIS AAA ND1 
3071  C CD2 . HIS A 424 ? 0.673 0.864 0.695 -0.025 0.036  -0.095 424 HIS AAA CD2 
3072  C CE1 . HIS A 424 ? 0.646 0.840 0.659 -0.021 0.031  -0.085 424 HIS AAA CE1 
3073  N NE2 . HIS A 424 ? 0.652 0.834 0.668 -0.023 0.035  -0.087 424 HIS AAA NE2 
3074  N N   . LEU A 425 ? 0.580 0.818 0.595 -0.014 0.022  -0.083 425 LEU AAA N   
3075  C CA  . LEU A 425 ? 0.559 0.804 0.570 -0.010 0.018  -0.074 425 LEU AAA CA  
3076  C C   . LEU A 425 ? 0.561 0.816 0.571 -0.007 0.015  -0.070 425 LEU AAA C   
3077  O O   . LEU A 425 ? 0.481 0.741 0.486 -0.003 0.013  -0.061 425 LEU AAA O   
3078  C CB  . LEU A 425 ? 0.572 0.798 0.577 -0.010 0.019  -0.065 425 LEU AAA CB  
3079  C CG  . LEU A 425 ? 0.573 0.790 0.577 -0.012 0.020  -0.067 425 LEU AAA CG  
3080  C CD1 . LEU A 425 ? 0.538 0.737 0.539 -0.013 0.021  -0.060 425 LEU AAA CD1 
3081  C CD2 . LEU A 425 ? 0.567 0.797 0.570 -0.010 0.019  -0.067 425 LEU AAA CD2 
3082  N N   . ARG A 426 ? 0.512 0.771 0.526 -0.008 0.016  -0.076 426 ARG AAA N   
3083  C CA  . ARG A 426 ? 0.513 0.783 0.526 -0.004 0.014  -0.073 426 ARG AAA CA  
3084  C C   . ARG A 426 ? 0.545 0.838 0.559 -0.000 0.011  -0.075 426 ARG AAA C   
3085  O O   . ARG A 426 ? 0.497 0.800 0.515 -0.002 0.012  -0.085 426 ARG AAA O   
3086  C CB  . ARG A 426 ? 0.494 0.761 0.512 -0.007 0.016  -0.079 426 ARG AAA CB  
3087  C CG  . ARG A 426 ? 0.457 0.703 0.474 -0.010 0.018  -0.075 426 ARG AAA CG  
3088  C CD  . ARG A 426 ? 0.428 0.669 0.441 -0.007 0.015  -0.063 426 ARG AAA CD  
3089  N NE  . ARG A 426 ? 0.434 0.688 0.448 -0.004 0.013  -0.063 426 ARG AAA NE  
3090  C CZ  . ARG A 426 ? 0.411 0.664 0.428 -0.005 0.014  -0.067 426 ARG AAA CZ  
3091  N NH1 . ARG A 426 ? 0.415 0.654 0.434 -0.009 0.017  -0.070 426 ARG AAA NH1 
3092  N NH2 . ARG A 426 ? 0.395 0.662 0.413 -0.001 0.012  -0.066 426 ARG AAA NH2 
3093  N N   . GLU A 427 ? 0.607 0.908 0.617 0.005  0.009  -0.067 427 GLU AAA N   
3094  C CA  . GLU A 427 ? 0.655 0.979 0.665 0.010  0.006  -0.067 427 GLU AAA CA  
3095  C C   . GLU A 427 ? 0.651 0.989 0.663 0.013  0.005  -0.069 427 GLU AAA C   
3096  O O   . GLU A 427 ? 0.692 1.051 0.705 0.017  0.003  -0.072 427 GLU AAA O   
3097  C CB  . GLU A 427 ? 0.705 1.030 0.710 0.014  0.005  -0.056 427 GLU AAA CB  
3098  C CG  . GLU A 427 ? 0.716 1.048 0.720 0.014  0.005  -0.059 427 GLU AAA CG  
3099  C CD  . GLU A 427 ? 0.714 1.042 0.712 0.016  0.004  -0.049 427 GLU AAA CD  
3100  O OE1 . GLU A 427 ? 0.651 0.970 0.649 0.013  0.005  -0.050 427 GLU AAA OE1 
3101  O OE2 . GLU A 427 ? 0.690 1.024 0.685 0.021  0.003  -0.039 427 GLU AAA OE2 
3102  N N   . ASN A 428 ? 0.601 0.927 0.613 0.012  0.005  -0.066 428 ASN AAA N   
3103  C CA  . ASN A 428 ? 0.576 0.914 0.589 0.016  0.004  -0.064 428 ASN AAA CA  
3104  C C   . ASN A 428 ? 0.537 0.858 0.552 0.012  0.005  -0.064 428 ASN AAA C   
3105  O O   . ASN A 428 ? 0.528 0.833 0.544 0.007  0.007  -0.067 428 ASN AAA O   
3106  C CB  . ASN A 428 ? 0.600 0.946 0.609 0.022  0.002  -0.053 428 ASN AAA CB  
3107  C CG  . ASN A 428 ? 0.554 0.881 0.558 0.022  0.002  -0.042 428 ASN AAA CG  
3108  O OD1 . ASN A 428 ? 0.536 0.846 0.540 0.019  0.003  -0.038 428 ASN AAA OD1 
3109  N ND2 . ASN A 428 ? 0.539 0.872 0.539 0.025  0.002  -0.035 428 ASN AAA ND2 
3110  N N   . GLU A 429 ? 0.500 0.827 0.515 0.016  0.004  -0.060 429 GLU AAA N   
3111  C CA  . GLU A 429 ? 0.542 0.855 0.558 0.013  0.005  -0.059 429 GLU AAA CA  
3112  C C   . GLU A 429 ? 0.521 0.817 0.533 0.014  0.005  -0.047 429 GLU AAA C   
3113  O O   . GLU A 429 ? 0.560 0.844 0.574 0.012  0.006  -0.046 429 GLU AAA O   
3114  C CB  . GLU A 429 ? 0.578 0.906 0.597 0.016  0.003  -0.063 429 GLU AAA CB  
3115  C CG  . GLU A 429 ? 0.608 0.955 0.632 0.016  0.003  -0.075 429 GLU AAA CG  
3116  C CD  . GLU A 429 ? 0.625 0.965 0.653 0.010  0.006  -0.086 429 GLU AAA CD  
3117  O OE1 . GLU A 429 ? 0.650 0.974 0.680 0.005  0.008  -0.088 429 GLU AAA OE1 
3118  O OE2 . GLU A 429 ? 0.660 1.011 0.689 0.010  0.006  -0.091 429 GLU AAA OE2 
3119  N N   . MET A 430 ? 0.491 0.786 0.499 0.016  0.004  -0.039 430 MET AAA N   
3120  C CA  . MET A 430 ? 0.523 0.804 0.529 0.017  0.004  -0.027 430 MET AAA CA  
3121  C C   . MET A 430 ? 0.536 0.804 0.539 0.015  0.005  -0.024 430 MET AAA C   
3122  O O   . MET A 430 ? 0.503 0.760 0.504 0.015  0.006  -0.015 430 MET AAA O   
3123  C CB  . MET A 430 ? 0.541 0.833 0.545 0.024  0.003  -0.018 430 MET AAA CB  
3124  C CG  . MET A 430 ? 0.619 0.928 0.621 0.028  0.002  -0.018 430 MET AAA CG  
3125  S SD  . MET A 430 ? 0.629 0.949 0.627 0.036  0.001  -0.005 430 MET AAA SD  
3126  C CE  . MET A 430 ? 0.670 1.003 0.666 0.038  0.001  -0.007 430 MET AAA CE  
3127  N N   . ASP A 431 ? 0.481 0.750 0.485 0.012  0.006  -0.031 431 ASP AAA N   
3128  C CA  . ASP A 431 ? 0.446 0.703 0.448 0.009  0.007  -0.029 431 ASP AAA CA  
3129  C C   . ASP A 431 ? 0.404 0.644 0.407 0.003  0.009  -0.035 431 ASP AAA C   
3130  O O   . ASP A 431 ? 0.378 0.612 0.381 0.001  0.011  -0.038 431 ASP AAA O   
3131  C CB  . ASP A 431 ? 0.466 0.735 0.466 0.010  0.007  -0.032 431 ASP AAA CB  
3132  C CG  . ASP A 431 ? 0.476 0.751 0.480 0.007  0.008  -0.044 431 ASP AAA CG  
3133  O OD1 . ASP A 431 ? 0.520 0.801 0.528 0.006  0.008  -0.051 431 ASP AAA OD1 
3134  O OD2 . ASP A 431 ? 0.493 0.768 0.497 0.006  0.008  -0.047 431 ASP AAA OD2 
3135  N N   . PHE A 432 ? 0.364 0.598 0.369 0.002  0.010  -0.036 432 PHE AAA N   
3136  C CA  . PHE A 432 ? 0.359 0.578 0.366 -0.003 0.013  -0.041 432 PHE AAA CA  
3137  C C   . PHE A 432 ? 0.353 0.555 0.357 -0.005 0.013  -0.036 432 PHE AAA C   
3138  O O   . PHE A 432 ? 0.363 0.555 0.367 -0.008 0.016  -0.040 432 PHE AAA O   
3139  C CB  . PHE A 432 ? 0.346 0.565 0.356 -0.003 0.013  -0.044 432 PHE AAA CB  
3140  C CG  . PHE A 432 ? 0.364 0.582 0.373 -0.000 0.011  -0.035 432 PHE AAA CG  
3141  C CD1 . PHE A 432 ? 0.376 0.578 0.384 -0.002 0.012  -0.030 432 PHE AAA CD1 
3142  C CD2 . PHE A 432 ? 0.363 0.597 0.372 0.004  0.009  -0.033 432 PHE AAA CD2 
3143  C CE1 . PHE A 432 ? 0.381 0.582 0.389 0.001  0.011  -0.023 432 PHE AAA CE1 
3144  C CE2 . PHE A 432 ? 0.361 0.592 0.369 0.007  0.008  -0.025 432 PHE AAA CE2 
3145  C CZ  . PHE A 432 ? 0.372 0.587 0.380 0.005  0.009  -0.020 432 PHE AAA CZ  
3146  N N   . ALA A 433 ? 0.354 0.551 0.356 -0.002 0.012  -0.027 433 ALA AAA N   
3147  C CA  . ALA A 433 ? 0.341 0.522 0.340 -0.004 0.013  -0.021 433 ALA AAA CA  
3148  C C   . ALA A 433 ? 0.342 0.520 0.339 -0.004 0.013  -0.020 433 ALA AAA C   
3149  O O   . ALA A 433 ? 0.341 0.529 0.337 -0.002 0.012  -0.019 433 ALA AAA O   
3150  C CB  . ALA A 433 ? 0.327 0.506 0.326 -0.001 0.011  -0.013 433 ALA AAA CB  
3151  N N   . LEU A 434 ? 0.335 0.498 0.330 -0.007 0.014  -0.020 434 LEU AAA N   
3152  C CA  . LEU A 434 ? 0.325 0.482 0.318 -0.007 0.014  -0.017 434 LEU AAA CA  
3153  C C   . LEU A 434 ? 0.312 0.470 0.304 -0.004 0.013  -0.009 434 LEU AAA C   
3154  O O   . LEU A 434 ? 0.332 0.489 0.326 -0.003 0.012  -0.005 434 LEU AAA O   
3155  C CB  . LEU A 434 ? 0.319 0.460 0.311 -0.009 0.016  -0.018 434 LEU AAA CB  
3156  C CG  . LEU A 434 ? 0.320 0.458 0.312 -0.012 0.019  -0.026 434 LEU AAA CG  
3157  C CD1 . LEU A 434 ? 0.343 0.465 0.332 -0.013 0.020  -0.025 434 LEU AAA CD1 
3158  C CD2 . LEU A 434 ? 0.313 0.461 0.305 -0.012 0.019  -0.030 434 LEU AAA CD2 
3159  N N   . PRO A 435 ? 0.278 0.437 0.269 -0.003 0.012  -0.006 435 PRO AAA N   
3160  C CA  . PRO A 435 ? 0.280 0.436 0.270 -0.001 0.012  0.002  435 PRO AAA CA  
3161  C C   . PRO A 435 ? 0.282 0.425 0.273 -0.003 0.012  0.005  435 PRO AAA C   
3162  O O   . PRO A 435 ? 0.281 0.415 0.272 -0.005 0.013  0.001  435 PRO AAA O   
3163  C CB  . PRO A 435 ? 0.269 0.426 0.258 -0.001 0.012  0.003  435 PRO AAA CB  
3164  C CG  . PRO A 435 ? 0.262 0.429 0.250 -0.002 0.012  -0.003 435 PRO AAA CG  
3165  C CD  . PRO A 435 ? 0.264 0.425 0.253 -0.004 0.013  -0.009 435 PRO AAA CD  
3166  N N   . LEU A 436 ? 0.270 0.413 0.264 -0.001 0.012  0.011  436 LEU AAA N   
3167  C CA  . LEU A 436 ? 0.265 0.396 0.260 -0.002 0.012  0.013  436 LEU AAA CA  
3168  C C   . LEU A 436 ? 0.250 0.373 0.243 -0.004 0.012  0.011  436 LEU AAA C   
3169  O O   . LEU A 436 ? 0.233 0.360 0.225 -0.003 0.012  0.012  436 LEU AAA O   
3170  C CB  . LEU A 436 ? 0.266 0.400 0.265 0.000  0.012  0.021  436 LEU AAA CB  
3171  C CG  . LEU A 436 ? 0.290 0.433 0.291 0.003  0.012  0.023  436 LEU AAA CG  
3172  C CD1 . LEU A 436 ? 0.296 0.441 0.300 0.005  0.012  0.031  436 LEU AAA CD1 
3173  C CD2 . LEU A 436 ? 0.289 0.427 0.291 0.002  0.012  0.021  436 LEU AAA CD2 
3174  N N   . ASN A 437 ? 0.242 0.354 0.234 -0.005 0.013  0.009  437 ASN AAA N   
3175  C CA  . ASN A 437 ? 0.246 0.351 0.235 -0.006 0.013  0.006  437 ASN AAA CA  
3176  C C   . ASN A 437 ? 0.243 0.345 0.234 -0.006 0.013  0.010  437 ASN AAA C   
3177  O O   . ASN A 437 ? 0.248 0.347 0.236 -0.006 0.013  0.009  437 ASN AAA O   
3178  C CB  . ASN A 437 ? 0.242 0.338 0.229 -0.008 0.014  0.002  437 ASN AAA CB  
3179  C CG  . ASN A 437 ? 0.243 0.333 0.233 -0.008 0.014  0.004  437 ASN AAA CG  
3180  O OD1 . ASN A 437 ? 0.260 0.353 0.253 -0.007 0.014  0.007  437 ASN AAA OD1 
3181  N ND2 . ASN A 437 ? 0.255 0.336 0.242 -0.008 0.015  0.001  437 ASN AAA ND2 
3182  N N   . CYS A 438 ? 0.247 0.349 0.241 -0.005 0.013  0.015  438 CYS AAA N   
3183  C CA  . CYS A 438 ? 0.256 0.354 0.254 -0.005 0.013  0.017  438 CYS AAA CA  
3184  C C   . CYS A 438 ? 0.250 0.355 0.251 -0.003 0.013  0.023  438 CYS AAA C   
3185  O O   . CYS A 438 ? 0.235 0.346 0.238 -0.002 0.013  0.026  438 CYS AAA O   
3186  C CB  . CYS A 438 ? 0.271 0.363 0.272 -0.005 0.013  0.018  438 CYS AAA CB  
3187  S SG  . CYS A 438 ? 0.282 0.365 0.279 -0.006 0.013  0.012  438 CYS AAA SG  
3188  N N   . LEU A 439 ? 0.255 0.357 0.257 -0.004 0.013  0.024  439 LEU AAA N   
3189  C CA  . LEU A 439 ? 0.278 0.384 0.284 -0.003 0.014  0.029  439 LEU AAA CA  
3190  C C   . LEU A 439 ? 0.267 0.367 0.277 -0.003 0.014  0.029  439 LEU AAA C   
3191  O O   . LEU A 439 ? 0.252 0.350 0.259 -0.004 0.014  0.025  439 LEU AAA O   
3192  C CB  . LEU A 439 ? 0.292 0.406 0.295 -0.002 0.014  0.030  439 LEU AAA CB  
3193  C CG  . LEU A 439 ? 0.320 0.439 0.328 -0.000 0.015  0.035  439 LEU AAA CG  
3194  C CD1 . LEU A 439 ? 0.336 0.460 0.347 0.001  0.016  0.041  439 LEU AAA CD1 
3195  C CD2 . LEU A 439 ? 0.323 0.448 0.328 0.000  0.015  0.036  439 LEU AAA CD2 
3196  N N   . ALA A 440 ? 0.263 0.362 0.279 -0.003 0.016  0.032  440 ALA AAA N   
3197  C CA  . ALA A 440 ? 0.270 0.364 0.292 -0.004 0.016  0.032  440 ALA AAA CA  
3198  C C   . ALA A 440 ? 0.261 0.359 0.288 -0.003 0.018  0.037  440 ALA AAA C   
3199  O O   . ALA A 440 ? 0.260 0.362 0.289 -0.002 0.020  0.042  440 ALA AAA O   
3200  C CB  . ALA A 440 ? 0.265 0.354 0.292 -0.005 0.017  0.031  440 ALA AAA CB  
3201  N N   . LYS A 441 ? 0.258 0.356 0.287 -0.004 0.019  0.036  441 LYS AAA N   
3202  C CA  . LYS A 441 ? 0.274 0.375 0.309 -0.004 0.021  0.040  441 LYS AAA CA  
3203  C C   . LYS A 441 ? 0.272 0.369 0.312 -0.005 0.022  0.037  441 LYS AAA C   
3204  O O   . LYS A 441 ? 0.278 0.374 0.314 -0.006 0.020  0.032  441 LYS AAA O   
3205  C CB  . LYS A 441 ? 0.284 0.392 0.313 -0.003 0.021  0.042  441 LYS AAA CB  
3206  C CG  . LYS A 441 ? 0.286 0.398 0.320 -0.002 0.023  0.046  441 LYS AAA CG  
3207  C CD  . LYS A 441 ? 0.291 0.411 0.321 -0.000 0.023  0.049  441 LYS AAA CD  
3208  C CE  . LYS A 441 ? 0.282 0.404 0.304 -0.001 0.021  0.045  441 LYS AAA CE  
3209  N NZ  . LYS A 441 ? 0.294 0.425 0.313 0.001  0.021  0.048  441 LYS AAA NZ  
3210  N N   . LEU A 442 ? 0.275 0.372 0.325 -0.006 0.025  0.041  442 LEU AAA N   
3211  C CA  . LEU A 442 ? 0.280 0.376 0.338 -0.007 0.026  0.039  442 LEU AAA CA  
3212  C C   . LEU A 442 ? 0.283 0.383 0.344 -0.006 0.029  0.045  442 LEU AAA C   
3213  O O   . LEU A 442 ? 0.274 0.377 0.337 -0.005 0.032  0.051  442 LEU AAA O   
3214  C CB  . LEU A 442 ? 0.287 0.377 0.355 -0.008 0.028  0.039  442 LEU AAA CB  
3215  C CG  . LEU A 442 ? 0.296 0.382 0.361 -0.009 0.026  0.033  442 LEU AAA CG  
3216  C CD1 . LEU A 442 ? 0.316 0.398 0.392 -0.010 0.028  0.033  442 LEU AAA CD1 
3217  C CD2 . LEU A 442 ? 0.289 0.374 0.351 -0.009 0.023  0.026  442 LEU AAA CD2 
3218  N N   . VAL A 443 ? 0.300 0.401 0.363 -0.007 0.029  0.042  443 VAL AAA N   
3219  C CA  . VAL A 443 ? 0.312 0.417 0.379 -0.007 0.032  0.046  443 VAL AAA CA  
3220  C C   . VAL A 443 ? 0.320 0.422 0.399 -0.009 0.035  0.044  443 VAL AAA C   
3221  O O   . VAL A 443 ? 0.308 0.408 0.387 -0.011 0.033  0.036  443 VAL AAA O   
3222  C CB  . VAL A 443 ? 0.308 0.418 0.366 -0.007 0.030  0.044  443 VAL AAA CB  
3223  C CG1 . VAL A 443 ? 0.308 0.423 0.371 -0.006 0.033  0.049  443 VAL AAA CG1 
3224  C CG2 . VAL A 443 ? 0.301 0.413 0.349 -0.005 0.027  0.044  443 VAL AAA CG2 
3225  N N   . VAL A 444 ? 0.344 0.445 0.432 -0.009 0.040  0.049  444 VAL AAA N   
3226  C CA  . VAL A 444 ? 0.345 0.443 0.447 -0.011 0.043  0.047  444 VAL AAA CA  
3227  C C   . VAL A 444 ? 0.345 0.445 0.454 -0.011 0.048  0.052  444 VAL AAA C   
3228  O O   . VAL A 444 ? 0.312 0.416 0.417 -0.009 0.050  0.060  444 VAL AAA O   
3229  C CB  . VAL A 444 ? 0.345 0.438 0.454 -0.012 0.045  0.049  444 VAL AAA CB  
3230  C CG1 . VAL A 444 ? 0.348 0.439 0.449 -0.011 0.041  0.044  444 VAL AAA CG1 
3231  C CG2 . VAL A 444 ? 0.361 0.454 0.473 -0.010 0.049  0.058  444 VAL AAA CG2 
3232  N N   . VAL A 445 ? 0.351 0.451 0.471 -0.014 0.051  0.048  445 VAL AAA N   
3233  C CA  . VAL A 445 ? 0.386 0.486 0.515 -0.015 0.056  0.052  445 VAL AAA CA  
3234  C C   . VAL A 445 ? 0.408 0.503 0.551 -0.015 0.062  0.055  445 VAL AAA C   
3235  O O   . VAL A 445 ? 0.421 0.512 0.572 -0.018 0.062  0.049  445 VAL AAA O   
3236  C CB  . VAL A 445 ? 0.382 0.484 0.515 -0.017 0.056  0.044  445 VAL AAA CB  
3237  C CG1 . VAL A 445 ? 0.387 0.491 0.531 -0.018 0.062  0.048  445 VAL AAA CG1 
3238  C CG2 . VAL A 445 ? 0.374 0.481 0.493 -0.016 0.050  0.041  445 VAL AAA CG2 
3239  N N   . LYS A 446 ? 0.439 0.535 0.585 -0.014 0.067  0.065  446 LYS AAA N   
3240  C CA  . LYS A 446 ? 0.480 0.571 0.639 -0.014 0.073  0.070  446 LYS AAA CA  
3241  C C   . LYS A 446 ? 0.451 0.539 0.626 -0.017 0.078  0.066  446 LYS AAA C   
3242  O O   . LYS A 446 ? 0.442 0.525 0.628 -0.019 0.080  0.062  446 LYS AAA O   
3243  C CB  . LYS A 446 ? 0.506 0.599 0.663 -0.010 0.078  0.082  446 LYS AAA CB  
3244  C CG  . LYS A 446 ? 0.519 0.616 0.661 -0.007 0.073  0.086  446 LYS AAA CG  
3245  C CD  . LYS A 446 ? 0.568 0.663 0.712 -0.003 0.077  0.096  446 LYS AAA CD  
3246  C CE  . LYS A 446 ? 0.587 0.688 0.730 0.000  0.082  0.106  446 LYS AAA CE  
3247  N NZ  . LYS A 446 ? 0.628 0.730 0.769 0.004  0.084  0.115  446 LYS AAA NZ  
3248  N N   . SER A 447 ? 0.460 0.552 0.636 -0.018 0.079  0.064  447 SER AAA N   
3249  C CA  . SER A 447 ? 0.484 0.575 0.677 -0.022 0.085  0.060  447 SER AAA CA  
3250  C C   . SER A 447 ? 0.490 0.580 0.687 -0.025 0.081  0.047  447 SER AAA C   
3251  O O   . SER A 447 ? 0.511 0.601 0.721 -0.028 0.084  0.041  447 SER AAA O   
3252  C CB  . SER A 447 ? 0.462 0.557 0.654 -0.022 0.087  0.061  447 SER AAA CB  
3253  O OG  . SER A 447 ? 0.456 0.557 0.636 -0.022 0.080  0.056  447 SER AAA OG  
3254  N N   . GLN A 448 ? 0.499 0.589 0.686 -0.024 0.074  0.042  448 GLN AAA N   
3255  C CA  . GLN A 448 ? 0.510 0.599 0.700 -0.026 0.070  0.030  448 GLN AAA CA  
3256  C C   . GLN A 448 ? 0.485 0.570 0.674 -0.026 0.068  0.030  448 GLN AAA C   
3257  O O   . GLN A 448 ? 0.435 0.521 0.618 -0.026 0.063  0.022  448 GLN AAA O   
3258  C CB  . GLN A 448 ? 0.512 0.607 0.689 -0.025 0.064  0.024  448 GLN AAA CB  
3259  C CG  . GLN A 448 ? 0.538 0.637 0.717 -0.026 0.065  0.024  448 GLN AAA CG  
3260  C CD  . GLN A 448 ? 0.573 0.677 0.740 -0.025 0.059  0.018  448 GLN AAA CD  
3261  O OE1 . GLN A 448 ? 0.645 0.749 0.808 -0.025 0.054  0.010  448 GLN AAA OE1 
3262  N NE2 . GLN A 448 ? 0.585 0.693 0.744 -0.024 0.059  0.023  448 GLN AAA NE2 
3263  N N   . GLY A 449 ? 0.453 0.534 0.650 -0.025 0.073  0.037  449 GLY AAA N   
3264  C CA  . GLY A 449 ? 0.472 0.548 0.669 -0.024 0.072  0.038  449 GLY AAA CA  
3265  C C   . GLY A 449 ? 0.462 0.539 0.641 -0.022 0.066  0.038  449 GLY AAA C   
3266  O O   . GLY A 449 ? 0.461 0.537 0.638 -0.022 0.062  0.033  449 GLY AAA O   
3267  N N   . GLU A 450 ? 0.454 0.535 0.621 -0.019 0.064  0.045  450 GLU AAA N   
3268  C CA  . GLU A 450 ? 0.431 0.514 0.581 -0.017 0.058  0.046  450 GLU AAA CA  
3269  C C   . GLU A 450 ? 0.406 0.491 0.550 -0.018 0.052  0.036  450 GLU AAA C   
3270  O O   . GLU A 450 ? 0.355 0.439 0.492 -0.017 0.048  0.033  450 GLU AAA O   
3271  C CB  . GLU A 450 ? 0.436 0.517 0.585 -0.015 0.058  0.051  450 GLU AAA CB  
3272  C CG  . GLU A 450 ? 0.460 0.541 0.612 -0.013 0.064  0.062  450 GLU AAA CG  
3273  C CD  . GLU A 450 ? 0.479 0.559 0.624 -0.010 0.062  0.068  450 GLU AAA CD  
3274  O OE1 . GLU A 450 ? 0.504 0.580 0.652 -0.011 0.062  0.065  450 GLU AAA OE1 
3275  O OE2 . GLU A 450 ? 0.509 0.593 0.646 -0.007 0.062  0.074  450 GLU AAA OE2 
3276  N N   . LYS A 451 ? 0.402 0.489 0.548 -0.019 0.052  0.030  451 LYS AAA N   
3277  C CA  . LYS A 451 ? 0.386 0.476 0.524 -0.020 0.046  0.021  451 LYS AAA CA  
3278  C C   . LYS A 451 ? 0.349 0.441 0.471 -0.017 0.041  0.024  451 LYS AAA C   
3279  O O   . LYS A 451 ? 0.305 0.399 0.422 -0.016 0.043  0.030  451 LYS AAA O   
3280  C CB  . LYS A 451 ? 0.425 0.518 0.568 -0.021 0.046  0.015  451 LYS AAA CB  
3281  C CG  . LYS A 451 ? 0.455 0.551 0.592 -0.021 0.041  0.006  451 LYS AAA CG  
3282  C CD  . LYS A 451 ? 0.497 0.598 0.636 -0.021 0.041  0.001  451 LYS AAA CD  
3283  C CE  . LYS A 451 ? 0.507 0.611 0.646 -0.021 0.037  -0.010 451 LYS AAA CE  
3284  N NZ  . LYS A 451 ? 0.516 0.626 0.651 -0.021 0.035  -0.013 451 LYS AAA NZ  
3285  N N   . VAL A 452 ? 0.331 0.421 0.444 -0.016 0.037  0.019  452 VAL AAA N   
3286  C CA  . VAL A 452 ? 0.321 0.413 0.419 -0.014 0.033  0.020  452 VAL AAA CA  
3287  C C   . VAL A 452 ? 0.304 0.400 0.396 -0.014 0.030  0.016  452 VAL AAA C   
3288  O O   . VAL A 452 ? 0.271 0.367 0.365 -0.015 0.029  0.009  452 VAL AAA O   
3289  C CB  . VAL A 452 ? 0.311 0.399 0.402 -0.014 0.029  0.017  452 VAL AAA CB  
3290  C CG1 . VAL A 452 ? 0.310 0.400 0.387 -0.012 0.026  0.018  452 VAL AAA CG1 
3291  C CG2 . VAL A 452 ? 0.329 0.414 0.427 -0.014 0.031  0.021  452 VAL AAA CG2 
3292  N N   . VAL A 453 ? 0.310 0.409 0.396 -0.013 0.031  0.021  453 VAL AAA N   
3293  C CA  . VAL A 453 ? 0.329 0.432 0.410 -0.013 0.029  0.018  453 VAL AAA CA  
3294  C C   . VAL A 453 ? 0.313 0.417 0.380 -0.011 0.025  0.019  453 VAL AAA C   
3295  O O   . VAL A 453 ? 0.327 0.433 0.388 -0.010 0.023  0.015  453 VAL AAA O   
3296  C CB  . VAL A 453 ? 0.347 0.454 0.433 -0.013 0.032  0.022  453 VAL AAA CB  
3297  C CG1 . VAL A 453 ? 0.341 0.447 0.443 -0.016 0.036  0.020  453 VAL AAA CG1 
3298  C CG2 . VAL A 453 ? 0.354 0.462 0.438 -0.012 0.034  0.031  453 VAL AAA CG2 
3299  N N   . GLY A 454 ? 0.299 0.401 0.362 -0.010 0.025  0.023  454 GLY AAA N   
3300  C CA  . GLY A 454 ? 0.281 0.384 0.332 -0.009 0.022  0.023  454 GLY AAA CA  
3301  C C   . GLY A 454 ? 0.275 0.373 0.323 -0.008 0.021  0.023  454 GLY AAA C   
3302  O O   . GLY A 454 ? 0.269 0.366 0.323 -0.008 0.023  0.028  454 GLY AAA O   
3303  N N   . PHE A 455 ? 0.258 0.354 0.299 -0.008 0.018  0.019  455 PHE AAA N   
3304  C CA  . PHE A 455 ? 0.248 0.340 0.285 -0.007 0.017  0.018  455 PHE AAA CA  
3305  C C   . PHE A 455 ? 0.243 0.336 0.269 -0.006 0.015  0.018  455 PHE AAA C   
3306  O O   . PHE A 455 ? 0.243 0.337 0.264 -0.005 0.014  0.015  455 PHE AAA O   
3307  C CB  . PHE A 455 ? 0.245 0.333 0.284 -0.007 0.016  0.013  455 PHE AAA CB  
3308  C CG  . PHE A 455 ? 0.247 0.331 0.281 -0.007 0.014  0.011  455 PHE AAA CG  
3309  C CD1 . PHE A 455 ? 0.249 0.332 0.273 -0.006 0.013  0.009  455 PHE AAA CD1 
3310  C CD2 . PHE A 455 ? 0.255 0.337 0.295 -0.007 0.015  0.012  455 PHE AAA CD2 
3311  C CE1 . PHE A 455 ? 0.245 0.324 0.264 -0.005 0.012  0.008  455 PHE AAA CE1 
3312  C CE2 . PHE A 455 ? 0.262 0.340 0.296 -0.007 0.014  0.011  455 PHE AAA CE2 
3313  C CZ  . PHE A 455 ? 0.257 0.334 0.281 -0.006 0.012  0.009  455 PHE AAA CZ  
3314  N N   . HIS A 456 ? 0.229 0.323 0.253 -0.006 0.015  0.021  456 HIS AAA N   
3315  C CA  . HIS A 456 ? 0.213 0.308 0.228 -0.005 0.014  0.021  456 HIS AAA CA  
3316  C C   . HIS A 456 ? 0.210 0.302 0.222 -0.005 0.014  0.020  456 HIS AAA C   
3317  O O   . HIS A 456 ? 0.223 0.315 0.240 -0.005 0.015  0.024  456 HIS AAA O   
3318  C CB  . HIS A 456 ? 0.216 0.318 0.231 -0.005 0.015  0.025  456 HIS AAA CB  
3319  C CG  . HIS A 456 ? 0.215 0.321 0.233 -0.005 0.016  0.026  456 HIS AAA CG  
3320  N ND1 . HIS A 456 ? 0.222 0.329 0.234 -0.004 0.014  0.023  456 HIS AAA ND1 
3321  C CD2 . HIS A 456 ? 0.221 0.327 0.246 -0.005 0.018  0.028  456 HIS AAA CD2 
3322  C CE1 . HIS A 456 ? 0.224 0.334 0.239 -0.004 0.015  0.024  456 HIS AAA CE1 
3323  N NE2 . HIS A 456 ? 0.229 0.338 0.252 -0.005 0.017  0.027  456 HIS AAA NE2 
3324  N N   . PHE A 457 ? 0.197 0.286 0.202 -0.005 0.012  0.017  457 PHE AAA N   
3325  C CA  . PHE A 457 ? 0.195 0.282 0.199 -0.005 0.012  0.016  457 PHE AAA CA  
3326  C C   . PHE A 457 ? 0.206 0.293 0.202 -0.004 0.012  0.014  457 PHE AAA C   
3327  O O   . PHE A 457 ? 0.232 0.316 0.224 -0.004 0.011  0.011  457 PHE AAA O   
3328  C CB  . PHE A 457 ? 0.190 0.270 0.195 -0.005 0.012  0.013  457 PHE AAA CB  
3329  C CG  . PHE A 457 ? 0.182 0.260 0.185 -0.005 0.012  0.013  457 PHE AAA CG  
3330  C CD1 . PHE A 457 ? 0.179 0.258 0.187 -0.006 0.012  0.016  457 PHE AAA CD1 
3331  C CD2 . PHE A 457 ? 0.175 0.249 0.171 -0.005 0.011  0.010  457 PHE AAA CD2 
3332  C CE1 . PHE A 457 ? 0.174 0.251 0.180 -0.006 0.012  0.015  457 PHE AAA CE1 
3333  C CE2 . PHE A 457 ? 0.173 0.246 0.168 -0.005 0.012  0.009  457 PHE AAA CE2 
3334  C CZ  . PHE A 457 ? 0.172 0.246 0.171 -0.006 0.012  0.012  457 PHE AAA CZ  
3335  N N   . VAL A 458 ? 0.212 0.304 0.208 -0.005 0.012  0.016  458 VAL AAA N   
3336  C CA  . VAL A 458 ? 0.216 0.308 0.206 -0.005 0.012  0.013  458 VAL AAA CA  
3337  C C   . VAL A 458 ? 0.213 0.301 0.203 -0.005 0.012  0.012  458 VAL AAA C   
3338  O O   . VAL A 458 ? 0.216 0.306 0.210 -0.005 0.012  0.015  458 VAL AAA O   
3339  C CB  . VAL A 458 ? 0.224 0.326 0.214 -0.004 0.012  0.015  458 VAL AAA CB  
3340  C CG1 . VAL A 458 ? 0.224 0.328 0.210 -0.004 0.012  0.012  458 VAL AAA CG1 
3341  C CG2 . VAL A 458 ? 0.232 0.338 0.222 -0.004 0.012  0.017  458 VAL AAA CG2 
3342  N N   . GLY A 459 ? 0.217 0.301 0.203 -0.005 0.012  0.008  459 GLY AAA N   
3343  C CA  . GLY A 459 ? 0.226 0.306 0.211 -0.006 0.013  0.006  459 GLY AAA CA  
3344  C C   . GLY A 459 ? 0.235 0.307 0.216 -0.006 0.014  0.003  459 GLY AAA C   
3345  O O   . GLY A 459 ? 0.250 0.321 0.229 -0.005 0.014  0.002  459 GLY AAA O   
3346  N N   . PRO A 460 ? 0.239 0.306 0.220 -0.006 0.014  0.001  460 PRO AAA N   
3347  C CA  . PRO A 460 ? 0.245 0.305 0.222 -0.005 0.016  -0.001 460 PRO AAA CA  
3348  C C   . PRO A 460 ? 0.231 0.288 0.208 -0.004 0.015  -0.001 460 PRO AAA C   
3349  O O   . PRO A 460 ? 0.227 0.285 0.208 -0.004 0.013  0.001  460 PRO AAA O   
3350  C CB  . PRO A 460 ? 0.249 0.305 0.226 -0.006 0.017  -0.002 460 PRO AAA CB  
3351  C CG  . PRO A 460 ? 0.256 0.319 0.236 -0.007 0.016  -0.001 460 PRO AAA CG  
3352  C CD  . PRO A 460 ? 0.246 0.315 0.230 -0.007 0.014  0.002  460 PRO AAA CD  
3353  N N   . ASN A 461 ? 0.232 0.284 0.204 -0.002 0.015  -0.003 461 ASN AAA N   
3354  C CA  . ASN A 461 ? 0.241 0.291 0.213 -0.000 0.015  -0.004 461 ASN AAA CA  
3355  C C   . ASN A 461 ? 0.232 0.286 0.208 -0.000 0.013  -0.002 461 ASN AAA C   
3356  O O   . ASN A 461 ? 0.227 0.282 0.207 -0.000 0.012  -0.003 461 ASN AAA O   
3357  C CB  . ASN A 461 ? 0.245 0.290 0.217 -0.000 0.015  -0.004 461 ASN AAA CB  
3358  C CG  . ASN A 461 ? 0.257 0.299 0.227 -0.001 0.017  -0.005 461 ASN AAA CG  
3359  O OD1 . ASN A 461 ? 0.261 0.299 0.225 0.001  0.019  -0.007 461 ASN AAA OD1 
3360  N ND2 . ASN A 461 ? 0.241 0.284 0.215 -0.002 0.017  -0.004 461 ASN AAA ND2 
3361  N N   . ALA A 462 ? 0.221 0.279 0.197 -0.001 0.013  -0.001 462 ALA AAA N   
3362  C CA  . ALA A 462 ? 0.227 0.290 0.207 -0.001 0.011  0.000  462 ALA AAA CA  
3363  C C   . ALA A 462 ? 0.225 0.288 0.206 0.000  0.010  -0.002 462 ALA AAA C   
3364  O O   . ALA A 462 ? 0.212 0.277 0.198 0.000  0.010  -0.001 462 ALA AAA O   
3365  C CB  . ALA A 462 ? 0.229 0.298 0.209 -0.002 0.011  0.002  462 ALA AAA CB  
3366  N N   . GLY A 463 ? 0.244 0.304 0.218 0.003  0.011  -0.004 463 GLY AAA N   
3367  C CA  . GLY A 463 ? 0.271 0.330 0.244 0.005  0.010  -0.006 463 GLY AAA CA  
3368  C C   . GLY A 463 ? 0.289 0.347 0.265 0.006  0.009  -0.008 463 GLY AAA C   
3369  O O   . GLY A 463 ? 0.297 0.358 0.277 0.006  0.008  -0.009 463 GLY AAA O   
3370  N N   . GLU A 464 ? 0.317 0.371 0.290 0.006  0.010  -0.007 464 GLU AAA N   
3371  C CA  . GLU A 464 ? 0.327 0.379 0.303 0.006  0.010  -0.009 464 GLU AAA CA  
3372  C C   . GLU A 464 ? 0.301 0.357 0.286 0.004  0.009  -0.008 464 GLU AAA C   
3373  O O   . GLU A 464 ? 0.324 0.382 0.314 0.005  0.008  -0.011 464 GLU AAA O   
3374  C CB  . GLU A 464 ? 0.361 0.408 0.334 0.006  0.011  -0.009 464 GLU AAA CB  
3375  C CG  . GLU A 464 ? 0.392 0.435 0.356 0.009  0.013  -0.009 464 GLU AAA CG  
3376  C CD  . GLU A 464 ? 0.423 0.465 0.382 0.013  0.013  -0.011 464 GLU AAA CD  
3377  O OE1 . GLU A 464 ? 0.458 0.503 0.420 0.014  0.011  -0.013 464 GLU AAA OE1 
3378  O OE2 . GLU A 464 ? 0.440 0.477 0.392 0.015  0.015  -0.011 464 GLU AAA OE2 
3379  N N   . ILE A 465 ? 0.271 0.329 0.260 0.001  0.009  -0.005 465 ILE AAA N   
3380  C CA  . ILE A 465 ? 0.256 0.317 0.254 -0.001 0.009  -0.003 465 ILE AAA CA  
3381  C C   . ILE A 465 ? 0.274 0.339 0.277 -0.001 0.009  -0.004 465 ILE AAA C   
3382  O O   . ILE A 465 ? 0.273 0.340 0.284 -0.001 0.009  -0.005 465 ILE AAA O   
3383  C CB  . ILE A 465 ? 0.254 0.316 0.253 -0.002 0.010  0.001  465 ILE AAA CB  
3384  C CG1 . ILE A 465 ? 0.253 0.311 0.249 -0.003 0.010  0.000  465 ILE AAA CG1 
3385  C CG2 . ILE A 465 ? 0.257 0.322 0.265 -0.004 0.010  0.003  465 ILE AAA CG2 
3386  C CD1 . ILE A 465 ? 0.253 0.312 0.249 -0.004 0.011  0.003  465 ILE AAA CD1 
3387  N N   . THR A 466 ? 0.275 0.341 0.273 0.000  0.008  -0.004 466 THR AAA N   
3388  C CA  . THR A 466 ? 0.269 0.340 0.272 -0.000 0.008  -0.004 466 THR AAA CA  
3389  C C   . THR A 466 ? 0.263 0.335 0.268 0.001  0.007  -0.008 466 THR AAA C   
3390  O O   . THR A 466 ? 0.255 0.331 0.267 0.001  0.007  -0.009 466 THR AAA O   
3391  C CB  . THR A 466 ? 0.269 0.342 0.267 0.000  0.008  -0.002 466 THR AAA CB  
3392  O OG1 . THR A 466 ? 0.267 0.341 0.266 -0.002 0.009  0.002  466 THR AAA OG1 
3393  C CG2 . THR A 466 ? 0.253 0.331 0.255 -0.000 0.008  -0.003 466 THR AAA CG2 
3394  N N   . GLN A 467 ? 0.271 0.341 0.269 0.004  0.006  -0.011 467 GLN AAA N   
3395  C CA  . GLN A 467 ? 0.258 0.330 0.256 0.006  0.005  -0.016 467 GLN AAA CA  
3396  C C   . GLN A 467 ? 0.253 0.328 0.262 0.005  0.005  -0.018 467 GLN AAA C   
3397  O O   . GLN A 467 ? 0.282 0.362 0.297 0.005  0.005  -0.020 467 GLN AAA O   
3398  C CB  . GLN A 467 ? 0.277 0.346 0.267 0.010  0.005  -0.018 467 GLN AAA CB  
3399  C CG  . GLN A 467 ? 0.273 0.346 0.262 0.013  0.004  -0.023 467 GLN AAA CG  
3400  C CD  . GLN A 467 ? 0.283 0.359 0.269 0.015  0.003  -0.023 467 GLN AAA CD  
3401  O OE1 . GLN A 467 ? 0.291 0.364 0.268 0.017  0.004  -0.022 467 GLN AAA OE1 
3402  N NE2 . GLN A 467 ? 0.281 0.361 0.273 0.013  0.003  -0.025 467 GLN AAA NE2 
3403  N N   . GLY A 468 ? 0.234 0.307 0.246 0.004  0.005  -0.018 468 GLY AAA N   
3404  C CA  . GLY A 468 ? 0.226 0.301 0.248 0.003  0.006  -0.021 468 GLY AAA CA  
3405  C C   . GLY A 468 ? 0.217 0.294 0.249 -0.000 0.007  -0.018 468 GLY AAA C   
3406  O O   . GLY A 468 ? 0.213 0.294 0.255 -0.001 0.007  -0.022 468 GLY AAA O   
3407  N N   . PHE A 469 ? 0.213 0.288 0.244 -0.002 0.008  -0.013 469 PHE AAA N   
3408  C CA  . PHE A 469 ? 0.210 0.287 0.249 -0.004 0.010  -0.009 469 PHE AAA CA  
3409  C C   . PHE A 469 ? 0.221 0.302 0.261 -0.004 0.010  -0.011 469 PHE AAA C   
3410  O O   . PHE A 469 ? 0.241 0.325 0.292 -0.006 0.012  -0.011 469 PHE AAA O   
3411  C CB  . PHE A 469 ? 0.210 0.286 0.246 -0.005 0.011  -0.003 469 PHE AAA CB  
3412  C CG  . PHE A 469 ? 0.213 0.285 0.252 -0.006 0.012  -0.001 469 PHE AAA CG  
3413  C CD1 . PHE A 469 ? 0.212 0.285 0.263 -0.008 0.014  -0.001 469 PHE AAA CD1 
3414  C CD2 . PHE A 469 ? 0.217 0.287 0.250 -0.006 0.011  0.000  469 PHE AAA CD2 
3415  C CE1 . PHE A 469 ? 0.225 0.294 0.278 -0.008 0.014  0.001  469 PHE AAA CE1 
3416  C CE2 . PHE A 469 ? 0.219 0.286 0.254 -0.006 0.012  0.002  469 PHE AAA CE2 
3417  C CZ  . PHE A 469 ? 0.220 0.288 0.266 -0.008 0.013  0.002  469 PHE AAA CZ  
3418  N N   . SER A 470 ? 0.221 0.303 0.253 -0.002 0.009  -0.012 470 SER AAA N   
3419  C CA  . SER A 470 ? 0.235 0.321 0.267 -0.002 0.008  -0.014 470 SER AAA CA  
3420  C C   . SER A 470 ? 0.251 0.341 0.291 -0.001 0.008  -0.020 470 SER AAA C   
3421  O O   . SER A 470 ? 0.253 0.347 0.301 -0.003 0.009  -0.020 470 SER AAA O   
3422  C CB  . SER A 470 ? 0.236 0.322 0.257 0.001  0.007  -0.015 470 SER AAA CB  
3423  O OG  . SER A 470 ? 0.234 0.320 0.251 0.004  0.005  -0.019 470 SER AAA OG  
3424  N N   . LEU A 471 ? 0.276 0.366 0.316 0.000  0.007  -0.024 471 LEU AAA N   
3425  C CA  . LEU A 471 ? 0.285 0.379 0.333 0.001  0.006  -0.031 471 LEU AAA CA  
3426  C C   . LEU A 471 ? 0.306 0.401 0.368 -0.003 0.009  -0.030 471 LEU AAA C   
3427  O O   . LEU A 471 ? 0.305 0.404 0.376 -0.004 0.010  -0.034 471 LEU AAA O   
3428  C CB  . LEU A 471 ? 0.286 0.380 0.330 0.003  0.004  -0.035 471 LEU AAA CB  
3429  C CG  . LEU A 471 ? 0.286 0.385 0.338 0.004  0.004  -0.043 471 LEU AAA CG  
3430  C CD1 . LEU A 471 ? 0.291 0.397 0.345 0.005  0.003  -0.047 471 LEU AAA CD1 
3431  C CD2 . LEU A 471 ? 0.289 0.389 0.336 0.007  0.002  -0.046 471 LEU AAA CD2 
3432  N N   . ALA A 472 ? 0.310 0.400 0.373 -0.005 0.010  -0.026 472 ALA AAA N   
3433  C CA  . ALA A 472 ? 0.312 0.401 0.389 -0.008 0.013  -0.025 472 ALA AAA CA  
3434  C C   . ALA A 472 ? 0.311 0.402 0.393 -0.009 0.015  -0.021 472 ALA AAA C   
3435  O O   . ALA A 472 ? 0.301 0.394 0.395 -0.011 0.018  -0.023 472 ALA AAA O   
3436  C CB  . ALA A 472 ? 0.302 0.386 0.378 -0.008 0.014  -0.019 472 ALA AAA CB  
3437  N N   . VAL A 473 ? 0.307 0.397 0.379 -0.009 0.015  -0.016 473 VAL AAA N   
3438  C CA  . VAL A 473 ? 0.326 0.418 0.403 -0.010 0.017  -0.012 473 VAL AAA CA  
3439  C C   . VAL A 473 ? 0.331 0.428 0.412 -0.010 0.017  -0.017 473 VAL AAA C   
3440  O O   . VAL A 473 ? 0.321 0.420 0.413 -0.012 0.020  -0.017 473 VAL AAA O   
3441  C CB  . VAL A 473 ? 0.333 0.424 0.399 -0.009 0.017  -0.006 473 VAL AAA CB  
3442  C CG1 . VAL A 473 ? 0.347 0.442 0.416 -0.010 0.019  -0.002 473 VAL AAA CG1 
3443  C CG2 . VAL A 473 ? 0.322 0.410 0.387 -0.010 0.018  0.000  473 VAL AAA CG2 
3444  N N   . LYS A 474 ? 0.334 0.433 0.408 -0.008 0.014  -0.023 474 LYS AAA N   
3445  C CA  . LYS A 474 ? 0.354 0.460 0.433 -0.007 0.013  -0.029 474 LYS AAA CA  
3446  C C   . LYS A 474 ? 0.384 0.492 0.476 -0.009 0.015  -0.035 474 LYS AAA C   
3447  O O   . LYS A 474 ? 0.329 0.442 0.430 -0.010 0.016  -0.038 474 LYS AAA O   
3448  C CB  . LYS A 474 ? 0.378 0.485 0.445 -0.004 0.010  -0.033 474 LYS AAA CB  
3449  C CG  . LYS A 474 ? 0.410 0.524 0.479 -0.002 0.008  -0.040 474 LYS AAA CG  
3450  C CD  . LYS A 474 ? 0.411 0.527 0.468 0.002  0.005  -0.043 474 LYS AAA CD  
3451  C CE  . LYS A 474 ? 0.380 0.502 0.436 0.004  0.004  -0.048 474 LYS AAA CE  
3452  N NZ  . LYS A 474 ? 0.385 0.509 0.432 0.009  0.001  -0.053 474 LYS AAA NZ  
3453  N N   . LEU A 475 ? 0.398 0.503 0.494 -0.009 0.015  -0.036 475 LEU AAA N   
3454  C CA  . LEU A 475 ? 0.414 0.523 0.526 -0.011 0.017  -0.043 475 LEU AAA CA  
3455  C C   . LEU A 475 ? 0.404 0.510 0.528 -0.015 0.022  -0.038 475 LEU AAA C   
3456  O O   . LEU A 475 ? 0.417 0.524 0.555 -0.017 0.024  -0.043 475 LEU AAA O   
3457  C CB  . LEU A 475 ? 0.435 0.542 0.545 -0.010 0.015  -0.046 475 LEU AAA CB  
3458  C CG  . LEU A 475 ? 0.452 0.562 0.552 -0.006 0.011  -0.052 475 LEU AAA CG  
3459  C CD1 . LEU A 475 ? 0.444 0.553 0.542 -0.005 0.010  -0.054 475 LEU AAA CD1 
3460  C CD2 . LEU A 475 ? 0.446 0.565 0.553 -0.005 0.010  -0.061 475 LEU AAA CD2 
3461  N N   . GLY A 476 ? 0.381 0.483 0.502 -0.016 0.023  -0.029 476 GLY AAA N   
3462  C CA  . GLY A 476 ? 0.365 0.465 0.496 -0.018 0.028  -0.024 476 GLY AAA CA  
3463  C C   . GLY A 476 ? 0.353 0.448 0.487 -0.019 0.031  -0.018 476 GLY AAA C   
3464  O O   . GLY A 476 ? 0.354 0.446 0.500 -0.021 0.035  -0.015 476 GLY AAA O   
3465  N N   . ALA A 477 ? 0.337 0.429 0.460 -0.017 0.028  -0.015 477 ALA AAA N   
3466  C CA  . ALA A 477 ? 0.331 0.417 0.455 -0.018 0.029  -0.009 477 ALA AAA CA  
3467  C C   . ALA A 477 ? 0.318 0.403 0.445 -0.018 0.033  -0.000 477 ALA AAA C   
3468  O O   . ALA A 477 ? 0.351 0.438 0.472 -0.018 0.033  0.004  477 ALA AAA O   
3469  C CB  . ALA A 477 ? 0.333 0.417 0.442 -0.015 0.025  -0.008 477 ALA AAA CB  
3470  N N   . THR A 478 ? 0.303 0.384 0.440 -0.020 0.037  0.003  478 THR AAA N   
3471  C CA  . THR A 478 ? 0.306 0.386 0.448 -0.020 0.041  0.012  478 THR AAA CA  
3472  C C   . THR A 478 ? 0.308 0.384 0.441 -0.018 0.040  0.019  478 THR AAA C   
3473  O O   . THR A 478 ? 0.326 0.401 0.455 -0.017 0.037  0.015  478 THR AAA O   
3474  C CB  . THR A 478 ? 0.309 0.386 0.467 -0.022 0.047  0.012  478 THR AAA CB  
3475  O OG1 . THR A 478 ? 0.301 0.375 0.464 -0.022 0.047  0.009  478 THR AAA OG1 
3476  C CG2 . THR A 478 ? 0.308 0.389 0.476 -0.024 0.049  0.006  478 THR AAA CG2 
3477  N N   . LYS A 479 ? 0.304 0.381 0.437 -0.017 0.043  0.027  479 LYS AAA N   
3478  C CA  . LYS A 479 ? 0.319 0.393 0.446 -0.015 0.043  0.033  479 LYS AAA CA  
3479  C C   . LYS A 479 ? 0.326 0.396 0.462 -0.016 0.044  0.031  479 LYS AAA C   
3480  O O   . LYS A 479 ? 0.329 0.398 0.459 -0.015 0.041  0.031  479 LYS AAA O   
3481  C CB  . LYS A 479 ? 0.316 0.392 0.443 -0.013 0.047  0.043  479 LYS AAA CB  
3482  C CG  . LYS A 479 ? 0.321 0.397 0.443 -0.011 0.046  0.049  479 LYS AAA CG  
3483  C CD  . LYS A 479 ? 0.330 0.407 0.438 -0.010 0.040  0.046  479 LYS AAA CD  
3484  C CE  . LYS A 479 ? 0.337 0.416 0.438 -0.008 0.040  0.052  479 LYS AAA CE  
3485  N NZ  . LYS A 479 ? 0.348 0.424 0.456 -0.007 0.042  0.056  479 LYS AAA NZ  
3486  N N   . LYS A 480 ? 0.344 0.413 0.494 -0.018 0.048  0.028  480 LYS AAA N   
3487  C CA  . LYS A 480 ? 0.369 0.433 0.529 -0.019 0.049  0.026  480 LYS AAA CA  
3488  C C   . LYS A 480 ? 0.365 0.430 0.519 -0.019 0.044  0.017  480 LYS AAA C   
3489  O O   . LYS A 480 ? 0.317 0.379 0.470 -0.019 0.043  0.017  480 LYS AAA O   
3490  C CB  . LYS A 480 ? 0.372 0.435 0.550 -0.021 0.055  0.024  480 LYS AAA CB  
3491  C CG  . LYS A 480 ? 0.394 0.454 0.584 -0.023 0.057  0.019  480 LYS AAA CG  
3492  C CD  . LYS A 480 ? 0.417 0.474 0.626 -0.025 0.064  0.020  480 LYS AAA CD  
3493  C CE  . LYS A 480 ? 0.458 0.513 0.680 -0.027 0.065  0.013  480 LYS AAA CE  
3494  N NZ  . LYS A 480 ? 0.467 0.519 0.683 -0.025 0.062  0.014  480 LYS AAA NZ  
3495  N N   . ASP A 481 ? 0.352 0.420 0.503 -0.020 0.041  0.010  481 ASP AAA N   
3496  C CA  . ASP A 481 ? 0.352 0.421 0.496 -0.019 0.036  0.002  481 ASP AAA CA  
3497  C C   . ASP A 481 ? 0.363 0.431 0.493 -0.017 0.033  0.006  481 ASP AAA C   
3498  O O   . ASP A 481 ? 0.344 0.410 0.472 -0.017 0.031  0.002  481 ASP AAA O   
3499  C CB  . ASP A 481 ? 0.354 0.428 0.495 -0.019 0.034  -0.004 481 ASP AAA CB  
3500  C CG  . ASP A 481 ? 0.366 0.442 0.521 -0.021 0.037  -0.009 481 ASP AAA CG  
3501  O OD1 . ASP A 481 ? 0.359 0.434 0.528 -0.023 0.040  -0.011 481 ASP AAA OD1 
3502  O OD2 . ASP A 481 ? 0.366 0.446 0.520 -0.022 0.037  -0.011 481 ASP AAA OD2 
3503  N N   . PHE A 482 ? 0.350 0.419 0.471 -0.016 0.033  0.012  482 PHE AAA N   
3504  C CA  . PHE A 482 ? 0.352 0.420 0.460 -0.014 0.030  0.015  482 PHE AAA CA  
3505  C C   . PHE A 482 ? 0.357 0.422 0.468 -0.014 0.031  0.019  482 PHE AAA C   
3506  O O   . PHE A 482 ? 0.355 0.419 0.460 -0.013 0.029  0.018  482 PHE AAA O   
3507  C CB  . PHE A 482 ? 0.352 0.424 0.453 -0.013 0.030  0.021  482 PHE AAA CB  
3508  C CG  . PHE A 482 ? 0.342 0.416 0.433 -0.013 0.027  0.017  482 PHE AAA CG  
3509  C CD1 . PHE A 482 ? 0.345 0.421 0.440 -0.014 0.027  0.013  482 PHE AAA CD1 
3510  C CD2 . PHE A 482 ? 0.359 0.433 0.437 -0.011 0.023  0.016  482 PHE AAA CD2 
3511  C CE1 . PHE A 482 ? 0.351 0.430 0.439 -0.013 0.024  0.009  482 PHE AAA CE1 
3512  C CE2 . PHE A 482 ? 0.351 0.427 0.422 -0.011 0.021  0.012  482 PHE AAA CE2 
3513  C CZ  . PHE A 482 ? 0.363 0.441 0.438 -0.011 0.021  0.009  482 PHE AAA CZ  
3514  N N   . ASP A 483 ? 0.339 0.403 0.461 -0.014 0.036  0.025  483 ASP AAA N   
3515  C CA  . ASP A 483 ? 0.345 0.406 0.471 -0.014 0.037  0.029  483 ASP AAA CA  
3516  C C   . ASP A 483 ? 0.356 0.414 0.488 -0.015 0.037  0.023  483 ASP AAA C   
3517  O O   . ASP A 483 ? 0.398 0.454 0.528 -0.014 0.036  0.025  483 ASP AAA O   
3518  C CB  . ASP A 483 ? 0.368 0.429 0.504 -0.013 0.043  0.037  483 ASP AAA CB  
3519  C CG  . ASP A 483 ? 0.384 0.448 0.513 -0.011 0.044  0.044  483 ASP AAA CG  
3520  O OD1 . ASP A 483 ? 0.393 0.460 0.509 -0.010 0.040  0.044  483 ASP AAA OD1 
3521  O OD2 . ASP A 483 ? 0.432 0.496 0.569 -0.011 0.048  0.050  483 ASP AAA OD2 
3522  N N   . ASP A 484 ? 0.368 0.426 0.508 -0.017 0.037  0.016  484 ASP AAA N   
3523  C CA  . ASP A 484 ? 0.346 0.402 0.493 -0.018 0.037  0.009  484 ASP AAA CA  
3524  C C   . ASP A 484 ? 0.317 0.374 0.454 -0.017 0.032  0.003  484 ASP AAA C   
3525  O O   . ASP A 484 ? 0.302 0.359 0.444 -0.018 0.031  -0.003 484 ASP AAA O   
3526  C CB  . ASP A 484 ? 0.358 0.415 0.521 -0.020 0.040  0.005  484 ASP AAA CB  
3527  C CG  . ASP A 484 ? 0.377 0.431 0.552 -0.021 0.046  0.011  484 ASP AAA CG  
3528  O OD1 . ASP A 484 ? 0.406 0.459 0.578 -0.019 0.048  0.020  484 ASP AAA OD1 
3529  O OD2 . ASP A 484 ? 0.395 0.450 0.583 -0.023 0.050  0.008  484 ASP AAA OD2 
3530  N N   . MET A 485 ? 0.301 0.361 0.425 -0.016 0.029  0.003  485 MET AAA N   
3531  C CA  . MET A 485 ? 0.306 0.366 0.419 -0.015 0.025  -0.001 485 MET AAA CA  
3532  C C   . MET A 485 ? 0.298 0.355 0.405 -0.014 0.023  0.001  485 MET AAA C   
3533  O O   . MET A 485 ? 0.289 0.345 0.392 -0.013 0.024  0.007  485 MET AAA O   
3534  C CB  . MET A 485 ? 0.305 0.367 0.406 -0.013 0.023  0.000  485 MET AAA CB  
3535  C CG  . MET A 485 ? 0.317 0.379 0.405 -0.012 0.019  -0.003 485 MET AAA CG  
3536  S SD  . MET A 485 ? 0.326 0.390 0.402 -0.011 0.017  -0.001 485 MET AAA SD  
3537  C CE  . MET A 485 ? 0.335 0.400 0.410 -0.011 0.019  0.008  485 MET AAA CE  
3538  N N   . ILE A 486 ? 0.285 0.341 0.392 -0.014 0.022  -0.005 486 ILE AAA N   
3539  C CA  . ILE A 486 ? 0.285 0.339 0.387 -0.013 0.020  -0.004 486 ILE AAA CA  
3540  C C   . ILE A 486 ? 0.283 0.337 0.370 -0.012 0.018  -0.003 486 ILE AAA C   
3541  O O   . ILE A 486 ? 0.267 0.323 0.348 -0.011 0.016  -0.007 486 ILE AAA O   
3542  C CB  . ILE A 486 ? 0.285 0.338 0.391 -0.013 0.019  -0.011 486 ILE AAA CB  
3543  C CG1 . ILE A 486 ? 0.284 0.337 0.406 -0.015 0.022  -0.013 486 ILE AAA CG1 
3544  C CG2 . ILE A 486 ? 0.281 0.331 0.381 -0.012 0.019  -0.009 486 ILE AAA CG2 
3545  C CD1 . ILE A 486 ? 0.286 0.336 0.416 -0.015 0.025  -0.007 486 ILE AAA CD1 
3546  N N   . GLY A 487 ? 0.279 0.332 0.361 -0.011 0.018  0.002  487 GLY AAA N   
3547  C CA  . GLY A 487 ? 0.277 0.329 0.346 -0.010 0.016  0.003  487 GLY AAA CA  
3548  C C   . GLY A 487 ? 0.265 0.316 0.329 -0.009 0.014  -0.001 487 GLY AAA C   
3549  O O   . GLY A 487 ? 0.282 0.332 0.352 -0.010 0.014  -0.004 487 GLY AAA O   
3550  N N   . ILE A 488 ? 0.250 0.301 0.303 -0.008 0.013  -0.003 488 ILE AAA N   
3551  C CA  . ILE A 488 ? 0.257 0.305 0.302 -0.007 0.012  -0.005 488 ILE AAA CA  
3552  C C   . ILE A 488 ? 0.255 0.302 0.295 -0.008 0.012  -0.001 488 ILE AAA C   
3553  O O   . ILE A 488 ? 0.260 0.310 0.297 -0.008 0.012  0.002  488 ILE AAA O   
3554  C CB  . ILE A 488 ? 0.258 0.306 0.294 -0.006 0.011  -0.008 488 ILE AAA CB  
3555  C CG1 . ILE A 488 ? 0.259 0.310 0.299 -0.005 0.010  -0.012 488 ILE AAA CG1 
3556  C CG2 . ILE A 488 ? 0.256 0.301 0.286 -0.005 0.010  -0.010 488 ILE AAA CG2 
3557  C CD1 . ILE A 488 ? 0.253 0.304 0.285 -0.003 0.009  -0.015 488 ILE AAA CD1 
3558  N N   . HIS A 489 ? 0.253 0.299 0.294 -0.008 0.012  -0.001 489 HIS AAA N   
3559  C CA  . HIS A 489 ? 0.259 0.305 0.296 -0.008 0.013  0.003  489 HIS AAA CA  
3560  C C   . HIS A 489 ? 0.251 0.294 0.281 -0.008 0.012  -0.000 489 HIS AAA C   
3561  O O   . HIS A 489 ? 0.268 0.309 0.298 -0.008 0.012  -0.004 489 HIS AAA O   
3562  C CB  . HIS A 489 ? 0.260 0.307 0.306 -0.009 0.014  0.005  489 HIS AAA CB  
3563  C CG  . HIS A 489 ? 0.278 0.326 0.321 -0.009 0.014  0.009  489 HIS AAA CG  
3564  N ND1 . HIS A 489 ? 0.289 0.341 0.328 -0.008 0.014  0.012  489 HIS AAA ND1 
3565  C CD2 . HIS A 489 ? 0.280 0.327 0.323 -0.009 0.014  0.009  489 HIS AAA CD2 
3566  C CE1 . HIS A 489 ? 0.292 0.346 0.331 -0.008 0.014  0.014  489 HIS AAA CE1 
3567  N NE2 . HIS A 489 ? 0.287 0.339 0.329 -0.008 0.014  0.012  489 HIS AAA NE2 
3568  N N   . PRO A 490 ? 0.254 0.297 0.277 -0.008 0.013  0.001  490 PRO AAA N   
3569  C CA  . PRO A 490 ? 0.263 0.310 0.285 -0.008 0.013  0.004  490 PRO AAA CA  
3570  C C   . PRO A 490 ? 0.269 0.316 0.285 -0.008 0.013  0.003  490 PRO AAA C   
3571  O O   . PRO A 490 ? 0.305 0.349 0.314 -0.007 0.013  0.000  490 PRO AAA O   
3572  C CB  . PRO A 490 ? 0.259 0.307 0.277 -0.009 0.013  0.004  490 PRO AAA CB  
3573  C CG  . PRO A 490 ? 0.254 0.298 0.271 -0.009 0.014  0.001  490 PRO AAA CG  
3574  C CD  . PRO A 490 ? 0.255 0.295 0.272 -0.008 0.013  -0.002 490 PRO AAA CD  
3575  N N   . THR A 491 ? 0.262 0.312 0.281 -0.008 0.012  0.005  491 THR AAA N   
3576  C CA  . THR A 491 ? 0.256 0.307 0.270 -0.007 0.012  0.004  491 THR AAA CA  
3577  C C   . THR A 491 ? 0.264 0.320 0.279 -0.007 0.012  0.008  491 THR AAA C   
3578  O O   . THR A 491 ? 0.279 0.338 0.299 -0.008 0.013  0.011  491 THR AAA O   
3579  C CB  . THR A 491 ? 0.249 0.299 0.265 -0.006 0.012  0.002  491 THR AAA CB  
3580  O OG1 . THR A 491 ? 0.247 0.300 0.272 -0.007 0.012  0.004  491 THR AAA OG1 
3581  C CG2 . THR A 491 ? 0.247 0.293 0.261 -0.006 0.011  -0.002 491 THR AAA CG2 
3582  N N   . ASP A 492 ? 0.260 0.317 0.270 -0.007 0.012  0.008  492 ASP AAA N   
3583  C CA  . ASP A 492 ? 0.264 0.326 0.275 -0.007 0.013  0.011  492 ASP AAA CA  
3584  C C   . ASP A 492 ? 0.273 0.336 0.290 -0.007 0.013  0.012  492 ASP AAA C   
3585  O O   . ASP A 492 ? 0.292 0.360 0.314 -0.007 0.013  0.016  492 ASP AAA O   
3586  C CB  . ASP A 492 ? 0.268 0.332 0.272 -0.007 0.012  0.010  492 ASP AAA CB  
3587  C CG  . ASP A 492 ? 0.275 0.339 0.275 -0.007 0.013  0.009  492 ASP AAA CG  
3588  O OD1 . ASP A 492 ? 0.282 0.348 0.286 -0.007 0.013  0.010  492 ASP AAA OD1 
3589  O OD2 . ASP A 492 ? 0.316 0.380 0.312 -0.007 0.013  0.006  492 ASP AAA OD2 
3590  N N   . ALA A 493 ? 0.253 0.313 0.270 -0.007 0.012  0.009  493 ALA AAA N   
3591  C CA  . ALA A 493 ? 0.245 0.307 0.268 -0.007 0.012  0.008  493 ALA AAA CA  
3592  C C   . ALA A 493 ? 0.243 0.304 0.275 -0.007 0.013  0.010  493 ALA AAA C   
3593  O O   . ALA A 493 ? 0.245 0.309 0.284 -0.008 0.014  0.011  493 ALA AAA O   
3594  C CB  . ALA A 493 ? 0.256 0.316 0.276 -0.006 0.011  0.004  493 ALA AAA CB  
3595  N N   . GLU A 494 ? 0.236 0.295 0.270 -0.008 0.013  0.011  494 GLU AAA N   
3596  C CA  . GLU A 494 ? 0.246 0.306 0.291 -0.008 0.015  0.013  494 GLU AAA CA  
3597  C C   . GLU A 494 ? 0.234 0.297 0.282 -0.008 0.016  0.019  494 GLU AAA C   
3598  O O   . GLU A 494 ? 0.216 0.280 0.273 -0.008 0.018  0.022  494 GLU AAA O   
3599  C CB  . GLU A 494 ? 0.274 0.330 0.319 -0.008 0.015  0.012  494 GLU AAA CB  
3600  C CG  . GLU A 494 ? 0.289 0.348 0.331 -0.008 0.015  0.015  494 GLU AAA CG  
3601  C CD  . GLU A 494 ? 0.324 0.379 0.367 -0.008 0.015  0.014  494 GLU AAA CD  
3602  O OE1 . GLU A 494 ? 0.355 0.409 0.406 -0.009 0.016  0.015  494 GLU AAA OE1 
3603  O OE2 . GLU A 494 ? 0.356 0.412 0.393 -0.008 0.014  0.013  494 GLU AAA OE2 
3604  N N   . VAL A 495 ? 0.243 0.309 0.284 -0.007 0.016  0.021  495 VAL AAA N   
3605  C CA  . VAL A 495 ? 0.244 0.315 0.288 -0.007 0.018  0.027  495 VAL AAA CA  
3606  C C   . VAL A 495 ? 0.251 0.323 0.302 -0.007 0.019  0.029  495 VAL AAA C   
3607  O O   . VAL A 495 ? 0.281 0.355 0.339 -0.007 0.021  0.034  495 VAL AAA O   
3608  C CB  . VAL A 495 ? 0.246 0.322 0.281 -0.006 0.017  0.028  495 VAL AAA CB  
3609  C CG1 . VAL A 495 ? 0.263 0.340 0.295 -0.006 0.016  0.026  495 VAL AAA CG1 
3610  C CG2 . VAL A 495 ? 0.250 0.332 0.288 -0.004 0.018  0.035  495 VAL AAA CG2 
3611  N N   . PHE A 496 ? 0.242 0.312 0.292 -0.008 0.018  0.024  496 PHE AAA N   
3612  C CA  . PHE A 496 ? 0.248 0.320 0.304 -0.008 0.020  0.025  496 PHE AAA CA  
3613  C C   . PHE A 496 ? 0.259 0.328 0.327 -0.009 0.022  0.025  496 PHE AAA C   
3614  O O   . PHE A 496 ? 0.274 0.345 0.350 -0.010 0.024  0.026  496 PHE AAA O   
3615  C CB  . PHE A 496 ? 0.238 0.309 0.291 -0.009 0.018  0.019  496 PHE AAA CB  
3616  C CG  . PHE A 496 ? 0.233 0.308 0.277 -0.008 0.017  0.020  496 PHE AAA CG  
3617  C CD1 . PHE A 496 ? 0.230 0.309 0.276 -0.008 0.018  0.024  496 PHE AAA CD1 
3618  C CD2 . PHE A 496 ? 0.234 0.307 0.269 -0.007 0.015  0.017  496 PHE AAA CD2 
3619  C CE1 . PHE A 496 ? 0.226 0.307 0.263 -0.007 0.017  0.024  496 PHE AAA CE1 
3620  C CE2 . PHE A 496 ? 0.234 0.310 0.262 -0.007 0.014  0.018  496 PHE AAA CE2 
3621  C CZ  . PHE A 496 ? 0.229 0.310 0.258 -0.007 0.015  0.021  496 PHE AAA CZ  
3622  N N   . GLY A 497 ? 0.270 0.337 0.341 -0.009 0.022  0.025  497 GLY AAA N   
3623  C CA  . GLY A 497 ? 0.292 0.356 0.375 -0.010 0.025  0.025  497 GLY AAA CA  
3624  C C   . GLY A 497 ? 0.298 0.362 0.385 -0.009 0.028  0.033  497 GLY AAA C   
3625  O O   . GLY A 497 ? 0.309 0.372 0.407 -0.010 0.030  0.034  497 GLY AAA O   
3626  N N   . ILE A 498 ? 0.336 0.404 0.417 -0.008 0.027  0.038  498 ILE AAA N   
3627  C CA  . ILE A 498 ? 0.344 0.414 0.427 -0.006 0.030  0.045  498 ILE AAA CA  
3628  C C   . ILE A 498 ? 0.340 0.416 0.419 -0.004 0.030  0.050  498 ILE AAA C   
3629  O O   . ILE A 498 ? 0.359 0.439 0.435 -0.002 0.030  0.055  498 ILE AAA O   
3630  C CB  . ILE A 498 ? 0.358 0.427 0.437 -0.005 0.028  0.044  498 ILE AAA CB  
3631  C CG1 . ILE A 498 ? 0.380 0.451 0.447 -0.005 0.024  0.041  498 ILE AAA CG1 
3632  C CG2 . ILE A 498 ? 0.364 0.428 0.450 -0.006 0.028  0.040  498 ILE AAA CG2 
3633  C CD1 . ILE A 498 ? 0.398 0.471 0.462 -0.004 0.023  0.042  498 ILE AAA CD1 
3634  N N   . LEU A 499 ? 0.338 0.416 0.415 -0.005 0.030  0.049  499 LEU AAA N   
3635  C CA  . LEU A 499 ? 0.363 0.447 0.436 -0.003 0.031  0.054  499 LEU AAA CA  
3636  C C   . LEU A 499 ? 0.400 0.484 0.482 -0.001 0.036  0.062  499 LEU AAA C   
3637  O O   . LEU A 499 ? 0.421 0.502 0.513 -0.003 0.038  0.061  499 LEU AAA O   
3638  C CB  . LEU A 499 ? 0.363 0.448 0.431 -0.004 0.029  0.051  499 LEU AAA CB  
3639  C CG  . LEU A 499 ? 0.359 0.444 0.418 -0.005 0.025  0.044  499 LEU AAA CG  
3640  C CD1 . LEU A 499 ? 0.358 0.444 0.416 -0.006 0.025  0.041  499 LEU AAA CD1 
3641  C CD2 . LEU A 499 ? 0.343 0.433 0.393 -0.003 0.024  0.046  499 LEU AAA CD2 
3642  N N   . GLU A 500 ? 0.418 0.508 0.498 0.002  0.037  0.069  500 GLU AAA N   
3643  C CA  . GLU A 500 ? 0.443 0.534 0.531 0.004  0.042  0.077  500 GLU AAA CA  
3644  C C   . GLU A 500 ? 0.416 0.514 0.499 0.007  0.043  0.084  500 GLU AAA C   
3645  O O   . GLU A 500 ? 0.436 0.535 0.526 0.009  0.048  0.090  500 GLU AAA O   
3646  C CB  . GLU A 500 ? 0.496 0.583 0.589 0.005  0.043  0.080  500 GLU AAA CB  
3647  C CG  . GLU A 500 ? 0.538 0.630 0.622 0.007  0.040  0.080  500 GLU AAA CG  
3648  C CD  . GLU A 500 ? 0.612 0.700 0.701 0.008  0.041  0.082  500 GLU AAA CD  
3649  O OE1 . GLU A 500 ? 0.676 0.760 0.776 0.008  0.045  0.084  500 GLU AAA OE1 
3650  O OE2 . GLU A 500 ? 0.723 0.815 0.807 0.009  0.039  0.080  500 GLU AAA OE2 
3651  N N   . VAL A 501 ? 0.397 0.502 0.470 0.008  0.040  0.082  501 VAL AAA N   
3652  C CA  . VAL A 501 ? 0.387 0.501 0.454 0.012  0.040  0.088  501 VAL AAA CA  
3653  C C   . VAL A 501 ? 0.391 0.506 0.457 0.010  0.041  0.087  501 VAL AAA C   
3654  O O   . VAL A 501 ? 0.379 0.492 0.443 0.007  0.038  0.080  501 VAL AAA O   
3655  C CB  . VAL A 501 ? 0.370 0.492 0.427 0.014  0.036  0.086  501 VAL AAA CB  
3656  C CG1 . VAL A 501 ? 0.365 0.498 0.417 0.017  0.037  0.091  501 VAL AAA CG1 
3657  C CG2 . VAL A 501 ? 0.376 0.497 0.435 0.015  0.036  0.087  501 VAL AAA CG2 
3658  N N   . THR A 502 ? 0.397 0.517 0.466 0.013  0.044  0.094  502 THR AAA N   
3659  C CA  . THR A 502 ? 0.382 0.504 0.451 0.012  0.045  0.093  502 THR AAA CA  
3660  C C   . THR A 502 ? 0.374 0.507 0.433 0.015  0.044  0.096  502 THR AAA C   
3661  O O   . THR A 502 ? 0.392 0.531 0.449 0.018  0.044  0.101  502 THR AAA O   
3662  C CB  . THR A 502 ? 0.377 0.495 0.457 0.011  0.051  0.099  502 THR AAA CB  
3663  O OG1 . THR A 502 ? 0.390 0.514 0.471 0.016  0.055  0.108  502 THR AAA OG1 
3664  C CG2 . THR A 502 ? 0.376 0.485 0.466 0.009  0.053  0.096  502 THR AAA CG2 
3665  N N   . LYS A 503 ? 0.397 0.533 0.452 0.013  0.041  0.092  503 LYS AAA N   
3666  C CA  . LYS A 503 ? 0.447 0.594 0.495 0.016  0.041  0.094  503 LYS AAA CA  
3667  C C   . LYS A 503 ? 0.450 0.602 0.502 0.020  0.046  0.105  503 LYS AAA C   
3668  O O   . LYS A 503 ? 0.453 0.613 0.500 0.024  0.046  0.109  503 LYS AAA O   
3669  C CB  . LYS A 503 ? 0.489 0.637 0.533 0.014  0.039  0.090  503 LYS AAA CB  
3670  C CG  . LYS A 503 ? 0.532 0.691 0.568 0.016  0.038  0.091  503 LYS AAA CG  
3671  C CD  . LYS A 503 ? 0.567 0.727 0.599 0.014  0.036  0.085  503 LYS AAA CD  
3672  C CE  . LYS A 503 ? 0.589 0.759 0.612 0.015  0.032  0.082  503 LYS AAA CE  
3673  N NZ  . LYS A 503 ? 0.620 0.796 0.640 0.016  0.032  0.081  503 LYS AAA NZ  
3674  N N   . ARG A 504 ? 0.446 0.592 0.506 0.019  0.050  0.108  504 ARG AAA N   
3675  C CA  . ARG A 504 ? 0.470 0.619 0.536 0.023  0.056  0.118  504 ARG AAA CA  
3676  C C   . ARG A 504 ? 0.472 0.624 0.537 0.027  0.058  0.125  504 ARG AAA C   
3677  O O   . ARG A 504 ? 0.430 0.591 0.493 0.032  0.060  0.133  504 ARG AAA O   
3678  C CB  . ARG A 504 ? 0.486 0.626 0.564 0.020  0.061  0.120  504 ARG AAA CB  
3679  C CG  . ARG A 504 ? 0.504 0.645 0.588 0.023  0.068  0.131  504 ARG AAA CG  
3680  C CD  . ARG A 504 ? 0.538 0.671 0.634 0.020  0.073  0.131  504 ARG AAA CD  
3681  N NE  . ARG A 504 ? 0.551 0.686 0.646 0.018  0.072  0.127  504 ARG AAA NE  
3682  C CZ  . ARG A 504 ? 0.571 0.700 0.671 0.013  0.071  0.119  504 ARG AAA CZ  
3683  N NH1 . ARG A 504 ? 0.626 0.746 0.733 0.010  0.071  0.114  504 ARG AAA NH1 
3684  N NH2 . ARG A 504 ? 0.556 0.688 0.655 0.011  0.070  0.116  504 ARG AAA NH2 
3685  N N   . SER A 505 ? 0.449 0.594 0.518 0.026  0.057  0.122  505 SER AAA N   
3686  C CA  . SER A 505 ? 0.462 0.609 0.532 0.030  0.058  0.128  505 SER AAA CA  
3687  C C   . SER A 505 ? 0.453 0.613 0.512 0.034  0.055  0.130  505 SER AAA C   
3688  O O   . SER A 505 ? 0.435 0.600 0.494 0.039  0.057  0.136  505 SER AAA O   
3689  C CB  . SER A 505 ? 0.450 0.588 0.523 0.027  0.056  0.123  505 SER AAA CB  
3690  O OG  . SER A 505 ? 0.425 0.566 0.490 0.026  0.050  0.116  505 SER AAA OG  
3691  N N   . GLY A 506 ? 0.448 0.614 0.499 0.033  0.050  0.123  506 GLY AAA N   
3692  C CA  . GLY A 506 ? 0.444 0.622 0.484 0.036  0.047  0.122  506 GLY AAA CA  
3693  C C   . GLY A 506 ? 0.460 0.639 0.498 0.037  0.044  0.119  506 GLY AAA C   
3694  O O   . GLY A 506 ? 0.392 0.582 0.423 0.040  0.041  0.117  506 GLY AAA O   
3695  N N   . GLU A 507 ? 0.480 0.648 0.525 0.035  0.044  0.117  507 GLU AAA N   
3696  C CA  . GLU A 507 ? 0.518 0.686 0.561 0.035  0.042  0.114  507 GLU AAA CA  
3697  C C   . GLU A 507 ? 0.481 0.649 0.518 0.031  0.036  0.104  507 GLU AAA C   
3698  O O   . GLU A 507 ? 0.432 0.597 0.467 0.027  0.035  0.099  507 GLU AAA O   
3699  C CB  . GLU A 507 ? 0.577 0.733 0.629 0.033  0.045  0.116  507 GLU AAA CB  
3700  C CG  . GLU A 507 ? 0.618 0.775 0.676 0.038  0.050  0.127  507 GLU AAA CG  
3701  C CD  . GLU A 507 ? 0.715 0.860 0.783 0.037  0.053  0.129  507 GLU AAA CD  
3702  O OE1 . GLU A 507 ? 0.676 0.812 0.751 0.033  0.056  0.127  507 GLU AAA OE1 
3703  O OE2 . GLU A 507 ? 0.858 1.002 0.927 0.039  0.053  0.130  507 GLU AAA OE2 
3704  N N   . SER A 508 ? 0.443 0.614 0.477 0.032  0.034  0.100  508 SER AAA N   
3705  C CA  . SER A 508 ? 0.438 0.608 0.466 0.028  0.029  0.091  508 SER AAA CA  
3706  C C   . SER A 508 ? 0.392 0.547 0.424 0.023  0.029  0.085  508 SER AAA C   
3707  O O   . SER A 508 ? 0.384 0.532 0.422 0.023  0.031  0.088  508 SER AAA O   
3708  C CB  . SER A 508 ? 0.458 0.635 0.483 0.031  0.027  0.089  508 SER AAA CB  
3709  O OG  . SER A 508 ? 0.471 0.645 0.492 0.027  0.024  0.079  508 SER AAA OG  
3710  N N   . PHE A 509 ? 0.365 0.518 0.393 0.019  0.026  0.078  509 PHE AAA N   
3711  C CA  . PHE A 509 ? 0.374 0.515 0.405 0.015  0.025  0.073  509 PHE AAA CA  
3712  C C   . PHE A 509 ? 0.381 0.520 0.407 0.013  0.022  0.065  509 PHE AAA C   
3713  O O   . PHE A 509 ? 0.351 0.482 0.378 0.009  0.021  0.060  509 PHE AAA O   
3714  C CB  . PHE A 509 ? 0.346 0.484 0.376 0.012  0.026  0.071  509 PHE AAA CB  
3715  C CG  . PHE A 509 ? 0.347 0.493 0.371 0.013  0.024  0.068  509 PHE AAA CG  
3716  C CD1 . PHE A 509 ? 0.341 0.486 0.359 0.011  0.021  0.060  509 PHE AAA CD1 
3717  C CD2 . PHE A 509 ? 0.367 0.521 0.390 0.016  0.025  0.073  509 PHE AAA CD2 
3718  C CE1 . PHE A 509 ? 0.353 0.505 0.366 0.011  0.019  0.058  509 PHE AAA CE1 
3719  C CE2 . PHE A 509 ? 0.370 0.532 0.387 0.016  0.024  0.070  509 PHE AAA CE2 
3720  C CZ  . PHE A 509 ? 0.353 0.514 0.365 0.013  0.021  0.062  509 PHE AAA CZ  
3721  N N   . VAL A 510 ? 0.407 0.556 0.429 0.015  0.021  0.065  510 VAL AAA N   
3722  C CA  . VAL A 510 ? 0.467 0.615 0.486 0.013  0.018  0.058  510 VAL AAA CA  
3723  C C   . VAL A 510 ? 0.492 0.634 0.515 0.013  0.019  0.059  510 VAL AAA C   
3724  O O   . VAL A 510 ? 0.537 0.680 0.564 0.016  0.021  0.065  510 VAL AAA O   
3725  C CB  . VAL A 510 ? 0.478 0.638 0.491 0.016  0.017  0.056  510 VAL AAA CB  
3726  C CG1 . VAL A 510 ? 0.470 0.632 0.482 0.015  0.015  0.050  510 VAL AAA CG1 
3727  C CG2 . VAL A 510 ? 0.469 0.635 0.478 0.016  0.016  0.054  510 VAL AAA CG2 
3728  N N   . SER A 511 ? 0.541 0.674 0.563 0.010  0.018  0.053  511 SER AAA N   
3729  C CA  . SER A 511 ? 0.599 0.730 0.624 0.010  0.017  0.052  511 SER AAA CA  
3730  C C   . SER A 511 ? 0.628 0.761 0.647 0.009  0.015  0.045  511 SER AAA C   
3731  O O   . SER A 511 ? 0.591 0.721 0.607 0.006  0.014  0.039  511 SER AAA O   
3732  C CB  . SER A 511 ? 0.574 0.693 0.604 0.007  0.018  0.051  511 SER AAA CB  
3733  O OG  . SER A 511 ? 0.501 0.613 0.527 0.004  0.017  0.045  511 SER AAA OG  
3734  N N   . SER A 512 ? 0.718 0.858 0.737 0.011  0.015  0.045  512 SER AAA N   
3735  C CA  . SER A 512 ? 0.812 0.958 0.828 0.010  0.013  0.039  512 SER AAA CA  
3736  C C   . SER A 512 ? 0.855 0.993 0.872 0.008  0.013  0.034  512 SER AAA C   
3737  O O   . SER A 512 ? 0.829 0.965 0.843 0.005  0.012  0.028  512 SER AAA O   
3738  C CB  . SER A 512 ? 0.894 1.053 0.909 0.014  0.013  0.041  512 SER AAA CB  
3739  O OG  . SER A 512 ? 0.952 1.121 0.965 0.017  0.013  0.044  512 SER AAA OG  
3740  N N   . GLY A 513 ? 0.922 1.054 0.944 0.008  0.014  0.038  513 GLY AAA N   
3741  C CA  . GLY A 513 ? 0.997 1.120 1.021 0.006  0.014  0.035  513 GLY AAA CA  
3742  C C   . GLY A 513 ? 0.993 1.106 1.014 0.002  0.013  0.030  513 GLY AAA C   
3743  O O   . GLY A 513 ? 1.044 1.154 1.065 0.002  0.014  0.032  513 GLY AAA O   
3744  N N   . GLY A 514 ? 0.917 1.025 0.937 0.000  0.013  0.025  514 GLY AAA N   
3745  C CA  . GLY A 514 ? 0.935 1.035 0.953 -0.003 0.013  0.020  514 GLY AAA CA  
3746  C C   . GLY A 514 ? 0.911 1.000 0.931 -0.004 0.013  0.020  514 GLY AAA C   
3747  O O   . GLY A 514 ? 0.814 0.899 0.833 -0.006 0.013  0.015  514 GLY AAA O   
3748  N N   . CYS A 515 ? 0.943 1.031 0.968 -0.003 0.014  0.024  515 CYS AAA N   
3749  C CA  . CYS A 515 ? 0.969 1.047 0.997 -0.004 0.014  0.023  515 CYS AAA CA  
3750  C C   . CYS A 515 ? 0.901 0.975 0.926 -0.006 0.014  0.021  515 CYS AAA C   
3751  O O   . CYS A 515 ? 0.976 1.045 1.005 -0.006 0.014  0.020  515 CYS AAA O   
3752  C CB  . CYS A 515 ? 1.035 1.114 1.071 -0.003 0.015  0.028  515 CYS AAA CB  
3753  S SG  . CYS A 515 ? 1.138 1.224 1.177 -0.000 0.016  0.034  515 CYS AAA SG  
3754  N N   . GLY A 516 ? 0.749 0.827 0.770 -0.006 0.014  0.020  516 GLY AAA N   
3755  C CA  . GLY A 516 ? 0.681 0.755 0.698 -0.006 0.014  0.018  516 GLY AAA CA  
3756  C C   . GLY A 516 ? 0.641 0.717 0.662 -0.006 0.014  0.022  516 GLY AAA C   
3757  O O   . GLY A 516 ? 0.679 0.760 0.703 -0.004 0.014  0.026  516 GLY AAA O   
3758  N N   . GLY A 517 ? 0.702 0.773 0.725 -0.006 0.014  0.020  517 GLY AAA N   
3759  C CA  . GLY A 517 ? 0.730 0.802 0.757 -0.006 0.014  0.023  517 GLY AAA CA  
3760  C C   . GLY A 517 ? 0.754 0.824 0.790 -0.006 0.016  0.026  517 GLY AAA C   
3761  O O   . GLY A 517 ? 0.726 0.798 0.766 -0.006 0.017  0.029  517 GLY AAA O   
3762  N N   . GLY A 518 ? 0.846 0.914 0.884 -0.006 0.016  0.025  518 GLY AAA N   
3763  C CA  . GLY A 518 ? 0.889 0.954 0.936 -0.006 0.017  0.027  518 GLY AAA CA  
3764  C C   . GLY A 518 ? 0.942 1.010 0.993 -0.005 0.018  0.032  518 GLY AAA C   
3765  O O   . GLY A 518 ? 0.915 0.989 0.964 -0.003 0.018  0.036  518 GLY AAA O   
3766  N N   . LYS A 519 ? 1.001 1.066 1.058 -0.005 0.019  0.031  519 LYS AAA N   
3767  C CA  . LYS A 519 ? 1.053 1.120 1.113 -0.004 0.019  0.035  519 LYS AAA CA  
3768  C C   . LYS A 519 ? 0.983 1.045 1.046 -0.005 0.019  0.031  519 LYS AAA C   
3769  O O   . LYS A 519 ? 0.967 1.025 1.035 -0.006 0.019  0.028  519 LYS AAA O   
3770  C CB  . LYS A 519 ? 1.149 1.217 1.216 -0.002 0.022  0.042  519 LYS AAA CB  
3771  C CG  . LYS A 519 ? 1.225 1.301 1.289 0.000  0.023  0.047  519 LYS AAA CG  
3772  C CD  . LYS A 519 ? 1.267 1.347 1.335 0.004  0.024  0.053  519 LYS AAA CD  
3773  C CE  . LYS A 519 ? 1.271 1.359 1.335 0.006  0.025  0.059  519 LYS AAA CE  
3774  N NZ  . LYS A 519 ? 1.241 1.328 1.313 0.008  0.029  0.065  519 LYS AAA NZ  
3775  N N   . CYS A 520 ? 0.899 0.961 0.957 -0.005 0.018  0.029  520 CYS AAA N   
3776  C CA  A CYS A 520 ? 0.877 0.936 0.939 -0.005 0.018  0.026  520 CYS AAA CA  
3777  C CA  B CYS A 520 ? 0.839 0.898 0.901 -0.005 0.018  0.026  520 CYS AAA CA  
3778  C C   . CYS A 520 ? 0.897 0.955 0.969 -0.004 0.020  0.030  520 CYS AAA C   
3779  O O   . CYS A 520 ? 0.931 0.985 1.007 -0.005 0.020  0.028  520 CYS AAA O   
3780  C CB  A CYS A 520 ? 0.817 0.877 0.872 -0.005 0.016  0.024  520 CYS AAA CB  
3781  C CB  B CYS A 520 ? 0.726 0.787 0.782 -0.005 0.016  0.024  520 CYS AAA CB  
3782  S SG  A CYS A 520 ? 0.728 0.793 0.773 -0.005 0.015  0.023  520 CYS AAA SG  
3783  S SG  B CYS A 520 ? 0.647 0.704 0.694 -0.007 0.015  0.017  520 CYS AAA SG  
3784  N N   . GLY A 521 ? 0.936 0.997 1.010 -0.002 0.021  0.037  521 GLY AAA N   
3785  C CA  . GLY A 521 ? 0.981 1.042 1.065 -0.001 0.024  0.042  521 GLY AAA CA  
3786  C C   . GLY A 521 ? 1.036 1.103 1.120 0.002  0.026  0.049  521 GLY AAA C   
3787  O O   . GLY A 521 ? 1.096 1.167 1.173 0.003  0.025  0.050  521 GLY AAA O   
3788  O OXT . GLY A 521 ? 0.971 1.037 1.062 0.004  0.029  0.055  521 GLY AAA OXT 
3789  N N   . LEU B 24  ? 1.011 0.893 1.028 0.075  0.124  0.059  24  LEU BBB N   
3790  C CA  . LEU B 24  ? 1.039 0.927 1.073 0.067  0.125  0.052  24  LEU BBB CA  
3791  C C   . LEU B 24  ? 1.023 0.925 1.059 0.066  0.114  0.048  24  LEU BBB C   
3792  O O   . LEU B 24  ? 1.064 0.971 1.090 0.071  0.107  0.050  24  LEU BBB O   
3793  C CB  . LEU B 24  ? 1.026 0.917 1.068 0.058  0.127  0.048  24  LEU BBB CB  
3794  C CG  . LEU B 24  ? 1.022 0.911 1.080 0.051  0.135  0.043  24  LEU BBB CG  
3795  C CD1 . LEU B 24  ? 1.047 0.920 1.106 0.056  0.145  0.046  24  LEU BBB CD1 
3796  C CD2 . LEU B 24  ? 1.005 0.892 1.067 0.045  0.139  0.041  24  LEU BBB CD2 
3797  N N   . THR B 25  ? 1.000 0.908 1.048 0.061  0.114  0.041  25  THR BBB N   
3798  C CA  . THR B 25  ? 0.979 0.897 1.031 0.061  0.107  0.038  25  THR BBB CA  
3799  C C   . THR B 25  ? 0.909 0.843 0.962 0.057  0.097  0.033  25  THR BBB C   
3800  O O   . THR B 25  ? 0.992 0.935 1.051 0.055  0.092  0.028  25  THR BBB O   
3801  C CB  . THR B 25  ? 1.022 0.939 1.088 0.057  0.111  0.033  25  THR BBB CB  
3802  O OG1 . THR B 25  ? 0.970 0.889 1.046 0.049  0.115  0.028  25  THR BBB OG1 
3803  C CG2 . THR B 25  ? 1.018 0.921 1.083 0.063  0.120  0.037  25  THR BBB CG2 
3804  N N   . PHE B 26  ? 0.805 0.741 0.851 0.056  0.095  0.034  26  PHE BBB N   
3805  C CA  . PHE B 26  ? 0.758 0.708 0.804 0.052  0.086  0.030  26  PHE BBB CA  
3806  C C   . PHE B 26  ? 0.700 0.651 0.732 0.057  0.081  0.034  26  PHE BBB C   
3807  O O   . PHE B 26  ? 0.661 0.604 0.686 0.059  0.085  0.039  26  PHE BBB O   
3808  C CB  . PHE B 26  ? 0.736 0.690 0.789 0.044  0.087  0.026  26  PHE BBB CB  
3809  C CG  . PHE B 26  ? 0.725 0.678 0.792 0.039  0.092  0.021  26  PHE BBB CG  
3810  C CD1 . PHE B 26  ? 0.679 0.640 0.753 0.037  0.088  0.016  26  PHE BBB CD1 
3811  C CD2 . PHE B 26  ? 0.720 0.666 0.793 0.036  0.099  0.021  26  PHE BBB CD2 
3812  C CE1 . PHE B 26  ? 0.676 0.636 0.762 0.033  0.092  0.011  26  PHE BBB CE1 
3813  C CE2 . PHE B 26  ? 0.722 0.668 0.808 0.031  0.104  0.015  26  PHE BBB CE2 
3814  C CZ  . PHE B 26  ? 0.712 0.665 0.804 0.030  0.100  0.011  26  PHE BBB CZ  
3815  N N   . MET B 27  ? 0.618 0.578 0.647 0.059  0.073  0.032  27  MET BBB N   
3816  C CA  . MET B 27  ? 0.638 0.602 0.656 0.063  0.068  0.035  27  MET BBB CA  
3817  C C   . MET B 27  ? 0.613 0.579 0.629 0.058  0.067  0.034  27  MET BBB C   
3818  O O   . MET B 27  ? 0.587 0.549 0.594 0.062  0.068  0.039  27  MET BBB O   
3819  C CB  . MET B 27  ? 0.654 0.630 0.672 0.064  0.059  0.031  27  MET BBB CB  
3820  C CG  . MET B 27  ? 0.652 0.626 0.670 0.071  0.059  0.032  27  MET BBB CG  
3821  S SD  . MET B 27  ? 0.679 0.668 0.701 0.070  0.050  0.026  27  MET BBB SD  
3822  C CE  . MET B 27  ? 0.681 0.675 0.691 0.075  0.043  0.027  27  MET BBB CE  
3823  N N   . TYR B 28  ? 0.584 0.557 0.609 0.050  0.066  0.029  28  TYR BBB N   
3824  C CA  . TYR B 28  ? 0.566 0.543 0.591 0.045  0.065  0.028  28  TYR BBB CA  
3825  C C   . TYR B 28  ? 0.546 0.518 0.579 0.039  0.072  0.026  28  TYR BBB C   
3826  O O   . TYR B 28  ? 0.509 0.479 0.551 0.037  0.075  0.024  28  TYR BBB O   
3827  C CB  . TYR B 28  ? 0.543 0.532 0.570 0.041  0.058  0.023  28  TYR BBB CB  
3828  C CG  . TYR B 28  ? 0.529 0.524 0.548 0.046  0.051  0.024  28  TYR BBB CG  
3829  C CD1 . TYR B 28  ? 0.516 0.513 0.536 0.050  0.049  0.023  28  TYR BBB CD1 
3830  C CD2 . TYR B 28  ? 0.535 0.532 0.547 0.047  0.048  0.025  28  TYR BBB CD2 
3831  C CE1 . TYR B 28  ? 0.518 0.521 0.532 0.054  0.043  0.023  28  TYR BBB CE1 
3832  C CE2 . TYR B 28  ? 0.527 0.529 0.532 0.051  0.043  0.026  28  TYR BBB CE2 
3833  C CZ  . TYR B 28  ? 0.519 0.525 0.526 0.055  0.040  0.024  28  TYR BBB CZ  
3834  O OH  . TYR B 28  ? 0.527 0.539 0.528 0.060  0.034  0.023  28  TYR BBB OH  
3835  N N   . ASP B 29  ? 0.528 0.499 0.560 0.037  0.073  0.027  29  ASP BBB N   
3836  C CA  . ASP B 29  ? 0.529 0.498 0.569 0.030  0.077  0.024  29  ASP BBB CA  
3837  C C   . ASP B 29  ? 0.499 0.480 0.545 0.024  0.072  0.017  29  ASP BBB C   
3838  O O   . ASP B 29  ? 0.466 0.448 0.523 0.020  0.075  0.013  29  ASP BBB O   
3839  C CB  . ASP B 29  ? 0.545 0.508 0.579 0.030  0.081  0.027  29  ASP BBB CB  
3840  C CG  . ASP B 29  ? 0.573 0.524 0.602 0.036  0.088  0.033  29  ASP BBB CG  
3841  O OD1 . ASP B 29  ? 0.552 0.495 0.587 0.036  0.095  0.033  29  ASP BBB OD1 
3842  O OD2 . ASP B 29  ? 0.580 0.528 0.597 0.041  0.086  0.038  29  ASP BBB OD2 
3843  N N   . LEU B 30  ? 0.455 0.445 0.497 0.025  0.065  0.017  30  LEU BBB N   
3844  C CA  . LEU B 30  ? 0.443 0.442 0.488 0.019  0.060  0.011  30  LEU BBB CA  
3845  C C   . LEU B 30  ? 0.430 0.437 0.470 0.021  0.053  0.011  30  LEU BBB C   
3846  O O   . LEU B 30  ? 0.415 0.422 0.447 0.025  0.051  0.014  30  LEU BBB O   
3847  C CB  . LEU B 30  ? 0.451 0.451 0.494 0.016  0.060  0.011  30  LEU BBB CB  
3848  C CG  . LEU B 30  ? 0.439 0.450 0.485 0.011  0.055  0.006  30  LEU BBB CG  
3849  C CD1 . LEU B 30  ? 0.433 0.446 0.489 0.007  0.056  0.001  30  LEU BBB CD1 
3850  C CD2 . LEU B 30  ? 0.437 0.447 0.479 0.009  0.054  0.007  30  LEU BBB CD2 
3851  N N   . VAL B 31  ? 0.392 0.406 0.439 0.018  0.050  0.006  31  VAL BBB N   
3852  C CA  . VAL B 31  ? 0.409 0.431 0.453 0.019  0.044  0.004  31  VAL BBB CA  
3853  C C   . VAL B 31  ? 0.392 0.421 0.439 0.013  0.042  -0.001 31  VAL BBB C   
3854  O O   . VAL B 31  ? 0.392 0.422 0.447 0.010  0.044  -0.004 31  VAL BBB O   
3855  C CB  . VAL B 31  ? 0.397 0.421 0.445 0.021  0.043  0.003  31  VAL BBB CB  
3856  C CG1 . VAL B 31  ? 0.382 0.415 0.430 0.020  0.038  -0.001 31  VAL BBB CG1 
3857  C CG2 . VAL B 31  ? 0.417 0.434 0.459 0.028  0.045  0.008  31  VAL BBB CG2 
3858  N N   . VAL B 32  ? 0.361 0.396 0.404 0.012  0.038  -0.001 32  VAL BBB N   
3859  C CA  . VAL B 32  ? 0.333 0.374 0.377 0.007  0.035  -0.004 32  VAL BBB CA  
3860  C C   . VAL B 32  ? 0.316 0.364 0.359 0.007  0.031  -0.007 32  VAL BBB C   
3861  O O   . VAL B 32  ? 0.286 0.335 0.324 0.010  0.029  -0.005 32  VAL BBB O   
3862  C CB  . VAL B 32  ? 0.317 0.356 0.354 0.007  0.035  -0.002 32  VAL BBB CB  
3863  C CG1 . VAL B 32  ? 0.311 0.356 0.349 0.002  0.032  -0.006 32  VAL BBB CG1 
3864  C CG2 . VAL B 32  ? 0.315 0.348 0.354 0.007  0.039  -0.000 32  VAL BBB CG2 
3865  N N   . ILE B 33  ? 0.308 0.359 0.356 0.004  0.031  -0.011 33  ILE BBB N   
3866  C CA  . ILE B 33  ? 0.321 0.379 0.368 0.003  0.027  -0.014 33  ILE BBB CA  
3867  C C   . ILE B 33  ? 0.306 0.368 0.351 -0.000 0.025  -0.015 33  ILE BBB C   
3868  O O   . ILE B 33  ? 0.340 0.404 0.389 -0.003 0.026  -0.018 33  ILE BBB O   
3869  C CB  . ILE B 33  ? 0.336 0.396 0.390 0.003  0.028  -0.017 33  ILE BBB CB  
3870  C CG1 . ILE B 33  ? 0.356 0.412 0.413 0.006  0.030  -0.015 33  ILE BBB CG1 
3871  C CG2 . ILE B 33  ? 0.324 0.391 0.378 0.002  0.025  -0.020 33  ILE BBB CG2 
3872  C CD1 . ILE B 33  ? 0.363 0.420 0.428 0.006  0.031  -0.018 33  ILE BBB CD1 
3873  N N   . GLY B 34  ? 0.299 0.363 0.339 0.000  0.023  -0.014 34  GLY BBB N   
3874  C CA  . GLY B 34  ? 0.293 0.360 0.329 -0.003 0.022  -0.015 34  GLY BBB CA  
3875  C C   . GLY B 34  ? 0.289 0.352 0.319 -0.002 0.021  -0.012 34  GLY BBB C   
3876  O O   . GLY B 34  ? 0.303 0.362 0.334 -0.001 0.024  -0.010 34  GLY BBB O   
3877  N N   . GLY B 35  ? 0.278 0.344 0.304 -0.002 0.019  -0.012 35  GLY BBB N   
3878  C CA  . GLY B 35  ? 0.289 0.353 0.309 -0.001 0.018  -0.009 35  GLY BBB CA  
3879  C C   . GLY B 35  ? 0.276 0.342 0.294 -0.004 0.018  -0.010 35  GLY BBB C   
3880  O O   . GLY B 35  ? 0.276 0.344 0.290 -0.004 0.016  -0.010 35  GLY BBB O   
3881  N N   . GLY B 36  ? 0.285 0.350 0.305 -0.007 0.019  -0.012 36  GLY BBB N   
3882  C CA  . GLY B 36  ? 0.298 0.364 0.315 -0.009 0.019  -0.012 36  GLY BBB CA  
3883  C C   . GLY B 36  ? 0.294 0.356 0.311 -0.009 0.020  -0.011 36  GLY BBB C   
3884  O O   . GLY B 36  ? 0.272 0.331 0.289 -0.007 0.021  -0.008 36  GLY BBB O   
3885  N N   . SER B 37  ? 0.319 0.382 0.335 -0.011 0.020  -0.012 37  SER BBB N   
3886  C CA  . SER B 37  ? 0.343 0.403 0.358 -0.012 0.021  -0.011 37  SER BBB CA  
3887  C C   . SER B 37  ? 0.347 0.404 0.368 -0.011 0.024  -0.011 37  SER BBB C   
3888  O O   . SER B 37  ? 0.389 0.442 0.409 -0.010 0.025  -0.009 37  SER BBB O   
3889  C CB  . SER B 37  ? 0.346 0.408 0.360 -0.014 0.020  -0.014 37  SER BBB CB  
3890  O OG  . SER B 37  ? 0.358 0.422 0.367 -0.014 0.019  -0.014 37  SER BBB OG  
3891  N N   . GLY B 38  ? 0.339 0.397 0.365 -0.011 0.025  -0.014 38  GLY BBB N   
3892  C CA  . GLY B 38  ? 0.331 0.387 0.363 -0.011 0.027  -0.015 38  GLY BBB CA  
3893  C C   . GLY B 38  ? 0.334 0.386 0.367 -0.008 0.029  -0.011 38  GLY BBB C   
3894  O O   . GLY B 38  ? 0.328 0.375 0.361 -0.008 0.032  -0.010 38  GLY BBB O   
3895  N N   . GLY B 39  ? 0.329 0.382 0.360 -0.007 0.028  -0.011 39  GLY BBB N   
3896  C CA  . GLY B 39  ? 0.346 0.396 0.377 -0.004 0.029  -0.008 39  GLY BBB CA  
3897  C C   . GLY B 39  ? 0.356 0.402 0.381 -0.002 0.029  -0.004 39  GLY BBB C   
3898  O O   . GLY B 39  ? 0.356 0.397 0.382 0.001  0.032  -0.001 39  GLY BBB O   
3899  N N   . MET B 40  ? 0.370 0.419 0.390 -0.002 0.026  -0.003 40  MET BBB N   
3900  C CA  . MET B 40  ? 0.391 0.437 0.405 0.001  0.026  0.001  40  MET BBB CA  
3901  C C   . MET B 40  ? 0.366 0.407 0.380 -0.000 0.029  0.002  40  MET BBB C   
3902  O O   . MET B 40  ? 0.363 0.400 0.375 0.003  0.031  0.006  40  MET BBB O   
3903  C CB  . MET B 40  ? 0.410 0.460 0.419 -0.000 0.023  0.000  40  MET BBB CB  
3904  C CG  . MET B 40  ? 0.436 0.490 0.444 0.001  0.020  -0.001 40  MET BBB CG  
3905  S SD  . MET B 40  ? 0.454 0.513 0.457 0.001  0.017  -0.001 40  MET BBB SD  
3906  C CE  . MET B 40  ? 0.454 0.513 0.457 -0.004 0.017  -0.003 40  MET BBB CE  
3907  N N   . ALA B 41  ? 0.338 0.380 0.356 -0.003 0.030  -0.000 41  ALA BBB N   
3908  C CA  . ALA B 41  ? 0.329 0.368 0.349 -0.004 0.033  -0.000 41  ALA BBB CA  
3909  C C   . ALA B 41  ? 0.338 0.371 0.363 -0.003 0.037  0.001  41  ALA BBB C   
3910  O O   . ALA B 41  ? 0.339 0.367 0.362 -0.002 0.041  0.004  41  ALA BBB O   
3911  C CB  . ALA B 41  ? 0.328 0.370 0.350 -0.008 0.032  -0.004 41  ALA BBB CB  
3912  N N   . ALA B 42  ? 0.321 0.355 0.351 -0.004 0.038  -0.002 42  ALA BBB N   
3913  C CA  . ALA B 42  ? 0.331 0.361 0.367 -0.003 0.043  -0.001 42  ALA BBB CA  
3914  C C   . ALA B 42  ? 0.354 0.378 0.385 0.002  0.044  0.004  42  ALA BBB C   
3915  O O   . ALA B 42  ? 0.339 0.356 0.371 0.003  0.049  0.006  42  ALA BBB O   
3916  C CB  . ALA B 42  ? 0.327 0.360 0.369 -0.003 0.042  -0.005 42  ALA BBB CB  
3917  N N   . ALA B 43  ? 0.369 0.396 0.395 0.004  0.041  0.005  43  ALA BBB N   
3918  C CA  . ALA B 43  ? 0.393 0.417 0.414 0.009  0.041  0.009  43  ALA BBB CA  
3919  C C   . ALA B 43  ? 0.405 0.423 0.419 0.011  0.043  0.014  43  ALA BBB C   
3920  O O   . ALA B 43  ? 0.404 0.415 0.417 0.015  0.047  0.017  43  ALA BBB O   
3921  C CB  . ALA B 43  ? 0.376 0.405 0.394 0.010  0.036  0.008  43  ALA BBB CB  
3922  N N   . LYS B 44  ? 0.447 0.468 0.457 0.010  0.040  0.013  44  LYS BBB N   
3923  C CA  . LYS B 44  ? 0.461 0.478 0.464 0.012  0.041  0.017  44  LYS BBB CA  
3924  C C   . LYS B 44  ? 0.455 0.465 0.462 0.010  0.047  0.018  44  LYS BBB C   
3925  O O   . LYS B 44  ? 0.475 0.479 0.476 0.013  0.050  0.022  44  LYS BBB O   
3926  C CB  . LYS B 44  ? 0.460 0.483 0.460 0.009  0.037  0.016  44  LYS BBB CB  
3927  C CG  . LYS B 44  ? 0.515 0.542 0.510 0.011  0.032  0.016  44  LYS BBB CG  
3928  C CD  . LYS B 44  ? 0.547 0.578 0.538 0.009  0.029  0.015  44  LYS BBB CD  
3929  C CE  . LYS B 44  ? 0.543 0.581 0.537 0.005  0.026  0.011  44  LYS BBB CE  
3930  N NZ  . LYS B 44  ? 0.584 0.625 0.574 0.004  0.024  0.010  44  LYS BBB NZ  
3931  N N   . GLU B 45  ? 0.446 0.458 0.461 0.006  0.048  0.014  45  GLU BBB N   
3932  C CA  . GLU B 45  ? 0.458 0.464 0.478 0.004  0.054  0.014  45  GLU BBB CA  
3933  C C   . GLU B 45  ? 0.446 0.445 0.468 0.007  0.060  0.016  45  GLU BBB C   
3934  O O   . GLU B 45  ? 0.415 0.406 0.436 0.008  0.065  0.019  45  GLU BBB O   
3935  C CB  . GLU B 45  ? 0.461 0.471 0.488 -0.000 0.054  0.008  45  GLU BBB CB  
3936  C CG  . GLU B 45  ? 0.467 0.473 0.500 -0.002 0.059  0.007  45  GLU BBB CG  
3937  C CD  . GLU B 45  ? 0.488 0.494 0.515 -0.003 0.058  0.008  45  GLU BBB CD  
3938  O OE1 . GLU B 45  ? 0.496 0.505 0.515 -0.002 0.054  0.010  45  GLU BBB OE1 
3939  O OE2 . GLU B 45  ? 0.523 0.526 0.555 -0.005 0.062  0.007  45  GLU BBB OE2 
3940  N N   . ALA B 46  ? 0.445 0.445 0.470 0.008  0.059  0.015  46  ALA BBB N   
3941  C CA  . ALA B 46  ? 0.441 0.434 0.468 0.011  0.064  0.017  46  ALA BBB CA  
3942  C C   . ALA B 46  ? 0.450 0.436 0.467 0.017  0.065  0.023  46  ALA BBB C   
3943  O O   . ALA B 46  ? 0.466 0.444 0.483 0.018  0.071  0.026  46  ALA BBB O   
3944  C CB  . ALA B 46  ? 0.434 0.432 0.465 0.011  0.061  0.015  46  ALA BBB CB  
3945  N N   . ALA B 47  ? 0.463 0.453 0.472 0.019  0.059  0.025  47  ALA BBB N   
3946  C CA  . ALA B 47  ? 0.481 0.467 0.480 0.026  0.059  0.030  47  ALA BBB CA  
3947  C C   . ALA B 47  ? 0.499 0.479 0.493 0.026  0.063  0.034  47  ALA BBB C   
3948  O O   . ALA B 47  ? 0.531 0.503 0.518 0.031  0.066  0.039  47  ALA BBB O   
3949  C CB  . ALA B 47  ? 0.464 0.459 0.458 0.027  0.052  0.029  47  ALA BBB CB  
3950  N N   . LYS B 48  ? 0.526 0.509 0.524 0.021  0.063  0.031  48  LYS BBB N   
3951  C CA  . LYS B 48  ? 0.590 0.567 0.585 0.020  0.067  0.033  48  LYS BBB CA  
3952  C C   . LYS B 48  ? 0.596 0.563 0.594 0.022  0.076  0.036  48  LYS BBB C   
3953  O O   . LYS B 48  ? 0.577 0.537 0.569 0.024  0.080  0.040  48  LYS BBB O   
3954  C CB  . LYS B 48  ? 0.616 0.599 0.618 0.014  0.066  0.028  48  LYS BBB CB  
3955  C CG  . LYS B 48  ? 0.672 0.659 0.667 0.013  0.061  0.029  48  LYS BBB CG  
3956  C CD  . LYS B 48  ? 0.728 0.719 0.728 0.008  0.061  0.025  48  LYS BBB CD  
3957  C CE  . LYS B 48  ? 0.808 0.791 0.811 0.007  0.068  0.025  48  LYS BBB CE  
3958  N NZ  . LYS B 48  ? 0.817 0.804 0.821 0.004  0.067  0.024  48  LYS BBB NZ  
3959  N N   . TYR B 49  ? 0.621 0.585 0.626 0.021  0.079  0.034  49  TYR BBB N   
3960  C CA  . TYR B 49  ? 0.647 0.601 0.657 0.021  0.088  0.035  49  TYR BBB CA  
3961  C C   . TYR B 49  ? 0.655 0.601 0.658 0.028  0.091  0.041  49  TYR BBB C   
3962  O O   . TYR B 49  ? 0.710 0.647 0.717 0.029  0.098  0.042  49  TYR BBB O   
3963  C CB  . TYR B 49  ? 0.667 0.624 0.691 0.016  0.090  0.029  49  TYR BBB CB  
3964  C CG  . TYR B 49  ? 0.692 0.655 0.721 0.010  0.089  0.024  49  TYR BBB CG  
3965  C CD1 . TYR B 49  ? 0.735 0.693 0.763 0.009  0.093  0.025  49  TYR BBB CD1 
3966  C CD2 . TYR B 49  ? 0.699 0.673 0.734 0.006  0.083  0.019  49  TYR BBB CD2 
3967  C CE1 . TYR B 49  ? 0.778 0.743 0.811 0.004  0.091  0.021  49  TYR BBB CE1 
3968  C CE2 . TYR B 49  ? 0.696 0.675 0.734 0.002  0.081  0.014  49  TYR BBB CE2 
3969  C CZ  . TYR B 49  ? 0.739 0.713 0.777 0.001  0.085  0.015  49  TYR BBB CZ  
3970  O OH  . TYR B 49  ? 0.805 0.785 0.847 -0.003 0.083  0.011  49  TYR BBB OH  
3971  N N   . GLY B 50  ? 0.641 0.590 0.634 0.033  0.085  0.044  50  GLY BBB N   
3972  C CA  . GLY B 50  ? 0.622 0.565 0.607 0.040  0.086  0.049  50  GLY BBB CA  
3973  C C   . GLY B 50  ? 0.571 0.516 0.561 0.041  0.085  0.047  50  GLY BBB C   
3974  O O   . GLY B 50  ? 0.566 0.504 0.553 0.047  0.088  0.050  50  GLY BBB O   
3975  N N   . LYS B 51  ? 0.540 0.495 0.540 0.035  0.081  0.041  51  LYS BBB N   
3976  C CA  . LYS B 51  ? 0.518 0.476 0.525 0.035  0.079  0.038  51  LYS BBB CA  
3977  C C   . LYS B 51  ? 0.489 0.454 0.489 0.039  0.071  0.038  51  LYS BBB C   
3978  O O   . LYS B 51  ? 0.474 0.445 0.468 0.039  0.066  0.038  51  LYS BBB O   
3979  C CB  . LYS B 51  ? 0.565 0.529 0.583 0.028  0.079  0.031  51  LYS BBB CB  
3980  C CG  . LYS B 51  ? 0.598 0.556 0.624 0.024  0.086  0.030  51  LYS BBB CG  
3981  C CD  . LYS B 51  ? 0.639 0.585 0.665 0.027  0.095  0.034  51  LYS BBB CD  
3982  C CE  . LYS B 51  ? 0.669 0.610 0.706 0.023  0.102  0.031  51  LYS BBB CE  
3983  N NZ  . LYS B 51  ? 0.687 0.615 0.721 0.026  0.111  0.036  51  LYS BBB NZ  
3984  N N   . LYS B 52  ? 0.488 0.453 0.489 0.043  0.071  0.038  52  LYS BBB N   
3985  C CA  . LYS B 52  ? 0.481 0.453 0.479 0.046  0.064  0.037  52  LYS BBB CA  
3986  C C   . LYS B 52  ? 0.449 0.431 0.455 0.040  0.059  0.031  52  LYS BBB C   
3987  O O   . LYS B 52  ? 0.436 0.419 0.452 0.036  0.062  0.028  52  LYS BBB O   
3988  C CB  . LYS B 52  ? 0.514 0.480 0.509 0.053  0.066  0.040  52  LYS BBB CB  
3989  C CG  . LYS B 52  ? 0.533 0.505 0.520 0.059  0.059  0.041  52  LYS BBB CG  
3990  C CD  . LYS B 52  ? 0.555 0.525 0.543 0.064  0.059  0.042  52  LYS BBB CD  
3991  C CE  . LYS B 52  ? 0.546 0.525 0.529 0.069  0.051  0.040  52  LYS BBB CE  
3992  N NZ  . LYS B 52  ? 0.551 0.530 0.536 0.073  0.050  0.040  52  LYS BBB NZ  
3993  N N   . VAL B 53  ? 0.421 0.413 0.425 0.039  0.053  0.029  53  VAL BBB N   
3994  C CA  . VAL B 53  ? 0.412 0.414 0.422 0.032  0.048  0.023  53  VAL BBB CA  
3995  C C   . VAL B 53  ? 0.407 0.417 0.415 0.035  0.042  0.021  53  VAL BBB C   
3996  O O   . VAL B 53  ? 0.402 0.413 0.402 0.039  0.039  0.024  53  VAL BBB O   
3997  C CB  . VAL B 53  ? 0.417 0.420 0.427 0.028  0.048  0.022  53  VAL BBB CB  
3998  C CG1 . VAL B 53  ? 0.416 0.428 0.433 0.022  0.045  0.016  53  VAL BBB CG1 
3999  C CG2 . VAL B 53  ? 0.428 0.423 0.439 0.026  0.055  0.024  53  VAL BBB CG2 
4000  N N   . ALA B 54  ? 0.396 0.411 0.410 0.032  0.040  0.017  54  ALA BBB N   
4001  C CA  . ALA B 54  ? 0.381 0.406 0.396 0.032  0.034  0.014  54  ALA BBB CA  
4002  C C   . ALA B 54  ? 0.358 0.390 0.378 0.025  0.032  0.009  54  ALA BBB C   
4003  O O   . ALA B 54  ? 0.364 0.394 0.390 0.022  0.035  0.007  54  ALA BBB O   
4004  C CB  . ALA B 54  ? 0.394 0.419 0.411 0.036  0.033  0.013  54  ALA BBB CB  
4005  N N   . LEU B 55  ? 0.343 0.381 0.360 0.024  0.027  0.007  55  LEU BBB N   
4006  C CA  . LEU B 55  ? 0.319 0.363 0.340 0.019  0.026  0.003  55  LEU BBB CA  
4007  C C   . LEU B 55  ? 0.318 0.370 0.340 0.019  0.022  -0.000 55  LEU BBB C   
4008  O O   . LEU B 55  ? 0.333 0.387 0.351 0.022  0.019  0.000  55  LEU BBB O   
4009  C CB  . LEU B 55  ? 0.302 0.348 0.320 0.016  0.025  0.004  55  LEU BBB CB  
4010  C CG  . LEU B 55  ? 0.285 0.336 0.305 0.010  0.024  -0.000 55  LEU BBB CG  
4011  C CD1 . LEU B 55  ? 0.282 0.330 0.300 0.008  0.025  0.001  55  LEU BBB CD1 
4012  C CD2 . LEU B 55  ? 0.281 0.339 0.300 0.010  0.020  -0.002 55  LEU BBB CD2 
4013  N N   . PHE B 56  ? 0.331 0.387 0.359 0.015  0.021  -0.004 56  PHE BBB N   
4014  C CA  . PHE B 56  ? 0.355 0.419 0.386 0.014  0.018  -0.008 56  PHE BBB CA  
4015  C C   . PHE B 56  ? 0.357 0.424 0.387 0.009  0.017  -0.011 56  PHE BBB C   
4016  O O   . PHE B 56  ? 0.356 0.421 0.388 0.006  0.019  -0.011 56  PHE BBB O   
4017  C CB  . PHE B 56  ? 0.371 0.435 0.408 0.014  0.019  -0.010 56  PHE BBB CB  
4018  C CG  . PHE B 56  ? 0.394 0.454 0.431 0.020  0.020  -0.008 56  PHE BBB CG  
4019  C CD1 . PHE B 56  ? 0.407 0.471 0.444 0.024  0.017  -0.009 56  PHE BBB CD1 
4020  C CD2 . PHE B 56  ? 0.422 0.475 0.461 0.021  0.024  -0.005 56  PHE BBB CD2 
4021  C CE1 . PHE B 56  ? 0.422 0.482 0.458 0.029  0.018  -0.006 56  PHE BBB CE1 
4022  C CE2 . PHE B 56  ? 0.441 0.489 0.479 0.026  0.026  -0.003 56  PHE BBB CE2 
4023  C CZ  . PHE B 56  ? 0.427 0.479 0.463 0.031  0.022  -0.003 56  PHE BBB CZ  
4024  N N   . ASP B 57  ? 0.350 0.422 0.378 0.009  0.014  -0.012 57  ASP BBB N   
4025  C CA  . ASP B 57  ? 0.338 0.414 0.367 0.005  0.014  -0.015 57  ASP BBB CA  
4026  C C   . ASP B 57  ? 0.330 0.413 0.361 0.005  0.011  -0.019 57  ASP BBB C   
4027  O O   . ASP B 57  ? 0.302 0.387 0.331 0.009  0.009  -0.018 57  ASP BBB O   
4028  C CB  . ASP B 57  ? 0.333 0.409 0.357 0.003  0.013  -0.013 57  ASP BBB CB  
4029  C CG  . ASP B 57  ? 0.347 0.424 0.370 -0.001 0.013  -0.016 57  ASP BBB CG  
4030  O OD1 . ASP B 57  ? 0.332 0.408 0.357 -0.004 0.015  -0.017 57  ASP BBB OD1 
4031  O OD2 . ASP B 57  ? 0.343 0.424 0.364 -0.002 0.012  -0.018 57  ASP BBB OD2 
4032  N N   . PHE B 58  ? 0.327 0.413 0.361 0.002  0.012  -0.022 58  PHE BBB N   
4033  C CA  . PHE B 58  ? 0.343 0.435 0.380 0.001  0.010  -0.026 58  PHE BBB CA  
4034  C C   . PHE B 58  ? 0.341 0.434 0.378 -0.004 0.012  -0.029 58  PHE BBB C   
4035  O O   . PHE B 58  ? 0.314 0.404 0.352 -0.006 0.014  -0.028 58  PHE BBB O   
4036  C CB  . PHE B 58  ? 0.367 0.461 0.409 0.003  0.010  -0.028 58  PHE BBB CB  
4037  C CG  . PHE B 58  ? 0.375 0.476 0.421 0.002  0.008  -0.033 58  PHE BBB CG  
4038  C CD1 . PHE B 58  ? 0.380 0.484 0.429 -0.002 0.010  -0.036 58  PHE BBB CD1 
4039  C CD2 . PHE B 58  ? 0.366 0.471 0.412 0.006  0.006  -0.034 58  PHE BBB CD2 
4040  C CE1 . PHE B 58  ? 0.386 0.496 0.439 -0.003 0.009  -0.041 58  PHE BBB CE1 
4041  C CE2 . PHE B 58  ? 0.369 0.481 0.419 0.005  0.005  -0.039 58  PHE BBB CE2 
4042  C CZ  . PHE B 58  ? 0.385 0.499 0.439 0.000  0.007  -0.043 58  PHE BBB CZ  
4043  N N   . VAL B 59  ? 0.334 0.430 0.370 -0.006 0.011  -0.031 59  VAL BBB N   
4044  C CA  . VAL B 59  ? 0.341 0.438 0.377 -0.010 0.013  -0.033 59  VAL BBB CA  
4045  C C   . VAL B 59  ? 0.335 0.436 0.376 -0.012 0.014  -0.037 59  VAL BBB C   
4046  O O   . VAL B 59  ? 0.336 0.441 0.379 -0.012 0.013  -0.040 59  VAL BBB O   
4047  C CB  . VAL B 59  ? 0.332 0.429 0.363 -0.012 0.013  -0.032 59  VAL BBB CB  
4048  C CG1 . VAL B 59  ? 0.328 0.424 0.357 -0.016 0.016  -0.034 59  VAL BBB CG1 
4049  C CG2 . VAL B 59  ? 0.345 0.438 0.372 -0.010 0.012  -0.028 59  VAL BBB CG2 
4050  N N   . LYS B 60  ? 0.339 0.439 0.381 -0.013 0.016  -0.038 60  LYS BBB N   
4051  C CA  . LYS B 60  ? 0.360 0.463 0.406 -0.015 0.017  -0.042 60  LYS BBB CA  
4052  C C   . LYS B 60  ? 0.357 0.460 0.399 -0.019 0.019  -0.043 60  LYS BBB C   
4053  O O   . LYS B 60  ? 0.360 0.459 0.397 -0.020 0.020  -0.041 60  LYS BBB O   
4054  C CB  . LYS B 60  ? 0.366 0.468 0.414 -0.016 0.019  -0.042 60  LYS BBB CB  
4055  C CG  . LYS B 60  ? 0.396 0.499 0.449 -0.013 0.017  -0.042 60  LYS BBB CG  
4056  C CD  . LYS B 60  ? 0.383 0.485 0.439 -0.013 0.018  -0.043 60  LYS BBB CD  
4057  C CE  . LYS B 60  ? 0.385 0.483 0.438 -0.014 0.019  -0.041 60  LYS BBB CE  
4058  N NZ  . LYS B 60  ? 0.404 0.498 0.454 -0.012 0.019  -0.037 60  LYS BBB NZ  
4059  N N   . PRO B 61  ? 0.354 0.461 0.400 -0.020 0.020  -0.047 61  PRO BBB N   
4060  C CA  . PRO B 61  ? 0.355 0.461 0.398 -0.023 0.023  -0.048 61  PRO BBB CA  
4061  C C   . PRO B 61  ? 0.353 0.455 0.392 -0.026 0.026  -0.048 61  PRO BBB C   
4062  O O   . PRO B 61  ? 0.370 0.473 0.411 -0.025 0.026  -0.048 61  PRO BBB O   
4063  C CB  . PRO B 61  ? 0.347 0.458 0.396 -0.024 0.024  -0.053 61  PRO BBB CB  
4064  C CG  . PRO B 61  ? 0.343 0.458 0.397 -0.021 0.020  -0.054 61  PRO BBB CG  
4065  C CD  . PRO B 61  ? 0.345 0.457 0.397 -0.019 0.019  -0.050 61  PRO BBB CD  
4066  N N   . SER B 62  ? 0.343 0.442 0.376 -0.028 0.028  -0.046 62  SER BBB N   
4067  C CA  . SER B 62  ? 0.347 0.442 0.375 -0.029 0.031  -0.046 62  SER BBB CA  
4068  C C   . SER B 62  ? 0.357 0.454 0.388 -0.031 0.034  -0.049 62  SER BBB C   
4069  O O   . SER B 62  ? 0.334 0.435 0.372 -0.031 0.034  -0.053 62  SER BBB O   
4070  C CB  . SER B 62  ? 0.349 0.440 0.371 -0.030 0.033  -0.044 62  SER BBB CB  
4071  O OG  . SER B 62  ? 0.364 0.456 0.387 -0.033 0.036  -0.046 62  SER BBB OG  
4072  N N   . THR B 63  ? 0.363 0.457 0.390 -0.032 0.037  -0.049 63  THR BBB N   
4073  C CA  . THR B 63  ? 0.398 0.492 0.426 -0.034 0.041  -0.052 63  THR BBB CA  
4074  C C   . THR B 63  ? 0.417 0.511 0.447 -0.036 0.044  -0.055 63  THR BBB C   
4075  O O   . THR B 63  ? 0.421 0.517 0.455 -0.038 0.047  -0.058 63  THR BBB O   
4076  C CB  . THR B 63  ? 0.395 0.484 0.415 -0.034 0.044  -0.051 63  THR BBB CB  
4077  O OG1 . THR B 63  ? 0.394 0.479 0.407 -0.034 0.045  -0.048 63  THR BBB OG1 
4078  C CG2 . THR B 63  ? 0.373 0.464 0.394 -0.031 0.041  -0.050 63  THR BBB CG2 
4079  N N   . GLN B 64  ? 0.425 0.518 0.453 -0.037 0.044  -0.053 64  GLN BBB N   
4080  C CA  . GLN B 64  ? 0.423 0.516 0.453 -0.039 0.047  -0.056 64  GLN BBB CA  
4081  C C   . GLN B 64  ? 0.389 0.488 0.427 -0.039 0.044  -0.058 64  GLN BBB C   
4082  O O   . GLN B 64  ? 0.410 0.510 0.449 -0.041 0.046  -0.060 64  GLN BBB O   
4083  C CB  . GLN B 64  ? 0.445 0.532 0.467 -0.041 0.051  -0.053 64  GLN BBB CB  
4084  C CG  . GLN B 64  ? 0.483 0.565 0.498 -0.041 0.055  -0.052 64  GLN BBB CG  
4085  C CD  . GLN B 64  ? 0.505 0.587 0.523 -0.044 0.060  -0.056 64  GLN BBB CD  
4086  O OE1 . GLN B 64  ? 0.500 0.584 0.525 -0.046 0.063  -0.060 64  GLN BBB OE1 
4087  N NE2 . GLN B 64  ? 0.510 0.589 0.524 -0.043 0.063  -0.056 64  GLN BBB NE2 
4088  N N   . GLY B 65  ? 0.352 0.455 0.393 -0.036 0.039  -0.058 65  GLY BBB N   
4089  C CA  . GLY B 65  ? 0.347 0.456 0.395 -0.034 0.036  -0.060 65  GLY BBB CA  
4090  C C   . GLY B 65  ? 0.368 0.475 0.411 -0.033 0.033  -0.056 65  GLY BBB C   
4091  O O   . GLY B 65  ? 0.370 0.482 0.418 -0.031 0.030  -0.058 65  GLY BBB O   
4092  N N   . THR B 66  ? 0.360 0.461 0.395 -0.033 0.033  -0.052 66  THR BBB N   
4093  C CA  . THR B 66  ? 0.368 0.467 0.399 -0.031 0.031  -0.049 66  THR BBB CA  
4094  C C   . THR B 66  ? 0.376 0.478 0.409 -0.028 0.026  -0.046 66  THR BBB C   
4095  O O   . THR B 66  ? 0.384 0.483 0.415 -0.027 0.026  -0.045 66  THR BBB O   
4096  C CB  . THR B 66  ? 0.357 0.450 0.381 -0.032 0.033  -0.045 66  THR BBB CB  
4097  O OG1 . THR B 66  ? 0.407 0.498 0.430 -0.035 0.038  -0.047 66  THR BBB OG1 
4098  C CG2 . THR B 66  ? 0.360 0.452 0.381 -0.032 0.031  -0.043 66  THR BBB CG2 
4099  N N   . LYS B 67  ? 0.379 0.482 0.412 -0.026 0.023  -0.046 67  LYS BBB N   
4100  C CA  . LYS B 67  ? 0.414 0.518 0.447 -0.022 0.019  -0.043 67  LYS BBB CA  
4101  C C   . LYS B 67  ? 0.379 0.482 0.408 -0.021 0.018  -0.041 67  LYS BBB C   
4102  O O   . LYS B 67  ? 0.339 0.442 0.367 -0.023 0.019  -0.042 67  LYS BBB O   
4103  C CB  . LYS B 67  ? 0.473 0.582 0.512 -0.019 0.017  -0.046 67  LYS BBB CB  
4104  C CG  . LYS B 67  ? 0.519 0.634 0.563 -0.019 0.015  -0.049 67  LYS BBB CG  
4105  C CD  . LYS B 67  ? 0.597 0.718 0.647 -0.016 0.014  -0.053 67  LYS BBB CD  
4106  C CE  . LYS B 67  ? 0.662 0.788 0.715 -0.012 0.010  -0.055 67  LYS BBB CE  
4107  N NZ  . LYS B 67  ? 0.704 0.832 0.759 -0.008 0.007  -0.055 67  LYS BBB NZ  
4108  N N   . TRP B 68  ? 0.335 0.437 0.363 -0.018 0.015  -0.037 68  TRP BBB N   
4109  C CA  . TRP B 68  ? 0.311 0.410 0.334 -0.016 0.014  -0.034 68  TRP BBB CA  
4110  C C   . TRP B 68  ? 0.306 0.404 0.328 -0.012 0.011  -0.031 68  TRP BBB C   
4111  O O   . TRP B 68  ? 0.291 0.391 0.316 -0.010 0.010  -0.032 68  TRP BBB O   
4112  C CB  . TRP B 68  ? 0.292 0.385 0.309 -0.019 0.016  -0.031 68  TRP BBB CB  
4113  C CG  . TRP B 68  ? 0.276 0.367 0.293 -0.019 0.017  -0.030 68  TRP BBB CG  
4114  C CD1 . TRP B 68  ? 0.278 0.366 0.294 -0.017 0.015  -0.027 68  TRP BBB CD1 
4115  C CD2 . TRP B 68  ? 0.284 0.374 0.301 -0.021 0.019  -0.031 68  TRP BBB CD2 
4116  N NE1 . TRP B 68  ? 0.280 0.367 0.297 -0.018 0.017  -0.027 68  TRP BBB NE1 
4117  C CE2 . TRP B 68  ? 0.273 0.360 0.289 -0.020 0.019  -0.030 68  TRP BBB CE2 
4118  C CE3 . TRP B 68  ? 0.293 0.384 0.311 -0.024 0.022  -0.034 68  TRP BBB CE3 
4119  C CZ2 . TRP B 68  ? 0.278 0.365 0.294 -0.022 0.021  -0.031 68  TRP BBB CZ2 
4120  C CZ3 . TRP B 68  ? 0.299 0.388 0.315 -0.025 0.024  -0.035 68  TRP BBB CZ3 
4121  C CH2 . TRP B 68  ? 0.295 0.382 0.311 -0.024 0.023  -0.033 68  TRP BBB CH2 
4122  N N   . GLY B 69  ? 0.296 0.393 0.314 -0.011 0.010  -0.028 69  GLY BBB N   
4123  C CA  . GLY B 69  ? 0.303 0.399 0.319 -0.006 0.007  -0.025 69  GLY BBB CA  
4124  C C   . GLY B 69  ? 0.304 0.394 0.318 -0.006 0.009  -0.021 69  GLY BBB C   
4125  O O   . GLY B 69  ? 0.303 0.391 0.317 -0.009 0.011  -0.022 69  GLY BBB O   
4126  N N   . LEU B 70  ? 0.303 0.391 0.315 -0.002 0.008  -0.018 70  LEU BBB N   
4127  C CA  . LEU B 70  ? 0.296 0.377 0.305 -0.002 0.009  -0.014 70  LEU BBB CA  
4128  C C   . LEU B 70  ? 0.299 0.377 0.305 -0.005 0.011  -0.013 70  LEU BBB C   
4129  O O   . LEU B 70  ? 0.319 0.398 0.323 -0.006 0.010  -0.013 70  LEU BBB O   
4130  C CB  . LEU B 70  ? 0.291 0.371 0.298 0.003  0.008  -0.011 70  LEU BBB CB  
4131  C CG  . LEU B 70  ? 0.284 0.357 0.288 0.004  0.010  -0.007 70  LEU BBB CG  
4132  C CD1 . LEU B 70  ? 0.278 0.349 0.287 0.004  0.012  -0.008 70  LEU BBB CD1 
4133  C CD2 . LEU B 70  ? 0.291 0.362 0.292 0.009  0.009  -0.004 70  LEU BBB CD2 
4134  N N   . GLY B 71  ? 0.278 0.353 0.286 -0.006 0.012  -0.012 71  GLY BBB N   
4135  C CA  . GLY B 71  ? 0.271 0.342 0.276 -0.008 0.013  -0.010 71  GLY BBB CA  
4136  C C   . GLY B 71  ? 0.256 0.327 0.263 -0.010 0.015  -0.012 71  GLY BBB C   
4137  O O   . GLY B 71  ? 0.272 0.340 0.277 -0.011 0.016  -0.012 71  GLY BBB O   
4138  N N   . GLY B 72  ? 0.238 0.313 0.248 -0.011 0.015  -0.015 72  GLY BBB N   
4139  C CA  . GLY B 72  ? 0.247 0.321 0.259 -0.013 0.016  -0.017 72  GLY BBB CA  
4140  C C   . GLY B 72  ? 0.250 0.325 0.259 -0.015 0.016  -0.018 72  GLY BBB C   
4141  O O   . GLY B 72  ? 0.265 0.341 0.271 -0.016 0.016  -0.018 72  GLY BBB O   
4142  N N   . THR B 73  ? 0.250 0.325 0.259 -0.016 0.017  -0.020 73  THR BBB N   
4143  C CA  . THR B 73  ? 0.275 0.349 0.280 -0.018 0.018  -0.021 73  THR BBB CA  
4144  C C   . THR B 73  ? 0.288 0.360 0.288 -0.019 0.018  -0.019 73  THR BBB C   
4145  O O   . THR B 73  ? 0.272 0.343 0.268 -0.020 0.019  -0.019 73  THR BBB O   
4146  C CB  . THR B 73  ? 0.272 0.347 0.278 -0.018 0.019  -0.023 73  THR BBB CB  
4147  O OG1 . THR B 73  ? 0.248 0.324 0.259 -0.018 0.019  -0.025 73  THR BBB OG1 
4148  C CG2 . THR B 73  ? 0.287 0.360 0.287 -0.019 0.020  -0.024 73  THR BBB CG2 
4149  N N   . CYS B 74  ? 0.314 0.384 0.313 -0.018 0.017  -0.017 74  CYS BBB N   
4150  C CA  A CYS B 74  ? 0.327 0.395 0.321 -0.018 0.017  -0.016 74  CYS BBB CA  
4151  C CA  B CYS B 74  ? 0.348 0.416 0.342 -0.018 0.017  -0.016 74  CYS BBB CA  
4152  C C   . CYS B 74  ? 0.337 0.404 0.329 -0.018 0.017  -0.015 74  CYS BBB C   
4153  O O   . CYS B 74  ? 0.350 0.417 0.338 -0.020 0.017  -0.015 74  CYS BBB O   
4154  C CB  A CYS B 74  ? 0.344 0.410 0.339 -0.017 0.017  -0.015 74  CYS BBB CB  
4155  C CB  B CYS B 74  ? 0.399 0.465 0.396 -0.017 0.017  -0.014 74  CYS BBB CB  
4156  S SG  A CYS B 74  ? 0.362 0.425 0.351 -0.018 0.017  -0.014 74  CYS BBB SG  
4157  S SG  B CYS B 74  ? 0.452 0.515 0.444 -0.017 0.016  -0.012 74  CYS BBB SG  
4158  N N   . VAL B 75  ? 0.306 0.376 0.301 -0.017 0.016  -0.014 75  VAL BBB N   
4159  C CA  . VAL B 75  ? 0.284 0.354 0.277 -0.017 0.015  -0.013 75  VAL BBB CA  
4160  C C   . VAL B 75  ? 0.264 0.336 0.257 -0.019 0.016  -0.015 75  VAL BBB C   
4161  O O   . VAL B 75  ? 0.243 0.315 0.234 -0.020 0.016  -0.016 75  VAL BBB O   
4162  C CB  . VAL B 75  ? 0.285 0.356 0.281 -0.015 0.014  -0.012 75  VAL BBB CB  
4163  C CG1 . VAL B 75  ? 0.275 0.348 0.270 -0.014 0.013  -0.012 75  VAL BBB CG1 
4164  C CG2 . VAL B 75  ? 0.294 0.362 0.289 -0.013 0.014  -0.009 75  VAL BBB CG2 
4165  N N   . ASN B 76  ? 0.244 0.318 0.241 -0.019 0.017  -0.018 76  ASN BBB N   
4166  C CA  . ASN B 76  ? 0.240 0.318 0.239 -0.020 0.017  -0.020 76  ASN BBB CA  
4167  C C   . ASN B 76  ? 0.244 0.320 0.240 -0.023 0.020  -0.022 76  ASN BBB C   
4168  O O   . ASN B 76  ? 0.239 0.315 0.234 -0.024 0.021  -0.023 76  ASN BBB O   
4169  C CB  . ASN B 76  ? 0.243 0.323 0.247 -0.019 0.017  -0.022 76  ASN BBB CB  
4170  C CG  . ASN B 76  ? 0.232 0.314 0.237 -0.016 0.014  -0.021 76  ASN BBB CG  
4171  O OD1 . ASN B 76  ? 0.217 0.302 0.223 -0.016 0.013  -0.022 76  ASN BBB OD1 
4172  N ND2 . ASN B 76  ? 0.235 0.315 0.241 -0.014 0.014  -0.018 76  ASN BBB ND2 
4173  N N   . VAL B 77  ? 0.248 0.322 0.243 -0.023 0.021  -0.021 77  VAL BBB N   
4174  C CA  . VAL B 77  ? 0.254 0.327 0.247 -0.024 0.023  -0.023 77  VAL BBB CA  
4175  C C   . VAL B 77  ? 0.273 0.343 0.261 -0.023 0.023  -0.022 77  VAL BBB C   
4176  O O   . VAL B 77  ? 0.300 0.369 0.287 -0.023 0.024  -0.023 77  VAL BBB O   
4177  C CB  . VAL B 77  ? 0.247 0.323 0.245 -0.024 0.024  -0.026 77  VAL BBB CB  
4178  C CG1 . VAL B 77  ? 0.245 0.323 0.246 -0.026 0.024  -0.028 77  VAL BBB CG1 
4179  C CG2 . VAL B 77  ? 0.243 0.321 0.245 -0.023 0.022  -0.026 77  VAL BBB CG2 
4180  N N   . GLY B 78  ? 0.291 0.359 0.277 -0.022 0.022  -0.020 78  GLY BBB N   
4181  C CA  . GLY B 78  ? 0.290 0.356 0.272 -0.021 0.021  -0.019 78  GLY BBB CA  
4182  C C   . GLY B 78  ? 0.285 0.348 0.263 -0.021 0.021  -0.017 78  GLY BBB C   
4183  O O   . GLY B 78  ? 0.294 0.356 0.268 -0.022 0.022  -0.017 78  GLY BBB O   
4184  N N   . CYS B 79  ? 0.294 0.357 0.273 -0.020 0.019  -0.016 79  CYS BBB N   
4185  C CA  . CYS B 79  ? 0.309 0.370 0.284 -0.019 0.018  -0.015 79  CYS BBB CA  
4186  C C   . CYS B 79  ? 0.292 0.352 0.265 -0.020 0.019  -0.013 79  CYS BBB C   
4187  O O   . CYS B 79  ? 0.310 0.367 0.277 -0.021 0.020  -0.013 79  CYS BBB O   
4188  C CB  . CYS B 79  ? 0.363 0.424 0.341 -0.018 0.017  -0.015 79  CYS BBB CB  
4189  S SG  . CYS B 79  ? 0.391 0.454 0.376 -0.018 0.017  -0.016 79  CYS BBB SG  
4190  N N   . VAL B 80  ? 0.276 0.338 0.253 -0.021 0.018  -0.013 80  VAL BBB N   
4191  C CA  . VAL B 80  ? 0.271 0.333 0.247 -0.021 0.018  -0.012 80  VAL BBB CA  
4192  C C   . VAL B 80  ? 0.276 0.337 0.249 -0.023 0.020  -0.013 80  VAL BBB C   
4193  O O   . VAL B 80  ? 0.284 0.342 0.253 -0.024 0.021  -0.012 80  VAL BBB O   
4194  C CB  . VAL B 80  ? 0.254 0.318 0.234 -0.021 0.017  -0.012 80  VAL BBB CB  
4195  C CG1 . VAL B 80  ? 0.259 0.324 0.238 -0.021 0.017  -0.011 80  VAL BBB CG1 
4196  C CG2 . VAL B 80  ? 0.247 0.310 0.228 -0.019 0.016  -0.010 80  VAL BBB CG2 
4197  N N   . PRO B 81  ? 0.280 0.342 0.255 -0.024 0.022  -0.015 81  PRO BBB N   
4198  C CA  . PRO B 81  ? 0.284 0.346 0.258 -0.026 0.024  -0.016 81  PRO BBB CA  
4199  C C   . PRO B 81  ? 0.298 0.354 0.265 -0.026 0.026  -0.015 81  PRO BBB C   
4200  O O   . PRO B 81  ? 0.312 0.366 0.276 -0.027 0.029  -0.015 81  PRO BBB O   
4201  C CB  . PRO B 81  ? 0.286 0.350 0.264 -0.027 0.025  -0.019 81  PRO BBB CB  
4202  C CG  . PRO B 81  ? 0.292 0.358 0.274 -0.025 0.023  -0.019 81  PRO BBB CG  
4203  C CD  . PRO B 81  ? 0.279 0.345 0.260 -0.023 0.021  -0.016 81  PRO BBB CD  
4204  N N   . LYS B 82  ? 0.311 0.367 0.276 -0.024 0.026  -0.015 82  LYS BBB N   
4205  C CA  . LYS B 82  ? 0.336 0.388 0.295 -0.023 0.027  -0.015 82  LYS BBB CA  
4206  C C   . LYS B 82  ? 0.329 0.378 0.283 -0.023 0.027  -0.013 82  LYS BBB C   
4207  O O   . LYS B 82  ? 0.330 0.375 0.278 -0.023 0.029  -0.012 82  LYS BBB O   
4208  C CB  . LYS B 82  ? 0.380 0.433 0.338 -0.021 0.026  -0.015 82  LYS BBB CB  
4209  C CG  . LYS B 82  ? 0.413 0.463 0.364 -0.019 0.026  -0.015 82  LYS BBB CG  
4210  C CD  . LYS B 82  ? 0.432 0.481 0.381 -0.017 0.024  -0.014 82  LYS BBB CD  
4211  C CE  . LYS B 82  ? 0.430 0.483 0.384 -0.017 0.021  -0.015 82  LYS BBB CE  
4212  N NZ  . LYS B 82  ? 0.446 0.501 0.403 -0.015 0.020  -0.017 82  LYS BBB NZ  
4213  N N   . LYS B 83  ? 0.307 0.358 0.264 -0.022 0.024  -0.012 83  LYS BBB N   
4214  C CA  . LYS B 83  ? 0.304 0.352 0.257 -0.021 0.023  -0.010 83  LYS BBB CA  
4215  C C   . LYS B 83  ? 0.304 0.351 0.256 -0.023 0.025  -0.010 83  LYS BBB C   
4216  O O   . LYS B 83  ? 0.295 0.339 0.242 -0.023 0.026  -0.008 83  LYS BBB O   
4217  C CB  . LYS B 83  ? 0.304 0.355 0.260 -0.021 0.020  -0.010 83  LYS BBB CB  
4218  C CG  . LYS B 83  ? 0.313 0.362 0.266 -0.020 0.019  -0.008 83  LYS BBB CG  
4219  C CD  . LYS B 83  ? 0.320 0.368 0.269 -0.018 0.019  -0.009 83  LYS BBB CD  
4220  C CE  . LYS B 83  ? 0.332 0.377 0.277 -0.017 0.018  -0.007 83  LYS BBB CE  
4221  N NZ  . LYS B 83  ? 0.333 0.380 0.282 -0.016 0.016  -0.008 83  LYS BBB NZ  
4222  N N   . LEU B 84  ? 0.295 0.345 0.251 -0.025 0.025  -0.011 84  LEU BBB N   
4223  C CA  . LEU B 84  ? 0.292 0.342 0.249 -0.027 0.027  -0.011 84  LEU BBB CA  
4224  C C   . LEU B 84  ? 0.308 0.353 0.260 -0.028 0.031  -0.012 84  LEU BBB C   
4225  O O   . LEU B 84  ? 0.303 0.344 0.252 -0.029 0.033  -0.011 84  LEU BBB O   
4226  C CB  . LEU B 84  ? 0.287 0.341 0.251 -0.028 0.026  -0.013 84  LEU BBB CB  
4227  C CG  . LEU B 84  ? 0.273 0.331 0.240 -0.026 0.023  -0.012 84  LEU BBB CG  
4228  C CD1 . LEU B 84  ? 0.263 0.325 0.235 -0.026 0.022  -0.014 84  LEU BBB CD1 
4229  C CD2 . LEU B 84  ? 0.274 0.330 0.238 -0.026 0.022  -0.010 84  LEU BBB CD2 
4230  N N   . MET B 85  ? 0.297 0.341 0.249 -0.028 0.033  -0.013 85  MET BBB N   
4231  C CA  . MET B 85  ? 0.313 0.353 0.260 -0.028 0.037  -0.013 85  MET BBB CA  
4232  C C   . MET B 85  ? 0.287 0.322 0.226 -0.026 0.038  -0.010 85  MET BBB C   
4233  O O   . MET B 85  ? 0.294 0.324 0.229 -0.027 0.041  -0.010 85  MET BBB O   
4234  C CB  . MET B 85  ? 0.342 0.383 0.291 -0.028 0.039  -0.014 85  MET BBB CB  
4235  C CG  . MET B 85  ? 0.372 0.418 0.329 -0.030 0.038  -0.017 85  MET BBB CG  
4236  S SD  . MET B 85  ? 0.423 0.469 0.384 -0.033 0.043  -0.020 85  MET BBB SD  
4237  C CE  . MET B 85  ? 0.452 0.492 0.405 -0.033 0.048  -0.019 85  MET BBB CE  
4238  N N   . HIS B 86  ? 0.276 0.311 0.213 -0.024 0.034  -0.010 86  HIS BBB N   
4239  C CA  . HIS B 86  ? 0.277 0.309 0.207 -0.021 0.034  -0.008 86  HIS BBB CA  
4240  C C   . HIS B 86  ? 0.272 0.301 0.199 -0.021 0.034  -0.006 86  HIS BBB C   
4241  O O   . HIS B 86  ? 0.280 0.303 0.201 -0.020 0.037  -0.005 86  HIS BBB O   
4242  C CB  . HIS B 86  ? 0.282 0.317 0.213 -0.018 0.030  -0.008 86  HIS BBB CB  
4243  C CG  . HIS B 86  ? 0.302 0.335 0.227 -0.015 0.028  -0.007 86  HIS BBB CG  
4244  N ND1 . HIS B 86  ? 0.306 0.334 0.222 -0.013 0.030  -0.007 86  HIS BBB ND1 
4245  C CD2 . HIS B 86  ? 0.306 0.340 0.232 -0.014 0.025  -0.007 86  HIS BBB CD2 
4246  C CE1 . HIS B 86  ? 0.308 0.336 0.221 -0.010 0.028  -0.007 86  HIS BBB CE1 
4247  N NE2 . HIS B 86  ? 0.308 0.339 0.227 -0.011 0.025  -0.007 86  HIS BBB NE2 
4248  N N   . TYR B 87  ? 0.259 0.292 0.193 -0.023 0.032  -0.007 87  TYR BBB N   
4249  C CA  . TYR B 87  ? 0.265 0.296 0.198 -0.024 0.032  -0.006 87  TYR BBB CA  
4250  C C   . TYR B 87  ? 0.259 0.286 0.190 -0.026 0.037  -0.006 87  TYR BBB C   
4251  O O   . TYR B 87  ? 0.249 0.272 0.175 -0.025 0.039  -0.005 87  TYR BBB O   
4252  C CB  . TYR B 87  ? 0.280 0.316 0.220 -0.025 0.029  -0.006 87  TYR BBB CB  
4253  C CG  . TYR B 87  ? 0.328 0.363 0.266 -0.025 0.028  -0.005 87  TYR BBB CG  
4254  C CD1 . TYR B 87  ? 0.368 0.401 0.302 -0.023 0.027  -0.004 87  TYR BBB CD1 
4255  C CD2 . TYR B 87  ? 0.338 0.375 0.280 -0.027 0.029  -0.006 87  TYR BBB CD2 
4256  C CE1 . TYR B 87  ? 0.385 0.417 0.318 -0.024 0.026  -0.003 87  TYR BBB CE1 
4257  C CE2 . TYR B 87  ? 0.359 0.396 0.301 -0.028 0.029  -0.005 87  TYR BBB CE2 
4258  C CZ  . TYR B 87  ? 0.388 0.422 0.325 -0.026 0.027  -0.004 87  TYR BBB CZ  
4259  O OH  . TYR B 87  ? 0.423 0.456 0.359 -0.026 0.027  -0.003 87  TYR BBB OH  
4260  N N   . SER B 88  ? 0.259 0.288 0.194 -0.028 0.039  -0.008 88  SER BBB N   
4261  C CA  . SER B 88  ? 0.263 0.288 0.198 -0.030 0.045  -0.009 88  SER BBB CA  
4262  C C   . SER B 88  ? 0.260 0.277 0.186 -0.028 0.048  -0.007 88  SER BBB C   
4263  O O   . SER B 88  ? 0.264 0.276 0.186 -0.029 0.052  -0.006 88  SER BBB O   
4264  C CB  . SER B 88  ? 0.274 0.303 0.216 -0.033 0.046  -0.012 88  SER BBB CB  
4265  O OG  . SER B 88  ? 0.291 0.316 0.233 -0.035 0.052  -0.013 88  SER BBB OG  
4266  N N   . ALA B 89  ? 0.263 0.280 0.184 -0.026 0.047  -0.006 89  ALA BBB N   
4267  C CA  . ALA B 89  ? 0.278 0.288 0.189 -0.023 0.050  -0.004 89  ALA BBB CA  
4268  C C   . ALA B 89  ? 0.289 0.295 0.194 -0.020 0.049  -0.002 89  ALA BBB C   
4269  O O   . ALA B 89  ? 0.294 0.292 0.191 -0.019 0.053  -0.000 89  ALA BBB O   
4270  C CB  . ALA B 89  ? 0.276 0.288 0.185 -0.020 0.048  -0.005 89  ALA BBB CB  
4271  N N   . LEU B 90  ? 0.287 0.298 0.195 -0.019 0.043  -0.002 90  LEU BBB N   
4272  C CA  . LEU B 90  ? 0.307 0.315 0.210 -0.017 0.042  -0.000 90  LEU BBB CA  
4273  C C   . LEU B 90  ? 0.314 0.318 0.217 -0.019 0.045  0.001  90  LEU BBB C   
4274  O O   . LEU B 90  ? 0.311 0.309 0.207 -0.017 0.046  0.002  90  LEU BBB O   
4275  C CB  . LEU B 90  ? 0.303 0.317 0.210 -0.016 0.036  -0.001 90  LEU BBB CB  
4276  C CG  . LEU B 90  ? 0.300 0.317 0.207 -0.013 0.033  -0.002 90  LEU BBB CG  
4277  C CD1 . LEU B 90  ? 0.294 0.317 0.207 -0.013 0.028  -0.002 90  LEU BBB CD1 
4278  C CD2 . LEU B 90  ? 0.302 0.314 0.199 -0.009 0.033  -0.001 90  LEU BBB CD2 
4279  N N   . ILE B 91  ? 0.343 0.350 0.253 -0.023 0.046  -0.001 91  ILE BBB N   
4280  C CA  . ILE B 91  ? 0.350 0.355 0.262 -0.026 0.049  -0.001 91  ILE BBB CA  
4281  C C   . ILE B 91  ? 0.375 0.371 0.281 -0.026 0.056  -0.001 91  ILE BBB C   
4282  O O   . ILE B 91  ? 0.378 0.369 0.279 -0.025 0.058  0.001  91  ILE BBB O   
4283  C CB  . ILE B 91  ? 0.332 0.343 0.254 -0.029 0.048  -0.004 91  ILE BBB CB  
4284  C CG1 . ILE B 91  ? 0.322 0.339 0.248 -0.029 0.042  -0.004 91  ILE BBB CG1 
4285  C CG2 . ILE B 91  ? 0.335 0.344 0.259 -0.032 0.053  -0.005 91  ILE BBB CG2 
4286  C CD1 . ILE B 91  ? 0.319 0.343 0.254 -0.031 0.041  -0.007 91  ILE BBB CD1 
4287  N N   . ALA B 92  ? 0.381 0.377 0.287 -0.027 0.059  -0.002 92  ALA BBB N   
4288  C CA  . ALA B 92  ? 0.402 0.389 0.301 -0.026 0.066  -0.001 92  ALA BBB CA  
4289  C C   . ALA B 92  ? 0.414 0.393 0.301 -0.021 0.066  0.003  92  ALA BBB C   
4290  O O   . ALA B 92  ? 0.407 0.379 0.290 -0.021 0.071  0.004  92  ALA BBB O   
4291  C CB  . ALA B 92  ? 0.399 0.387 0.299 -0.026 0.067  -0.002 92  ALA BBB CB  
4292  N N   . SER B 93  ? 0.427 0.409 0.311 -0.018 0.061  0.004  93  SER BBB N   
4293  C CA  . SER B 93  ? 0.453 0.429 0.325 -0.012 0.061  0.006  93  SER BBB CA  
4294  C C   . SER B 93  ? 0.442 0.415 0.312 -0.012 0.060  0.008  93  SER BBB C   
4295  O O   . SER B 93  ? 0.448 0.412 0.309 -0.009 0.064  0.010  93  SER BBB O   
4296  C CB  . SER B 93  ? 0.456 0.438 0.328 -0.009 0.055  0.006  93  SER BBB CB  
4297  O OG  . SER B 93  ? 0.511 0.489 0.372 -0.004 0.053  0.007  93  SER BBB OG  
4298  N N   . SER B 94  ? 0.417 0.397 0.295 -0.014 0.056  0.007  94  SER BBB N   
4299  C CA  . SER B 94  ? 0.425 0.404 0.303 -0.014 0.055  0.007  94  SER BBB CA  
4300  C C   . SER B 94  ? 0.421 0.393 0.298 -0.016 0.061  0.008  94  SER BBB C   
4301  O O   . SER B 94  ? 0.422 0.388 0.293 -0.014 0.063  0.010  94  SER BBB O   
4302  C CB  . SER B 94  ? 0.421 0.409 0.308 -0.016 0.049  0.006  94  SER BBB CB  
4303  O OG  . SER B 94  ? 0.494 0.481 0.384 -0.018 0.050  0.006  94  SER BBB OG  
4304  N N   . ILE B 95  ? 0.414 0.387 0.297 -0.021 0.065  0.006  95  ILE BBB N   
4305  C CA  . ILE B 95  ? 0.419 0.386 0.304 -0.024 0.072  0.006  95  ILE BBB CA  
4306  C C   . ILE B 95  ? 0.413 0.369 0.286 -0.021 0.079  0.008  95  ILE BBB C   
4307  O O   . ILE B 95  ? 0.401 0.349 0.270 -0.021 0.083  0.010  95  ILE BBB O   
4308  C CB  . ILE B 95  ? 0.432 0.405 0.328 -0.029 0.074  0.002  95  ILE BBB CB  
4309  C CG1 . ILE B 95  ? 0.399 0.381 0.304 -0.031 0.069  -0.001 95  ILE BBB CG1 
4310  C CG2 . ILE B 95  ? 0.451 0.416 0.346 -0.032 0.083  0.001  95  ILE BBB CG2 
4311  C CD1 . ILE B 95  ? 0.402 0.390 0.318 -0.036 0.070  -0.005 95  ILE BBB CD1 
4312  N N   . HIS B 96  ? 0.423 0.377 0.292 -0.019 0.080  0.009  96  HIS BBB N   
4313  C CA  . HIS B 96  ? 0.460 0.403 0.317 -0.015 0.086  0.012  96  HIS BBB CA  
4314  C C   . HIS B 96  ? 0.475 0.412 0.321 -0.010 0.084  0.015  96  HIS BBB C   
4315  O O   . HIS B 96  ? 0.467 0.394 0.306 -0.008 0.090  0.018  96  HIS BBB O   
4316  C CB  . HIS B 96  ? 0.484 0.427 0.338 -0.014 0.086  0.012  96  HIS BBB CB  
4317  C CG  . HIS B 96  ? 0.560 0.492 0.401 -0.010 0.093  0.015  96  HIS BBB CG  
4318  N ND1 . HIS B 96  ? 0.619 0.548 0.448 -0.004 0.091  0.017  96  HIS BBB ND1 
4319  C CD2 . HIS B 96  ? 0.594 0.517 0.433 -0.012 0.103  0.015  96  HIS BBB CD2 
4320  C CE1 . HIS B 96  ? 0.631 0.549 0.451 -0.001 0.099  0.020  96  HIS BBB CE1 
4321  N NE2 . HIS B 96  ? 0.632 0.545 0.457 -0.006 0.106  0.019  96  HIS BBB NE2 
4322  N N   . HIS B 97  ? 0.480 0.424 0.325 -0.006 0.076  0.015  97  HIS BBB N   
4323  C CA  . HIS B 97  ? 0.474 0.413 0.307 0.001  0.074  0.018  97  HIS BBB CA  
4324  C C   . HIS B 97  ? 0.477 0.417 0.312 0.001  0.071  0.018  97  HIS BBB C   
4325  O O   . HIS B 97  ? 0.517 0.449 0.341 0.005  0.073  0.021  97  HIS BBB O   
4326  C CB  . HIS B 97  ? 0.459 0.405 0.291 0.004  0.067  0.017  97  HIS BBB CB  
4327  C CG  . HIS B 97  ? 0.455 0.400 0.282 0.006  0.069  0.017  97  HIS BBB CG  
4328  N ND1 . HIS B 97  ? 0.456 0.390 0.270 0.011  0.074  0.020  97  HIS BBB ND1 
4329  C CD2 . HIS B 97  ? 0.449 0.401 0.282 0.004  0.067  0.014  97  HIS BBB CD2 
4330  C CE1 . HIS B 97  ? 0.471 0.407 0.284 0.011  0.075  0.019  97  HIS BBB CE1 
4331  N NE2 . HIS B 97  ? 0.457 0.404 0.282 0.007  0.070  0.016  97  HIS BBB NE2 
4332  N N   . ASP B 98  ? 0.462 0.409 0.307 -0.004 0.067  0.016  98  ASP BBB N   
4333  C CA  . ASP B 98  ? 0.454 0.405 0.301 -0.003 0.062  0.016  98  ASP BBB CA  
4334  C C   . ASP B 98  ? 0.444 0.394 0.298 -0.007 0.065  0.015  98  ASP BBB C   
4335  O O   . ASP B 98  ? 0.412 0.359 0.262 -0.005 0.064  0.016  98  ASP BBB O   
4336  C CB  . ASP B 98  ? 0.444 0.407 0.300 -0.004 0.055  0.013  98  ASP BBB CB  
4337  C CG  . ASP B 98  ? 0.439 0.405 0.291 0.000  0.051  0.013  98  ASP BBB CG  
4338  O OD1 . ASP B 98  ? 0.447 0.407 0.289 0.005  0.053  0.015  98  ASP BBB OD1 
4339  O OD2 . ASP B 98  ? 0.431 0.405 0.290 -0.001 0.046  0.011  98  ASP BBB OD2 
4340  N N   . ALA B 99  ? 0.451 0.403 0.313 -0.013 0.068  0.013  99  ALA BBB N   
4341  C CA  . ALA B 99  ? 0.476 0.430 0.346 -0.017 0.070  0.011  99  ALA BBB CA  
4342  C C   . ALA B 99  ? 0.514 0.459 0.379 -0.016 0.075  0.013  99  ALA BBB C   
4343  O O   . ALA B 99  ? 0.530 0.476 0.396 -0.017 0.072  0.013  99  ALA BBB O   
4344  C CB  . ALA B 99  ? 0.471 0.429 0.351 -0.022 0.073  0.008  99  ALA BBB CB  
4345  N N   . GLN B 100 ? 0.546 0.481 0.403 -0.015 0.082  0.015  100 GLN BBB N   
4346  C CA  . GLN B 100 ? 0.580 0.504 0.431 -0.014 0.088  0.017  100 GLN BBB CA  
4347  C C   . GLN B 100 ? 0.552 0.473 0.394 -0.008 0.084  0.020  100 GLN BBB C   
4348  O O   . GLN B 100 ? 0.566 0.485 0.410 -0.009 0.085  0.020  100 GLN BBB O   
4349  C CB  . GLN B 100 ? 0.619 0.532 0.463 -0.013 0.097  0.019  100 GLN BBB CB  
4350  C CG  . GLN B 100 ? 0.662 0.563 0.498 -0.012 0.104  0.022  100 GLN BBB CG  
4351  C CD  . GLN B 100 ? 0.737 0.627 0.569 -0.012 0.114  0.023  100 GLN BBB CD  
4352  O OE1 . GLN B 100 ? 0.724 0.616 0.557 -0.013 0.116  0.022  100 GLN BBB OE1 
4353  N NE2 . GLN B 100 ? 0.725 0.604 0.553 -0.012 0.122  0.025  100 GLN BBB NE2 
4354  N N   . MET B 101 ? 0.511 0.433 0.346 -0.003 0.079  0.022  101 MET BBB N   
4355  C CA  . MET B 101 ? 0.518 0.439 0.345 0.003  0.075  0.023  101 MET BBB CA  
4356  C C   . MET B 101 ? 0.495 0.424 0.330 0.001  0.069  0.022  101 MET BBB C   
4357  O O   . MET B 101 ? 0.542 0.468 0.372 0.004  0.068  0.023  101 MET BBB O   
4358  C CB  . MET B 101 ? 0.525 0.449 0.346 0.008  0.070  0.024  101 MET BBB CB  
4359  C CG  . MET B 101 ? 0.545 0.460 0.354 0.013  0.075  0.027  101 MET BBB CG  
4360  S SD  . MET B 101 ? 0.607 0.507 0.401 0.019  0.081  0.031  101 MET BBB SD  
4361  C CE  . MET B 101 ? 0.586 0.491 0.375 0.025  0.072  0.031  101 MET BBB CE  
4362  N N   . PHE B 102 ? 0.443 0.382 0.289 -0.004 0.066  0.019  102 PHE BBB N   
4363  C CA  . PHE B 102 ? 0.438 0.385 0.292 -0.006 0.060  0.017  102 PHE BBB CA  
4364  C C   . PHE B 102 ? 0.431 0.378 0.293 -0.011 0.063  0.015  102 PHE BBB C   
4365  O O   . PHE B 102 ? 0.410 0.365 0.279 -0.014 0.059  0.013  102 PHE BBB O   
4366  C CB  . PHE B 102 ? 0.423 0.381 0.284 -0.007 0.054  0.015  102 PHE BBB CB  
4367  C CG  . PHE B 102 ? 0.424 0.383 0.278 -0.001 0.049  0.015  102 PHE BBB CG  
4368  C CD1 . PHE B 102 ? 0.419 0.375 0.267 0.002  0.050  0.016  102 PHE BBB CD1 
4369  C CD2 . PHE B 102 ? 0.435 0.398 0.290 0.001  0.044  0.015  102 PHE BBB CD2 
4370  C CE1 . PHE B 102 ? 0.430 0.387 0.272 0.008  0.046  0.016  102 PHE BBB CE1 
4371  C CE2 . PHE B 102 ? 0.425 0.390 0.275 0.006  0.039  0.015  102 PHE BBB CE2 
4372  C CZ  . PHE B 102 ? 0.413 0.375 0.256 0.009  0.041  0.015  102 PHE BBB CZ  
4373  N N   . GLY B 103 ? 0.451 0.390 0.310 -0.012 0.071  0.016  103 GLY BBB N   
4374  C CA  . GLY B 103 ? 0.438 0.374 0.303 -0.016 0.075  0.015  103 GLY BBB CA  
4375  C C   . GLY B 103 ? 0.443 0.383 0.318 -0.022 0.078  0.011  103 GLY BBB C   
4376  O O   . GLY B 103 ? 0.432 0.373 0.314 -0.026 0.081  0.009  103 GLY BBB O   
4377  N N   . HIS B 104 ? 0.454 0.400 0.331 -0.023 0.077  0.010  104 HIS BBB N   
4378  C CA  . HIS B 104 ? 0.467 0.419 0.355 -0.028 0.078  0.007  104 HIS BBB CA  
4379  C C   . HIS B 104 ? 0.499 0.443 0.384 -0.029 0.086  0.007  104 HIS BBB C   
4380  O O   . HIS B 104 ? 0.499 0.443 0.380 -0.027 0.085  0.008  104 HIS BBB O   
4381  C CB  . HIS B 104 ? 0.444 0.406 0.337 -0.029 0.071  0.005  104 HIS BBB CB  
4382  C CG  . HIS B 104 ? 0.413 0.382 0.309 -0.028 0.064  0.005  104 HIS BBB CG  
4383  N ND1 . HIS B 104 ? 0.401 0.376 0.306 -0.031 0.063  0.002  104 HIS BBB ND1 
4384  C CD2 . HIS B 104 ? 0.410 0.381 0.301 -0.024 0.059  0.007  104 HIS BBB CD2 
4385  C CE1 . HIS B 104 ? 0.392 0.372 0.297 -0.030 0.057  0.002  104 HIS BBB CE1 
4386  N NE2 . HIS B 104 ? 0.397 0.375 0.294 -0.026 0.055  0.005  104 HIS BBB NE2 
4387  N N   . LYS B 105 ? 0.562 0.498 0.447 -0.031 0.094  0.006  105 LYS BBB N   
4388  C CA  . LYS B 105 ? 0.605 0.534 0.489 -0.033 0.102  0.006  105 LYS BBB CA  
4389  C C   . LYS B 105 ? 0.587 0.526 0.484 -0.038 0.102  0.001  105 LYS BBB C   
4390  O O   . LYS B 105 ? 0.564 0.509 0.471 -0.042 0.101  -0.003 105 LYS BBB O   
4391  C CB  . LYS B 105 ? 0.650 0.569 0.533 -0.034 0.111  0.007  105 LYS BBB CB  
4392  C CG  . LYS B 105 ? 0.698 0.607 0.578 -0.036 0.121  0.007  105 LYS BBB CG  
4393  C CD  . LYS B 105 ? 0.744 0.644 0.610 -0.030 0.123  0.012  105 LYS BBB CD  
4394  C CE  . LYS B 105 ? 0.753 0.647 0.617 -0.031 0.131  0.012  105 LYS BBB CE  
4395  N NZ  . LYS B 105 ? 0.745 0.629 0.612 -0.034 0.142  0.011  105 LYS BBB NZ  
4396  N N   . THR B 106 ? 0.579 0.519 0.474 -0.037 0.102  0.002  106 THR BBB N   
4397  C CA  . THR B 106 ? 0.585 0.534 0.491 -0.041 0.100  -0.003 106 THR BBB CA  
4398  C C   . THR B 106 ? 0.566 0.509 0.471 -0.042 0.108  -0.003 106 THR BBB C   
4399  O O   . THR B 106 ? 0.627 0.561 0.521 -0.039 0.111  0.001  106 THR BBB O   
4400  C CB  . THR B 106 ? 0.576 0.533 0.480 -0.038 0.091  -0.002 106 THR BBB CB  
4401  O OG1 . THR B 106 ? 0.635 0.584 0.528 -0.034 0.093  0.002  106 THR BBB OG1 
4402  C CG2 . THR B 106 ? 0.556 0.518 0.460 -0.036 0.084  -0.001 106 THR BBB CG2 
4403  N N   . SER B 107 ? 0.529 0.477 0.445 -0.047 0.110  -0.009 107 SER BBB N   
4404  C CA  . SER B 107 ? 0.532 0.479 0.450 -0.049 0.116  -0.010 107 SER BBB CA  
4405  C C   . SER B 107 ? 0.500 0.460 0.428 -0.051 0.109  -0.014 107 SER BBB C   
4406  O O   . SER B 107 ? 0.514 0.483 0.450 -0.052 0.104  -0.017 107 SER BBB O   
4407  C CB  . SER B 107 ? 0.537 0.478 0.460 -0.053 0.126  -0.013 107 SER BBB CB  
4408  O OG  . SER B 107 ? 0.513 0.460 0.449 -0.057 0.125  -0.019 107 SER BBB OG  
4409  N N   . SER B 108 ? 0.489 0.450 0.414 -0.050 0.109  -0.013 108 SER BBB N   
4410  C CA  . SER B 108 ? 0.474 0.445 0.405 -0.050 0.102  -0.015 108 SER BBB CA  
4411  C C   . SER B 108 ? 0.483 0.454 0.417 -0.052 0.107  -0.018 108 SER BBB C   
4412  O O   . SER B 108 ? 0.507 0.467 0.432 -0.050 0.113  -0.015 108 SER BBB O   
4413  C CB  . SER B 108 ? 0.467 0.440 0.390 -0.045 0.095  -0.011 108 SER BBB CB  
4414  O OG  . SER B 108 ? 0.460 0.443 0.389 -0.045 0.088  -0.013 108 SER BBB OG  
4415  N N   . SER B 109 ? 0.462 0.443 0.407 -0.054 0.104  -0.022 109 SER BBB N   
4416  C CA  . SER B 109 ? 0.460 0.443 0.407 -0.055 0.106  -0.024 109 SER BBB CA  
4417  C C   . SER B 109 ? 0.428 0.422 0.380 -0.054 0.097  -0.026 109 SER BBB C   
4418  O O   . SER B 109 ? 0.434 0.436 0.394 -0.055 0.092  -0.028 109 SER BBB O   
4419  C CB  . SER B 109 ? 0.463 0.444 0.418 -0.060 0.114  -0.029 109 SER BBB CB  
4420  O OG  . SER B 109 ? 0.444 0.432 0.411 -0.063 0.114  -0.034 109 SER BBB OG  
4421  N N   . PHE B 110 ? 0.439 0.433 0.387 -0.052 0.096  -0.024 110 PHE BBB N   
4422  C CA  . PHE B 110 ? 0.450 0.453 0.401 -0.050 0.089  -0.024 110 PHE BBB CA  
4423  C C   . PHE B 110 ? 0.435 0.445 0.398 -0.054 0.089  -0.030 110 PHE BBB C   
4424  O O   . PHE B 110 ? 0.462 0.468 0.426 -0.056 0.096  -0.032 110 PHE BBB O   
4425  C CB  . PHE B 110 ? 0.430 0.428 0.371 -0.047 0.088  -0.020 110 PHE BBB CB  
4426  C CG  . PHE B 110 ? 0.407 0.414 0.351 -0.045 0.081  -0.021 110 PHE BBB CG  
4427  C CD1 . PHE B 110 ? 0.380 0.394 0.328 -0.044 0.073  -0.020 110 PHE BBB CD1 
4428  C CD2 . PHE B 110 ? 0.381 0.389 0.327 -0.046 0.082  -0.022 110 PHE BBB CD2 
4429  C CE1 . PHE B 110 ? 0.358 0.379 0.310 -0.043 0.068  -0.021 110 PHE BBB CE1 
4430  C CE2 . PHE B 110 ? 0.363 0.380 0.314 -0.044 0.076  -0.023 110 PHE BBB CE2 
4431  C CZ  . PHE B 110 ? 0.348 0.371 0.302 -0.043 0.069  -0.022 110 PHE BBB CZ  
4432  N N   . GLU B 111 ? 0.424 0.445 0.394 -0.054 0.083  -0.032 111 GLU BBB N   
4433  C CA  . GLU B 111 ? 0.436 0.465 0.418 -0.056 0.082  -0.038 111 GLU BBB CA  
4434  C C   . GLU B 111 ? 0.410 0.445 0.392 -0.053 0.075  -0.037 111 GLU BBB C   
4435  O O   . GLU B 111 ? 0.418 0.459 0.402 -0.051 0.069  -0.037 111 GLU BBB O   
4436  C CB  . GLU B 111 ? 0.445 0.480 0.436 -0.058 0.082  -0.043 111 GLU BBB CB  
4437  C CG  . GLU B 111 ? 0.500 0.528 0.491 -0.061 0.089  -0.044 111 GLU BBB CG  
4438  C CD  . GLU B 111 ? 0.555 0.578 0.549 -0.065 0.099  -0.047 111 GLU BBB CD  
4439  O OE1 . GLU B 111 ? 0.582 0.596 0.573 -0.066 0.106  -0.046 111 GLU BBB OE1 
4440  O OE2 . GLU B 111 ? 0.574 0.600 0.573 -0.066 0.100  -0.050 111 GLU BBB OE2 
4441  N N   . TRP B 112 ? 0.384 0.418 0.365 -0.053 0.077  -0.037 112 TRP BBB N   
4442  C CA  . TRP B 112 ? 0.363 0.402 0.343 -0.050 0.071  -0.035 112 TRP BBB CA  
4443  C C   . TRP B 112 ? 0.349 0.398 0.338 -0.050 0.065  -0.039 112 TRP BBB C   
4444  O O   . TRP B 112 ? 0.310 0.362 0.297 -0.047 0.059  -0.036 112 TRP BBB O   
4445  C CB  . TRP B 112 ? 0.351 0.387 0.329 -0.051 0.076  -0.036 112 TRP BBB CB  
4446  C CG  . TRP B 112 ? 0.343 0.384 0.323 -0.049 0.071  -0.036 112 TRP BBB CG  
4447  C CD1 . TRP B 112 ? 0.325 0.375 0.314 -0.050 0.069  -0.040 112 TRP BBB CD1 
4448  C CD2 . TRP B 112 ? 0.330 0.369 0.302 -0.045 0.067  -0.032 112 TRP BBB CD2 
4449  N NE1 . TRP B 112 ? 0.324 0.376 0.312 -0.047 0.064  -0.038 112 TRP BBB NE1 
4450  C CE2 . TRP B 112 ? 0.319 0.365 0.296 -0.045 0.063  -0.033 112 TRP BBB CE2 
4451  C CE3 . TRP B 112 ? 0.334 0.367 0.296 -0.043 0.066  -0.027 112 TRP BBB CE3 
4452  C CZ2 . TRP B 112 ? 0.319 0.365 0.292 -0.042 0.059  -0.031 112 TRP BBB CZ2 
4453  C CZ3 . TRP B 112 ? 0.331 0.365 0.289 -0.040 0.062  -0.025 112 TRP BBB CZ3 
4454  C CH2 . TRP B 112 ? 0.316 0.356 0.280 -0.039 0.059  -0.027 112 TRP BBB CH2 
4455  N N   . GLY B 113 ? 0.347 0.401 0.346 -0.053 0.067  -0.045 113 GLY BBB N   
4456  C CA  . GLY B 113 ? 0.341 0.406 0.349 -0.052 0.062  -0.048 113 GLY BBB CA  
4457  C C   . GLY B 113 ? 0.333 0.401 0.340 -0.050 0.056  -0.047 113 GLY BBB C   
4458  O O   . GLY B 113 ? 0.316 0.391 0.327 -0.048 0.050  -0.048 113 GLY BBB O   
4459  N N   . LYS B 114 ? 0.334 0.398 0.337 -0.051 0.058  -0.045 114 LYS BBB N   
4460  C CA  . LYS B 114 ? 0.335 0.401 0.337 -0.049 0.053  -0.043 114 LYS BBB CA  
4461  C C   . LYS B 114 ? 0.331 0.395 0.325 -0.045 0.048  -0.038 114 LYS BBB C   
4462  O O   . LYS B 114 ? 0.314 0.383 0.309 -0.043 0.043  -0.038 114 LYS BBB O   
4463  C CB  . LYS B 114 ? 0.350 0.409 0.348 -0.051 0.057  -0.043 114 LYS BBB CB  
4464  C CG  . LYS B 114 ? 0.355 0.417 0.352 -0.049 0.053  -0.041 114 LYS BBB CG  
4465  C CD  . LYS B 114 ? 0.370 0.442 0.375 -0.048 0.048  -0.045 114 LYS BBB CD  
4466  C CE  . LYS B 114 ? 0.400 0.473 0.402 -0.046 0.044  -0.044 114 LYS BBB CE  
4467  N NZ  . LYS B 114 ? 0.427 0.510 0.437 -0.045 0.040  -0.049 114 LYS BBB NZ  
4468  N N   . LEU B 115 ? 0.338 0.395 0.325 -0.045 0.050  -0.034 115 LEU BBB N   
4469  C CA  . LEU B 115 ? 0.343 0.399 0.324 -0.042 0.046  -0.029 115 LEU BBB CA  
4470  C C   . LEU B 115 ? 0.349 0.411 0.334 -0.040 0.042  -0.030 115 LEU BBB C   
4471  O O   . LEU B 115 ? 0.355 0.419 0.339 -0.038 0.038  -0.028 115 LEU BBB O   
4472  C CB  . LEU B 115 ? 0.352 0.399 0.324 -0.041 0.050  -0.026 115 LEU BBB CB  
4473  C CG  . LEU B 115 ? 0.344 0.390 0.310 -0.038 0.046  -0.022 115 LEU BBB CG  
4474  C CD1 . LEU B 115 ? 0.333 0.380 0.297 -0.036 0.042  -0.020 115 LEU BBB CD1 
4475  C CD2 . LEU B 115 ? 0.350 0.389 0.308 -0.038 0.050  -0.020 115 LEU BBB CD2 
4476  N N   . VAL B 116 ? 0.361 0.424 0.350 -0.042 0.045  -0.033 116 VAL BBB N   
4477  C CA  . VAL B 116 ? 0.335 0.404 0.329 -0.040 0.042  -0.035 116 VAL BBB CA  
4478  C C   . VAL B 116 ? 0.310 0.387 0.310 -0.039 0.037  -0.037 116 VAL BBB C   
4479  O O   . VAL B 116 ? 0.290 0.368 0.289 -0.036 0.033  -0.035 116 VAL BBB O   
4480  C CB  . VAL B 116 ? 0.320 0.391 0.320 -0.043 0.046  -0.039 116 VAL BBB CB  
4481  C CG1 . VAL B 116 ? 0.315 0.394 0.322 -0.041 0.042  -0.042 116 VAL BBB CG1 
4482  C CG2 . VAL B 116 ? 0.328 0.392 0.322 -0.043 0.049  -0.037 116 VAL BBB CG2 
4483  N N   . GLU B 117 ? 0.314 0.393 0.318 -0.041 0.038  -0.040 117 GLU BBB N   
4484  C CA  . GLU B 117 ? 0.329 0.415 0.338 -0.039 0.034  -0.043 117 GLU BBB CA  
4485  C C   . GLU B 117 ? 0.302 0.387 0.305 -0.036 0.030  -0.038 117 GLU BBB C   
4486  O O   . GLU B 117 ? 0.279 0.367 0.282 -0.033 0.025  -0.037 117 GLU BBB O   
4487  C CB  . GLU B 117 ? 0.340 0.429 0.355 -0.041 0.036  -0.048 117 GLU BBB CB  
4488  C CG  . GLU B 117 ? 0.386 0.483 0.405 -0.039 0.032  -0.051 117 GLU BBB CG  
4489  C CD  . GLU B 117 ? 0.421 0.521 0.446 -0.042 0.035  -0.056 117 GLU BBB CD  
4490  O OE1 . GLU B 117 ? 0.449 0.547 0.470 -0.042 0.034  -0.055 117 GLU BBB OE1 
4491  O OE2 . GLU B 117 ? 0.468 0.571 0.500 -0.044 0.037  -0.062 117 GLU BBB OE2 
4492  N N   . THR B 118 ? 0.280 0.358 0.276 -0.037 0.031  -0.034 118 THR BBB N   
4493  C CA  . THR B 118 ? 0.279 0.355 0.270 -0.034 0.028  -0.030 118 THR BBB CA  
4494  C C   . THR B 118 ? 0.277 0.353 0.266 -0.032 0.025  -0.027 118 THR BBB C   
4495  O O   . THR B 118 ? 0.253 0.330 0.241 -0.029 0.022  -0.025 118 THR BBB O   
4496  C CB  . THR B 118 ? 0.294 0.364 0.279 -0.036 0.031  -0.027 118 THR BBB CB  
4497  O OG1 . THR B 118 ? 0.271 0.342 0.259 -0.037 0.032  -0.030 118 THR BBB OG1 
4498  C CG2 . THR B 118 ? 0.301 0.368 0.280 -0.033 0.028  -0.023 118 THR BBB CG2 
4499  N N   . LEU B 119 ? 0.282 0.355 0.270 -0.033 0.028  -0.026 119 LEU BBB N   
4500  C CA  . LEU B 119 ? 0.289 0.362 0.276 -0.031 0.025  -0.024 119 LEU BBB CA  
4501  C C   . LEU B 119 ? 0.281 0.360 0.273 -0.029 0.022  -0.026 119 LEU BBB C   
4502  O O   . LEU B 119 ? 0.272 0.351 0.263 -0.026 0.019  -0.024 119 LEU BBB O   
4503  C CB  . LEU B 119 ? 0.312 0.382 0.298 -0.032 0.028  -0.025 119 LEU BBB CB  
4504  C CG  . LEU B 119 ? 0.324 0.388 0.302 -0.031 0.030  -0.021 119 LEU BBB CG  
4505  C CD1 . LEU B 119 ? 0.337 0.397 0.311 -0.033 0.032  -0.021 119 LEU BBB CD1 
4506  C CD2 . LEU B 119 ? 0.352 0.414 0.329 -0.032 0.032  -0.022 119 LEU BBB CD2 
4507  N N   . ARG B 120 ? 0.286 0.369 0.284 -0.030 0.024  -0.030 120 ARG BBB N   
4508  C CA  A ARG B 120 ? 0.288 0.377 0.292 -0.028 0.021  -0.033 120 ARG BBB CA  
4509  C CA  B ARG B 120 ? 0.292 0.381 0.296 -0.028 0.021  -0.033 120 ARG BBB CA  
4510  C C   . ARG B 120 ? 0.289 0.381 0.292 -0.025 0.017  -0.032 120 ARG BBB C   
4511  O O   . ARG B 120 ? 0.298 0.392 0.301 -0.022 0.014  -0.030 120 ARG BBB O   
4512  C CB  A ARG B 120 ? 0.296 0.391 0.307 -0.030 0.023  -0.039 120 ARG BBB CB  
4513  C CB  B ARG B 120 ? 0.306 0.400 0.317 -0.030 0.022  -0.039 120 ARG BBB CB  
4514  C CG  A ARG B 120 ? 0.304 0.398 0.317 -0.031 0.025  -0.040 120 ARG BBB CG  
4515  C CG  B ARG B 120 ? 0.321 0.413 0.332 -0.032 0.026  -0.040 120 ARG BBB CG  
4516  C CD  A ARG B 120 ? 0.308 0.409 0.330 -0.032 0.026  -0.047 120 ARG BBB CD  
4517  C CD  B ARG B 120 ? 0.332 0.428 0.348 -0.031 0.026  -0.042 120 ARG BBB CD  
4518  N NE  A ARG B 120 ? 0.318 0.416 0.341 -0.036 0.031  -0.050 120 ARG BBB NE  
4519  N NE  B ARG B 120 ? 0.342 0.445 0.363 -0.028 0.021  -0.044 120 ARG BBB NE  
4520  C CZ  A ARG B 120 ? 0.324 0.425 0.350 -0.038 0.032  -0.053 120 ARG BBB CZ  
4521  C CZ  B ARG B 120 ? 0.345 0.454 0.374 -0.029 0.021  -0.050 120 ARG BBB CZ  
4522  N NH1 A ARG B 120 ? 0.319 0.424 0.346 -0.036 0.028  -0.053 120 ARG BBB NH1 
4523  N NH1 B ARG B 120 ? 0.366 0.474 0.398 -0.032 0.026  -0.053 120 ARG BBB NH1 
4524  N NH2 A ARG B 120 ? 0.333 0.431 0.361 -0.042 0.038  -0.055 120 ARG BBB NH2 
4525  N NH2 B ARG B 120 ? 0.334 0.449 0.366 -0.025 0.017  -0.051 120 ARG BBB NH2 
4526  N N   . ASN B 121 ? 0.307 0.399 0.309 -0.026 0.017  -0.033 121 ASN BBB N   
4527  C CA  . ASN B 121 ? 0.332 0.428 0.333 -0.023 0.014  -0.032 121 ASN BBB CA  
4528  C C   . ASN B 121 ? 0.338 0.429 0.334 -0.020 0.012  -0.026 121 ASN BBB C   
4529  O O   . ASN B 121 ? 0.373 0.465 0.368 -0.017 0.009  -0.025 121 ASN BBB O   
4530  C CB  . ASN B 121 ? 0.348 0.444 0.349 -0.024 0.014  -0.034 121 ASN BBB CB  
4531  C CG  . ASN B 121 ? 0.384 0.486 0.392 -0.026 0.016  -0.040 121 ASN BBB CG  
4532  O OD1 . ASN B 121 ? 0.410 0.515 0.423 -0.026 0.016  -0.043 121 ASN BBB OD1 
4533  N ND2 . ASN B 121 ? 0.376 0.477 0.384 -0.028 0.018  -0.042 121 ASN BBB ND2 
4534  N N   . HIS B 122 ? 0.327 0.412 0.318 -0.022 0.014  -0.023 122 HIS BBB N   
4535  C CA  . HIS B 122 ? 0.319 0.400 0.306 -0.021 0.013  -0.019 122 HIS BBB CA  
4536  C C   . HIS B 122 ? 0.313 0.394 0.301 -0.019 0.012  -0.018 122 HIS BBB C   
4537  O O   . HIS B 122 ? 0.304 0.384 0.291 -0.016 0.010  -0.015 122 HIS BBB O   
4538  C CB  . HIS B 122 ? 0.314 0.389 0.296 -0.023 0.015  -0.017 122 HIS BBB CB  
4539  C CG  . HIS B 122 ? 0.310 0.382 0.289 -0.021 0.014  -0.013 122 HIS BBB CG  
4540  N ND1 . HIS B 122 ? 0.324 0.396 0.300 -0.020 0.013  -0.011 122 HIS BBB ND1 
4541  C CD2 . HIS B 122 ? 0.312 0.382 0.290 -0.020 0.014  -0.011 122 HIS BBB CD2 
4542  C CE1 . HIS B 122 ? 0.329 0.398 0.303 -0.019 0.012  -0.008 122 HIS BBB CE1 
4543  N NE2 . HIS B 122 ? 0.330 0.398 0.305 -0.019 0.013  -0.008 122 HIS BBB NE2 
4544  N N   . ILE B 123 ? 0.323 0.404 0.314 -0.020 0.013  -0.019 123 ILE BBB N   
4545  C CA  . ILE B 123 ? 0.323 0.405 0.316 -0.018 0.013  -0.019 123 ILE BBB CA  
4546  C C   . ILE B 123 ? 0.336 0.422 0.332 -0.015 0.010  -0.020 123 ILE BBB C   
4547  O O   . ILE B 123 ? 0.329 0.414 0.324 -0.012 0.009  -0.018 123 ILE BBB O   
4548  C CB  . ILE B 123 ? 0.305 0.387 0.300 -0.021 0.015  -0.021 123 ILE BBB CB  
4549  C CG1 . ILE B 123 ? 0.306 0.383 0.297 -0.022 0.017  -0.019 123 ILE BBB CG1 
4550  C CG2 . ILE B 123 ? 0.297 0.380 0.295 -0.019 0.014  -0.022 123 ILE BBB CG2 
4551  C CD1 . ILE B 123 ? 0.291 0.366 0.281 -0.025 0.020  -0.021 123 ILE BBB CD1 
4552  N N   . ARG B 124 ? 0.350 0.441 0.349 -0.015 0.009  -0.024 124 ARG BBB N   
4553  C CA  . ARG B 124 ? 0.366 0.462 0.367 -0.011 0.006  -0.025 124 ARG BBB CA  
4554  C C   . ARG B 124 ? 0.358 0.452 0.355 -0.008 0.005  -0.021 124 ARG BBB C   
4555  O O   . ARG B 124 ? 0.391 0.484 0.386 -0.004 0.003  -0.019 124 ARG BBB O   
4556  C CB  . ARG B 124 ? 0.383 0.485 0.388 -0.012 0.006  -0.030 124 ARG BBB CB  
4557  C CG  . ARG B 124 ? 0.396 0.505 0.405 -0.008 0.003  -0.033 124 ARG BBB CG  
4558  C CD  . ARG B 124 ? 0.391 0.506 0.404 -0.008 0.002  -0.039 124 ARG BBB CD  
4559  N NE  . ARG B 124 ? 0.373 0.489 0.391 -0.013 0.005  -0.043 124 ARG BBB NE  
4560  C CZ  . ARG B 124 ? 0.384 0.499 0.402 -0.017 0.008  -0.044 124 ARG BBB CZ  
4561  N NH1 . ARG B 124 ? 0.388 0.503 0.404 -0.016 0.007  -0.043 124 ARG BBB NH1 
4562  N NH2 . ARG B 124 ? 0.428 0.543 0.451 -0.021 0.012  -0.047 124 ARG BBB NH2 
4563  N N   . MET B 125 ? 0.375 0.466 0.367 -0.009 0.005  -0.019 125 MET BBB N   
4564  C CA  . MET B 125 ? 0.402 0.491 0.390 -0.006 0.004  -0.016 125 MET BBB CA  
4565  C C   . MET B 125 ? 0.381 0.464 0.367 -0.005 0.005  -0.012 125 MET BBB C   
4566  O O   . MET B 125 ? 0.368 0.450 0.352 -0.001 0.004  -0.009 125 MET BBB O   
4567  C CB  . MET B 125 ? 0.456 0.543 0.441 -0.008 0.005  -0.015 125 MET BBB CB  
4568  C CG  . MET B 125 ? 0.541 0.625 0.521 -0.006 0.004  -0.011 125 MET BBB CG  
4569  S SD  . MET B 125 ? 0.606 0.683 0.583 -0.006 0.006  -0.006 125 MET BBB SD  
4570  C CE  . MET B 125 ? 0.641 0.715 0.617 -0.011 0.008  -0.007 125 MET BBB CE  
4571  N N   . LEU B 126 ? 0.361 0.441 0.348 -0.008 0.007  -0.011 126 LEU BBB N   
4572  C CA  . LEU B 126 ? 0.335 0.411 0.322 -0.007 0.008  -0.008 126 LEU BBB CA  
4573  C C   . LEU B 126 ? 0.317 0.395 0.307 -0.005 0.007  -0.009 126 LEU BBB C   
4574  O O   . LEU B 126 ? 0.303 0.378 0.292 -0.002 0.008  -0.006 126 LEU BBB O   
4575  C CB  . LEU B 126 ? 0.350 0.424 0.338 -0.011 0.010  -0.009 126 LEU BBB CB  
4576  C CG  . LEU B 126 ? 0.362 0.433 0.345 -0.013 0.011  -0.008 126 LEU BBB CG  
4577  C CD1 . LEU B 126 ? 0.373 0.443 0.357 -0.016 0.012  -0.009 126 LEU BBB CD1 
4578  C CD2 . LEU B 126 ? 0.361 0.429 0.343 -0.011 0.011  -0.004 126 LEU BBB CD2 
4579  N N   . ASN B 127 ? 0.291 0.374 0.285 -0.005 0.007  -0.012 127 ASN BBB N   
4580  C CA  . ASN B 127 ? 0.295 0.379 0.292 -0.002 0.006  -0.013 127 ASN BBB CA  
4581  C C   . ASN B 127 ? 0.322 0.406 0.316 0.003  0.004  -0.011 127 ASN BBB C   
4582  O O   . ASN B 127 ? 0.322 0.402 0.315 0.005  0.005  -0.008 127 ASN BBB O   
4583  C CB  . ASN B 127 ? 0.271 0.361 0.273 -0.003 0.005  -0.018 127 ASN BBB CB  
4584  C CG  . ASN B 127 ? 0.259 0.349 0.263 -0.008 0.007  -0.020 127 ASN BBB CG  
4585  O OD1 . ASN B 127 ? 0.244 0.338 0.250 -0.010 0.007  -0.024 127 ASN BBB OD1 
4586  N ND2 . ASN B 127 ? 0.250 0.336 0.254 -0.009 0.009  -0.018 127 ASN BBB ND2 
4587  N N   . PHE B 128 ? 0.358 0.445 0.350 0.004  0.002  -0.012 128 PHE BBB N   
4588  C CA  . PHE B 128 ? 0.402 0.489 0.390 0.009  0.000  -0.010 128 PHE BBB CA  
4589  C C   . PHE B 128 ? 0.394 0.474 0.377 0.011  0.002  -0.005 128 PHE BBB C   
4590  O O   . PHE B 128 ? 0.407 0.484 0.388 0.015  0.002  -0.002 128 PHE BBB O   
4591  C CB  . PHE B 128 ? 0.465 0.558 0.453 0.010  -0.002 -0.013 128 PHE BBB CB  
4592  C CG  . PHE B 128 ? 0.587 0.680 0.570 0.016  -0.004 -0.011 128 PHE BBB CG  
4593  C CD1 . PHE B 128 ? 0.656 0.751 0.639 0.021  -0.006 -0.011 128 PHE BBB CD1 
4594  C CD2 . PHE B 128 ? 0.660 0.749 0.637 0.017  -0.004 -0.008 128 PHE BBB CD2 
4595  C CE1 . PHE B 128 ? 0.709 0.802 0.686 0.028  -0.007 -0.009 128 PHE BBB CE1 
4596  C CE2 . PHE B 128 ? 0.689 0.777 0.661 0.023  -0.005 -0.005 128 PHE BBB CE2 
4597  C CZ  . PHE B 128 ? 0.719 0.809 0.690 0.028  -0.007 -0.006 128 PHE BBB CZ  
4598  N N   . SER B 129 ? 0.403 0.481 0.385 0.007  0.004  -0.004 129 SER BBB N   
4599  C CA  . SER B 129 ? 0.403 0.474 0.381 0.007  0.006  0.001  129 SER BBB CA  
4600  C C   . SER B 129 ? 0.417 0.483 0.397 0.008  0.008  0.003  129 SER BBB C   
4601  O O   . SER B 129 ? 0.404 0.466 0.381 0.011  0.009  0.006  129 SER BBB O   
4602  C CB  . SER B 129 ? 0.391 0.461 0.369 0.003  0.007  0.000  129 SER BBB CB  
4603  O OG  . SER B 129 ? 0.455 0.519 0.430 0.002  0.009  0.003  129 SER BBB OG  
4604  N N   . TYR B 130 ? 0.446 0.514 0.431 0.006  0.008  0.001  130 TYR BBB N   
4605  C CA  . TYR B 130 ? 0.449 0.513 0.436 0.006  0.011  0.002  130 TYR BBB CA  
4606  C C   . TYR B 130 ? 0.480 0.544 0.468 0.011  0.010  0.003  130 TYR BBB C   
4607  O O   . TYR B 130 ? 0.454 0.512 0.440 0.014  0.012  0.006  130 TYR BBB O   
4608  C CB  . TYR B 130 ? 0.463 0.528 0.455 0.002  0.011  -0.001 130 TYR BBB CB  
4609  C CG  . TYR B 130 ? 0.478 0.542 0.470 -0.001 0.013  -0.001 130 TYR BBB CG  
4610  C CD1 . TYR B 130 ? 0.519 0.577 0.509 -0.001 0.015  0.002  130 TYR BBB CD1 
4611  C CD2 . TYR B 130 ? 0.500 0.566 0.492 -0.005 0.012  -0.003 130 TYR BBB CD2 
4612  C CE1 . TYR B 130 ? 0.524 0.581 0.515 -0.005 0.016  0.001  130 TYR BBB CE1 
4613  C CE2 . TYR B 130 ? 0.497 0.561 0.488 -0.008 0.013  -0.003 130 TYR BBB CE2 
4614  C CZ  . TYR B 130 ? 0.522 0.582 0.512 -0.007 0.014  -0.001 130 TYR BBB CZ  
4615  O OH  . TYR B 130 ? 0.533 0.592 0.522 -0.010 0.015  -0.002 130 TYR BBB OH  
4616  N N   . ARG B 131 ? 0.474 0.544 0.462 0.013  0.007  0.000  131 ARG BBB N   
4617  C CA  . ARG B 131 ? 0.522 0.592 0.509 0.019  0.006  0.001  131 ARG BBB CA  
4618  C C   . ARG B 131 ? 0.501 0.566 0.482 0.024  0.007  0.005  131 ARG BBB C   
4619  O O   . ARG B 131 ? 0.504 0.565 0.484 0.027  0.008  0.008  131 ARG BBB O   
4620  C CB  . ARG B 131 ? 0.555 0.633 0.543 0.021  0.002  -0.003 131 ARG BBB CB  
4621  C CG  . ARG B 131 ? 0.594 0.676 0.588 0.020  0.001  -0.007 131 ARG BBB CG  
4622  C CD  . ARG B 131 ? 0.652 0.741 0.647 0.024  -0.002 -0.010 131 ARG BBB CD  
4623  N NE  . ARG B 131 ? 0.684 0.778 0.678 0.025  -0.005 -0.013 131 ARG BBB NE  
4624  C CZ  . ARG B 131 ? 0.725 0.824 0.723 0.020  -0.005 -0.017 131 ARG BBB CZ  
4625  N NH1 . ARG B 131 ? 0.734 0.831 0.736 0.014  -0.002 -0.018 131 ARG BBB NH1 
4626  N NH2 . ARG B 131 ? 0.727 0.831 0.725 0.020  -0.007 -0.020 131 ARG BBB NH2 
4627  N N   . THR B 132 ? 0.481 0.547 0.458 0.023  0.006  0.006  132 THR BBB N   
4628  C CA  . THR B 132 ? 0.519 0.580 0.489 0.028  0.006  0.010  132 THR BBB CA  
4629  C C   . THR B 132 ? 0.501 0.554 0.470 0.026  0.011  0.014  132 THR BBB C   
4630  O O   . THR B 132 ? 0.522 0.570 0.487 0.031  0.013  0.018  132 THR BBB O   
4631  C CB  . THR B 132 ? 0.502 0.566 0.468 0.027  0.004  0.009  132 THR BBB CB  
4632  O OG1 . THR B 132 ? 0.472 0.545 0.440 0.029  0.000  0.005  132 THR BBB OG1 
4633  C CG2 . THR B 132 ? 0.501 0.562 0.460 0.031  0.005  0.013  132 THR BBB CG2 
4634  N N   . GLY B 133 ? 0.495 0.547 0.467 0.021  0.013  0.013  133 GLY BBB N   
4635  C CA  . GLY B 133 ? 0.489 0.535 0.463 0.019  0.017  0.015  133 GLY BBB CA  
4636  C C   . GLY B 133 ? 0.491 0.531 0.467 0.021  0.019  0.017  133 GLY BBB C   
4637  O O   . GLY B 133 ? 0.523 0.556 0.498 0.022  0.023  0.020  133 GLY BBB O   
4638  N N   . LEU B 134 ? 0.438 0.482 0.417 0.022  0.018  0.015  134 LEU BBB N   
4639  C CA  . LEU B 134 ? 0.441 0.482 0.424 0.024  0.020  0.016  134 LEU BBB CA  
4640  C C   . LEU B 134 ? 0.496 0.533 0.472 0.031  0.020  0.019  134 LEU BBB C   
4641  O O   . LEU B 134 ? 0.481 0.511 0.457 0.033  0.025  0.023  134 LEU BBB O   
4642  C CB  . LEU B 134 ? 0.413 0.460 0.402 0.022  0.018  0.012  134 LEU BBB CB  
4643  C CG  . LEU B 134 ? 0.381 0.429 0.376 0.016  0.019  0.009  134 LEU BBB CG  
4644  C CD1 . LEU B 134 ? 0.373 0.427 0.373 0.015  0.017  0.005  134 LEU BBB CD1 
4645  C CD2 . LEU B 134 ? 0.365 0.406 0.362 0.015  0.023  0.011  134 LEU BBB CD2 
4646  N N   . ARG B 135 ? 0.518 0.560 0.491 0.035  0.016  0.018  135 ARG BBB N   
4647  C CA  . ARG B 135 ? 0.581 0.621 0.546 0.042  0.016  0.022  135 ARG BBB CA  
4648  C C   . ARG B 135 ? 0.559 0.590 0.518 0.044  0.019  0.027  135 ARG BBB C   
4649  O O   . ARG B 135 ? 0.550 0.574 0.505 0.049  0.023  0.030  135 ARG BBB O   
4650  C CB  . ARG B 135 ? 0.615 0.663 0.578 0.045  0.010  0.018  135 ARG BBB CB  
4651  C CG  . ARG B 135 ? 0.676 0.724 0.635 0.054  0.009  0.020  135 ARG BBB CG  
4652  C CD  . ARG B 135 ? 0.708 0.764 0.663 0.058  0.003  0.017  135 ARG BBB CD  
4653  N NE  . ARG B 135 ? 0.728 0.784 0.678 0.058  0.003  0.018  135 ARG BBB NE  
4654  C CZ  . ARG B 135 ? 0.732 0.793 0.684 0.053  0.001  0.015  135 ARG BBB CZ  
4655  N NH1 . ARG B 135 ? 0.752 0.820 0.712 0.047  -0.001 0.010  135 ARG BBB NH1 
4656  N NH2 . ARG B 135 ? 0.690 0.751 0.637 0.053  0.001  0.016  135 ARG BBB NH2 
4657  N N   . VAL B 136 ? 0.534 0.567 0.491 0.041  0.019  0.026  136 VAL BBB N   
4658  C CA  . VAL B 136 ? 0.538 0.564 0.489 0.042  0.023  0.030  136 VAL BBB CA  
4659  C C   . VAL B 136 ? 0.561 0.579 0.516 0.040  0.029  0.033  136 VAL BBB C   
4660  O O   . VAL B 136 ? 0.566 0.575 0.516 0.043  0.033  0.037  136 VAL BBB O   
4661  C CB  . VAL B 136 ? 0.519 0.548 0.469 0.038  0.021  0.029  136 VAL BBB CB  
4662  C CG1 . VAL B 136 ? 0.500 0.523 0.448 0.037  0.025  0.032  136 VAL BBB CG1 
4663  C CG2 . VAL B 136 ? 0.516 0.553 0.462 0.042  0.016  0.027  136 VAL BBB CG2 
4664  N N   . GLY B 137 ? 0.550 0.569 0.513 0.034  0.029  0.030  137 GLY BBB N   
4665  C CA  . GLY B 137 ? 0.522 0.535 0.491 0.031  0.035  0.030  137 GLY BBB CA  
4666  C C   . GLY B 137 ? 0.517 0.525 0.488 0.035  0.038  0.032  137 GLY BBB C   
4667  O O   . GLY B 137 ? 0.503 0.507 0.480 0.032  0.042  0.032  137 GLY BBB O   
4668  N N   . ASN B 138 ? 0.516 0.525 0.482 0.040  0.035  0.033  138 ASN BBB N   
4669  C CA  . ASN B 138 ? 0.537 0.540 0.502 0.045  0.038  0.036  138 ASN BBB CA  
4670  C C   . ASN B 138 ? 0.515 0.521 0.489 0.042  0.038  0.032  138 ASN BBB C   
4671  O O   . ASN B 138 ? 0.497 0.497 0.474 0.043  0.042  0.034  138 ASN BBB O   
4672  C CB  . ASN B 138 ? 0.581 0.573 0.542 0.048  0.044  0.041  138 ASN BBB CB  
4673  C CG  . ASN B 138 ? 0.630 0.615 0.588 0.055  0.047  0.044  138 ASN BBB CG  
4674  O OD1 . ASN B 138 ? 0.663 0.652 0.616 0.060  0.042  0.044  138 ASN BBB OD1 
4675  N ND2 . ASN B 138 ? 0.627 0.603 0.587 0.055  0.054  0.047  138 ASN BBB ND2 
4676  N N   . VAL B 139 ? 0.519 0.535 0.498 0.038  0.033  0.027  139 VAL BBB N   
4677  C CA  . VAL B 139 ? 0.479 0.499 0.467 0.035  0.032  0.024  139 VAL BBB CA  
4678  C C   . VAL B 139 ? 0.474 0.501 0.460 0.039  0.027  0.022  139 VAL BBB C   
4679  O O   . VAL B 139 ? 0.463 0.495 0.445 0.039  0.023  0.020  139 VAL BBB O   
4680  C CB  . VAL B 139 ? 0.466 0.491 0.460 0.028  0.031  0.019  139 VAL BBB CB  
4681  C CG1 . VAL B 139 ? 0.462 0.492 0.463 0.025  0.030  0.015  139 VAL BBB CG1 
4682  C CG2 . VAL B 139 ? 0.476 0.496 0.471 0.024  0.035  0.020  139 VAL BBB CG2 
4683  N N   . GLU B 140 ? 0.494 0.519 0.483 0.041  0.028  0.021  140 GLU BBB N   
4684  C CA  . GLU B 140 ? 0.510 0.542 0.499 0.044  0.023  0.019  140 GLU BBB CA  
4685  C C   . GLU B 140 ? 0.476 0.517 0.474 0.038  0.020  0.013  140 GLU BBB C   
4686  O O   . GLU B 140 ? 0.453 0.493 0.457 0.035  0.022  0.011  140 GLU BBB O   
4687  C CB  . GLU B 140 ? 0.541 0.568 0.531 0.049  0.025  0.020  140 GLU BBB CB  
4688  C CG  . GLU B 140 ? 0.572 0.606 0.561 0.054  0.020  0.018  140 GLU BBB CG  
4689  C CD  . GLU B 140 ? 0.619 0.649 0.609 0.059  0.022  0.020  140 GLU BBB CD  
4690  O OE1 . GLU B 140 ? 0.661 0.682 0.652 0.060  0.027  0.023  140 GLU BBB OE1 
4691  O OE2 . GLU B 140 ? 0.647 0.684 0.639 0.063  0.017  0.017  140 GLU BBB OE2 
4692  N N   . TYR B 141 ? 0.453 0.501 0.449 0.037  0.016  0.010  141 TYR BBB N   
4693  C CA  . TYR B 141 ? 0.448 0.504 0.450 0.031  0.014  0.005  141 TYR BBB CA  
4694  C C   . TYR B 141 ? 0.445 0.506 0.450 0.034  0.011  0.002  141 TYR BBB C   
4695  O O   . TYR B 141 ? 0.468 0.532 0.469 0.039  0.008  0.002  141 TYR BBB O   
4696  C CB  . TYR B 141 ? 0.420 0.480 0.419 0.029  0.011  0.004  141 TYR BBB CB  
4697  C CG  . TYR B 141 ? 0.418 0.486 0.422 0.024  0.009  -0.001 141 TYR BBB CG  
4698  C CD1 . TYR B 141 ? 0.425 0.493 0.434 0.020  0.010  -0.004 141 TYR BBB CD1 
4699  C CD2 . TYR B 141 ? 0.415 0.490 0.417 0.025  0.005  -0.004 141 TYR BBB CD2 
4700  C CE1 . TYR B 141 ? 0.416 0.491 0.429 0.016  0.009  -0.008 141 TYR BBB CE1 
4701  C CE2 . TYR B 141 ? 0.402 0.483 0.408 0.021  0.004  -0.009 141 TYR BBB CE2 
4702  C CZ  . TYR B 141 ? 0.423 0.504 0.435 0.016  0.006  -0.011 141 TYR BBB CZ  
4703  O OH  . TYR B 141 ? 0.441 0.527 0.456 0.013  0.005  -0.015 141 TYR BBB OH  
4704  N N   . ILE B 142 ? 0.437 0.500 0.448 0.031  0.011  -0.001 142 ILE BBB N   
4705  C CA  . ILE B 142 ? 0.442 0.512 0.458 0.032  0.009  -0.005 142 ILE BBB CA  
4706  C C   . ILE B 142 ? 0.417 0.493 0.438 0.026  0.008  -0.010 142 ILE BBB C   
4707  O O   . ILE B 142 ? 0.400 0.474 0.425 0.022  0.010  -0.010 142 ILE BBB O   
4708  C CB  . ILE B 142 ? 0.445 0.510 0.464 0.035  0.011  -0.004 142 ILE BBB CB  
4709  C CG1 . ILE B 142 ? 0.476 0.534 0.489 0.041  0.013  0.002  142 ILE BBB CG1 
4710  C CG2 . ILE B 142 ? 0.429 0.501 0.453 0.036  0.008  -0.008 142 ILE BBB CG2 
4711  C CD1 . ILE B 142 ? 0.486 0.537 0.502 0.043  0.016  0.004  142 ILE BBB CD1 
4712  N N   . ASN B 143 ? 0.403 0.486 0.424 0.026  0.004  -0.013 143 ASN BBB N   
4713  C CA  . ASN B 143 ? 0.408 0.497 0.434 0.021  0.004  -0.018 143 ASN BBB CA  
4714  C C   . ASN B 143 ? 0.375 0.468 0.408 0.021  0.004  -0.022 143 ASN BBB C   
4715  O O   . ASN B 143 ? 0.370 0.469 0.405 0.022  0.001  -0.025 143 ASN BBB O   
4716  C CB  . ASN B 143 ? 0.419 0.514 0.444 0.021  0.001  -0.021 143 ASN BBB CB  
4717  C CG  . ASN B 143 ? 0.420 0.520 0.449 0.015  0.001  -0.025 143 ASN BBB CG  
4718  O OD1 . ASN B 143 ? 0.439 0.536 0.469 0.010  0.004  -0.025 143 ASN BBB OD1 
4719  N ND2 . ASN B 143 ? 0.416 0.522 0.445 0.015  -0.001 -0.029 143 ASN BBB ND2 
4720  N N   . ALA B 144 ? 0.362 0.450 0.397 0.019  0.006  -0.020 144 ALA BBB N   
4721  C CA  . ALA B 144 ? 0.362 0.454 0.404 0.018  0.007  -0.024 144 ALA BBB CA  
4722  C C   . ALA B 144 ? 0.361 0.449 0.406 0.014  0.010  -0.024 144 ALA BBB C   
4723  O O   . ALA B 144 ? 0.355 0.437 0.397 0.013  0.012  -0.020 144 ALA BBB O   
4724  C CB  . ALA B 144 ? 0.360 0.450 0.403 0.024  0.006  -0.023 144 ALA BBB CB  
4725  N N   . LEU B 145 ? 0.352 0.443 0.402 0.011  0.010  -0.027 145 LEU BBB N   
4726  C CA  . LEU B 145 ? 0.365 0.454 0.419 0.008  0.013  -0.028 145 LEU BBB CA  
4727  C C   . LEU B 145 ? 0.387 0.472 0.443 0.011  0.015  -0.026 145 LEU BBB C   
4728  O O   . LEU B 145 ? 0.388 0.474 0.446 0.015  0.013  -0.026 145 LEU BBB O   
4729  C CB  . LEU B 145 ? 0.372 0.466 0.431 0.005  0.013  -0.033 145 LEU BBB CB  
4730  C CG  . LEU B 145 ? 0.386 0.484 0.443 0.001  0.013  -0.035 145 LEU BBB CG  
4731  C CD1 . LEU B 145 ? 0.365 0.468 0.427 -0.002 0.013  -0.040 145 LEU BBB CD1 
4732  C CD2 . LEU B 145 ? 0.373 0.467 0.427 -0.002 0.015  -0.033 145 LEU BBB CD2 
4733  N N   . ALA B 146 ? 0.406 0.484 0.461 0.010  0.017  -0.023 146 ALA BBB N   
4734  C CA  . ALA B 146 ? 0.403 0.476 0.462 0.012  0.020  -0.021 146 ALA BBB CA  
4735  C C   . ALA B 146 ? 0.389 0.464 0.454 0.009  0.022  -0.025 146 ALA BBB C   
4736  O O   . ALA B 146 ? 0.392 0.470 0.458 0.005  0.022  -0.027 146 ALA BBB O   
4737  C CB  . ALA B 146 ? 0.403 0.470 0.458 0.013  0.022  -0.017 146 ALA BBB CB  
4738  N N   . LYS B 147 ? 0.428 0.500 0.498 0.011  0.023  -0.025 147 LYS BBB N   
4739  C CA  . LYS B 147 ? 0.453 0.525 0.529 0.008  0.026  -0.028 147 LYS BBB CA  
4740  C C   . LYS B 147 ? 0.420 0.486 0.500 0.010  0.029  -0.026 147 LYS BBB C   
4741  O O   . LYS B 147 ? 0.382 0.443 0.459 0.014  0.030  -0.022 147 LYS BBB O   
4742  C CB  . LYS B 147 ? 0.502 0.581 0.583 0.007  0.024  -0.032 147 LYS BBB CB  
4743  C CG  . LYS B 147 ? 0.559 0.638 0.642 0.011  0.023  -0.032 147 LYS BBB CG  
4744  C CD  . LYS B 147 ? 0.624 0.707 0.714 0.010  0.024  -0.036 147 LYS BBB CD  
4745  C CE  . LYS B 147 ? 0.636 0.726 0.727 0.008  0.021  -0.040 147 LYS BBB CE  
4746  N NZ  . LYS B 147 ? 0.622 0.716 0.719 0.006  0.022  -0.045 147 LYS BBB NZ  
4747  N N   . LEU B 148 ? 0.416 0.481 0.501 0.007  0.032  -0.028 148 LEU BBB N   
4748  C CA  . LEU B 148 ? 0.435 0.494 0.526 0.008  0.036  -0.027 148 LEU BBB CA  
4749  C C   . LEU B 148 ? 0.460 0.520 0.556 0.011  0.037  -0.028 148 LEU BBB C   
4750  O O   . LEU B 148 ? 0.434 0.499 0.533 0.009  0.035  -0.032 148 LEU BBB O   
4751  C CB  . LEU B 148 ? 0.433 0.493 0.529 0.004  0.039  -0.030 148 LEU BBB CB  
4752  C CG  . LEU B 148 ? 0.413 0.472 0.504 0.002  0.038  -0.029 148 LEU BBB CG  
4753  C CD1 . LEU B 148 ? 0.410 0.471 0.507 -0.002 0.040  -0.034 148 LEU BBB CD1 
4754  C CD2 . LEU B 148 ? 0.414 0.465 0.501 0.004  0.040  -0.024 148 LEU BBB CD2 
4755  N N   . ILE B 149 ? 0.506 0.558 0.602 0.015  0.039  -0.025 149 ILE BBB N   
4756  C CA  . ILE B 149 ? 0.512 0.562 0.613 0.018  0.041  -0.026 149 ILE BBB CA  
4757  C C   . ILE B 149 ? 0.497 0.543 0.606 0.016  0.046  -0.027 149 ILE BBB C   
4758  O O   . ILE B 149 ? 0.526 0.574 0.642 0.015  0.047  -0.030 149 ILE BBB O   
4759  C CB  . ILE B 149 ? 0.543 0.589 0.638 0.024  0.040  -0.021 149 ILE BBB CB  
4760  C CG1 . ILE B 149 ? 0.544 0.597 0.635 0.026  0.035  -0.022 149 ILE BBB CG1 
4761  C CG2 . ILE B 149 ? 0.571 0.612 0.671 0.028  0.043  -0.020 149 ILE BBB CG2 
4762  C CD1 . ILE B 149 ? 0.539 0.599 0.635 0.024  0.032  -0.027 149 ILE BBB CD1 
4763  N N   . ASP B 150 ? 0.512 0.552 0.620 0.016  0.050  -0.024 150 ASP BBB N   
4764  C CA  . ASP B 150 ? 0.508 0.543 0.624 0.014  0.055  -0.026 150 ASP BBB CA  
4765  C C   . ASP B 150 ? 0.493 0.524 0.606 0.012  0.057  -0.024 150 ASP BBB C   
4766  O O   . ASP B 150 ? 0.532 0.563 0.637 0.012  0.055  -0.021 150 ASP BBB O   
4767  C CB  . ASP B 150 ? 0.519 0.546 0.638 0.018  0.059  -0.024 150 ASP BBB CB  
4768  C CG  . ASP B 150 ? 0.538 0.556 0.649 0.023  0.062  -0.017 150 ASP BBB CG  
4769  O OD1 . ASP B 150 ? 0.508 0.523 0.615 0.023  0.063  -0.014 150 ASP BBB OD1 
4770  O OD2 . ASP B 150 ? 0.591 0.605 0.701 0.028  0.062  -0.014 150 ASP BBB OD2 
4771  N N   . PRO B 151 ? 0.477 0.504 0.598 0.009  0.062  -0.026 151 PRO BBB N   
4772  C CA  . PRO B 151 ? 0.482 0.506 0.601 0.007  0.065  -0.025 151 PRO BBB CA  
4773  C C   . PRO B 151 ? 0.488 0.505 0.598 0.011  0.066  -0.018 151 PRO BBB C   
4774  O O   . PRO B 151 ? 0.513 0.529 0.621 0.009  0.067  -0.018 151 PRO BBB O   
4775  C CB  . PRO B 151 ? 0.487 0.506 0.616 0.006  0.071  -0.028 151 PRO BBB CB  
4776  C CG  . PRO B 151 ? 0.478 0.501 0.616 0.005  0.071  -0.032 151 PRO BBB CG  
4777  C CD  . PRO B 151 ? 0.474 0.500 0.605 0.008  0.066  -0.030 151 PRO BBB CD  
4778  N N   . HIS B 152 ? 0.476 0.489 0.580 0.016  0.065  -0.013 152 HIS BBB N   
4779  C CA  . HIS B 152 ? 0.482 0.488 0.576 0.020  0.066  -0.007 152 HIS BBB CA  
4780  C C   . HIS B 152 ? 0.478 0.487 0.563 0.025  0.061  -0.004 152 HIS BBB C   
4781  O O   . HIS B 152 ? 0.504 0.507 0.581 0.029  0.061  0.001  152 HIS BBB O   
4782  C CB  . HIS B 152 ? 0.490 0.483 0.585 0.024  0.074  -0.003 152 HIS BBB CB  
4783  C CG  . HIS B 152 ? 0.494 0.483 0.597 0.020  0.080  -0.005 152 HIS BBB CG  
4784  N ND1 . HIS B 152 ? 0.483 0.471 0.584 0.018  0.081  -0.004 152 HIS BBB ND1 
4785  C CD2 . HIS B 152 ? 0.501 0.488 0.616 0.018  0.085  -0.009 152 HIS BBB CD2 
4786  C CE1 . HIS B 152 ? 0.494 0.479 0.605 0.014  0.087  -0.008 152 HIS BBB CE1 
4787  N NE2 . HIS B 152 ? 0.508 0.492 0.627 0.014  0.090  -0.011 152 HIS BBB NE2 
4788  N N   . SER B 153 ? 0.469 0.487 0.555 0.024  0.055  -0.008 153 SER BBB N   
4789  C CA  . SER B 153 ? 0.472 0.494 0.552 0.028  0.050  -0.006 153 SER BBB CA  
4790  C C   . SER B 153 ? 0.462 0.494 0.541 0.024  0.045  -0.010 153 SER BBB C   
4791  O O   . SER B 153 ? 0.414 0.451 0.499 0.020  0.044  -0.015 153 SER BBB O   
4792  C CB  . SER B 153 ? 0.466 0.486 0.549 0.031  0.051  -0.007 153 SER BBB CB  
4793  O OG  . SER B 153 ? 0.485 0.495 0.571 0.034  0.057  -0.004 153 SER BBB OG  
4794  N N   . VAL B 154 ? 0.504 0.538 0.575 0.027  0.041  -0.008 154 VAL BBB N   
4795  C CA  . VAL B 154 ? 0.540 0.583 0.609 0.024  0.035  -0.011 154 VAL BBB CA  
4796  C C   . VAL B 154 ? 0.549 0.596 0.614 0.028  0.031  -0.011 154 VAL BBB C   
4797  O O   . VAL B 154 ? 0.560 0.602 0.620 0.034  0.032  -0.007 154 VAL BBB O   
4798  C CB  . VAL B 154 ? 0.582 0.626 0.646 0.021  0.035  -0.010 154 VAL BBB CB  
4799  C CG1 . VAL B 154 ? 0.588 0.629 0.656 0.017  0.038  -0.011 154 VAL BBB CG1 
4800  C CG2 . VAL B 154 ? 0.639 0.678 0.695 0.026  0.035  -0.005 154 VAL BBB CG2 
4801  N N   . GLU B 155 ? 0.553 0.609 0.622 0.026  0.028  -0.015 155 GLU BBB N   
4802  C CA  . GLU B 155 ? 0.559 0.620 0.626 0.030  0.024  -0.017 155 GLU BBB CA  
4803  C C   . GLU B 155 ? 0.544 0.612 0.608 0.028  0.020  -0.019 155 GLU BBB C   
4804  O O   . GLU B 155 ? 0.537 0.609 0.603 0.022  0.020  -0.021 155 GLU BBB O   
4805  C CB  . GLU B 155 ? 0.582 0.647 0.656 0.028  0.024  -0.021 155 GLU BBB CB  
4806  C CG  . GLU B 155 ? 0.628 0.699 0.703 0.032  0.020  -0.023 155 GLU BBB CG  
4807  C CD  . GLU B 155 ? 0.656 0.731 0.739 0.031  0.020  -0.028 155 GLU BBB CD  
4808  O OE1 . GLU B 155 ? 0.651 0.729 0.738 0.025  0.021  -0.031 155 GLU BBB OE1 
4809  O OE2 . GLU B 155 ? 0.737 0.812 0.822 0.036  0.019  -0.027 155 GLU BBB OE2 
4810  N N   . TYR B 156 ? 0.583 0.654 0.642 0.032  0.017  -0.018 156 TYR BBB N   
4811  C CA  . TYR B 156 ? 0.569 0.647 0.626 0.030  0.013  -0.020 156 TYR BBB CA  
4812  C C   . TYR B 156 ? 0.585 0.668 0.641 0.035  0.009  -0.023 156 TYR BBB C   
4813  O O   . TYR B 156 ? 0.522 0.601 0.577 0.042  0.009  -0.020 156 TYR BBB O   
4814  C CB  . TYR B 156 ? 0.552 0.627 0.602 0.030  0.013  -0.017 156 TYR BBB CB  
4815  C CG  . TYR B 156 ? 0.547 0.617 0.590 0.037  0.013  -0.013 156 TYR BBB CG  
4816  C CD1 . TYR B 156 ? 0.539 0.601 0.581 0.040  0.016  -0.008 156 TYR BBB CD1 
4817  C CD2 . TYR B 156 ? 0.540 0.615 0.579 0.040  0.009  -0.013 156 TYR BBB CD2 
4818  C CE1 . TYR B 156 ? 0.539 0.595 0.573 0.046  0.016  -0.004 156 TYR BBB CE1 
4819  C CE2 . TYR B 156 ? 0.533 0.603 0.564 0.047  0.008  -0.009 156 TYR BBB CE2 
4820  C CZ  . TYR B 156 ? 0.550 0.611 0.579 0.050  0.012  -0.004 156 TYR BBB CZ  
4821  O OH  . TYR B 156 ? 0.558 0.615 0.580 0.057  0.012  0.000  156 TYR BBB OH  
4822  N N   . GLU B 157 ? 0.638 0.729 0.697 0.033  0.007  -0.027 157 GLU BBB N   
4823  C CA  . GLU B 157 ? 0.666 0.764 0.726 0.037  0.002  -0.031 157 GLU BBB CA  
4824  C C   . GLU B 157 ? 0.688 0.787 0.741 0.040  0.000  -0.029 157 GLU BBB C   
4825  O O   . GLU B 157 ? 0.673 0.770 0.722 0.037  0.001  -0.027 157 GLU BBB O   
4826  C CB  . GLU B 157 ? 0.702 0.809 0.767 0.032  0.001  -0.037 157 GLU BBB CB  
4827  C CG  . GLU B 157 ? 0.776 0.886 0.849 0.031  0.002  -0.041 157 GLU BBB CG  
4828  C CD  . GLU B 157 ? 0.805 0.924 0.883 0.029  -0.001 -0.047 157 GLU BBB CD  
4829  O OE1 . GLU B 157 ? 0.831 0.954 0.907 0.029  -0.003 -0.049 157 GLU BBB OE1 
4830  O OE2 . GLU B 157 ? 0.854 0.975 0.938 0.028  0.000  -0.050 157 GLU BBB OE2 
4831  N N   . ASP B 158 ? 0.728 0.830 0.779 0.047  -0.003 -0.029 158 ASP BBB N   
4832  C CA  . ASP B 158 ? 0.737 0.840 0.781 0.052  -0.006 -0.028 158 ASP BBB CA  
4833  C C   . ASP B 158 ? 0.767 0.878 0.813 0.058  -0.011 -0.033 158 ASP BBB C   
4834  O O   . ASP B 158 ? 0.713 0.821 0.758 0.064  -0.011 -0.031 158 ASP BBB O   
4835  C CB  . ASP B 158 ? 0.733 0.826 0.769 0.057  -0.004 -0.021 158 ASP BBB CB  
4836  C CG  . ASP B 158 ? 0.710 0.804 0.738 0.063  -0.007 -0.019 158 ASP BBB CG  
4837  O OD1 . ASP B 158 ? 0.695 0.794 0.722 0.061  -0.009 -0.022 158 ASP BBB OD1 
4838  O OD2 . ASP B 158 ? 0.690 0.777 0.712 0.071  -0.007 -0.015 158 ASP BBB OD2 
4839  N N   . ASN B 159 ? 0.786 0.905 0.835 0.056  -0.013 -0.038 159 ASN BBB N   
4840  C CA  . ASN B 159 ? 0.828 0.958 0.883 0.059  -0.018 -0.045 159 ASN BBB CA  
4841  C C   . ASN B 159 ? 0.835 0.965 0.896 0.058  -0.016 -0.047 159 ASN BBB C   
4842  O O   . ASN B 159 ? 0.791 0.924 0.855 0.064  -0.019 -0.049 159 ASN BBB O   
4843  C CB  . ASN B 159 ? 0.872 1.001 0.920 0.069  -0.021 -0.043 159 ASN BBB CB  
4844  C CG  . ASN B 159 ? 0.895 1.027 0.937 0.071  -0.023 -0.043 159 ASN BBB CG  
4845  O OD1 . ASN B 159 ? 0.800 0.941 0.845 0.071  -0.027 -0.049 159 ASN BBB OD1 
4846  N ND2 . ASN B 159 ? 0.881 1.003 0.914 0.073  -0.021 -0.036 159 ASN BBB ND2 
4847  N N   . GLY B 160 ? 0.833 0.962 0.899 0.050  -0.013 -0.048 160 GLY BBB N   
4848  C CA  . GLY B 160 ? 0.867 0.996 0.940 0.048  -0.011 -0.050 160 GLY BBB CA  
4849  C C   . GLY B 160 ? 0.915 1.039 0.987 0.053  -0.010 -0.047 160 GLY BBB C   
4850  O O   . GLY B 160 ? 0.882 1.009 0.960 0.055  -0.011 -0.050 160 GLY BBB O   
4851  N N   . GLN B 161 ? 0.967 1.081 1.031 0.056  -0.009 -0.040 161 GLN BBB N   
4852  C CA  . GLN B 161 ? 0.927 1.033 0.990 0.062  -0.007 -0.035 161 GLN BBB CA  
4853  C C   . GLN B 161 ? 0.865 0.961 0.925 0.058  -0.002 -0.030 161 GLN BBB C   
4854  O O   . GLN B 161 ? 0.793 0.885 0.846 0.059  -0.001 -0.025 161 GLN BBB O   
4855  C CB  . GLN B 161 ? 0.978 1.083 1.033 0.071  -0.010 -0.033 161 GLN BBB CB  
4856  C CG  . GLN B 161 ? 1.043 1.157 1.101 0.076  -0.015 -0.038 161 GLN BBB CG  
4857  C CD  . GLN B 161 ? 1.066 1.179 1.117 0.087  -0.017 -0.036 161 GLN BBB CD  
4858  O OE1 . GLN B 161 ? 1.100 1.203 1.142 0.091  -0.015 -0.029 161 GLN BBB OE1 
4859  N NE2 . GLN B 161 ? 1.026 1.148 1.080 0.092  -0.022 -0.041 161 GLN BBB NE2 
4860  N N   . LYS B 162 ? 0.818 0.913 0.884 0.053  0.001  -0.031 162 LYS BBB N   
4861  C CA  . LYS B 162 ? 0.800 0.886 0.866 0.050  0.006  -0.026 162 LYS BBB CA  
4862  C C   . LYS B 162 ? 0.752 0.828 0.810 0.056  0.008  -0.020 162 LYS BBB C   
4863  O O   . LYS B 162 ? 0.678 0.753 0.734 0.064  0.007  -0.019 162 LYS BBB O   
4864  C CB  . LYS B 162 ? 0.823 0.908 0.897 0.048  0.009  -0.029 162 LYS BBB CB  
4865  C CG  . LYS B 162 ? 0.888 0.982 0.969 0.041  0.008  -0.035 162 LYS BBB CG  
4866  C CD  . LYS B 162 ? 0.930 1.025 1.009 0.034  0.009  -0.035 162 LYS BBB CD  
4867  C CE  . LYS B 162 ? 0.986 1.085 1.072 0.028  0.010  -0.039 162 LYS BBB CE  
4868  N NZ  . LYS B 162 ? 1.020 1.116 1.104 0.022  0.012  -0.038 162 LYS BBB NZ  
4869  N N   . LYS B 163 ? 0.701 0.772 0.756 0.054  0.011  -0.016 163 LYS BBB N   
4870  C CA  . LYS B 163 ? 0.709 0.770 0.757 0.058  0.014  -0.010 163 LYS BBB CA  
4871  C C   . LYS B 163 ? 0.695 0.749 0.747 0.052  0.019  -0.008 163 LYS BBB C   
4872  O O   . LYS B 163 ? 0.708 0.767 0.764 0.045  0.019  -0.011 163 LYS BBB O   
4873  C CB  . LYS B 163 ? 0.733 0.793 0.772 0.061  0.012  -0.007 163 LYS BBB CB  
4874  C CG  . LYS B 163 ? 0.759 0.825 0.795 0.067  0.007  -0.009 163 LYS BBB CG  
4875  C CD  . LYS B 163 ? 0.808 0.871 0.833 0.072  0.006  -0.005 163 LYS BBB CD  
4876  C CE  . LYS B 163 ? 0.846 0.915 0.868 0.080  0.000  -0.007 163 LYS BBB CE  
4877  N NZ  . LYS B 163 ? 0.893 0.958 0.904 0.087  -0.000 -0.002 163 LYS BBB NZ  
4878  N N   . THR B 164 ? 0.665 0.709 0.715 0.056  0.024  -0.004 164 THR BBB N   
4879  C CA  . THR B 164 ? 0.622 0.660 0.676 0.051  0.029  -0.002 164 THR BBB CA  
4880  C C   . THR B 164 ? 0.615 0.643 0.661 0.054  0.033  0.004  164 THR BBB C   
4881  O O   . THR B 164 ? 0.628 0.652 0.668 0.061  0.033  0.007  164 THR BBB O   
4882  C CB  . THR B 164 ? 0.617 0.652 0.679 0.051  0.032  -0.004 164 THR BBB CB  
4883  O OG1 . THR B 164 ? 0.586 0.631 0.654 0.048  0.029  -0.010 164 THR BBB OG1 
4884  C CG2 . THR B 164 ? 0.626 0.656 0.694 0.046  0.038  -0.003 164 THR BBB CG2 
4885  N N   . ILE B 165 ? 0.578 0.604 0.626 0.049  0.036  0.004  165 ILE BBB N   
4886  C CA  . ILE B 165 ? 0.578 0.594 0.620 0.051  0.040  0.010  165 ILE BBB CA  
4887  C C   . ILE B 165 ? 0.556 0.567 0.605 0.045  0.046  0.009  165 ILE BBB C   
4888  O O   . ILE B 165 ? 0.509 0.527 0.566 0.039  0.045  0.004  165 ILE BBB O   
4889  C CB  . ILE B 165 ? 0.583 0.602 0.617 0.050  0.037  0.011  165 ILE BBB CB  
4890  C CG1 . ILE B 165 ? 0.589 0.615 0.628 0.042  0.036  0.007  165 ILE BBB CG1 
4891  C CG2 . ILE B 165 ? 0.570 0.594 0.598 0.056  0.032  0.011  165 ILE BBB CG2 
4892  C CD1 . ILE B 165 ? 0.597 0.624 0.630 0.041  0.034  0.008  165 ILE BBB CD1 
4893  N N   . THR B 166 ? 0.578 0.579 0.625 0.047  0.052  0.013  166 THR BBB N   
4894  C CA  . THR B 166 ? 0.557 0.552 0.612 0.043  0.058  0.013  166 THR BBB CA  
4895  C C   . THR B 166 ? 0.567 0.558 0.618 0.040  0.061  0.015  166 THR BBB C   
4896  O O   . THR B 166 ? 0.593 0.581 0.635 0.044  0.060  0.019  166 THR BBB O   
4897  C CB  . THR B 166 ? 0.564 0.549 0.620 0.048  0.064  0.016  166 THR BBB CB  
4898  O OG1 . THR B 166 ? 0.592 0.569 0.637 0.055  0.066  0.022  166 THR BBB OG1 
4899  C CG2 . THR B 166 ? 0.571 0.559 0.630 0.050  0.062  0.013  166 THR BBB CG2 
4900  N N   . SER B 167 ? 0.534 0.527 0.593 0.034  0.064  0.011  167 SER BBB N   
4901  C CA  . SER B 167 ? 0.511 0.501 0.570 0.031  0.066  0.012  167 SER BBB CA  
4902  C C   . SER B 167 ? 0.518 0.503 0.586 0.027  0.073  0.009  167 SER BBB C   
4903  O O   . SER B 167 ? 0.518 0.507 0.596 0.024  0.073  0.005  167 SER BBB O   
4904  C CB  . SER B 167 ? 0.506 0.506 0.564 0.026  0.061  0.008  167 SER BBB CB  
4905  O OG  . SER B 167 ? 0.525 0.522 0.577 0.026  0.061  0.011  167 SER BBB OG  
4906  N N   . ARG B 168 ? 0.526 0.503 0.593 0.026  0.078  0.012  168 ARG BBB N   
4907  C CA  . ARG B 168 ? 0.518 0.492 0.595 0.022  0.084  0.009  168 ARG BBB CA  
4908  C C   . ARG B 168 ? 0.489 0.474 0.573 0.015  0.080  0.002  168 ARG BBB C   
4909  O O   . ARG B 168 ? 0.502 0.490 0.597 0.012  0.082  -0.003 168 ARG BBB O   
4910  C CB  . ARG B 168 ? 0.564 0.530 0.638 0.022  0.090  0.013  168 ARG BBB CB  
4911  C CG  . ARG B 168 ? 0.612 0.572 0.696 0.018  0.098  0.010  168 ARG BBB CG  
4912  C CD  . ARG B 168 ? 0.672 0.620 0.751 0.021  0.105  0.015  168 ARG BBB CD  
4913  N NE  . ARG B 168 ? 0.721 0.665 0.811 0.016  0.112  0.011  168 ARG BBB NE  
4914  C CZ  . ARG B 168 ? 0.720 0.655 0.810 0.016  0.120  0.014  168 ARG BBB CZ  
4915  N NH1 . ARG B 168 ? 0.756 0.684 0.833 0.021  0.121  0.021  168 ARG BBB NH1 
4916  N NH2 . ARG B 168 ? 0.693 0.626 0.795 0.011  0.126  0.009  168 ARG BBB NH2 
4917  N N   . TYR B 169 ? 0.463 0.454 0.541 0.014  0.074  0.002  169 TYR BBB N   
4918  C CA  . TYR B 169 ? 0.442 0.444 0.524 0.009  0.070  -0.004 169 TYR BBB CA  
4919  C C   . TYR B 169 ? 0.423 0.432 0.498 0.010  0.063  -0.004 169 TYR BBB C   
4920  O O   . TYR B 169 ? 0.435 0.443 0.502 0.013  0.060  0.000  169 TYR BBB O   
4921  C CB  . TYR B 169 ? 0.441 0.440 0.522 0.007  0.072  -0.004 169 TYR BBB CB  
4922  C CG  . TYR B 169 ? 0.445 0.437 0.533 0.005  0.080  -0.004 169 TYR BBB CG  
4923  C CD1 . TYR B 169 ? 0.441 0.435 0.541 0.002  0.083  -0.010 169 TYR BBB CD1 
4924  C CD2 . TYR B 169 ? 0.468 0.451 0.551 0.007  0.085  0.001  169 TYR BBB CD2 
4925  C CE1 . TYR B 169 ? 0.439 0.425 0.547 0.001  0.091  -0.011 169 TYR BBB CE1 
4926  C CE2 . TYR B 169 ? 0.454 0.429 0.544 0.006  0.093  -0.000 169 TYR BBB CE2 
4927  C CZ  . TYR B 169 ? 0.436 0.414 0.540 0.002  0.096  -0.006 169 TYR BBB CZ  
4928  O OH  . TYR B 169 ? 0.428 0.398 0.540 0.001  0.104  -0.007 169 TYR BBB OH  
4929  N N   . ILE B 170 ? 0.414 0.432 0.495 0.006  0.059  -0.010 170 ILE BBB N   
4930  C CA  . ILE B 170 ? 0.401 0.427 0.477 0.006  0.053  -0.011 170 ILE BBB CA  
4931  C C   . ILE B 170 ? 0.378 0.411 0.455 0.001  0.050  -0.015 170 ILE BBB C   
4932  O O   . ILE B 170 ? 0.425 0.458 0.509 -0.002 0.053  -0.019 170 ILE BBB O   
4933  C CB  . ILE B 170 ? 0.406 0.437 0.486 0.006  0.051  -0.013 170 ILE BBB CB  
4934  C CG1 . ILE B 170 ? 0.415 0.440 0.492 0.012  0.052  -0.009 170 ILE BBB CG1 
4935  C CG2 . ILE B 170 ? 0.423 0.462 0.499 0.005  0.045  -0.015 170 ILE BBB CG2 
4936  C CD1 . ILE B 170 ? 0.413 0.440 0.496 0.012  0.052  -0.012 170 ILE BBB CD1 
4937  N N   . LEU B 171 ? 0.334 0.369 0.403 0.001  0.046  -0.013 171 LEU BBB N   
4938  C CA  . LEU B 171 ? 0.310 0.351 0.379 -0.002 0.044  -0.016 171 LEU BBB CA  
4939  C C   . LEU B 171 ? 0.287 0.334 0.352 -0.003 0.039  -0.018 171 LEU BBB C   
4940  O O   . LEU B 171 ? 0.274 0.322 0.334 -0.001 0.037  -0.015 171 LEU BBB O   
4941  C CB  . LEU B 171 ? 0.312 0.350 0.374 -0.002 0.044  -0.013 171 LEU BBB CB  
4942  C CG  . LEU B 171 ? 0.305 0.348 0.365 -0.005 0.041  -0.016 171 LEU BBB CG  
4943  C CD1 . LEU B 171 ? 0.314 0.360 0.381 -0.008 0.042  -0.021 171 LEU BBB CD1 
4944  C CD2 . LEU B 171 ? 0.315 0.355 0.369 -0.005 0.041  -0.012 171 LEU BBB CD2 
4945  N N   . LEU B 172 ? 0.278 0.332 0.348 -0.006 0.038  -0.023 172 LEU BBB N   
4946  C CA  . LEU B 172 ? 0.274 0.333 0.340 -0.007 0.034  -0.025 172 LEU BBB CA  
4947  C C   . LEU B 172 ? 0.269 0.331 0.330 -0.009 0.032  -0.025 172 LEU BBB C   
4948  O O   . LEU B 172 ? 0.262 0.324 0.326 -0.010 0.033  -0.027 172 LEU BBB O   
4949  C CB  . LEU B 172 ? 0.269 0.333 0.343 -0.008 0.034  -0.030 172 LEU BBB CB  
4950  C CG  . LEU B 172 ? 0.276 0.337 0.355 -0.007 0.037  -0.030 172 LEU BBB CG  
4951  C CD1 . LEU B 172 ? 0.280 0.345 0.367 -0.008 0.037  -0.035 172 LEU BBB CD1 
4952  C CD2 . LEU B 172 ? 0.273 0.333 0.349 -0.004 0.035  -0.027 172 LEU BBB CD2 
4953  N N   . ALA B 173 ? 0.277 0.340 0.331 -0.008 0.029  -0.023 173 ALA BBB N   
4954  C CA  . ALA B 173 ? 0.278 0.343 0.326 -0.010 0.027  -0.023 173 ALA BBB CA  
4955  C C   . ALA B 173 ? 0.279 0.347 0.323 -0.010 0.025  -0.023 173 ALA BBB C   
4956  O O   . ALA B 173 ? 0.259 0.327 0.298 -0.009 0.023  -0.021 173 ALA BBB O   
4957  C CB  . ALA B 173 ? 0.279 0.340 0.324 -0.009 0.028  -0.020 173 ALA BBB CB  
4958  N N   . THR B 174 ? 0.296 0.368 0.343 -0.011 0.024  -0.026 174 THR BBB N   
4959  C CA  . THR B 174 ? 0.294 0.370 0.339 -0.011 0.022  -0.027 174 THR BBB CA  
4960  C C   . THR B 174 ? 0.288 0.366 0.328 -0.013 0.021  -0.028 174 THR BBB C   
4961  O O   . THR B 174 ? 0.292 0.372 0.329 -0.014 0.020  -0.029 174 THR BBB O   
4962  C CB  . THR B 174 ? 0.283 0.360 0.332 -0.010 0.023  -0.029 174 THR BBB CB  
4963  O OG1 . THR B 174 ? 0.259 0.338 0.313 -0.012 0.024  -0.032 174 THR BBB OG1 
4964  C CG2 . THR B 174 ? 0.286 0.361 0.339 -0.008 0.024  -0.027 174 THR BBB CG2 
4965  N N   . GLY B 175 ? 0.283 0.360 0.322 -0.014 0.022  -0.029 175 GLY BBB N   
4966  C CA  . GLY B 175 ? 0.293 0.371 0.326 -0.015 0.021  -0.030 175 GLY BBB CA  
4967  C C   . GLY B 175 ? 0.296 0.377 0.329 -0.016 0.021  -0.033 175 GLY BBB C   
4968  O O   . GLY B 175 ? 0.304 0.387 0.342 -0.016 0.022  -0.035 175 GLY BBB O   
4969  N N   . GLY B 176 ? 0.298 0.379 0.325 -0.017 0.021  -0.034 176 GLY BBB N   
4970  C CA  . GLY B 176 ? 0.296 0.380 0.322 -0.018 0.021  -0.036 176 GLY BBB CA  
4971  C C   . GLY B 176 ? 0.302 0.386 0.325 -0.019 0.022  -0.035 176 GLY BBB C   
4972  O O   . GLY B 176 ? 0.279 0.362 0.301 -0.019 0.021  -0.033 176 GLY BBB O   
4973  N N   . ARG B 177 ? 0.307 0.392 0.328 -0.019 0.023  -0.037 177 ARG BBB N   
4974  C CA  . ARG B 177 ? 0.303 0.388 0.320 -0.021 0.024  -0.037 177 ARG BBB CA  
4975  C C   . ARG B 177 ? 0.295 0.379 0.306 -0.021 0.026  -0.038 177 ARG BBB C   
4976  O O   . ARG B 177 ? 0.266 0.351 0.277 -0.020 0.026  -0.040 177 ARG BBB O   
4977  C CB  . ARG B 177 ? 0.313 0.401 0.336 -0.021 0.025  -0.038 177 ARG BBB CB  
4978  C CG  . ARG B 177 ? 0.325 0.413 0.352 -0.020 0.023  -0.037 177 ARG BBB CG  
4979  C CD  . ARG B 177 ? 0.318 0.404 0.341 -0.020 0.022  -0.034 177 ARG BBB CD  
4980  N NE  . ARG B 177 ? 0.317 0.405 0.339 -0.022 0.023  -0.035 177 ARG BBB NE  
4981  C CZ  . ARG B 177 ? 0.322 0.413 0.349 -0.022 0.023  -0.037 177 ARG BBB CZ  
4982  N NH1 . ARG B 177 ? 0.306 0.398 0.337 -0.020 0.021  -0.036 177 ARG BBB NH1 
4983  N NH2 . ARG B 177 ? 0.321 0.413 0.347 -0.023 0.024  -0.038 177 ARG BBB NH2 
4984  N N   . PRO B 178 ? 0.315 0.397 0.321 -0.022 0.028  -0.037 178 PRO BBB N   
4985  C CA  . PRO B 178 ? 0.348 0.428 0.347 -0.022 0.030  -0.038 178 PRO BBB CA  
4986  C C   . PRO B 178 ? 0.386 0.468 0.386 -0.022 0.031  -0.041 178 PRO BBB C   
4987  O O   . PRO B 178 ? 0.401 0.486 0.408 -0.023 0.032  -0.043 178 PRO BBB O   
4988  C CB  . PRO B 178 ? 0.348 0.425 0.342 -0.024 0.033  -0.037 178 PRO BBB CB  
4989  C CG  . PRO B 178 ? 0.338 0.416 0.335 -0.024 0.031  -0.035 178 PRO BBB CG  
4990  C CD  . PRO B 178 ? 0.322 0.403 0.327 -0.024 0.028  -0.036 178 PRO BBB CD  
4991  N N   . SER B 179 ? 0.429 0.510 0.424 -0.020 0.032  -0.042 179 SER BBB N   
4992  C CA  . SER B 179 ? 0.462 0.545 0.458 -0.020 0.033  -0.045 179 SER BBB CA  
4993  C C   . SER B 179 ? 0.449 0.529 0.437 -0.020 0.037  -0.045 179 SER BBB C   
4994  O O   . SER B 179 ? 0.414 0.489 0.393 -0.019 0.038  -0.043 179 SER BBB O   
4995  C CB  . SER B 179 ? 0.491 0.576 0.487 -0.018 0.031  -0.047 179 SER BBB CB  
4996  O OG  . SER B 179 ? 0.562 0.651 0.562 -0.017 0.032  -0.050 179 SER BBB OG  
4997  N N   . ILE B 180 ? 0.481 0.562 0.472 -0.022 0.039  -0.047 180 ILE BBB N   
4998  C CA  . ILE B 180 ? 0.492 0.570 0.476 -0.022 0.044  -0.047 180 ILE BBB CA  
4999  C C   . ILE B 180 ? 0.487 0.567 0.472 -0.021 0.045  -0.050 180 ILE BBB C   
5000  O O   . ILE B 180 ? 0.484 0.569 0.478 -0.022 0.043  -0.052 180 ILE BBB O   
5001  C CB  . ILE B 180 ? 0.501 0.579 0.490 -0.026 0.047  -0.047 180 ILE BBB CB  
5002  C CG1 . ILE B 180 ? 0.501 0.577 0.491 -0.027 0.045  -0.045 180 ILE BBB CG1 
5003  C CG2 . ILE B 180 ? 0.507 0.581 0.489 -0.027 0.052  -0.048 180 ILE BBB CG2 
5004  C CD1 . ILE B 180 ? 0.519 0.596 0.514 -0.030 0.048  -0.046 180 ILE BBB CD1 
5005  N N   . PRO B 181 ? 0.523 0.600 0.498 -0.019 0.047  -0.050 181 PRO BBB N   
5006  C CA  . PRO B 181 ? 0.513 0.593 0.488 -0.018 0.048  -0.053 181 PRO BBB CA  
5007  C C   . PRO B 181 ? 0.527 0.607 0.506 -0.020 0.051  -0.055 181 PRO BBB C   
5008  O O   . PRO B 181 ? 0.481 0.557 0.456 -0.022 0.056  -0.054 181 PRO BBB O   
5009  C CB  . PRO B 181 ? 0.538 0.613 0.499 -0.014 0.050  -0.052 181 PRO BBB CB  
5010  C CG  . PRO B 181 ? 0.529 0.598 0.484 -0.015 0.052  -0.048 181 PRO BBB CG  
5011  C CD  . PRO B 181 ? 0.532 0.603 0.496 -0.017 0.049  -0.047 181 PRO BBB CD  
5012  N N   . GLU B 182 ? 0.606 0.692 0.594 -0.021 0.049  -0.058 182 GLU BBB N   
5013  C CA  . GLU B 182 ? 0.694 0.782 0.689 -0.023 0.052  -0.061 182 GLU BBB CA  
5014  C C   . GLU B 182 ? 0.714 0.801 0.702 -0.023 0.056  -0.062 182 GLU BBB C   
5015  O O   . GLU B 182 ? 0.686 0.771 0.676 -0.025 0.060  -0.064 182 GLU BBB O   
5016  C CB  . GLU B 182 ? 0.739 0.834 0.746 -0.024 0.048  -0.063 182 GLU BBB CB  
5017  C CG  . GLU B 182 ? 0.788 0.884 0.802 -0.025 0.045  -0.062 182 GLU BBB CG  
5018  C CD  . GLU B 182 ? 0.898 0.997 0.917 -0.023 0.040  -0.062 182 GLU BBB CD  
5019  O OE1 . GLU B 182 ? 0.912 1.013 0.932 -0.021 0.039  -0.065 182 GLU BBB OE1 
5020  O OE2 . GLU B 182 ? 0.922 1.020 0.942 -0.023 0.038  -0.060 182 GLU BBB OE2 
5021  N N   . THR B 183 ? 0.750 0.835 0.729 -0.019 0.055  -0.062 183 THR BBB N   
5022  C CA  . THR B 183 ? 0.789 0.872 0.759 -0.017 0.059  -0.063 183 THR BBB CA  
5023  C C   . THR B 183 ? 0.769 0.844 0.729 -0.017 0.065  -0.060 183 THR BBB C   
5024  O O   . THR B 183 ? 0.716 0.788 0.672 -0.018 0.070  -0.061 183 THR BBB O   
5025  C CB  . THR B 183 ? 0.809 0.893 0.773 -0.012 0.056  -0.064 183 THR BBB CB  
5026  O OG1 . THR B 183 ? 0.850 0.930 0.807 -0.010 0.054  -0.061 183 THR BBB OG1 
5027  C CG2 . THR B 183 ? 0.808 0.900 0.784 -0.012 0.051  -0.068 183 THR BBB CG2 
5028  N N   . VAL B 184 ? 0.732 0.803 0.688 -0.018 0.065  -0.057 184 VAL BBB N   
5029  C CA  . VAL B 184 ? 0.719 0.781 0.665 -0.018 0.071  -0.054 184 VAL BBB CA  
5030  C C   . VAL B 184 ? 0.689 0.751 0.644 -0.023 0.075  -0.055 184 VAL BBB C   
5031  O O   . VAL B 184 ? 0.677 0.742 0.640 -0.026 0.073  -0.055 184 VAL BBB O   
5032  C CB  . VAL B 184 ? 0.682 0.740 0.621 -0.016 0.070  -0.050 184 VAL BBB CB  
5033  C CG1 . VAL B 184 ? 0.698 0.748 0.630 -0.018 0.076  -0.047 184 VAL BBB CG1 
5034  C CG2 . VAL B 184 ? 0.701 0.759 0.631 -0.011 0.067  -0.050 184 VAL BBB CG2 
5035  N N   . PRO B 185 ? 0.704 0.763 0.656 -0.025 0.081  -0.056 185 PRO BBB N   
5036  C CA  . PRO B 185 ? 0.686 0.746 0.648 -0.030 0.085  -0.058 185 PRO BBB CA  
5037  C C   . PRO B 185 ? 0.657 0.713 0.618 -0.032 0.088  -0.056 185 PRO BBB C   
5038  O O   . PRO B 185 ? 0.658 0.706 0.608 -0.030 0.091  -0.053 185 PRO BBB O   
5039  C CB  . PRO B 185 ? 0.703 0.760 0.660 -0.030 0.092  -0.060 185 PRO BBB CB  
5040  C CG  . PRO B 185 ? 0.724 0.780 0.671 -0.025 0.091  -0.059 185 PRO BBB CG  
5041  C CD  . PRO B 185 ? 0.741 0.797 0.683 -0.022 0.085  -0.056 185 PRO BBB CD  
5042  N N   . GLY B 186 ? 0.599 0.660 0.573 -0.036 0.087  -0.058 186 GLY BBB N   
5043  C CA  . GLY B 186 ? 0.625 0.683 0.601 -0.038 0.088  -0.057 186 GLY BBB CA  
5044  C C   . GLY B 186 ? 0.603 0.662 0.578 -0.037 0.082  -0.054 186 GLY BBB C   
5045  O O   . GLY B 186 ? 0.589 0.648 0.569 -0.039 0.082  -0.054 186 GLY BBB O   
5046  N N   . ALA B 187 ? 0.587 0.647 0.558 -0.033 0.077  -0.052 187 ALA BBB N   
5047  C CA  . ALA B 187 ? 0.575 0.636 0.545 -0.031 0.072  -0.050 187 ALA BBB CA  
5048  C C   . ALA B 187 ? 0.562 0.629 0.544 -0.034 0.068  -0.051 187 ALA BBB C   
5049  O O   . ALA B 187 ? 0.568 0.633 0.550 -0.035 0.067  -0.049 187 ALA BBB O   
5050  C CB  . ALA B 187 ? 0.568 0.630 0.533 -0.027 0.067  -0.049 187 ALA BBB CB  
5051  N N   . ILE B 188 ? 0.537 0.610 0.528 -0.034 0.065  -0.054 188 ILE BBB N   
5052  C CA  . ILE B 188 ? 0.522 0.601 0.524 -0.035 0.060  -0.055 188 ILE BBB CA  
5053  C C   . ILE B 188 ? 0.538 0.617 0.544 -0.039 0.063  -0.057 188 ILE BBB C   
5054  O O   . ILE B 188 ? 0.539 0.621 0.550 -0.039 0.060  -0.056 188 ILE BBB O   
5055  C CB  . ILE B 188 ? 0.536 0.621 0.546 -0.035 0.058  -0.058 188 ILE BBB CB  
5056  C CG1 . ILE B 188 ? 0.522 0.608 0.530 -0.032 0.053  -0.057 188 ILE BBB CG1 
5057  C CG2 . ILE B 188 ? 0.539 0.630 0.560 -0.036 0.056  -0.061 188 ILE BBB CG2 
5058  C CD1 . ILE B 188 ? 0.508 0.599 0.521 -0.031 0.052  -0.059 188 ILE BBB CD1 
5059  N N   . GLN B 189 ? 0.580 0.657 0.586 -0.041 0.069  -0.059 189 GLN BBB N   
5060  C CA  . GLN B 189 ? 0.589 0.668 0.602 -0.044 0.073  -0.062 189 GLN BBB CA  
5061  C C   . GLN B 189 ? 0.582 0.655 0.590 -0.045 0.075  -0.059 189 GLN BBB C   
5062  O O   . GLN B 189 ? 0.636 0.712 0.650 -0.047 0.074  -0.061 189 GLN BBB O   
5063  C CB  . GLN B 189 ? 0.625 0.703 0.640 -0.046 0.079  -0.065 189 GLN BBB CB  
5064  C CG  . GLN B 189 ? 0.646 0.728 0.671 -0.050 0.081  -0.070 189 GLN BBB CG  
5065  C CD  . GLN B 189 ? 0.674 0.754 0.701 -0.052 0.088  -0.074 189 GLN BBB CD  
5066  O OE1 . GLN B 189 ? 0.675 0.754 0.698 -0.051 0.090  -0.074 189 GLN BBB OE1 
5067  N NE2 . GLN B 189 ? 0.705 0.786 0.739 -0.056 0.093  -0.077 189 GLN BBB NE2 
5068  N N   . TYR B 190 ? 0.537 0.603 0.533 -0.044 0.078  -0.056 190 TYR BBB N   
5069  C CA  . TYR B 190 ? 0.533 0.592 0.524 -0.045 0.083  -0.054 190 TYR BBB CA  
5070  C C   . TYR B 190 ? 0.481 0.537 0.465 -0.043 0.079  -0.050 190 TYR BBB C   
5071  O O   . TYR B 190 ? 0.478 0.530 0.460 -0.044 0.082  -0.048 190 TYR BBB O   
5072  C CB  . TYR B 190 ? 0.568 0.619 0.550 -0.046 0.091  -0.054 190 TYR BBB CB  
5073  C CG  . TYR B 190 ? 0.627 0.680 0.616 -0.049 0.096  -0.058 190 TYR BBB CG  
5074  C CD1 . TYR B 190 ? 0.638 0.695 0.638 -0.053 0.098  -0.062 190 TYR BBB CD1 
5075  C CD2 . TYR B 190 ? 0.642 0.693 0.627 -0.048 0.099  -0.059 190 TYR BBB CD2 
5076  C CE1 . TYR B 190 ? 0.645 0.704 0.653 -0.056 0.103  -0.067 190 TYR BBB CE1 
5077  C CE2 . TYR B 190 ? 0.645 0.699 0.638 -0.051 0.104  -0.064 190 TYR BBB CE2 
5078  C CZ  . TYR B 190 ? 0.650 0.707 0.654 -0.055 0.106  -0.068 190 TYR BBB CZ  
5079  O OH  . TYR B 190 ? 0.734 0.793 0.745 -0.058 0.112  -0.073 190 TYR BBB OH  
5080  N N   . SER B 191 ? 0.439 0.497 0.419 -0.039 0.074  -0.048 191 SER BBB N   
5081  C CA  . SER B 191 ? 0.449 0.504 0.423 -0.037 0.070  -0.044 191 SER BBB CA  
5082  C C   . SER B 191 ? 0.419 0.480 0.401 -0.037 0.065  -0.044 191 SER BBB C   
5083  O O   . SER B 191 ? 0.433 0.500 0.424 -0.038 0.062  -0.046 191 SER BBB O   
5084  C CB  . SER B 191 ? 0.462 0.516 0.429 -0.033 0.067  -0.042 191 SER BBB CB  
5085  O OG  . SER B 191 ? 0.489 0.541 0.450 -0.032 0.072  -0.043 191 SER BBB OG  
5086  N N   . ILE B 192 ? 0.403 0.461 0.380 -0.036 0.063  -0.041 192 ILE BBB N   
5087  C CA  . ILE B 192 ? 0.385 0.447 0.367 -0.036 0.058  -0.040 192 ILE BBB CA  
5088  C C   . ILE B 192 ? 0.367 0.429 0.345 -0.032 0.053  -0.037 192 ILE BBB C   
5089  O O   . ILE B 192 ? 0.364 0.423 0.335 -0.030 0.054  -0.036 192 ILE BBB O   
5090  C CB  . ILE B 192 ? 0.387 0.447 0.369 -0.037 0.059  -0.039 192 ILE BBB CB  
5091  C CG1 . ILE B 192 ? 0.404 0.456 0.375 -0.036 0.062  -0.036 192 ILE BBB CG1 
5092  C CG2 . ILE B 192 ? 0.379 0.440 0.368 -0.041 0.063  -0.043 192 ILE BBB CG2 
5093  C CD1 . ILE B 192 ? 0.414 0.464 0.385 -0.037 0.062  -0.034 192 ILE BBB CD1 
5094  N N   . THR B 193 ? 0.340 0.405 0.321 -0.032 0.048  -0.036 193 THR BBB N   
5095  C CA  . THR B 193 ? 0.322 0.387 0.301 -0.029 0.044  -0.034 193 THR BBB CA  
5096  C C   . THR B 193 ? 0.327 0.391 0.305 -0.029 0.042  -0.032 193 THR BBB C   
5097  O O   . THR B 193 ? 0.318 0.382 0.298 -0.031 0.044  -0.032 193 THR BBB O   
5098  C CB  . THR B 193 ? 0.316 0.387 0.302 -0.028 0.041  -0.036 193 THR BBB CB  
5099  O OG1 . THR B 193 ? 0.308 0.382 0.302 -0.029 0.039  -0.037 193 THR BBB OG1 
5100  C CG2 . THR B 193 ? 0.325 0.397 0.312 -0.028 0.043  -0.039 193 THR BBB CG2 
5101  N N   . SER B 194 ? 0.320 0.385 0.298 -0.027 0.038  -0.030 194 SER BBB N   
5102  C CA  . SER B 194 ? 0.320 0.385 0.297 -0.026 0.035  -0.028 194 SER BBB CA  
5103  C C   . SER B 194 ? 0.316 0.385 0.301 -0.028 0.034  -0.029 194 SER BBB C   
5104  O O   . SER B 194 ? 0.322 0.391 0.308 -0.028 0.033  -0.028 194 SER BBB O   
5105  C CB  . SER B 194 ? 0.313 0.378 0.289 -0.024 0.032  -0.027 194 SER BBB CB  
5106  O OG  . SER B 194 ? 0.311 0.379 0.292 -0.023 0.030  -0.029 194 SER BBB OG  
5107  N N   . ASP B 195 ? 0.307 0.380 0.299 -0.028 0.033  -0.031 195 ASP BBB N   
5108  C CA  . ASP B 195 ? 0.301 0.378 0.300 -0.028 0.032  -0.033 195 ASP BBB CA  
5109  C C   . ASP B 195 ? 0.282 0.359 0.282 -0.031 0.034  -0.034 195 ASP BBB C   
5110  O O   . ASP B 195 ? 0.258 0.339 0.263 -0.031 0.032  -0.035 195 ASP BBB O   
5111  C CB  . ASP B 195 ? 0.310 0.391 0.315 -0.028 0.031  -0.035 195 ASP BBB CB  
5112  C CG  . ASP B 195 ? 0.322 0.404 0.329 -0.026 0.028  -0.034 195 ASP BBB CG  
5113  O OD1 . ASP B 195 ? 0.300 0.379 0.303 -0.025 0.027  -0.032 195 ASP BBB OD1 
5114  O OD2 . ASP B 195 ? 0.349 0.433 0.361 -0.025 0.028  -0.036 195 ASP BBB OD2 
5115  N N   . ASP B 196 ? 0.276 0.350 0.272 -0.032 0.038  -0.035 196 ASP BBB N   
5116  C CA  . ASP B 196 ? 0.281 0.355 0.280 -0.035 0.042  -0.037 196 ASP BBB CA  
5117  C C   . ASP B 196 ? 0.279 0.348 0.271 -0.036 0.044  -0.035 196 ASP BBB C   
5118  O O   . ASP B 196 ? 0.269 0.339 0.265 -0.038 0.045  -0.037 196 ASP BBB O   
5119  C CB  . ASP B 196 ? 0.290 0.364 0.290 -0.037 0.046  -0.040 196 ASP BBB CB  
5120  C CG  . ASP B 196 ? 0.294 0.372 0.298 -0.036 0.044  -0.042 196 ASP BBB CG  
5121  O OD1 . ASP B 196 ? 0.273 0.356 0.285 -0.035 0.041  -0.044 196 ASP BBB OD1 
5122  O OD2 . ASP B 196 ? 0.307 0.382 0.308 -0.035 0.045  -0.041 196 ASP BBB OD2 
5123  N N   . ILE B 197 ? 0.275 0.339 0.259 -0.034 0.044  -0.032 197 ILE BBB N   
5124  C CA  . ILE B 197 ? 0.298 0.356 0.275 -0.035 0.047  -0.030 197 ILE BBB CA  
5125  C C   . ILE B 197 ? 0.310 0.368 0.288 -0.035 0.046  -0.029 197 ILE BBB C   
5126  O O   . ILE B 197 ? 0.309 0.365 0.286 -0.037 0.049  -0.030 197 ILE BBB O   
5127  C CB  . ILE B 197 ? 0.310 0.364 0.279 -0.032 0.047  -0.027 197 ILE BBB CB  
5128  C CG1 . ILE B 197 ? 0.314 0.360 0.274 -0.033 0.051  -0.025 197 ILE BBB CG1 
5129  C CG2 . ILE B 197 ? 0.310 0.366 0.279 -0.030 0.042  -0.026 197 ILE BBB CG2 
5130  C CD1 . ILE B 197 ? 0.314 0.357 0.274 -0.035 0.057  -0.027 197 ILE BBB CD1 
5131  N N   . PHE B 198 ? 0.309 0.372 0.292 -0.034 0.041  -0.029 198 PHE BBB N   
5132  C CA  . PHE B 198 ? 0.331 0.394 0.314 -0.034 0.039  -0.028 198 PHE BBB CA  
5133  C C   . PHE B 198 ? 0.344 0.412 0.334 -0.036 0.040  -0.031 198 PHE BBB C   
5134  O O   . PHE B 198 ? 0.342 0.410 0.332 -0.036 0.039  -0.031 198 PHE BBB O   
5135  C CB  . PHE B 198 ? 0.337 0.403 0.320 -0.032 0.034  -0.026 198 PHE BBB CB  
5136  C CG  . PHE B 198 ? 0.355 0.417 0.333 -0.030 0.033  -0.023 198 PHE BBB CG  
5137  C CD1 . PHE B 198 ? 0.351 0.408 0.321 -0.029 0.035  -0.021 198 PHE BBB CD1 
5138  C CD2 . PHE B 198 ? 0.361 0.425 0.340 -0.028 0.031  -0.023 198 PHE BBB CD2 
5139  C CE1 . PHE B 198 ? 0.341 0.395 0.305 -0.027 0.034  -0.020 198 PHE BBB CE1 
5140  C CE2 . PHE B 198 ? 0.343 0.405 0.318 -0.027 0.030  -0.022 198 PHE BBB CE2 
5141  C CZ  . PHE B 198 ? 0.335 0.392 0.302 -0.026 0.032  -0.020 198 PHE BBB CZ  
5142  N N   . PHE B 199 ? 0.372 0.444 0.368 -0.037 0.041  -0.035 199 PHE BBB N   
5143  C CA  . PHE B 199 ? 0.366 0.443 0.370 -0.038 0.040  -0.039 199 PHE BBB CA  
5144  C C   . PHE B 199 ? 0.357 0.434 0.365 -0.041 0.046  -0.043 199 PHE BBB C   
5145  O O   . PHE B 199 ? 0.333 0.416 0.348 -0.042 0.046  -0.047 199 PHE BBB O   
5146  C CB  . PHE B 199 ? 0.366 0.449 0.375 -0.036 0.036  -0.040 199 PHE BBB CB  
5147  C CG  . PHE B 199 ? 0.403 0.486 0.410 -0.033 0.031  -0.036 199 PHE BBB CG  
5148  C CD1 . PHE B 199 ? 0.425 0.508 0.430 -0.032 0.030  -0.035 199 PHE BBB CD1 
5149  C CD2 . PHE B 199 ? 0.419 0.501 0.424 -0.031 0.030  -0.034 199 PHE BBB CD2 
5150  C CE1 . PHE B 199 ? 0.435 0.516 0.436 -0.030 0.026  -0.031 199 PHE BBB CE1 
5151  C CE2 . PHE B 199 ? 0.434 0.516 0.437 -0.029 0.026  -0.031 199 PHE BBB CE2 
5152  C CZ  . PHE B 199 ? 0.419 0.500 0.419 -0.028 0.025  -0.029 199 PHE BBB CZ  
5153  N N   . LEU B 200 ? 0.374 0.445 0.377 -0.043 0.050  -0.042 200 LEU BBB N   
5154  C CA  . LEU B 200 ? 0.404 0.474 0.409 -0.046 0.057  -0.045 200 LEU BBB CA  
5155  C C   . LEU B 200 ? 0.414 0.486 0.425 -0.048 0.058  -0.049 200 LEU BBB C   
5156  O O   . LEU B 200 ? 0.389 0.458 0.396 -0.048 0.058  -0.047 200 LEU BBB O   
5157  C CB  . LEU B 200 ? 0.415 0.476 0.411 -0.046 0.062  -0.042 200 LEU BBB CB  
5158  C CG  . LEU B 200 ? 0.430 0.488 0.420 -0.044 0.062  -0.040 200 LEU BBB CG  
5159  C CD1 . LEU B 200 ? 0.440 0.489 0.421 -0.044 0.067  -0.038 200 LEU BBB CD1 
5160  C CD2 . LEU B 200 ? 0.430 0.493 0.427 -0.045 0.062  -0.044 200 LEU BBB CD2 
5161  N N   . SER B 201 ? 0.443 0.521 0.463 -0.050 0.060  -0.055 201 SER BBB N   
5162  C CA  . SER B 201 ? 0.464 0.545 0.492 -0.053 0.062  -0.060 201 SER BBB CA  
5163  C C   . SER B 201 ? 0.455 0.528 0.478 -0.056 0.070  -0.059 201 SER BBB C   
5164  O O   . SER B 201 ? 0.457 0.531 0.484 -0.057 0.071  -0.061 201 SER BBB O   
5165  C CB  . SER B 201 ? 0.501 0.590 0.540 -0.054 0.063  -0.067 201 SER BBB CB  
5166  O OG  . SER B 201 ? 0.552 0.647 0.594 -0.051 0.058  -0.067 201 SER BBB OG  
5167  N N   . LYS B 202 ? 0.472 0.537 0.489 -0.056 0.074  -0.056 202 LYS BBB N   
5168  C CA  . LYS B 202 ? 0.530 0.586 0.541 -0.058 0.082  -0.055 202 LYS BBB CA  
5169  C C   . LYS B 202 ? 0.482 0.530 0.480 -0.055 0.082  -0.048 202 LYS BBB C   
5170  O O   . LYS B 202 ? 0.476 0.525 0.470 -0.053 0.078  -0.045 202 LYS BBB O   
5171  C CB  . LYS B 202 ? 0.598 0.652 0.613 -0.061 0.090  -0.059 202 LYS BBB CB  
5172  C CG  . LYS B 202 ? 0.681 0.742 0.709 -0.064 0.091  -0.067 202 LYS BBB CG  
5173  C CD  . LYS B 202 ? 0.726 0.790 0.760 -0.066 0.092  -0.070 202 LYS BBB CD  
5174  C CE  . LYS B 202 ? 0.743 0.818 0.792 -0.068 0.091  -0.078 202 LYS BBB CE  
5175  N NZ  . LYS B 202 ? 0.792 0.870 0.847 -0.070 0.091  -0.082 202 LYS BBB NZ  
5176  N N   . SER B 203 ? 0.450 0.489 0.441 -0.056 0.086  -0.046 203 SER BBB N   
5177  C CA  . SER B 203 ? 0.452 0.483 0.430 -0.053 0.087  -0.039 203 SER BBB CA  
5178  C C   . SER B 203 ? 0.445 0.472 0.417 -0.052 0.090  -0.038 203 SER BBB C   
5179  O O   . SER B 203 ? 0.444 0.471 0.421 -0.055 0.096  -0.042 203 SER BBB O   
5180  C CB  . SER B 203 ? 0.450 0.473 0.422 -0.054 0.091  -0.037 203 SER BBB CB  
5181  O OG  . SER B 203 ? 0.458 0.474 0.430 -0.056 0.101  -0.039 203 SER BBB OG  
5182  N N   . PRO B 204 ? 0.429 0.453 0.392 -0.048 0.087  -0.034 204 PRO BBB N   
5183  C CA  . PRO B 204 ? 0.429 0.452 0.388 -0.047 0.089  -0.033 204 PRO BBB CA  
5184  C C   . PRO B 204 ? 0.440 0.452 0.389 -0.047 0.097  -0.032 204 PRO BBB C   
5185  O O   . PRO B 204 ? 0.432 0.443 0.379 -0.046 0.100  -0.032 204 PRO BBB O   
5186  C CB  . PRO B 204 ? 0.424 0.448 0.376 -0.042 0.082  -0.030 204 PRO BBB CB  
5187  C CG  . PRO B 204 ? 0.432 0.453 0.380 -0.041 0.080  -0.027 204 PRO BBB CG  
5188  C CD  . PRO B 204 ? 0.437 0.462 0.395 -0.045 0.081  -0.030 204 PRO BBB CD  
5189  N N   . GLY B 205 ? 0.449 0.455 0.395 -0.048 0.102  -0.030 205 GLY BBB N   
5190  C CA  . GLY B 205 ? 0.473 0.466 0.408 -0.047 0.110  -0.028 205 GLY BBB CA  
5191  C C   . GLY B 205 ? 0.492 0.481 0.414 -0.042 0.109  -0.023 205 GLY BBB C   
5192  O O   . GLY B 205 ? 0.505 0.498 0.425 -0.038 0.101  -0.021 205 GLY BBB O   
5193  N N   . LYS B 206 ? 0.488 0.469 0.402 -0.041 0.116  -0.022 206 LYS BBB N   
5194  C CA  . LYS B 206 ? 0.504 0.480 0.404 -0.035 0.115  -0.018 206 LYS BBB CA  
5195  C C   . LYS B 206 ? 0.475 0.461 0.380 -0.034 0.108  -0.020 206 LYS BBB C   
5196  O O   . LYS B 206 ? 0.487 0.478 0.401 -0.037 0.108  -0.024 206 LYS BBB O   
5197  C CB  . LYS B 206 ? 0.540 0.505 0.432 -0.035 0.125  -0.017 206 LYS BBB CB  
5198  C CG  . LYS B 206 ? 0.558 0.520 0.437 -0.030 0.125  -0.015 206 LYS BBB CG  
5199  C CD  . LYS B 206 ? 0.579 0.529 0.447 -0.028 0.136  -0.012 206 LYS BBB CD  
5200  C CE  . LYS B 206 ? 0.603 0.548 0.455 -0.021 0.134  -0.009 206 LYS BBB CE  
5201  N NZ  . LYS B 206 ? 0.637 0.572 0.480 -0.020 0.144  -0.008 206 LYS BBB NZ  
5202  N N   . THR B 207 ? 0.454 0.441 0.352 -0.029 0.101  -0.017 207 THR BBB N   
5203  C CA  . THR B 207 ? 0.456 0.453 0.361 -0.028 0.093  -0.019 207 THR BBB CA  
5204  C C   . THR B 207 ? 0.458 0.453 0.352 -0.023 0.091  -0.017 207 THR BBB C   
5205  O O   . THR B 207 ? 0.476 0.466 0.360 -0.019 0.091  -0.014 207 THR BBB O   
5206  C CB  . THR B 207 ? 0.426 0.431 0.338 -0.029 0.085  -0.019 207 THR BBB CB  
5207  O OG1 . THR B 207 ? 0.424 0.430 0.346 -0.034 0.087  -0.022 207 THR BBB OG1 
5208  C CG2 . THR B 207 ? 0.408 0.421 0.326 -0.028 0.078  -0.021 207 THR BBB CG2 
5209  N N   . LEU B 208 ? 0.449 0.451 0.348 -0.023 0.088  -0.020 208 LEU BBB N   
5210  C CA  . LEU B 208 ? 0.468 0.471 0.360 -0.018 0.084  -0.019 208 LEU BBB CA  
5211  C C   . LEU B 208 ? 0.431 0.445 0.333 -0.018 0.076  -0.021 208 LEU BBB C   
5212  O O   . LEU B 208 ? 0.412 0.432 0.325 -0.022 0.074  -0.024 208 LEU BBB O   
5213  C CB  . LEU B 208 ? 0.470 0.473 0.361 -0.018 0.088  -0.021 208 LEU BBB CB  
5214  C CG  . LEU B 208 ? 0.488 0.494 0.374 -0.013 0.084  -0.022 208 LEU BBB CG  
5215  C CD1 . LEU B 208 ? 0.493 0.492 0.363 -0.007 0.084  -0.018 208 LEU BBB CD1 
5216  C CD2 . LEU B 208 ? 0.513 0.520 0.400 -0.014 0.088  -0.024 208 LEU BBB CD2 
5217  N N   . VAL B 209 ? 0.418 0.433 0.315 -0.014 0.071  -0.020 209 VAL BBB N   
5218  C CA  . VAL B 209 ? 0.403 0.426 0.308 -0.013 0.063  -0.022 209 VAL BBB CA  
5219  C C   . VAL B 209 ? 0.395 0.420 0.294 -0.009 0.061  -0.023 209 VAL BBB C   
5220  O O   . VAL B 209 ? 0.380 0.400 0.267 -0.004 0.062  -0.021 209 VAL BBB O   
5221  C CB  . VAL B 209 ? 0.407 0.430 0.311 -0.012 0.059  -0.020 209 VAL BBB CB  
5222  C CG1 . VAL B 209 ? 0.415 0.446 0.326 -0.011 0.052  -0.021 209 VAL BBB CG1 
5223  C CG2 . VAL B 209 ? 0.412 0.434 0.320 -0.016 0.061  -0.019 209 VAL BBB CG2 
5224  N N   . ILE B 210 ? 0.376 0.408 0.284 -0.010 0.058  -0.026 210 ILE BBB N   
5225  C CA  . ILE B 210 ? 0.384 0.420 0.289 -0.006 0.056  -0.028 210 ILE BBB CA  
5226  C C   . ILE B 210 ? 0.376 0.417 0.287 -0.005 0.049  -0.030 210 ILE BBB C   
5227  O O   . ILE B 210 ? 0.375 0.422 0.297 -0.008 0.046  -0.031 210 ILE BBB O   
5228  C CB  . ILE B 210 ? 0.380 0.418 0.290 -0.008 0.058  -0.031 210 ILE BBB CB  
5229  C CG1 . ILE B 210 ? 0.378 0.410 0.283 -0.010 0.065  -0.030 210 ILE BBB CG1 
5230  C CG2 . ILE B 210 ? 0.384 0.426 0.291 -0.004 0.055  -0.033 210 ILE BBB CG2 
5231  C CD1 . ILE B 210 ? 0.375 0.409 0.292 -0.016 0.068  -0.031 210 ILE BBB CD1 
5232  N N   . GLY B 211 ? 0.384 0.426 0.288 -0.000 0.046  -0.030 211 GLY BBB N   
5233  C CA  . GLY B 211 ? 0.377 0.425 0.287 0.001  0.040  -0.031 211 GLY BBB CA  
5234  C C   . GLY B 211 ? 0.383 0.427 0.286 0.004  0.039  -0.029 211 GLY BBB C   
5235  O O   . GLY B 211 ? 0.378 0.418 0.280 0.001  0.041  -0.026 211 GLY BBB O   
5236  N N   . ALA B 212 ? 0.408 0.454 0.306 0.009  0.035  -0.030 212 ALA BBB N   
5237  C CA  . ALA B 212 ? 0.432 0.477 0.325 0.011  0.033  -0.029 212 ALA BBB CA  
5238  C C   . ALA B 212 ? 0.428 0.480 0.332 0.011  0.027  -0.032 212 ALA BBB C   
5239  O O   . ALA B 212 ? 0.430 0.483 0.331 0.014  0.024  -0.033 212 ALA BBB O   
5240  C CB  . ALA B 212 ? 0.445 0.487 0.326 0.018  0.033  -0.030 212 ALA BBB CB  
5241  N N   . SER B 213 ? 0.442 0.497 0.357 0.006  0.027  -0.033 213 SER BBB N   
5242  C CA  . SER B 213 ? 0.420 0.480 0.347 0.004  0.024  -0.034 213 SER BBB CA  
5243  C C   . SER B 213 ? 0.398 0.455 0.324 0.002  0.024  -0.031 213 SER BBB C   
5244  O O   . SER B 213 ? 0.387 0.438 0.306 0.002  0.027  -0.028 213 SER BBB O   
5245  C CB  . SER B 213 ? 0.407 0.471 0.344 -0.000 0.024  -0.035 213 SER BBB CB  
5246  O OG  . SER B 213 ? 0.389 0.448 0.324 -0.003 0.028  -0.032 213 SER BBB OG  
5247  N N   . TYR B 214 ? 0.353 0.413 0.287 0.001  0.021  -0.031 214 TYR BBB N   
5248  C CA  . TYR B 214 ? 0.336 0.393 0.269 -0.001 0.021  -0.028 214 TYR BBB CA  
5249  C C   . TYR B 214 ? 0.314 0.368 0.249 -0.005 0.024  -0.025 214 TYR BBB C   
5250  O O   . TYR B 214 ? 0.322 0.372 0.252 -0.005 0.026  -0.023 214 TYR BBB O   
5251  C CB  . TYR B 214 ? 0.337 0.398 0.278 -0.001 0.018  -0.030 214 TYR BBB CB  
5252  C CG  . TYR B 214 ? 0.329 0.393 0.281 -0.005 0.017  -0.030 214 TYR BBB CG  
5253  C CD1 . TYR B 214 ? 0.330 0.392 0.284 -0.008 0.018  -0.027 214 TYR BBB CD1 
5254  C CD2 . TYR B 214 ? 0.340 0.408 0.300 -0.006 0.017  -0.033 214 TYR BBB CD2 
5255  C CE1 . TYR B 214 ? 0.329 0.393 0.292 -0.010 0.018  -0.026 214 TYR BBB CE1 
5256  C CE2 . TYR B 214 ? 0.358 0.428 0.327 -0.008 0.017  -0.032 214 TYR BBB CE2 
5257  C CZ  . TYR B 214 ? 0.351 0.419 0.321 -0.011 0.017  -0.029 214 TYR BBB CZ  
5258  O OH  . TYR B 214 ? 0.352 0.421 0.329 -0.013 0.017  -0.028 214 TYR BBB OH  
5259  N N   . ILE B 215 ? 0.282 0.338 0.223 -0.007 0.025  -0.026 215 ILE BBB N   
5260  C CA  . ILE B 215 ? 0.271 0.326 0.215 -0.011 0.028  -0.025 215 ILE BBB CA  
5261  C C   . ILE B 215 ? 0.282 0.331 0.217 -0.011 0.032  -0.023 215 ILE BBB C   
5262  O O   . ILE B 215 ? 0.284 0.330 0.217 -0.012 0.034  -0.021 215 ILE BBB O   
5263  C CB  . ILE B 215 ? 0.268 0.328 0.221 -0.013 0.027  -0.026 215 ILE BBB CB  
5264  C CG1 . ILE B 215 ? 0.263 0.326 0.224 -0.014 0.024  -0.027 215 ILE BBB CG1 
5265  C CG2 . ILE B 215 ? 0.273 0.331 0.228 -0.016 0.030  -0.026 215 ILE BBB CG2 
5266  C CD1 . ILE B 215 ? 0.258 0.325 0.227 -0.014 0.024  -0.029 215 ILE BBB CD1 
5267  N N   . GLY B 216 ? 0.302 0.350 0.231 -0.008 0.033  -0.024 216 GLY BBB N   
5268  C CA  . GLY B 216 ? 0.310 0.353 0.230 -0.007 0.038  -0.023 216 GLY BBB CA  
5269  C C   . GLY B 216 ? 0.330 0.367 0.241 -0.005 0.039  -0.020 216 GLY BBB C   
5270  O O   . GLY B 216 ? 0.351 0.383 0.259 -0.007 0.043  -0.018 216 GLY BBB O   
5271  N N   . LEU B 217 ? 0.339 0.376 0.246 -0.002 0.035  -0.021 217 LEU BBB N   
5272  C CA  . LEU B 217 ? 0.352 0.384 0.250 0.001  0.036  -0.018 217 LEU BBB CA  
5273  C C   . LEU B 217 ? 0.361 0.392 0.263 -0.003 0.036  -0.016 217 LEU BBB C   
5274  O O   . LEU B 217 ? 0.373 0.397 0.269 -0.003 0.040  -0.013 217 LEU BBB O   
5275  C CB  . LEU B 217 ? 0.356 0.391 0.251 0.006  0.031  -0.020 217 LEU BBB CB  
5276  C CG  . LEU B 217 ? 0.368 0.404 0.257 0.010  0.031  -0.022 217 LEU BBB CG  
5277  C CD1 . LEU B 217 ? 0.373 0.411 0.257 0.016  0.026  -0.023 217 LEU BBB CD1 
5278  C CD2 . LEU B 217 ? 0.393 0.421 0.270 0.012  0.036  -0.019 217 LEU BBB CD2 
5279  N N   . GLU B 218 ? 0.362 0.398 0.274 -0.005 0.033  -0.017 218 GLU BBB N   
5280  C CA  . GLU B 218 ? 0.383 0.419 0.300 -0.009 0.033  -0.015 218 GLU BBB CA  
5281  C C   . GLU B 218 ? 0.380 0.412 0.297 -0.012 0.037  -0.014 218 GLU BBB C   
5282  O O   . GLU B 218 ? 0.382 0.411 0.297 -0.013 0.040  -0.012 218 GLU BBB O   
5283  C CB  . GLU B 218 ? 0.374 0.416 0.302 -0.011 0.029  -0.016 218 GLU BBB CB  
5284  C CG  . GLU B 218 ? 0.400 0.445 0.329 -0.008 0.025  -0.018 218 GLU BBB CG  
5285  C CD  . GLU B 218 ? 0.416 0.466 0.355 -0.010 0.023  -0.019 218 GLU BBB CD  
5286  O OE1 . GLU B 218 ? 0.449 0.501 0.395 -0.012 0.023  -0.019 218 GLU BBB OE1 
5287  O OE2 . GLU B 218 ? 0.446 0.497 0.387 -0.009 0.020  -0.019 218 GLU BBB OE2 
5288  N N   . THR B 219 ? 0.384 0.419 0.306 -0.013 0.039  -0.016 219 THR BBB N   
5289  C CA  . THR B 219 ? 0.393 0.426 0.317 -0.017 0.043  -0.016 219 THR BBB CA  
5290  C C   . THR B 219 ? 0.399 0.424 0.314 -0.016 0.049  -0.014 219 THR BBB C   
5291  O O   . THR B 219 ? 0.381 0.403 0.296 -0.019 0.052  -0.013 219 THR BBB O   
5292  C CB  . THR B 219 ? 0.388 0.425 0.318 -0.018 0.044  -0.018 219 THR BBB CB  
5293  O OG1 . THR B 219 ? 0.379 0.423 0.318 -0.018 0.039  -0.020 219 THR BBB OG1 
5294  C CG2 . THR B 219 ? 0.380 0.417 0.315 -0.022 0.048  -0.019 219 THR BBB CG2 
5295  N N   . ALA B 220 ? 0.410 0.432 0.316 -0.012 0.050  -0.014 220 ALA BBB N   
5296  C CA  . ALA B 220 ? 0.442 0.456 0.337 -0.011 0.055  -0.012 220 ALA BBB CA  
5297  C C   . ALA B 220 ? 0.433 0.442 0.323 -0.010 0.055  -0.009 220 ALA BBB C   
5298  O O   . ALA B 220 ? 0.436 0.438 0.322 -0.011 0.061  -0.008 220 ALA BBB O   
5299  C CB  . ALA B 220 ? 0.466 0.478 0.352 -0.006 0.055  -0.012 220 ALA BBB CB  
5300  N N   . GLY B 221 ? 0.414 0.427 0.305 -0.008 0.050  -0.009 221 GLY BBB N   
5301  C CA  . GLY B 221 ? 0.405 0.414 0.291 -0.006 0.049  -0.007 221 GLY BBB CA  
5302  C C   . GLY B 221 ? 0.395 0.404 0.287 -0.011 0.051  -0.006 221 GLY BBB C   
5303  O O   . GLY B 221 ? 0.383 0.384 0.269 -0.011 0.055  -0.004 221 GLY BBB O   
5304  N N   . PHE B 222 ? 0.382 0.396 0.285 -0.015 0.049  -0.008 222 PHE BBB N   
5305  C CA  . PHE B 222 ? 0.391 0.405 0.299 -0.019 0.051  -0.008 222 PHE BBB CA  
5306  C C   . PHE B 222 ? 0.385 0.395 0.293 -0.021 0.057  -0.009 222 PHE BBB C   
5307  O O   . PHE B 222 ? 0.374 0.380 0.282 -0.023 0.061  -0.008 222 PHE BBB O   
5308  C CB  . PHE B 222 ? 0.379 0.401 0.297 -0.021 0.046  -0.009 222 PHE BBB CB  
5309  C CG  . PHE B 222 ? 0.397 0.425 0.324 -0.022 0.045  -0.012 222 PHE BBB CG  
5310  C CD1 . PHE B 222 ? 0.410 0.438 0.341 -0.026 0.049  -0.013 222 PHE BBB CD1 
5311  C CD2 . PHE B 222 ? 0.395 0.428 0.326 -0.021 0.040  -0.013 222 PHE BBB CD2 
5312  C CE1 . PHE B 222 ? 0.407 0.440 0.346 -0.027 0.048  -0.016 222 PHE BBB CE1 
5313  C CE2 . PHE B 222 ? 0.390 0.428 0.329 -0.023 0.040  -0.015 222 PHE BBB CE2 
5314  C CZ  . PHE B 222 ? 0.397 0.435 0.339 -0.025 0.043  -0.016 222 PHE BBB CZ  
5315  N N   . LEU B 223 ? 0.397 0.408 0.306 -0.022 0.060  -0.010 223 LEU BBB N   
5316  C CA  . LEU B 223 ? 0.411 0.417 0.319 -0.024 0.067  -0.011 223 LEU BBB CA  
5317  C C   . LEU B 223 ? 0.430 0.426 0.327 -0.022 0.072  -0.008 223 LEU BBB C   
5318  O O   . LEU B 223 ? 0.437 0.429 0.336 -0.025 0.077  -0.008 223 LEU BBB O   
5319  C CB  . LEU B 223 ? 0.398 0.406 0.308 -0.025 0.068  -0.013 223 LEU BBB CB  
5320  C CG  . LEU B 223 ? 0.386 0.403 0.308 -0.027 0.064  -0.016 223 LEU BBB CG  
5321  C CD1 . LEU B 223 ? 0.375 0.394 0.299 -0.027 0.066  -0.018 223 LEU BBB CD1 
5322  C CD2 . LEU B 223 ? 0.396 0.417 0.328 -0.031 0.065  -0.018 223 LEU BBB CD2 
5323  N N   . ASN B 224 ? 0.459 0.451 0.346 -0.017 0.071  -0.006 224 ASN BBB N   
5324  C CA  . ASN B 224 ? 0.475 0.457 0.349 -0.014 0.076  -0.002 224 ASN BBB CA  
5325  C C   . ASN B 224 ? 0.469 0.449 0.345 -0.016 0.075  -0.001 224 ASN BBB C   
5326  O O   . ASN B 224 ? 0.478 0.451 0.351 -0.017 0.082  0.000  224 ASN BBB O   
5327  C CB  . ASN B 224 ? 0.486 0.466 0.350 -0.008 0.073  -0.001 224 ASN BBB CB  
5328  C CG  . ASN B 224 ? 0.493 0.462 0.343 -0.004 0.078  0.003  224 ASN BBB CG  
5329  O OD1 . ASN B 224 ? 0.542 0.504 0.386 -0.004 0.085  0.004  224 ASN BBB OD1 
5330  N ND2 . ASN B 224 ? 0.505 0.472 0.350 -0.001 0.075  0.005  224 ASN BBB ND2 
5331  N N   . GLU B 225 ? 0.455 0.441 0.335 -0.015 0.068  -0.001 225 GLU BBB N   
5332  C CA  . GLU B 225 ? 0.459 0.444 0.340 -0.016 0.067  -0.000 225 GLU BBB CA  
5333  C C   . GLU B 225 ? 0.451 0.436 0.340 -0.021 0.071  -0.002 225 GLU BBB C   
5334  O O   . GLU B 225 ? 0.492 0.473 0.379 -0.022 0.074  -0.001 225 GLU BBB O   
5335  C CB  . GLU B 225 ? 0.464 0.456 0.349 -0.015 0.060  -0.001 225 GLU BBB CB  
5336  C CG  . GLU B 225 ? 0.485 0.474 0.361 -0.010 0.057  0.001  225 GLU BBB CG  
5337  C CD  . GLU B 225 ? 0.519 0.515 0.400 -0.009 0.050  0.000  225 GLU BBB CD  
5338  O OE1 . GLU B 225 ? 0.560 0.564 0.447 -0.009 0.046  -0.002 225 GLU BBB OE1 
5339  O OE2 . GLU B 225 ? 0.552 0.547 0.431 -0.008 0.048  0.002  225 GLU BBB OE2 
5340  N N   . LEU B 226 ? 0.422 0.412 0.319 -0.025 0.072  -0.005 226 LEU BBB N   
5341  C CA  . LEU B 226 ? 0.397 0.390 0.305 -0.030 0.075  -0.007 226 LEU BBB CA  
5342  C C   . LEU B 226 ? 0.417 0.402 0.321 -0.032 0.084  -0.008 226 LEU BBB C   
5343  O O   . LEU B 226 ? 0.404 0.391 0.317 -0.036 0.087  -0.011 226 LEU BBB O   
5344  C CB  . LEU B 226 ? 0.383 0.385 0.301 -0.032 0.071  -0.011 226 LEU BBB CB  
5345  C CG  . LEU B 226 ? 0.354 0.364 0.278 -0.031 0.063  -0.011 226 LEU BBB CG  
5346  C CD1 . LEU B 226 ? 0.326 0.344 0.259 -0.033 0.060  -0.014 226 LEU BBB CD1 
5347  C CD2 . LEU B 226 ? 0.348 0.358 0.274 -0.033 0.063  -0.011 226 LEU BBB CD2 
5348  N N   . GLY B 227 ? 0.438 0.415 0.332 -0.028 0.088  -0.005 227 GLY BBB N   
5349  C CA  . GLY B 227 ? 0.455 0.422 0.343 -0.029 0.097  -0.004 227 GLY BBB CA  
5350  C C   . GLY B 227 ? 0.463 0.430 0.353 -0.030 0.101  -0.006 227 GLY BBB C   
5351  O O   . GLY B 227 ? 0.470 0.430 0.357 -0.032 0.109  -0.006 227 GLY BBB O   
5352  N N   . PHE B 228 ? 0.433 0.408 0.327 -0.030 0.095  -0.008 228 PHE BBB N   
5353  C CA  . PHE B 228 ? 0.448 0.424 0.343 -0.031 0.098  -0.010 228 PHE BBB CA  
5354  C C   . PHE B 228 ? 0.474 0.443 0.355 -0.026 0.101  -0.007 228 PHE BBB C   
5355  O O   . PHE B 228 ? 0.475 0.444 0.349 -0.021 0.096  -0.004 228 PHE BBB O   
5356  C CB  . PHE B 228 ? 0.428 0.416 0.335 -0.032 0.092  -0.013 228 PHE BBB CB  
5357  C CG  . PHE B 228 ? 0.417 0.411 0.336 -0.037 0.091  -0.017 228 PHE BBB CG  
5358  C CD1 . PHE B 228 ? 0.424 0.417 0.350 -0.041 0.097  -0.020 228 PHE BBB CD1 
5359  C CD2 . PHE B 228 ? 0.404 0.406 0.329 -0.037 0.083  -0.017 228 PHE BBB CD2 
5360  C CE1 . PHE B 228 ? 0.423 0.422 0.360 -0.045 0.096  -0.023 228 PHE BBB CE1 
5361  C CE2 . PHE B 228 ? 0.401 0.408 0.336 -0.040 0.082  -0.020 228 PHE BBB CE2 
5362  C CZ  . PHE B 228 ? 0.411 0.417 0.352 -0.044 0.088  -0.023 228 PHE BBB CZ  
5363  N N   . ASP B 229 ? 0.497 0.461 0.376 -0.026 0.108  -0.007 229 ASP BBB N   
5364  C CA  . ASP B 229 ? 0.499 0.456 0.365 -0.022 0.111  -0.005 229 ASP BBB CA  
5365  C C   . ASP B 229 ? 0.466 0.433 0.335 -0.020 0.103  -0.006 229 ASP BBB C   
5366  O O   . ASP B 229 ? 0.454 0.427 0.333 -0.023 0.103  -0.010 229 ASP BBB O   
5367  C CB  . ASP B 229 ? 0.525 0.474 0.388 -0.024 0.121  -0.005 229 ASP BBB CB  
5368  C CG  . ASP B 229 ? 0.552 0.493 0.401 -0.019 0.125  -0.003 229 ASP BBB CG  
5369  O OD1 . ASP B 229 ? 0.589 0.534 0.433 -0.014 0.119  -0.002 229 ASP BBB OD1 
5370  O OD2 . ASP B 229 ? 0.579 0.511 0.424 -0.020 0.135  -0.002 229 ASP BBB OD2 
5371  N N   . THR B 230 ? 0.450 0.417 0.310 -0.014 0.098  -0.004 230 THR BBB N   
5372  C CA  . THR B 230 ? 0.445 0.422 0.310 -0.013 0.090  -0.006 230 THR BBB CA  
5373  C C   . THR B 230 ? 0.457 0.431 0.310 -0.007 0.089  -0.005 230 THR BBB C   
5374  O O   . THR B 230 ? 0.453 0.420 0.294 -0.002 0.090  -0.002 230 THR BBB O   
5375  C CB  . THR B 230 ? 0.445 0.427 0.315 -0.012 0.082  -0.006 230 THR BBB CB  
5376  O OG1 . THR B 230 ? 0.468 0.454 0.349 -0.018 0.083  -0.008 230 THR BBB OG1 
5377  C CG2 . THR B 230 ? 0.435 0.427 0.309 -0.010 0.074  -0.008 230 THR BBB CG2 
5378  N N   . THR B 231 ? 0.447 0.428 0.305 -0.007 0.087  -0.008 231 THR BBB N   
5379  C CA  . THR B 231 ? 0.463 0.442 0.310 -0.001 0.086  -0.008 231 THR BBB CA  
5380  C C   . THR B 231 ? 0.435 0.426 0.292 -0.001 0.078  -0.011 231 THR BBB C   
5381  O O   . THR B 231 ? 0.426 0.424 0.296 -0.006 0.076  -0.013 231 THR BBB O   
5382  C CB  . THR B 231 ? 0.484 0.458 0.327 -0.002 0.094  -0.008 231 THR BBB CB  
5383  O OG1 . THR B 231 ? 0.504 0.467 0.340 -0.003 0.101  -0.005 231 THR BBB OG1 
5384  C CG2 . THR B 231 ? 0.486 0.459 0.318 0.005  0.093  -0.007 231 THR BBB CG2 
5385  N N   . VAL B 232 ? 0.440 0.433 0.290 0.005  0.073  -0.011 232 VAL BBB N   
5386  C CA  . VAL B 232 ? 0.416 0.420 0.275 0.006  0.065  -0.014 232 VAL BBB CA  
5387  C C   . VAL B 232 ? 0.432 0.435 0.282 0.010  0.066  -0.016 232 VAL BBB C   
5388  O O   . VAL B 232 ? 0.425 0.423 0.262 0.016  0.067  -0.014 232 VAL BBB O   
5389  C CB  . VAL B 232 ? 0.398 0.406 0.257 0.008  0.059  -0.014 232 VAL BBB CB  
5390  C CG1 . VAL B 232 ? 0.378 0.395 0.243 0.010  0.052  -0.018 232 VAL BBB CG1 
5391  C CG2 . VAL B 232 ? 0.391 0.400 0.259 0.003  0.058  -0.014 232 VAL BBB CG2 
5392  N N   . ALA B 233 ? 0.441 0.451 0.300 0.007  0.065  -0.019 233 ALA BBB N   
5393  C CA  . ALA B 233 ? 0.462 0.474 0.317 0.011  0.065  -0.021 233 ALA BBB CA  
5394  C C   . ALA B 233 ? 0.476 0.498 0.337 0.013  0.057  -0.025 233 ALA BBB C   
5395  O O   . ALA B 233 ? 0.497 0.526 0.371 0.009  0.053  -0.027 233 ALA BBB O   
5396  C CB  . ALA B 233 ? 0.459 0.473 0.321 0.007  0.068  -0.023 233 ALA BBB CB  
5397  N N   . MET B 234 ? 0.496 0.518 0.348 0.020  0.054  -0.025 234 MET BBB N   
5398  C CA  . MET B 234 ? 0.497 0.526 0.352 0.023  0.046  -0.028 234 MET BBB CA  
5399  C C   . MET B 234 ? 0.528 0.561 0.379 0.027  0.046  -0.032 234 MET BBB C   
5400  O O   . MET B 234 ? 0.529 0.556 0.366 0.033  0.048  -0.030 234 MET BBB O   
5401  C CB  . MET B 234 ? 0.500 0.526 0.347 0.028  0.044  -0.026 234 MET BBB CB  
5402  C CG  . MET B 234 ? 0.507 0.541 0.356 0.032  0.037  -0.030 234 MET BBB CG  
5403  S SD  . MET B 234 ? 0.559 0.591 0.402 0.035  0.034  -0.029 234 MET BBB SD  
5404  C CE  . MET B 234 ? 0.578 0.598 0.401 0.041  0.039  -0.024 234 MET BBB CE  
5405  N N   . ARG B 235 ? 0.530 0.571 0.393 0.025  0.043  -0.036 235 ARG BBB N   
5406  C CA  . ARG B 235 ? 0.552 0.598 0.413 0.028  0.042  -0.040 235 ARG BBB CA  
5407  C C   . ARG B 235 ? 0.581 0.628 0.433 0.036  0.037  -0.042 235 ARG BBB C   
5408  O O   . ARG B 235 ? 0.554 0.600 0.395 0.042  0.039  -0.043 235 ARG BBB O   
5409  C CB  . ARG B 235 ? 0.560 0.615 0.437 0.024  0.039  -0.044 235 ARG BBB CB  
5410  C CG  . ARG B 235 ? 0.604 0.663 0.481 0.027  0.038  -0.048 235 ARG BBB CG  
5411  C CD  . ARG B 235 ? 0.627 0.694 0.520 0.022  0.036  -0.052 235 ARG BBB CD  
5412  N NE  . ARG B 235 ? 0.699 0.769 0.591 0.024  0.037  -0.055 235 ARG BBB NE  
5413  C CZ  . ARG B 235 ? 0.731 0.806 0.619 0.029  0.034  -0.059 235 ARG BBB CZ  
5414  N NH1 . ARG B 235 ? 0.709 0.787 0.595 0.033  0.030  -0.061 235 ARG BBB NH1 
5415  N NH2 . ARG B 235 ? 0.762 0.839 0.650 0.030  0.036  -0.062 235 ARG BBB NH2 
5416  N N   . SER B 236 ? 0.544 0.595 0.400 0.037  0.032  -0.043 236 SER BBB N   
5417  C CA  . SER B 236 ? 0.545 0.600 0.395 0.044  0.027  -0.046 236 SER BBB CA  
5418  C C   . SER B 236 ? 0.527 0.580 0.375 0.046  0.025  -0.044 236 SER BBB C   
5419  O O   . SER B 236 ? 0.535 0.580 0.368 0.050  0.028  -0.040 236 SER BBB O   
5420  C CB  . SER B 236 ? 0.539 0.606 0.400 0.045  0.022  -0.053 236 SER BBB CB  
5421  O OG  . SER B 236 ? 0.548 0.619 0.425 0.038  0.021  -0.054 236 SER BBB OG  
5422  N N   . ILE B 237 ? 0.502 0.560 0.362 0.042  0.021  -0.046 237 ILE BBB N   
5423  C CA  . ILE B 237 ? 0.512 0.570 0.371 0.044  0.018  -0.045 237 ILE BBB CA  
5424  C C   . ILE B 237 ? 0.514 0.572 0.384 0.037  0.019  -0.042 237 ILE BBB C   
5425  O O   . ILE B 237 ? 0.527 0.586 0.407 0.031  0.020  -0.043 237 ILE BBB O   
5426  C CB  . ILE B 237 ? 0.497 0.565 0.361 0.048  0.012  -0.052 237 ILE BBB CB  
5427  C CG1 . ILE B 237 ? 0.493 0.570 0.375 0.044  0.010  -0.056 237 ILE BBB CG1 
5428  C CG2 . ILE B 237 ? 0.489 0.558 0.341 0.057  0.011  -0.055 237 ILE BBB CG2 
5429  C CD1 . ILE B 237 ? 0.471 0.557 0.360 0.047  0.004  -0.063 237 ILE BBB CD1 
5430  N N   . PRO B 238 ? 0.530 0.583 0.396 0.037  0.019  -0.039 238 PRO BBB N   
5431  C CA  . PRO B 238 ? 0.504 0.556 0.379 0.031  0.020  -0.037 238 PRO BBB CA  
5432  C C   . PRO B 238 ? 0.493 0.553 0.382 0.029  0.015  -0.041 238 PRO BBB C   
5433  O O   . PRO B 238 ? 0.488 0.553 0.377 0.033  0.011  -0.044 238 PRO BBB O   
5434  C CB  . PRO B 238 ? 0.515 0.560 0.381 0.033  0.021  -0.033 238 PRO BBB CB  
5435  C CG  . PRO B 238 ? 0.534 0.580 0.389 0.041  0.018  -0.035 238 PRO BBB CG  
5436  C CD  . PRO B 238 ? 0.550 0.598 0.402 0.044  0.019  -0.038 238 PRO BBB CD  
5437  N N   . LEU B 239 ? 0.482 0.544 0.383 0.022  0.016  -0.040 239 LEU BBB N   
5438  C CA  . LEU B 239 ? 0.487 0.555 0.400 0.020  0.012  -0.043 239 LEU BBB CA  
5439  C C   . LEU B 239 ? 0.487 0.563 0.405 0.023  0.009  -0.049 239 LEU BBB C   
5440  O O   . LEU B 239 ? 0.480 0.559 0.401 0.026  0.005  -0.052 239 LEU BBB O   
5441  C CB  . LEU B 239 ? 0.485 0.551 0.396 0.021  0.011  -0.041 239 LEU BBB CB  
5442  C CG  . LEU B 239 ? 0.481 0.539 0.388 0.018  0.014  -0.035 239 LEU BBB CG  
5443  C CD1 . LEU B 239 ? 0.488 0.544 0.392 0.019  0.012  -0.034 239 LEU BBB CD1 
5444  C CD2 . LEU B 239 ? 0.470 0.529 0.386 0.012  0.016  -0.033 239 LEU BBB CD2 
5445  N N   . ARG B 240 ? 0.499 0.577 0.419 0.023  0.009  -0.051 240 ARG BBB N   
5446  C CA  . ARG B 240 ? 0.523 0.610 0.450 0.026  0.006  -0.058 240 ARG BBB CA  
5447  C C   . ARG B 240 ? 0.473 0.565 0.413 0.023  0.004  -0.061 240 ARG BBB C   
5448  O O   . ARG B 240 ? 0.427 0.518 0.376 0.018  0.005  -0.059 240 ARG BBB O   
5449  C CB  . ARG B 240 ? 0.576 0.664 0.504 0.025  0.008  -0.059 240 ARG BBB CB  
5450  C CG  . ARG B 240 ? 0.647 0.743 0.580 0.028  0.005  -0.066 240 ARG BBB CG  
5451  C CD  . ARG B 240 ? 0.718 0.816 0.658 0.024  0.008  -0.067 240 ARG BBB CD  
5452  N NE  . ARG B 240 ? 0.779 0.872 0.724 0.018  0.010  -0.062 240 ARG BBB NE  
5453  C CZ  . ARG B 240 ? 0.742 0.837 0.699 0.014  0.010  -0.063 240 ARG BBB CZ  
5454  N NH1 . ARG B 240 ? 0.717 0.818 0.682 0.015  0.007  -0.067 240 ARG BBB NH1 
5455  N NH2 . ARG B 240 ? 0.775 0.867 0.736 0.010  0.012  -0.058 240 ARG BBB NH2 
5456  N N   . GLY B 241 ? 0.471 0.569 0.415 0.027  0.000  -0.067 241 GLY BBB N   
5457  C CA  . GLY B 241 ? 0.460 0.564 0.417 0.025  -0.002 -0.071 241 GLY BBB CA  
5458  C C   . GLY B 241 ? 0.470 0.572 0.424 0.026  -0.003 -0.069 241 GLY BBB C   
5459  O O   . GLY B 241 ? 0.471 0.577 0.432 0.026  -0.006 -0.074 241 GLY BBB O   
5460  N N   . PHE B 242 ? 0.452 0.546 0.395 0.026  -0.002 -0.063 242 PHE BBB N   
5461  C CA  . PHE B 242 ? 0.455 0.546 0.394 0.027  -0.003 -0.061 242 PHE BBB CA  
5462  C C   . PHE B 242 ? 0.458 0.551 0.388 0.034  -0.006 -0.064 242 PHE BBB C   
5463  O O   . PHE B 242 ? 0.531 0.624 0.452 0.038  -0.006 -0.065 242 PHE BBB O   
5464  C CB  . PHE B 242 ? 0.492 0.575 0.425 0.024  0.001  -0.053 242 PHE BBB CB  
5465  C CG  . PHE B 242 ? 0.531 0.612 0.472 0.017  0.003  -0.050 242 PHE BBB CG  
5466  C CD1 . PHE B 242 ? 0.552 0.635 0.500 0.014  0.004  -0.051 242 PHE BBB CD1 
5467  C CD2 . PHE B 242 ? 0.549 0.626 0.491 0.014  0.004  -0.046 242 PHE BBB CD2 
5468  C CE1 . PHE B 242 ? 0.565 0.646 0.521 0.009  0.006  -0.048 242 PHE BBB CE1 
5469  C CE2 . PHE B 242 ? 0.545 0.621 0.494 0.009  0.006  -0.043 242 PHE BBB CE2 
5470  C CZ  . PHE B 242 ? 0.545 0.623 0.501 0.007  0.007  -0.044 242 PHE BBB CZ  
5471  N N   . ASP B 243 ? 0.417 0.511 0.347 0.035  -0.008 -0.065 243 ASP BBB N   
5472  C CA  . ASP B 243 ? 0.400 0.495 0.320 0.042  -0.011 -0.067 243 ASP BBB CA  
5473  C C   . ASP B 243 ? 0.404 0.491 0.307 0.046  -0.009 -0.063 243 ASP BBB C   
5474  O O   . ASP B 243 ? 0.408 0.488 0.306 0.043  -0.006 -0.056 243 ASP BBB O   
5475  C CB  . ASP B 243 ? 0.400 0.493 0.321 0.042  -0.012 -0.066 243 ASP BBB CB  
5476  C CG  . ASP B 243 ? 0.407 0.502 0.319 0.050  -0.016 -0.069 243 ASP BBB CG  
5477  O OD1 . ASP B 243 ? 0.389 0.493 0.307 0.053  -0.020 -0.077 243 ASP BBB OD1 
5478  O OD2 . ASP B 243 ? 0.410 0.499 0.310 0.052  -0.015 -0.064 243 ASP BBB OD2 
5479  N N   . ARG B 244 ? 0.401 0.492 0.297 0.053  -0.011 -0.066 244 ARG BBB N   
5480  C CA  . ARG B 244 ? 0.420 0.504 0.299 0.058  -0.009 -0.062 244 ARG BBB CA  
5481  C C   . ARG B 244 ? 0.416 0.492 0.284 0.060  -0.008 -0.057 244 ARG BBB C   
5482  O O   . ARG B 244 ? 0.408 0.474 0.268 0.058  -0.003 -0.050 244 ARG BBB O   
5483  C CB  . ARG B 244 ? 0.444 0.532 0.316 0.066  -0.012 -0.068 244 ARG BBB CB  
5484  C CG  . ARG B 244 ? 0.437 0.533 0.319 0.064  -0.012 -0.073 244 ARG BBB CG  
5485  C CD  . ARG B 244 ? 0.458 0.548 0.337 0.060  -0.007 -0.067 244 ARG BBB CD  
5486  N NE  . ARG B 244 ? 0.441 0.529 0.332 0.051  -0.005 -0.064 244 ARG BBB NE  
5487  C CZ  . ARG B 244 ? 0.437 0.517 0.325 0.046  -0.000 -0.058 244 ARG BBB CZ  
5488  N NH1 . ARG B 244 ? 0.440 0.513 0.315 0.049  0.003  -0.053 244 ARG BBB NH1 
5489  N NH2 . ARG B 244 ? 0.452 0.533 0.352 0.039  0.001  -0.056 244 ARG BBB NH2 
5490  N N   . GLN B 245 ? 0.391 0.470 0.258 0.064  -0.012 -0.060 245 GLN BBB N   
5491  C CA  . GLN B 245 ? 0.411 0.483 0.268 0.067  -0.012 -0.055 245 GLN BBB CA  
5492  C C   . GLN B 245 ? 0.411 0.475 0.270 0.060  -0.007 -0.048 245 GLN BBB C   
5493  O O   . GLN B 245 ? 0.416 0.470 0.262 0.061  -0.003 -0.042 245 GLN BBB O   
5494  C CB  . GLN B 245 ? 0.417 0.495 0.277 0.071  -0.017 -0.060 245 GLN BBB CB  
5495  C CG  . GLN B 245 ? 0.434 0.505 0.281 0.076  -0.017 -0.057 245 GLN BBB CG  
5496  C CD  . GLN B 245 ? 0.441 0.518 0.292 0.079  -0.022 -0.062 245 GLN BBB CD  
5497  O OE1 . GLN B 245 ? 0.425 0.511 0.291 0.077  -0.025 -0.068 245 GLN BBB OE1 
5498  N NE2 . GLN B 245 ? 0.452 0.525 0.291 0.086  -0.023 -0.060 245 GLN BBB NE2 
5499  N N   . CYS B 246 ? 0.398 0.466 0.271 0.053  -0.007 -0.049 246 CYS BBB N   
5500  C CA  . CYS B 246 ? 0.415 0.476 0.291 0.046  -0.003 -0.043 246 CYS BBB CA  
5501  C C   . CYS B 246 ? 0.416 0.472 0.289 0.043  0.002  -0.039 246 CYS BBB C   
5502  O O   . CYS B 246 ? 0.421 0.469 0.287 0.041  0.005  -0.033 246 CYS BBB O   
5503  C CB  . CYS B 246 ? 0.418 0.485 0.310 0.040  -0.004 -0.046 246 CYS BBB CB  
5504  S SG  . CYS B 246 ? 0.436 0.509 0.334 0.042  -0.009 -0.050 246 CYS BBB SG  
5505  N N   . SER B 247 ? 0.419 0.479 0.296 0.042  0.002  -0.042 247 SER BBB N   
5506  C CA  . SER B 247 ? 0.432 0.488 0.308 0.039  0.006  -0.038 247 SER BBB CA  
5507  C C   . SER B 247 ? 0.465 0.512 0.324 0.043  0.010  -0.034 247 SER BBB C   
5508  O O   . SER B 247 ? 0.477 0.517 0.333 0.039  0.015  -0.029 247 SER BBB O   
5509  C CB  . SER B 247 ? 0.420 0.482 0.302 0.038  0.005  -0.043 247 SER BBB CB  
5510  O OG  . SER B 247 ? 0.395 0.464 0.292 0.034  0.003  -0.046 247 SER BBB OG  
5511  N N   . GLU B 248 ? 0.501 0.548 0.350 0.050  0.007  -0.036 248 GLU BBB N   
5512  C CA  . GLU B 248 ? 0.514 0.552 0.345 0.056  0.011  -0.032 248 GLU BBB CA  
5513  C C   . GLU B 248 ? 0.495 0.525 0.320 0.056  0.013  -0.027 248 GLU BBB C   
5514  O O   . GLU B 248 ? 0.467 0.487 0.282 0.056  0.019  -0.022 248 GLU BBB O   
5515  C CB  . GLU B 248 ? 0.546 0.588 0.368 0.065  0.007  -0.036 248 GLU BBB CB  
5516  C CG  . GLU B 248 ? 0.561 0.608 0.387 0.065  0.007  -0.040 248 GLU BBB CG  
5517  C CD  . GLU B 248 ? 0.582 0.636 0.404 0.073  0.002  -0.046 248 GLU BBB CD  
5518  O OE1 . GLU B 248 ? 0.590 0.644 0.403 0.080  -0.001 -0.047 248 GLU BBB OE1 
5519  O OE2 . GLU B 248 ? 0.646 0.708 0.475 0.073  -0.000 -0.051 248 GLU BBB OE2 
5520  N N   . LYS B 249 ? 0.482 0.515 0.312 0.055  0.009  -0.028 249 LYS BBB N   
5521  C CA  . LYS B 249 ? 0.489 0.515 0.315 0.054  0.012  -0.023 249 LYS BBB CA  
5522  C C   . LYS B 249 ? 0.481 0.502 0.312 0.046  0.017  -0.019 249 LYS BBB C   
5523  O O   . LYS B 249 ? 0.507 0.519 0.330 0.046  0.022  -0.014 249 LYS BBB O   
5524  C CB  . LYS B 249 ? 0.488 0.519 0.321 0.054  0.007  -0.026 249 LYS BBB CB  
5525  C CG  . LYS B 249 ? 0.493 0.516 0.322 0.053  0.009  -0.021 249 LYS BBB CG  
5526  C CD  . LYS B 249 ? 0.498 0.526 0.332 0.053  0.005  -0.023 249 LYS BBB CD  
5527  C CE  . LYS B 249 ? 0.523 0.543 0.351 0.053  0.008  -0.018 249 LYS BBB CE  
5528  N NZ  . LYS B 249 ? 0.560 0.571 0.372 0.058  0.011  -0.015 249 LYS BBB NZ  
5529  N N   . ILE B 250 ? 0.451 0.477 0.295 0.040  0.016  -0.021 250 ILE BBB N   
5530  C CA  . ILE B 250 ? 0.457 0.480 0.307 0.033  0.021  -0.017 250 ILE BBB CA  
5531  C C   . ILE B 250 ? 0.476 0.491 0.315 0.034  0.027  -0.014 250 ILE BBB C   
5532  O O   . ILE B 250 ? 0.470 0.478 0.306 0.031  0.032  -0.010 250 ILE BBB O   
5533  C CB  . ILE B 250 ? 0.449 0.479 0.313 0.027  0.019  -0.020 250 ILE BBB CB  
5534  C CG1 . ILE B 250 ? 0.444 0.480 0.318 0.026  0.015  -0.022 250 ILE BBB CG1 
5535  C CG2 . ILE B 250 ? 0.436 0.463 0.305 0.021  0.024  -0.017 250 ILE BBB CG2 
5536  C CD1 . ILE B 250 ? 0.439 0.483 0.325 0.023  0.012  -0.026 250 ILE BBB CD1 
5537  N N   . VAL B 251 ? 0.477 0.494 0.312 0.037  0.027  -0.017 251 VAL BBB N   
5538  C CA  . VAL B 251 ? 0.486 0.496 0.313 0.038  0.033  -0.014 251 VAL BBB CA  
5539  C C   . VAL B 251 ? 0.497 0.497 0.308 0.043  0.036  -0.010 251 VAL BBB C   
5540  O O   . VAL B 251 ? 0.536 0.527 0.343 0.040  0.042  -0.006 251 VAL BBB O   
5541  C CB  . VAL B 251 ? 0.483 0.498 0.309 0.041  0.031  -0.018 251 VAL BBB CB  
5542  C CG1 . VAL B 251 ? 0.493 0.499 0.305 0.044  0.037  -0.015 251 VAL BBB CG1 
5543  C CG2 . VAL B 251 ? 0.456 0.479 0.296 0.036  0.029  -0.021 251 VAL BBB CG2 
5544  N N   . GLU B 252 ? 0.499 0.499 0.303 0.049  0.032  -0.011 252 GLU BBB N   
5545  C CA  . GLU B 252 ? 0.509 0.499 0.298 0.055  0.035  -0.007 252 GLU BBB CA  
5546  C C   . GLU B 252 ? 0.474 0.458 0.266 0.049  0.039  -0.003 252 GLU BBB C   
5547  O O   . GLU B 252 ? 0.466 0.440 0.249 0.049  0.045  0.001  252 GLU BBB O   
5548  C CB  . GLU B 252 ? 0.568 0.562 0.352 0.062  0.029  -0.010 252 GLU BBB CB  
5549  C CG  . GLU B 252 ? 0.645 0.630 0.414 0.068  0.031  -0.006 252 GLU BBB CG  
5550  C CD  . GLU B 252 ? 0.677 0.667 0.443 0.075  0.024  -0.009 252 GLU BBB CD  
5551  O OE1 . GLU B 252 ? 0.734 0.731 0.498 0.081  0.020  -0.013 252 GLU BBB OE1 
5552  O OE2 . GLU B 252 ? 0.698 0.687 0.468 0.074  0.023  -0.008 252 GLU BBB OE2 
5553  N N   . TYR B 253 ? 0.458 0.449 0.264 0.043  0.036  -0.004 253 TYR BBB N   
5554  C CA  . TYR B 253 ? 0.445 0.431 0.254 0.038  0.039  -0.001 253 TYR BBB CA  
5555  C C   . TYR B 253 ? 0.445 0.427 0.258 0.032  0.045  0.001  253 TYR BBB C   
5556  O O   . TYR B 253 ? 0.458 0.431 0.266 0.031  0.051  0.005  253 TYR BBB O   
5557  C CB  . TYR B 253 ? 0.431 0.424 0.253 0.035  0.034  -0.003 253 TYR BBB CB  
5558  C CG  . TYR B 253 ? 0.412 0.402 0.238 0.030  0.036  -0.000 253 TYR BBB CG  
5559  C CD1 . TYR B 253 ? 0.410 0.400 0.245 0.023  0.039  0.000  253 TYR BBB CD1 
5560  C CD2 . TYR B 253 ? 0.417 0.402 0.236 0.033  0.036  0.002  253 TYR BBB CD2 
5561  C CE1 . TYR B 253 ? 0.419 0.406 0.257 0.019  0.041  0.003  253 TYR BBB CE1 
5562  C CE2 . TYR B 253 ? 0.421 0.401 0.241 0.029  0.039  0.004  253 TYR BBB CE2 
5563  C CZ  . TYR B 253 ? 0.422 0.403 0.252 0.022  0.041  0.005  253 TYR BBB CZ  
5564  O OH  . TYR B 253 ? 0.463 0.441 0.295 0.018  0.044  0.007  253 TYR BBB OH  
5565  N N   . MET B 254 ? 0.433 0.421 0.255 0.029  0.044  -0.002 254 MET BBB N   
5566  C CA  . MET B 254 ? 0.453 0.439 0.280 0.023  0.050  -0.001 254 MET BBB CA  
5567  C C   . MET B 254 ? 0.491 0.466 0.305 0.026  0.057  0.002  254 MET BBB C   
5568  O O   . MET B 254 ? 0.485 0.454 0.300 0.021  0.063  0.004  254 MET BBB O   
5569  C CB  . MET B 254 ? 0.445 0.440 0.282 0.020  0.047  -0.004 254 MET BBB CB  
5570  C CG  . MET B 254 ? 0.441 0.444 0.290 0.017  0.041  -0.007 254 MET BBB CG  
5571  S SD  . MET B 254 ? 0.437 0.449 0.299 0.013  0.040  -0.010 254 MET BBB SD  
5572  C CE  . MET B 254 ? 0.443 0.450 0.307 0.007  0.047  -0.008 254 MET BBB CE  
5573  N N   . LYS B 255 ? 0.519 0.492 0.321 0.033  0.057  0.002  255 LYS BBB N   
5574  C CA  . LYS B 255 ? 0.551 0.514 0.339 0.037  0.063  0.005  255 LYS BBB CA  
5575  C C   . LYS B 255 ? 0.528 0.480 0.307 0.038  0.068  0.010  255 LYS BBB C   
5576  O O   . LYS B 255 ? 0.521 0.464 0.296 0.036  0.076  0.012  255 LYS BBB O   
5577  C CB  . LYS B 255 ? 0.605 0.568 0.381 0.045  0.060  0.004  255 LYS BBB CB  
5578  C CG  . LYS B 255 ? 0.677 0.644 0.454 0.045  0.061  0.002  255 LYS BBB CG  
5579  C CD  . LYS B 255 ? 0.747 0.717 0.514 0.054  0.057  -0.001 255 LYS BBB CD  
5580  C CE  . LYS B 255 ? 0.795 0.769 0.562 0.055  0.057  -0.003 255 LYS BBB CE  
5581  N NZ  . LYS B 255 ? 0.799 0.782 0.565 0.061  0.050  -0.008 255 LYS BBB NZ  
5582  N N   . ALA B 256 ? 0.510 0.463 0.287 0.041  0.063  0.010  256 ALA BBB N   
5583  C CA  . ALA B 256 ? 0.522 0.466 0.292 0.042  0.067  0.014  256 ALA BBB CA  
5584  C C   . ALA B 256 ? 0.518 0.459 0.297 0.034  0.071  0.015  256 ALA BBB C   
5585  O O   . ALA B 256 ? 0.555 0.487 0.327 0.035  0.076  0.018  256 ALA BBB O   
5586  C CB  . ALA B 256 ? 0.516 0.463 0.283 0.047  0.060  0.013  256 ALA BBB CB  
5587  N N   . THR B 257 ? 0.514 0.464 0.308 0.027  0.069  0.012  257 THR BBB N   
5588  C CA  . THR B 257 ? 0.514 0.463 0.318 0.020  0.072  0.012  257 THR BBB CA  
5589  C C   . THR B 257 ? 0.508 0.456 0.317 0.015  0.079  0.012  257 THR BBB C   
5590  O O   . THR B 257 ? 0.508 0.457 0.327 0.008  0.081  0.011  257 THR BBB O   
5591  C CB  . THR B 257 ? 0.511 0.470 0.329 0.016  0.066  0.010  257 THR BBB CB  
5592  O OG1 . THR B 257 ? 0.508 0.478 0.335 0.015  0.061  0.006  257 THR BBB OG1 
5593  C CG2 . THR B 257 ? 0.504 0.464 0.319 0.019  0.061  0.011  257 THR BBB CG2 
5594  N N   . GLY B 258 ? 0.506 0.452 0.309 0.018  0.081  0.012  258 GLY BBB N   
5595  C CA  . GLY B 258 ? 0.526 0.467 0.330 0.014  0.088  0.012  258 GLY BBB CA  
5596  C C   . GLY B 258 ? 0.512 0.461 0.324 0.011  0.086  0.008  258 GLY BBB C   
5597  O O   . GLY B 258 ? 0.520 0.466 0.334 0.008  0.093  0.008  258 GLY BBB O   
5598  N N   . THR B 259 ? 0.504 0.464 0.322 0.013  0.078  0.005  259 THR BBB N   
5599  C CA  . THR B 259 ? 0.507 0.475 0.332 0.011  0.076  0.002  259 THR BBB CA  
5600  C C   . THR B 259 ? 0.532 0.495 0.344 0.017  0.079  0.003  259 THR BBB C   
5601  O O   . THR B 259 ? 0.521 0.482 0.322 0.024  0.076  0.004  259 THR BBB O   
5602  C CB  . THR B 259 ? 0.502 0.481 0.338 0.010  0.068  -0.001 259 THR BBB CB  
5603  O OG1 . THR B 259 ? 0.514 0.496 0.360 0.005  0.067  -0.001 259 THR BBB OG1 
5604  C CG2 . THR B 259 ? 0.498 0.484 0.342 0.007  0.066  -0.004 259 THR BBB CG2 
5605  N N   . LYS B 260 ? 0.548 0.510 0.361 0.015  0.083  0.002  260 LYS BBB N   
5606  C CA  . LYS B 260 ? 0.577 0.535 0.379 0.020  0.086  0.002  260 LYS BBB CA  
5607  C C   . LYS B 260 ? 0.557 0.526 0.366 0.020  0.080  -0.002 260 LYS BBB C   
5608  O O   . LYS B 260 ? 0.548 0.524 0.370 0.015  0.077  -0.004 260 LYS BBB O   
5609  C CB  . LYS B 260 ? 0.619 0.568 0.418 0.017  0.096  0.004  260 LYS BBB CB  
5610  C CG  . LYS B 260 ? 0.668 0.604 0.457 0.018  0.104  0.008  260 LYS BBB CG  
5611  C CD  . LYS B 260 ? 0.701 0.630 0.492 0.013  0.114  0.009  260 LYS BBB CD  
5612  C CE  . LYS B 260 ? 0.701 0.636 0.509 0.004  0.114  0.006  260 LYS BBB CE  
5613  N NZ  . LYS B 260 ? 0.715 0.645 0.526 -0.001 0.123  0.005  260 LYS BBB NZ  
5614  N N   . PHE B 261 ? 0.566 0.535 0.365 0.027  0.077  -0.002 261 PHE BBB N   
5615  C CA  . PHE B 261 ? 0.561 0.541 0.365 0.029  0.070  -0.007 261 PHE BBB CA  
5616  C C   . PHE B 261 ? 0.578 0.554 0.372 0.033  0.074  -0.007 261 PHE BBB C   
5617  O O   . PHE B 261 ? 0.590 0.560 0.369 0.040  0.076  -0.004 261 PHE BBB O   
5618  C CB  . PHE B 261 ? 0.553 0.538 0.355 0.034  0.062  -0.008 261 PHE BBB CB  
5619  C CG  . PHE B 261 ? 0.520 0.511 0.335 0.030  0.058  -0.009 261 PHE BBB CG  
5620  C CD1 . PHE B 261 ? 0.518 0.503 0.330 0.029  0.059  -0.006 261 PHE BBB CD1 
5621  C CD2 . PHE B 261 ? 0.508 0.510 0.337 0.027  0.052  -0.013 261 PHE BBB CD2 
5622  C CE1 . PHE B 261 ? 0.504 0.495 0.326 0.025  0.055  -0.006 261 PHE BBB CE1 
5623  C CE2 . PHE B 261 ? 0.493 0.500 0.332 0.023  0.048  -0.013 261 PHE BBB CE2 
5624  C CZ  . PHE B 261 ? 0.496 0.498 0.332 0.023  0.049  -0.010 261 PHE BBB CZ  
5625  N N   . LEU B 262 ? 0.609 0.591 0.411 0.029  0.074  -0.010 262 LEU BBB N   
5626  C CA  . LEU B 262 ? 0.624 0.606 0.420 0.033  0.076  -0.011 262 LEU BBB CA  
5627  C C   . LEU B 262 ? 0.626 0.620 0.428 0.036  0.067  -0.016 262 LEU BBB C   
5628  O O   . LEU B 262 ? 0.641 0.644 0.457 0.031  0.064  -0.019 262 LEU BBB O   
5629  C CB  . LEU B 262 ? 0.640 0.622 0.445 0.026  0.081  -0.012 262 LEU BBB CB  
5630  C CG  . LEU B 262 ? 0.646 0.620 0.452 0.021  0.089  -0.009 262 LEU BBB CG  
5631  C CD1 . LEU B 262 ? 0.649 0.625 0.465 0.015  0.094  -0.011 262 LEU BBB CD1 
5632  C CD2 . LEU B 262 ? 0.665 0.626 0.453 0.026  0.096  -0.005 262 LEU BBB CD2 
5633  N N   . VAL B 263 ? 0.650 0.643 0.440 0.044  0.065  -0.016 263 VAL BBB N   
5634  C CA  . VAL B 263 ? 0.641 0.645 0.434 0.048  0.056  -0.021 263 VAL BBB CA  
5635  C C   . VAL B 263 ? 0.640 0.648 0.432 0.050  0.056  -0.025 263 VAL BBB C   
5636  O O   . VAL B 263 ? 0.672 0.673 0.451 0.054  0.062  -0.023 263 VAL BBB O   
5637  C CB  . VAL B 263 ? 0.650 0.651 0.431 0.056  0.053  -0.020 263 VAL BBB CB  
5638  C CG1 . VAL B 263 ? 0.644 0.657 0.429 0.061  0.044  -0.026 263 VAL BBB CG1 
5639  C CG2 . VAL B 263 ? 0.628 0.623 0.408 0.054  0.054  -0.016 263 VAL BBB CG2 
5640  N N   . GLY B 264 ? 0.626 0.645 0.432 0.048  0.052  -0.030 264 GLY BBB N   
5641  C CA  . GLY B 264 ? 0.655 0.680 0.462 0.049  0.051  -0.034 264 GLY BBB CA  
5642  C C   . GLY B 264 ? 0.671 0.691 0.480 0.044  0.058  -0.032 264 GLY BBB C   
5643  O O   . GLY B 264 ? 0.720 0.741 0.525 0.046  0.060  -0.034 264 GLY BBB O   
5644  N N   . VAL B 265 ? 0.694 0.710 0.510 0.037  0.062  -0.029 265 VAL BBB N   
5645  C CA  . VAL B 265 ? 0.723 0.735 0.543 0.032  0.069  -0.028 265 VAL BBB CA  
5646  C C   . VAL B 265 ? 0.713 0.731 0.550 0.024  0.067  -0.030 265 VAL BBB C   
5647  O O   . VAL B 265 ? 0.700 0.719 0.543 0.022  0.064  -0.028 265 VAL BBB O   
5648  C CB  . VAL B 265 ? 0.773 0.772 0.580 0.032  0.077  -0.023 265 VAL BBB CB  
5649  C CG1 . VAL B 265 ? 0.797 0.791 0.609 0.026  0.084  -0.022 265 VAL BBB CG1 
5650  C CG2 . VAL B 265 ? 0.795 0.787 0.583 0.040  0.079  -0.020 265 VAL BBB CG2 
5651  N N   . VAL B 266 ? 0.729 0.750 0.575 0.019  0.069  -0.032 266 VAL BBB N   
5652  C CA  . VAL B 266 ? 0.718 0.744 0.580 0.012  0.068  -0.033 266 VAL BBB CA  
5653  C C   . VAL B 266 ? 0.737 0.759 0.601 0.008  0.075  -0.033 266 VAL BBB C   
5654  O O   . VAL B 266 ? 0.740 0.758 0.595 0.010  0.080  -0.033 266 VAL BBB O   
5655  C CB  . VAL B 266 ? 0.717 0.754 0.592 0.011  0.061  -0.037 266 VAL BBB CB  
5656  C CG1 . VAL B 266 ? 0.711 0.752 0.586 0.014  0.055  -0.038 266 VAL BBB CG1 
5657  C CG2 . VAL B 266 ? 0.724 0.765 0.598 0.013  0.061  -0.041 266 VAL BBB CG2 
5658  N N   . PRO B 267 ? 0.733 0.757 0.608 0.001  0.077  -0.033 267 PRO BBB N   
5659  C CA  . PRO B 267 ? 0.721 0.743 0.601 -0.003 0.083  -0.034 267 PRO BBB CA  
5660  C C   . PRO B 267 ? 0.668 0.698 0.554 -0.003 0.081  -0.039 267 PRO BBB C   
5661  O O   . PRO B 267 ? 0.669 0.706 0.562 -0.002 0.074  -0.041 267 PRO BBB O   
5662  C CB  . PRO B 267 ? 0.700 0.726 0.594 -0.009 0.082  -0.035 267 PRO BBB CB  
5663  C CG  . PRO B 267 ? 0.705 0.730 0.597 -0.008 0.078  -0.032 267 PRO BBB CG  
5664  C CD  . PRO B 267 ? 0.709 0.736 0.594 -0.002 0.073  -0.032 267 PRO BBB CD  
5665  N N   . ILE B 268 ? 0.664 0.689 0.546 -0.004 0.087  -0.039 268 ILE BBB N   
5666  C CA  . ILE B 268 ? 0.672 0.703 0.560 -0.004 0.088  -0.043 268 ILE BBB CA  
5667  C C   . ILE B 268 ? 0.643 0.674 0.541 -0.011 0.093  -0.045 268 ILE BBB C   
5668  O O   . ILE B 268 ? 0.648 0.685 0.554 -0.012 0.092  -0.048 268 ILE BBB O   
5669  C CB  . ILE B 268 ? 0.693 0.720 0.567 0.001  0.090  -0.043 268 ILE BBB CB  
5670  C CG1 . ILE B 268 ? 0.718 0.733 0.579 0.002  0.099  -0.039 268 ILE BBB CG1 
5671  C CG2 . ILE B 268 ? 0.679 0.709 0.546 0.008  0.084  -0.043 268 ILE BBB CG2 
5672  C CD1 . ILE B 268 ? 0.767 0.777 0.613 0.008  0.103  -0.039 268 ILE BBB CD1 
5673  N N   . ASN B 269 ? 0.610 0.634 0.507 -0.014 0.098  -0.042 269 ASN BBB N   
5674  C CA  . ASN B 269 ? 0.616 0.641 0.524 -0.020 0.102  -0.045 269 ASN BBB CA  
5675  C C   . ASN B 269 ? 0.578 0.600 0.489 -0.023 0.104  -0.043 269 ASN BBB C   
5676  O O   . ASN B 269 ? 0.618 0.633 0.519 -0.021 0.106  -0.039 269 ASN BBB O   
5677  C CB  . ASN B 269 ? 0.633 0.653 0.535 -0.021 0.111  -0.045 269 ASN BBB CB  
5678  C CG  . ASN B 269 ? 0.626 0.649 0.541 -0.027 0.115  -0.049 269 ASN BBB CG  
5679  O OD1 . ASN B 269 ? 0.742 0.759 0.657 -0.030 0.122  -0.049 269 ASN BBB OD1 
5680  N ND2 . ASN B 269 ? 0.576 0.609 0.505 -0.029 0.110  -0.053 269 ASN BBB ND2 
5681  N N   . ILE B 270 ? 0.542 0.569 0.467 -0.028 0.103  -0.046 270 ILE BBB N   
5682  C CA  . ILE B 270 ? 0.541 0.568 0.473 -0.032 0.104  -0.045 270 ILE BBB CA  
5683  C C   . ILE B 270 ? 0.535 0.563 0.477 -0.037 0.110  -0.049 270 ILE BBB C   
5684  O O   . ILE B 270 ? 0.475 0.512 0.428 -0.039 0.106  -0.053 270 ILE BBB O   
5685  C CB  . ILE B 270 ? 0.509 0.543 0.447 -0.032 0.095  -0.045 270 ILE BBB CB  
5686  C CG1 . ILE B 270 ? 0.537 0.568 0.464 -0.026 0.092  -0.041 270 ILE BBB CG1 
5687  C CG2 . ILE B 270 ? 0.511 0.546 0.458 -0.035 0.096  -0.045 270 ILE BBB CG2 
5688  C CD1 . ILE B 270 ? 0.535 0.571 0.467 -0.025 0.083  -0.041 270 ILE BBB CD1 
5689  N N   . GLU B 271 ? 0.565 0.585 0.503 -0.040 0.118  -0.048 271 GLU BBB N   
5690  C CA  . GLU B 271 ? 0.666 0.688 0.615 -0.045 0.124  -0.053 271 GLU BBB CA  
5691  C C   . GLU B 271 ? 0.670 0.689 0.623 -0.048 0.127  -0.053 271 GLU BBB C   
5692  O O   . GLU B 271 ? 0.671 0.683 0.615 -0.047 0.129  -0.049 271 GLU BBB O   
5693  C CB  . GLU B 271 ? 0.671 0.684 0.610 -0.045 0.134  -0.053 271 GLU BBB CB  
5694  C CG  . GLU B 271 ? 0.701 0.718 0.640 -0.043 0.132  -0.055 271 GLU BBB CG  
5695  C CD  . GLU B 271 ? 0.765 0.775 0.694 -0.041 0.141  -0.054 271 GLU BBB CD  
5696  O OE1 . GLU B 271 ? 0.753 0.752 0.670 -0.040 0.148  -0.050 271 GLU BBB OE1 
5697  O OE2 . GLU B 271 ? 0.800 0.813 0.731 -0.041 0.141  -0.056 271 GLU BBB OE2 
5698  N N   . LYS B 272 ? 0.682 0.707 0.649 -0.053 0.128  -0.058 272 LYS BBB N   
5699  C CA  . LYS B 272 ? 0.728 0.751 0.701 -0.057 0.133  -0.060 272 LYS BBB CA  
5700  C C   . LYS B 272 ? 0.703 0.717 0.673 -0.060 0.145  -0.061 272 LYS BBB C   
5701  O O   . LYS B 272 ? 0.611 0.627 0.587 -0.062 0.149  -0.065 272 LYS BBB O   
5702  C CB  . LYS B 272 ? 0.729 0.763 0.720 -0.061 0.129  -0.066 272 LYS BBB CB  
5703  C CG  . LYS B 272 ? 0.743 0.777 0.739 -0.063 0.130  -0.067 272 LYS BBB CG  
5704  C CD  . LYS B 272 ? 0.766 0.800 0.757 -0.060 0.123  -0.062 272 LYS BBB CD  
5705  C CE  . LYS B 272 ? 0.793 0.833 0.794 -0.062 0.119  -0.065 272 LYS BBB CE  
5706  N NZ  . LYS B 272 ? 0.809 0.853 0.807 -0.059 0.110  -0.061 272 LYS BBB NZ  
5707  N N   . VAL B 273 ? 0.741 0.743 0.699 -0.059 0.151  -0.056 273 VAL BBB N   
5708  C CA  . VAL B 273 ? 0.782 0.775 0.737 -0.061 0.164  -0.057 273 VAL BBB CA  
5709  C C   . VAL B 273 ? 0.796 0.787 0.758 -0.066 0.167  -0.059 273 VAL BBB C   
5710  O O   . VAL B 273 ? 0.749 0.734 0.704 -0.064 0.168  -0.055 273 VAL BBB O   
5711  C CB  . VAL B 273 ? 0.805 0.784 0.739 -0.057 0.169  -0.050 273 VAL BBB CB  
5712  C CG1 . VAL B 273 ? 0.806 0.773 0.736 -0.059 0.182  -0.050 273 VAL BBB CG1 
5713  C CG2 . VAL B 273 ? 0.819 0.800 0.747 -0.053 0.166  -0.050 273 VAL BBB CG2 
5714  N N   . ASN B 274 ? 0.817 0.816 0.796 -0.071 0.168  -0.066 274 ASN BBB N   
5715  C CA  . ASN B 274 ? 0.843 0.844 0.834 -0.075 0.171  -0.070 274 ASN BBB CA  
5716  C C   . ASN B 274 ? 0.775 0.784 0.769 -0.073 0.160  -0.069 274 ASN BBB C   
5717  O O   . ASN B 274 ? 0.710 0.730 0.710 -0.072 0.150  -0.071 274 ASN BBB O   
5718  C CB  . ASN B 274 ? 0.901 0.890 0.886 -0.077 0.183  -0.069 274 ASN BBB CB  
5719  C CG  . ASN B 274 ? 0.964 0.945 0.947 -0.080 0.194  -0.071 274 ASN BBB CG  
5720  O OD1 . ASN B 274 ? 1.022 0.991 0.991 -0.077 0.201  -0.066 274 ASN BBB OD1 
5721  N ND2 . ASN B 274 ? 0.934 0.924 0.933 -0.084 0.196  -0.078 274 ASN BBB ND2 
5722  N N   . GLU B 275 ? 0.744 0.747 0.733 -0.073 0.161  -0.066 275 GLU BBB N   
5723  C CA  . GLU B 275 ? 0.769 0.779 0.761 -0.072 0.151  -0.065 275 GLU BBB CA  
5724  C C   . GLU B 275 ? 0.715 0.721 0.693 -0.066 0.145  -0.058 275 GLU BBB C   
5725  O O   . GLU B 275 ? 0.624 0.636 0.604 -0.064 0.137  -0.057 275 GLU BBB O   
5726  C CB  . GLU B 275 ? 0.814 0.821 0.812 -0.075 0.156  -0.067 275 GLU BBB CB  
5727  C CG  . GLU B 275 ? 0.899 0.891 0.883 -0.074 0.165  -0.061 275 GLU BBB CG  
5728  C CD  . GLU B 275 ? 0.968 0.950 0.949 -0.077 0.178  -0.062 275 GLU BBB CD  
5729  O OE1 . GLU B 275 ? 0.999 0.986 0.991 -0.080 0.181  -0.069 275 GLU BBB OE1 
5730  O OE2 . GLU B 275 ? 0.999 0.968 0.966 -0.074 0.184  -0.057 275 GLU BBB OE2 
5731  N N   . ASN B 276 ? 0.680 0.677 0.644 -0.063 0.150  -0.053 276 ASN BBB N   
5732  C CA  . ASN B 276 ? 0.630 0.623 0.580 -0.057 0.145  -0.047 276 ASN BBB CA  
5733  C C   . ASN B 276 ? 0.598 0.598 0.548 -0.054 0.138  -0.047 276 ASN BBB C   
5734  O O   . ASN B 276 ? 0.604 0.609 0.562 -0.057 0.140  -0.051 276 ASN BBB O   
5735  C CB  . ASN B 276 ? 0.662 0.641 0.596 -0.055 0.153  -0.042 276 ASN BBB CB  
5736  C CG  . ASN B 276 ? 0.685 0.657 0.617 -0.056 0.158  -0.040 276 ASN BBB CG  
5737  O OD1 . ASN B 276 ? 0.595 0.571 0.533 -0.057 0.152  -0.041 276 ASN BBB OD1 
5738  N ND2 . ASN B 276 ? 0.750 0.708 0.672 -0.056 0.168  -0.037 276 ASN BBB ND2 
5739  N N   . ILE B 277 ? 0.567 0.567 0.508 -0.049 0.132  -0.042 277 ILE BBB N   
5740  C CA  . ILE B 277 ? 0.545 0.548 0.482 -0.046 0.126  -0.042 277 ILE BBB CA  
5741  C C   . ILE B 277 ? 0.561 0.555 0.481 -0.041 0.130  -0.037 277 ILE BBB C   
5742  O O   . ILE B 277 ? 0.550 0.539 0.459 -0.037 0.128  -0.033 277 ILE BBB O   
5743  C CB  . ILE B 277 ? 0.490 0.503 0.431 -0.044 0.115  -0.041 277 ILE BBB CB  
5744  C CG1 . ILE B 277 ? 0.480 0.502 0.438 -0.048 0.112  -0.046 277 ILE BBB CG1 
5745  C CG2 . ILE B 277 ? 0.479 0.495 0.417 -0.040 0.110  -0.041 277 ILE BBB CG2 
5746  C CD1 . ILE B 277 ? 0.469 0.498 0.431 -0.047 0.103  -0.045 277 ILE BBB CD1 
5747  N N   . LYS B 278 ? 0.561 0.552 0.478 -0.041 0.136  -0.039 278 LYS BBB N   
5748  C CA  . LYS B 278 ? 0.576 0.559 0.477 -0.036 0.139  -0.035 278 LYS BBB CA  
5749  C C   . LYS B 278 ? 0.513 0.503 0.411 -0.031 0.130  -0.035 278 LYS BBB C   
5750  O O   . LYS B 278 ? 0.479 0.478 0.387 -0.033 0.126  -0.038 278 LYS BBB O   
5751  C CB  . LYS B 278 ? 0.635 0.613 0.534 -0.038 0.149  -0.037 278 LYS BBB CB  
5752  C CG  . LYS B 278 ? 0.686 0.653 0.567 -0.033 0.155  -0.033 278 LYS BBB CG  
5753  C CD  . LYS B 278 ? 0.736 0.700 0.617 -0.035 0.163  -0.035 278 LYS BBB CD  
5754  C CE  . LYS B 278 ? 0.801 0.755 0.663 -0.029 0.169  -0.031 278 LYS BBB CE  
5755  N NZ  . LYS B 278 ? 0.816 0.769 0.678 -0.030 0.175  -0.034 278 LYS BBB NZ  
5756  N N   . VAL B 279 ? 0.494 0.481 0.381 -0.026 0.126  -0.031 279 VAL BBB N   
5757  C CA  . VAL B 279 ? 0.497 0.490 0.381 -0.021 0.117  -0.030 279 VAL BBB CA  
5758  C C   . VAL B 279 ? 0.513 0.500 0.381 -0.016 0.121  -0.028 279 VAL BBB C   
5759  O O   . VAL B 279 ? 0.492 0.469 0.347 -0.013 0.126  -0.024 279 VAL BBB O   
5760  C CB  . VAL B 279 ? 0.492 0.488 0.376 -0.020 0.110  -0.028 279 VAL BBB CB  
5761  C CG1 . VAL B 279 ? 0.488 0.489 0.367 -0.014 0.102  -0.028 279 VAL BBB CG1 
5762  C CG2 . VAL B 279 ? 0.475 0.479 0.374 -0.025 0.106  -0.031 279 VAL BBB CG2 
5763  N N   . SER B 280 ? 0.539 0.532 0.409 -0.014 0.118  -0.031 280 SER BBB N   
5764  C CA  . SER B 280 ? 0.557 0.545 0.412 -0.008 0.120  -0.030 280 SER BBB CA  
5765  C C   . SER B 280 ? 0.568 0.562 0.420 -0.003 0.110  -0.030 280 SER BBB C   
5766  O O   . SER B 280 ? 0.532 0.537 0.396 -0.005 0.103  -0.033 280 SER BBB O   
5767  C CB  . SER B 280 ? 0.556 0.546 0.414 -0.010 0.124  -0.033 280 SER BBB CB  
5768  O OG  . SER B 280 ? 0.547 0.528 0.404 -0.014 0.134  -0.032 280 SER BBB OG  
5769  N N   . PHE B 281 ? 0.622 0.610 0.458 0.004  0.111  -0.026 281 PHE BBB N   
5770  C CA  . PHE B 281 ? 0.660 0.653 0.492 0.009  0.102  -0.026 281 PHE BBB CA  
5771  C C   . PHE B 281 ? 0.720 0.715 0.544 0.015  0.100  -0.028 281 PHE BBB C   
5772  O O   . PHE B 281 ? 0.711 0.700 0.526 0.017  0.107  -0.027 281 PHE BBB O   
5773  C CB  . PHE B 281 ? 0.686 0.671 0.507 0.013  0.103  -0.022 281 PHE BBB CB  
5774  C CG  . PHE B 281 ? 0.683 0.668 0.513 0.008  0.102  -0.021 281 PHE BBB CG  
5775  C CD1 . PHE B 281 ? 0.665 0.660 0.507 0.006  0.093  -0.022 281 PHE BBB CD1 
5776  C CD2 . PHE B 281 ? 0.705 0.681 0.534 0.004  0.110  -0.018 281 PHE BBB CD2 
5777  C CE1 . PHE B 281 ? 0.646 0.641 0.495 0.002  0.092  -0.021 281 PHE BBB CE1 
5778  C CE2 . PHE B 281 ? 0.729 0.706 0.566 -0.000 0.108  -0.017 281 PHE BBB CE2 
5779  C CZ  . PHE B 281 ? 0.667 0.654 0.514 -0.001 0.100  -0.019 281 PHE BBB CZ  
5780  N N   . SER B 282 ? 0.780 0.784 0.607 0.018  0.092  -0.030 282 SER BBB N   
5781  C CA  . SER B 282 ? 0.798 0.808 0.620 0.024  0.088  -0.034 282 SER BBB CA  
5782  C C   . SER B 282 ? 0.804 0.805 0.606 0.032  0.091  -0.031 282 SER BBB C   
5783  O O   . SER B 282 ? 0.855 0.858 0.650 0.037  0.090  -0.033 282 SER BBB O   
5784  C CB  . SER B 282 ? 0.764 0.784 0.596 0.025  0.078  -0.037 282 SER BBB CB  
5785  O OG  . SER B 282 ? 0.757 0.775 0.581 0.030  0.075  -0.035 282 SER BBB OG  
5786  N N   . ASP B 283 ? 0.799 0.790 0.590 0.034  0.095  -0.026 283 ASP BBB N   
5787  C CA  . ASP B 283 ? 0.821 0.802 0.591 0.042  0.100  -0.023 283 ASP BBB CA  
5788  C C   . ASP B 283 ? 0.860 0.829 0.622 0.040  0.111  -0.020 283 ASP BBB C   
5789  O O   . ASP B 283 ? 0.852 0.811 0.596 0.046  0.116  -0.016 283 ASP BBB O   
5790  C CB  . ASP B 283 ? 0.809 0.784 0.570 0.046  0.098  -0.019 283 ASP BBB CB  
5791  C CG  . ASP B 283 ? 0.813 0.780 0.577 0.041  0.103  -0.015 283 ASP BBB CG  
5792  O OD1 . ASP B 283 ? 0.818 0.786 0.594 0.033  0.107  -0.016 283 ASP BBB OD1 
5793  O OD2 . ASP B 283 ? 0.727 0.688 0.481 0.044  0.103  -0.011 283 ASP BBB OD2 
5794  N N   . GLY B 284 ? 0.866 0.838 0.642 0.032  0.115  -0.022 284 GLY BBB N   
5795  C CA  . GLY B 284 ? 0.856 0.819 0.627 0.029  0.126  -0.020 284 GLY BBB CA  
5796  C C   . GLY B 284 ? 0.860 0.812 0.630 0.026  0.133  -0.016 284 GLY BBB C   
5797  O O   . GLY B 284 ? 0.835 0.778 0.602 0.023  0.143  -0.014 284 GLY BBB O   
5798  N N   . SER B 285 ? 0.832 0.785 0.605 0.025  0.128  -0.014 285 SER BBB N   
5799  C CA  . SER B 285 ? 0.826 0.770 0.599 0.021  0.135  -0.011 285 SER BBB CA  
5800  C C   . SER B 285 ? 0.764 0.714 0.557 0.012  0.135  -0.014 285 SER BBB C   
5801  O O   . SER B 285 ? 0.699 0.661 0.506 0.009  0.128  -0.018 285 SER BBB O   
5802  C CB  . SER B 285 ? 0.821 0.762 0.587 0.025  0.130  -0.007 285 SER BBB CB  
5803  O OG  . SER B 285 ? 0.825 0.778 0.605 0.023  0.121  -0.010 285 SER BBB OG  
5804  N N   . VAL B 286 ? 0.760 0.702 0.555 0.007  0.143  -0.012 286 VAL BBB N   
5805  C CA  . VAL B 286 ? 0.746 0.692 0.559 -0.002 0.145  -0.015 286 VAL BBB CA  
5806  C C   . VAL B 286 ? 0.733 0.675 0.548 -0.004 0.145  -0.013 286 VAL BBB C   
5807  O O   . VAL B 286 ? 0.732 0.663 0.532 0.000  0.150  -0.008 286 VAL BBB O   
5808  C CB  . VAL B 286 ? 0.790 0.732 0.605 -0.006 0.155  -0.017 286 VAL BBB CB  
5809  C CG1 . VAL B 286 ? 0.812 0.756 0.643 -0.015 0.158  -0.020 286 VAL BBB CG1 
5810  C CG2 . VAL B 286 ? 0.786 0.734 0.603 -0.005 0.153  -0.020 286 VAL BBB CG2 
5811  N N   . GLU B 287 ? 0.694 0.645 0.526 -0.010 0.141  -0.015 287 GLU BBB N   
5812  C CA  . GLU B 287 ? 0.675 0.622 0.510 -0.013 0.143  -0.014 287 GLU BBB CA  
5813  C C   . GLU B 287 ? 0.641 0.597 0.496 -0.021 0.141  -0.018 287 GLU BBB C   
5814  O O   . GLU B 287 ? 0.588 0.554 0.452 -0.022 0.134  -0.022 287 GLU BBB O   
5815  C CB  . GLU B 287 ? 0.697 0.645 0.525 -0.008 0.135  -0.011 287 GLU BBB CB  
5816  C CG  . GLU B 287 ? 0.708 0.649 0.534 -0.009 0.138  -0.008 287 GLU BBB CG  
5817  C CD  . GLU B 287 ? 0.727 0.668 0.545 -0.004 0.131  -0.005 287 GLU BBB CD  
5818  O OE1 . GLU B 287 ? 0.752 0.700 0.569 0.000  0.123  -0.006 287 GLU BBB OE1 
5819  O OE2 . GLU B 287 ? 0.683 0.617 0.499 -0.004 0.134  -0.002 287 GLU BBB OE2 
5820  N N   . GLU B 288 ? 0.647 0.597 0.506 -0.025 0.147  -0.018 288 GLU BBB N   
5821  C CA  . GLU B 288 ? 0.638 0.597 0.515 -0.032 0.146  -0.023 288 GLU BBB CA  
5822  C C   . GLU B 288 ? 0.581 0.545 0.463 -0.032 0.138  -0.022 288 GLU BBB C   
5823  O O   . GLU B 288 ? 0.572 0.528 0.443 -0.029 0.138  -0.018 288 GLU BBB O   
5824  C CB  . GLU B 288 ? 0.647 0.599 0.528 -0.037 0.157  -0.025 288 GLU BBB CB  
5825  C CG  . GLU B 288 ? 0.678 0.627 0.557 -0.038 0.164  -0.027 288 GLU BBB CG  
5826  C CD  . GLU B 288 ? 0.679 0.625 0.567 -0.044 0.174  -0.031 288 GLU BBB CD  
5827  O OE1 . GLU B 288 ? 0.642 0.592 0.543 -0.049 0.174  -0.034 288 GLU BBB OE1 
5828  O OE2 . GLU B 288 ? 0.757 0.699 0.641 -0.044 0.181  -0.031 288 GLU BBB OE2 
5829  N N   . PHE B 289 ? 0.542 0.518 0.439 -0.035 0.131  -0.026 289 PHE BBB N   
5830  C CA  . PHE B 289 ? 0.545 0.527 0.449 -0.036 0.124  -0.026 289 PHE BBB CA  
5831  C C   . PHE B 289 ? 0.517 0.506 0.437 -0.042 0.124  -0.031 289 PHE BBB C   
5832  O O   . PHE B 289 ? 0.492 0.485 0.419 -0.045 0.126  -0.035 289 PHE BBB O   
5833  C CB  . PHE B 289 ? 0.539 0.528 0.441 -0.032 0.114  -0.025 289 PHE BBB CB  
5834  C CG  . PHE B 289 ? 0.542 0.525 0.429 -0.026 0.113  -0.021 289 PHE BBB CG  
5835  C CD1 . PHE B 289 ? 0.546 0.528 0.427 -0.023 0.114  -0.022 289 PHE BBB CD1 
5836  C CD2 . PHE B 289 ? 0.555 0.534 0.433 -0.022 0.111  -0.017 289 PHE BBB CD2 
5837  C CE1 . PHE B 289 ? 0.582 0.560 0.449 -0.017 0.113  -0.019 289 PHE BBB CE1 
5838  C CE2 . PHE B 289 ? 0.580 0.554 0.444 -0.016 0.110  -0.014 289 PHE BBB CE2 
5839  C CZ  . PHE B 289 ? 0.583 0.557 0.442 -0.013 0.111  -0.015 289 PHE BBB CZ  
5840  N N   . GLU B 290 ? 0.519 0.511 0.445 -0.044 0.121  -0.031 290 GLU BBB N   
5841  C CA  . GLU B 290 ? 0.509 0.510 0.451 -0.048 0.118  -0.036 290 GLU BBB CA  
5842  C C   . GLU B 290 ? 0.477 0.488 0.425 -0.047 0.108  -0.037 290 GLU BBB C   
5843  O O   . GLU B 290 ? 0.462 0.481 0.422 -0.050 0.106  -0.042 290 GLU BBB O   
5844  C CB  . GLU B 290 ? 0.533 0.532 0.477 -0.050 0.119  -0.036 290 GLU BBB CB  
5845  C CG  . GLU B 290 ? 0.571 0.579 0.531 -0.055 0.118  -0.041 290 GLU BBB CG  
5846  C CD  . GLU B 290 ? 0.603 0.609 0.567 -0.058 0.121  -0.043 290 GLU BBB CD  
5847  O OE1 . GLU B 290 ? 0.610 0.625 0.585 -0.060 0.116  -0.046 290 GLU BBB OE1 
5848  O OE2 . GLU B 290 ? 0.654 0.649 0.609 -0.058 0.128  -0.040 290 GLU BBB OE2 
5849  N N   . THR B 291 ? 0.465 0.477 0.406 -0.043 0.102  -0.033 291 THR BBB N   
5850  C CA  . THR B 291 ? 0.425 0.446 0.372 -0.041 0.093  -0.034 291 THR BBB CA  
5851  C C   . THR B 291 ? 0.426 0.445 0.363 -0.037 0.090  -0.031 291 THR BBB C   
5852  O O   . THR B 291 ? 0.439 0.452 0.364 -0.033 0.091  -0.028 291 THR BBB O   
5853  C CB  . THR B 291 ? 0.423 0.446 0.372 -0.041 0.088  -0.033 291 THR BBB CB  
5854  O OG1 . THR B 291 ? 0.397 0.422 0.354 -0.045 0.090  -0.036 291 THR BBB OG1 
5855  C CG2 . THR B 291 ? 0.401 0.433 0.356 -0.039 0.079  -0.033 291 THR BBB CG2 
5856  N N   . VAL B 292 ? 0.395 0.422 0.338 -0.036 0.085  -0.033 292 VAL BBB N   
5857  C CA  . VAL B 292 ? 0.376 0.404 0.313 -0.032 0.081  -0.032 292 VAL BBB CA  
5858  C C   . VAL B 292 ? 0.363 0.399 0.307 -0.031 0.073  -0.033 292 VAL BBB C   
5859  O O   . VAL B 292 ? 0.338 0.381 0.294 -0.034 0.071  -0.036 292 VAL BBB O   
5860  C CB  . VAL B 292 ? 0.380 0.408 0.315 -0.031 0.084  -0.034 292 VAL BBB CB  
5861  C CG1 . VAL B 292 ? 0.367 0.397 0.297 -0.027 0.079  -0.033 292 VAL BBB CG1 
5862  C CG2 . VAL B 292 ? 0.388 0.406 0.314 -0.031 0.093  -0.032 292 VAL BBB CG2 
5863  N N   . LEU B 293 ? 0.363 0.399 0.302 -0.028 0.068  -0.030 293 LEU BBB N   
5864  C CA  . LEU B 293 ? 0.355 0.397 0.300 -0.027 0.061  -0.031 293 LEU BBB CA  
5865  C C   . LEU B 293 ? 0.375 0.419 0.317 -0.023 0.058  -0.031 293 LEU BBB C   
5866  O O   . LEU B 293 ? 0.413 0.453 0.345 -0.020 0.058  -0.029 293 LEU BBB O   
5867  C CB  . LEU B 293 ? 0.350 0.391 0.294 -0.027 0.059  -0.028 293 LEU BBB CB  
5868  C CG  . LEU B 293 ? 0.335 0.382 0.286 -0.027 0.053  -0.028 293 LEU BBB CG  
5869  C CD1 . LEU B 293 ? 0.332 0.377 0.284 -0.028 0.053  -0.027 293 LEU BBB CD1 
5870  C CD2 . LEU B 293 ? 0.339 0.387 0.287 -0.023 0.049  -0.027 293 LEU BBB CD2 
5871  N N   . TYR B 294 ? 0.383 0.434 0.334 -0.024 0.054  -0.033 294 TYR BBB N   
5872  C CA  . TYR B 294 ? 0.400 0.454 0.349 -0.020 0.051  -0.034 294 TYR BBB CA  
5873  C C   . TYR B 294 ? 0.390 0.447 0.342 -0.019 0.045  -0.033 294 TYR BBB C   
5874  O O   . TYR B 294 ? 0.351 0.412 0.312 -0.021 0.043  -0.034 294 TYR BBB O   
5875  C CB  . TYR B 294 ? 0.412 0.471 0.369 -0.021 0.050  -0.037 294 TYR BBB CB  
5876  C CG  . TYR B 294 ? 0.447 0.504 0.397 -0.020 0.054  -0.038 294 TYR BBB CG  
5877  C CD1 . TYR B 294 ? 0.463 0.519 0.406 -0.016 0.053  -0.039 294 TYR BBB CD1 
5878  C CD2 . TYR B 294 ? 0.468 0.523 0.420 -0.023 0.060  -0.039 294 TYR BBB CD2 
5879  C CE1 . TYR B 294 ? 0.482 0.535 0.418 -0.015 0.057  -0.040 294 TYR BBB CE1 
5880  C CE2 . TYR B 294 ? 0.490 0.541 0.435 -0.022 0.064  -0.040 294 TYR BBB CE2 
5881  C CZ  . TYR B 294 ? 0.512 0.562 0.449 -0.018 0.063  -0.040 294 TYR BBB CZ  
5882  O OH  . TYR B 294 ? 0.525 0.572 0.455 -0.016 0.067  -0.041 294 TYR BBB OH  
5883  N N   . ALA B 295 ? 0.389 0.444 0.334 -0.016 0.044  -0.032 295 ALA BBB N   
5884  C CA  . ALA B 295 ? 0.417 0.475 0.365 -0.014 0.039  -0.032 295 ALA BBB CA  
5885  C C   . ALA B 295 ? 0.422 0.483 0.368 -0.011 0.036  -0.034 295 ALA BBB C   
5886  O O   . ALA B 295 ? 0.413 0.473 0.354 -0.008 0.034  -0.034 295 ALA BBB O   
5887  C CB  . ALA B 295 ? 0.421 0.474 0.362 -0.014 0.039  -0.029 295 ALA BBB CB  
5888  N N   . THR B 296 ? 0.455 0.519 0.406 -0.011 0.036  -0.037 296 THR BBB N   
5889  C CA  . THR B 296 ? 0.475 0.542 0.424 -0.008 0.035  -0.040 296 THR BBB CA  
5890  C C   . THR B 296 ? 0.479 0.552 0.438 -0.008 0.030  -0.042 296 THR BBB C   
5891  O O   . THR B 296 ? 0.525 0.601 0.483 -0.005 0.028  -0.045 296 THR BBB O   
5892  C CB  . THR B 296 ? 0.477 0.545 0.425 -0.008 0.038  -0.041 296 THR BBB CB  
5893  O OG1 . THR B 296 ? 0.431 0.500 0.388 -0.013 0.039  -0.041 296 THR BBB OG1 
5894  C CG2 . THR B 296 ? 0.504 0.565 0.439 -0.007 0.042  -0.039 296 THR BBB CG2 
5895  N N   . GLY B 297 ? 0.463 0.537 0.430 -0.011 0.030  -0.041 297 GLY BBB N   
5896  C CA  . GLY B 297 ? 0.435 0.513 0.411 -0.011 0.026  -0.042 297 GLY BBB CA  
5897  C C   . GLY B 297 ? 0.419 0.499 0.404 -0.014 0.027  -0.041 297 GLY BBB C   
5898  O O   . GLY B 297 ? 0.431 0.509 0.415 -0.016 0.029  -0.040 297 GLY BBB O   
5899  N N   . ARG B 298 ? 0.411 0.493 0.404 -0.014 0.025  -0.043 298 ARG BBB N   
5900  C CA  . ARG B 298 ? 0.414 0.498 0.416 -0.016 0.024  -0.042 298 ARG BBB CA  
5901  C C   . ARG B 298 ? 0.410 0.498 0.420 -0.016 0.024  -0.045 298 ARG BBB C   
5902  O O   . ARG B 298 ? 0.413 0.502 0.424 -0.014 0.022  -0.047 298 ARG BBB O   
5903  C CB  . ARG B 298 ? 0.411 0.493 0.413 -0.017 0.023  -0.039 298 ARG BBB CB  
5904  C CG  . ARG B 298 ? 0.388 0.466 0.383 -0.017 0.024  -0.036 298 ARG BBB CG  
5905  C CD  . ARG B 298 ? 0.361 0.438 0.355 -0.017 0.023  -0.034 298 ARG BBB CD  
5906  N NE  . ARG B 298 ? 0.345 0.422 0.346 -0.018 0.022  -0.033 298 ARG BBB NE  
5907  C CZ  . ARG B 298 ? 0.344 0.421 0.346 -0.019 0.022  -0.031 298 ARG BBB CZ  
5908  N NH1 . ARG B 298 ? 0.355 0.431 0.353 -0.020 0.024  -0.031 298 ARG BBB NH1 
5909  N NH2 . ARG B 298 ? 0.345 0.423 0.352 -0.019 0.021  -0.030 298 ARG BBB NH2 
5910  N N   . ASN B 299 ? 0.409 0.498 0.425 -0.017 0.024  -0.046 299 ASN BBB N   
5911  C CA  . ASN B 299 ? 0.413 0.505 0.438 -0.017 0.024  -0.048 299 ASN BBB CA  
5912  C C   . ASN B 299 ? 0.394 0.485 0.425 -0.017 0.023  -0.046 299 ASN BBB C   
5913  O O   . ASN B 299 ? 0.400 0.489 0.429 -0.018 0.023  -0.043 299 ASN BBB O   
5914  C CB  . ASN B 299 ? 0.436 0.531 0.464 -0.018 0.025  -0.050 299 ASN BBB CB  
5915  C CG  . ASN B 299 ? 0.454 0.549 0.476 -0.017 0.026  -0.053 299 ASN BBB CG  
5916  O OD1 . ASN B 299 ? 0.474 0.568 0.493 -0.018 0.028  -0.052 299 ASN BBB OD1 
5917  N ND2 . ASN B 299 ? 0.450 0.546 0.471 -0.015 0.025  -0.055 299 ASN BBB ND2 
5918  N N   . PRO B 300 ? 0.359 0.451 0.396 -0.017 0.023  -0.047 300 PRO BBB N   
5919  C CA  . PRO B 300 ? 0.348 0.438 0.390 -0.017 0.022  -0.045 300 PRO BBB CA  
5920  C C   . PRO B 300 ? 0.360 0.451 0.406 -0.017 0.023  -0.045 300 PRO BBB C   
5921  O O   . PRO B 300 ? 0.352 0.445 0.401 -0.017 0.023  -0.047 300 PRO BBB O   
5922  C CB  . PRO B 300 ? 0.336 0.427 0.385 -0.016 0.023  -0.048 300 PRO BBB CB  
5923  C CG  . PRO B 300 ? 0.340 0.435 0.390 -0.016 0.023  -0.052 300 PRO BBB CG  
5924  C CD  . PRO B 300 ? 0.346 0.440 0.385 -0.016 0.022  -0.051 300 PRO BBB CD  
5925  N N   . ASP B 301 ? 0.398 0.486 0.443 -0.017 0.023  -0.041 301 ASP BBB N   
5926  C CA  . ASP B 301 ? 0.429 0.519 0.478 -0.016 0.023  -0.041 301 ASP BBB CA  
5927  C C   . ASP B 301 ? 0.425 0.514 0.480 -0.015 0.023  -0.041 301 ASP BBB C   
5928  O O   . ASP B 301 ? 0.423 0.509 0.478 -0.013 0.023  -0.038 301 ASP BBB O   
5929  C CB  . ASP B 301 ? 0.461 0.550 0.505 -0.016 0.022  -0.038 301 ASP BBB CB  
5930  C CG  . ASP B 301 ? 0.516 0.607 0.562 -0.016 0.021  -0.038 301 ASP BBB CG  
5931  O OD1 . ASP B 301 ? 0.624 0.718 0.674 -0.016 0.022  -0.041 301 ASP BBB OD1 
5932  O OD2 . ASP B 301 ? 0.515 0.605 0.560 -0.015 0.020  -0.036 301 ASP BBB OD2 
5933  N N   . VAL B 302 ? 0.427 0.518 0.488 -0.015 0.024  -0.044 302 VAL BBB N   
5934  C CA  . VAL B 302 ? 0.449 0.539 0.517 -0.014 0.025  -0.044 302 VAL BBB CA  
5935  C C   . VAL B 302 ? 0.480 0.572 0.553 -0.013 0.025  -0.047 302 VAL BBB C   
5936  O O   . VAL B 302 ? 0.523 0.614 0.602 -0.012 0.026  -0.047 302 VAL BBB O   
5937  C CB  . VAL B 302 ? 0.428 0.517 0.498 -0.014 0.026  -0.046 302 VAL BBB CB  
5938  C CG1 . VAL B 302 ? 0.418 0.505 0.485 -0.014 0.026  -0.044 302 VAL BBB CG1 
5939  C CG2 . VAL B 302 ? 0.414 0.507 0.484 -0.015 0.026  -0.051 302 VAL BBB CG2 
5940  N N   . LYS B 303 ? 0.496 0.592 0.567 -0.014 0.025  -0.048 303 LYS BBB N   
5941  C CA  . LYS B 303 ? 0.515 0.614 0.591 -0.014 0.025  -0.051 303 LYS BBB CA  
5942  C C   . LYS B 303 ? 0.493 0.591 0.573 -0.012 0.025  -0.050 303 LYS BBB C   
5943  O O   . LYS B 303 ? 0.523 0.621 0.608 -0.011 0.025  -0.051 303 LYS BBB O   
5944  C CB  . LYS B 303 ? 0.535 0.637 0.608 -0.016 0.025  -0.054 303 LYS BBB CB  
5945  C CG  . LYS B 303 ? 0.561 0.664 0.630 -0.017 0.026  -0.056 303 LYS BBB CG  
5946  C CD  . LYS B 303 ? 0.581 0.685 0.643 -0.019 0.026  -0.056 303 LYS BBB CD  
5947  C CE  . LYS B 303 ? 0.597 0.702 0.655 -0.019 0.027  -0.059 303 LYS BBB CE  
5948  N NZ  . LYS B 303 ? 0.578 0.684 0.633 -0.021 0.029  -0.060 303 LYS BBB NZ  
5949  N N   . GLY B 304 ? 0.475 0.571 0.550 -0.011 0.024  -0.046 304 GLY BBB N   
5950  C CA  . GLY B 304 ? 0.465 0.560 0.543 -0.008 0.023  -0.045 304 GLY BBB CA  
5951  C C   . GLY B 304 ? 0.469 0.559 0.549 -0.006 0.024  -0.042 304 GLY BBB C   
5952  O O   . GLY B 304 ? 0.457 0.546 0.538 -0.003 0.023  -0.040 304 GLY BBB O   
5953  N N   . LEU B 305 ? 0.462 0.550 0.544 -0.007 0.025  -0.042 305 LEU BBB N   
5954  C CA  . LEU B 305 ? 0.469 0.551 0.552 -0.005 0.027  -0.039 305 LEU BBB CA  
5955  C C   . LEU B 305 ? 0.472 0.553 0.562 -0.004 0.029  -0.040 305 LEU BBB C   
5956  O O   . LEU B 305 ? 0.531 0.607 0.623 -0.002 0.031  -0.037 305 LEU BBB O   
5957  C CB  . LEU B 305 ? 0.437 0.517 0.518 -0.007 0.028  -0.039 305 LEU BBB CB  
5958  C CG  . LEU B 305 ? 0.449 0.529 0.522 -0.007 0.027  -0.036 305 LEU BBB CG  
5959  C CD1 . LEU B 305 ? 0.465 0.543 0.537 -0.009 0.028  -0.036 305 LEU BBB CD1 
5960  C CD2 . LEU B 305 ? 0.445 0.521 0.515 -0.004 0.026  -0.031 305 LEU BBB CD2 
5961  N N   . ASN B 306 ? 0.487 0.572 0.582 -0.005 0.029  -0.044 306 ASN BBB N   
5962  C CA  . ASN B 306 ? 0.479 0.564 0.582 -0.004 0.031  -0.046 306 ASN BBB CA  
5963  C C   . ASN B 306 ? 0.471 0.553 0.578 -0.006 0.034  -0.048 306 ASN BBB C   
5964  O O   . ASN B 306 ? 0.455 0.533 0.568 -0.004 0.036  -0.047 306 ASN BBB O   
5965  C CB  . ASN B 306 ? 0.509 0.590 0.612 -0.000 0.031  -0.044 306 ASN BBB CB  
5966  C CG  . ASN B 306 ? 0.543 0.625 0.654 0.001  0.033  -0.046 306 ASN BBB CG  
5967  O OD1 . ASN B 306 ? 0.604 0.690 0.719 -0.002 0.032  -0.051 306 ASN BBB OD1 
5968  N ND2 . ASN B 306 ? 0.521 0.598 0.634 0.004  0.034  -0.043 306 ASN BBB ND2 
5969  N N   . LEU B 307 ? 0.456 0.540 0.562 -0.008 0.033  -0.050 307 LEU BBB N   
5970  C CA  . LEU B 307 ? 0.472 0.554 0.581 -0.009 0.036  -0.051 307 LEU BBB CA  
5971  C C   . LEU B 307 ? 0.510 0.595 0.629 -0.010 0.037  -0.056 307 LEU BBB C   
5972  O O   . LEU B 307 ? 0.503 0.584 0.628 -0.010 0.041  -0.057 307 LEU BBB O   
5973  C CB  . LEU B 307 ? 0.476 0.561 0.580 -0.011 0.034  -0.053 307 LEU BBB CB  
5974  C CG  . LEU B 307 ? 0.473 0.556 0.569 -0.011 0.032  -0.049 307 LEU BBB CG  
5975  C CD1 . LEU B 307 ? 0.479 0.565 0.571 -0.013 0.031  -0.051 307 LEU BBB CD1 
5976  C CD2 . LEU B 307 ? 0.476 0.553 0.572 -0.010 0.034  -0.045 307 LEU BBB CD2 
5977  N N   . ASN B 308 ? 0.534 0.624 0.653 -0.011 0.036  -0.060 308 ASN BBB N   
5978  C CA  . ASN B 308 ? 0.573 0.666 0.701 -0.012 0.037  -0.065 308 ASN BBB CA  
5979  C C   . ASN B 308 ? 0.548 0.637 0.684 -0.010 0.040  -0.064 308 ASN BBB C   
5980  O O   . ASN B 308 ? 0.556 0.644 0.699 -0.011 0.043  -0.067 308 ASN BBB O   
5981  C CB  . ASN B 308 ? 0.644 0.743 0.771 -0.013 0.035  -0.068 308 ASN BBB CB  
5982  C CG  . ASN B 308 ? 0.728 0.831 0.862 -0.014 0.036  -0.075 308 ASN BBB CG  
5983  O OD1 . ASN B 308 ? 0.695 0.797 0.837 -0.014 0.039  -0.077 308 ASN BBB OD1 
5984  N ND2 . ASN B 308 ? 0.818 0.926 0.950 -0.014 0.035  -0.078 308 ASN BBB ND2 
5985  N N   . ALA B 309 ? 0.515 0.601 0.648 -0.008 0.040  -0.061 309 ALA BBB N   
5986  C CA  . ALA B 309 ? 0.503 0.584 0.642 -0.005 0.042  -0.059 309 ALA BBB CA  
5987  C C   . ALA B 309 ? 0.484 0.558 0.625 -0.004 0.046  -0.056 309 ALA BBB C   
5988  O O   . ALA B 309 ? 0.517 0.587 0.665 -0.003 0.049  -0.057 309 ALA BBB O   
5989  C CB  . ALA B 309 ? 0.501 0.583 0.636 -0.003 0.040  -0.056 309 ALA BBB CB  
5990  N N   . ILE B 310 ? 0.479 0.551 0.614 -0.005 0.046  -0.053 310 ILE BBB N   
5991  C CA  . ILE B 310 ? 0.491 0.555 0.627 -0.004 0.049  -0.050 310 ILE BBB CA  
5992  C C   . ILE B 310 ? 0.439 0.504 0.582 -0.006 0.052  -0.054 310 ILE BBB C   
5993  O O   . ILE B 310 ? 0.421 0.480 0.569 -0.006 0.057  -0.053 310 ILE BBB O   
5994  C CB  . ILE B 310 ? 0.515 0.576 0.641 -0.002 0.048  -0.044 310 ILE BBB CB  
5995  C CG1 . ILE B 310 ? 0.535 0.596 0.654 0.001  0.045  -0.041 310 ILE BBB CG1 
5996  C CG2 . ILE B 310 ? 0.507 0.560 0.633 -0.001 0.052  -0.041 310 ILE BBB CG2 
5997  C CD1 . ILE B 310 ? 0.536 0.595 0.660 0.004  0.046  -0.040 310 ILE BBB CD1 
5998  N N   . GLY B 311 ? 0.430 0.502 0.574 -0.009 0.050  -0.060 311 GLY BBB N   
5999  C CA  . GLY B 311 ? 0.436 0.510 0.587 -0.012 0.052  -0.065 311 GLY BBB CA  
6000  C C   . GLY B 311 ? 0.438 0.513 0.584 -0.013 0.050  -0.064 311 GLY BBB C   
6001  O O   . GLY B 311 ? 0.454 0.529 0.606 -0.014 0.053  -0.068 311 GLY BBB O   
6002  N N   . VAL B 312 ? 0.420 0.496 0.556 -0.012 0.047  -0.061 312 VAL BBB N   
6003  C CA  . VAL B 312 ? 0.444 0.521 0.574 -0.013 0.045  -0.060 312 VAL BBB CA  
6004  C C   . VAL B 312 ? 0.452 0.538 0.582 -0.015 0.042  -0.066 312 VAL BBB C   
6005  O O   . VAL B 312 ? 0.459 0.548 0.583 -0.014 0.039  -0.065 312 VAL BBB O   
6006  C CB  . VAL B 312 ? 0.449 0.524 0.569 -0.012 0.043  -0.054 312 VAL BBB CB  
6007  C CG1 . VAL B 312 ? 0.435 0.512 0.548 -0.013 0.041  -0.054 312 VAL BBB CG1 
6008  C CG2 . VAL B 312 ? 0.443 0.510 0.562 -0.010 0.046  -0.048 312 VAL BBB CG2 
6009  N N   . GLU B 313 ? 0.462 0.550 0.596 -0.016 0.042  -0.070 313 GLU BBB N   
6010  C CA  . GLU B 313 ? 0.486 0.582 0.620 -0.017 0.040  -0.076 313 GLU BBB CA  
6011  C C   . GLU B 313 ? 0.468 0.566 0.591 -0.016 0.036  -0.074 313 GLU BBB C   
6012  O O   . GLU B 313 ? 0.448 0.541 0.565 -0.016 0.036  -0.070 313 GLU BBB O   
6013  C CB  . GLU B 313 ? 0.544 0.642 0.687 -0.017 0.042  -0.083 313 GLU BBB CB  
6014  C CG  . GLU B 313 ? 0.636 0.734 0.792 -0.018 0.045  -0.086 313 GLU BBB CG  
6015  C CD  . GLU B 313 ? 0.744 0.846 0.911 -0.019 0.047  -0.094 313 GLU BBB CD  
6016  O OE1 . GLU B 313 ? 0.746 0.852 0.920 -0.019 0.047  -0.100 313 GLU BBB OE1 
6017  O OE2 . GLU B 313 ? 0.881 0.983 1.050 -0.020 0.048  -0.096 313 GLU BBB OE2 
6018  N N   . VAL B 314 ? 0.443 0.546 0.561 -0.016 0.033  -0.076 314 VAL BBB N   
6019  C CA  . VAL B 314 ? 0.441 0.546 0.548 -0.016 0.030  -0.075 314 VAL BBB CA  
6020  C C   . VAL B 314 ? 0.455 0.565 0.562 -0.015 0.029  -0.081 314 VAL BBB C   
6021  O O   . VAL B 314 ? 0.430 0.545 0.544 -0.015 0.029  -0.086 314 VAL BBB O   
6022  C CB  . VAL B 314 ? 0.433 0.536 0.533 -0.016 0.029  -0.071 314 VAL BBB CB  
6023  C CG1 . VAL B 314 ? 0.406 0.504 0.506 -0.015 0.031  -0.065 314 VAL BBB CG1 
6024  C CG2 . VAL B 314 ? 0.424 0.532 0.527 -0.016 0.029  -0.074 314 VAL BBB CG2 
6025  N N   . SER B 315 ? 0.471 0.582 0.569 -0.014 0.026  -0.080 315 SER BBB N   
6026  C CA  . SER B 315 ? 0.475 0.592 0.570 -0.013 0.024  -0.085 315 SER BBB CA  
6027  C C   . SER B 315 ? 0.472 0.591 0.560 -0.012 0.023  -0.085 315 SER BBB C   
6028  O O   . SER B 315 ? 0.451 0.567 0.538 -0.013 0.024  -0.081 315 SER BBB O   
6029  C CB  . SER B 315 ? 0.473 0.590 0.562 -0.012 0.023  -0.084 315 SER BBB CB  
6030  O OG  . SER B 315 ? 0.509 0.622 0.586 -0.012 0.022  -0.079 315 SER BBB OG  
6031  N N   . ASP B 316 ? 0.500 0.624 0.584 -0.010 0.021  -0.089 316 ASP BBB N   
6032  C CA  . ASP B 316 ? 0.549 0.674 0.625 -0.009 0.021  -0.090 316 ASP BBB CA  
6033  C C   . ASP B 316 ? 0.574 0.695 0.640 -0.010 0.021  -0.083 316 ASP BBB C   
6034  O O   . ASP B 316 ? 0.510 0.630 0.572 -0.010 0.021  -0.082 316 ASP BBB O   
6035  C CB  . ASP B 316 ? 0.543 0.674 0.616 -0.006 0.019  -0.096 316 ASP BBB CB  
6036  C CG  . ASP B 316 ? 0.515 0.652 0.600 -0.006 0.018  -0.103 316 ASP BBB CG  
6037  O OD1 . ASP B 316 ? 0.477 0.616 0.571 -0.007 0.020  -0.106 316 ASP BBB OD1 
6038  O OD2 . ASP B 316 ? 0.495 0.634 0.579 -0.004 0.016  -0.106 316 ASP BBB OD2 
6039  N N   . SER B 317 ? 0.607 0.725 0.669 -0.010 0.020  -0.080 317 SER BBB N   
6040  C CA  . SER B 317 ? 0.603 0.715 0.654 -0.010 0.020  -0.074 317 SER BBB CA  
6041  C C   . SER B 317 ? 0.554 0.663 0.609 -0.013 0.022  -0.069 317 SER BBB C   
6042  O O   . SER B 317 ? 0.479 0.584 0.526 -0.013 0.022  -0.065 317 SER BBB O   
6043  C CB  . SER B 317 ? 0.619 0.729 0.665 -0.009 0.019  -0.072 317 SER BBB CB  
6044  O OG  . SER B 317 ? 0.657 0.766 0.711 -0.011 0.019  -0.072 317 SER BBB OG  
6045  N N   . GLY B 318 ? 0.523 0.632 0.588 -0.014 0.023  -0.071 318 GLY BBB N   
6046  C CA  . GLY B 318 ? 0.498 0.604 0.566 -0.015 0.024  -0.067 318 GLY BBB CA  
6047  C C   . GLY B 318 ? 0.467 0.569 0.537 -0.015 0.024  -0.063 318 GLY BBB C   
6048  O O   . GLY B 318 ? 0.504 0.603 0.576 -0.015 0.025  -0.060 318 GLY BBB O   
6049  N N   . LYS B 319 ? 0.408 0.510 0.477 -0.014 0.023  -0.064 319 LYS BBB N   
6050  C CA  . LYS B 319 ? 0.413 0.512 0.483 -0.015 0.024  -0.062 319 LYS BBB CA  
6051  C C   . LYS B 319 ? 0.422 0.520 0.503 -0.015 0.026  -0.063 319 LYS BBB C   
6052  O O   . LYS B 319 ? 0.454 0.556 0.542 -0.015 0.027  -0.069 319 LYS BBB O   
6053  C CB  . LYS B 319 ? 0.417 0.516 0.481 -0.014 0.022  -0.062 319 LYS BBB CB  
6054  C CG  . LYS B 319 ? 0.429 0.527 0.483 -0.014 0.021  -0.059 319 LYS BBB CG  
6055  C CD  . LYS B 319 ? 0.394 0.491 0.443 -0.013 0.020  -0.058 319 LYS BBB CD  
6056  C CE  . LYS B 319 ? 0.390 0.484 0.428 -0.013 0.019  -0.055 319 LYS BBB CE  
6057  N NZ  . LYS B 319 ? 0.393 0.487 0.428 -0.012 0.018  -0.054 319 LYS BBB NZ  
6058  N N   . ILE B 320 ? 0.379 0.472 0.462 -0.015 0.028  -0.060 320 ILE BBB N   
6059  C CA  . ILE B 320 ? 0.361 0.452 0.453 -0.016 0.031  -0.060 320 ILE BBB CA  
6060  C C   . ILE B 320 ? 0.354 0.446 0.451 -0.016 0.031  -0.065 320 ILE BBB C   
6061  O O   . ILE B 320 ? 0.353 0.445 0.445 -0.016 0.030  -0.064 320 ILE BBB O   
6062  C CB  . ILE B 320 ? 0.368 0.453 0.459 -0.015 0.032  -0.055 320 ILE BBB CB  
6063  C CG1 . ILE B 320 ? 0.371 0.455 0.457 -0.015 0.031  -0.051 320 ILE BBB CG1 
6064  C CG2 . ILE B 320 ? 0.363 0.444 0.463 -0.015 0.036  -0.055 320 ILE BBB CG2 
6065  C CD1 . ILE B 320 ? 0.380 0.459 0.464 -0.013 0.032  -0.045 320 ILE BBB CD1 
6066  N N   . ILE B 321 ? 0.334 0.428 0.441 -0.016 0.033  -0.070 321 ILE BBB N   
6067  C CA  . ILE B 321 ? 0.345 0.442 0.460 -0.017 0.034  -0.075 321 ILE BBB CA  
6068  C C   . ILE B 321 ? 0.328 0.418 0.447 -0.018 0.038  -0.072 321 ILE BBB C   
6069  O O   . ILE B 321 ? 0.313 0.399 0.437 -0.018 0.041  -0.069 321 ILE BBB O   
6070  C CB  . ILE B 321 ? 0.361 0.463 0.486 -0.017 0.035  -0.082 321 ILE BBB CB  
6071  C CG1 . ILE B 321 ? 0.372 0.480 0.491 -0.016 0.031  -0.086 321 ILE BBB CG1 
6072  C CG2 . ILE B 321 ? 0.352 0.455 0.487 -0.018 0.037  -0.088 321 ILE BBB CG2 
6073  C CD1 . ILE B 321 ? 0.374 0.487 0.503 -0.016 0.032  -0.092 321 ILE BBB CD1 
6074  N N   . ALA B 322 ? 0.323 0.411 0.438 -0.018 0.038  -0.070 322 ALA BBB N   
6075  C CA  . ALA B 322 ? 0.333 0.415 0.451 -0.018 0.041  -0.067 322 ALA BBB CA  
6076  C C   . ALA B 322 ? 0.337 0.421 0.454 -0.019 0.040  -0.069 322 ALA BBB C   
6077  O O   . ALA B 322 ? 0.302 0.383 0.411 -0.018 0.039  -0.064 322 ALA BBB O   
6078  C CB  . ALA B 322 ? 0.326 0.402 0.435 -0.017 0.041  -0.059 322 ALA BBB CB  
6079  N N   . PRO B 323 ? 0.365 0.455 0.489 -0.019 0.040  -0.077 323 PRO BBB N   
6080  C CA  . PRO B 323 ? 0.373 0.466 0.497 -0.019 0.038  -0.079 323 PRO BBB CA  
6081  C C   . PRO B 323 ? 0.357 0.444 0.482 -0.020 0.042  -0.076 323 PRO BBB C   
6082  O O   . PRO B 323 ? 0.345 0.432 0.465 -0.020 0.040  -0.076 323 PRO BBB O   
6083  C CB  . PRO B 323 ? 0.376 0.476 0.510 -0.019 0.038  -0.089 323 PRO BBB CB  
6084  C CG  . PRO B 323 ? 0.372 0.471 0.515 -0.020 0.042  -0.091 323 PRO BBB CG  
6085  C CD  . PRO B 323 ? 0.370 0.464 0.505 -0.019 0.041  -0.083 323 PRO BBB CD  
6086  N N   . LYS B 324 ? 0.380 0.460 0.510 -0.021 0.047  -0.073 324 LYS BBB N   
6087  C CA  . LYS B 324 ? 0.412 0.484 0.542 -0.021 0.051  -0.069 324 LYS BBB CA  
6088  C C   . LYS B 324 ? 0.357 0.422 0.480 -0.020 0.052  -0.060 324 LYS BBB C   
6089  O O   . LYS B 324 ? 0.329 0.387 0.454 -0.021 0.057  -0.057 324 LYS BBB O   
6090  C CB  . LYS B 324 ? 0.471 0.541 0.616 -0.023 0.057  -0.074 324 LYS BBB CB  
6091  C CG  . LYS B 324 ? 0.527 0.604 0.681 -0.024 0.057  -0.083 324 LYS BBB CG  
6092  C CD  . LYS B 324 ? 0.585 0.663 0.735 -0.024 0.056  -0.083 324 LYS BBB CD  
6093  C CE  . LYS B 324 ? 0.633 0.714 0.797 -0.026 0.059  -0.091 324 LYS BBB CE  
6094  N NZ  . LYS B 324 ? 0.661 0.740 0.821 -0.026 0.059  -0.089 324 LYS BBB NZ  
6095  N N   . ASP B 325 ? 0.359 0.426 0.473 -0.019 0.048  -0.057 325 ASP BBB N   
6096  C CA  . ASP B 325 ? 0.346 0.408 0.453 -0.018 0.048  -0.050 325 ASP BBB CA  
6097  C C   . ASP B 325 ? 0.364 0.423 0.477 -0.017 0.051  -0.049 325 ASP BBB C   
6098  O O   . ASP B 325 ? 0.439 0.496 0.546 -0.016 0.050  -0.045 325 ASP BBB O   
6099  C CB  . ASP B 325 ? 0.332 0.387 0.433 -0.017 0.050  -0.044 325 ASP BBB CB  
6100  C CG  . ASP B 325 ? 0.333 0.391 0.429 -0.018 0.047  -0.045 325 ASP BBB CG  
6101  O OD1 . ASP B 325 ? 0.355 0.419 0.448 -0.018 0.043  -0.048 325 ASP BBB OD1 
6102  O OD2 . ASP B 325 ? 0.330 0.384 0.425 -0.018 0.049  -0.042 325 ASP BBB OD2 
6103  N N   . ALA B 326 ? 0.364 0.422 0.487 -0.018 0.055  -0.054 326 ALA BBB N   
6104  C CA  . ALA B 326 ? 0.377 0.432 0.507 -0.018 0.059  -0.054 326 ALA BBB CA  
6105  C C   . ALA B 326 ? 0.374 0.436 0.506 -0.018 0.056  -0.058 326 ALA BBB C   
6106  O O   . ALA B 326 ? 0.342 0.411 0.479 -0.019 0.054  -0.065 326 ALA BBB O   
6107  C CB  . ALA B 326 ? 0.369 0.420 0.511 -0.019 0.065  -0.057 326 ALA BBB CB  
6108  N N   . THR B 327 ? 0.387 0.447 0.515 -0.016 0.054  -0.055 327 THR BBB N   
6109  C CA  . THR B 327 ? 0.372 0.438 0.503 -0.016 0.052  -0.059 327 THR BBB CA  
6110  C C   . THR B 327 ? 0.374 0.440 0.518 -0.017 0.056  -0.064 327 THR BBB C   
6111  O O   . THR B 327 ? 0.373 0.434 0.523 -0.018 0.061  -0.064 327 THR BBB O   
6112  C CB  . THR B 327 ? 0.396 0.461 0.520 -0.015 0.050  -0.054 327 THR BBB CB  
6113  O OG1 . THR B 327 ? 0.377 0.435 0.504 -0.013 0.054  -0.050 327 THR BBB OG1 
6114  C CG2 . THR B 327 ? 0.399 0.464 0.511 -0.014 0.046  -0.049 327 THR BBB CG2 
6115  N N   . SER B 328 ? 0.409 0.480 0.557 -0.017 0.055  -0.067 328 SER BBB N   
6116  C CA  . SER B 328 ? 0.424 0.495 0.584 -0.018 0.059  -0.072 328 SER BBB CA  
6117  C C   . SER B 328 ? 0.424 0.486 0.584 -0.016 0.063  -0.067 328 SER BBB C   
6118  O O   . SER B 328 ? 0.473 0.532 0.644 -0.017 0.068  -0.070 328 SER BBB O   
6119  C CB  . SER B 328 ? 0.405 0.483 0.565 -0.018 0.055  -0.076 328 SER BBB CB  
6120  O OG  . SER B 328 ? 0.411 0.489 0.562 -0.017 0.052  -0.072 328 SER BBB OG  
6121  N N   . VAL B 329 ? 0.397 0.454 0.548 -0.014 0.062  -0.059 329 VAL BBB N   
6122  C CA  . VAL B 329 ? 0.404 0.451 0.553 -0.012 0.066  -0.053 329 VAL BBB CA  
6123  C C   . VAL B 329 ? 0.401 0.442 0.547 -0.011 0.069  -0.049 329 VAL BBB C   
6124  O O   . VAL B 329 ? 0.431 0.472 0.567 -0.011 0.066  -0.045 329 VAL BBB O   
6125  C CB  . VAL B 329 ? 0.385 0.433 0.526 -0.009 0.062  -0.049 329 VAL BBB CB  
6126  C CG1 . VAL B 329 ? 0.384 0.423 0.523 -0.006 0.066  -0.042 329 VAL BBB CG1 
6127  C CG2 . VAL B 329 ? 0.379 0.433 0.525 -0.010 0.060  -0.053 329 VAL BBB CG2 
6128  N N   . PRO B 330 ? 0.409 0.442 0.562 -0.012 0.076  -0.049 330 PRO BBB N   
6129  C CA  . PRO B 330 ? 0.419 0.447 0.570 -0.012 0.079  -0.046 330 PRO BBB CA  
6130  C C   . PRO B 330 ? 0.409 0.429 0.549 -0.009 0.079  -0.038 330 PRO BBB C   
6131  O O   . PRO B 330 ? 0.391 0.408 0.529 -0.010 0.081  -0.036 330 PRO BBB O   
6132  C CB  . PRO B 330 ? 0.433 0.455 0.597 -0.013 0.087  -0.049 330 PRO BBB CB  
6133  C CG  . PRO B 330 ? 0.443 0.464 0.612 -0.012 0.088  -0.050 330 PRO BBB CG  
6134  C CD  . PRO B 330 ? 0.416 0.446 0.579 -0.011 0.081  -0.051 330 PRO BBB CD  
6135  N N   . SER B 331 ? 0.382 0.401 0.515 -0.006 0.077  -0.033 331 SER BBB N   
6136  C CA  . SER B 331 ? 0.370 0.383 0.491 -0.002 0.076  -0.025 331 SER BBB CA  
6137  C C   . SER B 331 ? 0.360 0.381 0.472 -0.002 0.069  -0.025 331 SER BBB C   
6138  O O   . SER B 331 ? 0.349 0.368 0.452 0.001  0.067  -0.019 331 SER BBB O   
6139  C CB  . SER B 331 ? 0.386 0.394 0.505 0.002  0.077  -0.021 331 SER BBB CB  
6140  O OG  . SER B 331 ? 0.365 0.380 0.486 0.002  0.073  -0.024 331 SER BBB OG  
6141  N N   . ILE B 332 ? 0.337 0.367 0.453 -0.005 0.065  -0.030 332 ILE BBB N   
6142  C CA  . ILE B 332 ? 0.318 0.355 0.426 -0.005 0.058  -0.030 332 ILE BBB CA  
6143  C C   . ILE B 332 ? 0.304 0.346 0.412 -0.009 0.056  -0.034 332 ILE BBB C   
6144  O O   . ILE B 332 ? 0.293 0.339 0.409 -0.011 0.057  -0.040 332 ILE BBB O   
6145  C CB  . ILE B 332 ? 0.314 0.357 0.423 -0.005 0.055  -0.033 332 ILE BBB CB  
6146  C CG1 . ILE B 332 ? 0.322 0.361 0.430 -0.002 0.056  -0.029 332 ILE BBB CG1 
6147  C CG2 . ILE B 332 ? 0.303 0.353 0.405 -0.006 0.049  -0.034 332 ILE BBB CG2 
6148  C CD1 . ILE B 332 ? 0.329 0.373 0.438 -0.001 0.053  -0.031 332 ILE BBB CD1 
6149  N N   . PHE B 333 ? 0.299 0.341 0.399 -0.008 0.054  -0.031 333 PHE BBB N   
6150  C CA  . PHE B 333 ? 0.305 0.351 0.403 -0.010 0.052  -0.033 333 PHE BBB CA  
6151  C C   . PHE B 333 ? 0.307 0.359 0.397 -0.011 0.046  -0.033 333 PHE BBB C   
6152  O O   . PHE B 333 ? 0.289 0.341 0.375 -0.009 0.044  -0.030 333 PHE BBB O   
6153  C CB  . PHE B 333 ? 0.300 0.339 0.394 -0.010 0.055  -0.029 333 PHE BBB CB  
6154  C CG  . PHE B 333 ? 0.300 0.333 0.403 -0.010 0.061  -0.030 333 PHE BBB CG  
6155  C CD1 . PHE B 333 ? 0.304 0.329 0.407 -0.008 0.065  -0.025 333 PHE BBB CD1 
6156  C CD2 . PHE B 333 ? 0.296 0.330 0.407 -0.013 0.064  -0.035 333 PHE BBB CD2 
6157  C CE1 . PHE B 333 ? 0.312 0.331 0.423 -0.008 0.072  -0.026 333 PHE BBB CE1 
6158  C CE2 . PHE B 333 ? 0.300 0.329 0.420 -0.013 0.070  -0.036 333 PHE BBB CE2 
6159  C CZ  . PHE B 333 ? 0.298 0.319 0.418 -0.011 0.075  -0.032 333 PHE BBB CZ  
6160  N N   . ALA B 334 ? 0.327 0.383 0.416 -0.012 0.044  -0.035 334 ALA BBB N   
6161  C CA  . ALA B 334 ? 0.306 0.367 0.387 -0.013 0.039  -0.035 334 ALA BBB CA  
6162  C C   . ALA B 334 ? 0.307 0.369 0.384 -0.014 0.038  -0.036 334 ALA BBB C   
6163  O O   . ALA B 334 ? 0.313 0.374 0.395 -0.015 0.040  -0.039 334 ALA BBB O   
6164  C CB  . ALA B 334 ? 0.310 0.377 0.394 -0.014 0.037  -0.040 334 ALA BBB CB  
6165  N N   . VAL B 335 ? 0.287 0.350 0.355 -0.013 0.035  -0.033 335 VAL BBB N   
6166  C CA  . VAL B 335 ? 0.287 0.351 0.350 -0.014 0.033  -0.033 335 VAL BBB CA  
6167  C C   . VAL B 335 ? 0.271 0.339 0.327 -0.014 0.029  -0.033 335 VAL BBB C   
6168  O O   . VAL B 335 ? 0.258 0.327 0.313 -0.014 0.028  -0.032 335 VAL BBB O   
6169  C CB  . VAL B 335 ? 0.302 0.361 0.362 -0.014 0.034  -0.029 335 VAL BBB CB  
6170  C CG1 . VAL B 335 ? 0.326 0.381 0.394 -0.014 0.039  -0.029 335 VAL BBB CG1 
6171  C CG2 . VAL B 335 ? 0.305 0.361 0.358 -0.012 0.033  -0.024 335 VAL BBB CG2 
6172  N N   . GLY B 336 ? 0.277 0.346 0.328 -0.015 0.027  -0.033 336 GLY BBB N   
6173  C CA  . GLY B 336 ? 0.283 0.355 0.327 -0.015 0.025  -0.032 336 GLY BBB CA  
6174  C C   . GLY B 336 ? 0.287 0.362 0.330 -0.015 0.023  -0.036 336 GLY BBB C   
6175  O O   . GLY B 336 ? 0.281 0.359 0.330 -0.015 0.024  -0.040 336 GLY BBB O   
6176  N N   . ASP B 337 ? 0.313 0.390 0.351 -0.015 0.022  -0.035 337 ASP BBB N   
6177  C CA  . ASP B 337 ? 0.321 0.402 0.356 -0.015 0.021  -0.038 337 ASP BBB CA  
6178  C C   . ASP B 337 ? 0.328 0.410 0.369 -0.015 0.021  -0.041 337 ASP BBB C   
6179  O O   . ASP B 337 ? 0.336 0.422 0.376 -0.015 0.021  -0.045 337 ASP BBB O   
6180  C CB  . ASP B 337 ? 0.324 0.403 0.351 -0.016 0.020  -0.035 337 ASP BBB CB  
6181  C CG  . ASP B 337 ? 0.341 0.418 0.360 -0.016 0.019  -0.033 337 ASP BBB CG  
6182  O OD1 . ASP B 337 ? 0.369 0.446 0.389 -0.015 0.019  -0.033 337 ASP BBB OD1 
6183  O OD2 . ASP B 337 ? 0.402 0.479 0.416 -0.016 0.019  -0.031 337 ASP BBB OD2 
6184  N N   . ILE B 338 ? 0.320 0.402 0.367 -0.015 0.023  -0.040 338 ILE BBB N   
6185  C CA  . ILE B 338 ? 0.326 0.410 0.379 -0.015 0.024  -0.043 338 ILE BBB CA  
6186  C C   . ILE B 338 ? 0.343 0.428 0.403 -0.015 0.025  -0.048 338 ILE BBB C   
6187  O O   . ILE B 338 ? 0.401 0.489 0.467 -0.015 0.025  -0.051 338 ILE BBB O   
6188  C CB  . ILE B 338 ? 0.321 0.403 0.378 -0.015 0.025  -0.041 338 ILE BBB CB  
6189  C CG1 . ILE B 338 ? 0.293 0.371 0.354 -0.014 0.027  -0.039 338 ILE BBB CG1 
6190  C CG2 . ILE B 338 ? 0.331 0.413 0.382 -0.015 0.024  -0.038 338 ILE BBB CG2 
6191  C CD1 . ILE B 338 ? 0.291 0.365 0.353 -0.013 0.028  -0.036 338 ILE BBB CD1 
6192  N N   . VAL B 339 ? 0.339 0.423 0.401 -0.015 0.025  -0.048 339 VAL BBB N   
6193  C CA  . VAL B 339 ? 0.339 0.425 0.409 -0.015 0.026  -0.053 339 VAL BBB CA  
6194  C C   . VAL B 339 ? 0.348 0.439 0.416 -0.015 0.024  -0.058 339 VAL BBB C   
6195  O O   . VAL B 339 ? 0.339 0.431 0.400 -0.014 0.022  -0.057 339 VAL BBB O   
6196  C CB  . VAL B 339 ? 0.319 0.401 0.393 -0.016 0.028  -0.052 339 VAL BBB CB  
6197  C CG1 . VAL B 339 ? 0.306 0.391 0.390 -0.016 0.030  -0.057 339 VAL BBB CG1 
6198  C CG2 . VAL B 339 ? 0.312 0.389 0.387 -0.016 0.031  -0.047 339 VAL BBB CG2 
6199  N N   . GLU B 340 ? 0.358 0.454 0.433 -0.014 0.024  -0.063 340 GLU BBB N   
6200  C CA  . GLU B 340 ? 0.384 0.485 0.457 -0.013 0.022  -0.069 340 GLU BBB CA  
6201  C C   . GLU B 340 ? 0.367 0.469 0.443 -0.013 0.022  -0.071 340 GLU BBB C   
6202  O O   . GLU B 340 ? 0.342 0.443 0.427 -0.014 0.024  -0.072 340 GLU BBB O   
6203  C CB  . GLU B 340 ? 0.429 0.535 0.510 -0.013 0.023  -0.074 340 GLU BBB CB  
6204  C CG  . GLU B 340 ? 0.510 0.622 0.592 -0.011 0.020  -0.081 340 GLU BBB CG  
6205  C CD  . GLU B 340 ? 0.586 0.703 0.667 -0.010 0.019  -0.085 340 GLU BBB CD  
6206  O OE1 . GLU B 340 ? 0.637 0.758 0.727 -0.010 0.020  -0.091 340 GLU BBB OE1 
6207  O OE2 . GLU B 340 ? 0.689 0.804 0.760 -0.009 0.018  -0.082 340 GLU BBB OE2 
6208  N N   . GLY B 341 ? 0.357 0.462 0.426 -0.011 0.019  -0.073 341 GLY BBB N   
6209  C CA  . GLY B 341 ? 0.341 0.449 0.412 -0.010 0.018  -0.077 341 GLY BBB CA  
6210  C C   . GLY B 341 ? 0.330 0.434 0.398 -0.010 0.018  -0.073 341 GLY BBB C   
6211  O O   . GLY B 341 ? 0.326 0.431 0.398 -0.010 0.018  -0.077 341 GLY BBB O   
6212  N N   . ARG B 342 ? 0.348 0.446 0.408 -0.011 0.018  -0.066 342 ARG BBB N   
6213  C CA  . ARG B 342 ? 0.321 0.416 0.377 -0.012 0.018  -0.062 342 ARG BBB CA  
6214  C C   . ARG B 342 ? 0.319 0.411 0.362 -0.011 0.017  -0.058 342 ARG BBB C   
6215  O O   . ARG B 342 ? 0.306 0.398 0.345 -0.011 0.017  -0.056 342 ARG BBB O   
6216  C CB  . ARG B 342 ? 0.327 0.417 0.388 -0.014 0.021  -0.059 342 ARG BBB CB  
6217  C CG  . ARG B 342 ? 0.325 0.411 0.383 -0.014 0.023  -0.054 342 ARG BBB CG  
6218  C CD  . ARG B 342 ? 0.316 0.397 0.379 -0.015 0.026  -0.050 342 ARG BBB CD  
6219  N NE  . ARG B 342 ? 0.305 0.386 0.378 -0.016 0.028  -0.054 342 ARG BBB NE  
6220  C CZ  . ARG B 342 ? 0.302 0.378 0.380 -0.017 0.032  -0.051 342 ARG BBB CZ  
6221  N NH1 . ARG B 342 ? 0.295 0.367 0.369 -0.017 0.033  -0.045 342 ARG BBB NH1 
6222  N NH2 . ARG B 342 ? 0.316 0.393 0.406 -0.017 0.035  -0.055 342 ARG BBB NH2 
6223  N N   . PRO B 343 ? 0.317 0.408 0.354 -0.010 0.015  -0.056 343 PRO BBB N   
6224  C CA  . PRO B 343 ? 0.331 0.419 0.357 -0.010 0.014  -0.052 343 PRO BBB CA  
6225  C C   . PRO B 343 ? 0.342 0.427 0.367 -0.011 0.016  -0.046 343 PRO BBB C   
6226  O O   . PRO B 343 ? 0.314 0.396 0.343 -0.013 0.017  -0.044 343 PRO BBB O   
6227  C CB  . PRO B 343 ? 0.333 0.421 0.356 -0.009 0.013  -0.051 343 PRO BBB CB  
6228  C CG  . PRO B 343 ? 0.328 0.419 0.360 -0.008 0.013  -0.057 343 PRO BBB CG  
6229  C CD  . PRO B 343 ? 0.323 0.415 0.365 -0.010 0.015  -0.058 343 PRO BBB CD  
6230  N N   . GLU B 344 ? 0.349 0.432 0.366 -0.011 0.015  -0.044 344 GLU BBB N   
6231  C CA  . GLU B 344 ? 0.354 0.434 0.369 -0.013 0.016  -0.039 344 GLU BBB CA  
6232  C C   . GLU B 344 ? 0.332 0.409 0.341 -0.013 0.016  -0.035 344 GLU BBB C   
6233  O O   . GLU B 344 ? 0.355 0.430 0.356 -0.013 0.016  -0.034 344 GLU BBB O   
6234  C CB  . GLU B 344 ? 0.396 0.477 0.407 -0.013 0.017  -0.039 344 GLU BBB CB  
6235  C CG  . GLU B 344 ? 0.441 0.525 0.458 -0.013 0.017  -0.043 344 GLU BBB CG  
6236  C CD  . GLU B 344 ? 0.524 0.610 0.537 -0.012 0.018  -0.044 344 GLU BBB CD  
6237  O OE1 . GLU B 344 ? 0.582 0.665 0.589 -0.013 0.018  -0.041 344 GLU BBB OE1 
6238  O OE2 . GLU B 344 ? 0.575 0.664 0.592 -0.012 0.018  -0.047 344 GLU BBB OE2 
6239  N N   . LEU B 345 ? 0.291 0.367 0.304 -0.014 0.016  -0.034 345 LEU BBB N   
6240  C CA  . LEU B 345 ? 0.268 0.340 0.275 -0.014 0.016  -0.031 345 LEU BBB CA  
6241  C C   . LEU B 345 ? 0.243 0.313 0.254 -0.015 0.017  -0.028 345 LEU BBB C   
6242  O O   . LEU B 345 ? 0.240 0.311 0.258 -0.015 0.019  -0.029 345 LEU BBB O   
6243  C CB  . LEU B 345 ? 0.264 0.338 0.271 -0.013 0.015  -0.033 345 LEU BBB CB  
6244  C CG  . LEU B 345 ? 0.260 0.335 0.261 -0.011 0.013  -0.036 345 LEU BBB CG  
6245  C CD1 . LEU B 345 ? 0.262 0.340 0.266 -0.009 0.012  -0.039 345 LEU BBB CD1 
6246  C CD2 . LEU B 345 ? 0.266 0.339 0.258 -0.011 0.013  -0.033 345 LEU BBB CD2 
6247  N N   . THR B 346 ? 0.238 0.306 0.244 -0.015 0.017  -0.024 346 THR BBB N   
6248  C CA  . THR B 346 ? 0.241 0.307 0.249 -0.016 0.018  -0.021 346 THR BBB CA  
6249  C C   . THR B 346 ? 0.241 0.305 0.253 -0.015 0.019  -0.021 346 THR BBB C   
6250  O O   . THR B 346 ? 0.223 0.286 0.240 -0.015 0.021  -0.020 346 THR BBB O   
6251  C CB  . THR B 346 ? 0.270 0.334 0.271 -0.016 0.017  -0.018 346 THR BBB CB  
6252  O OG1 . THR B 346 ? 0.295 0.360 0.296 -0.016 0.017  -0.018 346 THR BBB OG1 
6253  C CG2 . THR B 346 ? 0.273 0.335 0.275 -0.016 0.018  -0.015 346 THR BBB CG2 
6254  N N   . PRO B 347 ? 0.242 0.306 0.252 -0.015 0.019  -0.022 347 PRO BBB N   
6255  C CA  . PRO B 347 ? 0.251 0.312 0.266 -0.016 0.020  -0.022 347 PRO BBB CA  
6256  C C   . PRO B 347 ? 0.247 0.310 0.271 -0.016 0.022  -0.025 347 PRO BBB C   
6257  O O   . PRO B 347 ? 0.262 0.322 0.290 -0.016 0.025  -0.025 347 PRO BBB O   
6258  C CB  . PRO B 347 ? 0.260 0.322 0.272 -0.015 0.019  -0.024 347 PRO BBB CB  
6259  C CG  . PRO B 347 ? 0.258 0.321 0.262 -0.015 0.017  -0.021 347 PRO BBB CG  
6260  C CD  . PRO B 347 ? 0.250 0.314 0.254 -0.015 0.017  -0.022 347 PRO BBB CD  
6261  N N   . VAL B 348 ? 0.256 0.323 0.282 -0.015 0.021  -0.029 348 VAL BBB N   
6262  C CA  . VAL B 348 ? 0.247 0.315 0.282 -0.016 0.023  -0.033 348 VAL BBB CA  
6263  C C   . VAL B 348 ? 0.252 0.318 0.290 -0.016 0.025  -0.031 348 VAL BBB C   
6264  O O   . VAL B 348 ? 0.270 0.334 0.314 -0.016 0.028  -0.031 348 VAL BBB O   
6265  C CB  . VAL B 348 ? 0.260 0.333 0.295 -0.015 0.021  -0.038 348 VAL BBB CB  
6266  C CG1 . VAL B 348 ? 0.249 0.324 0.293 -0.015 0.022  -0.042 348 VAL BBB CG1 
6267  C CG2 . VAL B 348 ? 0.264 0.339 0.295 -0.014 0.019  -0.040 348 VAL BBB CG2 
6268  N N   . ALA B 349 ? 0.245 0.311 0.278 -0.015 0.024  -0.028 349 ALA BBB N   
6269  C CA  . ALA B 349 ? 0.245 0.309 0.280 -0.015 0.025  -0.025 349 ALA BBB CA  
6270  C C   . ALA B 349 ? 0.240 0.299 0.275 -0.014 0.027  -0.021 349 ALA BBB C   
6271  O O   . ALA B 349 ? 0.244 0.300 0.284 -0.014 0.030  -0.021 349 ALA BBB O   
6272  C CB  . ALA B 349 ? 0.243 0.308 0.271 -0.015 0.023  -0.023 349 ALA BBB CB  
6273  N N   . VAL B 350 ? 0.243 0.300 0.272 -0.014 0.026  -0.019 350 VAL BBB N   
6274  C CA  . VAL B 350 ? 0.246 0.298 0.273 -0.014 0.028  -0.015 350 VAL BBB CA  
6275  C C   . VAL B 350 ? 0.259 0.309 0.293 -0.014 0.032  -0.016 350 VAL BBB C   
6276  O O   . VAL B 350 ? 0.263 0.309 0.300 -0.013 0.035  -0.014 350 VAL BBB O   
6277  C CB  . VAL B 350 ? 0.239 0.291 0.259 -0.014 0.026  -0.013 350 VAL BBB CB  
6278  C CG1 . VAL B 350 ? 0.248 0.296 0.267 -0.013 0.028  -0.009 350 VAL BBB CG1 
6279  C CG2 . VAL B 350 ? 0.236 0.289 0.250 -0.013 0.024  -0.011 350 VAL BBB CG2 
6280  N N   . LYS B 351 ? 0.273 0.325 0.309 -0.015 0.032  -0.020 351 LYS BBB N   
6281  C CA  . LYS B 351 ? 0.290 0.340 0.334 -0.016 0.035  -0.022 351 LYS BBB CA  
6282  C C   . LYS B 351 ? 0.309 0.358 0.361 -0.016 0.038  -0.025 351 LYS BBB C   
6283  O O   . LYS B 351 ? 0.332 0.377 0.389 -0.016 0.042  -0.024 351 LYS BBB O   
6284  C CB  . LYS B 351 ? 0.286 0.339 0.331 -0.017 0.034  -0.026 351 LYS BBB CB  
6285  C CG  . LYS B 351 ? 0.300 0.352 0.354 -0.018 0.038  -0.029 351 LYS BBB CG  
6286  C CD  . LYS B 351 ? 0.326 0.380 0.380 -0.019 0.037  -0.033 351 LYS BBB CD  
6287  C CE  . LYS B 351 ? 0.339 0.391 0.385 -0.018 0.035  -0.029 351 LYS BBB CE  
6288  N NZ  . LYS B 351 ? 0.341 0.388 0.387 -0.018 0.039  -0.025 351 LYS BBB NZ  
6289  N N   . ALA B 352 ? 0.324 0.377 0.378 -0.016 0.036  -0.027 352 ALA BBB N   
6290  C CA  . ALA B 352 ? 0.348 0.401 0.410 -0.016 0.039  -0.030 352 ALA BBB CA  
6291  C C   . ALA B 352 ? 0.343 0.390 0.403 -0.015 0.041  -0.025 352 ALA BBB C   
6292  O O   . ALA B 352 ? 0.349 0.393 0.416 -0.015 0.046  -0.025 352 ALA BBB O   
6293  C CB  . ALA B 352 ? 0.361 0.420 0.424 -0.016 0.036  -0.033 352 ALA BBB CB  
6294  N N   . GLY B 353 ? 0.322 0.369 0.374 -0.013 0.039  -0.020 353 GLY BBB N   
6295  C CA  . GLY B 353 ? 0.328 0.370 0.378 -0.011 0.041  -0.015 353 GLY BBB CA  
6296  C C   . GLY B 353 ? 0.320 0.355 0.370 -0.010 0.045  -0.012 353 GLY BBB C   
6297  O O   . GLY B 353 ? 0.299 0.329 0.351 -0.009 0.049  -0.010 353 GLY BBB O   
6298  N N   . ILE B 354 ? 0.331 0.366 0.378 -0.011 0.044  -0.012 354 ILE BBB N   
6299  C CA  . ILE B 354 ? 0.338 0.366 0.383 -0.011 0.049  -0.009 354 ILE BBB CA  
6300  C C   . ILE B 354 ? 0.333 0.359 0.390 -0.012 0.054  -0.012 354 ILE BBB C   
6301  O O   . ILE B 354 ? 0.356 0.375 0.414 -0.011 0.059  -0.009 354 ILE BBB O   
6302  C CB  . ILE B 354 ? 0.337 0.367 0.377 -0.011 0.046  -0.008 354 ILE BBB CB  
6303  C CG1 . ILE B 354 ? 0.348 0.380 0.379 -0.010 0.042  -0.005 354 ILE BBB CG1 
6304  C CG2 . ILE B 354 ? 0.348 0.371 0.389 -0.011 0.051  -0.006 354 ILE BBB CG2 
6305  C CD1 . ILE B 354 ? 0.324 0.358 0.350 -0.011 0.040  -0.004 354 ILE BBB CD1 
6306  N N   . LEU B 355 ? 0.306 0.338 0.369 -0.015 0.053  -0.018 355 LEU BBB N   
6307  C CA  . LEU B 355 ? 0.301 0.331 0.375 -0.016 0.058  -0.023 355 LEU BBB CA  
6308  C C   . LEU B 355 ? 0.312 0.339 0.392 -0.015 0.061  -0.023 355 LEU BBB C   
6309  O O   . LEU B 355 ? 0.310 0.331 0.396 -0.016 0.067  -0.023 355 LEU BBB O   
6310  C CB  . LEU B 355 ? 0.291 0.329 0.371 -0.018 0.055  -0.030 355 LEU BBB CB  
6311  C CG  . LEU B 355 ? 0.298 0.338 0.373 -0.019 0.052  -0.031 355 LEU BBB CG  
6312  C CD1 . LEU B 355 ? 0.299 0.346 0.381 -0.021 0.050  -0.039 355 LEU BBB CD1 
6313  C CD2 . LEU B 355 ? 0.286 0.320 0.361 -0.019 0.057  -0.028 355 LEU BBB CD2 
6314  N N   . LEU B 356 ? 0.312 0.342 0.389 -0.014 0.058  -0.023 356 LEU BBB N   
6315  C CA  . LEU B 356 ? 0.339 0.367 0.421 -0.013 0.060  -0.022 356 LEU BBB CA  
6316  C C   . LEU B 356 ? 0.347 0.366 0.425 -0.011 0.065  -0.016 356 LEU BBB C   
6317  O O   . LEU B 356 ? 0.347 0.359 0.431 -0.011 0.071  -0.016 356 LEU BBB O   
6318  C CB  . LEU B 356 ? 0.347 0.379 0.425 -0.012 0.055  -0.022 356 LEU BBB CB  
6319  C CG  . LEU B 356 ? 0.363 0.392 0.444 -0.011 0.057  -0.021 356 LEU BBB CG  
6320  C CD1 . LEU B 356 ? 0.374 0.404 0.467 -0.012 0.062  -0.026 356 LEU BBB CD1 
6321  C CD2 . LEU B 356 ? 0.363 0.398 0.440 -0.010 0.052  -0.021 356 LEU BBB CD2 
6322  N N   . ALA B 357 ? 0.355 0.372 0.422 -0.008 0.062  -0.010 357 ALA BBB N   
6323  C CA  . ALA B 357 ? 0.368 0.377 0.429 -0.005 0.065  -0.004 357 ALA BBB CA  
6324  C C   . ALA B 357 ? 0.381 0.382 0.446 -0.006 0.072  -0.004 357 ALA BBB C   
6325  O O   . ALA B 357 ? 0.372 0.365 0.439 -0.004 0.078  -0.001 357 ALA BBB O   
6326  C CB  . ALA B 357 ? 0.360 0.369 0.410 -0.003 0.061  0.000  357 ALA BBB CB  
6327  N N   . ARG B 358 ? 0.398 0.402 0.466 -0.009 0.072  -0.007 358 ARG BBB N   
6328  C CA  . ARG B 358 ? 0.451 0.448 0.524 -0.010 0.079  -0.007 358 ARG BBB CA  
6329  C C   . ARG B 358 ? 0.440 0.436 0.526 -0.012 0.085  -0.012 358 ARG BBB C   
6330  O O   . ARG B 358 ? 0.473 0.460 0.561 -0.011 0.092  -0.010 358 ARG BBB O   
6331  C CB  . ARG B 358 ? 0.485 0.487 0.559 -0.013 0.077  -0.010 358 ARG BBB CB  
6332  C CG  . ARG B 358 ? 0.507 0.508 0.569 -0.011 0.074  -0.005 358 ARG BBB CG  
6333  C CD  . ARG B 358 ? 0.516 0.522 0.578 -0.014 0.071  -0.009 358 ARG BBB CD  
6334  N NE  . ARG B 358 ? 0.520 0.527 0.572 -0.012 0.067  -0.004 358 ARG BBB NE  
6335  C CZ  . ARG B 358 ? 0.541 0.552 0.590 -0.013 0.063  -0.006 358 ARG BBB CZ  
6336  N NH1 . ARG B 358 ? 0.571 0.588 0.627 -0.016 0.063  -0.012 358 ARG BBB NH1 
6337  N NH2 . ARG B 358 ? 0.545 0.557 0.585 -0.012 0.060  -0.002 358 ARG BBB NH2 
6338  N N   . ARG B 359 ? 0.443 0.446 0.536 -0.014 0.082  -0.018 359 ARG BBB N   
6339  C CA  . ARG B 359 ? 0.443 0.445 0.549 -0.016 0.087  -0.023 359 ARG BBB CA  
6340  C C   . ARG B 359 ? 0.477 0.471 0.582 -0.013 0.091  -0.019 359 ARG BBB C   
6341  O O   . ARG B 359 ? 0.512 0.501 0.626 -0.014 0.099  -0.020 359 ARG BBB O   
6342  C CB  . ARG B 359 ? 0.403 0.416 0.516 -0.018 0.082  -0.031 359 ARG BBB CB  
6343  C CG  . ARG B 359 ? 0.369 0.389 0.484 -0.020 0.079  -0.036 359 ARG BBB CG  
6344  C CD  . ARG B 359 ? 0.346 0.375 0.470 -0.022 0.076  -0.044 359 ARG BBB CD  
6345  N NE  . ARG B 359 ? 0.327 0.361 0.448 -0.021 0.071  -0.044 359 ARG BBB NE  
6346  C CZ  . ARG B 359 ? 0.308 0.346 0.419 -0.020 0.065  -0.042 359 ARG BBB CZ  
6347  N NH1 . ARG B 359 ? 0.302 0.342 0.406 -0.020 0.062  -0.041 359 ARG BBB NH1 
6348  N NH2 . ARG B 359 ? 0.303 0.344 0.412 -0.019 0.061  -0.042 359 ARG BBB NH2 
6349  N N   . LEU B 360 ? 0.497 0.491 0.593 -0.010 0.087  -0.014 360 LEU BBB N   
6350  C CA  . LEU B 360 ? 0.479 0.468 0.574 -0.007 0.090  -0.010 360 LEU BBB CA  
6351  C C   . LEU B 360 ? 0.501 0.477 0.590 -0.004 0.096  -0.003 360 LEU BBB C   
6352  O O   . LEU B 360 ? 0.494 0.463 0.587 -0.002 0.103  -0.002 360 LEU BBB O   
6353  C CB  . LEU B 360 ? 0.488 0.481 0.574 -0.004 0.083  -0.007 360 LEU BBB CB  
6354  C CG  . LEU B 360 ? 0.493 0.496 0.584 -0.006 0.078  -0.013 360 LEU BBB CG  
6355  C CD1 . LEU B 360 ? 0.477 0.483 0.559 -0.003 0.071  -0.010 360 LEU BBB CD1 
6356  C CD2 . LEU B 360 ? 0.496 0.497 0.598 -0.007 0.082  -0.017 360 LEU BBB CD2 
6357  N N   . PHE B 361 ? 0.496 0.471 0.577 -0.003 0.096  0.000  361 PHE BBB N   
6358  C CA  . PHE B 361 ? 0.520 0.484 0.591 0.002  0.100  0.008  361 PHE BBB CA  
6359  C C   . PHE B 361 ? 0.552 0.511 0.623 0.000  0.105  0.009  361 PHE BBB C   
6360  O O   . PHE B 361 ? 0.574 0.523 0.638 0.004  0.110  0.015  361 PHE BBB O   
6361  C CB  . PHE B 361 ? 0.529 0.496 0.588 0.006  0.093  0.013  361 PHE BBB CB  
6362  C CG  . PHE B 361 ? 0.523 0.495 0.581 0.008  0.088  0.012  361 PHE BBB CG  
6363  C CD1 . PHE B 361 ? 0.535 0.500 0.595 0.010  0.093  0.014  361 PHE BBB CD1 
6364  C CD2 . PHE B 361 ? 0.523 0.504 0.578 0.007  0.080  0.010  361 PHE BBB CD2 
6365  C CE1 . PHE B 361 ? 0.539 0.507 0.598 0.013  0.089  0.014  361 PHE BBB CE1 
6366  C CE2 . PHE B 361 ? 0.519 0.504 0.574 0.009  0.077  0.010  361 PHE BBB CE2 
6367  C CZ  . PHE B 361 ? 0.529 0.508 0.586 0.012  0.081  0.012  361 PHE BBB CZ  
6368  N N   . ALA B 362 ? 0.548 0.513 0.626 -0.005 0.104  0.003  362 ALA BBB N   
6369  C CA  . ALA B 362 ? 0.533 0.494 0.611 -0.006 0.108  0.003  362 ALA BBB CA  
6370  C C   . ALA B 362 ? 0.540 0.504 0.633 -0.011 0.112  -0.005 362 ALA BBB C   
6371  O O   . ALA B 362 ? 0.543 0.507 0.638 -0.014 0.114  -0.007 362 ALA BBB O   
6372  C CB  . ALA B 362 ? 0.515 0.482 0.584 -0.006 0.101  0.004  362 ALA BBB CB  
6373  N N   . GLY B 363 ? 0.555 0.520 0.658 -0.013 0.114  -0.009 363 GLY BBB N   
6374  C CA  . GLY B 363 ? 0.572 0.538 0.691 -0.017 0.119  -0.017 363 GLY BBB CA  
6375  C C   . GLY B 363 ? 0.575 0.552 0.698 -0.021 0.114  -0.024 363 GLY BBB C   
6376  O O   . GLY B 363 ? 0.611 0.590 0.747 -0.024 0.119  -0.031 363 GLY BBB O   
6377  N N   . SER B 364 ? 0.556 0.542 0.672 -0.020 0.105  -0.024 364 SER BBB N   
6378  C CA  . SER B 364 ? 0.556 0.553 0.675 -0.022 0.099  -0.030 364 SER BBB CA  
6379  C C   . SER B 364 ? 0.549 0.554 0.679 -0.024 0.097  -0.038 364 SER BBB C   
6380  O O   . SER B 364 ? 0.539 0.542 0.671 -0.023 0.098  -0.037 364 SER BBB O   
6381  C CB  . SER B 364 ? 0.570 0.571 0.675 -0.020 0.090  -0.026 364 SER BBB CB  
6382  O OG  . SER B 364 ? 0.562 0.574 0.670 -0.022 0.084  -0.032 364 SER BBB OG  
6383  N N   . ASN B 365 ? 0.569 0.582 0.706 -0.027 0.094  -0.046 365 ASN BBB N   
6384  C CA  . ASN B 365 ? 0.644 0.666 0.790 -0.028 0.091  -0.054 365 ASN BBB CA  
6385  C C   . ASN B 365 ? 0.671 0.704 0.813 -0.028 0.083  -0.057 365 ASN BBB C   
6386  O O   . ASN B 365 ? 0.652 0.693 0.803 -0.029 0.080  -0.066 365 ASN BBB O   
6387  C CB  . ASN B 365 ? 0.712 0.734 0.874 -0.031 0.098  -0.062 365 ASN BBB CB  
6388  C CG  . ASN B 365 ? 0.810 0.833 0.979 -0.033 0.101  -0.067 365 ASN BBB CG  
6389  O OD1 . ASN B 365 ? 0.862 0.889 1.025 -0.033 0.096  -0.066 365 ASN BBB OD1 
6390  N ND2 . ASN B 365 ? 0.879 0.899 1.062 -0.035 0.108  -0.072 365 ASN BBB ND2 
6391  N N   . GLU B 366 ? 0.658 0.689 0.787 -0.027 0.079  -0.051 366 GLU BBB N   
6392  C CA  . GLU B 366 ? 0.616 0.656 0.740 -0.026 0.071  -0.053 366 GLU BBB CA  
6393  C C   . GLU B 366 ? 0.543 0.588 0.660 -0.025 0.065  -0.052 366 GLU BBB C   
6394  O O   . GLU B 366 ? 0.482 0.522 0.592 -0.023 0.065  -0.046 366 GLU BBB O   
6395  C CB  . GLU B 366 ? 0.672 0.708 0.786 -0.026 0.071  -0.048 366 GLU BBB CB  
6396  C CG  . GLU B 366 ? 0.731 0.764 0.853 -0.028 0.076  -0.051 366 GLU BBB CG  
6397  C CD  . GLU B 366 ? 0.799 0.836 0.919 -0.028 0.073  -0.053 366 GLU BBB CD  
6398  O OE1 . GLU B 366 ? 0.840 0.874 0.949 -0.027 0.072  -0.046 366 GLU BBB OE1 
6399  O OE2 . GLU B 366 ? 0.810 0.853 0.938 -0.030 0.073  -0.061 366 GLU BBB OE2 
6400  N N   . PHE B 367 ? 0.477 0.530 0.596 -0.025 0.060  -0.059 367 PHE BBB N   
6401  C CA  . PHE B 367 ? 0.456 0.515 0.569 -0.023 0.054  -0.059 367 PHE BBB CA  
6402  C C   . PHE B 367 ? 0.443 0.507 0.548 -0.023 0.049  -0.059 367 PHE BBB C   
6403  O O   . PHE B 367 ? 0.429 0.494 0.537 -0.023 0.049  -0.061 367 PHE BBB O   
6404  C CB  . PHE B 367 ? 0.439 0.504 0.562 -0.024 0.054  -0.066 367 PHE BBB CB  
6405  C CG  . PHE B 367 ? 0.436 0.497 0.566 -0.024 0.059  -0.065 367 PHE BBB CG  
6406  C CD1 . PHE B 367 ? 0.418 0.475 0.559 -0.026 0.066  -0.068 367 PHE BBB CD1 
6407  C CD2 . PHE B 367 ? 0.428 0.489 0.553 -0.023 0.057  -0.062 367 PHE BBB CD2 
6408  C CE1 . PHE B 367 ? 0.422 0.473 0.568 -0.026 0.070  -0.067 367 PHE BBB CE1 
6409  C CE2 . PHE B 367 ? 0.432 0.488 0.563 -0.023 0.061  -0.061 367 PHE BBB CE2 
6410  C CZ  . PHE B 367 ? 0.436 0.487 0.577 -0.025 0.068  -0.063 367 PHE BBB CZ  
6411  N N   . ILE B 368 ? 0.432 0.499 0.528 -0.021 0.043  -0.057 368 ILE BBB N   
6412  C CA  . ILE B 368 ? 0.407 0.478 0.496 -0.020 0.038  -0.058 368 ILE BBB CA  
6413  C C   . ILE B 368 ? 0.401 0.480 0.498 -0.020 0.037  -0.067 368 ILE BBB C   
6414  O O   . ILE B 368 ? 0.420 0.503 0.525 -0.020 0.038  -0.072 368 ILE BBB O   
6415  C CB  . ILE B 368 ? 0.394 0.467 0.472 -0.019 0.034  -0.054 368 ILE BBB CB  
6416  C CG1 . ILE B 368 ? 0.390 0.456 0.460 -0.019 0.035  -0.046 368 ILE BBB CG1 
6417  C CG2 . ILE B 368 ? 0.390 0.468 0.463 -0.017 0.029  -0.056 368 ILE BBB CG2 
6418  C CD1 . ILE B 368 ? 0.374 0.440 0.437 -0.018 0.032  -0.043 368 ILE BBB CD1 
6419  N N   . ASP B 369 ? 0.385 0.468 0.479 -0.019 0.034  -0.069 369 ASP BBB N   
6420  C CA  . ASP B 369 ? 0.387 0.478 0.486 -0.018 0.031  -0.078 369 ASP BBB CA  
6421  C C   . ASP B 369 ? 0.406 0.500 0.493 -0.015 0.025  -0.076 369 ASP BBB C   
6422  O O   . ASP B 369 ? 0.426 0.519 0.503 -0.014 0.023  -0.072 369 ASP BBB O   
6423  C CB  . ASP B 369 ? 0.380 0.472 0.482 -0.018 0.031  -0.081 369 ASP BBB CB  
6424  C CG  . ASP B 369 ? 0.373 0.474 0.480 -0.016 0.028  -0.090 369 ASP BBB CG  
6425  O OD1 . ASP B 369 ? 0.352 0.459 0.458 -0.014 0.024  -0.094 369 ASP BBB OD1 
6426  O OD2 . ASP B 369 ? 0.360 0.462 0.471 -0.016 0.028  -0.094 369 ASP BBB OD2 
6427  N N   . TYR B 370 ? 0.415 0.513 0.504 -0.014 0.024  -0.079 370 TYR BBB N   
6428  C CA  . TYR B 370 ? 0.450 0.549 0.528 -0.012 0.020  -0.077 370 TYR BBB CA  
6429  C C   . TYR B 370 ? 0.444 0.549 0.518 -0.009 0.016  -0.082 370 TYR BBB C   
6430  O O   . TYR B 370 ? 0.501 0.607 0.565 -0.007 0.012  -0.080 370 TYR BBB O   
6431  C CB  . TYR B 370 ? 0.468 0.569 0.549 -0.012 0.020  -0.078 370 TYR BBB CB  
6432  C CG  . TYR B 370 ? 0.508 0.602 0.588 -0.014 0.024  -0.072 370 TYR BBB CG  
6433  C CD1 . TYR B 370 ? 0.505 0.595 0.574 -0.014 0.022  -0.065 370 TYR BBB CD1 
6434  C CD2 . TYR B 370 ? 0.536 0.628 0.627 -0.016 0.028  -0.073 370 TYR BBB CD2 
6435  C CE1 . TYR B 370 ? 0.507 0.592 0.576 -0.015 0.025  -0.059 370 TYR BBB CE1 
6436  C CE2 . TYR B 370 ? 0.529 0.615 0.619 -0.017 0.031  -0.067 370 TYR BBB CE2 
6437  C CZ  . TYR B 370 ? 0.533 0.615 0.611 -0.017 0.029  -0.060 370 TYR BBB CZ  
6438  O OH  . TYR B 370 ? 0.497 0.575 0.575 -0.017 0.031  -0.054 370 TYR BBB OH  
6439  N N   . ASP B 371 ? 0.443 0.552 0.524 -0.009 0.015  -0.087 371 ASP BBB N   
6440  C CA  . ASP B 371 ? 0.462 0.576 0.539 -0.005 0.011  -0.092 371 ASP BBB CA  
6441  C C   . ASP B 371 ? 0.452 0.563 0.517 -0.004 0.009  -0.086 371 ASP BBB C   
6442  O O   . ASP B 371 ? 0.452 0.566 0.510 -0.001 0.005  -0.088 371 ASP BBB O   
6443  C CB  . ASP B 371 ? 0.458 0.578 0.547 -0.005 0.011  -0.101 371 ASP BBB CB  
6444  C CG  . ASP B 371 ? 0.450 0.576 0.551 -0.006 0.013  -0.109 371 ASP BBB CG  
6445  O OD1 . ASP B 371 ? 0.464 0.592 0.562 -0.004 0.011  -0.110 371 ASP BBB OD1 
6446  O OD2 . ASP B 371 ? 0.424 0.551 0.538 -0.008 0.016  -0.115 371 ASP BBB OD2 
6447  N N   . PHE B 372 ? 0.422 0.525 0.485 -0.007 0.012  -0.079 372 PHE BBB N   
6448  C CA  . PHE B 372 ? 0.421 0.520 0.474 -0.007 0.011  -0.074 372 PHE BBB CA  
6449  C C   . PHE B 372 ? 0.390 0.483 0.435 -0.008 0.012  -0.065 372 PHE BBB C   
6450  O O   . PHE B 372 ? 0.410 0.497 0.455 -0.010 0.015  -0.061 372 PHE BBB O   
6451  C CB  . PHE B 372 ? 0.434 0.532 0.493 -0.008 0.013  -0.076 372 PHE BBB CB  
6452  C CG  . PHE B 372 ? 0.438 0.544 0.506 -0.006 0.011  -0.085 372 PHE BBB CG  
6453  C CD1 . PHE B 372 ? 0.456 0.567 0.518 -0.002 0.006  -0.088 372 PHE BBB CD1 
6454  C CD2 . PHE B 372 ? 0.439 0.548 0.521 -0.008 0.014  -0.091 372 PHE BBB CD2 
6455  C CE1 . PHE B 372 ? 0.452 0.570 0.520 -0.000 0.004  -0.097 372 PHE BBB CE1 
6456  C CE2 . PHE B 372 ? 0.452 0.569 0.542 -0.006 0.012  -0.101 372 PHE BBB CE2 
6457  C CZ  . PHE B 372 ? 0.451 0.572 0.534 -0.002 0.007  -0.104 372 PHE BBB CZ  
6458  N N   . VAL B 373 ? 0.360 0.453 0.398 -0.007 0.010  -0.064 373 VAL BBB N   
6459  C CA  . VAL B 373 ? 0.319 0.407 0.350 -0.008 0.011  -0.056 373 VAL BBB CA  
6460  C C   . VAL B 373 ? 0.297 0.384 0.316 -0.006 0.008  -0.054 373 VAL BBB C   
6461  O O   . VAL B 373 ? 0.290 0.380 0.304 -0.003 0.007  -0.056 373 VAL BBB O   
6462  C CB  . VAL B 373 ? 0.305 0.393 0.337 -0.009 0.012  -0.056 373 VAL BBB CB  
6463  C CG1 . VAL B 373 ? 0.302 0.386 0.327 -0.009 0.013  -0.050 373 VAL BBB CG1 
6464  C CG2 . VAL B 373 ? 0.304 0.392 0.348 -0.011 0.015  -0.058 373 VAL BBB CG2 
6465  N N   . PRO B 374 ? 0.289 0.372 0.302 -0.006 0.009  -0.050 374 PRO BBB N   
6466  C CA  . PRO B 374 ? 0.297 0.378 0.298 -0.004 0.006  -0.047 374 PRO BBB CA  
6467  C C   . PRO B 374 ? 0.316 0.394 0.311 -0.005 0.007  -0.042 374 PRO BBB C   
6468  O O   . PRO B 374 ? 0.301 0.378 0.300 -0.007 0.009  -0.040 374 PRO BBB O   
6469  C CB  . PRO B 374 ? 0.294 0.373 0.294 -0.005 0.007  -0.045 374 PRO BBB CB  
6470  C CG  . PRO B 374 ? 0.281 0.358 0.289 -0.008 0.010  -0.043 374 PRO BBB CG  
6471  C CD  . PRO B 374 ? 0.279 0.359 0.296 -0.009 0.011  -0.047 374 PRO BBB CD  
6472  N N   . THR B 375 ? 0.349 0.426 0.335 -0.003 0.006  -0.041 375 THR BBB N   
6473  C CA  . THR B 375 ? 0.361 0.434 0.340 -0.004 0.007  -0.037 375 THR BBB CA  
6474  C C   . THR B 375 ? 0.359 0.429 0.328 -0.002 0.007  -0.034 375 THR BBB C   
6475  O O   . THR B 375 ? 0.396 0.467 0.361 0.001  0.005  -0.037 375 THR BBB O   
6476  C CB  . THR B 375 ? 0.382 0.458 0.361 -0.003 0.007  -0.040 375 THR BBB CB  
6477  O OG1 . THR B 375 ? 0.457 0.530 0.430 -0.003 0.009  -0.036 375 THR BBB OG1 
6478  C CG2 . THR B 375 ? 0.405 0.485 0.382 0.001  0.005  -0.044 375 THR BBB CG2 
6479  N N   . THR B 376 ? 0.344 0.410 0.307 -0.004 0.008  -0.030 376 THR BBB N   
6480  C CA  . THR B 376 ? 0.335 0.397 0.288 -0.002 0.009  -0.027 376 THR BBB CA  
6481  C C   . THR B 376 ? 0.329 0.388 0.278 -0.003 0.011  -0.025 376 THR BBB C   
6482  O O   . THR B 376 ? 0.303 0.363 0.257 -0.006 0.012  -0.024 376 THR BBB O   
6483  C CB  . THR B 376 ? 0.333 0.392 0.285 -0.004 0.009  -0.024 376 THR BBB CB  
6484  O OG1 . THR B 376 ? 0.322 0.382 0.275 -0.003 0.007  -0.026 376 THR BBB OG1 
6485  C CG2 . THR B 376 ? 0.360 0.415 0.302 -0.003 0.010  -0.021 376 THR BBB CG2 
6486  N N   . VAL B 377 ? 0.337 0.395 0.278 -0.000 0.011  -0.025 377 VAL BBB N   
6487  C CA  . VAL B 377 ? 0.331 0.386 0.266 -0.001 0.014  -0.023 377 VAL BBB CA  
6488  C C   . VAL B 377 ? 0.331 0.380 0.259 -0.002 0.016  -0.020 377 VAL BBB C   
6489  O O   . VAL B 377 ? 0.340 0.386 0.262 0.001  0.015  -0.019 377 VAL BBB O   
6490  C CB  . VAL B 377 ? 0.352 0.407 0.281 0.003  0.014  -0.026 377 VAL BBB CB  
6491  C CG1 . VAL B 377 ? 0.371 0.421 0.292 0.003  0.017  -0.023 377 VAL BBB CG1 
6492  C CG2 . VAL B 377 ? 0.355 0.416 0.291 0.004  0.012  -0.030 377 VAL BBB CG2 
6493  N N   . PHE B 378 ? 0.312 0.359 0.242 -0.005 0.018  -0.017 378 PHE BBB N   
6494  C CA  . PHE B 378 ? 0.314 0.356 0.240 -0.006 0.020  -0.014 378 PHE BBB CA  
6495  C C   . PHE B 378 ? 0.320 0.357 0.237 -0.005 0.024  -0.013 378 PHE BBB C   
6496  O O   . PHE B 378 ? 0.332 0.366 0.249 -0.008 0.027  -0.011 378 PHE BBB O   
6497  C CB  . PHE B 378 ? 0.298 0.341 0.231 -0.010 0.021  -0.013 378 PHE BBB CB  
6498  C CG  . PHE B 378 ? 0.289 0.336 0.228 -0.011 0.018  -0.014 378 PHE BBB CG  
6499  C CD1 . PHE B 378 ? 0.287 0.333 0.225 -0.010 0.017  -0.012 378 PHE BBB CD1 
6500  C CD2 . PHE B 378 ? 0.294 0.345 0.240 -0.011 0.017  -0.015 378 PHE BBB CD2 
6501  C CE1 . PHE B 378 ? 0.287 0.335 0.231 -0.011 0.015  -0.013 378 PHE BBB CE1 
6502  C CE2 . PHE B 378 ? 0.280 0.333 0.233 -0.012 0.015  -0.016 378 PHE BBB CE2 
6503  C CZ  . PHE B 378 ? 0.280 0.332 0.231 -0.011 0.014  -0.015 378 PHE BBB CZ  
6504  N N   . THR B 379 ? 0.325 0.360 0.234 -0.001 0.023  -0.013 379 THR BBB N   
6505  C CA  . THR B 379 ? 0.353 0.382 0.252 0.001  0.027  -0.012 379 THR BBB CA  
6506  C C   . THR B 379 ? 0.370 0.393 0.263 0.001  0.029  -0.009 379 THR BBB C   
6507  O O   . THR B 379 ? 0.363 0.388 0.260 0.001  0.026  -0.009 379 THR BBB O   
6508  C CB  . THR B 379 ? 0.357 0.386 0.250 0.006  0.026  -0.014 379 THR BBB CB  
6509  O OG1 . THR B 379 ? 0.349 0.383 0.245 0.008  0.021  -0.016 379 THR BBB OG1 
6510  C CG2 . THR B 379 ? 0.353 0.385 0.250 0.005  0.027  -0.016 379 THR BBB CG2 
6511  N N   . PRO B 380 ? 0.385 0.402 0.270 0.002  0.033  -0.007 380 PRO BBB N   
6512  C CA  . PRO B 380 ? 0.397 0.407 0.277 0.002  0.035  -0.004 380 PRO BBB CA  
6513  C C   . PRO B 380 ? 0.409 0.420 0.286 0.005  0.031  -0.004 380 PRO BBB C   
6514  O O   . PRO B 380 ? 0.445 0.454 0.323 0.004  0.031  -0.003 380 PRO BBB O   
6515  C CB  . PRO B 380 ? 0.406 0.408 0.275 0.004  0.041  -0.002 380 PRO BBB CB  
6516  C CG  . PRO B 380 ? 0.407 0.412 0.281 0.001  0.042  -0.004 380 PRO BBB CG  
6517  C CD  . PRO B 380 ? 0.399 0.412 0.279 0.002  0.037  -0.007 380 PRO BBB CD  
6518  N N   . ILE B 381 ? 0.411 0.424 0.284 0.010  0.028  -0.006 381 ILE BBB N   
6519  C CA  . ILE B 381 ? 0.395 0.413 0.271 0.012  0.023  -0.008 381 ILE BBB CA  
6520  C C   . ILE B 381 ? 0.368 0.394 0.254 0.011  0.020  -0.011 381 ILE BBB C   
6521  O O   . ILE B 381 ? 0.367 0.394 0.252 0.012  0.021  -0.013 381 ILE BBB O   
6522  C CB  . ILE B 381 ? 0.432 0.448 0.297 0.019  0.021  -0.008 381 ILE BBB CB  
6523  C CG1 . ILE B 381 ? 0.438 0.453 0.297 0.023  0.022  -0.010 381 ILE BBB CG1 
6524  C CG2 . ILE B 381 ? 0.467 0.474 0.323 0.020  0.024  -0.005 381 ILE BBB CG2 
6525  C CD1 . ILE B 381 ? 0.459 0.472 0.306 0.030  0.020  -0.010 381 ILE BBB CD1 
6526  N N   . GLU B 382 ? 0.336 0.367 0.231 0.009  0.017  -0.013 382 GLU BBB N   
6527  C CA  . GLU B 382 ? 0.321 0.358 0.226 0.006  0.015  -0.015 382 GLU BBB CA  
6528  C C   . GLU B 382 ? 0.317 0.359 0.222 0.011  0.011  -0.020 382 GLU BBB C   
6529  O O   . GLU B 382 ? 0.334 0.374 0.232 0.015  0.010  -0.020 382 GLU BBB O   
6530  C CB  . GLU B 382 ? 0.309 0.349 0.222 0.003  0.014  -0.015 382 GLU BBB CB  
6531  C CG  . GLU B 382 ? 0.318 0.353 0.230 -0.001 0.017  -0.011 382 GLU BBB CG  
6532  C CD  . GLU B 382 ? 0.321 0.358 0.240 -0.004 0.016  -0.010 382 GLU BBB CD  
6533  O OE1 . GLU B 382 ? 0.326 0.366 0.250 -0.004 0.014  -0.012 382 GLU BBB OE1 
6534  O OE2 . GLU B 382 ? 0.338 0.373 0.258 -0.007 0.019  -0.008 382 GLU BBB OE2 
6535  N N   . TYR B 383 ? 0.306 0.354 0.219 0.010  0.010  -0.023 383 TYR BBB N   
6536  C CA  . TYR B 383 ? 0.298 0.351 0.214 0.013  0.006  -0.028 383 TYR BBB CA  
6537  C C   . TYR B 383 ? 0.277 0.336 0.205 0.010  0.005  -0.030 383 TYR BBB C   
6538  O O   . TYR B 383 ? 0.266 0.326 0.201 0.007  0.006  -0.030 383 TYR BBB O   
6539  C CB  . TYR B 383 ? 0.314 0.369 0.225 0.017  0.006  -0.029 383 TYR BBB CB  
6540  C CG  . TYR B 383 ? 0.321 0.382 0.237 0.019  0.003  -0.035 383 TYR BBB CG  
6541  C CD1 . TYR B 383 ? 0.312 0.377 0.230 0.022  -0.000 -0.039 383 TYR BBB CD1 
6542  C CD2 . TYR B 383 ? 0.330 0.395 0.249 0.020  0.003  -0.038 383 TYR BBB CD2 
6543  C CE1 . TYR B 383 ? 0.305 0.377 0.228 0.025  -0.003 -0.045 383 TYR BBB CE1 
6544  C CE2 . TYR B 383 ? 0.332 0.404 0.257 0.022  0.000  -0.044 383 TYR BBB CE2 
6545  C CZ  . TYR B 383 ? 0.308 0.383 0.235 0.025  -0.003 -0.048 383 TYR BBB CZ  
6546  O OH  . TYR B 383 ? 0.307 0.390 0.240 0.027  -0.006 -0.054 383 TYR BBB OH  
6547  N N   . GLY B 384 ? 0.270 0.332 0.203 0.011  0.003  -0.032 384 GLY BBB N   
6548  C CA  . GLY B 384 ? 0.278 0.344 0.223 0.008  0.002  -0.035 384 GLY BBB CA  
6549  C C   . GLY B 384 ? 0.300 0.372 0.249 0.011  -0.001 -0.041 384 GLY BBB C   
6550  O O   . GLY B 384 ? 0.309 0.382 0.252 0.016  -0.003 -0.043 384 GLY BBB O   
6551  N N   . HIS B 385 ? 0.286 0.363 0.246 0.009  -0.001 -0.045 385 HIS BBB N   
6552  C CA  . HIS B 385 ? 0.299 0.382 0.264 0.012  -0.003 -0.052 385 HIS BBB CA  
6553  C C   . HIS B 385 ? 0.291 0.377 0.269 0.008  -0.002 -0.054 385 HIS BBB C   
6554  O O   . HIS B 385 ? 0.297 0.381 0.278 0.005  0.001  -0.050 385 HIS BBB O   
6555  C CB  . HIS B 385 ? 0.293 0.379 0.253 0.016  -0.005 -0.055 385 HIS BBB CB  
6556  C CG  . HIS B 385 ? 0.298 0.386 0.264 0.014  -0.003 -0.056 385 HIS BBB CG  
6557  N ND1 . HIS B 385 ? 0.301 0.396 0.277 0.015  -0.004 -0.063 385 HIS BBB ND1 
6558  C CD2 . HIS B 385 ? 0.290 0.375 0.255 0.012  -0.001 -0.052 385 HIS BBB CD2 
6559  C CE1 . HIS B 385 ? 0.297 0.392 0.277 0.013  -0.003 -0.062 385 HIS BBB CE1 
6560  N NE2 . HIS B 385 ? 0.282 0.372 0.255 0.011  -0.001 -0.056 385 HIS BBB NE2 
6561  N N   . VAL B 386 ? 0.292 0.384 0.278 0.010  -0.004 -0.060 386 VAL BBB N   
6562  C CA  . VAL B 386 ? 0.298 0.394 0.298 0.007  -0.002 -0.065 386 VAL BBB CA  
6563  C C   . VAL B 386 ? 0.313 0.417 0.317 0.011  -0.005 -0.073 386 VAL BBB C   
6564  O O   . VAL B 386 ? 0.327 0.433 0.326 0.015  -0.008 -0.076 386 VAL BBB O   
6565  C CB  . VAL B 386 ? 0.288 0.382 0.296 0.004  -0.000 -0.064 386 VAL BBB CB  
6566  C CG1 . VAL B 386 ? 0.294 0.391 0.302 0.006  -0.002 -0.068 386 VAL BBB CG1 
6567  C CG2 . VAL B 386 ? 0.279 0.375 0.299 0.001  0.002  -0.066 386 VAL BBB CG2 
6568  N N   . GLY B 387 ? 0.319 0.427 0.333 0.009  -0.004 -0.077 387 GLY BBB N   
6569  C CA  . GLY B 387 ? 0.335 0.451 0.356 0.012  -0.006 -0.086 387 GLY BBB CA  
6570  C C   . GLY B 387 ? 0.346 0.463 0.357 0.017  -0.009 -0.087 387 GLY BBB C   
6571  O O   . GLY B 387 ? 0.342 0.455 0.346 0.016  -0.008 -0.082 387 GLY BBB O   
6572  N N   . LEU B 388 ? 0.366 0.491 0.378 0.022  -0.013 -0.094 388 LEU BBB N   
6573  C CA  . LEU B 388 ? 0.387 0.516 0.393 0.027  -0.015 -0.098 388 LEU BBB CA  
6574  C C   . LEU B 388 ? 0.412 0.536 0.400 0.032  -0.017 -0.094 388 LEU BBB C   
6575  O O   . LEU B 388 ? 0.438 0.562 0.423 0.033  -0.019 -0.093 388 LEU BBB O   
6576  C CB  . LEU B 388 ? 0.395 0.533 0.410 0.030  -0.018 -0.109 388 LEU BBB CB  
6577  C CG  . LEU B 388 ? 0.385 0.528 0.419 0.025  -0.015 -0.114 388 LEU BBB CG  
6578  C CD1 . LEU B 388 ? 0.371 0.524 0.415 0.028  -0.018 -0.125 388 LEU BBB CD1 
6579  C CD2 . LEU B 388 ? 0.378 0.518 0.414 0.021  -0.012 -0.111 388 LEU BBB CD2 
6580  N N   . SER B 389 ? 0.430 0.552 0.409 0.034  -0.017 -0.091 389 SER BBB N   
6581  C CA  . SER B 389 ? 0.464 0.583 0.426 0.040  -0.019 -0.089 389 SER BBB CA  
6582  C C   . SER B 389 ? 0.474 0.602 0.436 0.047  -0.023 -0.097 389 SER BBB C   
6583  O O   . SER B 389 ? 0.449 0.585 0.425 0.046  -0.025 -0.105 389 SER BBB O   
6584  C CB  . SER B 389 ? 0.463 0.579 0.418 0.040  -0.017 -0.086 389 SER BBB CB  
6585  O OG  . SER B 389 ? 0.498 0.621 0.461 0.041  -0.018 -0.092 389 SER BBB OG  
6586  N N   . SER B 390 ? 0.494 0.619 0.442 0.053  -0.026 -0.096 390 SER BBB N   
6587  C CA  . SER B 390 ? 0.519 0.652 0.464 0.061  -0.031 -0.104 390 SER BBB CA  
6588  C C   . SER B 390 ? 0.502 0.642 0.452 0.063  -0.031 -0.110 390 SER BBB C   
6589  O O   . SER B 390 ? 0.476 0.626 0.436 0.065  -0.035 -0.119 390 SER BBB O   
6590  C CB  . SER B 390 ? 0.557 0.684 0.482 0.068  -0.032 -0.099 390 SER BBB CB  
6591  O OG  . SER B 390 ? 0.561 0.682 0.482 0.066  -0.031 -0.094 390 SER BBB OG  
6592  N N   . GLU B 391 ? 0.501 0.636 0.446 0.061  -0.028 -0.105 391 GLU BBB N   
6593  C CA  . GLU B 391 ? 0.510 0.651 0.458 0.062  -0.029 -0.110 391 GLU BBB CA  
6594  C C   . GLU B 391 ? 0.480 0.629 0.448 0.057  -0.029 -0.117 391 GLU BBB C   
6595  O O   . GLU B 391 ? 0.528 0.686 0.502 0.061  -0.032 -0.126 391 GLU BBB O   
6596  C CB  . GLU B 391 ? 0.521 0.655 0.460 0.060  -0.025 -0.103 391 GLU BBB CB  
6597  C CG  . GLU B 391 ? 0.526 0.652 0.445 0.066  -0.025 -0.098 391 GLU BBB CG  
6598  C CD  . GLU B 391 ? 0.561 0.678 0.471 0.065  -0.023 -0.090 391 GLU BBB CD  
6599  O OE1 . GLU B 391 ? 0.533 0.646 0.449 0.058  -0.020 -0.085 391 GLU BBB OE1 
6600  O OE2 . GLU B 391 ? 0.611 0.726 0.508 0.072  -0.025 -0.089 391 GLU BBB OE2 
6601  N N   . ALA B 392 ? 0.432 0.577 0.410 0.049  -0.025 -0.113 392 ALA BBB N   
6602  C CA  . ALA B 392 ? 0.431 0.581 0.427 0.044  -0.024 -0.118 392 ALA BBB CA  
6603  C C   . ALA B 392 ? 0.444 0.602 0.450 0.046  -0.027 -0.127 392 ALA BBB C   
6604  O O   . ALA B 392 ? 0.452 0.618 0.473 0.045  -0.027 -0.135 392 ALA BBB O   
6605  C CB  . ALA B 392 ? 0.418 0.561 0.420 0.036  -0.019 -0.111 392 ALA BBB CB  
6606  N N   . ALA B 393 ? 0.446 0.603 0.445 0.049  -0.029 -0.125 393 ALA BBB N   
6607  C CA  . ALA B 393 ? 0.439 0.603 0.447 0.051  -0.032 -0.133 393 ALA BBB CA  
6608  C C   . ALA B 393 ? 0.424 0.598 0.432 0.059  -0.037 -0.143 393 ALA BBB C   
6609  O O   . ALA B 393 ? 0.369 0.552 0.391 0.058  -0.038 -0.153 393 ALA BBB O   
6610  C CB  . ALA B 393 ? 0.441 0.599 0.441 0.052  -0.032 -0.128 393 ALA BBB CB  
6611  N N   . ILE B 394 ? 0.478 0.651 0.469 0.065  -0.039 -0.141 394 ILE BBB N   
6612  C CA  . ILE B 394 ? 0.515 0.696 0.502 0.074  -0.044 -0.150 394 ILE BBB CA  
6613  C C   . ILE B 394 ? 0.550 0.739 0.549 0.072  -0.044 -0.157 394 ILE BBB C   
6614  O O   . ILE B 394 ? 0.536 0.737 0.547 0.074  -0.047 -0.168 394 ILE BBB O   
6615  C CB  . ILE B 394 ? 0.531 0.707 0.496 0.081  -0.046 -0.144 394 ILE BBB CB  
6616  C CG1 . ILE B 394 ? 0.524 0.696 0.480 0.085  -0.048 -0.141 394 ILE BBB CG1 
6617  C CG2 . ILE B 394 ? 0.556 0.739 0.515 0.089  -0.050 -0.151 394 ILE BBB CG2 
6618  C CD1 . ILE B 394 ? 0.532 0.696 0.465 0.091  -0.048 -0.133 394 ILE BBB CD1 
6619  N N   . ALA B 395 ? 0.581 0.764 0.580 0.066  -0.039 -0.151 395 ALA BBB N   
6620  C CA  . ALA B 395 ? 0.593 0.782 0.604 0.064  -0.038 -0.156 395 ALA BBB CA  
6621  C C   . ALA B 395 ? 0.588 0.784 0.620 0.059  -0.037 -0.164 395 ALA BBB C   
6622  O O   . ALA B 395 ? 0.598 0.804 0.641 0.061  -0.039 -0.174 395 ALA BBB O   
6623  C CB  . ALA B 395 ? 0.594 0.774 0.601 0.058  -0.033 -0.147 395 ALA BBB CB  
6624  N N   . LYS B 396 ? 0.570 0.761 0.610 0.054  -0.034 -0.161 396 LYS BBB N   
6625  C CA  . LYS B 396 ? 0.565 0.761 0.625 0.048  -0.032 -0.167 396 LYS BBB CA  
6626  C C   . LYS B 396 ? 0.572 0.778 0.641 0.051  -0.036 -0.178 396 LYS BBB C   
6627  O O   . LYS B 396 ? 0.584 0.798 0.670 0.050  -0.035 -0.188 396 LYS BBB O   
6628  C CB  . LYS B 396 ? 0.559 0.744 0.622 0.040  -0.027 -0.158 396 LYS BBB CB  
6629  C CG  . LYS B 396 ? 0.569 0.757 0.652 0.034  -0.023 -0.162 396 LYS BBB CG  
6630  C CD  . LYS B 396 ? 0.577 0.755 0.660 0.028  -0.018 -0.153 396 LYS BBB CD  
6631  C CE  . LYS B 396 ? 0.576 0.755 0.677 0.023  -0.015 -0.158 396 LYS BBB CE  
6632  N NZ  . LYS B 396 ? 0.581 0.760 0.693 0.019  -0.010 -0.159 396 LYS BBB NZ  
6633  N N   . TYR B 397 ? 0.583 0.788 0.642 0.056  -0.039 -0.177 397 TYR BBB N   
6634  C CA  . TYR B 397 ? 0.566 0.781 0.635 0.059  -0.042 -0.187 397 TYR BBB CA  
6635  C C   . TYR B 397 ? 0.573 0.797 0.633 0.069  -0.049 -0.194 397 TYR BBB C   
6636  O O   . TYR B 397 ? 0.558 0.791 0.626 0.073  -0.053 -0.205 397 TYR BBB O   
6637  C CB  . TYR B 397 ? 0.538 0.746 0.603 0.057  -0.041 -0.181 397 TYR BBB CB  
6638  C CG  . TYR B 397 ? 0.515 0.715 0.591 0.048  -0.035 -0.175 397 TYR BBB CG  
6639  C CD1 . TYR B 397 ? 0.498 0.704 0.594 0.043  -0.032 -0.183 397 TYR BBB CD1 
6640  C CD2 . TYR B 397 ? 0.510 0.698 0.576 0.043  -0.031 -0.163 397 TYR BBB CD2 
6641  C CE1 . TYR B 397 ? 0.499 0.698 0.604 0.035  -0.026 -0.178 397 TYR BBB CE1 
6642  C CE2 . TYR B 397 ? 0.507 0.689 0.583 0.036  -0.026 -0.158 397 TYR BBB CE2 
6643  C CZ  . TYR B 397 ? 0.504 0.691 0.598 0.032  -0.023 -0.165 397 TYR BBB CZ  
6644  O OH  . TYR B 397 ? 0.460 0.640 0.562 0.024  -0.017 -0.160 397 TYR BBB OH  
6645  N N   . GLY B 398 ? 0.584 0.804 0.626 0.075  -0.051 -0.189 398 GLY BBB N   
6646  C CA  . GLY B 398 ? 0.603 0.829 0.633 0.085  -0.057 -0.194 398 GLY BBB CA  
6647  C C   . GLY B 398 ? 0.637 0.857 0.650 0.090  -0.059 -0.188 398 GLY BBB C   
6648  O O   . GLY B 398 ? 0.643 0.860 0.661 0.086  -0.058 -0.186 398 GLY BBB O   
6649  N N   . GLU B 399 ? 0.706 0.924 0.700 0.098  -0.063 -0.185 399 GLU BBB N   
6650  C CA  . GLU B 399 ? 0.743 0.954 0.718 0.104  -0.064 -0.178 399 GLU BBB CA  
6651  C C   . GLU B 399 ? 0.744 0.960 0.724 0.107  -0.068 -0.184 399 GLU BBB C   
6652  O O   . GLU B 399 ? 0.765 0.973 0.736 0.107  -0.067 -0.177 399 GLU BBB O   
6653  C CB  . GLU B 399 ? 0.832 1.044 0.789 0.115  -0.068 -0.179 399 GLU BBB CB  
6654  C CG  . GLU B 399 ? 0.928 1.132 0.863 0.122  -0.070 -0.172 399 GLU BBB CG  
6655  C CD  . GLU B 399 ? 0.993 1.181 0.916 0.117  -0.064 -0.157 399 GLU BBB CD  
6656  O OE1 . GLU B 399 ? 1.053 1.237 0.973 0.114  -0.060 -0.153 399 GLU BBB OE1 
6657  O OE2 . GLU B 399 ? 1.031 1.212 0.948 0.116  -0.063 -0.151 399 GLU BBB OE2 
6658  N N   . ASP B 400 ? 0.728 0.959 0.724 0.109  -0.072 -0.198 400 ASP BBB N   
6659  C CA  . ASP B 400 ? 0.757 0.995 0.757 0.114  -0.076 -0.206 400 ASP BBB CA  
6660  C C   . ASP B 400 ? 0.664 0.901 0.681 0.105  -0.073 -0.206 400 ASP BBB C   
6661  O O   . ASP B 400 ? 0.617 0.857 0.635 0.108  -0.075 -0.209 400 ASP BBB O   
6662  C CB  . ASP B 400 ? 0.829 1.084 0.839 0.121  -0.082 -0.221 400 ASP BBB CB  
6663  C CG  . ASP B 400 ? 0.916 1.173 0.906 0.134  -0.088 -0.223 400 ASP BBB CG  
6664  O OD1 . ASP B 400 ? 0.976 1.222 0.946 0.136  -0.087 -0.212 400 ASP BBB OD1 
6665  O OD2 . ASP B 400 ? 1.019 1.289 1.014 0.141  -0.094 -0.236 400 ASP BBB OD2 
6666  N N   . ASP B 401 ? 0.630 0.863 0.659 0.095  -0.067 -0.203 401 ASP BBB N   
6667  C CA  . ASP B 401 ? 0.628 0.859 0.672 0.086  -0.062 -0.202 401 ASP BBB CA  
6668  C C   . ASP B 401 ? 0.611 0.826 0.643 0.081  -0.058 -0.187 401 ASP BBB C   
6669  O O   . ASP B 401 ? 0.654 0.865 0.697 0.073  -0.054 -0.184 401 ASP BBB O   
6670  C CB  . ASP B 401 ? 0.620 0.855 0.684 0.079  -0.059 -0.208 401 ASP BBB CB  
6671  C CG  . ASP B 401 ? 0.637 0.875 0.721 0.072  -0.055 -0.213 401 ASP BBB CG  
6672  O OD1 . ASP B 401 ? 0.646 0.886 0.731 0.074  -0.058 -0.215 401 ASP BBB OD1 
6673  O OD2 . ASP B 401 ? 0.643 0.881 0.741 0.065  -0.050 -0.214 401 ASP BBB OD2 
6674  N N   . ILE B 402 ? 0.576 0.783 0.588 0.086  -0.059 -0.178 402 ILE BBB N   
6675  C CA  . ILE B 402 ? 0.559 0.752 0.558 0.082  -0.055 -0.164 402 ILE BBB CA  
6676  C C   . ILE B 402 ? 0.549 0.737 0.533 0.088  -0.058 -0.160 402 ILE BBB C   
6677  O O   . ILE B 402 ? 0.528 0.719 0.499 0.097  -0.062 -0.162 402 ILE BBB O   
6678  C CB  . ILE B 402 ? 0.535 0.721 0.524 0.080  -0.052 -0.156 402 ILE BBB CB  
6679  C CG1 . ILE B 402 ? 0.526 0.713 0.530 0.073  -0.048 -0.158 402 ILE BBB CG1 
6680  C CG2 . ILE B 402 ? 0.546 0.718 0.520 0.079  -0.049 -0.143 402 ILE BBB CG2 
6681  C CD1 . ILE B 402 ? 0.507 0.692 0.526 0.064  -0.044 -0.156 402 ILE BBB CD1 
6682  N N   . GLU B 403 ? 0.561 0.743 0.546 0.083  -0.055 -0.153 403 GLU BBB N   
6683  C CA  . GLU B 403 ? 0.571 0.745 0.539 0.087  -0.057 -0.146 403 GLU BBB CA  
6684  C C   . GLU B 403 ? 0.557 0.718 0.517 0.081  -0.051 -0.133 403 GLU BBB C   
6685  O O   . GLU B 403 ? 0.535 0.693 0.506 0.073  -0.047 -0.131 403 GLU BBB O   
6686  C CB  . GLU B 403 ? 0.603 0.781 0.578 0.088  -0.059 -0.151 403 GLU BBB CB  
6687  C CG  . GLU B 403 ? 0.629 0.806 0.588 0.097  -0.063 -0.150 403 GLU BBB CG  
6688  C CD  . GLU B 403 ? 0.634 0.820 0.587 0.108  -0.069 -0.159 403 GLU BBB CD  
6689  O OE1 . GLU B 403 ? 0.669 0.868 0.637 0.110  -0.073 -0.171 403 GLU BBB OE1 
6690  O OE2 . GLU B 403 ? 0.614 0.795 0.549 0.115  -0.070 -0.154 403 GLU BBB OE2 
6691  N N   . GLU B 404 ? 0.571 0.723 0.512 0.086  -0.051 -0.126 404 GLU BBB N   
6692  C CA  . GLU B 404 ? 0.556 0.696 0.488 0.081  -0.046 -0.114 404 GLU BBB CA  
6693  C C   . GLU B 404 ? 0.549 0.684 0.471 0.085  -0.047 -0.110 404 GLU BBB C   
6694  O O   . GLU B 404 ? 0.565 0.700 0.474 0.093  -0.051 -0.111 404 GLU BBB O   
6695  C CB  . GLU B 404 ? 0.573 0.708 0.493 0.083  -0.044 -0.109 404 GLU BBB CB  
6696  C CG  . GLU B 404 ? 0.602 0.743 0.531 0.081  -0.044 -0.114 404 GLU BBB CG  
6697  C CD  . GLU B 404 ? 0.649 0.786 0.566 0.084  -0.043 -0.110 404 GLU BBB CD  
6698  O OE1 . GLU B 404 ? 0.621 0.747 0.525 0.083  -0.039 -0.100 404 GLU BBB OE1 
6699  O OE2 . GLU B 404 ? 0.747 0.891 0.666 0.088  -0.045 -0.117 404 GLU BBB OE2 
6700  N N   . TYR B 405 ? 0.510 0.641 0.439 0.078  -0.045 -0.106 405 TYR BBB N   
6701  C CA  . TYR B 405 ? 0.479 0.603 0.399 0.079  -0.045 -0.101 405 TYR BBB CA  
6702  C C   . TYR B 405 ? 0.471 0.583 0.382 0.075  -0.040 -0.090 405 TYR BBB C   
6703  O O   . TYR B 405 ? 0.459 0.568 0.377 0.068  -0.036 -0.087 405 TYR BBB O   
6704  C CB  . TYR B 405 ? 0.476 0.604 0.410 0.075  -0.045 -0.105 405 TYR BBB CB  
6705  C CG  . TYR B 405 ? 0.476 0.616 0.420 0.079  -0.050 -0.116 405 TYR BBB CG  
6706  C CD1 . TYR B 405 ? 0.475 0.618 0.413 0.086  -0.054 -0.120 405 TYR BBB CD1 
6707  C CD2 . TYR B 405 ? 0.475 0.624 0.436 0.076  -0.050 -0.124 405 TYR BBB CD2 
6708  C CE1 . TYR B 405 ? 0.490 0.644 0.439 0.090  -0.058 -0.131 405 TYR BBB CE1 
6709  C CE2 . TYR B 405 ? 0.474 0.635 0.446 0.079  -0.054 -0.136 405 TYR BBB CE2 
6710  C CZ  . TYR B 405 ? 0.484 0.647 0.449 0.086  -0.058 -0.139 405 TYR BBB CZ  
6711  O OH  . TYR B 405 ? 0.439 0.615 0.416 0.090  -0.063 -0.151 405 TYR BBB OH  
6712  N N   . LEU B 406 ? 0.462 0.566 0.357 0.080  -0.039 -0.084 406 LEU BBB N   
6713  C CA  . LEU B 406 ? 0.464 0.557 0.349 0.076  -0.034 -0.074 406 LEU BBB CA  
6714  C C   . LEU B 406 ? 0.462 0.546 0.333 0.080  -0.034 -0.068 406 LEU BBB C   
6715  O O   . LEU B 406 ? 0.462 0.548 0.328 0.087  -0.038 -0.072 406 LEU BBB O   
6716  C CB  . LEU B 406 ? 0.489 0.580 0.368 0.077  -0.033 -0.072 406 LEU BBB CB  
6717  C CG  . LEU B 406 ? 0.525 0.614 0.388 0.087  -0.035 -0.073 406 LEU BBB CG  
6718  C CD1 . LEU B 406 ? 0.535 0.621 0.392 0.086  -0.032 -0.070 406 LEU BBB CD1 
6719  C CD2 . LEU B 406 ? 0.541 0.641 0.407 0.094  -0.041 -0.083 406 LEU BBB CD2 
6720  N N   . SER B 407 ? 0.453 0.527 0.320 0.075  -0.029 -0.060 407 SER BBB N   
6721  C CA  . SER B 407 ? 0.466 0.532 0.322 0.077  -0.027 -0.054 407 SER BBB CA  
6722  C C   . SER B 407 ? 0.485 0.541 0.334 0.072  -0.021 -0.045 407 SER BBB C   
6723  O O   . SER B 407 ? 0.469 0.525 0.328 0.065  -0.019 -0.044 407 SER BBB O   
6724  C CB  . SER B 407 ? 0.448 0.515 0.312 0.073  -0.028 -0.054 407 SER BBB CB  
6725  O OG  . SER B 407 ? 0.454 0.511 0.306 0.075  -0.026 -0.048 407 SER BBB OG  
6726  N N   . GLU B 408 ? 0.508 0.554 0.341 0.077  -0.019 -0.041 408 GLU BBB N   
6727  C CA  . GLU B 408 ? 0.500 0.536 0.326 0.073  -0.013 -0.033 408 GLU BBB CA  
6728  C C   . GLU B 408 ? 0.498 0.526 0.317 0.073  -0.010 -0.028 408 GLU BBB C   
6729  O O   . GLU B 408 ? 0.530 0.556 0.339 0.081  -0.013 -0.028 408 GLU BBB O   
6730  C CB  . GLU B 408 ? 0.510 0.543 0.324 0.079  -0.011 -0.032 408 GLU BBB CB  
6731  C CG  . GLU B 408 ? 0.522 0.545 0.331 0.074  -0.004 -0.025 408 GLU BBB CG  
6732  C CD  . GLU B 408 ? 0.558 0.577 0.355 0.079  -0.002 -0.024 408 GLU BBB CD  
6733  O OE1 . GLU B 408 ? 0.596 0.617 0.384 0.088  -0.006 -0.027 408 GLU BBB OE1 
6734  O OE2 . GLU B 408 ? 0.582 0.597 0.379 0.075  0.003  -0.021 408 GLU BBB OE2 
6735  N N   . PHE B 409 ? 0.485 0.508 0.309 0.066  -0.006 -0.023 409 PHE BBB N   
6736  C CA  . PHE B 409 ? 0.472 0.488 0.292 0.065  -0.004 -0.019 409 PHE BBB CA  
6737  C C   . PHE B 409 ? 0.463 0.473 0.286 0.057  0.001  -0.014 409 PHE BBB C   
6738  O O   . PHE B 409 ? 0.466 0.478 0.295 0.053  0.003  -0.014 409 PHE BBB O   
6739  C CB  . PHE B 409 ? 0.446 0.469 0.276 0.063  -0.008 -0.023 409 PHE BBB CB  
6740  C CG  . PHE B 409 ? 0.421 0.451 0.267 0.056  -0.009 -0.025 409 PHE BBB CG  
6741  C CD1 . PHE B 409 ? 0.399 0.438 0.253 0.055  -0.012 -0.030 409 PHE BBB CD1 
6742  C CD2 . PHE B 409 ? 0.397 0.425 0.249 0.049  -0.006 -0.022 409 PHE BBB CD2 
6743  C CE1 . PHE B 409 ? 0.378 0.422 0.246 0.049  -0.012 -0.032 409 PHE BBB CE1 
6744  C CE2 . PHE B 409 ? 0.378 0.411 0.244 0.042  -0.006 -0.023 409 PHE BBB CE2 
6745  C CZ  . PHE B 409 ? 0.381 0.422 0.254 0.042  -0.009 -0.028 409 PHE BBB CZ  
6746  N N   . SER B 410 ? 0.494 0.498 0.313 0.056  0.004  -0.010 410 SER BBB N   
6747  C CA  . SER B 410 ? 0.498 0.496 0.320 0.049  0.009  -0.005 410 SER BBB CA  
6748  C C   . SER B 410 ? 0.477 0.479 0.310 0.044  0.007  -0.006 410 SER BBB C   
6749  O O   . SER B 410 ? 0.492 0.497 0.326 0.046  0.004  -0.008 410 SER BBB O   
6750  C CB  . SER B 410 ? 0.518 0.504 0.327 0.052  0.014  -0.000 410 SER BBB CB  
6751  O OG  . SER B 410 ? 0.549 0.531 0.362 0.045  0.018  0.003  410 SER BBB OG  
6752  N N   . THR B 411 ? 0.472 0.476 0.314 0.036  0.010  -0.005 411 THR BBB N   
6753  C CA  . THR B 411 ? 0.460 0.465 0.310 0.031  0.010  -0.004 411 THR BBB CA  
6754  C C   . THR B 411 ? 0.474 0.472 0.317 0.033  0.012  -0.001 411 THR BBB C   
6755  O O   . THR B 411 ? 0.458 0.447 0.290 0.035  0.016  0.002  411 THR BBB O   
6756  C CB  . THR B 411 ? 0.465 0.470 0.323 0.024  0.013  -0.003 411 THR BBB CB  
6757  O OG1 . THR B 411 ? 0.459 0.471 0.323 0.023  0.011  -0.005 411 THR BBB OG1 
6758  C CG2 . THR B 411 ? 0.455 0.462 0.321 0.018  0.013  -0.002 411 THR BBB CG2 
6759  N N   . LEU B 412 ? 0.464 0.464 0.312 0.032  0.010  -0.002 412 LEU BBB N   
6760  C CA  . LEU B 412 ? 0.463 0.457 0.305 0.033  0.011  0.000  412 LEU BBB CA  
6761  C C   . LEU B 412 ? 0.446 0.432 0.285 0.029  0.017  0.005  412 LEU BBB C   
6762  O O   . LEU B 412 ? 0.399 0.377 0.228 0.032  0.020  0.008  412 LEU BBB O   
6763  C CB  . LEU B 412 ? 0.486 0.485 0.338 0.030  0.008  -0.002 412 LEU BBB CB  
6764  C CG  . LEU B 412 ? 0.504 0.498 0.352 0.030  0.009  0.001  412 LEU BBB CG  
6765  C CD1 . LEU B 412 ? 0.518 0.506 0.353 0.038  0.009  0.001  412 LEU BBB CD1 
6766  C CD2 . LEU B 412 ? 0.519 0.519 0.376 0.027  0.006  -0.002 412 LEU BBB CD2 
6767  N N   . GLU B 413 ? 0.441 0.429 0.289 0.022  0.019  0.005  413 GLU BBB N   
6768  C CA  . GLU B 413 ? 0.452 0.435 0.300 0.018  0.024  0.008  413 GLU BBB CA  
6769  C C   . GLU B 413 ? 0.443 0.419 0.283 0.020  0.029  0.010  413 GLU BBB C   
6770  O O   . GLU B 413 ? 0.456 0.423 0.289 0.020  0.034  0.013  413 GLU BBB O   
6771  C CB  . GLU B 413 ? 0.454 0.442 0.313 0.011  0.024  0.007  413 GLU BBB CB  
6772  C CG  . GLU B 413 ? 0.464 0.459 0.332 0.010  0.020  0.005  413 GLU BBB CG  
6773  C CD  . GLU B 413 ? 0.469 0.472 0.342 0.010  0.015  0.002  413 GLU BBB CD  
6774  O OE1 . GLU B 413 ? 0.483 0.487 0.352 0.015  0.013  0.000  413 GLU BBB OE1 
6775  O OE2 . GLU B 413 ? 0.469 0.478 0.352 0.006  0.014  0.001  413 GLU BBB OE2 
6776  N N   . ILE B 414 ? 0.431 0.410 0.270 0.021  0.027  0.008  414 ILE BBB N   
6777  C CA  . ILE B 414 ? 0.447 0.420 0.278 0.024  0.031  0.010  414 ILE BBB CA  
6778  C C   . ILE B 414 ? 0.447 0.413 0.265 0.031  0.032  0.012  414 ILE BBB C   
6779  O O   . ILE B 414 ? 0.481 0.438 0.290 0.032  0.038  0.015  414 ILE BBB O   
6780  C CB  . ILE B 414 ? 0.453 0.432 0.287 0.024  0.029  0.008  414 ILE BBB CB  
6781  C CG1 . ILE B 414 ? 0.437 0.424 0.284 0.018  0.027  0.006  414 ILE BBB CG1 
6782  C CG2 . ILE B 414 ? 0.466 0.439 0.292 0.026  0.034  0.009  414 ILE BBB CG2 
6783  C CD1 . ILE B 414 ? 0.443 0.428 0.295 0.012  0.032  0.007  414 ILE BBB CD1 
6784  N N   . ALA B 415 ? 0.430 0.399 0.245 0.036  0.027  0.010  415 ALA BBB N   
6785  C CA  . ALA B 415 ? 0.431 0.393 0.232 0.044  0.027  0.012  415 ALA BBB CA  
6786  C C   . ALA B 415 ? 0.441 0.394 0.238 0.043  0.033  0.016  415 ALA BBB C   
6787  O O   . ALA B 415 ? 0.482 0.425 0.267 0.047  0.037  0.019  415 ALA BBB O   
6788  C CB  . ALA B 415 ? 0.430 0.399 0.232 0.049  0.021  0.008  415 ALA BBB CB  
6789  N N   . ALA B 416 ? 0.427 0.382 0.233 0.037  0.033  0.016  416 ALA BBB N   
6790  C CA  . ALA B 416 ? 0.433 0.379 0.235 0.036  0.038  0.019  416 ALA BBB CA  
6791  C C   . ALA B 416 ? 0.444 0.383 0.246 0.032  0.045  0.021  416 ALA BBB C   
6792  O O   . ALA B 416 ? 0.428 0.357 0.224 0.032  0.051  0.024  416 ALA BBB O   
6793  C CB  . ALA B 416 ? 0.423 0.375 0.236 0.031  0.035  0.017  416 ALA BBB CB  
6794  N N   . ALA B 417 ? 0.457 0.401 0.265 0.028  0.046  0.020  417 ALA BBB N   
6795  C CA  . ALA B 417 ? 0.481 0.419 0.289 0.023  0.053  0.022  417 ALA BBB CA  
6796  C C   . ALA B 417 ? 0.499 0.426 0.293 0.029  0.058  0.024  417 ALA BBB C   
6797  O O   . ALA B 417 ? 0.518 0.438 0.310 0.026  0.065  0.026  417 ALA BBB O   
6798  C CB  . ALA B 417 ? 0.456 0.402 0.275 0.018  0.051  0.019  417 ALA BBB CB  
6799  N N   . HIS B 418 ? 0.544 0.472 0.330 0.036  0.055  0.024  418 HIS BBB N   
6800  C CA  . HIS B 418 ? 0.584 0.503 0.355 0.042  0.059  0.027  418 HIS BBB CA  
6801  C C   . HIS B 418 ? 0.581 0.499 0.356 0.038  0.064  0.027  418 HIS BBB C   
6802  O O   . HIS B 418 ? 0.613 0.520 0.381 0.037  0.072  0.030  418 HIS BBB O   
6803  C CB  . HIS B 418 ? 0.602 0.508 0.362 0.046  0.064  0.031  418 HIS BBB CB  
6804  C CG  . HIS B 418 ? 0.634 0.541 0.389 0.052  0.059  0.031  418 HIS BBB CG  
6805  N ND1 . HIS B 418 ? 0.687 0.594 0.430 0.061  0.056  0.031  418 HIS BBB ND1 
6806  C CD2 . HIS B 418 ? 0.625 0.532 0.383 0.051  0.057  0.031  418 HIS BBB CD2 
6807  C CE1 . HIS B 418 ? 0.656 0.563 0.397 0.065  0.051  0.030  418 HIS BBB CE1 
6808  N NE2 . HIS B 418 ? 0.627 0.535 0.377 0.059  0.052  0.030  418 HIS BBB NE2 
6809  N N   . ARG B 419 ? 0.578 0.506 0.361 0.035  0.060  0.024  419 ARG BBB N   
6810  C CA  . ARG B 419 ? 0.590 0.519 0.377 0.031  0.064  0.023  419 ARG BBB CA  
6811  C C   . ARG B 419 ? 0.638 0.558 0.411 0.037  0.068  0.026  419 ARG BBB C   
6812  O O   . ARG B 419 ? 0.632 0.554 0.396 0.044  0.063  0.025  419 ARG BBB O   
6813  C CB  . ARG B 419 ? 0.564 0.506 0.363 0.028  0.057  0.019  419 ARG BBB CB  
6814  C CG  . ARG B 419 ? 0.527 0.477 0.340 0.021  0.054  0.017  419 ARG BBB CG  
6815  C CD  . ARG B 419 ? 0.493 0.453 0.317 0.017  0.050  0.014  419 ARG BBB CD  
6816  N NE  . ARG B 419 ? 0.487 0.452 0.323 0.011  0.049  0.013  419 ARG BBB NE  
6817  C CZ  . ARG B 419 ? 0.475 0.449 0.322 0.007  0.046  0.010  419 ARG BBB CZ  
6818  N NH1 . ARG B 419 ? 0.453 0.431 0.301 0.008  0.044  0.009  419 ARG BBB NH1 
6819  N NH2 . ARG B 419 ? 0.473 0.451 0.330 0.002  0.046  0.010  419 ARG BBB NH2 
6820  N N   . GLU B 420 ? 0.665 0.577 0.435 0.034  0.076  0.028  420 GLU BBB N   
6821  C CA  . GLU B 420 ? 0.694 0.596 0.450 0.039  0.082  0.030  420 GLU BBB CA  
6822  C C   . GLU B 420 ? 0.661 0.567 0.422 0.036  0.084  0.029  420 GLU BBB C   
6823  O O   . GLU B 420 ? 0.583 0.494 0.358 0.028  0.085  0.026  420 GLU BBB O   
6824  C CB  . GLU B 420 ? 0.760 0.648 0.509 0.039  0.092  0.034  420 GLU BBB CB  
6825  C CG  . GLU B 420 ? 0.823 0.706 0.564 0.044  0.090  0.037  420 GLU BBB CG  
6826  C CD  . GLU B 420 ? 0.883 0.750 0.614 0.046  0.100  0.041  420 GLU BBB CD  
6827  O OE1 . GLU B 420 ? 0.887 0.744 0.606 0.049  0.107  0.044  420 GLU BBB OE1 
6828  O OE2 . GLU B 420 ? 0.865 0.730 0.598 0.045  0.100  0.042  420 GLU BBB OE2 
6829  N N   . LYS B 421 ? 0.667 0.569 0.416 0.042  0.085  0.029  421 LYS BBB N   
6830  C CA  . LYS B 421 ? 0.697 0.599 0.447 0.040  0.089  0.029  421 LYS BBB CA  
6831  C C   . LYS B 421 ? 0.665 0.559 0.417 0.034  0.099  0.031  421 LYS BBB C   
6832  O O   . LYS B 421 ? 0.594 0.478 0.340 0.035  0.105  0.034  421 LYS BBB O   
6833  C CB  . LYS B 421 ? 0.735 0.632 0.468 0.049  0.090  0.031  421 LYS BBB CB  
6834  C CG  . LYS B 421 ? 0.769 0.676 0.501 0.055  0.081  0.028  421 LYS BBB CG  
6835  C CD  . LYS B 421 ? 0.826 0.727 0.543 0.062  0.083  0.029  421 LYS BBB CD  
6836  C CE  . LYS B 421 ? 0.876 0.789 0.596 0.065  0.075  0.024  421 LYS BBB CE  
6837  N NZ  . LYS B 421 ? 0.927 0.843 0.638 0.075  0.068  0.023  421 LYS BBB NZ  
6838  N N   . PRO B 422 ? 0.678 0.575 0.439 0.029  0.101  0.028  422 PRO BBB N   
6839  C CA  . PRO B 422 ? 0.722 0.610 0.483 0.024  0.112  0.029  422 PRO BBB CA  
6840  C C   . PRO B 422 ? 0.797 0.672 0.540 0.031  0.119  0.034  422 PRO BBB C   
6841  O O   . PRO B 422 ? 0.818 0.694 0.551 0.038  0.115  0.034  422 PRO BBB O   
6842  C CB  . PRO B 422 ? 0.697 0.594 0.470 0.019  0.111  0.026  422 PRO BBB CB  
6843  C CG  . PRO B 422 ? 0.701 0.613 0.483 0.018  0.100  0.023  422 PRO BBB CG  
6844  C CD  . PRO B 422 ? 0.683 0.594 0.454 0.026  0.095  0.024  422 PRO BBB CD  
6845  N N   . GLU B 423 ? 0.861 0.722 0.599 0.029  0.129  0.037  423 GLU BBB N   
6846  C CA  . GLU B 423 ? 0.919 0.766 0.638 0.037  0.136  0.042  423 GLU BBB CA  
6847  C C   . GLU B 423 ? 0.925 0.769 0.637 0.040  0.140  0.042  423 GLU BBB C   
6848  O O   . GLU B 423 ? 0.943 0.778 0.637 0.048  0.143  0.046  423 GLU BBB O   
6849  C CB  . GLU B 423 ? 0.991 0.825 0.706 0.035  0.145  0.045  423 GLU BBB CB  
6850  C CG  . GLU B 423 ? 1.055 0.879 0.772 0.031  0.158  0.046  423 GLU BBB CG  
6851  C CD  . GLU B 423 ? 1.108 0.922 0.827 0.027  0.166  0.047  423 GLU BBB CD  
6852  O OE1 . GLU B 423 ? 1.117 0.924 0.840 0.022  0.176  0.047  423 GLU BBB OE1 
6853  O OE2 . GLU B 423 ? 1.100 0.913 0.816 0.030  0.162  0.048  423 GLU BBB OE2 
6854  N N   . HIS B 424 ? 0.931 0.784 0.655 0.033  0.140  0.038  424 HIS BBB N   
6855  C CA  . HIS B 424 ? 0.961 0.812 0.679 0.035  0.143  0.038  424 HIS BBB CA  
6856  C C   . HIS B 424 ? 0.943 0.803 0.654 0.043  0.133  0.037  424 HIS BBB C   
6857  O O   . HIS B 424 ? 0.943 0.800 0.646 0.046  0.135  0.037  424 HIS BBB O   
6858  C CB  . HIS B 424 ? 0.933 0.791 0.666 0.026  0.145  0.034  424 HIS BBB CB  
6859  C CG  . HIS B 424 ? 0.941 0.816 0.692 0.021  0.135  0.029  424 HIS BBB CG  
6860  N ND1 . HIS B 424 ? 0.937 0.822 0.690 0.024  0.127  0.026  424 HIS BBB ND1 
6861  C CD2 . HIS B 424 ? 0.950 0.832 0.717 0.014  0.133  0.026  424 HIS BBB CD2 
6862  C CE1 . HIS B 424 ? 0.913 0.811 0.682 0.018  0.121  0.022  424 HIS BBB CE1 
6863  N NE2 . HIS B 424 ? 0.911 0.807 0.689 0.012  0.124  0.022  424 HIS BBB NE2 
6864  N N   . LEU B 425 ? 0.909 0.777 0.622 0.046  0.123  0.036  425 LEU BBB N   
6865  C CA  . LEU B 425 ? 0.879 0.756 0.588 0.053  0.114  0.034  425 LEU BBB CA  
6866  C C   . LEU B 425 ? 0.898 0.768 0.590 0.063  0.111  0.037  425 LEU BBB C   
6867  O O   . LEU B 425 ? 0.959 0.837 0.647 0.069  0.103  0.035  425 LEU BBB O   
6868  C CB  . LEU B 425 ? 0.859 0.752 0.585 0.048  0.104  0.029  425 LEU BBB CB  
6869  C CG  . LEU B 425 ? 0.839 0.739 0.579 0.040  0.104  0.025  425 LEU BBB CG  
6870  C CD1 . LEU B 425 ? 0.810 0.724 0.568 0.034  0.096  0.022  425 LEU BBB CD1 
6871  C CD2 . LEU B 425 ? 0.865 0.769 0.601 0.044  0.102  0.024  425 LEU BBB CD2 
6872  N N   . ARG B 426 ? 0.880 0.737 0.563 0.064  0.118  0.041  426 ARG BBB N   
6873  C CA  . ARG B 426 ? 0.871 0.721 0.539 0.074  0.117  0.044  426 ARG BBB CA  
6874  C C   . ARG B 426 ? 0.896 0.738 0.544 0.084  0.120  0.047  426 ARG BBB C   
6875  O O   . ARG B 426 ? 0.852 0.685 0.495 0.082  0.129  0.049  426 ARG BBB O   
6876  C CB  . ARG B 426 ? 0.857 0.695 0.522 0.072  0.124  0.048  426 ARG BBB CB  
6877  C CG  . ARG B 426 ? 0.823 0.668 0.505 0.064  0.120  0.046  426 ARG BBB CG  
6878  C CD  . ARG B 426 ? 0.798 0.652 0.480 0.069  0.110  0.045  426 ARG BBB CD  
6879  N NE  . ARG B 426 ? 0.810 0.652 0.473 0.078  0.112  0.049  426 ARG BBB NE  
6880  C CZ  . ARG B 426 ? 0.784 0.616 0.442 0.079  0.117  0.052  426 ARG BBB CZ  
6881  N NH1 . ARG B 426 ? 0.782 0.614 0.453 0.070  0.120  0.052  426 ARG BBB NH1 
6882  N NH2 . ARG B 426 ? 0.766 0.588 0.407 0.089  0.118  0.056  426 ARG BBB NH2 
6883  N N   . GLU B 427 ? 0.937 0.783 0.574 0.093  0.112  0.046  427 GLU BBB N   
6884  C CA  . GLU B 427 ? 0.979 0.820 0.598 0.104  0.113  0.048  427 GLU BBB CA  
6885  C C   . GLU B 427 ? 0.954 0.781 0.553 0.114  0.116  0.053  427 GLU BBB C   
6886  O O   . GLU B 427 ? 1.005 0.823 0.585 0.123  0.120  0.056  427 GLU BBB O   
6887  C CB  . GLU B 427 ? 1.050 0.907 0.672 0.109  0.101  0.043  427 GLU BBB CB  
6888  C CG  . GLU B 427 ? 1.111 0.973 0.736 0.107  0.101  0.040  427 GLU BBB CG  
6889  C CD  . GLU B 427 ? 1.144 1.022 0.775 0.109  0.090  0.033  427 GLU BBB CD  
6890  O OE1 . GLU B 427 ? 1.124 1.003 0.743 0.118  0.088  0.032  427 GLU BBB OE1 
6891  O OE2 . GLU B 427 ? 1.132 1.023 0.781 0.103  0.083  0.029  427 GLU BBB OE2 
6892  N N   . ASN B 428 ? 0.914 0.739 0.516 0.113  0.114  0.054  428 ASN BBB N   
6893  C CA  . ASN B 428 ? 0.923 0.735 0.506 0.123  0.117  0.059  428 ASN BBB CA  
6894  C C   . ASN B 428 ? 0.919 0.729 0.512 0.117  0.118  0.060  428 ASN BBB C   
6895  O O   . ASN B 428 ? 0.860 0.677 0.471 0.106  0.119  0.058  428 ASN BBB O   
6896  C CB  . ASN B 428 ? 0.921 0.738 0.491 0.135  0.108  0.058  428 ASN BBB CB  
6897  C CG  . ASN B 428 ? 0.912 0.749 0.498 0.133  0.095  0.051  428 ASN BBB CG  
6898  O OD1 . ASN B 428 ? 0.851 0.693 0.450 0.128  0.091  0.049  428 ASN BBB OD1 
6899  N ND2 . ASN B 428 ? 0.923 0.769 0.507 0.138  0.089  0.047  428 ASN BBB ND2 
6900  N N   . GLU B 429 ? 0.944 0.748 0.525 0.125  0.117  0.063  429 GLU BBB N   
6901  C CA  . GLU B 429 ? 0.968 0.769 0.555 0.122  0.117  0.065  429 GLU BBB CA  
6902  C C   . GLU B 429 ? 0.941 0.758 0.539 0.122  0.105  0.059  429 GLU BBB C   
6903  O O   . GLU B 429 ? 0.972 0.787 0.575 0.119  0.104  0.060  429 GLU BBB O   
6904  C CB  . GLU B 429 ? 0.972 0.755 0.538 0.131  0.124  0.071  429 GLU BBB CB  
6905  C CG  . GLU B 429 ? 1.033 0.799 0.585 0.133  0.137  0.076  429 GLU BBB CG  
6906  C CD  . GLU B 429 ? 1.025 0.789 0.591 0.120  0.145  0.076  429 GLU BBB CD  
6907  O OE1 . GLU B 429 ? 0.921 0.687 0.503 0.111  0.147  0.074  429 GLU BBB OE1 
6908  O OE2 . GLU B 429 ? 0.969 0.733 0.532 0.120  0.149  0.076  429 GLU BBB OE2 
6909  N N   . MET B 430 ? 0.908 0.739 0.510 0.124  0.095  0.054  430 MET BBB N   
6910  C CA  . MET B 430 ? 0.898 0.744 0.512 0.124  0.083  0.049  430 MET BBB CA  
6911  C C   . MET B 430 ? 0.867 0.729 0.499 0.116  0.078  0.043  430 MET BBB C   
6912  O O   . MET B 430 ? 0.886 0.762 0.528 0.116  0.068  0.038  430 MET BBB O   
6913  C CB  . MET B 430 ? 0.912 0.761 0.513 0.136  0.076  0.047  430 MET BBB CB  
6914  C CG  . MET B 430 ? 0.941 0.792 0.531 0.144  0.074  0.046  430 MET BBB CG  
6915  S SD  . MET B 430 ? 0.954 0.801 0.522 0.161  0.069  0.046  430 MET BBB SD  
6916  C CE  . MET B 430 ? 1.058 0.893 0.606 0.168  0.077  0.051  430 MET BBB CE  
6917  N N   . ASP B 431 ? 0.836 0.696 0.473 0.109  0.084  0.044  431 ASP BBB N   
6918  C CA  . ASP B 431 ? 0.819 0.692 0.473 0.100  0.080  0.039  431 ASP BBB CA  
6919  C C   . ASP B 431 ? 0.749 0.625 0.421 0.088  0.083  0.039  431 ASP BBB C   
6920  O O   . ASP B 431 ? 0.735 0.616 0.419 0.081  0.084  0.037  431 ASP BBB O   
6921  C CB  . ASP B 431 ? 0.873 0.743 0.520 0.102  0.085  0.040  431 ASP BBB CB  
6922  C CG  . ASP B 431 ? 0.914 0.793 0.576 0.093  0.084  0.036  431 ASP BBB CG  
6923  O OD1 . ASP B 431 ? 0.928 0.821 0.605 0.090  0.076  0.031  431 ASP BBB OD1 
6924  O OD2 . ASP B 431 ? 0.942 0.814 0.603 0.090  0.092  0.038  431 ASP BBB OD2 
6925  N N   . PHE B 432 ? 0.724 0.595 0.398 0.087  0.084  0.041  432 PHE BBB N   
6926  C CA  . PHE B 432 ? 0.736 0.605 0.423 0.076  0.088  0.041  432 PHE BBB CA  
6927  C C   . PHE B 432 ? 0.707 0.592 0.413 0.069  0.081  0.036  432 PHE BBB C   
6928  O O   . PHE B 432 ? 0.673 0.561 0.392 0.060  0.084  0.035  432 PHE BBB O   
6929  C CB  . PHE B 432 ? 0.741 0.601 0.422 0.078  0.092  0.045  432 PHE BBB CB  
6930  C CG  . PHE B 432 ? 0.760 0.623 0.435 0.085  0.084  0.044  432 PHE BBB CG  
6931  C CD1 . PHE B 432 ? 0.752 0.626 0.441 0.082  0.077  0.040  432 PHE BBB CD1 
6932  C CD2 . PHE B 432 ? 0.788 0.643 0.445 0.097  0.085  0.047  432 PHE BBB CD2 
6933  C CE1 . PHE B 432 ? 0.783 0.660 0.467 0.088  0.070  0.039  432 PHE BBB CE1 
6934  C CE2 . PHE B 432 ? 0.824 0.682 0.476 0.104  0.078  0.046  432 PHE BBB CE2 
6935  C CZ  . PHE B 432 ? 0.804 0.674 0.470 0.099  0.070  0.042  432 PHE BBB CZ  
6936  N N   . ALA B 433 ? 0.698 0.594 0.407 0.073  0.071  0.033  433 ALA BBB N   
6937  C CA  . ALA B 433 ? 0.678 0.588 0.404 0.067  0.063  0.028  433 ALA BBB CA  
6938  C C   . ALA B 433 ? 0.654 0.573 0.389 0.063  0.061  0.024  433 ALA BBB C   
6939  O O   . ALA B 433 ? 0.646 0.565 0.374 0.068  0.061  0.024  433 ALA BBB O   
6940  C CB  . ALA B 433 ? 0.679 0.596 0.403 0.074  0.055  0.025  433 ALA BBB CB  
6941  N N   . LEU B 434 ? 0.640 0.568 0.392 0.055  0.059  0.022  434 LEU BBB N   
6942  C CA  . LEU B 434 ? 0.603 0.544 0.367 0.052  0.053  0.017  434 LEU BBB CA  
6943  C C   . LEU B 434 ? 0.552 0.501 0.315 0.058  0.045  0.014  434 LEU BBB C   
6944  O O   . LEU B 434 ? 0.569 0.517 0.328 0.062  0.042  0.014  434 LEU BBB O   
6945  C CB  . LEU B 434 ? 0.611 0.557 0.390 0.043  0.052  0.016  434 LEU BBB CB  
6946  C CG  . LEU B 434 ? 0.622 0.563 0.406 0.036  0.060  0.018  434 LEU BBB CG  
6947  C CD1 . LEU B 434 ? 0.603 0.553 0.404 0.028  0.057  0.015  434 LEU BBB CD1 
6948  C CD2 . LEU B 434 ? 0.650 0.588 0.430 0.036  0.064  0.018  434 LEU BBB CD2 
6949  N N   . PRO B 435 ? 0.502 0.459 0.269 0.058  0.041  0.010  435 PRO BBB N   
6950  C CA  . PRO B 435 ? 0.494 0.462 0.265 0.062  0.033  0.005  435 PRO BBB CA  
6951  C C   . PRO B 435 ? 0.487 0.461 0.269 0.058  0.029  0.004  435 PRO BBB C   
6952  O O   . PRO B 435 ? 0.487 0.461 0.278 0.051  0.031  0.005  435 PRO BBB O   
6953  C CB  . PRO B 435 ? 0.480 0.456 0.258 0.060  0.031  0.002  435 PRO BBB CB  
6954  C CG  . PRO B 435 ? 0.491 0.459 0.262 0.059  0.038  0.005  435 PRO BBB CG  
6955  C CD  . PRO B 435 ? 0.503 0.461 0.273 0.055  0.044  0.010  435 PRO BBB CD  
6956  N N   . LEU B 436 ? 0.483 0.462 0.265 0.063  0.022  0.000  436 LEU BBB N   
6957  C CA  . LEU B 436 ? 0.465 0.452 0.259 0.059  0.018  -0.003 436 LEU BBB CA  
6958  C C   . LEU B 436 ? 0.443 0.437 0.252 0.052  0.017  -0.005 436 LEU BBB C   
6959  O O   . LEU B 436 ? 0.441 0.439 0.252 0.052  0.017  -0.007 436 LEU BBB O   
6960  C CB  . LEU B 436 ? 0.475 0.469 0.267 0.067  0.011  -0.007 436 LEU BBB CB  
6961  C CG  . LEU B 436 ? 0.490 0.477 0.267 0.075  0.011  -0.006 436 LEU BBB CG  
6962  C CD1 . LEU B 436 ? 0.495 0.490 0.271 0.083  0.004  -0.011 436 LEU BBB CD1 
6963  C CD2 . LEU B 436 ? 0.494 0.476 0.270 0.074  0.012  -0.003 436 LEU BBB CD2 
6964  N N   . ASN B 437 ? 0.439 0.435 0.258 0.045  0.017  -0.004 437 ASN BBB N   
6965  C CA  . ASN B 437 ? 0.425 0.426 0.257 0.038  0.018  -0.005 437 ASN BBB CA  
6966  C C   . ASN B 437 ? 0.406 0.418 0.249 0.037  0.012  -0.010 437 ASN BBB C   
6967  O O   . ASN B 437 ? 0.418 0.434 0.269 0.033  0.013  -0.011 437 ASN BBB O   
6968  C CB  . ASN B 437 ? 0.424 0.422 0.262 0.031  0.021  -0.002 437 ASN BBB CB  
6969  C CG  . ASN B 437 ? 0.429 0.430 0.272 0.030  0.018  -0.003 437 ASN BBB CG  
6970  O OD1 . ASN B 437 ? 0.417 0.419 0.256 0.035  0.015  -0.004 437 ASN BBB OD1 
6971  N ND2 . ASN B 437 ? 0.438 0.441 0.291 0.024  0.018  -0.002 437 ASN BBB ND2 
6972  N N   . CYS B 438 ? 0.388 0.405 0.231 0.042  0.008  -0.013 438 CYS BBB N   
6973  C CA  . CYS B 438 ? 0.383 0.409 0.238 0.040  0.003  -0.019 438 CYS BBB CA  
6974  C C   . CYS B 438 ? 0.413 0.445 0.265 0.047  -0.001 -0.024 438 CYS BBB C   
6975  O O   . CYS B 438 ? 0.404 0.432 0.244 0.054  -0.002 -0.023 438 CYS BBB O   
6976  C CB  . CYS B 438 ? 0.384 0.413 0.245 0.039  0.000  -0.020 438 CYS BBB CB  
6977  S SG  . CYS B 438 ? 0.377 0.401 0.242 0.031  0.004  -0.015 438 CYS BBB SG  
6978  N N   . LEU B 439 ? 0.421 0.461 0.284 0.045  -0.004 -0.028 439 LEU BBB N   
6979  C CA  . LEU B 439 ? 0.427 0.475 0.292 0.050  -0.008 -0.035 439 LEU BBB CA  
6980  C C   . LEU B 439 ? 0.398 0.455 0.279 0.046  -0.011 -0.040 439 LEU BBB C   
6981  O O   . LEU B 439 ? 0.357 0.415 0.245 0.041  -0.009 -0.039 439 LEU BBB O   
6982  C CB  . LEU B 439 ? 0.452 0.500 0.312 0.052  -0.007 -0.036 439 LEU BBB CB  
6983  C CG  . LEU B 439 ? 0.468 0.525 0.330 0.058  -0.012 -0.043 439 LEU BBB CG  
6984  C CD1 . LEU B 439 ? 0.509 0.565 0.360 0.066  -0.015 -0.044 439 LEU BBB CD1 
6985  C CD2 . LEU B 439 ? 0.487 0.545 0.347 0.059  -0.011 -0.044 439 LEU BBB CD2 
6986  N N   . ALA B 440 ? 0.396 0.459 0.280 0.049  -0.015 -0.044 440 ALA BBB N   
6987  C CA  . ALA B 440 ? 0.380 0.451 0.279 0.046  -0.017 -0.050 440 ALA BBB CA  
6988  C C   . ALA B 440 ? 0.390 0.469 0.292 0.052  -0.021 -0.058 440 ALA BBB C   
6989  O O   . ALA B 440 ? 0.394 0.473 0.285 0.059  -0.024 -0.060 440 ALA BBB O   
6990  C CB  . ALA B 440 ? 0.380 0.450 0.281 0.046  -0.018 -0.050 440 ALA BBB CB  
6991  N N   . LYS B 441 ? 0.397 0.482 0.310 0.048  -0.021 -0.062 441 LYS BBB N   
6992  C CA  . LYS B 441 ? 0.389 0.484 0.308 0.052  -0.025 -0.071 441 LYS BBB CA  
6993  C C   . LYS B 441 ? 0.367 0.468 0.303 0.047  -0.025 -0.076 441 LYS BBB C   
6994  O O   . LYS B 441 ? 0.372 0.471 0.315 0.041  -0.022 -0.073 441 LYS BBB O   
6995  C CB  . LYS B 441 ? 0.422 0.516 0.334 0.055  -0.024 -0.070 441 LYS BBB CB  
6996  C CG  . LYS B 441 ? 0.433 0.537 0.351 0.059  -0.028 -0.079 441 LYS BBB CG  
6997  C CD  . LYS B 441 ? 0.452 0.555 0.359 0.064  -0.028 -0.079 441 LYS BBB CD  
6998  C CE  . LYS B 441 ? 0.457 0.556 0.365 0.059  -0.024 -0.075 441 LYS BBB CE  
6999  N NZ  . LYS B 441 ? 0.462 0.560 0.359 0.064  -0.024 -0.075 441 LYS BBB NZ  
7000  N N   . LEU B 442 ? 0.363 0.472 0.306 0.050  -0.029 -0.084 442 LEU BBB N   
7001  C CA  . LEU B 442 ? 0.352 0.470 0.313 0.047  -0.029 -0.091 442 LEU BBB CA  
7002  C C   . LEU B 442 ? 0.378 0.504 0.340 0.052  -0.032 -0.100 442 LEU BBB C   
7003  O O   . LEU B 442 ? 0.358 0.487 0.312 0.060  -0.036 -0.103 442 LEU BBB O   
7004  C CB  . LEU B 442 ? 0.330 0.451 0.298 0.047  -0.030 -0.095 442 LEU BBB CB  
7005  C CG  . LEU B 442 ? 0.334 0.448 0.301 0.042  -0.027 -0.088 442 LEU BBB CG  
7006  C CD1 . LEU B 442 ? 0.324 0.442 0.298 0.043  -0.029 -0.093 442 LEU BBB CD1 
7007  C CD2 . LEU B 442 ? 0.319 0.430 0.295 0.034  -0.023 -0.084 442 LEU BBB CD2 
7008  N N   . VAL B 443 ? 0.398 0.528 0.371 0.049  -0.031 -0.103 443 VAL BBB N   
7009  C CA  . VAL B 443 ? 0.437 0.577 0.417 0.052  -0.033 -0.112 443 VAL BBB CA  
7010  C C   . VAL B 443 ? 0.437 0.584 0.435 0.049  -0.033 -0.120 443 VAL BBB C   
7011  O O   . VAL B 443 ? 0.461 0.605 0.469 0.042  -0.029 -0.117 443 VAL BBB O   
7012  C CB  . VAL B 443 ? 0.483 0.621 0.461 0.050  -0.031 -0.109 443 VAL BBB CB  
7013  C CG1 . VAL B 443 ? 0.504 0.651 0.487 0.054  -0.034 -0.117 443 VAL BBB CG1 
7014  C CG2 . VAL B 443 ? 0.499 0.627 0.459 0.052  -0.030 -0.100 443 VAL BBB CG2 
7015  N N   . VAL B 444 ? 0.433 0.590 0.435 0.054  -0.038 -0.129 444 VAL BBB N   
7016  C CA  . VAL B 444 ? 0.422 0.586 0.442 0.052  -0.038 -0.138 444 VAL BBB CA  
7017  C C   . VAL B 444 ? 0.444 0.620 0.473 0.056  -0.041 -0.150 444 VAL BBB C   
7018  O O   . VAL B 444 ? 0.427 0.606 0.445 0.063  -0.045 -0.152 444 VAL BBB O   
7019  C CB  . VAL B 444 ? 0.437 0.601 0.455 0.054  -0.040 -0.139 444 VAL BBB CB  
7020  C CG1 . VAL B 444 ? 0.428 0.581 0.436 0.051  -0.037 -0.128 444 VAL BBB CG1 
7021  C CG2 . VAL B 444 ? 0.437 0.608 0.447 0.064  -0.046 -0.145 444 VAL BBB CG2 
7022  N N   . VAL B 445 ? 0.477 0.659 0.525 0.051  -0.039 -0.157 445 VAL BBB N   
7023  C CA  . VAL B 445 ? 0.514 0.709 0.574 0.054  -0.042 -0.170 445 VAL BBB CA  
7024  C C   . VAL B 445 ? 0.509 0.712 0.577 0.057  -0.045 -0.180 445 VAL BBB C   
7025  O O   . VAL B 445 ? 0.440 0.642 0.519 0.052  -0.042 -0.181 445 VAL BBB O   
7026  C CB  . VAL B 445 ? 0.517 0.713 0.593 0.047  -0.037 -0.173 445 VAL BBB CB  
7027  C CG1 . VAL B 445 ? 0.519 0.728 0.608 0.050  -0.039 -0.186 445 VAL BBB CG1 
7028  C CG2 . VAL B 445 ? 0.518 0.706 0.586 0.044  -0.033 -0.163 445 VAL BBB CG2 
7029  N N   . LYS B 446 ? 0.582 0.793 0.644 0.066  -0.051 -0.187 446 LYS BBB N   
7030  C CA  . LYS B 446 ? 0.641 0.862 0.710 0.071  -0.056 -0.197 446 LYS BBB CA  
7031  C C   . LYS B 446 ? 0.609 0.839 0.702 0.066  -0.053 -0.209 446 LYS BBB C   
7032  O O   . LYS B 446 ? 0.649 0.881 0.750 0.064  -0.053 -0.212 446 LYS BBB O   
7033  C CB  . LYS B 446 ? 0.648 0.877 0.706 0.082  -0.063 -0.203 446 LYS BBB CB  
7034  C CG  . LYS B 446 ? 0.692 0.910 0.725 0.087  -0.064 -0.192 446 LYS BBB CG  
7035  C CD  . LYS B 446 ? 0.742 0.965 0.764 0.097  -0.071 -0.196 446 LYS BBB CD  
7036  C CE  . LYS B 446 ? 0.758 0.990 0.774 0.106  -0.076 -0.203 446 LYS BBB CE  
7037  N NZ  . LYS B 446 ? 0.794 1.026 0.794 0.117  -0.082 -0.203 446 LYS BBB NZ  
7038  N N   . SER B 447 ? 0.622 0.857 0.725 0.064  -0.052 -0.214 447 SER BBB N   
7039  C CA  . SER B 447 ? 0.614 0.859 0.741 0.060  -0.049 -0.226 447 SER BBB CA  
7040  C C   . SER B 447 ? 0.610 0.847 0.748 0.050  -0.041 -0.221 447 SER BBB C   
7041  O O   . SER B 447 ? 0.616 0.858 0.774 0.045  -0.038 -0.230 447 SER BBB O   
7042  C CB  . SER B 447 ? 0.588 0.839 0.722 0.061  -0.049 -0.233 447 SER BBB CB  
7043  O OG  . SER B 447 ? 0.546 0.787 0.673 0.056  -0.045 -0.222 447 SER BBB OG  
7044  N N   . GLN B 448 ? 0.616 0.840 0.743 0.047  -0.039 -0.208 448 GLN BBB N   
7045  C CA  . GLN B 448 ? 0.600 0.816 0.736 0.038  -0.031 -0.203 448 GLN BBB CA  
7046  C C   . GLN B 448 ? 0.590 0.800 0.717 0.038  -0.032 -0.196 448 GLN BBB C   
7047  O O   . GLN B 448 ? 0.590 0.789 0.713 0.033  -0.027 -0.186 448 GLN BBB O   
7048  C CB  . GLN B 448 ? 0.594 0.799 0.726 0.032  -0.026 -0.192 448 GLN BBB CB  
7049  C CG  . GLN B 448 ? 0.608 0.819 0.747 0.032  -0.026 -0.198 448 GLN BBB CG  
7050  C CD  . GLN B 448 ? 0.622 0.822 0.757 0.027  -0.021 -0.188 448 GLN BBB CD  
7051  O OE1 . GLN B 448 ? 0.688 0.878 0.809 0.026  -0.020 -0.176 448 GLN BBB OE1 
7052  N NE2 . GLN B 448 ? 0.601 0.804 0.748 0.024  -0.018 -0.192 448 GLN BBB NE2 
7053  N N   . GLY B 449 ? 0.570 0.787 0.693 0.045  -0.038 -0.203 449 GLY BBB N   
7054  C CA  . GLY B 449 ? 0.570 0.782 0.685 0.046  -0.039 -0.198 449 GLY BBB CA  
7055  C C   . GLY B 449 ? 0.545 0.746 0.640 0.047  -0.039 -0.184 449 GLY BBB C   
7056  O O   . GLY B 449 ? 0.537 0.730 0.629 0.043  -0.036 -0.176 449 GLY BBB O   
7057  N N   . GLU B 450 ? 0.513 0.713 0.595 0.051  -0.042 -0.180 450 GLU BBB N   
7058  C CA  . GLU B 450 ? 0.512 0.701 0.575 0.052  -0.042 -0.167 450 GLU BBB CA  
7059  C C   . GLU B 450 ? 0.490 0.669 0.555 0.043  -0.035 -0.158 450 GLU BBB C   
7060  O O   . GLU B 450 ? 0.520 0.689 0.574 0.042  -0.034 -0.148 450 GLU BBB O   
7061  C CB  . GLU B 450 ? 0.503 0.689 0.552 0.057  -0.046 -0.164 450 GLU BBB CB  
7062  C CG  . GLU B 450 ? 0.504 0.699 0.547 0.067  -0.052 -0.172 450 GLU BBB CG  
7063  C CD  . GLU B 450 ? 0.509 0.699 0.534 0.074  -0.056 -0.166 450 GLU BBB CD  
7064  O OE1 . GLU B 450 ? 0.527 0.713 0.551 0.072  -0.055 -0.163 450 GLU BBB OE1 
7065  O OE2 . GLU B 450 ? 0.546 0.735 0.557 0.080  -0.059 -0.165 450 GLU BBB OE2 
7066  N N   . LYS B 451 ? 0.450 0.629 0.527 0.038  -0.031 -0.160 451 LYS BBB N   
7067  C CA  . LYS B 451 ? 0.454 0.623 0.532 0.030  -0.025 -0.150 451 LYS BBB CA  
7068  C C   . LYS B 451 ? 0.428 0.589 0.488 0.032  -0.025 -0.140 451 LYS BBB C   
7069  O O   . LYS B 451 ? 0.405 0.570 0.459 0.037  -0.029 -0.142 451 LYS BBB O   
7070  C CB  . LYS B 451 ? 0.492 0.664 0.586 0.026  -0.020 -0.155 451 LYS BBB CB  
7071  C CG  . LYS B 451 ? 0.519 0.681 0.615 0.018  -0.014 -0.146 451 LYS BBB CG  
7072  C CD  . LYS B 451 ? 0.538 0.702 0.650 0.014  -0.009 -0.151 451 LYS BBB CD  
7073  C CE  . LYS B 451 ? 0.568 0.728 0.692 0.008  -0.003 -0.150 451 LYS BBB CE  
7074  N NZ  . LYS B 451 ? 0.577 0.742 0.718 0.005  0.001  -0.159 451 LYS BBB NZ  
7075  N N   . VAL B 452 ? 0.390 0.542 0.444 0.028  -0.022 -0.129 452 VAL BBB N   
7076  C CA  . VAL B 452 ? 0.392 0.536 0.431 0.028  -0.022 -0.120 452 VAL BBB CA  
7077  C C   . VAL B 452 ? 0.396 0.538 0.440 0.025  -0.018 -0.118 452 VAL BBB C   
7078  O O   . VAL B 452 ? 0.405 0.545 0.459 0.019  -0.014 -0.117 452 VAL BBB O   
7079  C CB  . VAL B 452 ? 0.387 0.521 0.417 0.026  -0.020 -0.110 452 VAL BBB CB  
7080  C CG1 . VAL B 452 ? 0.382 0.509 0.398 0.026  -0.019 -0.101 452 VAL BBB CG1 
7081  C CG2 . VAL B 452 ? 0.390 0.526 0.416 0.030  -0.023 -0.112 452 VAL BBB CG2 
7082  N N   . VAL B 453 ? 0.392 0.536 0.430 0.028  -0.020 -0.119 453 VAL BBB N   
7083  C CA  . VAL B 453 ? 0.392 0.535 0.434 0.025  -0.018 -0.118 453 VAL BBB CA  
7084  C C   . VAL B 453 ? 0.383 0.518 0.410 0.025  -0.017 -0.108 453 VAL BBB C   
7085  O O   . VAL B 453 ? 0.353 0.485 0.383 0.021  -0.014 -0.105 453 VAL BBB O   
7086  C CB  . VAL B 453 ? 0.397 0.549 0.446 0.028  -0.020 -0.127 453 VAL BBB CB  
7087  C CG1 . VAL B 453 ? 0.390 0.550 0.456 0.027  -0.020 -0.137 453 VAL BBB CG1 
7088  C CG2 . VAL B 453 ? 0.397 0.553 0.433 0.036  -0.025 -0.129 453 VAL BBB CG2 
7089  N N   . GLY B 454 ? 0.392 0.523 0.405 0.029  -0.019 -0.103 454 GLY BBB N   
7090  C CA  . GLY B 454 ? 0.392 0.515 0.391 0.029  -0.018 -0.094 454 GLY BBB CA  
7091  C C   . GLY B 454 ? 0.379 0.496 0.368 0.029  -0.018 -0.088 454 GLY BBB C   
7092  O O   . GLY B 454 ? 0.408 0.528 0.394 0.034  -0.022 -0.092 454 GLY BBB O   
7093  N N   . PHE B 455 ? 0.346 0.455 0.332 0.025  -0.015 -0.080 455 PHE BBB N   
7094  C CA  . PHE B 455 ? 0.332 0.435 0.308 0.025  -0.014 -0.074 455 PHE BBB CA  
7095  C C   . PHE B 455 ? 0.325 0.421 0.290 0.024  -0.013 -0.066 455 PHE BBB C   
7096  O O   . PHE B 455 ? 0.322 0.416 0.291 0.020  -0.010 -0.064 455 PHE BBB O   
7097  C CB  . PHE B 455 ? 0.324 0.424 0.308 0.019  -0.012 -0.071 455 PHE BBB CB  
7098  C CG  . PHE B 455 ? 0.316 0.409 0.291 0.018  -0.011 -0.064 455 PHE BBB CG  
7099  C CD1 . PHE B 455 ? 0.310 0.397 0.279 0.016  -0.008 -0.057 455 PHE BBB CD1 
7100  C CD2 . PHE B 455 ? 0.309 0.402 0.283 0.020  -0.012 -0.065 455 PHE BBB CD2 
7101  C CE1 . PHE B 455 ? 0.296 0.376 0.258 0.015  -0.007 -0.051 455 PHE BBB CE1 
7102  C CE2 . PHE B 455 ? 0.307 0.394 0.274 0.018  -0.011 -0.058 455 PHE BBB CE2 
7103  C CZ  . PHE B 455 ? 0.302 0.383 0.263 0.016  -0.009 -0.052 455 PHE BBB CZ  
7104  N N   . HIS B 456 ? 0.330 0.422 0.282 0.028  -0.014 -0.063 456 HIS BBB N   
7105  C CA  . HIS B 456 ? 0.342 0.427 0.283 0.029  -0.012 -0.057 456 HIS BBB CA  
7106  C C   . HIS B 456 ? 0.339 0.418 0.270 0.029  -0.011 -0.051 456 HIS BBB C   
7107  O O   . HIS B 456 ? 0.365 0.444 0.291 0.033  -0.013 -0.053 456 HIS BBB O   
7108  C CB  . HIS B 456 ? 0.356 0.444 0.289 0.035  -0.014 -0.060 456 HIS BBB CB  
7109  C CG  . HIS B 456 ? 0.348 0.442 0.290 0.034  -0.014 -0.066 456 HIS BBB CG  
7110  N ND1 . HIS B 456 ? 0.345 0.438 0.289 0.031  -0.012 -0.064 456 HIS BBB ND1 
7111  C CD2 . HIS B 456 ? 0.349 0.452 0.302 0.036  -0.017 -0.074 456 HIS BBB CD2 
7112  C CE1 . HIS B 456 ? 0.352 0.452 0.306 0.031  -0.013 -0.070 456 HIS BBB CE1 
7113  N NE2 . HIS B 456 ? 0.350 0.457 0.309 0.034  -0.016 -0.077 456 HIS BBB NE2 
7114  N N   . PHE B 457 ? 0.332 0.404 0.259 0.025  -0.007 -0.045 457 PHE BBB N   
7115  C CA  . PHE B 457 ? 0.322 0.387 0.240 0.025  -0.006 -0.040 457 PHE BBB CA  
7116  C C   . PHE B 457 ? 0.325 0.384 0.236 0.024  -0.003 -0.034 457 PHE BBB C   
7117  O O   . PHE B 457 ? 0.324 0.382 0.241 0.019  -0.000 -0.033 457 PHE BBB O   
7118  C CB  . PHE B 457 ? 0.312 0.377 0.237 0.021  -0.006 -0.038 457 PHE BBB CB  
7119  C CG  . PHE B 457 ? 0.323 0.381 0.239 0.022  -0.004 -0.033 457 PHE BBB CG  
7120  C CD1 . PHE B 457 ? 0.331 0.388 0.241 0.026  -0.007 -0.034 457 PHE BBB CD1 
7121  C CD2 . PHE B 457 ? 0.321 0.373 0.235 0.018  -0.001 -0.028 457 PHE BBB CD2 
7122  C CE1 . PHE B 457 ? 0.335 0.385 0.235 0.027  -0.005 -0.030 457 PHE BBB CE1 
7123  C CE2 . PHE B 457 ? 0.324 0.370 0.230 0.018  0.000  -0.024 457 PHE BBB CE2 
7124  C CZ  . PHE B 457 ? 0.324 0.369 0.223 0.023  -0.001 -0.025 457 PHE BBB CZ  
7125  N N   . VAL B 458 ? 0.330 0.384 0.229 0.028  -0.002 -0.032 458 VAL BBB N   
7126  C CA  . VAL B 458 ? 0.341 0.388 0.232 0.027  0.002  -0.027 458 VAL BBB CA  
7127  C C   . VAL B 458 ? 0.349 0.389 0.234 0.026  0.004  -0.023 458 VAL BBB C   
7128  O O   . VAL B 458 ? 0.369 0.409 0.249 0.030  0.001  -0.024 458 VAL BBB O   
7129  C CB  . VAL B 458 ? 0.349 0.393 0.228 0.032  0.003  -0.027 458 VAL BBB CB  
7130  C CG1 . VAL B 458 ? 0.355 0.390 0.226 0.031  0.008  -0.022 458 VAL BBB CG1 
7131  C CG2 . VAL B 458 ? 0.345 0.395 0.229 0.033  0.001  -0.032 458 VAL BBB CG2 
7132  N N   . GLY B 459 ? 0.332 0.368 0.219 0.021  0.007  -0.019 459 GLY BBB N   
7133  C CA  . GLY B 459 ? 0.332 0.362 0.215 0.020  0.009  -0.015 459 GLY BBB CA  
7134  C C   . GLY B 459 ? 0.321 0.351 0.211 0.013  0.011  -0.013 459 GLY BBB C   
7135  O O   . GLY B 459 ? 0.313 0.346 0.211 0.010  0.011  -0.014 459 GLY BBB O   
7136  N N   . PRO B 460 ? 0.317 0.343 0.206 0.012  0.012  -0.010 460 PRO BBB N   
7137  C CA  . PRO B 460 ? 0.323 0.349 0.219 0.006  0.014  -0.008 460 PRO BBB CA  
7138  C C   . PRO B 460 ? 0.321 0.354 0.228 0.004  0.011  -0.010 460 PRO BBB C   
7139  O O   . PRO B 460 ? 0.355 0.391 0.263 0.006  0.008  -0.013 460 PRO BBB O   
7140  C CB  . PRO B 460 ? 0.316 0.337 0.207 0.006  0.015  -0.005 460 PRO BBB CB  
7141  C CG  . PRO B 460 ? 0.331 0.348 0.212 0.011  0.016  -0.005 460 PRO BBB CG  
7142  C CD  . PRO B 460 ? 0.333 0.354 0.213 0.015  0.013  -0.008 460 PRO BBB CD  
7143  N N   . ASN B 461 ? 0.329 0.364 0.243 -0.000 0.012  -0.010 461 ASN BBB N   
7144  C CA  . ASN B 461 ? 0.324 0.363 0.246 -0.003 0.010  -0.011 461 ASN BBB CA  
7145  C C   . ASN B 461 ? 0.329 0.373 0.255 -0.000 0.008  -0.015 461 ASN BBB C   
7146  O O   . ASN B 461 ? 0.346 0.393 0.277 -0.000 0.006  -0.017 461 ASN BBB O   
7147  C CB  . ASN B 461 ? 0.334 0.372 0.256 -0.003 0.010  -0.010 461 ASN BBB CB  
7148  C CG  . ASN B 461 ? 0.348 0.381 0.265 -0.004 0.012  -0.007 461 ASN BBB CG  
7149  O OD1 . ASN B 461 ? 0.374 0.407 0.293 -0.007 0.014  -0.005 461 ASN BBB OD1 
7150  N ND2 . ASN B 461 ? 0.354 0.383 0.265 -0.002 0.012  -0.006 461 ASN BBB ND2 
7151  N N   . ALA B 462 ? 0.314 0.359 0.240 0.001  0.008  -0.016 462 ALA BBB N   
7152  C CA  . ALA B 462 ? 0.314 0.364 0.243 0.004  0.006  -0.021 462 ALA BBB CA  
7153  C C   . ALA B 462 ? 0.297 0.351 0.236 0.001  0.005  -0.023 462 ALA BBB C   
7154  O O   . ALA B 462 ? 0.290 0.349 0.235 0.002  0.003  -0.026 462 ALA BBB O   
7155  C CB  . ALA B 462 ? 0.320 0.370 0.244 0.007  0.006  -0.022 462 ALA BBB CB  
7156  N N   . GLY B 463 ? 0.303 0.356 0.246 -0.002 0.007  -0.020 463 GLY BBB N   
7157  C CA  . GLY B 463 ? 0.312 0.368 0.265 -0.005 0.007  -0.021 463 GLY BBB CA  
7158  C C   . GLY B 463 ? 0.314 0.370 0.270 -0.006 0.007  -0.021 463 GLY BBB C   
7159  O O   . GLY B 463 ? 0.304 0.363 0.268 -0.006 0.007  -0.023 463 GLY BBB O   
7160  N N   . GLU B 464 ? 0.336 0.389 0.287 -0.007 0.007  -0.018 464 GLU BBB N   
7161  C CA  . GLU B 464 ? 0.345 0.397 0.298 -0.008 0.007  -0.017 464 GLU BBB CA  
7162  C C   . GLU B 464 ? 0.358 0.413 0.313 -0.005 0.005  -0.021 464 GLU BBB C   
7163  O O   . GLU B 464 ? 0.356 0.413 0.317 -0.006 0.005  -0.022 464 GLU BBB O   
7164  C CB  . GLU B 464 ? 0.358 0.406 0.305 -0.008 0.008  -0.013 464 GLU BBB CB  
7165  C CG  . GLU B 464 ? 0.369 0.416 0.316 -0.011 0.010  -0.010 464 GLU BBB CG  
7166  C CD  . GLU B 464 ? 0.379 0.427 0.331 -0.013 0.011  -0.009 464 GLU BBB CD  
7167  O OE1 . GLU B 464 ? 0.381 0.430 0.338 -0.013 0.010  -0.010 464 GLU BBB OE1 
7168  O OE2 . GLU B 464 ? 0.427 0.474 0.379 -0.014 0.012  -0.008 464 GLU BBB OE2 
7169  N N   . ILE B 465 ? 0.360 0.415 0.310 -0.002 0.004  -0.023 465 ILE BBB N   
7170  C CA  . ILE B 465 ? 0.336 0.395 0.287 0.001  0.001  -0.027 465 ILE BBB CA  
7171  C C   . ILE B 465 ? 0.318 0.382 0.278 0.001  0.001  -0.032 465 ILE BBB C   
7172  O O   . ILE B 465 ? 0.339 0.406 0.305 0.002  -0.000 -0.036 465 ILE BBB O   
7173  C CB  . ILE B 465 ? 0.339 0.396 0.280 0.006  -0.000 -0.027 465 ILE BBB CB  
7174  C CG1 . ILE B 465 ? 0.353 0.405 0.287 0.005  0.001  -0.023 465 ILE BBB CG1 
7175  C CG2 . ILE B 465 ? 0.332 0.393 0.274 0.010  -0.003 -0.033 465 ILE BBB CG2 
7176  C CD1 . ILE B 465 ? 0.382 0.430 0.304 0.009  0.001  -0.022 465 ILE BBB CD1 
7177  N N   . THR B 466 ? 0.291 0.355 0.252 0.001  0.002  -0.032 466 THR BBB N   
7178  C CA  . THR B 466 ? 0.282 0.351 0.250 0.002  0.001  -0.037 466 THR BBB CA  
7179  C C   . THR B 466 ? 0.277 0.348 0.256 -0.002 0.003  -0.038 466 THR BBB C   
7180  O O   . THR B 466 ? 0.276 0.351 0.263 -0.001 0.002  -0.043 466 THR BBB O   
7181  C CB  . THR B 466 ? 0.280 0.350 0.246 0.002  0.001  -0.037 466 THR BBB CB  
7182  O OG1 . THR B 466 ? 0.276 0.345 0.232 0.006  -0.000 -0.037 466 THR BBB OG1 
7183  C CG2 . THR B 466 ? 0.272 0.347 0.246 0.002  0.001  -0.042 466 THR BBB CG2 
7184  N N   . GLN B 467 ? 0.277 0.344 0.256 -0.005 0.005  -0.033 467 GLN BBB N   
7185  C CA  . GLN B 467 ? 0.274 0.341 0.262 -0.008 0.007  -0.033 467 GLN BBB CA  
7186  C C   . GLN B 467 ? 0.294 0.364 0.289 -0.008 0.007  -0.037 467 GLN BBB C   
7187  O O   . GLN B 467 ? 0.329 0.402 0.333 -0.008 0.008  -0.041 467 GLN BBB O   
7188  C CB  . GLN B 467 ? 0.276 0.338 0.261 -0.010 0.009  -0.027 467 GLN BBB CB  
7189  C CG  . GLN B 467 ? 0.273 0.335 0.266 -0.012 0.012  -0.026 467 GLN BBB CG  
7190  C CD  . GLN B 467 ? 0.282 0.345 0.279 -0.013 0.013  -0.027 467 GLN BBB CD  
7191  O OE1 . GLN B 467 ? 0.262 0.324 0.255 -0.013 0.013  -0.024 467 GLN BBB OE1 
7192  N NE2 . GLN B 467 ? 0.279 0.345 0.283 -0.012 0.013  -0.032 467 GLN BBB NE2 
7193  N N   . GLY B 468 ? 0.281 0.350 0.273 -0.007 0.006  -0.037 468 GLY BBB N   
7194  C CA  . GLY B 468 ? 0.273 0.344 0.272 -0.007 0.007  -0.040 468 GLY BBB CA  
7195  C C   . GLY B 468 ? 0.267 0.343 0.270 -0.005 0.005  -0.048 468 GLY BBB C   
7196  O O   . GLY B 468 ? 0.296 0.375 0.309 -0.006 0.006  -0.052 468 GLY BBB O   
7197  N N   . PHE B 469 ? 0.270 0.349 0.267 -0.001 0.002  -0.049 469 PHE BBB N   
7198  C CA  . PHE B 469 ? 0.270 0.355 0.270 0.002  -0.001 -0.056 469 PHE BBB CA  
7199  C C   . PHE B 469 ? 0.281 0.369 0.289 0.001  0.000  -0.059 469 PHE BBB C   
7200  O O   . PHE B 469 ? 0.308 0.401 0.325 0.002  -0.000 -0.066 469 PHE BBB O   
7201  C CB  . PHE B 469 ? 0.265 0.349 0.253 0.006  -0.004 -0.055 469 PHE BBB CB  
7202  C CG  . PHE B 469 ? 0.253 0.336 0.235 0.009  -0.006 -0.055 469 PHE BBB CG  
7203  C CD1 . PHE B 469 ? 0.245 0.333 0.233 0.010  -0.008 -0.061 469 PHE BBB CD1 
7204  C CD2 . PHE B 469 ? 0.242 0.320 0.214 0.009  -0.006 -0.049 469 PHE BBB CD2 
7205  C CE1 . PHE B 469 ? 0.241 0.328 0.224 0.013  -0.010 -0.060 469 PHE BBB CE1 
7206  C CE2 . PHE B 469 ? 0.243 0.319 0.209 0.011  -0.008 -0.048 469 PHE BBB CE2 
7207  C CZ  . PHE B 469 ? 0.245 0.326 0.217 0.013  -0.010 -0.054 469 PHE BBB CZ  
7208  N N   . SER B 470 ? 0.288 0.372 0.295 -0.001 0.002  -0.055 470 SER BBB N   
7209  C CA  . SER B 470 ? 0.289 0.376 0.304 -0.002 0.004  -0.058 470 SER BBB CA  
7210  C C   . SER B 470 ? 0.298 0.385 0.325 -0.005 0.007  -0.061 470 SER BBB C   
7211  O O   . SER B 470 ? 0.323 0.416 0.360 -0.005 0.007  -0.067 470 SER BBB O   
7212  C CB  . SER B 470 ? 0.274 0.357 0.285 -0.004 0.005  -0.053 470 SER BBB CB  
7213  O OG  . SER B 470 ? 0.267 0.345 0.279 -0.007 0.008  -0.048 470 SER BBB OG  
7214  N N   . LEU B 471 ? 0.301 0.384 0.328 -0.008 0.009  -0.057 471 LEU BBB N   
7215  C CA  . LEU B 471 ? 0.327 0.410 0.366 -0.010 0.013  -0.060 471 LEU BBB CA  
7216  C C   . LEU B 471 ? 0.334 0.424 0.380 -0.009 0.011  -0.068 471 LEU BBB C   
7217  O O   . LEU B 471 ? 0.322 0.414 0.378 -0.010 0.013  -0.073 471 LEU BBB O   
7218  C CB  . LEU B 471 ? 0.328 0.406 0.364 -0.012 0.015  -0.054 471 LEU BBB CB  
7219  C CG  . LEU B 471 ? 0.337 0.413 0.383 -0.015 0.020  -0.056 471 LEU BBB CG  
7220  C CD1 . LEU B 471 ? 0.358 0.434 0.412 -0.016 0.023  -0.058 471 LEU BBB CD1 
7221  C CD2 . LEU B 471 ? 0.339 0.409 0.381 -0.016 0.022  -0.049 471 LEU BBB CD2 
7222  N N   . ALA B 472 ? 0.356 0.446 0.394 -0.006 0.008  -0.068 472 ALA BBB N   
7223  C CA  . ALA B 472 ? 0.353 0.450 0.398 -0.004 0.006  -0.076 472 ALA BBB CA  
7224  C C   . ALA B 472 ? 0.347 0.451 0.397 -0.001 0.003  -0.083 472 ALA BBB C   
7225  O O   . ALA B 472 ? 0.326 0.435 0.387 -0.002 0.004  -0.091 472 ALA BBB O   
7226  C CB  . ALA B 472 ? 0.341 0.437 0.375 -0.001 0.002  -0.074 472 ALA BBB CB  
7227  N N   . VAL B 473 ? 0.350 0.454 0.393 0.001  0.001  -0.081 473 VAL BBB N   
7228  C CA  . VAL B 473 ? 0.374 0.485 0.420 0.003  -0.001 -0.088 473 VAL BBB CA  
7229  C C   . VAL B 473 ? 0.401 0.513 0.461 -0.000 0.003  -0.092 473 VAL BBB C   
7230  O O   . VAL B 473 ? 0.464 0.584 0.534 0.001  0.002  -0.101 473 VAL BBB O   
7231  C CB  . VAL B 473 ? 0.356 0.466 0.390 0.006  -0.004 -0.085 473 VAL BBB CB  
7232  C CG1 . VAL B 473 ? 0.371 0.487 0.410 0.009  -0.005 -0.091 473 VAL BBB CG1 
7233  C CG2 . VAL B 473 ? 0.351 0.460 0.373 0.011  -0.007 -0.083 473 VAL BBB CG2 
7234  N N   . LYS B 474 ? 0.414 0.520 0.475 -0.004 0.007  -0.085 474 LYS BBB N   
7235  C CA  . LYS B 474 ? 0.421 0.526 0.493 -0.007 0.012  -0.088 474 LYS BBB CA  
7236  C C   . LYS B 474 ? 0.388 0.495 0.473 -0.009 0.015  -0.094 474 LYS BBB C   
7237  O O   . LYS B 474 ? 0.364 0.475 0.461 -0.010 0.017  -0.100 474 LYS BBB O   
7238  C CB  . LYS B 474 ? 0.423 0.520 0.491 -0.010 0.015  -0.079 474 LYS BBB CB  
7239  C CG  . LYS B 474 ? 0.440 0.536 0.519 -0.013 0.020  -0.080 474 LYS BBB CG  
7240  C CD  . LYS B 474 ? 0.455 0.543 0.530 -0.015 0.023  -0.071 474 LYS BBB CD  
7241  C CE  . LYS B 474 ? 0.463 0.549 0.546 -0.017 0.028  -0.073 474 LYS BBB CE  
7242  N NZ  . LYS B 474 ? 0.456 0.535 0.535 -0.019 0.031  -0.064 474 LYS BBB NZ  
7243  N N   . LEU B 475 ? 0.377 0.483 0.460 -0.009 0.015  -0.092 475 LEU BBB N   
7244  C CA  . LEU B 475 ? 0.378 0.486 0.473 -0.011 0.018  -0.098 475 LEU BBB CA  
7245  C C   . LEU B 475 ? 0.357 0.475 0.459 -0.008 0.014  -0.109 475 LEU BBB C   
7246  O O   . LEU B 475 ? 0.350 0.470 0.463 -0.010 0.016  -0.115 475 LEU BBB O   
7247  C CB  . LEU B 475 ? 0.379 0.481 0.468 -0.013 0.019  -0.092 475 LEU BBB CB  
7248  C CG  . LEU B 475 ? 0.373 0.466 0.459 -0.016 0.024  -0.083 475 LEU BBB CG  
7249  C CD1 . LEU B 475 ? 0.358 0.445 0.437 -0.017 0.025  -0.078 475 LEU BBB CD1 
7250  C CD2 . LEU B 475 ? 0.377 0.468 0.476 -0.019 0.030  -0.086 475 LEU BBB CD2 
7251  N N   . GLY B 476 ? 0.369 0.492 0.464 -0.004 0.008  -0.111 476 GLY BBB N   
7252  C CA  . GLY B 476 ? 0.350 0.483 0.451 -0.000 0.004  -0.122 476 GLY BBB CA  
7253  C C   . GLY B 476 ? 0.358 0.494 0.452 0.004  -0.001 -0.123 476 GLY BBB C   
7254  O O   . GLY B 476 ? 0.387 0.531 0.490 0.006  -0.002 -0.133 476 GLY BBB O   
7255  N N   . ALA B 477 ? 0.351 0.481 0.430 0.005  -0.003 -0.115 477 ALA BBB N   
7256  C CA  . ALA B 477 ? 0.357 0.488 0.427 0.010  -0.007 -0.115 477 ALA BBB CA  
7257  C C   . ALA B 477 ? 0.352 0.493 0.420 0.016  -0.013 -0.122 477 ALA BBB C   
7258  O O   . ALA B 477 ? 0.353 0.495 0.417 0.018  -0.014 -0.123 477 ALA BBB O   
7259  C CB  . ALA B 477 ? 0.354 0.477 0.408 0.010  -0.007 -0.104 477 ALA BBB CB  
7260  N N   . THR B 478 ? 0.359 0.505 0.429 0.019  -0.016 -0.129 478 THR BBB N   
7261  C CA  . THR B 478 ? 0.364 0.519 0.431 0.027  -0.022 -0.136 478 THR BBB CA  
7262  C C   . THR B 478 ? 0.365 0.516 0.415 0.032  -0.026 -0.131 478 THR BBB C   
7263  O O   . THR B 478 ? 0.326 0.470 0.370 0.029  -0.024 -0.123 478 THR BBB O   
7264  C CB  . THR B 478 ? 0.376 0.541 0.458 0.028  -0.024 -0.148 478 THR BBB CB  
7265  O OG1 . THR B 478 ? 0.379 0.540 0.459 0.027  -0.023 -0.146 478 THR BBB OG1 
7266  C CG2 . THR B 478 ? 0.383 0.551 0.483 0.022  -0.019 -0.155 478 THR BBB CG2 
7267  N N   . LYS B 479 ? 0.372 0.528 0.414 0.039  -0.032 -0.135 479 LYS BBB N   
7268  C CA  . LYS B 479 ? 0.394 0.547 0.420 0.044  -0.035 -0.131 479 LYS BBB CA  
7269  C C   . LYS B 479 ? 0.373 0.526 0.402 0.044  -0.036 -0.132 479 LYS BBB C   
7270  O O   . LYS B 479 ? 0.369 0.515 0.387 0.045  -0.036 -0.125 479 LYS BBB O   
7271  C CB  . LYS B 479 ? 0.420 0.578 0.438 0.053  -0.041 -0.136 479 LYS BBB CB  
7272  C CG  . LYS B 479 ? 0.442 0.596 0.442 0.059  -0.044 -0.131 479 LYS BBB CG  
7273  C CD  . LYS B 479 ? 0.451 0.592 0.438 0.056  -0.041 -0.118 479 LYS BBB CD  
7274  C CE  . LYS B 479 ? 0.473 0.610 0.442 0.063  -0.044 -0.113 479 LYS BBB CE  
7275  N NZ  . LYS B 479 ? 0.491 0.630 0.457 0.068  -0.047 -0.117 479 LYS BBB NZ  
7276  N N   . LYS B 480 ? 0.385 0.546 0.431 0.042  -0.036 -0.141 480 LYS BBB N   
7277  C CA  . LYS B 480 ? 0.411 0.572 0.461 0.042  -0.036 -0.144 480 LYS BBB CA  
7278  C C   . LYS B 480 ? 0.401 0.553 0.450 0.035  -0.030 -0.134 480 LYS BBB C   
7279  O O   . LYS B 480 ? 0.393 0.540 0.433 0.036  -0.031 -0.129 480 LYS BBB O   
7280  C CB  . LYS B 480 ? 0.407 0.579 0.476 0.041  -0.036 -0.157 480 LYS BBB CB  
7281  C CG  . LYS B 480 ? 0.411 0.585 0.488 0.039  -0.035 -0.159 480 LYS BBB CG  
7282  C CD  . LYS B 480 ? 0.449 0.635 0.540 0.042  -0.038 -0.173 480 LYS BBB CD  
7283  C CE  . LYS B 480 ? 0.452 0.639 0.555 0.038  -0.035 -0.177 480 LYS BBB CE  
7284  N NZ  . LYS B 480 ? 0.439 0.618 0.531 0.038  -0.035 -0.169 480 LYS BBB NZ  
7285  N N   . ASP B 481 ? 0.409 0.556 0.463 0.029  -0.025 -0.130 481 ASP BBB N   
7286  C CA  . ASP B 481 ? 0.408 0.545 0.460 0.022  -0.020 -0.121 481 ASP BBB CA  
7287  C C   . ASP B 481 ? 0.391 0.521 0.426 0.024  -0.021 -0.111 481 ASP BBB C   
7288  O O   . ASP B 481 ? 0.379 0.503 0.410 0.022  -0.020 -0.105 481 ASP BBB O   
7289  C CB  . ASP B 481 ? 0.415 0.550 0.475 0.017  -0.015 -0.118 481 ASP BBB CB  
7290  C CG  . ASP B 481 ? 0.430 0.571 0.508 0.014  -0.012 -0.128 481 ASP BBB CG  
7291  O OD1 . ASP B 481 ? 0.438 0.583 0.523 0.014  -0.012 -0.133 481 ASP BBB OD1 
7292  O OD2 . ASP B 481 ? 0.475 0.617 0.559 0.012  -0.010 -0.129 481 ASP BBB OD2 
7293  N N   . PHE B 482 ? 0.379 0.509 0.404 0.028  -0.024 -0.109 482 PHE BBB N   
7294  C CA  . PHE B 482 ? 0.390 0.511 0.398 0.030  -0.025 -0.100 482 PHE BBB CA  
7295  C C   . PHE B 482 ? 0.417 0.538 0.417 0.035  -0.029 -0.100 482 PHE BBB C   
7296  O O   . PHE B 482 ? 0.425 0.539 0.417 0.034  -0.027 -0.093 482 PHE BBB O   
7297  C CB  . PHE B 482 ? 0.377 0.498 0.377 0.034  -0.027 -0.099 482 PHE BBB CB  
7298  C CG  . PHE B 482 ? 0.359 0.476 0.361 0.029  -0.022 -0.093 482 PHE BBB CG  
7299  C CD1 . PHE B 482 ? 0.366 0.486 0.380 0.025  -0.020 -0.098 482 PHE BBB CD1 
7300  C CD2 . PHE B 482 ? 0.345 0.453 0.334 0.028  -0.021 -0.084 482 PHE BBB CD2 
7301  C CE1 . PHE B 482 ? 0.345 0.462 0.359 0.021  -0.017 -0.093 482 PHE BBB CE1 
7302  C CE2 . PHE B 482 ? 0.336 0.441 0.327 0.023  -0.018 -0.080 482 PHE BBB CE2 
7303  C CZ  . PHE B 482 ? 0.336 0.445 0.338 0.020  -0.016 -0.084 482 PHE BBB CZ  
7304  N N   . ASP B 483 ? 0.421 0.551 0.425 0.041  -0.033 -0.109 483 ASP BBB N   
7305  C CA  . ASP B 483 ? 0.409 0.540 0.405 0.046  -0.037 -0.111 483 ASP BBB CA  
7306  C C   . ASP B 483 ? 0.400 0.530 0.403 0.042  -0.035 -0.110 483 ASP BBB C   
7307  O O   . ASP B 483 ? 0.454 0.579 0.448 0.045  -0.036 -0.107 483 ASP BBB O   
7308  C CB  . ASP B 483 ? 0.413 0.554 0.413 0.053  -0.042 -0.122 483 ASP BBB CB  
7309  C CG  . ASP B 483 ? 0.417 0.560 0.407 0.059  -0.045 -0.122 483 ASP BBB CG  
7310  O OD1 . ASP B 483 ? 0.428 0.562 0.406 0.059  -0.043 -0.113 483 ASP BBB OD1 
7311  O OD2 . ASP B 483 ? 0.405 0.558 0.400 0.065  -0.049 -0.132 483 ASP BBB OD2 
7312  N N   . ASP B 484 ? 0.367 0.499 0.385 0.036  -0.031 -0.113 484 ASP BBB N   
7313  C CA  . ASP B 484 ? 0.376 0.507 0.401 0.032  -0.028 -0.113 484 ASP BBB CA  
7314  C C   . ASP B 484 ? 0.369 0.489 0.389 0.026  -0.024 -0.103 484 ASP BBB C   
7315  O O   . ASP B 484 ? 0.348 0.466 0.372 0.023  -0.021 -0.101 484 ASP BBB O   
7316  C CB  . ASP B 484 ? 0.391 0.528 0.434 0.029  -0.026 -0.122 484 ASP BBB CB  
7317  C CG  . ASP B 484 ? 0.408 0.556 0.458 0.034  -0.031 -0.134 484 ASP BBB CG  
7318  O OD1 . ASP B 484 ? 0.411 0.562 0.451 0.041  -0.036 -0.136 484 ASP BBB OD1 
7319  O OD2 . ASP B 484 ? 0.423 0.578 0.490 0.031  -0.029 -0.142 484 ASP BBB OD2 
7320  N N   . MET B 485 ? 0.371 0.486 0.383 0.025  -0.022 -0.096 485 MET BBB N   
7321  C CA  . MET B 485 ? 0.344 0.449 0.351 0.020  -0.018 -0.086 485 MET BBB CA  
7322  C C   . MET B 485 ? 0.323 0.423 0.317 0.022  -0.020 -0.080 485 MET BBB C   
7323  O O   . MET B 485 ? 0.310 0.410 0.294 0.027  -0.023 -0.079 485 MET BBB O   
7324  C CB  . MET B 485 ? 0.345 0.448 0.347 0.019  -0.017 -0.081 485 MET BBB CB  
7325  C CG  . MET B 485 ? 0.353 0.447 0.347 0.016  -0.014 -0.072 485 MET BBB CG  
7326  S SD  . MET B 485 ? 0.347 0.437 0.335 0.015  -0.013 -0.067 485 MET BBB SD  
7327  C CE  . MET B 485 ? 0.348 0.441 0.326 0.023  -0.018 -0.070 485 MET BBB CE  
7328  N N   . ILE B 486 ? 0.329 0.424 0.325 0.018  -0.017 -0.076 486 ILE BBB N   
7329  C CA  . ILE B 486 ? 0.328 0.418 0.314 0.019  -0.017 -0.070 486 ILE BBB CA  
7330  C C   . ILE B 486 ? 0.344 0.427 0.319 0.017  -0.016 -0.062 486 ILE BBB C   
7331  O O   . ILE B 486 ? 0.316 0.397 0.295 0.013  -0.012 -0.059 486 ILE BBB O   
7332  C CB  . ILE B 486 ? 0.337 0.425 0.327 0.015  -0.015 -0.068 486 ILE BBB CB  
7333  C CG1 . ILE B 486 ? 0.341 0.436 0.343 0.015  -0.015 -0.077 486 ILE BBB CG1 
7334  C CG2 . ILE B 486 ? 0.318 0.401 0.298 0.016  -0.016 -0.063 486 ILE BBB CG2 
7335  C CD1 . ILE B 486 ? 0.343 0.442 0.342 0.021  -0.020 -0.082 486 ILE BBB CD1 
7336  N N   . GLY B 487 ? 0.345 0.425 0.309 0.021  -0.018 -0.058 487 GLY BBB N   
7337  C CA  . GLY B 487 ? 0.335 0.408 0.288 0.021  -0.016 -0.051 487 GLY BBB CA  
7338  C C   . GLY B 487 ? 0.336 0.403 0.287 0.017  -0.013 -0.045 487 GLY BBB C   
7339  O O   . GLY B 487 ? 0.324 0.391 0.277 0.016  -0.013 -0.046 487 GLY BBB O   
7340  N N   . ILE B 488 ? 0.321 0.383 0.268 0.014  -0.011 -0.039 488 ILE BBB N   
7341  C CA  . ILE B 488 ? 0.331 0.387 0.273 0.011  -0.008 -0.033 488 ILE BBB CA  
7342  C C   . ILE B 488 ? 0.352 0.404 0.282 0.015  -0.009 -0.030 488 ILE BBB C   
7343  O O   . ILE B 488 ? 0.352 0.403 0.277 0.017  -0.009 -0.030 488 ILE BBB O   
7344  C CB  . ILE B 488 ? 0.310 0.364 0.254 0.006  -0.005 -0.029 488 ILE BBB CB  
7345  C CG1 . ILE B 488 ? 0.296 0.354 0.252 0.003  -0.004 -0.032 488 ILE BBB CG1 
7346  C CG2 . ILE B 488 ? 0.322 0.372 0.263 0.004  -0.003 -0.024 488 ILE BBB CG2 
7347  C CD1 . ILE B 488 ? 0.288 0.345 0.247 -0.001 -0.001 -0.029 488 ILE BBB CD1 
7348  N N   . HIS B 489 ? 0.360 0.408 0.285 0.016  -0.009 -0.028 489 HIS BBB N   
7349  C CA  . HIS B 489 ? 0.388 0.430 0.301 0.019  -0.009 -0.025 489 HIS BBB CA  
7350  C C   . HIS B 489 ? 0.382 0.419 0.292 0.016  -0.006 -0.020 489 HIS BBB C   
7351  O O   . HIS B 489 ? 0.388 0.426 0.303 0.012  -0.006 -0.019 489 HIS BBB O   
7352  C CB  . HIS B 489 ? 0.420 0.464 0.330 0.024  -0.012 -0.028 489 HIS BBB CB  
7353  C CG  . HIS B 489 ? 0.469 0.507 0.367 0.029  -0.012 -0.026 489 HIS BBB CG  
7354  N ND1 . HIS B 489 ? 0.511 0.546 0.401 0.033  -0.012 -0.025 489 HIS BBB ND1 
7355  C CD2 . HIS B 489 ? 0.495 0.528 0.386 0.031  -0.012 -0.024 489 HIS BBB CD2 
7356  C CE1 . HIS B 489 ? 0.554 0.584 0.434 0.037  -0.012 -0.022 489 HIS BBB CE1 
7357  N NE2 . HIS B 489 ? 0.539 0.567 0.419 0.036  -0.012 -0.021 489 HIS BBB NE2 
7358  N N   . PRO B 490 ? 0.361 0.392 0.263 0.016  -0.004 -0.016 490 PRO BBB N   
7359  C CA  . PRO B 490 ? 0.362 0.391 0.257 0.020  -0.004 -0.016 490 PRO BBB CA  
7360  C C   . PRO B 490 ? 0.349 0.380 0.248 0.016  -0.003 -0.015 490 PRO BBB C   
7361  O O   . PRO B 490 ? 0.350 0.379 0.252 0.012  0.000  -0.012 490 PRO BBB O   
7362  C CB  . PRO B 490 ? 0.373 0.395 0.258 0.021  -0.002 -0.011 490 PRO BBB CB  
7363  C CG  . PRO B 490 ? 0.379 0.399 0.266 0.018  -0.001 -0.009 490 PRO BBB CG  
7364  C CD  . PRO B 490 ? 0.366 0.391 0.264 0.014  -0.001 -0.011 490 PRO BBB CD  
7365  N N   . THR B 491 ? 0.328 0.364 0.231 0.018  -0.005 -0.019 491 THR BBB N   
7366  C CA  . THR B 491 ? 0.331 0.368 0.236 0.016  -0.003 -0.018 491 THR BBB CA  
7367  C C   . THR B 491 ? 0.335 0.373 0.235 0.021  -0.004 -0.020 491 THR BBB C   
7368  O O   . THR B 491 ? 0.335 0.374 0.230 0.026  -0.007 -0.022 491 THR BBB O   
7369  C CB  . THR B 491 ? 0.322 0.365 0.240 0.012  -0.004 -0.021 491 THR BBB CB  
7370  O OG1 . THR B 491 ? 0.317 0.366 0.239 0.015  -0.007 -0.027 491 THR BBB OG1 
7371  C CG2 . THR B 491 ? 0.314 0.357 0.237 0.008  -0.003 -0.019 491 THR BBB CG2 
7372  N N   . ASP B 492 ? 0.324 0.362 0.225 0.019  -0.003 -0.020 492 ASP BBB N   
7373  C CA  . ASP B 492 ? 0.322 0.362 0.219 0.024  -0.004 -0.022 492 ASP BBB CA  
7374  C C   . ASP B 492 ? 0.305 0.354 0.213 0.024  -0.007 -0.028 492 ASP BBB C   
7375  O O   . ASP B 492 ? 0.324 0.375 0.229 0.029  -0.010 -0.032 492 ASP BBB O   
7376  C CB  . ASP B 492 ? 0.325 0.362 0.220 0.022  -0.001 -0.019 492 ASP BBB CB  
7377  C CG  . ASP B 492 ? 0.348 0.377 0.232 0.022  0.002  -0.014 492 ASP BBB CG  
7378  O OD1 . ASP B 492 ? 0.354 0.379 0.231 0.026  0.001  -0.014 492 ASP BBB OD1 
7379  O OD2 . ASP B 492 ? 0.365 0.390 0.248 0.019  0.005  -0.012 492 ASP BBB OD2 
7380  N N   . ALA B 493 ? 0.285 0.336 0.203 0.019  -0.007 -0.029 493 ALA BBB N   
7381  C CA  . ALA B 493 ? 0.280 0.338 0.208 0.018  -0.008 -0.034 493 ALA BBB CA  
7382  C C   . ALA B 493 ? 0.297 0.360 0.229 0.021  -0.011 -0.039 493 ALA BBB C   
7383  O O   . ALA B 493 ? 0.283 0.352 0.222 0.022  -0.013 -0.045 493 ALA BBB O   
7384  C CB  . ALA B 493 ? 0.271 0.330 0.209 0.012  -0.006 -0.033 493 ALA BBB CB  
7385  N N   . GLU B 494 ? 0.310 0.370 0.237 0.023  -0.012 -0.038 494 GLU BBB N   
7386  C CA  . GLU B 494 ? 0.333 0.397 0.262 0.027  -0.015 -0.043 494 GLU BBB CA  
7387  C C   . GLU B 494 ? 0.338 0.407 0.262 0.034  -0.019 -0.048 494 GLU BBB C   
7388  O O   . GLU B 494 ? 0.324 0.398 0.252 0.037  -0.022 -0.054 494 GLU BBB O   
7389  C CB  . GLU B 494 ? 0.356 0.417 0.280 0.027  -0.015 -0.040 494 GLU BBB CB  
7390  C CG  . GLU B 494 ? 0.383 0.437 0.293 0.031  -0.015 -0.036 494 GLU BBB CG  
7391  C CD  . GLU B 494 ? 0.422 0.472 0.328 0.032  -0.015 -0.034 494 GLU BBB CD  
7392  O OE1 . GLU B 494 ? 0.446 0.501 0.358 0.033  -0.018 -0.039 494 GLU BBB OE1 
7393  O OE2 . GLU B 494 ? 0.437 0.480 0.335 0.031  -0.013 -0.028 494 GLU BBB OE2 
7394  N N   . VAL B 495 ? 0.346 0.410 0.261 0.036  -0.018 -0.045 495 VAL BBB N   
7395  C CA  . VAL B 495 ? 0.346 0.413 0.254 0.043  -0.021 -0.049 495 VAL BBB CA  
7396  C C   . VAL B 495 ? 0.339 0.416 0.259 0.043  -0.024 -0.057 495 VAL BBB C   
7397  O O   . VAL B 495 ? 0.354 0.437 0.274 0.049  -0.027 -0.063 495 VAL BBB O   
7398  C CB  . VAL B 495 ? 0.344 0.406 0.242 0.045  -0.019 -0.044 495 VAL BBB CB  
7399  C CG1 . VAL B 495 ? 0.338 0.403 0.243 0.041  -0.017 -0.045 495 VAL BBB CG1 
7400  C CG2 . VAL B 495 ? 0.357 0.419 0.244 0.053  -0.022 -0.047 495 VAL BBB CG2 
7401  N N   . PHE B 496 ? 0.328 0.407 0.259 0.037  -0.021 -0.057 496 PHE BBB N   
7402  C CA  . PHE B 496 ? 0.333 0.421 0.276 0.037  -0.023 -0.064 496 PHE BBB CA  
7403  C C   . PHE B 496 ? 0.355 0.449 0.307 0.038  -0.025 -0.071 496 PHE BBB C   
7404  O O   . PHE B 496 ? 0.388 0.490 0.350 0.039  -0.027 -0.079 496 PHE BBB O   
7405  C CB  . PHE B 496 ? 0.304 0.391 0.256 0.030  -0.019 -0.062 496 PHE BBB CB  
7406  C CG  . PHE B 496 ? 0.311 0.395 0.257 0.030  -0.018 -0.059 496 PHE BBB CG  
7407  C CD1 . PHE B 496 ? 0.310 0.400 0.257 0.034  -0.020 -0.064 496 PHE BBB CD1 
7408  C CD2 . PHE B 496 ? 0.300 0.376 0.239 0.027  -0.015 -0.052 496 PHE BBB CD2 
7409  C CE1 . PHE B 496 ? 0.321 0.407 0.262 0.034  -0.018 -0.061 496 PHE BBB CE1 
7410  C CE2 . PHE B 496 ? 0.315 0.389 0.250 0.027  -0.013 -0.049 496 PHE BBB CE2 
7411  C CZ  . PHE B 496 ? 0.322 0.401 0.257 0.030  -0.015 -0.053 496 PHE BBB CZ  
7412  N N   . GLY B 497 ? 0.360 0.452 0.308 0.039  -0.026 -0.070 497 GLY BBB N   
7413  C CA  . GLY B 497 ? 0.363 0.461 0.319 0.041  -0.029 -0.077 497 GLY BBB CA  
7414  C C   . GLY B 497 ? 0.377 0.479 0.326 0.049  -0.033 -0.081 497 GLY BBB C   
7415  O O   . GLY B 497 ? 0.359 0.467 0.315 0.051  -0.036 -0.088 497 GLY BBB O   
7416  N N   . ILE B 498 ? 0.402 0.499 0.336 0.054  -0.035 -0.078 498 ILE BBB N   
7417  C CA  . ILE B 498 ? 0.402 0.501 0.327 0.063  -0.039 -0.081 498 ILE BBB CA  
7418  C C   . ILE B 498 ? 0.408 0.507 0.324 0.069  -0.040 -0.081 498 ILE BBB C   
7419  O O   . ILE B 498 ? 0.402 0.497 0.303 0.076  -0.042 -0.079 498 ILE BBB O   
7420  C CB  . ILE B 498 ? 0.418 0.508 0.332 0.064  -0.038 -0.074 498 ILE BBB CB  
7421  C CG1 . ILE B 498 ? 0.432 0.512 0.336 0.061  -0.033 -0.064 498 ILE BBB CG1 
7422  C CG2 . ILE B 498 ? 0.404 0.495 0.326 0.060  -0.037 -0.075 498 ILE BBB CG2 
7423  C CD1 . ILE B 498 ? 0.444 0.514 0.334 0.064  -0.032 -0.058 498 ILE BBB CD1 
7424  N N   . LEU B 499 ? 0.407 0.510 0.330 0.066  -0.039 -0.083 499 LEU BBB N   
7425  C CA  . LEU B 499 ? 0.430 0.534 0.345 0.071  -0.041 -0.085 499 LEU BBB CA  
7426  C C   . LEU B 499 ? 0.483 0.598 0.401 0.079  -0.047 -0.095 499 LEU BBB C   
7427  O O   . LEU B 499 ? 0.500 0.623 0.433 0.077  -0.048 -0.102 499 LEU BBB O   
7428  C CB  . LEU B 499 ? 0.413 0.518 0.336 0.066  -0.038 -0.085 499 LEU BBB CB  
7429  C CG  . LEU B 499 ? 0.401 0.497 0.320 0.059  -0.033 -0.075 499 LEU BBB CG  
7430  C CD1 . LEU B 499 ? 0.393 0.493 0.324 0.053  -0.031 -0.077 499 LEU BBB CD1 
7431  C CD2 . LEU B 499 ? 0.407 0.495 0.310 0.063  -0.032 -0.069 499 LEU BBB CD2 
7432  N N   . GLU B 500 ? 0.538 0.652 0.442 0.088  -0.050 -0.096 500 GLU BBB N   
7433  C CA  . GLU B 500 ? 0.565 0.689 0.470 0.096  -0.056 -0.105 500 GLU BBB CA  
7434  C C   . GLU B 500 ? 0.557 0.682 0.450 0.105  -0.058 -0.107 500 GLU BBB C   
7435  O O   . GLU B 500 ? 0.603 0.739 0.501 0.110  -0.063 -0.117 500 GLU BBB O   
7436  C CB  . GLU B 500 ? 0.588 0.711 0.488 0.101  -0.059 -0.106 500 GLU BBB CB  
7437  C CG  . GLU B 500 ? 0.619 0.730 0.501 0.104  -0.057 -0.096 500 GLU BBB CG  
7438  C CD  . GLU B 500 ? 0.696 0.805 0.574 0.108  -0.059 -0.096 500 GLU BBB CD  
7439  O OE1 . GLU B 500 ? 0.701 0.817 0.593 0.105  -0.061 -0.102 500 GLU BBB OE1 
7440  O OE2 . GLU B 500 ? 0.730 0.831 0.592 0.114  -0.059 -0.091 500 GLU BBB OE2 
7441  N N   . VAL B 501 ? 0.533 0.648 0.412 0.105  -0.055 -0.098 501 VAL BBB N   
7442  C CA  . VAL B 501 ? 0.547 0.661 0.413 0.113  -0.057 -0.099 501 VAL BBB CA  
7443  C C   . VAL B 501 ? 0.552 0.673 0.428 0.109  -0.056 -0.103 501 VAL BBB C   
7444  O O   . VAL B 501 ? 0.548 0.666 0.432 0.100  -0.051 -0.099 501 VAL BBB O   
7445  C CB  . VAL B 501 ? 0.535 0.635 0.382 0.115  -0.053 -0.088 501 VAL BBB CB  
7446  C CG1 . VAL B 501 ? 0.553 0.652 0.386 0.123  -0.054 -0.088 501 VAL BBB CG1 
7447  C CG2 . VAL B 501 ? 0.534 0.629 0.372 0.119  -0.053 -0.085 501 VAL BBB CG2 
7448  N N   . THR B 502 ? 0.554 0.684 0.430 0.116  -0.060 -0.111 502 THR BBB N   
7449  C CA  . THR B 502 ? 0.570 0.706 0.455 0.113  -0.060 -0.116 502 THR BBB CA  
7450  C C   . THR B 502 ? 0.596 0.727 0.465 0.119  -0.059 -0.111 502 THR BBB C   
7451  O O   . THR B 502 ? 0.600 0.726 0.452 0.128  -0.061 -0.109 502 THR BBB O   
7452  C CB  . THR B 502 ? 0.558 0.710 0.458 0.116  -0.065 -0.129 502 THR BBB CB  
7453  O OG1 . THR B 502 ? 0.569 0.725 0.457 0.128  -0.071 -0.134 502 THR BBB OG1 
7454  C CG2 . THR B 502 ? 0.545 0.701 0.459 0.112  -0.066 -0.133 502 THR BBB CG2 
7455  N N   . LYS B 503 ? 0.634 0.764 0.507 0.114  -0.056 -0.110 503 LYS BBB N   
7456  C CA  . LYS B 503 ? 0.691 0.819 0.551 0.119  -0.055 -0.108 503 LYS BBB CA  
7457  C C   . LYS B 503 ? 0.711 0.848 0.565 0.130  -0.062 -0.117 503 LYS BBB C   
7458  O O   . LYS B 503 ? 0.671 0.803 0.507 0.139  -0.063 -0.114 503 LYS BBB O   
7459  C CB  . LYS B 503 ? 0.722 0.851 0.591 0.112  -0.052 -0.107 503 LYS BBB CB  
7460  C CG  . LYS B 503 ? 0.771 0.895 0.626 0.116  -0.050 -0.104 503 LYS BBB CG  
7461  C CD  . LYS B 503 ? 0.815 0.942 0.680 0.110  -0.048 -0.106 503 LYS BBB CD  
7462  C CE  . LYS B 503 ? 0.843 0.969 0.695 0.116  -0.047 -0.105 503 LYS BBB CE  
7463  N NZ  . LYS B 503 ? 0.847 0.959 0.683 0.116  -0.042 -0.094 503 LYS BBB NZ  
7464  N N   . ARG B 504 ? 0.730 0.881 0.601 0.130  -0.066 -0.128 504 ARG BBB N   
7465  C CA  . ARG B 504 ? 0.756 0.918 0.626 0.140  -0.072 -0.139 504 ARG BBB CA  
7466  C C   . ARG B 504 ? 0.772 0.931 0.626 0.151  -0.076 -0.138 504 ARG BBB C   
7467  O O   . ARG B 504 ? 0.769 0.930 0.609 0.161  -0.079 -0.140 504 ARG BBB O   
7468  C CB  . ARG B 504 ? 0.782 0.959 0.675 0.137  -0.076 -0.151 504 ARG BBB CB  
7469  C CG  . ARG B 504 ? 0.781 0.971 0.675 0.147  -0.083 -0.163 504 ARG BBB CG  
7470  C CD  . ARG B 504 ? 0.761 0.966 0.678 0.144  -0.086 -0.176 504 ARG BBB CD  
7471  N NE  . ARG B 504 ? 0.766 0.974 0.694 0.138  -0.083 -0.178 504 ARG BBB NE  
7472  C CZ  . ARG B 504 ? 0.746 0.955 0.692 0.127  -0.079 -0.179 504 ARG BBB CZ  
7473  N NH1 . ARG B 504 ? 0.776 0.983 0.733 0.121  -0.077 -0.178 504 ARG BBB NH1 
7474  N NH2 . ARG B 504 ? 0.744 0.955 0.699 0.122  -0.076 -0.180 504 ARG BBB NH2 
7475  N N   . SER B 505 ? 0.777 0.932 0.632 0.148  -0.075 -0.134 505 SER BBB N   
7476  C CA  . SER B 505 ? 0.779 0.931 0.619 0.158  -0.079 -0.133 505 SER BBB CA  
7477  C C   . SER B 505 ? 0.777 0.916 0.592 0.165  -0.076 -0.124 505 SER BBB C   
7478  O O   . SER B 505 ? 0.768 0.907 0.570 0.176  -0.080 -0.125 505 SER BBB O   
7479  C CB  . SER B 505 ? 0.797 0.944 0.642 0.153  -0.077 -0.129 505 SER BBB CB  
7480  O OG  . SER B 505 ? 0.785 0.917 0.620 0.147  -0.071 -0.117 505 SER BBB OG  
7481  N N   . GLY B 506 ? 0.737 0.867 0.548 0.159  -0.070 -0.116 506 GLY BBB N   
7482  C CA  . GLY B 506 ? 0.734 0.851 0.523 0.164  -0.066 -0.106 506 GLY BBB CA  
7483  C C   . GLY B 506 ? 0.725 0.829 0.502 0.165  -0.063 -0.097 506 GLY BBB C   
7484  O O   . GLY B 506 ? 0.723 0.815 0.482 0.168  -0.059 -0.089 506 GLY BBB O   
7485  N N   . GLU B 507 ? 0.717 0.823 0.502 0.163  -0.065 -0.099 507 GLU BBB N   
7486  C CA  . GLU B 507 ? 0.732 0.827 0.508 0.163  -0.062 -0.091 507 GLU BBB CA  
7487  C C   . GLU B 507 ? 0.665 0.748 0.441 0.152  -0.054 -0.080 507 GLU BBB C   
7488  O O   . GLU B 507 ? 0.650 0.735 0.437 0.144  -0.052 -0.080 507 GLU BBB O   
7489  C CB  . GLU B 507 ? 0.778 0.880 0.565 0.162  -0.067 -0.097 507 GLU BBB CB  
7490  C CG  . GLU B 507 ? 0.824 0.936 0.607 0.175  -0.075 -0.106 507 GLU BBB CG  
7491  C CD  . GLU B 507 ? 0.891 1.012 0.688 0.174  -0.079 -0.113 507 GLU BBB CD  
7492  O OE1 . GLU B 507 ? 0.962 1.093 0.779 0.166  -0.080 -0.120 507 GLU BBB OE1 
7493  O OE2 . GLU B 507 ? 0.918 1.036 0.705 0.181  -0.081 -0.112 507 GLU BBB OE2 
7494  N N   . SER B 508 ? 0.640 0.710 0.403 0.153  -0.050 -0.072 508 SER BBB N   
7495  C CA  . SER B 508 ? 0.661 0.718 0.422 0.144  -0.043 -0.062 508 SER BBB CA  
7496  C C   . SER B 508 ? 0.614 0.676 0.395 0.133  -0.042 -0.062 508 SER BBB C   
7497  O O   . SER B 508 ? 0.570 0.636 0.357 0.133  -0.045 -0.066 508 SER BBB O   
7498  C CB  . SER B 508 ? 0.673 0.716 0.416 0.149  -0.039 -0.053 508 SER BBB CB  
7499  O OG  . SER B 508 ? 0.675 0.708 0.419 0.140  -0.032 -0.045 508 SER BBB OG  
7500  N N   . PHE B 509 ? 0.601 0.661 0.390 0.123  -0.037 -0.059 509 PHE BBB N   
7501  C CA  . PHE B 509 ? 0.595 0.657 0.401 0.112  -0.036 -0.059 509 PHE BBB CA  
7502  C C   . PHE B 509 ? 0.603 0.653 0.404 0.106  -0.029 -0.049 509 PHE BBB C   
7503  O O   . PHE B 509 ? 0.581 0.631 0.394 0.097  -0.027 -0.048 509 PHE BBB O   
7504  C CB  . PHE B 509 ? 0.567 0.637 0.387 0.106  -0.035 -0.063 509 PHE BBB CB  
7505  C CG  . PHE B 509 ? 0.598 0.663 0.411 0.105  -0.032 -0.059 509 PHE BBB CG  
7506  C CD1 . PHE B 509 ? 0.580 0.636 0.392 0.098  -0.025 -0.051 509 PHE BBB CD1 
7507  C CD2 . PHE B 509 ? 0.589 0.659 0.397 0.112  -0.034 -0.064 509 PHE BBB CD2 
7508  C CE1 . PHE B 509 ? 0.579 0.631 0.385 0.098  -0.021 -0.048 509 PHE BBB CE1 
7509  C CE2 . PHE B 509 ? 0.593 0.659 0.395 0.111  -0.030 -0.060 509 PHE BBB CE2 
7510  C CZ  . PHE B 509 ? 0.591 0.647 0.391 0.104  -0.024 -0.052 509 PHE BBB CZ  
7511  N N   . VAL B 510 ? 0.666 0.705 0.450 0.111  -0.026 -0.043 510 VAL BBB N   
7512  C CA  . VAL B 510 ? 0.739 0.766 0.517 0.107  -0.020 -0.034 510 VAL BBB CA  
7513  C C   . VAL B 510 ? 0.811 0.837 0.591 0.108  -0.022 -0.034 510 VAL BBB C   
7514  O O   . VAL B 510 ? 0.842 0.872 0.617 0.116  -0.027 -0.039 510 VAL BBB O   
7515  C CB  . VAL B 510 ? 0.757 0.772 0.516 0.113  -0.015 -0.028 510 VAL BBB CB  
7516  C CG1 . VAL B 510 ? 0.801 0.803 0.554 0.110  -0.009 -0.020 510 VAL BBB CG1 
7517  C CG2 . VAL B 510 ? 0.751 0.766 0.510 0.111  -0.012 -0.028 510 VAL BBB CG2 
7518  N N   . SER B 511 ? 0.874 0.896 0.660 0.100  -0.018 -0.030 511 SER BBB N   
7519  C CA  . SER B 511 ? 0.935 0.953 0.720 0.100  -0.019 -0.028 511 SER BBB CA  
7520  C C   . SER B 511 ? 0.968 0.972 0.744 0.097  -0.012 -0.020 511 SER BBB C   
7521  O O   . SER B 511 ? 0.949 0.951 0.731 0.089  -0.007 -0.016 511 SER BBB O   
7522  C CB  . SER B 511 ? 0.935 0.961 0.736 0.093  -0.021 -0.032 511 SER BBB CB  
7523  O OG  . SER B 511 ? 0.931 0.969 0.741 0.096  -0.027 -0.040 511 SER BBB OG  
7524  N N   . SER B 512 ? 1.049 1.045 0.810 0.104  -0.010 -0.016 512 SER BBB N   
7525  C CA  . SER B 512 ? 1.158 1.140 0.908 0.103  -0.003 -0.008 512 SER BBB CA  
7526  C C   . SER B 512 ? 1.176 1.154 0.931 0.098  -0.001 -0.005 512 SER BBB C   
7527  O O   . SER B 512 ? 1.148 1.118 0.903 0.092  0.005  -0.000 512 SER BBB O   
7528  C CB  . SER B 512 ? 1.181 1.154 0.911 0.114  -0.002 -0.006 512 SER BBB CB  
7529  O OG  . SER B 512 ? 1.127 1.101 0.851 0.119  -0.002 -0.007 512 SER BBB OG  
7530  N N   . GLY B 513 ? 1.231 1.215 0.991 0.100  -0.007 -0.009 513 GLY BBB N   
7531  C CA  . GLY B 513 ? 1.278 1.262 1.047 0.094  -0.006 -0.008 513 GLY BBB CA  
7532  C C   . GLY B 513 ? 1.271 1.259 1.055 0.083  -0.004 -0.008 513 GLY BBB C   
7533  O O   . GLY B 513 ? 1.338 1.333 1.130 0.080  -0.006 -0.012 513 GLY BBB O   
7534  N N   . GLY B 514 ? 1.187 1.169 0.974 0.077  0.000  -0.004 514 GLY BBB N   
7535  C CA  . GLY B 514 ? 1.103 1.087 0.901 0.067  0.003  -0.002 514 GLY BBB CA  
7536  C C   . GLY B 514 ? 1.041 1.031 0.852 0.062  0.001  -0.005 514 GLY BBB C   
7537  O O   . GLY B 514 ? 0.919 0.905 0.733 0.056  0.004  -0.002 514 GLY BBB O   
7538  N N   . CYS B 515 ? 1.063 1.063 0.881 0.063  -0.005 -0.011 515 CYS BBB N   
7539  C CA  . CYS B 515 ? 1.043 1.050 0.875 0.058  -0.008 -0.014 515 CYS BBB CA  
7540  C C   . CYS B 515 ? 0.961 0.974 0.805 0.051  -0.007 -0.015 515 CYS BBB C   
7541  O O   . CYS B 515 ? 0.907 0.926 0.762 0.046  -0.008 -0.017 515 CYS BBB O   
7542  C CB  . CYS B 515 ? 1.103 1.118 0.938 0.063  -0.014 -0.020 515 CYS BBB CB  
7543  S SG  . CYS B 515 ? 1.126 1.138 0.946 0.075  -0.017 -0.021 515 CYS BBB SG  
7544  N N   . GLY B 516 ? 0.901 0.911 0.741 0.050  -0.004 -0.013 516 GLY BBB N   
7545  C CA  . GLY B 516 ? 0.864 0.879 0.713 0.044  -0.003 -0.014 516 GLY BBB CA  
7546  C C   . GLY B 516 ? 0.814 0.838 0.670 0.047  -0.008 -0.020 516 GLY BBB C   
7547  O O   . GLY B 516 ? 0.881 0.906 0.730 0.053  -0.010 -0.022 516 GLY BBB O   
7548  N N   . GLY B 517 ? 0.805 0.836 0.673 0.041  -0.009 -0.022 517 GLY BBB N   
7549  C CA  . GLY B 517 ? 0.803 0.843 0.680 0.043  -0.013 -0.029 517 GLY BBB CA  
7550  C C   . GLY B 517 ? 0.823 0.868 0.701 0.048  -0.017 -0.034 517 GLY BBB C   
7551  O O   . GLY B 517 ? 0.773 0.826 0.658 0.049  -0.020 -0.040 517 GLY BBB O   
7552  N N   . GLY B 518 ? 0.838 0.879 0.709 0.051  -0.017 -0.032 518 GLY BBB N   
7553  C CA  . GLY B 518 ? 0.824 0.866 0.689 0.059  -0.021 -0.036 518 GLY BBB CA  
7554  C C   . GLY B 518 ? 0.775 0.820 0.646 0.058  -0.023 -0.037 518 GLY BBB C   
7555  O O   . GLY B 518 ? 0.680 0.725 0.559 0.051  -0.021 -0.036 518 GLY BBB O   
7556  N N   . LEU C 24  ? 0.968 1.583 0.939 -0.017 0.039  0.033  24  LEU CCC N   
7557  C CA  . LEU C 24  ? 0.956 1.559 0.932 -0.006 0.040  0.021  24  LEU CCC CA  
7558  C C   . LEU C 24  ? 0.970 1.546 0.949 -0.004 0.037  0.027  24  LEU CCC C   
7559  O O   . LEU C 24  ? 0.916 1.481 0.893 -0.008 0.034  0.038  24  LEU CCC O   
7560  C CB  . LEU C 24  ? 0.929 1.532 0.904 -0.001 0.041  0.012  24  LEU CCC CB  
7561  C CG  . LEU C 24  ? 0.911 1.525 0.892 0.006  0.044  -0.004 24  LEU CCC CG  
7562  C CD1 . LEU C 24  ? 0.887 1.529 0.868 0.003  0.047  -0.008 24  LEU CCC CD1 
7563  C CD2 . LEU C 24  ? 0.878 1.492 0.858 0.011  0.044  -0.012 24  LEU CCC CD2 
7564  N N   . THR C 25  ? 1.001 1.567 0.986 0.003  0.038  0.021  25  THR CCC N   
7565  C CA  . THR C 25  ? 0.983 1.528 0.971 0.004  0.036  0.027  25  THR CCC CA  
7566  C C   . THR C 25  ? 0.943 1.467 0.928 0.004  0.033  0.033  25  THR CCC C   
7567  O O   . THR C 25  ? 0.978 1.488 0.965 0.003  0.030  0.040  25  THR CCC O   
7568  C CB  . THR C 25  ? 0.978 1.515 0.973 0.012  0.037  0.018  25  THR CCC CB  
7569  O OG1 . THR C 25  ? 1.011 1.568 1.008 0.013  0.039  0.010  25  THR CCC OG1 
7570  C CG2 . THR C 25  ? 0.955 1.477 0.952 0.011  0.035  0.024  25  THR CCC CG2 
7571  N N   . PHE C 26  ? 0.852 1.375 0.835 0.005  0.032  0.030  26  PHE CCC N   
7572  C CA  . PHE C 26  ? 0.752 1.253 0.733 0.007  0.029  0.035  26  PHE CCC CA  
7573  C C   . PHE C 26  ? 0.677 1.184 0.653 0.002  0.028  0.040  26  PHE CCC C   
7574  O O   . PHE C 26  ? 0.634 1.153 0.608 0.003  0.030  0.034  26  PHE CCC O   
7575  C CB  . PHE C 26  ? 0.710 1.198 0.694 0.015  0.029  0.026  26  PHE CCC CB  
7576  C CG  . PHE C 26  ? 0.694 1.177 0.684 0.020  0.030  0.020  26  PHE CCC CG  
7577  C CD1 . PHE C 26  ? 0.676 1.147 0.668 0.019  0.029  0.026  26  PHE CCC CD1 
7578  C CD2 . PHE C 26  ? 0.713 1.203 0.706 0.025  0.032  0.009  26  PHE CCC CD2 
7579  C CE1 . PHE C 26  ? 0.683 1.151 0.680 0.023  0.030  0.021  26  PHE CCC CE1 
7580  C CE2 . PHE C 26  ? 0.697 1.183 0.695 0.030  0.032  0.004  26  PHE CCC CE2 
7581  C CZ  . PHE C 26  ? 0.680 1.155 0.680 0.028  0.031  0.010  26  PHE CCC CZ  
7582  N N   . MET C 27  ? 0.629 1.127 0.605 -0.003 0.025  0.050  27  MET CCC N   
7583  C CA  . MET C 27  ? 0.603 1.101 0.574 -0.008 0.022  0.057  27  MET CCC CA  
7584  C C   . MET C 27  ? 0.570 1.059 0.540 -0.002 0.022  0.050  27  MET CCC C   
7585  O O   . MET C 27  ? 0.584 1.084 0.549 -0.004 0.023  0.049  27  MET CCC O   
7586  C CB  . MET C 27  ? 0.624 1.109 0.597 -0.013 0.018  0.068  27  MET CCC CB  
7587  C CG  . MET C 27  ? 0.653 1.147 0.627 -0.020 0.016  0.077  27  MET CCC CG  
7588  S SD  . MET C 27  ? 0.624 1.098 0.603 -0.023 0.010  0.088  27  MET CCC SD  
7589  C CE  . MET C 27  ? 0.622 1.095 0.598 -0.029 0.006  0.096  27  MET CCC CE  
7590  N N   . TYR C 28  ? 0.528 0.999 0.501 0.004  0.022  0.045  28  TYR CCC N   
7591  C CA  . TYR C 28  ? 0.491 0.951 0.463 0.010  0.022  0.039  28  TYR CCC CA  
7592  C C   . TYR C 28  ? 0.459 0.918 0.434 0.017  0.025  0.028  28  TYR CCC C   
7593  O O   . TYR C 28  ? 0.469 0.928 0.448 0.019  0.026  0.025  28  TYR CCC O   
7594  C CB  . TYR C 28  ? 0.460 0.899 0.434 0.010  0.019  0.044  28  TYR CCC CB  
7595  C CG  . TYR C 28  ? 0.453 0.891 0.425 0.003  0.015  0.055  28  TYR CCC CG  
7596  C CD1 . TYR C 28  ? 0.449 0.889 0.424 -0.003 0.013  0.063  28  TYR CCC CD1 
7597  C CD2 . TYR C 28  ? 0.470 0.907 0.439 0.002  0.014  0.056  28  TYR CCC CD2 
7598  C CE1 . TYR C 28  ? 0.451 0.890 0.425 -0.009 0.009  0.073  28  TYR CCC CE1 
7599  C CE2 . TYR C 28  ? 0.470 0.907 0.439 -0.005 0.010  0.066  28  TYR CCC CE2 
7600  C CZ  . TYR C 28  ? 0.477 0.915 0.449 -0.010 0.008  0.074  28  TYR CCC CZ  
7601  O OH  . TYR C 28  ? 0.461 0.898 0.432 -0.017 0.003  0.084  28  TYR CCC OH  
7602  N N   . ASP C 29  ? 0.446 0.903 0.421 0.022  0.025  0.021  29  ASP CCC N   
7603  C CA  . ASP C 29  ? 0.436 0.887 0.414 0.029  0.026  0.011  29  ASP CCC CA  
7604  C C   . ASP C 29  ? 0.404 0.832 0.384 0.032  0.024  0.012  29  ASP CCC C   
7605  O O   . ASP C 29  ? 0.372 0.794 0.356 0.036  0.024  0.007  29  ASP CCC O   
7606  C CB  . ASP C 29  ? 0.447 0.906 0.423 0.032  0.027  0.003  29  ASP CCC CB  
7607  C CG  . ASP C 29  ? 0.458 0.941 0.433 0.030  0.029  -0.000 29  ASP CCC CG  
7608  O OD1 . ASP C 29  ? 0.420 0.914 0.399 0.032  0.031  -0.007 29  ASP CCC OD1 
7609  O OD2 . ASP C 29  ? 0.469 0.962 0.439 0.025  0.029  0.003  29  ASP CCC OD2 
7610  N N   . LEU C 30  ? 0.401 0.818 0.379 0.030  0.022  0.019  30  LEU CCC N   
7611  C CA  . LEU C 30  ? 0.388 0.785 0.367 0.032  0.020  0.020  30  LEU CCC CA  
7612  C C   . LEU C 30  ? 0.351 0.740 0.330 0.027  0.018  0.029  30  LEU CCC C   
7613  O O   . LEU C 30  ? 0.316 0.710 0.292 0.023  0.017  0.033  30  LEU CCC O   
7614  C CB  . LEU C 30  ? 0.419 0.809 0.397 0.036  0.019  0.014  30  LEU CCC CB  
7615  C CG  . LEU C 30  ? 0.394 0.765 0.374 0.038  0.018  0.015  30  LEU CCC CG  
7616  C CD1 . LEU C 30  ? 0.414 0.777 0.398 0.041  0.018  0.012  30  LEU CCC CD1 
7617  C CD2 . LEU C 30  ? 0.394 0.762 0.372 0.041  0.017  0.010  30  LEU CCC CD2 
7618  N N   . VAL C 31  ? 0.333 0.710 0.315 0.027  0.016  0.032  31  VAL CCC N   
7619  C CA  . VAL C 31  ? 0.329 0.697 0.313 0.023  0.014  0.039  31  VAL CCC CA  
7620  C C   . VAL C 31  ? 0.320 0.671 0.306 0.027  0.013  0.036  31  VAL CCC C   
7621  O O   . VAL C 31  ? 0.299 0.646 0.287 0.030  0.014  0.032  31  VAL CCC O   
7622  C CB  . VAL C 31  ? 0.348 0.718 0.334 0.019  0.013  0.046  31  VAL CCC CB  
7623  C CG1 . VAL C 31  ? 0.352 0.709 0.341 0.016  0.010  0.051  31  VAL CCC CG1 
7624  C CG2 . VAL C 31  ? 0.378 0.765 0.362 0.014  0.013  0.050  31  VAL CCC CG2 
7625  N N   . VAL C 32  ? 0.342 0.685 0.328 0.026  0.011  0.038  32  VAL CCC N   
7626  C CA  . VAL C 32  ? 0.336 0.664 0.323 0.029  0.010  0.035  32  VAL CCC CA  
7627  C C   . VAL C 32  ? 0.359 0.679 0.350 0.026  0.008  0.040  32  VAL CCC C   
7628  O O   . VAL C 32  ? 0.378 0.699 0.369 0.022  0.005  0.046  32  VAL CCC O   
7629  C CB  . VAL C 32  ? 0.352 0.677 0.336 0.031  0.010  0.032  32  VAL CCC CB  
7630  C CG1 . VAL C 32  ? 0.356 0.667 0.342 0.033  0.009  0.029  32  VAL CCC CG1 
7631  C CG2 . VAL C 32  ? 0.345 0.679 0.326 0.034  0.012  0.026  32  VAL CCC CG2 
7632  N N   . ILE C 33  ? 0.349 0.660 0.343 0.027  0.008  0.039  33  ILE CCC N   
7633  C CA  . ILE C 33  ? 0.366 0.668 0.365 0.024  0.005  0.043  33  ILE CCC CA  
7634  C C   . ILE C 33  ? 0.352 0.643 0.351 0.026  0.004  0.039  33  ILE CCC C   
7635  O O   . ILE C 33  ? 0.330 0.615 0.330 0.029  0.006  0.034  33  ILE CCC O   
7636  C CB  . ILE C 33  ? 0.363 0.664 0.366 0.023  0.005  0.044  33  ILE CCC CB  
7637  C CG1 . ILE C 33  ? 0.376 0.689 0.378 0.021  0.006  0.047  33  ILE CCC CG1 
7638  C CG2 . ILE C 33  ? 0.365 0.658 0.374 0.021  0.002  0.047  33  ILE CCC CG2 
7639  C CD1 . ILE C 33  ? 0.381 0.694 0.385 0.021  0.007  0.048  33  ILE CCC CD1 
7640  N N   . GLY C 34  ? 0.346 0.635 0.347 0.025  0.002  0.040  34  GLY CCC N   
7641  C CA  . GLY C 34  ? 0.341 0.619 0.342 0.027  0.001  0.037  34  GLY CCC CA  
7642  C C   . GLY C 34  ? 0.348 0.629 0.345 0.028  0.001  0.036  34  GLY CCC C   
7643  O O   . GLY C 34  ? 0.359 0.646 0.352 0.030  0.004  0.033  34  GLY CCC O   
7644  N N   . GLY C 35  ? 0.350 0.627 0.350 0.026  -0.001 0.038  35  GLY CCC N   
7645  C CA  . GLY C 35  ? 0.338 0.616 0.334 0.027  -0.002 0.038  35  GLY CCC CA  
7646  C C   . GLY C 35  ? 0.363 0.632 0.360 0.029  -0.002 0.033  35  GLY CCC C   
7647  O O   . GLY C 35  ? 0.338 0.604 0.336 0.028  -0.004 0.034  35  GLY CCC O   
7648  N N   . GLY C 36  ? 0.380 0.645 0.377 0.032  0.000  0.028  36  GLY CCC N   
7649  C CA  . GLY C 36  ? 0.365 0.623 0.361 0.035  0.001  0.023  36  GLY CCC CA  
7650  C C   . GLY C 36  ? 0.383 0.643 0.373 0.038  0.003  0.019  36  GLY CCC C   
7651  O O   . GLY C 36  ? 0.382 0.651 0.369 0.038  0.003  0.020  36  GLY CCC O   
7652  N N   . SER C 37  ? 0.406 0.660 0.396 0.040  0.003  0.015  37  SER CCC N   
7653  C CA  . SER C 37  ? 0.408 0.664 0.394 0.043  0.004  0.011  37  SER CCC CA  
7654  C C   . SER C 37  ? 0.400 0.663 0.384 0.045  0.006  0.010  37  SER CCC C   
7655  O O   . SER C 37  ? 0.413 0.681 0.394 0.046  0.006  0.008  37  SER CCC O   
7656  C CB  . SER C 37  ? 0.422 0.670 0.408 0.044  0.004  0.007  37  SER CCC CB  
7657  O OG  . SER C 37  ? 0.430 0.673 0.419 0.043  0.003  0.007  37  SER CCC OG  
7658  N N   . GLY C 38  ? 0.392 0.655 0.377 0.044  0.006  0.010  38  GLY CCC N   
7659  C CA  . GLY C 38  ? 0.370 0.639 0.354 0.046  0.007  0.009  38  GLY CCC CA  
7660  C C   . GLY C 38  ? 0.366 0.646 0.350 0.045  0.008  0.012  38  GLY CCC C   
7661  O O   . GLY C 38  ? 0.383 0.669 0.365 0.047  0.009  0.009  38  GLY CCC O   
7662  N N   . GLY C 39  ? 0.379 0.660 0.365 0.041  0.007  0.017  39  GLY CCC N   
7663  C CA  . GLY C 39  ? 0.396 0.687 0.381 0.039  0.008  0.021  39  GLY CCC CA  
7664  C C   . GLY C 39  ? 0.390 0.688 0.372 0.039  0.008  0.021  39  GLY CCC C   
7665  O O   . GLY C 39  ? 0.355 0.664 0.335 0.039  0.009  0.020  39  GLY CCC O   
7666  N N   . MET C 40  ? 0.399 0.692 0.381 0.038  0.006  0.022  40  MET CCC N   
7667  C CA  . MET C 40  ? 0.413 0.712 0.391 0.037  0.005  0.023  40  MET CCC CA  
7668  C C   . MET C 40  ? 0.411 0.714 0.386 0.041  0.007  0.017  40  MET CCC C   
7669  O O   . MET C 40  ? 0.410 0.725 0.383 0.041  0.008  0.016  40  MET CCC O   
7670  C CB  . MET C 40  ? 0.428 0.720 0.408 0.036  0.003  0.025  40  MET CCC CB  
7671  C CG  . MET C 40  ? 0.453 0.743 0.437 0.031  0.000  0.032  40  MET CCC CG  
7672  S SD  . MET C 40  ? 0.524 0.807 0.509 0.030  -0.003 0.034  40  MET CCC SD  
7673  C CE  . MET C 40  ? 0.512 0.784 0.498 0.034  -0.002 0.027  40  MET CCC CE  
7674  N N   . ALA C 41  ? 0.366 0.663 0.343 0.045  0.007  0.012  41  ALA CCC N   
7675  C CA  . ALA C 41  ? 0.350 0.649 0.325 0.049  0.008  0.005  41  ALA CCC CA  
7676  C C   . ALA C 41  ? 0.341 0.651 0.316 0.050  0.010  0.003  41  ALA CCC C   
7677  O O   . ALA C 41  ? 0.324 0.645 0.298 0.051  0.011  0.000  41  ALA CCC O   
7678  C CB  . ALA C 41  ? 0.352 0.640 0.328 0.052  0.008  0.002  41  ALA CCC CB  
7679  N N   . ALA C 42  ? 0.341 0.651 0.318 0.049  0.010  0.005  42  ALA CCC N   
7680  C CA  . ALA C 42  ? 0.377 0.697 0.355 0.050  0.012  0.003  42  ALA CCC CA  
7681  C C   . ALA C 42  ? 0.404 0.739 0.380 0.047  0.013  0.005  42  ALA CCC C   
7682  O O   . ALA C 42  ? 0.396 0.742 0.371 0.049  0.014  0.001  42  ALA CCC O   
7683  C CB  . ALA C 42  ? 0.381 0.698 0.362 0.049  0.012  0.005  42  ALA CCC CB  
7684  N N   . ALA C 43  ? 0.428 0.762 0.403 0.042  0.012  0.012  43  ALA CCC N   
7685  C CA  . ALA C 43  ? 0.458 0.804 0.430 0.038  0.012  0.017  43  ALA CCC CA  
7686  C C   . ALA C 43  ? 0.499 0.855 0.468 0.038  0.013  0.015  43  ALA CCC C   
7687  O O   . ALA C 43  ? 0.461 0.833 0.428 0.037  0.014  0.013  43  ALA CCC O   
7688  C CB  . ALA C 43  ? 0.454 0.794 0.428 0.034  0.010  0.025  43  ALA CCC CB  
7689  N N   . LYS C 44  ? 0.517 0.865 0.485 0.040  0.011  0.014  44  LYS CCC N   
7690  C CA  . LYS C 44  ? 0.499 0.855 0.463 0.040  0.011  0.011  44  LYS CCC CA  
7691  C C   . LYS C 44  ? 0.485 0.848 0.449 0.045  0.013  0.002  44  LYS CCC C   
7692  O O   . LYS C 44  ? 0.514 0.892 0.477 0.044  0.014  -0.001 44  LYS CCC O   
7693  C CB  . LYS C 44  ? 0.505 0.849 0.469 0.041  0.009  0.011  44  LYS CCC CB  
7694  C CG  . LYS C 44  ? 0.529 0.869 0.492 0.036  0.007  0.020  44  LYS CCC CG  
7695  C CD  . LYS C 44  ? 0.544 0.874 0.507 0.037  0.005  0.020  44  LYS CCC CD  
7696  C CE  . LYS C 44  ? 0.560 0.875 0.528 0.038  0.004  0.019  44  LYS CCC CE  
7697  N NZ  . LYS C 44  ? 0.576 0.882 0.543 0.039  0.002  0.019  44  LYS CCC NZ  
7698  N N   . GLU C 45  ? 0.470 0.825 0.438 0.049  0.013  -0.003 45  GLU CCC N   
7699  C CA  . GLU C 45  ? 0.480 0.841 0.450 0.054  0.014  -0.012 45  GLU CCC CA  
7700  C C   . GLU C 45  ? 0.451 0.828 0.422 0.053  0.016  -0.014 45  GLU CCC C   
7701  O O   . GLU C 45  ? 0.446 0.836 0.418 0.056  0.017  -0.020 45  GLU CCC O   
7702  C CB  . GLU C 45  ? 0.475 0.823 0.449 0.058  0.013  -0.016 45  GLU CCC CB  
7703  C CG  . GLU C 45  ? 0.494 0.846 0.471 0.064  0.012  -0.025 45  GLU CCC CG  
7704  C CD  . GLU C 45  ? 0.538 0.888 0.514 0.066  0.011  -0.029 45  GLU CCC CD  
7705  O OE1 . GLU C 45  ? 0.537 0.885 0.509 0.063  0.011  -0.024 45  GLU CCC OE1 
7706  O OE2 . GLU C 45  ? 0.564 0.914 0.543 0.071  0.010  -0.036 45  GLU CCC OE2 
7707  N N   . ALA C 46  ? 0.415 0.791 0.387 0.050  0.016  -0.008 46  ALA CCC N   
7708  C CA  . ALA C 46  ? 0.447 0.838 0.419 0.049  0.018  -0.009 46  ALA CCC CA  
7709  C C   . ALA C 46  ? 0.463 0.872 0.431 0.045  0.019  -0.007 46  ALA CCC C   
7710  O O   . ALA C 46  ? 0.461 0.885 0.430 0.046  0.021  -0.014 46  ALA CCC O   
7711  C CB  . ALA C 46  ? 0.428 0.815 0.402 0.046  0.018  -0.002 46  ALA CCC CB  
7712  N N   . ALA C 47  ? 0.490 0.896 0.454 0.040  0.018  0.001  47  ALA CCC N   
7713  C CA  . ALA C 47  ? 0.504 0.925 0.464 0.035  0.018  0.004  47  ALA CCC CA  
7714  C C   . ALA C 47  ? 0.551 0.981 0.509 0.038  0.019  -0.004 47  ALA CCC C   
7715  O O   . ALA C 47  ? 0.541 0.990 0.496 0.034  0.021  -0.004 47  ALA CCC O   
7716  C CB  . ALA C 47  ? 0.519 0.931 0.477 0.030  0.016  0.014  47  ALA CCC CB  
7717  N N   . LYS C 48  ? 0.581 1.000 0.542 0.043  0.018  -0.010 48  LYS CCC N   
7718  C CA  . LYS C 48  ? 0.613 1.039 0.573 0.047  0.019  -0.018 48  LYS CCC CA  
7719  C C   . LYS C 48  ? 0.608 1.053 0.570 0.049  0.021  -0.027 48  LYS CCC C   
7720  O O   . LYS C 48  ? 0.607 1.065 0.567 0.050  0.022  -0.032 48  LYS CCC O   
7721  C CB  . LYS C 48  ? 0.639 1.048 0.602 0.053  0.017  -0.024 48  LYS CCC CB  
7722  C CG  . LYS C 48  ? 0.673 1.073 0.634 0.054  0.016  -0.023 48  LYS CCC CG  
7723  C CD  . LYS C 48  ? 0.709 1.099 0.673 0.060  0.014  -0.031 48  LYS CCC CD  
7724  C CE  . LYS C 48  ? 0.757 1.162 0.724 0.064  0.015  -0.041 48  LYS CCC CE  
7725  N NZ  . LYS C 48  ? 0.774 1.176 0.741 0.067  0.014  -0.047 48  LYS CCC NZ  
7726  N N   . TYR C 49  ? 0.594 1.040 0.561 0.050  0.022  -0.028 49  TYR CCC N   
7727  C CA  . TYR C 49  ? 0.649 1.111 0.619 0.053  0.024  -0.037 49  TYR CCC CA  
7728  C C   . TYR C 49  ? 0.681 1.163 0.648 0.047  0.026  -0.033 49  TYR CCC C   
7729  O O   . TYR C 49  ? 0.685 1.179 0.656 0.048  0.028  -0.039 49  TYR CCC O   
7730  C CB  . TYR C 49  ? 0.653 1.104 0.630 0.058  0.023  -0.041 49  TYR CCC CB  
7731  C CG  . TYR C 49  ? 0.670 1.105 0.651 0.064  0.020  -0.046 49  TYR CCC CG  
7732  C CD1 . TYR C 49  ? 0.655 1.095 0.637 0.068  0.020  -0.055 49  TYR CCC CD1 
7733  C CD2 . TYR C 49  ? 0.682 1.096 0.663 0.065  0.018  -0.041 49  TYR CCC CD2 
7734  C CE1 . TYR C 49  ? 0.676 1.102 0.661 0.072  0.017  -0.059 49  TYR CCC CE1 
7735  C CE2 . TYR C 49  ? 0.642 1.042 0.625 0.069  0.016  -0.044 49  TYR CCC CE2 
7736  C CZ  . TYR C 49  ? 0.681 1.087 0.667 0.073  0.015  -0.053 49  TYR CCC CZ  
7737  O OH  . TYR C 49  ? 0.680 1.072 0.668 0.077  0.012  -0.056 49  TYR CCC OH  
7738  N N   . GLY C 50  ? 0.681 1.166 0.642 0.040  0.026  -0.024 50  GLY CCC N   
7739  C CA  . GLY C 50  ? 0.653 1.156 0.610 0.033  0.027  -0.018 50  GLY CCC CA  
7740  C C   . GLY C 50  ? 0.617 1.116 0.576 0.030  0.027  -0.011 50  GLY CCC C   
7741  O O   . GLY C 50  ? 0.611 1.128 0.569 0.025  0.029  -0.009 50  GLY CCC O   
7742  N N   . LYS C 51  ? 0.560 1.038 0.522 0.033  0.026  -0.009 51  LYS CCC N   
7743  C CA  . LYS C 51  ? 0.550 1.024 0.514 0.031  0.026  -0.003 51  LYS CCC CA  
7744  C C   . LYS C 51  ? 0.525 0.994 0.486 0.024  0.024  0.009  51  LYS CCC C   
7745  O O   . LYS C 51  ? 0.538 0.999 0.496 0.023  0.022  0.013  51  LYS CCC O   
7746  C CB  . LYS C 51  ? 0.568 1.023 0.537 0.037  0.025  -0.007 51  LYS CCC CB  
7747  C CG  . LYS C 51  ? 0.575 1.035 0.550 0.044  0.026  -0.019 51  LYS CCC CG  
7748  C CD  . LYS C 51  ? 0.570 1.052 0.545 0.043  0.028  -0.025 51  LYS CCC CD  
7749  C CE  . LYS C 51  ? 0.593 1.076 0.576 0.050  0.028  -0.036 51  LYS CCC CE  
7750  N NZ  . LYS C 51  ? 0.598 1.102 0.583 0.052  0.030  -0.046 51  LYS CCC NZ  
7751  N N   . LYS C 52  ? 0.549 1.023 0.510 0.020  0.024  0.015  52  LYS CCC N   
7752  C CA  . LYS C 52  ? 0.565 1.033 0.525 0.013  0.021  0.028  52  LYS CCC CA  
7753  C C   . LYS C 52  ? 0.527 0.972 0.491 0.016  0.020  0.030  52  LYS CCC C   
7754  O O   . LYS C 52  ? 0.488 0.930 0.456 0.020  0.021  0.026  52  LYS CCC O   
7755  C CB  . LYS C 52  ? 0.651 1.136 0.611 0.007  0.022  0.033  52  LYS CCC CB  
7756  C CG  . LYS C 52  ? 0.729 1.215 0.685 -0.001 0.019  0.045  52  LYS CCC CG  
7757  C CD  . LYS C 52  ? 0.764 1.260 0.721 -0.007 0.019  0.053  52  LYS CCC CD  
7758  C CE  . LYS C 52  ? 0.773 1.264 0.729 -0.015 0.014  0.065  52  LYS CCC CE  
7759  N NZ  . LYS C 52  ? 0.780 1.276 0.739 -0.020 0.013  0.073  52  LYS CCC NZ  
7760  N N   . VAL C 53  ? 0.477 0.909 0.440 0.015  0.017  0.035  53  VAL CCC N   
7761  C CA  . VAL C 53  ? 0.446 0.857 0.414 0.018  0.015  0.036  53  VAL CCC CA  
7762  C C   . VAL C 53  ? 0.431 0.834 0.399 0.013  0.012  0.046  53  VAL CCC C   
7763  O O   . VAL C 53  ? 0.411 0.819 0.377 0.008  0.009  0.051  53  VAL CCC O   
7764  C CB  . VAL C 53  ? 0.470 0.871 0.437 0.023  0.015  0.030  53  VAL CCC CB  
7765  C CG1 . VAL C 53  ? 0.487 0.868 0.457 0.027  0.014  0.029  53  VAL CCC CG1 
7766  C CG2 . VAL C 53  ? 0.458 0.869 0.424 0.028  0.018  0.020  53  VAL CCC CG2 
7767  N N   . ALA C 54  ? 0.441 0.834 0.414 0.013  0.010  0.049  54  ALA CCC N   
7768  C CA  . ALA C 54  ? 0.431 0.813 0.407 0.009  0.007  0.057  54  ALA CCC CA  
7769  C C   . ALA C 54  ? 0.391 0.754 0.370 0.014  0.006  0.053  54  ALA CCC C   
7770  O O   . ALA C 54  ? 0.375 0.735 0.356 0.018  0.008  0.047  54  ALA CCC O   
7771  C CB  . ALA C 54  ? 0.444 0.830 0.422 0.004  0.005  0.063  54  ALA CCC CB  
7772  N N   . LEU C 55  ? 0.366 0.718 0.347 0.012  0.003  0.057  55  LEU CCC N   
7773  C CA  . LEU C 55  ? 0.382 0.718 0.367 0.016  0.002  0.054  55  LEU CCC CA  
7774  C C   . LEU C 55  ? 0.372 0.700 0.363 0.012  -0.002 0.060  55  LEU CCC C   
7775  O O   . LEU C 55  ? 0.383 0.715 0.375 0.007  -0.006 0.067  55  LEU CCC O   
7776  C CB  . LEU C 55  ? 0.388 0.719 0.371 0.019  0.002  0.049  55  LEU CCC CB  
7777  C CG  . LEU C 55  ? 0.404 0.720 0.390 0.022  0.002  0.045  55  LEU CCC CG  
7778  C CD1 . LEU C 55  ? 0.425 0.738 0.408 0.027  0.003  0.038  55  LEU CCC CD1 
7779  C CD2 . LEU C 55  ? 0.400 0.707 0.391 0.019  -0.002 0.050  55  LEU CCC CD2 
7780  N N   . PHE C 56  ? 0.357 0.677 0.353 0.013  -0.002 0.059  56  PHE CCC N   
7781  C CA  . PHE C 56  ? 0.378 0.688 0.380 0.011  -0.006 0.063  56  PHE CCC CA  
7782  C C   . PHE C 56  ? 0.393 0.691 0.398 0.014  -0.007 0.058  56  PHE CCC C   
7783  O O   . PHE C 56  ? 0.435 0.729 0.438 0.018  -0.003 0.051  56  PHE CCC O   
7784  C CB  . PHE C 56  ? 0.375 0.686 0.380 0.010  -0.005 0.064  56  PHE CCC CB  
7785  C CG  . PHE C 56  ? 0.397 0.720 0.401 0.006  -0.005 0.069  56  PHE CCC CG  
7786  C CD1 . PHE C 56  ? 0.418 0.743 0.425 0.001  -0.010 0.078  56  PHE CCC CD1 
7787  C CD2 . PHE C 56  ? 0.398 0.731 0.397 0.008  -0.001 0.066  56  PHE CCC CD2 
7788  C CE1 . PHE C 56  ? 0.436 0.774 0.442 -0.004 -0.010 0.083  56  PHE CCC CE1 
7789  C CE2 . PHE C 56  ? 0.416 0.762 0.414 0.004  -0.001 0.071  56  PHE CCC CE2 
7790  C CZ  . PHE C 56  ? 0.431 0.780 0.432 -0.002 -0.005 0.080  56  PHE CCC CZ  
7791  N N   . ASP C 57  ? 0.397 0.689 0.407 0.012  -0.011 0.061  57  ASP CCC N   
7792  C CA  . ASP C 57  ? 0.414 0.694 0.429 0.014  -0.012 0.057  57  ASP CCC CA  
7793  C C   . ASP C 57  ? 0.413 0.688 0.437 0.010  -0.018 0.062  57  ASP CCC C   
7794  O O   . ASP C 57  ? 0.423 0.701 0.448 0.007  -0.021 0.068  57  ASP CCC O   
7795  C CB  . ASP C 57  ? 0.430 0.707 0.442 0.016  -0.012 0.054  57  ASP CCC CB  
7796  C CG  . ASP C 57  ? 0.404 0.670 0.420 0.019  -0.012 0.048  57  ASP CCC CG  
7797  O OD1 . ASP C 57  ? 0.396 0.659 0.410 0.022  -0.009 0.043  57  ASP CCC OD1 
7798  O OD2 . ASP C 57  ? 0.404 0.664 0.425 0.018  -0.016 0.049  57  ASP CCC OD2 
7799  N N   . PHE C 58  ? 0.416 0.683 0.446 0.011  -0.018 0.059  58  PHE CCC N   
7800  C CA  . PHE C 58  ? 0.443 0.704 0.484 0.009  -0.024 0.061  58  PHE CCC CA  
7801  C C   . PHE C 58  ? 0.400 0.652 0.445 0.012  -0.023 0.053  58  PHE CCC C   
7802  O O   . PHE C 58  ? 0.412 0.665 0.455 0.015  -0.019 0.049  58  PHE CCC O   
7803  C CB  . PHE C 58  ? 0.483 0.746 0.529 0.006  -0.027 0.067  58  PHE CCC CB  
7804  C CG  . PHE C 58  ? 0.483 0.740 0.541 0.003  -0.033 0.069  58  PHE CCC CG  
7805  C CD1 . PHE C 58  ? 0.502 0.752 0.568 0.005  -0.034 0.064  58  PHE CCC CD1 
7806  C CD2 . PHE C 58  ? 0.493 0.751 0.555 -0.001 -0.039 0.077  58  PHE CCC CD2 
7807  C CE1 . PHE C 58  ? 0.535 0.780 0.613 0.003  -0.040 0.065  58  PHE CCC CE1 
7808  C CE2 . PHE C 58  ? 0.525 0.776 0.600 -0.003 -0.046 0.079  58  PHE CCC CE2 
7809  C CZ  . PHE C 58  ? 0.542 0.787 0.625 -0.001 -0.046 0.073  58  PHE CCC CZ  
7810  N N   . VAL C 59  ? 0.408 0.654 0.461 0.012  -0.027 0.052  59  VAL CCC N   
7811  C CA  . VAL C 59  ? 0.381 0.620 0.439 0.014  -0.026 0.044  59  VAL CCC CA  
7812  C C   . VAL C 59  ? 0.388 0.623 0.457 0.013  -0.030 0.043  59  VAL CCC C   
7813  O O   . VAL C 59  ? 0.360 0.592 0.438 0.011  -0.036 0.047  59  VAL CCC O   
7814  C CB  . VAL C 59  ? 0.380 0.614 0.439 0.016  -0.028 0.042  59  VAL CCC CB  
7815  C CG1 . VAL C 59  ? 0.376 0.606 0.441 0.018  -0.027 0.033  59  VAL CCC CG1 
7816  C CG2 . VAL C 59  ? 0.389 0.627 0.437 0.017  -0.025 0.042  59  VAL CCC CG2 
7817  N N   . LYS C 60  ? 0.405 0.641 0.474 0.014  -0.027 0.039  60  LYS CCC N   
7818  C CA  . LYS C 60  ? 0.412 0.645 0.491 0.014  -0.029 0.036  60  LYS CCC CA  
7819  C C   . LYS C 60  ? 0.421 0.649 0.507 0.015  -0.031 0.029  60  LYS CCC C   
7820  O O   . LYS C 60  ? 0.455 0.682 0.535 0.017  -0.027 0.024  60  LYS CCC O   
7821  C CB  . LYS C 60  ? 0.398 0.633 0.473 0.014  -0.025 0.033  60  LYS CCC CB  
7822  C CG  . LYS C 60  ? 0.404 0.644 0.475 0.013  -0.024 0.040  60  LYS CCC CG  
7823  C CD  . LYS C 60  ? 0.400 0.642 0.469 0.013  -0.021 0.038  60  LYS CCC CD  
7824  C CE  . LYS C 60  ? 0.401 0.646 0.461 0.016  -0.015 0.033  60  LYS CCC CE  
7825  N NZ  . LYS C 60  ? 0.406 0.654 0.455 0.016  -0.013 0.037  60  LYS CCC NZ  
7826  N N   . PRO C 61  ? 0.412 0.635 0.511 0.014  -0.037 0.028  61  PRO CCC N   
7827  C CA  . PRO C 61  ? 0.409 0.628 0.516 0.015  -0.038 0.021  61  PRO CCC CA  
7828  C C   . PRO C 61  ? 0.410 0.631 0.516 0.017  -0.034 0.011  61  PRO CCC C   
7829  O O   . PRO C 61  ? 0.445 0.668 0.550 0.017  -0.031 0.010  61  PRO CCC O   
7830  C CB  . PRO C 61  ? 0.393 0.609 0.517 0.014  -0.046 0.022  61  PRO CCC CB  
7831  C CG  . PRO C 61  ? 0.412 0.630 0.535 0.011  -0.049 0.032  61  PRO CCC CG  
7832  C CD  . PRO C 61  ? 0.402 0.625 0.510 0.011  -0.043 0.035  61  PRO CCC CD  
7833  N N   . SER C 62  ? 0.374 0.593 0.480 0.019  -0.032 0.004  62  SER CCC N   
7834  C CA  . SER C 62  ? 0.376 0.598 0.482 0.020  -0.028 -0.005 62  SER CCC CA  
7835  C C   . SER C 62  ? 0.374 0.596 0.493 0.019  -0.031 -0.010 62  SER CCC C   
7836  O O   . SER C 62  ? 0.366 0.585 0.495 0.018  -0.037 -0.007 62  SER CCC O   
7837  C CB  . SER C 62  ? 0.359 0.579 0.465 0.021  -0.027 -0.010 62  SER CCC CB  
7838  O OG  . SER C 62  ? 0.331 0.548 0.451 0.021  -0.033 -0.014 62  SER CCC OG  
7839  N N   . THR C 63  ? 0.408 0.633 0.526 0.019  -0.027 -0.018 63  THR CCC N   
7840  C CA  . THR C 63  ? 0.436 0.663 0.567 0.018  -0.030 -0.025 63  THR CCC CA  
7841  C C   . THR C 63  ? 0.444 0.668 0.590 0.019  -0.036 -0.030 63  THR CCC C   
7842  O O   . THR C 63  ? 0.430 0.655 0.590 0.018  -0.040 -0.034 63  THR CCC O   
7843  C CB  . THR C 63  ? 0.452 0.684 0.578 0.018  -0.024 -0.033 63  THR CCC CB  
7844  O OG1 . THR C 63  ? 0.453 0.686 0.576 0.019  -0.022 -0.038 63  THR CCC OG1 
7845  C CG2 . THR C 63  ? 0.454 0.689 0.569 0.017  -0.020 -0.029 63  THR CCC CG2 
7846  N N   . GLN C 64  ? 0.454 0.675 0.600 0.020  -0.037 -0.028 64  GLN CCC N   
7847  C CA  . GLN C 64  ? 0.466 0.684 0.627 0.020  -0.043 -0.033 64  GLN CCC CA  
7848  C C   . GLN C 64  ? 0.455 0.667 0.619 0.020  -0.049 -0.023 64  GLN CCC C   
7849  O O   . GLN C 64  ? 0.440 0.649 0.614 0.020  -0.054 -0.025 64  GLN CCC O   
7850  C CB  . GLN C 64  ? 0.476 0.695 0.636 0.022  -0.040 -0.041 64  GLN CCC CB  
7851  C CG  . GLN C 64  ? 0.478 0.705 0.639 0.021  -0.036 -0.052 64  GLN CCC CG  
7852  C CD  . GLN C 64  ? 0.483 0.712 0.661 0.021  -0.040 -0.060 64  GLN CCC CD  
7853  O OE1 . GLN C 64  ? 0.551 0.775 0.743 0.022  -0.047 -0.060 64  GLN CCC OE1 
7854  N NE2 . GLN C 64  ? 0.513 0.748 0.690 0.020  -0.037 -0.066 64  GLN CCC NE2 
7855  N N   . GLY C 65  ? 0.459 0.670 0.614 0.019  -0.049 -0.013 65  GLY CCC N   
7856  C CA  . GLY C 65  ? 0.459 0.667 0.617 0.017  -0.055 -0.003 65  GLY CCC CA  
7857  C C   . GLY C 65  ? 0.475 0.681 0.623 0.017  -0.053 0.002  65  GLY CCC C   
7858  O O   . GLY C 65  ? 0.499 0.703 0.649 0.016  -0.059 0.010  65  GLY CCC O   
7859  N N   . THR C 66  ? 0.473 0.681 0.609 0.019  -0.047 -0.002 66  THR CCC N   
7860  C CA  . THR C 66  ? 0.456 0.664 0.583 0.020  -0.046 0.002  66  THR CCC CA  
7861  C C   . THR C 66  ? 0.458 0.668 0.572 0.019  -0.043 0.011  66  THR CCC C   
7862  O O   . THR C 66  ? 0.475 0.689 0.582 0.019  -0.038 0.011  66  THR CCC O   
7863  C CB  . THR C 66  ? 0.438 0.647 0.559 0.022  -0.040 -0.006 66  THR CCC CB  
7864  O OG1 . THR C 66  ? 0.404 0.612 0.536 0.023  -0.042 -0.015 66  THR CCC OG1 
7865  C CG2 . THR C 66  ? 0.438 0.645 0.552 0.023  -0.040 -0.003 66  THR CCC CG2 
7866  N N   . LYS C 67  ? 0.460 0.669 0.571 0.018  -0.046 0.019  67  LYS CCC N   
7867  C CA  . LYS C 67  ? 0.460 0.674 0.559 0.017  -0.043 0.027  67  LYS CCC CA  
7868  C C   . LYS C 67  ? 0.441 0.655 0.533 0.017  -0.043 0.030  67  LYS CCC C   
7869  O O   . LYS C 67  ? 0.439 0.649 0.538 0.017  -0.046 0.027  67  LYS CCC O   
7870  C CB  . LYS C 67  ? 0.504 0.719 0.606 0.013  -0.047 0.035  67  LYS CCC CB  
7871  C CG  . LYS C 67  ? 0.524 0.737 0.636 0.010  -0.055 0.041  67  LYS CCC CG  
7872  C CD  . LYS C 67  ? 0.553 0.766 0.672 0.007  -0.060 0.048  67  LYS CCC CD  
7873  C CE  . LYS C 67  ? 0.582 0.798 0.700 0.003  -0.066 0.060  67  LYS CCC CE  
7874  N NZ  . LYS C 67  ? 0.595 0.808 0.726 -0.001 -0.074 0.065  67  LYS CCC NZ  
7875  N N   . TRP C 68  ? 0.393 0.612 0.473 0.016  -0.040 0.035  68  TRP CCC N   
7876  C CA  . TRP C 68  ? 0.386 0.606 0.457 0.017  -0.038 0.036  68  TRP CCC CA  
7877  C C   . TRP C 68  ? 0.420 0.647 0.481 0.016  -0.036 0.044  68  TRP CCC C   
7878  O O   . TRP C 68  ? 0.439 0.670 0.500 0.014  -0.036 0.047  68  TRP CCC O   
7879  C CB  . TRP C 68  ? 0.356 0.575 0.421 0.021  -0.032 0.028  68  TRP CCC CB  
7880  C CG  . TRP C 68  ? 0.350 0.571 0.409 0.022  -0.027 0.025  68  TRP CCC CG  
7881  C CD1 . TRP C 68  ? 0.315 0.542 0.364 0.023  -0.023 0.027  68  TRP CCC CD1 
7882  C CD2 . TRP C 68  ? 0.307 0.527 0.372 0.023  -0.025 0.019  68  TRP CCC CD2 
7883  N NE1 . TRP C 68  ? 0.303 0.530 0.351 0.024  -0.019 0.023  68  TRP CCC NE1 
7884  C CE2 . TRP C 68  ? 0.289 0.513 0.346 0.024  -0.021 0.018  68  TRP CCC CE2 
7885  C CE3 . TRP C 68  ? 0.311 0.527 0.386 0.023  -0.028 0.013  68  TRP CCC CE3 
7886  C CZ2 . TRP C 68  ? 0.300 0.523 0.358 0.024  -0.018 0.013  68  TRP CCC CZ2 
7887  C CZ3 . TRP C 68  ? 0.297 0.514 0.374 0.023  -0.025 0.007  68  TRP CCC CZ3 
7888  C CH2 . TRP C 68  ? 0.296 0.517 0.364 0.024  -0.021 0.008  68  TRP CCC CH2 
7889  N N   . GLY C 69  ? 0.406 0.635 0.459 0.016  -0.035 0.046  69  GLY CCC N   
7890  C CA  . GLY C 69  ? 0.391 0.629 0.436 0.014  -0.034 0.052  69  GLY CCC CA  
7891  C C   . GLY C 69  ? 0.362 0.604 0.396 0.017  -0.027 0.048  69  GLY CCC C   
7892  O O   . GLY C 69  ? 0.368 0.608 0.403 0.019  -0.024 0.042  69  GLY CCC O   
7893  N N   . LEU C 70  ? 0.354 0.605 0.381 0.016  -0.026 0.052  70  LEU CCC N   
7894  C CA  . LEU C 70  ? 0.377 0.633 0.394 0.018  -0.020 0.049  70  LEU CCC CA  
7895  C C   . LEU C 70  ? 0.386 0.638 0.399 0.023  -0.017 0.042  70  LEU CCC C   
7896  O O   . LEU C 70  ? 0.345 0.593 0.360 0.023  -0.018 0.040  70  LEU CCC O   
7897  C CB  . LEU C 70  ? 0.397 0.664 0.408 0.016  -0.020 0.055  70  LEU CCC CB  
7898  C CG  . LEU C 70  ? 0.446 0.721 0.448 0.018  -0.015 0.052  70  LEU CCC CG  
7899  C CD1 . LEU C 70  ? 0.446 0.725 0.448 0.019  -0.012 0.051  70  LEU CCC CD1 
7900  C CD2 . LEU C 70  ? 0.462 0.747 0.458 0.016  -0.016 0.056  70  LEU CCC CD2 
7901  N N   . GLY C 71  ? 0.397 0.652 0.406 0.025  -0.012 0.038  71  GLY CCC N   
7902  C CA  . GLY C 71  ? 0.403 0.655 0.407 0.029  -0.009 0.031  71  GLY CCC CA  
7903  C C   . GLY C 71  ? 0.401 0.648 0.406 0.031  -0.007 0.026  71  GLY CCC C   
7904  O O   . GLY C 71  ? 0.424 0.671 0.425 0.034  -0.004 0.022  71  GLY CCC O   
7905  N N   . GLY C 72  ? 0.382 0.626 0.393 0.029  -0.008 0.027  72  GLY CCC N   
7906  C CA  . GLY C 72  ? 0.386 0.628 0.399 0.030  -0.006 0.024  72  GLY CCC CA  
7907  C C   . GLY C 72  ? 0.375 0.611 0.391 0.031  -0.006 0.018  72  GLY CCC C   
7908  O O   . GLY C 72  ? 0.383 0.616 0.403 0.031  -0.009 0.018  72  GLY CCC O   
7909  N N   . THR C 73  ? 0.344 0.577 0.358 0.032  -0.004 0.014  73  THR CCC N   
7910  C CA  . THR C 73  ? 0.341 0.570 0.359 0.032  -0.004 0.009  73  THR CCC CA  
7911  C C   . THR C 73  ? 0.338 0.565 0.353 0.034  -0.003 0.006  73  THR CCC C   
7912  O O   . THR C 73  ? 0.297 0.520 0.316 0.033  -0.005 0.003  73  THR CCC O   
7913  C CB  . THR C 73  ? 0.355 0.585 0.371 0.032  -0.001 0.006  73  THR CCC CB  
7914  O OG1 . THR C 73  ? 0.341 0.572 0.361 0.030  -0.002 0.008  73  THR CCC OG1 
7915  C CG2 . THR C 73  ? 0.348 0.575 0.366 0.032  -0.000 0.000  73  THR CCC CG2 
7916  N N   . CYS C 74  ? 0.344 0.573 0.352 0.036  -0.002 0.006  74  CYS CCC N   
7917  C CA  A CYS C 74  ? 0.365 0.590 0.369 0.037  -0.002 0.003  74  CYS CCC CA  
7918  C CA  B CYS C 74  ? 0.363 0.589 0.368 0.037  -0.002 0.003  74  CYS CCC CA  
7919  C C   . CYS C 74  ? 0.381 0.605 0.389 0.037  -0.004 0.005  74  CYS CCC C   
7920  O O   . CYS C 74  ? 0.332 0.552 0.342 0.037  -0.005 0.002  74  CYS CCC O   
7921  C CB  A CYS C 74  ? 0.385 0.613 0.383 0.040  0.000  0.003  74  CYS CCC CB  
7922  C CB  B CYS C 74  ? 0.382 0.610 0.380 0.040  0.000  0.003  74  CYS CCC CB  
7923  S SG  A CYS C 74  ? 0.437 0.661 0.432 0.041  0.000  -0.001 74  CYS CCC SG  
7924  S SG  B CYS C 74  ? 0.429 0.653 0.424 0.041  0.000  -0.001 74  CYS CCC SG  
7925  N N   . VAL C 75  ? 0.390 0.617 0.398 0.036  -0.006 0.010  75  VAL CCC N   
7926  C CA  . VAL C 75  ? 0.383 0.610 0.394 0.035  -0.009 0.012  75  VAL CCC CA  
7927  C C   . VAL C 75  ? 0.354 0.576 0.374 0.034  -0.012 0.011  75  VAL CCC C   
7928  O O   . VAL C 75  ? 0.393 0.612 0.416 0.034  -0.014 0.010  75  VAL CCC O   
7929  C CB  . VAL C 75  ? 0.429 0.662 0.438 0.034  -0.010 0.019  75  VAL CCC CB  
7930  C CG1 . VAL C 75  ? 0.418 0.650 0.431 0.032  -0.014 0.022  75  VAL CCC CG1 
7931  C CG2 . VAL C 75  ? 0.449 0.687 0.449 0.036  -0.007 0.018  75  VAL CCC CG2 
7932  N N   . ASN C 76  ? 0.314 0.537 0.339 0.032  -0.012 0.012  76  ASN CCC N   
7933  C CA  . ASN C 76  ? 0.302 0.522 0.338 0.030  -0.016 0.012  76  ASN CCC CA  
7934  C C   . ASN C 76  ? 0.276 0.492 0.317 0.031  -0.015 0.005  76  ASN CCC C   
7935  O O   . ASN C 76  ? 0.274 0.487 0.323 0.030  -0.018 0.003  76  ASN CCC O   
7936  C CB  . ASN C 76  ? 0.303 0.525 0.342 0.028  -0.018 0.018  76  ASN CCC CB  
7937  C CG  . ASN C 76  ? 0.332 0.558 0.366 0.027  -0.020 0.025  76  ASN CCC CG  
7938  O OD1 . ASN C 76  ? 0.320 0.545 0.359 0.025  -0.024 0.028  76  ASN CCC OD1 
7939  N ND2 . ASN C 76  ? 0.349 0.581 0.376 0.027  -0.017 0.027  76  ASN CCC ND2 
7940  N N   . VAL C 77  ? 0.253 0.471 0.290 0.031  -0.012 0.002  77  VAL CCC N   
7941  C CA  . VAL C 77  ? 0.245 0.462 0.288 0.030  -0.011 -0.004 77  VAL CCC CA  
7942  C C   . VAL C 77  ? 0.239 0.457 0.274 0.031  -0.007 -0.008 77  VAL CCC C   
7943  O O   . VAL C 77  ? 0.244 0.463 0.281 0.030  -0.006 -0.011 77  VAL CCC O   
7944  C CB  . VAL C 77  ? 0.239 0.457 0.288 0.029  -0.012 -0.003 77  VAL CCC CB  
7945  C CG1 . VAL C 77  ? 0.252 0.468 0.311 0.028  -0.017 -0.001 77  VAL CCC CG1 
7946  C CG2 . VAL C 77  ? 0.238 0.459 0.281 0.028  -0.010 0.001  77  VAL CCC CG2 
7947  N N   . GLY C 78  ? 0.259 0.476 0.286 0.033  -0.006 -0.007 78  GLY CCC N   
7948  C CA  . GLY C 78  ? 0.274 0.492 0.295 0.033  -0.003 -0.009 78  GLY CCC CA  
7949  C C   . GLY C 78  ? 0.299 0.515 0.316 0.035  -0.002 -0.011 78  GLY CCC C   
7950  O O   . GLY C 78  ? 0.291 0.505 0.313 0.034  -0.004 -0.014 78  GLY CCC O   
7951  N N   . CYS C 79  ? 0.310 0.526 0.319 0.036  -0.001 -0.009 79  CYS CCC N   
7952  C CA  . CYS C 79  ? 0.318 0.533 0.323 0.038  -0.001 -0.011 79  CYS CCC CA  
7953  C C   . CYS C 79  ? 0.307 0.520 0.315 0.038  -0.003 -0.011 79  CYS CCC C   
7954  O O   . CYS C 79  ? 0.309 0.519 0.318 0.038  -0.003 -0.014 79  CYS CCC O   
7955  C CB  . CYS C 79  ? 0.367 0.583 0.365 0.040  -0.000 -0.008 79  CYS CCC CB  
7956  S SG  . CYS C 79  ? 0.356 0.576 0.352 0.040  0.001  -0.006 79  CYS CCC SG  
7957  N N   . VAL C 80  ? 0.294 0.507 0.304 0.039  -0.005 -0.007 80  VAL CCC N   
7958  C CA  . VAL C 80  ? 0.284 0.495 0.296 0.039  -0.007 -0.006 80  VAL CCC CA  
7959  C C   . VAL C 80  ? 0.281 0.490 0.301 0.038  -0.009 -0.010 80  VAL CCC C   
7960  O O   . VAL C 80  ? 0.260 0.466 0.280 0.038  -0.009 -0.013 80  VAL CCC O   
7961  C CB  . VAL C 80  ? 0.277 0.491 0.289 0.039  -0.009 -0.000 80  VAL CCC CB  
7962  C CG1 . VAL C 80  ? 0.281 0.493 0.296 0.038  -0.012 0.001  80  VAL CCC CG1 
7963  C CG2 . VAL C 80  ? 0.283 0.502 0.287 0.040  -0.007 0.002  80  VAL CCC CG2 
7964  N N   . PRO C 81  ? 0.284 0.493 0.311 0.036  -0.010 -0.010 81  PRO CCC N   
7965  C CA  . PRO C 81  ? 0.291 0.498 0.328 0.035  -0.012 -0.014 81  PRO CCC CA  
7966  C C   . PRO C 81  ? 0.292 0.499 0.328 0.035  -0.010 -0.021 81  PRO CCC C   
7967  O O   . PRO C 81  ? 0.298 0.504 0.339 0.035  -0.011 -0.025 81  PRO CCC O   
7968  C CB  . PRO C 81  ? 0.295 0.503 0.340 0.034  -0.014 -0.013 81  PRO CCC CB  
7969  C CG  . PRO C 81  ? 0.288 0.498 0.326 0.033  -0.012 -0.009 81  PRO CCC CG  
7970  C CD  . PRO C 81  ? 0.285 0.496 0.314 0.035  -0.011 -0.006 81  PRO CCC CD  
7971  N N   . LYS C 82  ? 0.283 0.493 0.314 0.034  -0.007 -0.021 82  LYS CCC N   
7972  C CA  . LYS C 82  ? 0.293 0.504 0.323 0.033  -0.004 -0.027 82  LYS CCC CA  
7973  C C   . LYS C 82  ? 0.297 0.506 0.323 0.034  -0.004 -0.028 82  LYS CCC C   
7974  O O   . LYS C 82  ? 0.294 0.503 0.323 0.033  -0.004 -0.033 82  LYS CCC O   
7975  C CB  . LYS C 82  ? 0.326 0.540 0.350 0.032  -0.002 -0.026 82  LYS CCC CB  
7976  C CG  . LYS C 82  ? 0.349 0.564 0.369 0.030  0.000  -0.030 82  LYS CCC CG  
7977  C CD  . LYS C 82  ? 0.353 0.567 0.366 0.031  0.001  -0.028 82  LYS CCC CD  
7978  C CE  . LYS C 82  ? 0.359 0.572 0.365 0.033  0.001  -0.023 82  LYS CCC CE  
7979  N NZ  . LYS C 82  ? 0.348 0.563 0.352 0.032  0.002  -0.023 82  LYS CCC NZ  
7980  N N   . LYS C 83  ? 0.296 0.503 0.315 0.036  -0.004 -0.024 83  LYS CCC N   
7981  C CA  . LYS C 83  ? 0.298 0.503 0.312 0.038  -0.004 -0.024 83  LYS CCC CA  
7982  C C   . LYS C 83  ? 0.303 0.505 0.323 0.038  -0.007 -0.026 83  LYS CCC C   
7983  O O   . LYS C 83  ? 0.292 0.493 0.312 0.038  -0.006 -0.029 83  LYS CCC O   
7984  C CB  . LYS C 83  ? 0.318 0.522 0.325 0.040  -0.004 -0.020 83  LYS CCC CB  
7985  C CG  . LYS C 83  ? 0.321 0.524 0.323 0.042  -0.004 -0.021 83  LYS CCC CG  
7986  C CD  . LYS C 83  ? 0.318 0.520 0.316 0.041  -0.003 -0.023 83  LYS CCC CD  
7987  C CE  . LYS C 83  ? 0.320 0.520 0.315 0.042  -0.003 -0.024 83  LYS CCC CE  
7988  N NZ  . LYS C 83  ? 0.306 0.506 0.295 0.044  -0.003 -0.023 83  LYS CCC NZ  
7989  N N   . LEU C 84  ? 0.305 0.507 0.331 0.038  -0.009 -0.024 84  LEU CCC N   
7990  C CA  . LEU C 84  ? 0.297 0.497 0.330 0.039  -0.012 -0.025 84  LEU CCC CA  
7991  C C   . LEU C 84  ? 0.303 0.503 0.344 0.037  -0.012 -0.032 84  LEU CCC C   
7992  O O   . LEU C 84  ? 0.311 0.510 0.355 0.037  -0.013 -0.035 84  LEU CCC O   
7993  C CB  . LEU C 84  ? 0.295 0.494 0.333 0.038  -0.015 -0.020 84  LEU CCC CB  
7994  C CG  . LEU C 84  ? 0.304 0.503 0.333 0.039  -0.015 -0.014 84  LEU CCC CG  
7995  C CD1 . LEU C 84  ? 0.312 0.512 0.346 0.038  -0.019 -0.008 84  LEU CCC CD1 
7996  C CD2 . LEU C 84  ? 0.310 0.509 0.334 0.041  -0.015 -0.013 84  LEU CCC CD2 
7997  N N   . MET C 85  ? 0.312 0.515 0.357 0.036  -0.011 -0.034 85  MET CCC N   
7998  C CA  . MET C 85  ? 0.348 0.553 0.400 0.034  -0.011 -0.042 85  MET CCC CA  
7999  C C   . MET C 85  ? 0.341 0.548 0.387 0.033  -0.008 -0.045 85  MET CCC C   
8000  O O   . MET C 85  ? 0.352 0.561 0.404 0.033  -0.008 -0.051 85  MET CCC O   
8001  C CB  . MET C 85  ? 0.380 0.589 0.436 0.032  -0.010 -0.043 85  MET CCC CB  
8002  C CG  . MET C 85  ? 0.414 0.622 0.477 0.033  -0.013 -0.040 85  MET CCC CG  
8003  S SD  . MET C 85  ? 0.514 0.724 0.594 0.032  -0.017 -0.048 85  MET CCC SD  
8004  C CE  . MET C 85  ? 0.532 0.737 0.619 0.032  -0.022 -0.042 85  MET CCC CE  
8005  N N   . HIS C 86  ? 0.336 0.544 0.373 0.033  -0.006 -0.042 86  HIS CCC N   
8006  C CA  . HIS C 86  ? 0.330 0.540 0.361 0.032  -0.003 -0.045 86  HIS CCC CA  
8007  C C   . HIS C 86  ? 0.317 0.524 0.348 0.033  -0.005 -0.045 86  HIS CCC C   
8008  O O   . HIS C 86  ? 0.264 0.472 0.296 0.032  -0.004 -0.050 86  HIS CCC O   
8009  C CB  . HIS C 86  ? 0.336 0.545 0.357 0.032  -0.002 -0.040 86  HIS CCC CB  
8010  C CG  . HIS C 86  ? 0.344 0.554 0.359 0.031  -0.001 -0.041 86  HIS CCC CG  
8011  N ND1 . HIS C 86  ? 0.333 0.547 0.348 0.027  0.001  -0.045 86  HIS CCC ND1 
8012  C CD2 . HIS C 86  ? 0.332 0.539 0.340 0.032  -0.001 -0.037 86  HIS CCC CD2 
8013  C CE1 . HIS C 86  ? 0.338 0.552 0.347 0.026  0.001  -0.044 86  HIS CCC CE1 
8014  N NE2 . HIS C 86  ? 0.317 0.526 0.322 0.030  0.000  -0.039 86  HIS CCC NE2 
8015  N N   . TYR C 87  ? 0.292 0.494 0.321 0.036  -0.007 -0.041 87  TYR CCC N   
8016  C CA  . TYR C 87  ? 0.296 0.495 0.325 0.038  -0.008 -0.041 87  TYR CCC CA  
8017  C C   . TYR C 87  ? 0.285 0.485 0.324 0.037  -0.010 -0.046 87  TYR CCC C   
8018  O O   . TYR C 87  ? 0.268 0.468 0.308 0.037  -0.010 -0.050 87  TYR CCC O   
8019  C CB  . TYR C 87  ? 0.340 0.536 0.365 0.040  -0.010 -0.035 87  TYR CCC CB  
8020  C CG  . TYR C 87  ? 0.381 0.574 0.404 0.042  -0.011 -0.034 87  TYR CCC CG  
8021  C CD1 . TYR C 87  ? 0.432 0.624 0.448 0.042  -0.010 -0.035 87  TYR CCC CD1 
8022  C CD2 . TYR C 87  ? 0.405 0.595 0.433 0.043  -0.014 -0.033 87  TYR CCC CD2 
8023  C CE1 . TYR C 87  ? 0.475 0.665 0.489 0.044  -0.011 -0.035 87  TYR CCC CE1 
8024  C CE2 . TYR C 87  ? 0.455 0.643 0.481 0.044  -0.015 -0.033 87  TYR CCC CE2 
8025  C CZ  . TYR C 87  ? 0.471 0.658 0.490 0.045  -0.013 -0.034 87  TYR CCC CZ  
8026  O OH  . TYR C 87  ? 0.578 0.763 0.595 0.046  -0.015 -0.034 87  TYR CCC OH  
8027  N N   . SER C 88  ? 0.286 0.485 0.334 0.037  -0.012 -0.047 88  SER CCC N   
8028  C CA  . SER C 88  ? 0.273 0.473 0.332 0.036  -0.014 -0.053 88  SER CCC CA  
8029  C C   . SER C 88  ? 0.268 0.474 0.328 0.034  -0.011 -0.061 88  SER CCC C   
8030  O O   . SER C 88  ? 0.254 0.461 0.320 0.034  -0.012 -0.066 88  SER CCC O   
8031  C CB  . SER C 88  ? 0.277 0.478 0.347 0.036  -0.017 -0.054 88  SER CCC CB  
8032  O OG  . SER C 88  ? 0.254 0.455 0.336 0.036  -0.020 -0.060 88  SER CCC OG  
8033  N N   . ALA C 89  ? 0.262 0.472 0.317 0.032  -0.008 -0.061 89  ALA CCC N   
8034  C CA  . ALA C 89  ? 0.258 0.475 0.313 0.029  -0.005 -0.067 89  ALA CCC CA  
8035  C C   . ALA C 89  ? 0.274 0.490 0.322 0.028  -0.004 -0.067 89  ALA CCC C   
8036  O O   . ALA C 89  ? 0.301 0.522 0.354 0.027  -0.004 -0.074 89  ALA CCC O   
8037  C CB  . ALA C 89  ? 0.236 0.457 0.286 0.026  -0.003 -0.066 89  ALA CCC CB  
8038  N N   . LEU C 90  ? 0.273 0.485 0.312 0.030  -0.004 -0.061 90  LEU CCC N   
8039  C CA  . LEU C 90  ? 0.298 0.509 0.331 0.030  -0.004 -0.060 90  LEU CCC CA  
8040  C C   . LEU C 90  ? 0.304 0.513 0.343 0.031  -0.006 -0.063 90  LEU CCC C   
8041  O O   . LEU C 90  ? 0.318 0.529 0.356 0.030  -0.005 -0.066 90  LEU CCC O   
8042  C CB  . LEU C 90  ? 0.299 0.505 0.322 0.032  -0.004 -0.053 90  LEU CCC CB  
8043  C CG  . LEU C 90  ? 0.325 0.533 0.342 0.030  -0.002 -0.050 90  LEU CCC CG  
8044  C CD1 . LEU C 90  ? 0.322 0.525 0.331 0.033  -0.003 -0.044 90  LEU CCC CD1 
8045  C CD2 . LEU C 90  ? 0.337 0.550 0.352 0.026  -0.000 -0.053 90  LEU CCC CD2 
8046  N N   . ILE C 91  ? 0.280 0.484 0.325 0.034  -0.008 -0.062 91  ILE CCC N   
8047  C CA  . ILE C 91  ? 0.277 0.479 0.328 0.035  -0.011 -0.065 91  ILE CCC CA  
8048  C C   . ILE C 91  ? 0.286 0.494 0.347 0.033  -0.010 -0.073 91  ILE CCC C   
8049  O O   . ILE C 91  ? 0.279 0.487 0.341 0.033  -0.010 -0.077 91  ILE CCC O   
8050  C CB  . ILE C 91  ? 0.269 0.466 0.326 0.038  -0.014 -0.060 91  ILE CCC CB  
8051  C CG1 . ILE C 91  ? 0.264 0.456 0.310 0.040  -0.014 -0.053 91  ILE CCC CG1 
8052  C CG2 . ILE C 91  ? 0.257 0.452 0.324 0.039  -0.018 -0.064 91  ILE CCC CG2 
8053  C CD1 . ILE C 91  ? 0.274 0.462 0.323 0.042  -0.018 -0.048 91  ILE CCC CD1 
8054  N N   . ALA C 92  ? 0.275 0.488 0.343 0.032  -0.010 -0.077 92  ALA CCC N   
8055  C CA  . ALA C 92  ? 0.299 0.519 0.377 0.029  -0.009 -0.087 92  ALA CCC CA  
8056  C C   . ALA C 92  ? 0.289 0.515 0.360 0.026  -0.006 -0.090 92  ALA CCC C   
8057  O O   . ALA C 92  ? 0.269 0.498 0.346 0.026  -0.006 -0.096 92  ALA CCC O   
8058  C CB  . ALA C 92  ? 0.316 0.541 0.399 0.028  -0.009 -0.089 92  ALA CCC CB  
8059  N N   . SER C 93  ? 0.292 0.519 0.352 0.024  -0.003 -0.086 93  SER CCC N   
8060  C CA  . SER C 93  ? 0.290 0.523 0.343 0.021  -0.001 -0.087 93  SER CCC CA  
8061  C C   . SER C 93  ? 0.281 0.510 0.332 0.022  -0.002 -0.086 93  SER CCC C   
8062  O O   . SER C 93  ? 0.281 0.516 0.334 0.019  -0.001 -0.092 93  SER CCC O   
8063  C CB  . SER C 93  ? 0.297 0.530 0.340 0.019  0.001  -0.081 93  SER CCC CB  
8064  O OG  . SER C 93  ? 0.356 0.597 0.402 0.016  0.003  -0.085 93  SER CCC OG  
8065  N N   A SER C 94  ? 0.285 0.505 0.331 0.025  -0.003 -0.080 94  SER CCC N   
8066  N N   B SER C 94  ? 0.280 0.500 0.326 0.025  -0.003 -0.080 94  SER CCC N   
8067  C CA  A SER C 94  ? 0.280 0.495 0.323 0.027  -0.005 -0.078 94  SER CCC CA  
8068  C CA  B SER C 94  ? 0.271 0.487 0.314 0.027  -0.005 -0.078 94  SER CCC CA  
8069  C C   A SER C 94  ? 0.288 0.505 0.341 0.028  -0.006 -0.085 94  SER CCC C   
8070  C C   B SER C 94  ? 0.283 0.500 0.336 0.028  -0.006 -0.085 94  SER CCC C   
8071  O O   A SER C 94  ? 0.288 0.507 0.341 0.026  -0.006 -0.088 94  SER CCC O   
8072  O O   B SER C 94  ? 0.283 0.502 0.336 0.026  -0.006 -0.088 94  SER CCC O   
8073  C CB  A SER C 94  ? 0.285 0.492 0.323 0.031  -0.007 -0.071 94  SER CCC CB  
8074  C CB  B SER C 94  ? 0.271 0.478 0.309 0.031  -0.007 -0.071 94  SER CCC CB  
8075  O OG  A SER C 94  ? 0.290 0.492 0.330 0.034  -0.009 -0.071 94  SER CCC OG  
8076  O OG  B SER C 94  ? 0.263 0.467 0.291 0.031  -0.006 -0.066 94  SER CCC OG  
8077  N N   . ILE C 95  ? 0.291 0.508 0.355 0.029  -0.008 -0.088 95  ILE CCC N   
8078  C CA  . ILE C 95  ? 0.315 0.533 0.392 0.030  -0.010 -0.095 95  ILE CCC CA  
8079  C C   . ILE C 95  ? 0.318 0.547 0.400 0.026  -0.008 -0.104 95  ILE CCC C   
8080  O O   . ILE C 95  ? 0.335 0.566 0.421 0.026  -0.008 -0.109 95  ILE CCC O   
8081  C CB  . ILE C 95  ? 0.327 0.541 0.414 0.033  -0.014 -0.095 95  ILE CCC CB  
8082  C CG1 . ILE C 95  ? 0.340 0.544 0.422 0.036  -0.017 -0.086 95  ILE CCC CG1 
8083  C CG2 . ILE C 95  ? 0.328 0.546 0.430 0.033  -0.016 -0.104 95  ILE CCC CG2 
8084  C CD1 . ILE C 95  ? 0.347 0.548 0.438 0.038  -0.021 -0.085 95  ILE CCC CD1 
8085  N N   . HIS C 96  ? 0.310 0.546 0.392 0.024  -0.006 -0.107 96  HIS CCC N   
8086  C CA  . HIS C 96  ? 0.308 0.557 0.395 0.019  -0.003 -0.116 96  HIS CCC CA  
8087  C C   . HIS C 96  ? 0.293 0.546 0.370 0.016  -0.000 -0.115 96  HIS CCC C   
8088  O O   . HIS C 96  ? 0.347 0.607 0.429 0.014  0.000  -0.122 96  HIS CCC O   
8089  C CB  . HIS C 96  ? 0.317 0.573 0.405 0.017  -0.001 -0.118 96  HIS CCC CB  
8090  C CG  . HIS C 96  ? 0.352 0.622 0.444 0.012  0.002  -0.128 96  HIS CCC CG  
8091  N ND1 . HIS C 96  ? 0.375 0.654 0.458 0.007  0.005  -0.127 96  HIS CCC ND1 
8092  C CD2 . HIS C 96  ? 0.363 0.641 0.469 0.011  0.001  -0.139 96  HIS CCC CD2 
8093  C CE1 . HIS C 96  ? 0.383 0.675 0.473 0.003  0.007  -0.137 96  HIS CCC CE1 
8094  N NE2 . HIS C 96  ? 0.392 0.685 0.496 0.006  0.005  -0.145 96  HIS CCC NE2 
8095  N N   . HIS C 97  ? 0.298 0.547 0.362 0.015  0.001  -0.107 97  HIS CCC N   
8096  C CA  . HIS C 97  ? 0.278 0.533 0.333 0.010  0.003  -0.105 97  HIS CCC CA  
8097  C C   . HIS C 97  ? 0.254 0.501 0.304 0.012  0.001  -0.102 97  HIS CCC C   
8098  O O   . HIS C 97  ? 0.265 0.518 0.312 0.008  0.002  -0.103 97  HIS CCC O   
8099  C CB  . HIS C 97  ? 0.280 0.533 0.324 0.008  0.004  -0.098 97  HIS CCC CB  
8100  C CG  . HIS C 97  ? 0.289 0.551 0.335 0.004  0.006  -0.101 97  HIS CCC CG  
8101  N ND1 . HIS C 97  ? 0.283 0.559 0.332 -0.001 0.008  -0.109 97  HIS CCC ND1 
8102  C CD2 . HIS C 97  ? 0.287 0.547 0.333 0.006  0.006  -0.099 97  HIS CCC CD2 
8103  C CE1 . HIS C 97  ? 0.270 0.552 0.321 -0.003 0.010  -0.111 97  HIS CCC CE1 
8104  N NE2 . HIS C 97  ? 0.292 0.564 0.341 0.001  0.008  -0.105 97  HIS CCC NE2 
8105  N N   . ASP C 98  ? 0.229 0.465 0.278 0.017  -0.001 -0.096 98  ASP CCC N   
8106  C CA  . ASP C 98  ? 0.222 0.451 0.263 0.019  -0.002 -0.090 98  ASP CCC CA  
8107  C C   . ASP C 98  ? 0.206 0.429 0.254 0.023  -0.005 -0.092 98  ASP CCC C   
8108  O O   . ASP C 98  ? 0.204 0.426 0.248 0.022  -0.005 -0.091 98  ASP CCC O   
8109  C CB  . ASP C 98  ? 0.227 0.447 0.260 0.022  -0.003 -0.082 98  ASP CCC CB  
8110  C CG  . ASP C 98  ? 0.239 0.462 0.265 0.019  -0.002 -0.078 98  ASP CCC CG  
8111  O OD1 . ASP C 98  ? 0.219 0.451 0.245 0.013  0.000  -0.081 98  ASP CCC OD1 
8112  O OD2 . ASP C 98  ? 0.250 0.467 0.270 0.021  -0.003 -0.072 98  ASP CCC OD2 
8113  N N   . ALA C 99  ? 0.201 0.421 0.257 0.026  -0.007 -0.094 99  ALA CCC N   
8114  C CA  . ALA C 99  ? 0.210 0.423 0.270 0.030  -0.010 -0.094 99  ALA CCC CA  
8115  C C   . ALA C 99  ? 0.230 0.448 0.296 0.028  -0.010 -0.100 99  ALA CCC C   
8116  O O   . ALA C 99  ? 0.236 0.447 0.298 0.030  -0.011 -0.097 99  ALA CCC O   
8117  C CB  . ALA C 99  ? 0.196 0.407 0.267 0.032  -0.012 -0.095 99  ALA CCC CB  
8118  N N   . GLN C 100 ? 0.258 0.485 0.331 0.025  -0.008 -0.108 100 GLN CCC N   
8119  C CA  . GLN C 100 ? 0.275 0.506 0.354 0.024  -0.008 -0.115 100 GLN CCC CA  
8120  C C   . GLN C 100 ? 0.291 0.523 0.359 0.021  -0.007 -0.111 100 GLN CCC C   
8121  O O   . GLN C 100 ? 0.289 0.517 0.356 0.023  -0.008 -0.111 100 GLN CCC O   
8122  C CB  . GLN C 100 ? 0.281 0.525 0.371 0.021  -0.007 -0.126 100 GLN CCC CB  
8123  C CG  . GLN C 100 ? 0.311 0.559 0.408 0.020  -0.007 -0.133 100 GLN CCC CG  
8124  C CD  . GLN C 100 ? 0.314 0.574 0.424 0.019  -0.006 -0.145 100 GLN CCC CD  
8125  O OE1 . GLN C 100 ? 0.314 0.580 0.429 0.017  -0.006 -0.149 100 GLN CCC OE1 
8126  N NE2 . GLN C 100 ? 0.326 0.590 0.444 0.018  -0.007 -0.152 100 GLN CCC NE2 
8127  N N   . MET C 101 ? 0.303 0.539 0.362 0.018  -0.004 -0.108 101 MET CCC N   
8128  C CA  . MET C 101 ? 0.307 0.544 0.356 0.015  -0.003 -0.104 101 MET CCC CA  
8129  C C   . MET C 101 ? 0.296 0.521 0.339 0.019  -0.006 -0.097 101 MET CCC C   
8130  O O   . MET C 101 ? 0.313 0.537 0.351 0.018  -0.006 -0.095 101 MET CCC O   
8131  C CB  . MET C 101 ? 0.323 0.564 0.363 0.010  -0.002 -0.100 101 MET CCC CB  
8132  C CG  . MET C 101 ? 0.328 0.583 0.372 0.005  0.001  -0.107 101 MET CCC CG  
8133  S SD  . MET C 101 ? 0.381 0.648 0.427 -0.001 0.003  -0.113 101 MET CCC SD  
8134  C CE  . MET C 101 ? 0.344 0.607 0.376 -0.004 0.002  -0.103 101 MET CCC CE  
8135  N N   . PHE C 102 ? 0.275 0.491 0.317 0.024  -0.008 -0.092 102 PHE CCC N   
8136  C CA  . PHE C 102 ? 0.274 0.479 0.310 0.028  -0.010 -0.086 102 PHE CCC CA  
8137  C C   . PHE C 102 ? 0.285 0.486 0.328 0.032  -0.012 -0.088 102 PHE CCC C   
8138  O O   . PHE C 102 ? 0.292 0.485 0.332 0.035  -0.014 -0.083 102 PHE CCC O   
8139  C CB  . PHE C 102 ? 0.263 0.463 0.292 0.030  -0.010 -0.079 102 PHE CCC CB  
8140  C CG  . PHE C 102 ? 0.249 0.453 0.271 0.026  -0.009 -0.075 102 PHE CCC CG  
8141  C CD1 . PHE C 102 ? 0.244 0.455 0.266 0.022  -0.007 -0.078 102 PHE CCC CD1 
8142  C CD2 . PHE C 102 ? 0.242 0.440 0.256 0.027  -0.010 -0.071 102 PHE CCC CD2 
8143  C CE1 . PHE C 102 ? 0.240 0.453 0.254 0.019  -0.006 -0.074 102 PHE CCC CE1 
8144  C CE2 . PHE C 102 ? 0.243 0.443 0.250 0.024  -0.010 -0.067 102 PHE CCC CE2 
8145  C CZ  . PHE C 102 ? 0.252 0.460 0.260 0.019  -0.008 -0.069 102 PHE CCC CZ  
8146  N N   . GLY C 103 ? 0.316 0.522 0.369 0.030  -0.012 -0.095 103 GLY CCC N   
8147  C CA  . GLY C 103 ? 0.318 0.521 0.379 0.033  -0.015 -0.098 103 GLY CCC CA  
8148  C C   . GLY C 103 ? 0.323 0.522 0.392 0.036  -0.017 -0.099 103 GLY CCC C   
8149  O O   . GLY C 103 ? 0.369 0.565 0.445 0.038  -0.020 -0.101 103 GLY CCC O   
8150  N N   . HIS C 104 ? 0.303 0.504 0.373 0.036  -0.017 -0.098 104 HIS CCC N   
8151  C CA  . HIS C 104 ? 0.300 0.497 0.379 0.038  -0.020 -0.098 104 HIS CCC CA  
8152  C C   . HIS C 104 ? 0.307 0.512 0.397 0.036  -0.019 -0.106 104 HIS CCC C   
8153  O O   . HIS C 104 ? 0.286 0.497 0.375 0.034  -0.017 -0.107 104 HIS CCC O   
8154  C CB  . HIS C 104 ? 0.281 0.474 0.352 0.040  -0.020 -0.090 104 HIS CCC CB  
8155  C CG  . HIS C 104 ? 0.269 0.455 0.329 0.042  -0.020 -0.082 104 HIS CCC CG  
8156  N ND1 . HIS C 104 ? 0.264 0.443 0.325 0.045  -0.023 -0.079 104 HIS CCC ND1 
8157  C CD2 . HIS C 104 ? 0.272 0.458 0.321 0.041  -0.018 -0.078 104 HIS CCC CD2 
8158  C CE1 . HIS C 104 ? 0.263 0.439 0.314 0.046  -0.023 -0.073 104 HIS CCC CE1 
8159  N NE2 . HIS C 104 ? 0.255 0.434 0.298 0.044  -0.020 -0.073 104 HIS CCC NE2 
8160  N N   . LYS C 105 ? 0.334 0.541 0.436 0.037  -0.021 -0.113 105 LYS CCC N   
8161  C CA  . LYS C 105 ? 0.375 0.590 0.492 0.036  -0.022 -0.123 105 LYS CCC CA  
8162  C C   . LYS C 105 ? 0.376 0.585 0.500 0.039  -0.026 -0.120 105 LYS CCC C   
8163  O O   . LYS C 105 ? 0.355 0.555 0.482 0.042  -0.030 -0.116 105 LYS CCC O   
8164  C CB  . LYS C 105 ? 0.386 0.604 0.513 0.036  -0.023 -0.131 105 LYS CCC CB  
8165  C CG  . LYS C 105 ? 0.429 0.657 0.572 0.035  -0.024 -0.143 105 LYS CCC CG  
8166  C CD  . LYS C 105 ? 0.465 0.706 0.606 0.031  -0.019 -0.149 105 LYS CCC CD  
8167  C CE  . LYS C 105 ? 0.496 0.745 0.647 0.030  -0.018 -0.156 105 LYS CCC CE  
8168  N NZ  . LYS C 105 ? 0.472 0.726 0.642 0.031  -0.022 -0.168 105 LYS CCC NZ  
8169  N N   . THR C 106 ? 0.367 0.581 0.494 0.037  -0.024 -0.122 106 THR CCC N   
8170  C CA  . THR C 106 ? 0.419 0.627 0.551 0.039  -0.028 -0.118 106 THR CCC CA  
8171  C C   . THR C 106 ? 0.446 0.662 0.593 0.038  -0.029 -0.128 106 THR CCC C   
8172  O O   . THR C 106 ? 0.525 0.751 0.671 0.035  -0.025 -0.135 106 THR CCC O   
8173  C CB  . THR C 106 ? 0.420 0.626 0.538 0.039  -0.025 -0.109 106 THR CCC CB  
8174  O OG1 . THR C 106 ? 0.462 0.678 0.579 0.035  -0.021 -0.115 106 THR CCC OG1 
8175  C CG2 . THR C 106 ? 0.408 0.609 0.511 0.039  -0.023 -0.102 106 THR CCC CG2 
8176  N N   . SER C 107 ? 0.424 0.636 0.582 0.040  -0.034 -0.127 107 SER CCC N   
8177  C CA  . SER C 107 ? 0.429 0.646 0.597 0.040  -0.034 -0.133 107 SER CCC CA  
8178  C C   . SER C 107 ? 0.380 0.590 0.544 0.040  -0.036 -0.124 107 SER CCC C   
8179  O O   . SER C 107 ? 0.358 0.559 0.518 0.042  -0.039 -0.115 107 SER CCC O   
8180  C CB  . SER C 107 ? 0.428 0.647 0.617 0.041  -0.039 -0.144 107 SER CCC CB  
8181  O OG  . SER C 107 ? 0.429 0.638 0.625 0.044  -0.046 -0.139 107 SER CCC OG  
8182  N N   . SER C 108 ? 0.371 0.586 0.535 0.039  -0.034 -0.126 108 SER CCC N   
8183  C CA  . SER C 108 ? 0.384 0.595 0.544 0.039  -0.035 -0.117 108 SER CCC CA  
8184  C C   . SER C 108 ? 0.399 0.615 0.570 0.039  -0.036 -0.124 108 SER CCC C   
8185  O O   . SER C 108 ? 0.390 0.616 0.565 0.037  -0.033 -0.134 108 SER CCC O   
8186  C CB  . SER C 108 ? 0.399 0.611 0.540 0.038  -0.029 -0.110 108 SER CCC CB  
8187  O OG  . SER C 108 ? 0.422 0.628 0.557 0.038  -0.030 -0.102 108 SER CCC OG  
8188  N N   . SER C 109 ? 0.406 0.616 0.583 0.040  -0.041 -0.118 109 SER CCC N   
8189  C CA  . SER C 109 ? 0.411 0.625 0.595 0.039  -0.041 -0.122 109 SER CCC CA  
8190  C C   . SER C 109 ? 0.397 0.605 0.572 0.039  -0.041 -0.111 109 SER CCC C   
8191  O O   . SER C 109 ? 0.381 0.581 0.551 0.040  -0.044 -0.101 109 SER CCC O   
8192  C CB  . SER C 109 ? 0.447 0.662 0.653 0.040  -0.047 -0.130 109 SER CCC CB  
8193  O OG  . SER C 109 ? 0.480 0.685 0.693 0.042  -0.054 -0.125 109 SER CCC OG  
8194  N N   . PHE C 110 ? 0.390 0.603 0.562 0.037  -0.038 -0.112 110 PHE CCC N   
8195  C CA  . PHE C 110 ? 0.393 0.602 0.555 0.037  -0.037 -0.102 110 PHE CCC CA  
8196  C C   . PHE C 110 ? 0.395 0.602 0.571 0.038  -0.043 -0.101 110 PHE CCC C   
8197  O O   . PHE C 110 ? 0.396 0.608 0.586 0.037  -0.045 -0.110 110 PHE CCC O   
8198  C CB  . PHE C 110 ? 0.384 0.601 0.536 0.035  -0.031 -0.103 110 PHE CCC CB  
8199  C CG  . PHE C 110 ? 0.401 0.614 0.544 0.035  -0.030 -0.094 110 PHE CCC CG  
8200  C CD1 . PHE C 110 ? 0.420 0.626 0.552 0.036  -0.031 -0.083 110 PHE CCC CD1 
8201  C CD2 . PHE C 110 ? 0.376 0.593 0.523 0.033  -0.030 -0.096 110 PHE CCC CD2 
8202  C CE1 . PHE C 110 ? 0.418 0.623 0.543 0.035  -0.030 -0.075 110 PHE CCC CE1 
8203  C CE2 . PHE C 110 ? 0.377 0.591 0.516 0.033  -0.029 -0.087 110 PHE CCC CE2 
8204  C CZ  . PHE C 110 ? 0.396 0.604 0.524 0.034  -0.029 -0.077 110 PHE CCC CZ  
8205  N N   . GLU C 111 ? 0.403 0.602 0.576 0.038  -0.047 -0.090 111 GLU CCC N   
8206  C CA  . GLU C 111 ? 0.433 0.629 0.617 0.038  -0.053 -0.087 111 GLU CCC CA  
8207  C C   . GLU C 111 ? 0.394 0.588 0.564 0.037  -0.050 -0.077 111 GLU CCC C   
8208  O O   . GLU C 111 ? 0.371 0.561 0.531 0.037  -0.050 -0.067 111 GLU CCC O   
8209  C CB  . GLU C 111 ? 0.500 0.688 0.695 0.039  -0.061 -0.084 111 GLU CCC CB  
8210  C CG  . GLU C 111 ? 0.580 0.771 0.791 0.040  -0.064 -0.096 111 GLU CCC CG  
8211  C CD  . GLU C 111 ? 0.643 0.840 0.872 0.041  -0.065 -0.108 111 GLU CCC CD  
8212  O OE1 . GLU C 111 ? 0.628 0.829 0.868 0.041  -0.066 -0.119 111 GLU CCC OE1 
8213  O OE2 . GLU C 111 ? 0.640 0.837 0.871 0.040  -0.066 -0.107 111 GLU CCC OE2 
8214  N N   . TRP C 112 ? 0.371 0.570 0.543 0.036  -0.048 -0.081 112 TRP CCC N   
8215  C CA  . TRP C 112 ? 0.354 0.554 0.515 0.035  -0.045 -0.074 112 TRP CCC CA  
8216  C C   . TRP C 112 ? 0.345 0.539 0.505 0.035  -0.049 -0.063 112 TRP CCC C   
8217  O O   . TRP C 112 ? 0.322 0.515 0.467 0.035  -0.046 -0.054 112 TRP CCC O   
8218  C CB  . TRP C 112 ? 0.349 0.555 0.518 0.034  -0.044 -0.081 112 TRP CCC CB  
8219  C CG  . TRP C 112 ? 0.349 0.555 0.510 0.033  -0.041 -0.075 112 TRP CCC CG  
8220  C CD1 . TRP C 112 ? 0.343 0.546 0.510 0.033  -0.046 -0.069 112 TRP CCC CD1 
8221  C CD2 . TRP C 112 ? 0.325 0.535 0.470 0.032  -0.035 -0.072 112 TRP CCC CD2 
8222  N NE1 . TRP C 112 ? 0.356 0.561 0.512 0.032  -0.042 -0.064 112 TRP CCC NE1 
8223  C CE2 . TRP C 112 ? 0.328 0.537 0.471 0.031  -0.035 -0.066 112 TRP CCC CE2 
8224  C CE3 . TRP C 112 ? 0.315 0.529 0.448 0.031  -0.028 -0.075 112 TRP CCC CE3 
8225  C CZ2 . TRP C 112 ? 0.313 0.525 0.443 0.030  -0.030 -0.062 112 TRP CCC CZ2 
8226  C CZ3 . TRP C 112 ? 0.288 0.505 0.409 0.030  -0.024 -0.071 112 TRP CCC CZ3 
8227  C CH2 . TRP C 112 ? 0.303 0.518 0.422 0.030  -0.024 -0.065 112 TRP CCC CH2 
8228  N N   . GLY C 113 ? 0.346 0.535 0.520 0.035  -0.057 -0.062 113 GLY CCC N   
8229  C CA  . GLY C 113 ? 0.372 0.556 0.547 0.034  -0.062 -0.050 113 GLY CCC CA  
8230  C C   . GLY C 113 ? 0.379 0.559 0.542 0.034  -0.062 -0.042 113 GLY CCC C   
8231  O O   . GLY C 113 ? 0.382 0.560 0.538 0.033  -0.063 -0.031 113 GLY CCC O   
8232  N N   . LYS C 114 ? 0.378 0.557 0.538 0.035  -0.061 -0.045 114 LYS CCC N   
8233  C CA  . LYS C 114 ? 0.376 0.553 0.525 0.035  -0.060 -0.038 114 LYS CCC CA  
8234  C C   . LYS C 114 ? 0.350 0.530 0.481 0.035  -0.053 -0.034 114 LYS CCC C   
8235  O O   . LYS C 114 ? 0.381 0.560 0.502 0.035  -0.053 -0.025 114 LYS CCC O   
8236  C CB  . LYS C 114 ? 0.393 0.568 0.546 0.037  -0.061 -0.044 114 LYS CCC CB  
8237  C CG  . LYS C 114 ? 0.410 0.583 0.553 0.037  -0.060 -0.038 114 LYS CCC CG  
8238  C CD  . LYS C 114 ? 0.433 0.602 0.574 0.036  -0.065 -0.027 114 LYS CCC CD  
8239  C CE  . LYS C 114 ? 0.464 0.631 0.596 0.036  -0.065 -0.022 114 LYS CCC CE  
8240  N NZ  . LYS C 114 ? 0.494 0.659 0.624 0.034  -0.070 -0.011 114 LYS CCC NZ  
8241  N N   . LEU C 115 ? 0.319 0.504 0.445 0.036  -0.047 -0.041 115 LEU CCC N   
8242  C CA  . LEU C 115 ? 0.304 0.492 0.414 0.036  -0.040 -0.038 115 LEU CCC CA  
8243  C C   . LEU C 115 ? 0.296 0.485 0.402 0.035  -0.040 -0.031 115 LEU CCC C   
8244  O O   . LEU C 115 ? 0.317 0.506 0.412 0.035  -0.038 -0.024 115 LEU CCC O   
8245  C CB  . LEU C 115 ? 0.276 0.469 0.385 0.036  -0.035 -0.047 115 LEU CCC CB  
8246  C CG  . LEU C 115 ? 0.259 0.455 0.353 0.036  -0.029 -0.044 115 LEU CCC CG  
8247  C CD1 . LEU C 115 ? 0.262 0.456 0.343 0.037  -0.026 -0.039 115 LEU CCC CD1 
8248  C CD2 . LEU C 115 ? 0.266 0.467 0.360 0.035  -0.024 -0.052 115 LEU CCC CD2 
8249  N N   . VAL C 116 ? 0.300 0.489 0.417 0.034  -0.043 -0.033 116 VAL CCC N   
8250  C CA  . VAL C 116 ? 0.321 0.511 0.437 0.032  -0.044 -0.026 116 VAL CCC CA  
8251  C C   . VAL C 116 ? 0.348 0.534 0.461 0.032  -0.048 -0.016 116 VAL CCC C   
8252  O O   . VAL C 116 ? 0.379 0.568 0.482 0.031  -0.046 -0.010 116 VAL CCC O   
8253  C CB  . VAL C 116 ? 0.319 0.509 0.450 0.032  -0.048 -0.031 116 VAL CCC CB  
8254  C CG1 . VAL C 116 ? 0.346 0.535 0.480 0.030  -0.052 -0.023 116 VAL CCC CG1 
8255  C CG2 . VAL C 116 ? 0.312 0.506 0.442 0.032  -0.043 -0.039 116 VAL CCC CG2 
8256  N N   . GLU C 117 ? 0.378 0.561 0.501 0.031  -0.054 -0.016 117 GLU CCC N   
8257  C CA  . GLU C 117 ? 0.395 0.575 0.515 0.030  -0.059 -0.006 117 GLU CCC CA  
8258  C C   . GLU C 117 ? 0.392 0.575 0.496 0.030  -0.054 -0.001 117 GLU CCC C   
8259  O O   . GLU C 117 ? 0.412 0.597 0.508 0.029  -0.054 0.007  117 GLU CCC O   
8260  C CB  . GLU C 117 ? 0.410 0.585 0.544 0.029  -0.067 -0.007 117 GLU CCC CB  
8261  C CG  . GLU C 117 ? 0.439 0.612 0.572 0.027  -0.072 0.003  117 GLU CCC CG  
8262  C CD  . GLU C 117 ? 0.492 0.660 0.634 0.028  -0.078 0.001  117 GLU CCC CD  
8263  O OE1 . GLU C 117 ? 0.516 0.684 0.649 0.028  -0.076 0.004  117 GLU CCC OE1 
8264  O OE2 . GLU C 117 ? 0.512 0.677 0.671 0.028  -0.083 -0.004 117 GLU CCC OE2 
8265  N N   . THR C 118 ? 0.369 0.552 0.467 0.032  -0.050 -0.007 118 THR CCC N   
8266  C CA  . THR C 118 ? 0.356 0.540 0.438 0.033  -0.045 -0.004 118 THR CCC CA  
8267  C C   . THR C 118 ? 0.342 0.531 0.414 0.033  -0.040 -0.002 118 THR CCC C   
8268  O O   . THR C 118 ? 0.329 0.521 0.391 0.033  -0.039 0.004  118 THR CCC O   
8269  C CB  . THR C 118 ? 0.368 0.551 0.448 0.036  -0.042 -0.011 118 THR CCC CB  
8270  O OG1 . THR C 118 ? 0.385 0.565 0.473 0.036  -0.047 -0.012 118 THR CCC OG1 
8271  C CG2 . THR C 118 ? 0.374 0.560 0.440 0.037  -0.037 -0.010 118 THR CCC CG2 
8272  N N   . LEU C 119 ? 0.329 0.520 0.404 0.034  -0.037 -0.006 119 LEU CCC N   
8273  C CA  . LEU C 119 ? 0.342 0.537 0.409 0.033  -0.033 -0.004 119 LEU CCC CA  
8274  C C   . LEU C 119 ? 0.342 0.539 0.409 0.031  -0.036 0.004  119 LEU CCC C   
8275  O O   . LEU C 119 ? 0.284 0.484 0.340 0.031  -0.034 0.009  119 LEU CCC O   
8276  C CB  . LEU C 119 ? 0.334 0.530 0.406 0.033  -0.031 -0.010 119 LEU CCC CB  
8277  C CG  . LEU C 119 ? 0.345 0.543 0.409 0.034  -0.025 -0.016 119 LEU CCC CG  
8278  C CD1 . LEU C 119 ? 0.362 0.557 0.429 0.035  -0.026 -0.021 119 LEU CCC CD1 
8279  C CD2 . LEU C 119 ? 0.347 0.547 0.415 0.034  -0.023 -0.021 119 LEU CCC CD2 
8280  N N   . ARG C 120 ? 0.378 0.572 0.456 0.029  -0.041 0.005  120 ARG CCC N   
8281  C CA  . ARG C 120 ? 0.411 0.607 0.493 0.027  -0.045 0.014  120 ARG CCC CA  
8282  C C   . ARG C 120 ? 0.414 0.612 0.487 0.025  -0.047 0.021  120 ARG CCC C   
8283  O O   . ARG C 120 ? 0.408 0.611 0.474 0.024  -0.045 0.027  120 ARG CCC O   
8284  C CB  . ARG C 120 ? 0.461 0.653 0.558 0.025  -0.052 0.014  120 ARG CCC CB  
8285  C CG  . ARG C 120 ? 0.535 0.727 0.639 0.025  -0.052 0.010  120 ARG CCC CG  
8286  C CD  . ARG C 120 ? 0.649 0.838 0.769 0.023  -0.060 0.012  120 ARG CCC CD  
8287  N NE  . ARG C 120 ? 0.714 0.899 0.848 0.024  -0.064 0.004  120 ARG CCC NE  
8288  C CZ  . ARG C 120 ? 0.733 0.914 0.875 0.024  -0.069 0.004  120 ARG CCC CZ  
8289  N NH1 . ARG C 120 ? 0.764 0.944 0.900 0.023  -0.071 0.011  120 ARG CCC NH1 
8290  N NH2 . ARG C 120 ? 0.763 0.942 0.918 0.026  -0.072 -0.005 120 ARG CCC NH2 
8291  N N   . ASN C 121 ? 0.422 0.617 0.497 0.026  -0.049 0.021  121 ASN CCC N   
8292  C CA  . ASN C 121 ? 0.423 0.620 0.490 0.024  -0.051 0.028  121 ASN CCC CA  
8293  C C   . ASN C 121 ? 0.406 0.609 0.459 0.026  -0.045 0.028  121 ASN CCC C   
8294  O O   . ASN C 121 ? 0.390 0.599 0.437 0.024  -0.045 0.035  121 ASN CCC O   
8295  C CB  . ASN C 121 ? 0.457 0.650 0.528 0.024  -0.055 0.027  121 ASN CCC CB  
8296  C CG  . ASN C 121 ? 0.491 0.679 0.579 0.023  -0.063 0.028  121 ASN CCC CG  
8297  O OD1 . ASN C 121 ? 0.511 0.698 0.606 0.021  -0.066 0.030  121 ASN CCC OD1 
8298  N ND2 . ASN C 121 ? 0.537 0.721 0.630 0.023  -0.066 0.026  121 ASN CCC ND2 
8299  N N   . HIS C 122 ? 0.388 0.590 0.437 0.029  -0.039 0.021  122 HIS CCC N   
8300  C CA  . HIS C 122 ? 0.389 0.596 0.425 0.031  -0.034 0.021  122 HIS CCC CA  
8301  C C   . HIS C 122 ? 0.391 0.603 0.423 0.030  -0.031 0.023  122 HIS CCC C   
8302  O O   . HIS C 122 ? 0.373 0.591 0.396 0.030  -0.029 0.027  122 HIS CCC O   
8303  C CB  . HIS C 122 ? 0.373 0.577 0.407 0.034  -0.030 0.013  122 HIS CCC CB  
8304  C CG  . HIS C 122 ? 0.348 0.556 0.370 0.036  -0.025 0.012  122 HIS CCC CG  
8305  N ND1 . HIS C 122 ? 0.351 0.561 0.368 0.037  -0.021 0.010  122 HIS CCC ND1 
8306  C CD2 . HIS C 122 ? 0.342 0.552 0.358 0.037  -0.025 0.013  122 HIS CCC CD2 
8307  C CE1 . HIS C 122 ? 0.358 0.571 0.366 0.039  -0.018 0.009  122 HIS CCC CE1 
8308  N NE2 . HIS C 122 ? 0.345 0.558 0.352 0.039  -0.021 0.011  122 HIS CCC NE2 
8309  N N   . ILE C 123 ? 0.375 0.585 0.413 0.029  -0.031 0.021  123 ILE CCC N   
8310  C CA  . ILE C 123 ? 0.384 0.599 0.419 0.029  -0.029 0.024  123 ILE CCC CA  
8311  C C   . ILE C 123 ? 0.431 0.650 0.467 0.025  -0.033 0.032  123 ILE CCC C   
8312  O O   . ILE C 123 ? 0.419 0.644 0.447 0.025  -0.030 0.035  123 ILE CCC O   
8313  C CB  . ILE C 123 ? 0.349 0.561 0.392 0.029  -0.028 0.019  123 ILE CCC CB  
8314  C CG1 . ILE C 123 ? 0.345 0.555 0.384 0.032  -0.024 0.012  123 ILE CCC CG1 
8315  C CG2 . ILE C 123 ? 0.354 0.570 0.397 0.027  -0.028 0.023  123 ILE CCC CG2 
8316  C CD1 . ILE C 123 ? 0.354 0.562 0.401 0.032  -0.023 0.006  123 ILE CCC CD1 
8317  N N   . ARG C 124 ? 0.434 0.650 0.479 0.023  -0.039 0.036  124 ARG CCC N   
8318  C CA  . ARG C 124 ? 0.474 0.695 0.519 0.018  -0.043 0.045  124 ARG CCC CA  
8319  C C   . ARG C 124 ? 0.500 0.728 0.533 0.018  -0.041 0.049  124 ARG CCC C   
8320  O O   . ARG C 124 ? 0.434 0.670 0.461 0.016  -0.039 0.053  124 ARG CCC O   
8321  C CB  . ARG C 124 ? 0.500 0.715 0.556 0.016  -0.051 0.049  124 ARG CCC CB  
8322  C CG  . ARG C 124 ? 0.560 0.778 0.621 0.011  -0.056 0.058  124 ARG CCC CG  
8323  C CD  . ARG C 124 ? 0.601 0.812 0.675 0.008  -0.065 0.061  124 ARG CCC CD  
8324  N NE  . ARG C 124 ? 0.625 0.829 0.711 0.011  -0.066 0.053  124 ARG CCC NE  
8325  C CZ  . ARG C 124 ? 0.645 0.843 0.736 0.013  -0.068 0.047  124 ARG CCC CZ  
8326  N NH1 . ARG C 124 ? 0.658 0.855 0.744 0.013  -0.069 0.049  124 ARG CCC NH1 
8327  N NH2 . ARG C 124 ? 0.637 0.830 0.740 0.016  -0.069 0.040  124 ARG CCC NH2 
8328  N N   . MET C 125 ? 0.508 0.734 0.537 0.020  -0.040 0.046  125 MET CCC N   
8329  C CA  . MET C 125 ? 0.524 0.758 0.543 0.020  -0.037 0.047  125 MET CCC CA  
8330  C C   . MET C 125 ? 0.501 0.741 0.511 0.022  -0.031 0.045  125 MET CCC C   
8331  O O   . MET C 125 ? 0.508 0.757 0.511 0.020  -0.030 0.049  125 MET CCC O   
8332  C CB  . MET C 125 ? 0.592 0.821 0.609 0.023  -0.037 0.042  125 MET CCC CB  
8333  C CG  . MET C 125 ? 0.620 0.856 0.627 0.023  -0.035 0.043  125 MET CCC CG  
8334  S SD  . MET C 125 ? 0.804 1.046 0.801 0.028  -0.027 0.037  125 MET CCC SD  
8335  C CE  . MET C 125 ? 0.746 0.977 0.747 0.032  -0.025 0.028  125 MET CCC CE  
8336  N N   . LEU C 126 ? 0.476 0.713 0.488 0.025  -0.028 0.039  126 LEU CCC N   
8337  C CA  . LEU C 126 ? 0.434 0.675 0.438 0.027  -0.022 0.036  126 LEU CCC CA  
8338  C C   . LEU C 126 ? 0.390 0.638 0.396 0.024  -0.023 0.041  126 LEU CCC C   
8339  O O   . LEU C 126 ? 0.368 0.623 0.367 0.025  -0.020 0.041  126 LEU CCC O   
8340  C CB  . LEU C 126 ? 0.423 0.658 0.429 0.031  -0.019 0.028  126 LEU CCC CB  
8341  C CG  . LEU C 126 ? 0.413 0.644 0.416 0.034  -0.017 0.023  126 LEU CCC CG  
8342  C CD1 . LEU C 126 ? 0.417 0.642 0.423 0.036  -0.015 0.017  126 LEU CCC CD1 
8343  C CD2 . LEU C 126 ? 0.411 0.648 0.405 0.036  -0.014 0.021  126 LEU CCC CD2 
8344  N N   . ASN C 127 ? 0.383 0.626 0.396 0.022  -0.026 0.044  127 ASN CCC N   
8345  C CA  . ASN C 127 ? 0.385 0.634 0.400 0.019  -0.028 0.050  127 ASN CCC CA  
8346  C C   . ASN C 127 ? 0.403 0.661 0.412 0.015  -0.029 0.056  127 ASN CCC C   
8347  O O   . ASN C 127 ? 0.422 0.689 0.426 0.015  -0.026 0.057  127 ASN CCC O   
8348  C CB  . ASN C 127 ? 0.380 0.623 0.406 0.016  -0.033 0.053  127 ASN CCC CB  
8349  C CG  . ASN C 127 ? 0.363 0.598 0.396 0.018  -0.032 0.046  127 ASN CCC CG  
8350  O OD1 . ASN C 127 ? 0.355 0.584 0.398 0.018  -0.037 0.046  127 ASN CCC OD1 
8351  N ND2 . ASN C 127 ? 0.352 0.587 0.381 0.021  -0.027 0.041  127 ASN CCC ND2 
8352  N N   . PHE C 128 ? 0.405 0.663 0.415 0.013  -0.033 0.060  128 PHE CCC N   
8353  C CA  . PHE C 128 ? 0.419 0.688 0.424 0.009  -0.034 0.067  128 PHE CCC CA  
8354  C C   . PHE C 128 ? 0.421 0.698 0.415 0.012  -0.029 0.062  128 PHE CCC C   
8355  O O   . PHE C 128 ? 0.420 0.709 0.409 0.009  -0.027 0.065  128 PHE CCC O   
8356  C CB  . PHE C 128 ? 0.390 0.654 0.398 0.006  -0.040 0.071  128 PHE CCC CB  
8357  C CG  . PHE C 128 ? 0.389 0.650 0.407 0.001  -0.047 0.078  128 PHE CCC CG  
8358  C CD1 . PHE C 128 ? 0.382 0.652 0.399 -0.004 -0.050 0.087  128 PHE CCC CD1 
8359  C CD2 . PHE C 128 ? 0.384 0.633 0.413 0.002  -0.052 0.077  128 PHE CCC CD2 
8360  C CE1 . PHE C 128 ? 0.391 0.657 0.417 -0.009 -0.057 0.094  128 PHE CCC CE1 
8361  C CE2 . PHE C 128 ? 0.393 0.639 0.433 -0.002 -0.059 0.083  128 PHE CCC CE2 
8362  C CZ  . PHE C 128 ? 0.395 0.649 0.433 -0.007 -0.061 0.092  128 PHE CCC CZ  
8363  N N   . SER C 129 ? 0.399 0.671 0.391 0.016  -0.026 0.055  129 SER CCC N   
8364  C CA  . SER C 129 ? 0.424 0.703 0.407 0.020  -0.021 0.050  129 SER CCC CA  
8365  C C   . SER C 129 ? 0.440 0.726 0.421 0.021  -0.017 0.048  129 SER CCC C   
8366  O O   . SER C 129 ? 0.397 0.695 0.372 0.021  -0.014 0.047  129 SER CCC O   
8367  C CB  . SER C 129 ? 0.466 0.736 0.450 0.024  -0.019 0.043  129 SER CCC CB  
8368  O OG  . SER C 129 ? 0.509 0.783 0.486 0.028  -0.015 0.037  129 SER CCC OG  
8369  N N   . TYR C 130 ? 0.442 0.723 0.427 0.022  -0.016 0.047  130 TYR CCC N   
8370  C CA  . TYR C 130 ? 0.477 0.763 0.460 0.023  -0.013 0.045  130 TYR CCC CA  
8371  C C   . TYR C 130 ? 0.481 0.777 0.463 0.018  -0.014 0.052  130 TYR CCC C   
8372  O O   . TYR C 130 ? 0.476 0.783 0.453 0.018  -0.011 0.051  130 TYR CCC O   
8373  C CB  . TYR C 130 ? 0.484 0.761 0.472 0.025  -0.012 0.041  130 TYR CCC CB  
8374  C CG  . TYR C 130 ? 0.504 0.774 0.490 0.030  -0.009 0.034  130 TYR CCC CG  
8375  C CD1 . TYR C 130 ? 0.543 0.819 0.523 0.033  -0.006 0.029  130 TYR CCC CD1 
8376  C CD2 . TYR C 130 ? 0.519 0.778 0.509 0.031  -0.010 0.031  130 TYR CCC CD2 
8377  C CE1 . TYR C 130 ? 0.545 0.815 0.524 0.037  -0.004 0.023  130 TYR CCC CE1 
8378  C CE2 . TYR C 130 ? 0.508 0.762 0.497 0.035  -0.008 0.024  130 TYR CCC CE2 
8379  C CZ  . TYR C 130 ? 0.538 0.797 0.521 0.038  -0.005 0.021  130 TYR CCC CZ  
8380  O OH  . TYR C 130 ? 0.522 0.776 0.503 0.042  -0.003 0.015  130 TYR CCC OH  
8381  N N   . ARG C 131 ? 0.489 0.784 0.476 0.013  -0.019 0.059  131 ARG CCC N   
8382  C CA  . ARG C 131 ? 0.503 0.809 0.490 0.007  -0.021 0.067  131 ARG CCC CA  
8383  C C   . ARG C 131 ? 0.494 0.813 0.472 0.006  -0.019 0.068  131 ARG CCC C   
8384  O O   . ARG C 131 ? 0.524 0.855 0.498 0.004  -0.017 0.069  131 ARG CCC O   
8385  C CB  . ARG C 131 ? 0.571 0.872 0.564 0.002  -0.028 0.076  131 ARG CCC CB  
8386  C CG  . ARG C 131 ? 0.618 0.913 0.619 0.001  -0.030 0.079  131 ARG CCC CG  
8387  C CD  . ARG C 131 ? 0.672 0.958 0.682 -0.003 -0.037 0.084  131 ARG CCC CD  
8388  N NE  . ARG C 131 ? 0.702 0.996 0.711 -0.009 -0.042 0.093  131 ARG CCC NE  
8389  C CZ  . ARG C 131 ? 0.716 1.006 0.734 -0.014 -0.049 0.101  131 ARG CCC CZ  
8390  N NH1 . ARG C 131 ? 0.744 1.021 0.772 -0.012 -0.053 0.098  131 ARG CCC NH1 
8391  N NH2 . ARG C 131 ? 0.707 1.004 0.722 -0.020 -0.054 0.110  131 ARG CCC NH2 
8392  N N   . THR C 132 ? 0.494 0.812 0.470 0.006  -0.020 0.067  132 THR CCC N   
8393  C CA  . THR C 132 ? 0.517 0.849 0.486 0.005  -0.019 0.067  132 THR CCC CA  
8394  C C   . THR C 132 ? 0.521 0.860 0.484 0.010  -0.013 0.059  132 THR CCC C   
8395  O O   . THR C 132 ? 0.570 0.924 0.528 0.007  -0.011 0.059  132 THR CCC O   
8396  C CB  . THR C 132 ? 0.540 0.866 0.508 0.005  -0.022 0.067  132 THR CCC CB  
8397  O OG1 . THR C 132 ? 0.533 0.854 0.506 -0.000 -0.028 0.076  132 THR CCC OG1 
8398  C CG2 . THR C 132 ? 0.539 0.878 0.499 0.004  -0.020 0.066  132 THR CCC CG2 
8399  N N   . GLY C 133 ? 0.480 0.808 0.445 0.016  -0.011 0.051  133 GLY CCC N   
8400  C CA  . GLY C 133 ? 0.489 0.821 0.450 0.021  -0.006 0.042  133 GLY CCC CA  
8401  C C   . GLY C 133 ? 0.526 0.868 0.487 0.020  -0.003 0.042  133 GLY CCC C   
8402  O O   . GLY C 133 ? 0.531 0.884 0.488 0.022  -0.000 0.037  133 GLY CCC O   
8403  N N   . LEU C 134 ? 0.519 0.858 0.484 0.017  -0.005 0.048  134 LEU CCC N   
8404  C CA  . LEU C 134 ? 0.527 0.875 0.492 0.016  -0.003 0.049  134 LEU CCC CA  
8405  C C   . LEU C 134 ? 0.530 0.895 0.490 0.010  -0.004 0.054  134 LEU CCC C   
8406  O O   . LEU C 134 ? 0.459 0.837 0.416 0.011  -0.000 0.051  134 LEU CCC O   
8407  C CB  . LEU C 134 ? 0.514 0.852 0.485 0.014  -0.005 0.054  134 LEU CCC CB  
8408  C CG  . LEU C 134 ? 0.540 0.865 0.514 0.019  -0.004 0.048  134 LEU CCC CG  
8409  C CD1 . LEU C 134 ? 0.537 0.855 0.517 0.017  -0.005 0.052  134 LEU CCC CD1 
8410  C CD2 . LEU C 134 ? 0.556 0.886 0.528 0.024  0.001  0.040  134 LEU CCC CD2 
8411  N N   . ARG C 135 ? 0.568 0.933 0.529 0.004  -0.008 0.063  135 ARG CCC N   
8412  C CA  . ARG C 135 ? 0.610 0.992 0.567 -0.002 -0.009 0.069  135 ARG CCC CA  
8413  C C   . ARG C 135 ? 0.617 1.012 0.567 -0.001 -0.006 0.063  135 ARG CCC C   
8414  O O   . ARG C 135 ? 0.677 1.089 0.623 -0.003 -0.003 0.062  135 ARG CCC O   
8415  C CB  . ARG C 135 ? 0.651 1.029 0.611 -0.008 -0.015 0.079  135 ARG CCC CB  
8416  C CG  . ARG C 135 ? 0.698 1.090 0.655 -0.017 -0.018 0.089  135 ARG CCC CG  
8417  C CD  . ARG C 135 ? 0.722 1.108 0.683 -0.023 -0.025 0.099  135 ARG CCC CD  
8418  N NE  . ARG C 135 ? 0.771 1.152 0.732 -0.022 -0.027 0.098  135 ARG CCC NE  
8419  C CZ  . ARG C 135 ? 0.780 1.142 0.746 -0.018 -0.030 0.096  135 ARG CCC CZ  
8420  N NH1 . ARG C 135 ? 0.754 1.103 0.727 -0.015 -0.031 0.095  135 ARG CCC NH1 
8421  N NH2 . ARG C 135 ? 0.720 1.079 0.685 -0.017 -0.031 0.095  135 ARG CCC NH2 
8422  N N   . VAL C 136 ? 0.626 1.015 0.575 0.003  -0.006 0.059  136 VAL CCC N   
8423  C CA  . VAL C 136 ? 0.608 1.009 0.552 0.005  -0.003 0.052  136 VAL CCC CA  
8424  C C   . VAL C 136 ? 0.580 0.987 0.524 0.010  0.002  0.042  136 VAL CCC C   
8425  O O   . VAL C 136 ? 0.565 0.989 0.504 0.010  0.004  0.039  136 VAL CCC O   
8426  C CB  . VAL C 136 ? 0.649 1.038 0.593 0.009  -0.005 0.049  136 VAL CCC CB  
8427  C CG1 . VAL C 136 ? 0.629 1.024 0.569 0.013  -0.001 0.039  136 VAL CCC CG1 
8428  C CG2 . VAL C 136 ? 0.668 1.056 0.611 0.003  -0.010 0.057  136 VAL CCC CG2 
8429  N N   . GLY C 137 ? 0.579 0.972 0.527 0.015  0.003  0.039  137 GLY CCC N   
8430  C CA  . GLY C 137 ? 0.559 0.955 0.508 0.021  0.006  0.030  137 GLY CCC CA  
8431  C C   . GLY C 137 ? 0.528 0.936 0.477 0.018  0.008  0.031  137 GLY CCC C   
8432  O O   . GLY C 137 ? 0.591 0.999 0.542 0.023  0.011  0.025  137 GLY CCC O   
8433  N N   . ASN C 138 ? 0.490 0.906 0.438 0.011  0.006  0.040  138 ASN CCC N   
8434  C CA  . ASN C 138 ? 0.482 0.913 0.430 0.007  0.008  0.043  138 ASN CCC CA  
8435  C C   . ASN C 138 ? 0.438 0.858 0.390 0.009  0.008  0.043  138 ASN CCC C   
8436  O O   . ASN C 138 ? 0.403 0.833 0.356 0.010  0.011  0.040  138 ASN CCC O   
8437  C CB  . ASN C 138 ? 0.501 0.951 0.445 0.009  0.012  0.035  138 ASN CCC CB  
8438  C CG  . ASN C 138 ? 0.503 0.971 0.445 0.003  0.013  0.038  138 ASN CCC CG  
8439  O OD1 . ASN C 138 ? 0.495 0.968 0.437 -0.004 0.010  0.049  138 ASN CCC OD1 
8440  N ND2 . ASN C 138 ? 0.487 0.966 0.430 0.007  0.017  0.030  138 ASN CCC ND2 
8441  N N   . VAL C 139 ? 0.425 0.827 0.381 0.010  0.006  0.047  139 VAL CCC N   
8442  C CA  . VAL C 139 ? 0.427 0.819 0.388 0.011  0.005  0.049  139 VAL CCC CA  
8443  C C   . VAL C 139 ? 0.434 0.824 0.397 0.004  0.001  0.060  139 VAL CCC C   
8444  O O   . VAL C 139 ? 0.406 0.792 0.370 0.001  -0.002 0.065  139 VAL CCC O   
8445  C CB  . VAL C 139 ? 0.425 0.798 0.389 0.017  0.005  0.044  139 VAL CCC CB  
8446  C CG1 . VAL C 139 ? 0.432 0.795 0.401 0.017  0.005  0.046  139 VAL CCC CG1 
8447  C CG2 . VAL C 139 ? 0.430 0.804 0.393 0.023  0.008  0.034  139 VAL CCC CG2 
8448  N N   . GLU C 140 ? 0.450 0.845 0.415 0.002  0.001  0.064  140 GLU CCC N   
8449  C CA  . GLU C 140 ? 0.455 0.845 0.424 -0.004 -0.003 0.074  140 GLU CCC CA  
8450  C C   . GLU C 140 ? 0.411 0.782 0.386 -0.001 -0.005 0.073  140 GLU CCC C   
8451  O O   . GLU C 140 ? 0.367 0.734 0.345 0.002  -0.003 0.070  140 GLU CCC O   
8452  C CB  . GLU C 140 ? 0.471 0.875 0.439 -0.009 -0.002 0.078  140 GLU CCC CB  
8453  C CG  . GLU C 140 ? 0.502 0.905 0.474 -0.016 -0.008 0.089  140 GLU CCC CG  
8454  C CD  . GLU C 140 ? 0.552 0.964 0.525 -0.020 -0.007 0.094  140 GLU CCC CD  
8455  O OE1 . GLU C 140 ? 0.581 0.994 0.555 -0.016 -0.003 0.088  140 GLU CCC OE1 
8456  O OE2 . GLU C 140 ? 0.581 0.999 0.556 -0.028 -0.012 0.104  140 GLU CCC OE2 
8457  N N   . TYR C 141 ? 0.403 0.763 0.381 -0.002 -0.009 0.076  141 TYR CCC N   
8458  C CA  . TYR C 141 ? 0.407 0.750 0.392 -0.000 -0.011 0.076  141 TYR CCC CA  
8459  C C   . TYR C 141 ? 0.402 0.744 0.393 -0.006 -0.016 0.085  141 TYR CCC C   
8460  O O   . TYR C 141 ? 0.393 0.740 0.384 -0.012 -0.020 0.093  141 TYR CCC O   
8461  C CB  . TYR C 141 ? 0.415 0.749 0.402 0.001  -0.014 0.075  141 TYR CCC CB  
8462  C CG  . TYR C 141 ? 0.419 0.738 0.414 0.001  -0.018 0.076  141 TYR CCC CG  
8463  C CD1 . TYR C 141 ? 0.416 0.726 0.414 0.005  -0.016 0.071  141 TYR CCC CD1 
8464  C CD2 . TYR C 141 ? 0.436 0.748 0.435 -0.001 -0.023 0.081  141 TYR CCC CD2 
8465  C CE1 . TYR C 141 ? 0.428 0.725 0.434 0.006  -0.019 0.071  141 TYR CCC CE1 
8466  C CE2 . TYR C 141 ? 0.447 0.746 0.454 -0.001 -0.026 0.080  141 TYR CCC CE2 
8467  C CZ  . TYR C 141 ? 0.428 0.720 0.439 0.003  -0.024 0.075  141 TYR CCC CZ  
8468  O OH  . TYR C 141 ? 0.406 0.686 0.426 0.004  -0.027 0.074  141 TYR CCC OH  
8469  N N   . ILE C 142 ? 0.430 0.764 0.426 -0.004 -0.016 0.084  142 ILE CCC N   
8470  C CA  . ILE C 142 ? 0.435 0.766 0.439 -0.009 -0.020 0.091  142 ILE CCC CA  
8471  C C   . ILE C 142 ? 0.423 0.738 0.435 -0.005 -0.022 0.087  142 ILE CCC C   
8472  O O   . ILE C 142 ? 0.431 0.740 0.442 -0.001 -0.018 0.080  142 ILE CCC O   
8473  C CB  . ILE C 142 ? 0.441 0.781 0.444 -0.010 -0.018 0.092  142 ILE CCC CB  
8474  C CG1 . ILE C 142 ? 0.460 0.817 0.455 -0.013 -0.016 0.095  142 ILE CCC CG1 
8475  C CG2 . ILE C 142 ? 0.428 0.763 0.439 -0.014 -0.023 0.099  142 ILE CCC CG2 
8476  C CD1 . ILE C 142 ? 0.456 0.823 0.450 -0.013 -0.012 0.093  142 ILE CCC CD1 
8477  N N   . ASN C 143 ? 0.389 0.697 0.408 -0.008 -0.028 0.092  143 ASN CCC N   
8478  C CA  . ASN C 143 ? 0.385 0.678 0.412 -0.006 -0.031 0.089  143 ASN CCC CA  
8479  C C   . ASN C 143 ? 0.387 0.678 0.421 -0.008 -0.033 0.091  143 ASN CCC C   
8480  O O   . ASN C 143 ? 0.406 0.693 0.449 -0.011 -0.039 0.097  143 ASN CCC O   
8481  C CB  . ASN C 143 ? 0.380 0.667 0.413 -0.008 -0.037 0.092  143 ASN CCC CB  
8482  C CG  . ASN C 143 ? 0.385 0.659 0.427 -0.005 -0.039 0.087  143 ASN CCC CG  
8483  O OD1 . ASN C 143 ? 0.393 0.661 0.435 -0.000 -0.035 0.079  143 ASN CCC OD1 
8484  N ND2 . ASN C 143 ? 0.383 0.651 0.433 -0.008 -0.046 0.091  143 ASN CCC ND2 
8485  N N   . ALA C 144 ? 0.401 0.694 0.433 -0.005 -0.028 0.087  144 ALA CCC N   
8486  C CA  . ALA C 144 ? 0.386 0.676 0.424 -0.006 -0.029 0.088  144 ALA CCC CA  
8487  C C   . ALA C 144 ? 0.359 0.647 0.395 -0.001 -0.023 0.079  144 ALA CCC C   
8488  O O   . ALA C 144 ? 0.349 0.640 0.376 0.003  -0.019 0.075  144 ALA CCC O   
8489  C CB  . ALA C 144 ? 0.365 0.666 0.402 -0.011 -0.030 0.096  144 ALA CCC CB  
8490  N N   . LEU C 145 ? 0.385 0.666 0.427 -0.000 -0.025 0.078  145 LEU CCC N   
8491  C CA  . LEU C 145 ? 0.424 0.705 0.464 0.003  -0.020 0.072  145 LEU CCC CA  
8492  C C   . LEU C 145 ? 0.461 0.751 0.495 0.002  -0.017 0.074  145 LEU CCC C   
8493  O O   . LEU C 145 ? 0.492 0.788 0.530 -0.002 -0.019 0.081  145 LEU CCC O   
8494  C CB  . LEU C 145 ? 0.441 0.713 0.490 0.003  -0.022 0.070  145 LEU CCC CB  
8495  C CG  . LEU C 145 ? 0.458 0.721 0.513 0.006  -0.024 0.064  145 LEU CCC CG  
8496  C CD1 . LEU C 145 ? 0.454 0.711 0.519 0.005  -0.027 0.062  145 LEU CCC CD1 
8497  C CD2 . LEU C 145 ? 0.456 0.717 0.504 0.010  -0.019 0.056  145 LEU CCC CD2 
8498  N N   . ALA C 146 ? 0.485 0.778 0.512 0.006  -0.011 0.069  146 ALA CCC N   
8499  C CA  . ALA C 146 ? 0.504 0.807 0.526 0.006  -0.008 0.069  146 ALA CCC CA  
8500  C C   . ALA C 146 ? 0.488 0.787 0.512 0.009  -0.006 0.065  146 ALA CCC C   
8501  O O   . ALA C 146 ? 0.449 0.739 0.475 0.011  -0.005 0.060  146 ALA CCC O   
8502  C CB  . ALA C 146 ? 0.527 0.837 0.542 0.009  -0.004 0.066  146 ALA CCC CB  
8503  N N   . LYS C 147 ? 0.543 0.849 0.566 0.007  -0.004 0.067  147 LYS CCC N   
8504  C CA  . LYS C 147 ? 0.565 0.869 0.589 0.010  -0.002 0.063  147 LYS CCC CA  
8505  C C   . LYS C 147 ? 0.510 0.825 0.529 0.011  0.002  0.063  147 LYS CCC C   
8506  O O   . LYS C 147 ? 0.465 0.790 0.482 0.008  0.002  0.067  147 LYS CCC O   
8507  C CB  . LYS C 147 ? 0.575 0.873 0.606 0.008  -0.004 0.065  147 LYS CCC CB  
8508  C CG  . LYS C 147 ? 0.619 0.924 0.653 0.003  -0.007 0.073  147 LYS CCC CG  
8509  C CD  . LYS C 147 ? 0.640 0.940 0.682 0.002  -0.009 0.074  147 LYS CCC CD  
8510  C CE  . LYS C 147 ? 0.654 0.947 0.704 -0.000 -0.015 0.076  147 LYS CCC CE  
8511  N NZ  . LYS C 147 ? 0.676 0.961 0.733 0.000  -0.016 0.073  147 LYS CCC NZ  
8512  N N   . LEU C 148 ? 0.480 0.794 0.498 0.014  0.005  0.058  148 LEU CCC N   
8513  C CA  . LEU C 148 ? 0.529 0.852 0.543 0.015  0.007  0.056  148 LEU CCC CA  
8514  C C   . LEU C 148 ? 0.494 0.822 0.512 0.012  0.007  0.061  148 LEU CCC C   
8515  O O   . LEU C 148 ? 0.440 0.760 0.462 0.011  0.005  0.062  148 LEU CCC O   
8516  C CB  . LEU C 148 ? 0.528 0.846 0.541 0.019  0.010  0.049  148 LEU CCC CB  
8517  C CG  . LEU C 148 ? 0.514 0.829 0.524 0.023  0.010  0.045  148 LEU CCC CG  
8518  C CD1 . LEU C 148 ? 0.506 0.814 0.515 0.026  0.012  0.039  148 LEU CCC CD1 
8519  C CD2 . LEU C 148 ? 0.490 0.814 0.496 0.023  0.012  0.044  148 LEU CCC CD2 
8520  N N   . ILE C 149 ? 0.529 0.869 0.544 0.010  0.008  0.064  149 ILE CCC N   
8521  C CA  . ILE C 149 ? 0.578 0.925 0.596 0.007  0.007  0.068  149 ILE CCC CA  
8522  C C   . ILE C 149 ? 0.605 0.957 0.621 0.010  0.011  0.063  149 ILE CCC C   
8523  O O   . ILE C 149 ? 0.640 0.990 0.660 0.010  0.011  0.063  149 ILE CCC O   
8524  C CB  . ILE C 149 ? 0.631 0.989 0.648 0.002  0.006  0.075  149 ILE CCC CB  
8525  C CG1 . ILE C 149 ? 0.646 0.998 0.667 -0.002 0.001  0.081  149 ILE CCC CG1 
8526  C CG2 . ILE C 149 ? 0.649 1.018 0.667 -0.001 0.007  0.078  149 ILE CCC CG2 
8527  C CD1 . ILE C 149 ? 0.668 1.010 0.695 -0.003 -0.002 0.084  149 ILE CCC CD1 
8528  N N   . ASP C 150 ? 0.614 0.972 0.626 0.013  0.013  0.058  150 ASP CCC N   
8529  C CA  . ASP C 150 ? 0.586 0.948 0.598 0.017  0.016  0.052  150 ASP CCC CA  
8530  C C   . ASP C 150 ? 0.504 0.867 0.512 0.021  0.017  0.045  150 ASP CCC C   
8531  O O   . ASP C 150 ? 0.424 0.786 0.431 0.021  0.017  0.046  150 ASP CCC O   
8532  C CB  . ASP C 150 ? 0.601 0.977 0.613 0.015  0.017  0.054  150 ASP CCC CB  
8533  C CG  . ASP C 150 ? 0.689 1.080 0.698 0.012  0.018  0.056  150 ASP CCC CG  
8534  O OD1 . ASP C 150 ? 0.780 1.174 0.786 0.015  0.019  0.051  150 ASP CCC OD1 
8535  O OD2 . ASP C 150 ? 0.672 1.073 0.682 0.008  0.018  0.061  150 ASP CCC OD2 
8536  N N   . PRO C 151 ? 0.495 0.862 0.504 0.025  0.019  0.039  151 PRO CCC N   
8537  C CA  . PRO C 151 ? 0.471 0.838 0.479 0.029  0.020  0.033  151 PRO CCC CA  
8538  C C   . PRO C 151 ? 0.495 0.872 0.499 0.028  0.020  0.032  151 PRO CCC C   
8539  O O   . PRO C 151 ? 0.471 0.847 0.474 0.032  0.021  0.027  151 PRO CCC O   
8540  C CB  . PRO C 151 ? 0.468 0.841 0.478 0.033  0.021  0.027  151 PRO CCC CB  
8541  C CG  . PRO C 151 ? 0.457 0.826 0.470 0.031  0.020  0.030  151 PRO CCC CG  
8542  C CD  . PRO C 151 ? 0.480 0.850 0.492 0.026  0.020  0.038  151 PRO CCC CD  
8543  N N   . HIS C 152 ? 0.500 0.887 0.503 0.024  0.021  0.038  152 HIS CCC N   
8544  C CA  . HIS C 152 ? 0.470 0.869 0.469 0.022  0.021  0.038  152 HIS CCC CA  
8545  C C   . HIS C 152 ? 0.443 0.843 0.441 0.016  0.019  0.047  152 HIS CCC C   
8546  O O   . HIS C 152 ? 0.434 0.845 0.429 0.013  0.020  0.048  152 HIS CCC O   
8547  C CB  . HIS C 152 ? 0.498 0.916 0.497 0.022  0.024  0.035  152 HIS CCC CB  
8548  C CG  . HIS C 152 ? 0.498 0.917 0.499 0.028  0.025  0.025  152 HIS CCC CG  
8549  N ND1 . HIS C 152 ? 0.470 0.889 0.471 0.032  0.025  0.019  152 HIS CCC ND1 
8550  C CD2 . HIS C 152 ? 0.491 0.911 0.496 0.030  0.026  0.021  152 HIS CCC CD2 
8551  C CE1 . HIS C 152 ? 0.468 0.887 0.472 0.037  0.026  0.011  152 HIS CCC CE1 
8552  N NE2 . HIS C 152 ? 0.483 0.904 0.490 0.036  0.026  0.013  152 HIS CCC NE2 
8553  N N   . SER C 153 ? 0.460 0.848 0.461 0.014  0.017  0.052  153 SER CCC N   
8554  C CA  . SER C 153 ? 0.470 0.857 0.470 0.008  0.014  0.061  153 SER CCC CA  
8555  C C   . SER C 153 ? 0.481 0.851 0.484 0.009  0.011  0.063  153 SER CCC C   
8556  O O   . SER C 153 ? 0.448 0.808 0.454 0.012  0.011  0.060  153 SER CCC O   
8557  C CB  . SER C 153 ? 0.467 0.861 0.470 0.004  0.013  0.067  153 SER CCC CB  
8558  O OG  . SER C 153 ? 0.513 0.922 0.514 0.004  0.016  0.064  153 SER CCC OG  
8559  N N   . VAL C 154 ? 0.546 0.915 0.548 0.006  0.009  0.067  154 VAL CCC N   
8560  C CA  . VAL C 154 ? 0.574 0.929 0.580 0.005  0.005  0.069  154 VAL CCC CA  
8561  C C   . VAL C 154 ? 0.556 0.912 0.565 -0.001 0.001  0.078  154 VAL CCC C   
8562  O O   . VAL C 154 ? 0.506 0.875 0.512 -0.005 0.001  0.083  154 VAL CCC O   
8563  C CB  . VAL C 154 ? 0.606 0.957 0.609 0.009  0.006  0.065  154 VAL CCC CB  
8564  C CG1 . VAL C 154 ? 0.651 1.011 0.650 0.005  0.005  0.068  154 VAL CCC CG1 
8565  C CG2 . VAL C 154 ? 0.656 0.991 0.662 0.010  0.004  0.064  154 VAL CCC CG2 
8566  N N   . GLU C 155 ? 0.580 0.925 0.595 -0.002 -0.002 0.081  155 GLU CCC N   
8567  C CA  . GLU C 155 ? 0.621 0.965 0.642 -0.007 -0.008 0.089  155 GLU CCC CA  
8568  C C   . GLU C 155 ? 0.612 0.944 0.636 -0.007 -0.011 0.090  155 GLU CCC C   
8569  O O   . GLU C 155 ? 0.564 0.886 0.590 -0.003 -0.010 0.083  155 GLU CCC O   
8570  C CB  . GLU C 155 ? 0.685 1.023 0.711 -0.008 -0.009 0.091  155 GLU CCC CB  
8571  C CG  . GLU C 155 ? 0.774 1.111 0.807 -0.014 -0.015 0.100  155 GLU CCC CG  
8572  C CD  . GLU C 155 ? 0.897 1.232 0.936 -0.015 -0.016 0.101  155 GLU CCC CD  
8573  O OE1 . GLU C 155 ? 0.997 1.322 1.039 -0.011 -0.015 0.095  155 GLU CCC OE1 
8574  O OE2 . GLU C 155 ? 0.975 1.317 1.016 -0.020 -0.019 0.109  155 GLU CCC OE2 
8575  N N   . TYR C 156 ? 0.604 0.939 0.629 -0.012 -0.016 0.097  156 TYR CCC N   
8576  C CA  . TYR C 156 ? 0.632 0.957 0.663 -0.013 -0.021 0.099  156 TYR CCC CA  
8577  C C   . TYR C 156 ? 0.636 0.962 0.674 -0.019 -0.028 0.109  156 TYR CCC C   
8578  O O   . TYR C 156 ? 0.670 1.007 0.704 -0.024 -0.028 0.115  156 TYR CCC O   
8579  C CB  . TYR C 156 ? 0.596 0.922 0.622 -0.011 -0.019 0.096  156 TYR CCC CB  
8580  C CG  . TYR C 156 ? 0.566 0.906 0.586 -0.016 -0.020 0.102  156 TYR CCC CG  
8581  C CD1 . TYR C 156 ? 0.576 0.929 0.588 -0.016 -0.015 0.100  156 TYR CCC CD1 
8582  C CD2 . TYR C 156 ? 0.563 0.902 0.585 -0.021 -0.026 0.109  156 TYR CCC CD2 
8583  C CE1 . TYR C 156 ? 0.593 0.960 0.600 -0.020 -0.015 0.105  156 TYR CCC CE1 
8584  C CE2 . TYR C 156 ? 0.595 0.948 0.612 -0.025 -0.026 0.115  156 TYR CCC CE2 
8585  C CZ  . TYR C 156 ? 0.600 0.968 0.609 -0.025 -0.021 0.113  156 TYR CCC CZ  
8586  O OH  . TYR C 156 ? 0.635 1.017 0.638 -0.030 -0.021 0.118  156 TYR CCC OH  
8587  N N   . GLU C 157 ? 0.633 0.947 0.679 -0.020 -0.033 0.110  157 GLU CCC N   
8588  C CA  . GLU C 157 ? 0.662 0.975 0.716 -0.026 -0.041 0.119  157 GLU CCC CA  
8589  C C   . GLU C 157 ? 0.708 1.024 0.759 -0.029 -0.044 0.123  157 GLU CCC C   
8590  O O   . GLU C 157 ? 0.714 1.028 0.761 -0.025 -0.041 0.117  157 GLU CCC O   
8591  C CB  . GLU C 157 ? 0.700 1.000 0.767 -0.025 -0.046 0.117  157 GLU CCC CB  
8592  C CG  . GLU C 157 ? 0.751 1.041 0.823 -0.023 -0.050 0.115  157 GLU CCC CG  
8593  C CD  . GLU C 157 ? 0.812 1.091 0.899 -0.024 -0.057 0.116  157 GLU CCC CD  
8594  O OE1 . GLU C 157 ? 0.853 1.133 0.945 -0.028 -0.061 0.121  157 GLU CCC OE1 
8595  O OE2 . GLU C 157 ? 0.809 1.079 0.902 -0.022 -0.059 0.111  157 GLU CCC OE2 
8596  N N   . ASP C 158 ? 0.728 1.050 0.781 -0.036 -0.050 0.134  158 ASP CCC N   
8597  C CA  . ASP C 158 ? 0.751 1.078 0.802 -0.040 -0.053 0.140  158 ASP CCC CA  
8598  C C   . ASP C 158 ? 0.777 1.103 0.836 -0.048 -0.063 0.152  158 ASP CCC C   
8599  O O   . ASP C 158 ? 0.834 1.171 0.892 -0.053 -0.063 0.159  158 ASP CCC O   
8600  C CB  . ASP C 158 ? 0.744 1.087 0.782 -0.041 -0.047 0.140  158 ASP CCC CB  
8601  C CG  . ASP C 158 ? 0.773 1.125 0.808 -0.047 -0.051 0.148  158 ASP CCC CG  
8602  O OD1 . ASP C 158 ? 0.741 1.084 0.778 -0.047 -0.055 0.148  158 ASP CCC OD1 
8603  O OD2 . ASP C 158 ? 0.818 1.186 0.846 -0.052 -0.050 0.153  158 ASP CCC OD2 
8604  N N   . ASN C 159 ? 0.826 1.141 0.896 -0.049 -0.070 0.153  159 ASN CCC N   
8605  C CA  . ASN C 159 ? 0.846 1.156 0.928 -0.055 -0.080 0.163  159 ASN CCC CA  
8606  C C   . ASN C 159 ? 0.874 1.182 0.963 -0.054 -0.080 0.162  159 ASN CCC C   
8607  O O   . ASN C 159 ? 0.836 1.149 0.928 -0.061 -0.085 0.172  159 ASN CCC O   
8608  C CB  . ASN C 159 ? 0.883 1.205 0.961 -0.064 -0.085 0.176  159 ASN CCC CB  
8609  C CG  . ASN C 159 ? 0.937 1.260 1.012 -0.065 -0.087 0.178  159 ASN CCC CG  
8610  O OD1 . ASN C 159 ? 0.932 1.246 1.017 -0.067 -0.096 0.182  159 ASN CCC OD1 
8611  N ND2 . ASN C 159 ? 0.906 1.240 0.967 -0.064 -0.080 0.175  159 ASN CCC ND2 
8612  N N   . GLY C 160 ? 0.886 1.186 0.976 -0.047 -0.075 0.151  160 GLY CCC N   
8613  C CA  . GLY C 160 ? 0.891 1.188 0.986 -0.045 -0.075 0.149  160 GLY CCC CA  
8614  C C   . GLY C 160 ? 0.922 1.232 1.010 -0.049 -0.071 0.154  160 GLY CCC C   
8615  O O   . GLY C 160 ? 0.926 1.236 1.021 -0.052 -0.075 0.158  160 GLY CCC O   
8616  N N   . GLN C 161 ? 0.921 1.243 0.996 -0.049 -0.064 0.153  161 GLN CCC N   
8617  C CA  . GLN C 161 ? 0.931 1.268 0.998 -0.052 -0.060 0.157  161 GLN CCC CA  
8618  C C   . GLN C 161 ? 0.918 1.259 0.975 -0.045 -0.050 0.147  161 GLN CCC C   
8619  O O   . GLN C 161 ? 0.923 1.270 0.971 -0.044 -0.046 0.144  161 GLN CCC O   
8620  C CB  . GLN C 161 ? 0.977 1.326 1.039 -0.060 -0.063 0.168  161 GLN CCC CB  
8621  C CG  . GLN C 161 ? 1.007 1.354 1.081 -0.067 -0.074 0.179  161 GLN CCC CG  
8622  C CD  . GLN C 161 ? 1.017 1.380 1.086 -0.076 -0.076 0.191  161 GLN CCC CD  
8623  O OE1 . GLN C 161 ? 1.024 1.401 1.084 -0.076 -0.069 0.189  161 GLN CCC OE1 
8624  N NE2 . GLN C 161 ? 1.029 1.391 1.105 -0.084 -0.086 0.202  161 GLN CCC NE2 
8625  N N   . LYS C 162 ? 0.918 1.257 0.975 -0.041 -0.046 0.141  162 LYS CCC N   
8626  C CA  . LYS C 162 ? 0.904 1.248 0.953 -0.035 -0.037 0.132  162 LYS CCC CA  
8627  C C   . LYS C 162 ? 0.881 1.242 0.920 -0.038 -0.033 0.134  162 LYS CCC C   
8628  O O   . LYS C 162 ? 0.903 1.274 0.941 -0.045 -0.035 0.143  162 LYS CCC O   
8629  C CB  . LYS C 162 ? 0.953 1.296 1.004 -0.034 -0.035 0.130  162 LYS CCC CB  
8630  C CG  . LYS C 162 ? 1.026 1.354 1.086 -0.031 -0.037 0.126  162 LYS CCC CG  
8631  C CD  . LYS C 162 ? 1.046 1.364 1.106 -0.025 -0.035 0.117  162 LYS CCC CD  
8632  C CE  . LYS C 162 ? 1.073 1.380 1.140 -0.021 -0.034 0.110  162 LYS CCC CE  
8633  N NZ  . LYS C 162 ? 1.127 1.429 1.190 -0.015 -0.029 0.100  162 LYS CCC NZ  
8634  N N   . LYS C 163 ? 0.835 1.197 0.865 -0.033 -0.028 0.127  163 LYS CCC N   
8635  C CA  . LYS C 163 ? 0.799 1.178 0.821 -0.034 -0.023 0.126  163 LYS CCC CA  
8636  C C   . LYS C 163 ? 0.781 1.159 0.798 -0.027 -0.016 0.115  163 LYS CCC C   
8637  O O   . LYS C 163 ? 0.751 1.116 0.770 -0.021 -0.015 0.108  163 LYS CCC O   
8638  C CB  . LYS C 163 ? 0.818 1.200 0.835 -0.036 -0.024 0.128  163 LYS CCC CB  
8639  C CG  . LYS C 163 ? 0.835 1.219 0.855 -0.044 -0.032 0.139  163 LYS CCC CG  
8640  C CD  . LYS C 163 ? 0.847 1.243 0.861 -0.048 -0.032 0.142  163 LYS CCC CD  
8641  C CE  . LYS C 163 ? 0.865 1.265 0.882 -0.057 -0.040 0.155  163 LYS CCC CE  
8642  N NZ  . LYS C 163 ? 0.842 1.256 0.852 -0.061 -0.040 0.158  163 LYS CCC NZ  
8643  N N   . THR C 164 ? 0.727 1.120 0.738 -0.027 -0.011 0.113  164 THR CCC N   
8644  C CA  . THR C 164 ? 0.687 1.082 0.694 -0.021 -0.005 0.103  164 THR CCC CA  
8645  C C   . THR C 164 ? 0.614 1.023 0.614 -0.020 -0.001 0.099  164 THR CCC C   
8646  O O   . THR C 164 ? 0.653 1.076 0.650 -0.026 -0.003 0.105  164 THR CCC O   
8647  C CB  . THR C 164 ? 0.708 1.107 0.718 -0.020 -0.003 0.102  164 THR CCC CB  
8648  O OG1 . THR C 164 ? 0.720 1.104 0.736 -0.020 -0.006 0.104  164 THR CCC OG1 
8649  C CG2 . THR C 164 ? 0.717 1.119 0.723 -0.014 0.003  0.093  164 THR CCC CG2 
8650  N N   . ILE C 165 ? 0.556 0.961 0.553 -0.014 0.002  0.090  165 ILE CCC N   
8651  C CA  . ILE C 165 ? 0.518 0.936 0.509 -0.012 0.006  0.085  165 ILE CCC CA  
8652  C C   . ILE C 165 ? 0.489 0.907 0.480 -0.005 0.010  0.075  165 ILE CCC C   
8653  O O   . ILE C 165 ? 0.510 0.913 0.504 -0.001 0.010  0.071  165 ILE CCC O   
8654  C CB  . ILE C 165 ? 0.550 0.963 0.538 -0.012 0.004  0.085  165 ILE CCC CB  
8655  C CG1 . ILE C 165 ? 0.506 0.901 0.497 -0.006 0.004  0.079  165 ILE CCC CG1 
8656  C CG2 . ILE C 165 ? 0.544 0.958 0.534 -0.019 -0.001 0.096  165 ILE CCC CG2 
8657  C CD1 . ILE C 165 ? 0.508 0.901 0.496 -0.004 0.004  0.076  165 ILE CCC CD1 
8658  N N   . THR C 166 ? 0.422 0.855 0.409 -0.004 0.014  0.069  166 THR CCC N   
8659  C CA  . THR C 166 ? 0.398 0.833 0.385 0.002  0.018  0.060  166 THR CCC CA  
8660  C C   . THR C 166 ? 0.387 0.823 0.372 0.007  0.020  0.052  166 THR CCC C   
8661  O O   . THR C 166 ? 0.389 0.834 0.370 0.004  0.019  0.053  166 THR CCC O   
8662  C CB  . THR C 166 ? 0.394 0.848 0.382 -0.001 0.020  0.060  166 THR CCC CB  
8663  O OG1 . THR C 166 ? 0.391 0.862 0.374 -0.005 0.020  0.062  166 THR CCC OG1 
8664  C CG2 . THR C 166 ? 0.390 0.842 0.380 -0.005 0.018  0.068  166 THR CCC CG2 
8665  N N   . SER C 167 ? 0.389 0.817 0.376 0.013  0.021  0.044  167 SER CCC N   
8666  C CA  . SER C 167 ? 0.400 0.826 0.386 0.019  0.022  0.035  167 SER CCC CA  
8667  C C   . SER C 167 ? 0.404 0.832 0.393 0.025  0.024  0.026  167 SER CCC C   
8668  O O   . SER C 167 ? 0.418 0.839 0.410 0.026  0.024  0.027  167 SER CCC O   
8669  C CB  . SER C 167 ? 0.364 0.773 0.350 0.021  0.020  0.036  167 SER CCC CB  
8670  O OG  . SER C 167 ? 0.335 0.746 0.318 0.023  0.021  0.031  167 SER CCC OG  
8671  N N   . ARG C 168 ? 0.423 0.861 0.412 0.028  0.026  0.018  168 ARG CCC N   
8672  C CA  . ARG C 168 ? 0.463 0.900 0.455 0.034  0.027  0.009  168 ARG CCC CA  
8673  C C   . ARG C 168 ? 0.406 0.823 0.401 0.038  0.025  0.008  168 ARG CCC C   
8674  O O   . ARG C 168 ? 0.408 0.820 0.407 0.040  0.024  0.006  168 ARG CCC O   
8675  C CB  . ARG C 168 ? 0.523 0.974 0.515 0.037  0.028  0.000  168 ARG CCC CB  
8676  C CG  . ARG C 168 ? 0.595 1.049 0.592 0.043  0.028  -0.010 168 ARG CCC CG  
8677  C CD  . ARG C 168 ? 0.716 1.174 0.718 0.044  0.029  -0.012 168 ARG CCC CD  
8678  N NE  . ARG C 168 ? 0.830 1.283 0.838 0.051  0.028  -0.021 168 ARG CCC NE  
8679  C CZ  . ARG C 168 ? 0.902 1.349 0.916 0.053  0.027  -0.022 168 ARG CCC CZ  
8680  N NH1 . ARG C 168 ? 0.904 1.348 0.917 0.049  0.027  -0.015 168 ARG CCC NH1 
8681  N NH2 . ARG C 168 ? 0.934 1.377 0.954 0.058  0.025  -0.030 168 ARG CCC NH2 
8682  N N   . TYR C 169 ? 0.388 0.793 0.380 0.038  0.023  0.010  169 TYR CCC N   
8683  C CA  . TYR C 169 ? 0.400 0.787 0.393 0.041  0.021  0.009  169 TYR CCC CA  
8684  C C   . TYR C 169 ? 0.390 0.766 0.381 0.037  0.020  0.017  169 TYR CCC C   
8685  O O   . TYR C 169 ? 0.413 0.795 0.402 0.033  0.020  0.022  169 TYR CCC O   
8686  C CB  . TYR C 169 ? 0.402 0.787 0.395 0.045  0.021  0.002  169 TYR CCC CB  
8687  C CG  . TYR C 169 ? 0.424 0.818 0.421 0.050  0.022  -0.007 169 TYR CCC CG  
8688  C CD1 . TYR C 169 ? 0.417 0.807 0.418 0.053  0.021  -0.010 169 TYR CCC CD1 
8689  C CD2 . TYR C 169 ? 0.447 0.854 0.443 0.051  0.023  -0.012 169 TYR CCC CD2 
8690  C CE1 . TYR C 169 ? 0.424 0.823 0.431 0.057  0.021  -0.018 169 TYR CCC CE1 
8691  C CE2 . TYR C 169 ? 0.451 0.868 0.452 0.056  0.023  -0.021 169 TYR CCC CE2 
8692  C CZ  . TYR C 169 ? 0.448 0.860 0.454 0.058  0.022  -0.024 169 TYR CCC CZ  
8693  O OH  . TYR C 169 ? 0.455 0.877 0.468 0.063  0.022  -0.033 169 TYR CCC OH  
8694  N N   . ILE C 170 ? 0.365 0.727 0.358 0.038  0.019  0.019  170 ILE CCC N   
8695  C CA  . ILE C 170 ? 0.373 0.724 0.366 0.035  0.017  0.024  170 ILE CCC CA  
8696  C C   . ILE C 170 ? 0.364 0.701 0.357 0.038  0.016  0.021  170 ILE CCC C   
8697  O O   . ILE C 170 ? 0.375 0.708 0.370 0.041  0.016  0.016  170 ILE CCC O   
8698  C CB  . ILE C 170 ? 0.375 0.723 0.370 0.032  0.016  0.030  170 ILE CCC CB  
8699  C CG1 . ILE C 170 ? 0.376 0.738 0.371 0.028  0.017  0.034  170 ILE CCC CG1 
8700  C CG2 . ILE C 170 ? 0.373 0.708 0.369 0.030  0.014  0.034  170 ILE CCC CG2 
8701  C CD1 . ILE C 170 ? 0.374 0.735 0.371 0.025  0.016  0.039  170 ILE CCC CD1 
8702  N N   . LEU C 171 ? 0.351 0.681 0.342 0.038  0.015  0.022  171 LEU CCC N   
8703  C CA  . LEU C 171 ? 0.337 0.655 0.328 0.040  0.014  0.019  171 LEU CCC CA  
8704  C C   . LEU C 171 ? 0.325 0.634 0.318 0.037  0.012  0.023  171 LEU CCC C   
8705  O O   . LEU C 171 ? 0.328 0.638 0.320 0.034  0.012  0.028  171 LEU CCC O   
8706  C CB  . LEU C 171 ? 0.347 0.667 0.336 0.042  0.014  0.016  171 LEU CCC CB  
8707  C CG  . LEU C 171 ? 0.347 0.654 0.335 0.043  0.012  0.014  171 LEU CCC CG  
8708  C CD1 . LEU C 171 ? 0.354 0.655 0.344 0.046  0.012  0.010  171 LEU CCC CD1 
8709  C CD2 . LEU C 171 ? 0.338 0.646 0.324 0.045  0.012  0.012  171 LEU CCC CD2 
8710  N N   . LEU C 172 ? 0.305 0.605 0.300 0.038  0.012  0.022  172 LEU CCC N   
8711  C CA  . LEU C 172 ? 0.291 0.581 0.288 0.035  0.011  0.025  172 LEU CCC CA  
8712  C C   . LEU C 172 ? 0.312 0.595 0.308 0.037  0.010  0.021  172 LEU CCC C   
8713  O O   . LEU C 172 ? 0.293 0.574 0.288 0.040  0.010  0.017  172 LEU CCC O   
8714  C CB  . LEU C 172 ? 0.296 0.583 0.296 0.035  0.011  0.025  172 LEU CCC CB  
8715  C CG  . LEU C 172 ? 0.274 0.568 0.274 0.034  0.012  0.027  172 LEU CCC CG  
8716  C CD1 . LEU C 172 ? 0.266 0.556 0.269 0.034  0.012  0.026  172 LEU CCC CD1 
8717  C CD2 . LEU C 172 ? 0.278 0.579 0.280 0.031  0.011  0.032  172 LEU CCC CD2 
8718  N N   . ALA C 173 ? 0.339 0.618 0.335 0.035  0.009  0.023  173 ALA CCC N   
8719  C CA  . ALA C 173 ? 0.340 0.612 0.336 0.036  0.008  0.021  173 ALA CCC CA  
8720  C C   . ALA C 173 ? 0.324 0.591 0.324 0.034  0.006  0.023  173 ALA CCC C   
8721  O O   . ALA C 173 ? 0.319 0.585 0.318 0.033  0.005  0.024  173 ALA CCC O   
8722  C CB  . ALA C 173 ? 0.370 0.645 0.362 0.039  0.008  0.019  173 ALA CCC CB  
8723  N N   . THR C 174 ? 0.344 0.608 0.347 0.032  0.006  0.024  174 THR CCC N   
8724  C CA  . THR C 174 ? 0.343 0.603 0.351 0.029  0.004  0.026  174 THR CCC CA  
8725  C C   . THR C 174 ? 0.322 0.575 0.332 0.030  0.003  0.022  174 THR CCC C   
8726  O O   . THR C 174 ? 0.303 0.553 0.319 0.028  0.001  0.022  174 THR CCC O   
8727  C CB  . THR C 174 ? 0.346 0.608 0.358 0.027  0.004  0.029  174 THR CCC CB  
8728  O OG1 . THR C 174 ? 0.322 0.583 0.333 0.028  0.005  0.025  174 THR CCC OG1 
8729  C CG2 . THR C 174 ? 0.359 0.629 0.370 0.026  0.003  0.033  174 THR CCC CG2 
8730  N N   . GLY C 175 ? 0.320 0.571 0.327 0.032  0.005  0.018  175 GLY CCC N   
8731  C CA  . GLY C 175 ? 0.339 0.584 0.346 0.032  0.005  0.014  175 GLY CCC CA  
8732  C C   . GLY C 175 ? 0.352 0.595 0.364 0.029  0.005  0.012  175 GLY CCC C   
8733  O O   . GLY C 175 ? 0.393 0.638 0.407 0.028  0.005  0.014  175 GLY CCC O   
8734  N N   . GLY C 176 ? 0.363 0.603 0.377 0.029  0.004  0.008  176 GLY CCC N   
8735  C CA  . GLY C 176 ? 0.366 0.605 0.385 0.026  0.004  0.006  176 GLY CCC CA  
8736  C C   . GLY C 176 ? 0.375 0.612 0.401 0.026  0.002  0.005  176 GLY CCC C   
8737  O O   . GLY C 176 ? 0.467 0.703 0.494 0.026  0.000  0.007  176 GLY CCC O   
8738  N N   . ARG C 177 ? 0.352 0.588 0.384 0.024  0.001  0.001  177 ARG CCC N   
8739  C CA  . ARG C 177 ? 0.349 0.583 0.389 0.023  -0.001 -0.002 177 ARG CCC CA  
8740  C C   . ARG C 177 ? 0.354 0.590 0.396 0.021  0.000  -0.009 177 ARG CCC C   
8741  O O   . ARG C 177 ? 0.349 0.586 0.387 0.020  0.002  -0.010 177 ARG CCC O   
8742  C CB  . ARG C 177 ? 0.340 0.574 0.388 0.022  -0.004 0.001  177 ARG CCC CB  
8743  C CG  . ARG C 177 ? 0.368 0.602 0.414 0.023  -0.005 0.008  177 ARG CCC CG  
8744  C CD  . ARG C 177 ? 0.367 0.600 0.413 0.024  -0.007 0.009  177 ARG CCC CD  
8745  N NE  . ARG C 177 ? 0.378 0.608 0.434 0.023  -0.011 0.006  177 ARG CCC NE  
8746  C CZ  . ARG C 177 ? 0.368 0.598 0.432 0.022  -0.015 0.011  177 ARG CCC CZ  
8747  N NH1 . ARG C 177 ? 0.363 0.594 0.423 0.021  -0.015 0.017  177 ARG CCC NH1 
8748  N NH2 . ARG C 177 ? 0.354 0.580 0.428 0.021  -0.019 0.008  177 ARG CCC NH2 
8749  N N   . PRO C 178 ? 0.331 0.566 0.380 0.021  -0.001 -0.014 178 PRO CCC N   
8750  C CA  . PRO C 178 ? 0.349 0.586 0.399 0.019  0.000  -0.021 178 PRO CCC CA  
8751  C C   . PRO C 178 ? 0.383 0.624 0.437 0.017  0.001  -0.023 178 PRO CCC C   
8752  O O   . PRO C 178 ? 0.399 0.639 0.459 0.018  -0.002 -0.020 178 PRO CCC O   
8753  C CB  . PRO C 178 ? 0.337 0.573 0.396 0.020  -0.002 -0.025 178 PRO CCC CB  
8754  C CG  . PRO C 178 ? 0.329 0.561 0.388 0.022  -0.004 -0.020 178 PRO CCC CG  
8755  C CD  . PRO C 178 ? 0.329 0.561 0.383 0.022  -0.004 -0.013 178 PRO CCC CD  
8756  N N   . SER C 179 ? 0.428 0.673 0.479 0.015  0.003  -0.026 179 SER CCC N   
8757  C CA  . SER C 179 ? 0.463 0.712 0.517 0.013  0.003  -0.029 179 SER CCC CA  
8758  C C   . SER C 179 ? 0.471 0.724 0.532 0.011  0.003  -0.038 179 SER CCC C   
8759  O O   . SER C 179 ? 0.420 0.676 0.479 0.010  0.005  -0.042 179 SER CCC O   
8760  C CB  . SER C 179 ? 0.481 0.732 0.526 0.011  0.006  -0.027 179 SER CCC CB  
8761  O OG  . SER C 179 ? 0.506 0.760 0.555 0.010  0.006  -0.028 179 SER CCC OG  
8762  N N   . ILE C 180 ? 0.492 0.747 0.563 0.011  0.001  -0.041 180 ILE CCC N   
8763  C CA  . ILE C 180 ? 0.542 0.803 0.623 0.009  0.001  -0.051 180 ILE CCC CA  
8764  C C   . ILE C 180 ? 0.546 0.812 0.627 0.006  0.002  -0.053 180 ILE CCC C   
8765  O O   . ILE C 180 ? 0.577 0.842 0.660 0.007  0.001  -0.049 180 ILE CCC O   
8766  C CB  . ILE C 180 ? 0.574 0.832 0.668 0.011  -0.003 -0.053 180 ILE CCC CB  
8767  C CG1 . ILE C 180 ? 0.596 0.848 0.690 0.013  -0.005 -0.051 180 ILE CCC CG1 
8768  C CG2 . ILE C 180 ? 0.587 0.851 0.692 0.009  -0.004 -0.064 180 ILE CCC CG2 
8769  C CD1 . ILE C 180 ? 0.616 0.865 0.724 0.015  -0.010 -0.051 180 ILE CCC CD1 
8770  N N   . PRO C 181 ? 0.523 0.797 0.603 0.003  0.005  -0.060 181 PRO CCC N   
8771  C CA  . PRO C 181 ? 0.550 0.831 0.631 -0.000 0.006  -0.063 181 PRO CCC CA  
8772  C C   . PRO C 181 ? 0.555 0.837 0.648 0.001  0.003  -0.067 181 PRO CCC C   
8773  O O   . PRO C 181 ? 0.517 0.802 0.621 0.001  0.001  -0.075 181 PRO CCC O   
8774  C CB  . PRO C 181 ? 0.540 0.830 0.617 -0.004 0.008  -0.070 181 PRO CCC CB  
8775  C CG  . PRO C 181 ? 0.538 0.827 0.618 -0.003 0.008  -0.073 181 PRO CCC CG  
8776  C CD  . PRO C 181 ? 0.520 0.799 0.598 0.001  0.006  -0.065 181 PRO CCC CD  
8777  N N   . GLU C 182 ? 0.588 0.868 0.681 0.001  0.002  -0.062 182 GLU CCC N   
8778  C CA  . GLU C 182 ? 0.657 0.937 0.762 0.002  -0.001 -0.064 182 GLU CCC CA  
8779  C C   . GLU C 182 ? 0.644 0.934 0.754 -0.001 0.000  -0.074 182 GLU CCC C   
8780  O O   . GLU C 182 ? 0.643 0.935 0.767 -0.001 -0.003 -0.081 182 GLU CCC O   
8781  C CB  . GLU C 182 ? 0.701 0.976 0.802 0.003  -0.001 -0.055 182 GLU CCC CB  
8782  C CG  . GLU C 182 ? 0.731 0.998 0.829 0.006  -0.003 -0.046 182 GLU CCC CG  
8783  C CD  . GLU C 182 ? 0.778 1.041 0.876 0.006  -0.005 -0.039 182 GLU CCC CD  
8784  O OE1 . GLU C 182 ? 0.691 0.957 0.789 0.005  -0.004 -0.039 182 GLU CCC OE1 
8785  O OE2 . GLU C 182 ? 0.710 0.967 0.808 0.009  -0.007 -0.032 182 GLU CCC OE2 
8786  N N   . THR C 183 ? 0.639 0.936 0.740 -0.005 0.004  -0.076 183 THR CCC N   
8787  C CA  . THR C 183 ? 0.647 0.955 0.750 -0.009 0.006  -0.085 183 THR CCC CA  
8788  C C   . THR C 183 ? 0.645 0.960 0.758 -0.009 0.005  -0.097 183 THR CCC C   
8789  O O   . THR C 183 ? 0.632 0.957 0.755 -0.011 0.005  -0.106 183 THR CCC O   
8790  C CB  . THR C 183 ? 0.647 0.960 0.735 -0.013 0.010  -0.082 183 THR CCC CB  
8791  O OG1 . THR C 183 ? 0.662 0.975 0.744 -0.014 0.011  -0.081 183 THR CCC OG1 
8792  C CG2 . THR C 183 ? 0.661 0.968 0.741 -0.013 0.010  -0.071 183 THR CCC CG2 
8793  N N   . VAL C 184 ? 0.638 0.951 0.751 -0.008 0.005  -0.097 184 VAL CCC N   
8794  C CA  . VAL C 184 ? 0.606 0.925 0.728 -0.008 0.005  -0.108 184 VAL CCC CA  
8795  C C   . VAL C 184 ? 0.588 0.902 0.727 -0.004 0.000  -0.112 184 VAL CCC C   
8796  O O   . VAL C 184 ? 0.536 0.839 0.676 -0.001 -0.003 -0.105 184 VAL CCC O   
8797  C CB  . VAL C 184 ? 0.593 0.910 0.707 -0.008 0.007  -0.106 184 VAL CCC CB  
8798  C CG1 . VAL C 184 ? 0.611 0.933 0.736 -0.008 0.006  -0.117 184 VAL CCC CG1 
8799  C CG2 . VAL C 184 ? 0.577 0.901 0.676 -0.013 0.011  -0.104 184 VAL CCC CG2 
8800  N N   . PRO C 185 ? 0.603 0.925 0.755 -0.005 -0.002 -0.123 185 PRO CCC N   
8801  C CA  . PRO C 185 ? 0.562 0.880 0.733 -0.001 -0.007 -0.127 185 PRO CCC CA  
8802  C C   . PRO C 185 ? 0.515 0.828 0.692 0.002  -0.010 -0.130 185 PRO CCC C   
8803  O O   . PRO C 185 ? 0.479 0.800 0.655 -0.000 -0.007 -0.137 185 PRO CCC O   
8804  C CB  . PRO C 185 ? 0.609 0.940 0.792 -0.003 -0.007 -0.141 185 PRO CCC CB  
8805  C CG  . PRO C 185 ? 0.624 0.964 0.793 -0.008 -0.002 -0.140 185 PRO CCC CG  
8806  C CD  . PRO C 185 ? 0.612 0.948 0.764 -0.009 0.002  -0.132 185 PRO CCC CD  
8807  N N   . GLY C 186 ? 0.496 0.799 0.682 0.005  -0.015 -0.125 186 GLY CCC N   
8808  C CA  . GLY C 186 ? 0.498 0.795 0.692 0.008  -0.019 -0.125 186 GLY CCC CA  
8809  C C   . GLY C 186 ? 0.460 0.749 0.640 0.009  -0.017 -0.114 186 GLY CCC C   
8810  O O   . GLY C 186 ? 0.425 0.706 0.610 0.011  -0.021 -0.112 186 GLY CCC O   
8811  N N   . ALA C 187 ? 0.458 0.747 0.620 0.007  -0.012 -0.108 187 ALA CCC N   
8812  C CA  . ALA C 187 ? 0.508 0.791 0.655 0.007  -0.009 -0.098 187 ALA CCC CA  
8813  C C   . ALA C 187 ? 0.555 0.826 0.704 0.011  -0.013 -0.088 187 ALA CCC C   
8814  O O   . ALA C 187 ? 0.566 0.832 0.715 0.012  -0.015 -0.086 187 ALA CCC O   
8815  C CB  . ALA C 187 ? 0.510 0.797 0.642 0.005  -0.004 -0.093 187 ALA CCC CB  
8816  N N   . ILE C 188 ? 0.534 0.802 0.684 0.011  -0.015 -0.082 188 ILE CCC N   
8817  C CA  . ILE C 188 ? 0.497 0.755 0.647 0.013  -0.019 -0.071 188 ILE CCC CA  
8818  C C   . ILE C 188 ? 0.493 0.747 0.658 0.015  -0.025 -0.074 188 ILE CCC C   
8819  O O   . ILE C 188 ? 0.532 0.779 0.695 0.016  -0.028 -0.067 188 ILE CCC O   
8820  C CB  . ILE C 188 ? 0.500 0.758 0.648 0.012  -0.019 -0.065 188 ILE CCC CB  
8821  C CG1 . ILE C 188 ? 0.475 0.733 0.605 0.011  -0.014 -0.059 188 ILE CCC CG1 
8822  C CG2 . ILE C 188 ? 0.505 0.754 0.660 0.014  -0.025 -0.058 188 ILE CCC CG2 
8823  C CD1 . ILE C 188 ? 0.469 0.729 0.598 0.010  -0.013 -0.057 188 ILE CCC CD1 
8824  N N   . GLN C 189 ? 0.519 0.777 0.699 0.015  -0.028 -0.084 189 GLN CCC N   
8825  C CA  . GLN C 189 ? 0.562 0.815 0.759 0.017  -0.035 -0.087 189 GLN CCC CA  
8826  C C   . GLN C 189 ? 0.582 0.834 0.781 0.018  -0.036 -0.091 189 GLN CCC C   
8827  O O   . GLN C 189 ? 0.613 0.858 0.819 0.019  -0.041 -0.087 189 GLN CCC O   
8828  C CB  . GLN C 189 ? 0.596 0.855 0.810 0.017  -0.038 -0.098 189 GLN CCC CB  
8829  C CG  . GLN C 189 ? 0.635 0.887 0.868 0.018  -0.047 -0.098 189 GLN CCC CG  
8830  C CD  . GLN C 189 ? 0.662 0.921 0.915 0.019  -0.051 -0.111 189 GLN CCC CD  
8831  O OE1 . GLN C 189 ? 0.650 0.916 0.902 0.017  -0.048 -0.117 189 GLN CCC OE1 
8832  N NE2 . GLN C 189 ? 0.634 0.888 0.904 0.021  -0.059 -0.115 189 GLN CCC NE2 
8833  N N   . TYR C 190 ? 0.530 0.791 0.724 0.017  -0.030 -0.099 190 TYR CCC N   
8834  C CA  . TYR C 190 ? 0.530 0.793 0.730 0.018  -0.031 -0.107 190 TYR CCC CA  
8835  C C   . TYR C 190 ? 0.459 0.719 0.643 0.017  -0.027 -0.102 190 TYR CCC C   
8836  O O   . TYR C 190 ? 0.406 0.666 0.594 0.019  -0.028 -0.105 190 TYR CCC O   
8837  C CB  . TYR C 190 ? 0.580 0.854 0.789 0.016  -0.029 -0.122 190 TYR CCC CB  
8838  C CG  . TYR C 190 ? 0.646 0.921 0.875 0.017  -0.035 -0.129 190 TYR CCC CG  
8839  C CD1 . TYR C 190 ? 0.666 0.934 0.911 0.020  -0.043 -0.129 190 TYR CCC CD1 
8840  C CD2 . TYR C 190 ? 0.700 0.985 0.933 0.016  -0.033 -0.137 190 TYR CCC CD2 
8841  C CE1 . TYR C 190 ? 0.719 0.988 0.984 0.021  -0.049 -0.136 190 TYR CCC CE1 
8842  C CE2 . TYR C 190 ? 0.749 1.036 1.001 0.017  -0.039 -0.144 190 TYR CCC CE2 
8843  C CZ  . TYR C 190 ? 0.768 1.046 1.036 0.019  -0.047 -0.144 190 TYR CCC CZ  
8844  O OH  . TYR C 190 ? 0.805 1.084 1.093 0.021  -0.053 -0.152 190 TYR CCC OH  
8845  N N   . SER C 191 ? 0.429 0.690 0.596 0.016  -0.021 -0.095 191 SER CCC N   
8846  C CA  . SER C 191 ? 0.432 0.692 0.583 0.016  -0.017 -0.090 191 SER CCC CA  
8847  C C   . SER C 191 ? 0.412 0.662 0.557 0.018  -0.019 -0.078 191 SER CCC C   
8848  O O   . SER C 191 ? 0.420 0.666 0.567 0.018  -0.022 -0.071 191 SER CCC O   
8849  C CB  . SER C 191 ? 0.414 0.680 0.552 0.013  -0.011 -0.089 191 SER CCC CB  
8850  O OG  . SER C 191 ? 0.498 0.760 0.628 0.013  -0.011 -0.079 191 SER CCC OG  
8851  N N   . ILE C 192 ? 0.382 0.631 0.520 0.018  -0.017 -0.076 192 ILE CCC N   
8852  C CA  . ILE C 192 ? 0.372 0.612 0.501 0.020  -0.018 -0.065 192 ILE CCC CA  
8853  C C   . ILE C 192 ? 0.351 0.592 0.463 0.019  -0.013 -0.061 192 ILE CCC C   
8854  O O   . ILE C 192 ? 0.354 0.602 0.462 0.017  -0.009 -0.065 192 ILE CCC O   
8855  C CB  . ILE C 192 ? 0.366 0.602 0.500 0.022  -0.021 -0.067 192 ILE CCC CB  
8856  C CG1 . ILE C 192 ? 0.371 0.612 0.502 0.021  -0.018 -0.074 192 ILE CCC CG1 
8857  C CG2 . ILE C 192 ? 0.367 0.601 0.520 0.023  -0.028 -0.071 192 ILE CCC CG2 
8858  C CD1 . ILE C 192 ? 0.368 0.604 0.499 0.023  -0.020 -0.073 192 ILE CCC CD1 
8859  N N   . THR C 193 ? 0.334 0.570 0.438 0.020  -0.013 -0.052 193 THR CCC N   
8860  C CA  . THR C 193 ? 0.328 0.564 0.416 0.020  -0.008 -0.046 193 THR CCC CA  
8861  C C   . THR C 193 ? 0.342 0.573 0.425 0.022  -0.009 -0.042 193 THR CCC C   
8862  O O   . THR C 193 ? 0.333 0.561 0.424 0.023  -0.013 -0.043 193 THR CCC O   
8863  C CB  . THR C 193 ? 0.325 0.560 0.407 0.020  -0.008 -0.039 193 THR CCC CB  
8864  O OG1 . THR C 193 ? 0.276 0.506 0.361 0.021  -0.011 -0.032 193 THR CCC OG1 
8865  C CG2 . THR C 193 ? 0.331 0.571 0.420 0.018  -0.008 -0.043 193 THR CCC CG2 
8866  N N   . SER C 194 ? 0.358 0.588 0.428 0.022  -0.006 -0.037 194 SER CCC N   
8867  C CA  . SER C 194 ? 0.338 0.564 0.402 0.024  -0.006 -0.033 194 SER CCC CA  
8868  C C   . SER C 194 ? 0.352 0.575 0.420 0.025  -0.010 -0.026 194 SER CCC C   
8869  O O   . SER C 194 ? 0.381 0.601 0.448 0.027  -0.012 -0.024 194 SER CCC O   
8870  C CB  . SER C 194 ? 0.327 0.553 0.378 0.024  -0.003 -0.029 194 SER CCC CB  
8871  O OG  . SER C 194 ? 0.322 0.550 0.370 0.024  -0.002 -0.026 194 SER CCC OG  
8872  N N   . ASP C 195 ? 0.373 0.596 0.444 0.025  -0.012 -0.023 195 ASP CCC N   
8873  C CA  . ASP C 195 ? 0.367 0.587 0.443 0.025  -0.016 -0.017 195 ASP CCC CA  
8874  C C   . ASP C 195 ? 0.364 0.581 0.452 0.025  -0.021 -0.020 195 ASP CCC C   
8875  O O   . ASP C 195 ? 0.374 0.589 0.465 0.025  -0.024 -0.014 195 ASP CCC O   
8876  C CB  . ASP C 195 ? 0.359 0.581 0.438 0.024  -0.016 -0.014 195 ASP CCC CB  
8877  C CG  . ASP C 195 ? 0.359 0.583 0.426 0.024  -0.013 -0.009 195 ASP CCC CG  
8878  O OD1 . ASP C 195 ? 0.352 0.576 0.410 0.025  -0.010 -0.008 195 ASP CCC OD1 
8879  O OD2 . ASP C 195 ? 0.370 0.595 0.439 0.023  -0.013 -0.006 195 ASP CCC OD2 
8880  N N   . ASP C 196 ? 0.342 0.560 0.438 0.025  -0.021 -0.028 196 ASP CCC N   
8881  C CA  . ASP C 196 ? 0.335 0.551 0.445 0.025  -0.026 -0.031 196 ASP CCC CA  
8882  C C   . ASP C 196 ? 0.352 0.567 0.463 0.026  -0.026 -0.037 196 ASP CCC C   
8883  O O   . ASP C 196 ? 0.377 0.588 0.497 0.027  -0.031 -0.037 196 ASP CCC O   
8884  C CB  . ASP C 196 ? 0.317 0.536 0.440 0.024  -0.028 -0.038 196 ASP CCC CB  
8885  C CG  . ASP C 196 ? 0.296 0.516 0.418 0.023  -0.028 -0.035 196 ASP CCC CG  
8886  O OD1 . ASP C 196 ? 0.281 0.498 0.404 0.023  -0.031 -0.027 196 ASP CCC OD1 
8887  O OD2 . ASP C 196 ? 0.294 0.519 0.413 0.022  -0.024 -0.039 196 ASP CCC OD2 
8888  N N   . ILE C 197 ? 0.339 0.557 0.441 0.026  -0.021 -0.041 197 ILE CCC N   
8889  C CA  . ILE C 197 ? 0.312 0.531 0.416 0.027  -0.020 -0.048 197 ILE CCC CA  
8890  C C   . ILE C 197 ? 0.319 0.533 0.421 0.028  -0.022 -0.043 197 ILE CCC C   
8891  O O   . ILE C 197 ? 0.353 0.566 0.462 0.029  -0.024 -0.048 197 ILE CCC O   
8892  C CB  . ILE C 197 ? 0.301 0.525 0.394 0.026  -0.014 -0.051 197 ILE CCC CB  
8893  C CG1 . ILE C 197 ? 0.308 0.534 0.403 0.025  -0.013 -0.058 197 ILE CCC CG1 
8894  C CG2 . ILE C 197 ? 0.305 0.527 0.384 0.026  -0.011 -0.043 197 ILE CCC CG2 
8895  C CD1 . ILE C 197 ? 0.329 0.557 0.440 0.025  -0.016 -0.067 197 ILE CCC CD1 
8896  N N   . PHE C 198 ? 0.324 0.536 0.417 0.029  -0.022 -0.034 198 PHE CCC N   
8897  C CA  . PHE C 198 ? 0.337 0.544 0.426 0.030  -0.024 -0.030 198 PHE CCC CA  
8898  C C   . PHE C 198 ? 0.353 0.556 0.453 0.030  -0.030 -0.028 198 PHE CCC C   
8899  O O   . PHE C 198 ? 0.342 0.543 0.443 0.031  -0.032 -0.026 198 PHE CCC O   
8900  C CB  . PHE C 198 ? 0.313 0.520 0.388 0.030  -0.021 -0.023 198 PHE CCC CB  
8901  C CG  . PHE C 198 ? 0.311 0.521 0.377 0.030  -0.015 -0.026 198 PHE CCC CG  
8902  C CD1 . PHE C 198 ? 0.313 0.525 0.377 0.031  -0.013 -0.031 198 PHE CCC CD1 
8903  C CD2 . PHE C 198 ? 0.311 0.524 0.370 0.030  -0.013 -0.023 198 PHE CCC CD2 
8904  C CE1 . PHE C 198 ? 0.303 0.517 0.358 0.030  -0.009 -0.033 198 PHE CCC CE1 
8905  C CE2 . PHE C 198 ? 0.289 0.504 0.340 0.030  -0.009 -0.025 198 PHE CCC CE2 
8906  C CZ  . PHE C 198 ? 0.300 0.516 0.350 0.030  -0.007 -0.029 198 PHE CCC CZ  
8907  N N   . PHE C 199 ? 0.402 0.606 0.513 0.029  -0.034 -0.027 199 PHE CCC N   
8908  C CA  . PHE C 199 ? 0.430 0.629 0.551 0.028  -0.041 -0.023 199 PHE CCC CA  
8909  C C   . PHE C 199 ? 0.427 0.626 0.566 0.028  -0.045 -0.030 199 PHE CCC C   
8910  O O   . PHE C 199 ? 0.439 0.634 0.589 0.027  -0.052 -0.027 199 PHE CCC O   
8911  C CB  . PHE C 199 ? 0.444 0.644 0.562 0.027  -0.042 -0.014 199 PHE CCC CB  
8912  C CG  . PHE C 199 ? 0.470 0.671 0.571 0.027  -0.038 -0.007 199 PHE CCC CG  
8913  C CD1 . PHE C 199 ? 0.503 0.703 0.599 0.028  -0.038 -0.004 199 PHE CCC CD1 
8914  C CD2 . PHE C 199 ? 0.479 0.684 0.572 0.027  -0.033 -0.005 199 PHE CCC CD2 
8915  C CE1 . PHE C 199 ? 0.508 0.710 0.590 0.028  -0.034 0.000  199 PHE CCC CE1 
8916  C CE2 . PHE C 199 ? 0.478 0.686 0.558 0.027  -0.029 -0.001 199 PHE CCC CE2 
8917  C CZ  . PHE C 199 ? 0.513 0.719 0.587 0.028  -0.030 0.002  199 PHE CCC CZ  
8918  N N   . LEU C 200 ? 0.428 0.631 0.570 0.029  -0.042 -0.040 200 LEU CCC N   
8919  C CA  . LEU C 200 ? 0.414 0.618 0.574 0.029  -0.047 -0.049 200 LEU CCC CA  
8920  C C   . LEU C 200 ? 0.402 0.600 0.573 0.029  -0.054 -0.048 200 LEU CCC C   
8921  O O   . LEU C 200 ? 0.354 0.551 0.522 0.030  -0.053 -0.049 200 LEU CCC O   
8922  C CB  . LEU C 200 ? 0.403 0.613 0.563 0.029  -0.042 -0.060 200 LEU CCC CB  
8923  C CG  . LEU C 200 ? 0.394 0.610 0.548 0.028  -0.036 -0.063 200 LEU CCC CG  
8924  C CD1 . LEU C 200 ? 0.381 0.604 0.538 0.027  -0.033 -0.075 200 LEU CCC CD1 
8925  C CD2 . LEU C 200 ? 0.418 0.634 0.580 0.027  -0.040 -0.062 200 LEU CCC CD2 
8926  N N   . SER C 201 ? 0.442 0.637 0.629 0.029  -0.061 -0.048 201 SER CCC N   
8927  C CA  A SER C 201 ? 0.463 0.653 0.665 0.029  -0.069 -0.048 201 SER CCC CA  
8928  C CA  B SER C 201 ? 0.479 0.669 0.681 0.029  -0.069 -0.048 201 SER CCC CA  
8929  C C   . SER C 201 ? 0.499 0.692 0.710 0.031  -0.069 -0.060 201 SER CCC C   
8930  O O   . SER C 201 ? 0.496 0.684 0.713 0.032  -0.073 -0.061 201 SER CCC O   
8931  C CB  A SER C 201 ? 0.451 0.638 0.668 0.028  -0.078 -0.045 201 SER CCC CB  
8932  C CB  B SER C 201 ? 0.484 0.671 0.701 0.028  -0.077 -0.044 201 SER CCC CB  
8933  O OG  A SER C 201 ? 0.433 0.624 0.659 0.028  -0.077 -0.053 201 SER CCC OG  
8934  O OG  B SER C 201 ? 0.515 0.699 0.721 0.026  -0.078 -0.032 201 SER CCC OG  
8935  N N   . LYS C 202 ? 0.513 0.713 0.726 0.031  -0.064 -0.071 202 LYS CCC N   
8936  C CA  . LYS C 202 ? 0.548 0.752 0.769 0.032  -0.063 -0.084 202 LYS CCC CA  
8937  C C   . LYS C 202 ? 0.513 0.724 0.719 0.032  -0.054 -0.087 202 LYS CCC C   
8938  O O   . LYS C 202 ? 0.531 0.744 0.723 0.031  -0.049 -0.083 202 LYS CCC O   
8939  C CB  . LYS C 202 ? 0.646 0.855 0.886 0.033  -0.066 -0.094 202 LYS CCC CB  
8940  C CG  . LYS C 202 ? 0.770 0.984 1.023 0.034  -0.067 -0.108 202 LYS CCC CG  
8941  C CD  . LYS C 202 ? 0.862 1.082 1.131 0.034  -0.069 -0.120 202 LYS CCC CD  
8942  C CE  . LYS C 202 ? 0.941 1.167 1.224 0.035  -0.070 -0.135 202 LYS CCC CE  
8943  N NZ  . LYS C 202 ? 0.952 1.187 1.220 0.034  -0.061 -0.140 202 LYS CCC NZ  
8944  N N   . SER C 203 ? 0.447 0.661 0.654 0.033  -0.052 -0.095 203 SER CCC N   
8945  C CA  . SER C 203 ? 0.434 0.655 0.628 0.032  -0.044 -0.099 203 SER CCC CA  
8946  C C   . SER C 203 ? 0.434 0.664 0.630 0.030  -0.040 -0.107 203 SER CCC C   
8947  O O   . SER C 203 ? 0.485 0.718 0.696 0.030  -0.044 -0.114 203 SER CCC O   
8948  C CB  . SER C 203 ? 0.411 0.634 0.608 0.032  -0.043 -0.107 203 SER CCC CB  
8949  O OG  . SER C 203 ? 0.368 0.596 0.584 0.033  -0.046 -0.119 203 SER CCC OG  
8950  N N   . PRO C 204 ? 0.419 0.653 0.598 0.028  -0.033 -0.105 204 PRO CCC N   
8951  C CA  . PRO C 204 ? 0.398 0.641 0.577 0.026  -0.029 -0.110 204 PRO CCC CA  
8952  C C   . PRO C 204 ? 0.375 0.629 0.563 0.025  -0.028 -0.125 204 PRO CCC C   
8953  O O   . PRO C 204 ? 0.356 0.618 0.547 0.023  -0.026 -0.130 204 PRO CCC O   
8954  C CB  . PRO C 204 ? 0.419 0.662 0.577 0.025  -0.023 -0.103 204 PRO CCC CB  
8955  C CG  . PRO C 204 ? 0.414 0.654 0.565 0.026  -0.022 -0.100 204 PRO CCC CG  
8956  C CD  . PRO C 204 ? 0.418 0.650 0.579 0.028  -0.029 -0.098 204 PRO CCC CD  
8957  N N   . GLY C 205 ? 0.375 0.630 0.568 0.026  -0.028 -0.131 205 GLY CCC N   
8958  C CA  . GLY C 205 ? 0.384 0.652 0.584 0.024  -0.026 -0.144 205 GLY CCC CA  
8959  C C   . GLY C 205 ? 0.361 0.639 0.547 0.020  -0.018 -0.146 205 GLY CCC C   
8960  O O   . GLY C 205 ? 0.328 0.601 0.496 0.019  -0.015 -0.136 205 GLY CCC O   
8961  N N   . LYS C 206 ? 0.324 0.614 0.518 0.018  -0.017 -0.158 206 LYS CCC N   
8962  C CA  . LYS C 206 ? 0.333 0.635 0.516 0.013  -0.010 -0.161 206 LYS CCC CA  
8963  C C   . LYS C 206 ? 0.323 0.620 0.495 0.013  -0.009 -0.150 206 LYS CCC C   
8964  O O   . LYS C 206 ? 0.326 0.621 0.507 0.014  -0.012 -0.151 206 LYS CCC O   
8965  C CB  . LYS C 206 ? 0.339 0.656 0.536 0.011  -0.010 -0.176 206 LYS CCC CB  
8966  C CG  . LYS C 206 ? 0.364 0.694 0.551 0.006  -0.004 -0.179 206 LYS CCC CG  
8967  C CD  . LYS C 206 ? 0.376 0.724 0.575 0.003  -0.002 -0.196 206 LYS CCC CD  
8968  C CE  . LYS C 206 ? 0.383 0.745 0.569 -0.003 0.004  -0.197 206 LYS CCC CE  
8969  N NZ  . LYS C 206 ? 0.394 0.773 0.592 -0.005 0.005  -0.213 206 LYS CCC NZ  
8970  N N   . THR C 207 ? 0.301 0.598 0.455 0.011  -0.005 -0.142 207 THR CCC N   
8971  C CA  . THR C 207 ? 0.299 0.589 0.442 0.011  -0.004 -0.131 207 THR CCC CA  
8972  C C   . THR C 207 ? 0.296 0.595 0.427 0.006  0.001  -0.131 207 THR CCC C   
8973  O O   . THR C 207 ? 0.311 0.616 0.434 0.003  0.005  -0.133 207 THR CCC O   
8974  C CB  . THR C 207 ? 0.295 0.573 0.428 0.013  -0.005 -0.119 207 THR CCC CB  
8975  O OG1 . THR C 207 ? 0.287 0.557 0.431 0.017  -0.010 -0.119 207 THR CCC OG1 
8976  C CG2 . THR C 207 ? 0.295 0.567 0.418 0.013  -0.004 -0.108 207 THR CCC CG2 
8977  N N   . LEU C 208 ? 0.285 0.585 0.415 0.005  0.002  -0.128 208 LEU CCC N   
8978  C CA  . LEU C 208 ? 0.297 0.602 0.413 0.001  0.006  -0.124 208 LEU CCC CA  
8979  C C   . LEU C 208 ? 0.288 0.581 0.393 0.003  0.006  -0.111 208 LEU CCC C   
8980  O O   . LEU C 208 ? 0.272 0.558 0.383 0.006  0.003  -0.107 208 LEU CCC O   
8981  C CB  . LEU C 208 ? 0.310 0.624 0.434 -0.001 0.006  -0.132 208 LEU CCC CB  
8982  C CG  . LEU C 208 ? 0.310 0.630 0.422 -0.006 0.010  -0.128 208 LEU CCC CG  
8983  C CD1 . LEU C 208 ? 0.320 0.650 0.422 -0.011 0.014  -0.130 208 LEU CCC CD1 
8984  C CD2 . LEU C 208 ? 0.303 0.630 0.423 -0.007 0.009  -0.134 208 LEU CCC CD2 
8985  N N   . VAL C 209 ? 0.292 0.585 0.383 0.001  0.008  -0.105 209 VAL CCC N   
8986  C CA  . VAL C 209 ? 0.287 0.571 0.366 0.002  0.009  -0.093 209 VAL CCC CA  
8987  C C   . VAL C 209 ? 0.294 0.585 0.366 -0.003 0.011  -0.092 209 VAL CCC C   
8988  O O   . VAL C 209 ? 0.289 0.588 0.355 -0.007 0.014  -0.095 209 VAL CCC O   
8989  C CB  . VAL C 209 ? 0.288 0.565 0.358 0.003  0.009  -0.087 209 VAL CCC CB  
8990  C CG1 . VAL C 209 ? 0.311 0.581 0.371 0.004  0.009  -0.077 209 VAL CCC CG1 
8991  C CG2 . VAL C 209 ? 0.288 0.559 0.366 0.007  0.006  -0.088 209 VAL CCC CG2 
8992  N N   . ILE C 210 ? 0.307 0.595 0.377 -0.002 0.011  -0.087 210 ILE CCC N   
8993  C CA  . ILE C 210 ? 0.310 0.604 0.373 -0.006 0.013  -0.085 210 ILE CCC CA  
8994  C C   . ILE C 210 ? 0.294 0.579 0.345 -0.005 0.013  -0.074 210 ILE CCC C   
8995  O O   . ILE C 210 ? 0.303 0.580 0.355 -0.000 0.011  -0.068 210 ILE CCC O   
8996  C CB  . ILE C 210 ? 0.325 0.621 0.395 -0.006 0.012  -0.088 210 ILE CCC CB  
8997  C CG1 . ILE C 210 ? 0.322 0.626 0.406 -0.006 0.011  -0.100 210 ILE CCC CG1 
8998  C CG2 . ILE C 210 ? 0.319 0.622 0.382 -0.010 0.014  -0.086 210 ILE CCC CG2 
8999  C CD1 . ILE C 210 ? 0.308 0.605 0.405 -0.001 0.008  -0.100 210 ILE CCC CD1 
9000  N N   . GLY C 211 ? 0.278 0.567 0.319 -0.008 0.015  -0.072 211 GLY CCC N   
9001  C CA  . GLY C 211 ? 0.281 0.562 0.311 -0.008 0.014  -0.062 211 GLY CCC CA  
9002  C C   . GLY C 211 ? 0.302 0.583 0.328 -0.008 0.014  -0.062 211 GLY CCC C   
9003  O O   . GLY C 211 ? 0.304 0.581 0.334 -0.005 0.014  -0.064 211 GLY CCC O   
9004  N N   . ALA C 212 ? 0.309 0.592 0.326 -0.012 0.015  -0.058 212 ALA CCC N   
9005  C CA  . ALA C 212 ? 0.326 0.606 0.336 -0.013 0.014  -0.055 212 ALA CCC CA  
9006  C C   . ALA C 212 ? 0.319 0.589 0.323 -0.010 0.012  -0.047 212 ALA CCC C   
9007  O O   . ALA C 212 ? 0.313 0.582 0.310 -0.012 0.011  -0.043 212 ALA CCC O   
9008  C CB  . ALA C 212 ? 0.313 0.604 0.320 -0.021 0.015  -0.058 212 ALA CCC CB  
9009  N N   . SER C 213 ? 0.316 0.581 0.322 -0.006 0.012  -0.044 213 SER CCC N   
9010  C CA  . SER C 213 ? 0.338 0.594 0.341 -0.001 0.010  -0.037 213 SER CCC CA  
9011  C C   . SER C 213 ? 0.317 0.567 0.320 0.003  0.010  -0.037 213 SER CCC C   
9012  O O   . SER C 213 ? 0.317 0.570 0.325 0.002  0.010  -0.043 213 SER CCC O   
9013  C CB  . SER C 213 ? 0.360 0.612 0.367 0.003  0.010  -0.036 213 SER CCC CB  
9014  O OG  . SER C 213 ? 0.341 0.595 0.357 0.005  0.011  -0.041 213 SER CCC OG  
9015  N N   . TYR C 214 ? 0.299 0.542 0.298 0.006  0.008  -0.032 214 TYR CCC N   
9016  C CA  . TYR C 214 ? 0.302 0.541 0.301 0.010  0.008  -0.032 214 TYR CCC CA  
9017  C C   . TYR C 214 ? 0.286 0.523 0.292 0.012  0.008  -0.035 214 TYR CCC C   
9018  O O   . TYR C 214 ? 0.284 0.521 0.293 0.013  0.008  -0.038 214 TYR CCC O   
9019  C CB  . TYR C 214 ? 0.335 0.568 0.329 0.013  0.006  -0.026 214 TYR CCC CB  
9020  C CG  . TYR C 214 ? 0.338 0.566 0.333 0.018  0.006  -0.024 214 TYR CCC CG  
9021  C CD1 . TYR C 214 ? 0.339 0.564 0.336 0.021  0.005  -0.023 214 TYR CCC CD1 
9022  C CD2 . TYR C 214 ? 0.325 0.554 0.320 0.018  0.006  -0.020 214 TYR CCC CD2 
9023  C CE1 . TYR C 214 ? 0.342 0.565 0.340 0.025  0.005  -0.020 214 TYR CCC CE1 
9024  C CE2 . TYR C 214 ? 0.351 0.578 0.346 0.022  0.006  -0.017 214 TYR CCC CE2 
9025  C CZ  . TYR C 214 ? 0.369 0.593 0.365 0.025  0.005  -0.017 214 TYR CCC CZ  
9026  O OH  . TYR C 214 ? 0.444 0.667 0.441 0.028  0.005  -0.014 214 TYR CCC OH  
9027  N N   . ILE C 215 ? 0.265 0.503 0.276 0.014  0.008  -0.034 215 ILE CCC N   
9028  C CA  . ILE C 215 ? 0.257 0.493 0.276 0.016  0.007  -0.036 215 ILE CCC CA  
9029  C C   . ILE C 215 ? 0.263 0.504 0.288 0.014  0.007  -0.044 215 ILE CCC C   
9030  O O   . ILE C 215 ? 0.259 0.499 0.289 0.015  0.006  -0.047 215 ILE CCC O   
9031  C CB  . ILE C 215 ? 0.246 0.481 0.267 0.018  0.006  -0.033 215 ILE CCC CB  
9032  C CG1 . ILE C 215 ? 0.251 0.482 0.266 0.021  0.006  -0.027 215 ILE CCC CG1 
9033  C CG2 . ILE C 215 ? 0.235 0.469 0.265 0.019  0.005  -0.036 215 ILE CCC CG2 
9034  C CD1 . ILE C 215 ? 0.247 0.479 0.262 0.021  0.006  -0.023 215 ILE CCC CD1 
9035  N N   . GLY C 216 ? 0.256 0.504 0.282 0.010  0.009  -0.047 216 GLY CCC N   
9036  C CA  . GLY C 216 ? 0.257 0.512 0.289 0.007  0.010  -0.055 216 GLY CCC CA  
9037  C C   . GLY C 216 ? 0.266 0.523 0.297 0.006  0.010  -0.059 216 GLY CCC C   
9038  O O   . GLY C 216 ? 0.258 0.516 0.296 0.006  0.009  -0.065 216 GLY CCC O   
9039  N N   . LEU C 217 ? 0.261 0.517 0.283 0.004  0.010  -0.055 217 LEU CCC N   
9040  C CA  . LEU C 217 ? 0.259 0.517 0.278 0.002  0.011  -0.057 217 LEU CCC CA  
9041  C C   . LEU C 217 ? 0.260 0.511 0.282 0.007  0.009  -0.057 217 LEU CCC C   
9042  O O   . LEU C 217 ? 0.226 0.479 0.253 0.006  0.009  -0.062 217 LEU CCC O   
9043  C CB  . LEU C 217 ? 0.271 0.529 0.281 -0.001 0.011  -0.052 217 LEU CCC CB  
9044  C CG  . LEU C 217 ? 0.278 0.545 0.285 -0.007 0.012  -0.053 217 LEU CCC CG  
9045  C CD1 . LEU C 217 ? 0.289 0.555 0.287 -0.011 0.011  -0.049 217 LEU CCC CD1 
9046  C CD2 . LEU C 217 ? 0.298 0.575 0.311 -0.011 0.014  -0.062 217 LEU CCC CD2 
9047  N N   . GLU C 218 ? 0.276 0.519 0.295 0.011  0.008  -0.050 218 GLU CCC N   
9048  C CA  . GLU C 218 ? 0.287 0.523 0.308 0.015  0.006  -0.049 218 GLU CCC CA  
9049  C C   . GLU C 218 ? 0.267 0.504 0.299 0.016  0.005  -0.054 218 GLU CCC C   
9050  O O   . GLU C 218 ? 0.242 0.478 0.277 0.017  0.005  -0.057 218 GLU CCC O   
9051  C CB  . GLU C 218 ? 0.302 0.532 0.320 0.019  0.005  -0.042 218 GLU CCC CB  
9052  C CG  . GLU C 218 ? 0.332 0.560 0.341 0.019  0.005  -0.037 218 GLU CCC CG  
9053  C CD  . GLU C 218 ? 0.362 0.585 0.368 0.023  0.005  -0.032 218 GLU CCC CD  
9054  O OE1 . GLU C 218 ? 0.371 0.593 0.380 0.024  0.004  -0.031 218 GLU CCC OE1 
9055  O OE2 . GLU C 218 ? 0.412 0.632 0.412 0.024  0.004  -0.029 218 GLU CCC OE2 
9056  N N   . THR C 219 ? 0.261 0.500 0.298 0.016  0.005  -0.055 219 THR CCC N   
9057  C CA  . THR C 219 ? 0.280 0.520 0.329 0.017  0.003  -0.060 219 THR CCC CA  
9058  C C   . THR C 219 ? 0.265 0.512 0.321 0.015  0.004  -0.069 219 THR CCC C   
9059  O O   . THR C 219 ? 0.264 0.509 0.327 0.017  0.002  -0.073 219 THR CCC O   
9060  C CB  . THR C 219 ? 0.293 0.535 0.347 0.017  0.003  -0.059 219 THR CCC CB  
9061  O OG1 . THR C 219 ? 0.293 0.529 0.340 0.019  0.003  -0.051 219 THR CCC OG1 
9062  C CG2 . THR C 219 ? 0.293 0.534 0.359 0.019  -0.000 -0.063 219 THR CCC CG2 
9063  N N   . ALA C 220 ? 0.271 0.526 0.323 0.011  0.007  -0.073 220 ALA CCC N   
9064  C CA  . ALA C 220 ? 0.270 0.534 0.328 0.008  0.008  -0.082 220 ALA CCC CA  
9065  C C   . ALA C 220 ? 0.280 0.542 0.335 0.008  0.008  -0.082 220 ALA CCC C   
9066  O O   . ALA C 220 ? 0.270 0.535 0.334 0.008  0.007  -0.089 220 ALA CCC O   
9067  C CB  . ALA C 220 ? 0.256 0.529 0.310 0.002  0.010  -0.084 220 ALA CCC CB  
9068  N N   . GLY C 221 ? 0.287 0.544 0.332 0.008  0.008  -0.075 221 GLY CCC N   
9069  C CA  . GLY C 221 ? 0.306 0.560 0.347 0.009  0.008  -0.074 221 GLY CCC CA  
9070  C C   . GLY C 221 ? 0.306 0.555 0.354 0.013  0.005  -0.075 221 GLY CCC C   
9071  O O   . GLY C 221 ? 0.393 0.644 0.444 0.013  0.005  -0.081 221 GLY CCC O   
9072  N N   . PHE C 222 ? 0.273 0.514 0.323 0.017  0.003  -0.071 222 PHE CCC N   
9073  C CA  . PHE C 222 ? 0.284 0.519 0.340 0.020  0.001  -0.071 222 PHE CCC CA  
9074  C C   . PHE C 222 ? 0.291 0.531 0.361 0.020  -0.001 -0.079 222 PHE CCC C   
9075  O O   . PHE C 222 ? 0.281 0.519 0.358 0.022  -0.003 -0.083 222 PHE CCC O   
9076  C CB  . PHE C 222 ? 0.285 0.512 0.338 0.024  -0.001 -0.063 222 PHE CCC CB  
9077  C CG  . PHE C 222 ? 0.271 0.497 0.327 0.025  -0.002 -0.060 222 PHE CCC CG  
9078  C CD1 . PHE C 222 ? 0.269 0.495 0.337 0.025  -0.005 -0.063 222 PHE CCC CD1 
9079  C CD2 . PHE C 222 ? 0.264 0.488 0.312 0.025  -0.001 -0.053 222 PHE CCC CD2 
9080  C CE1 . PHE C 222 ? 0.275 0.500 0.346 0.026  -0.006 -0.060 222 PHE CCC CE1 
9081  C CE2 . PHE C 222 ? 0.287 0.510 0.337 0.026  -0.002 -0.050 222 PHE CCC CE2 
9082  C CZ  . PHE C 222 ? 0.282 0.505 0.343 0.026  -0.005 -0.053 222 PHE CCC CZ  
9083  N N   . LEU C 223 ? 0.292 0.537 0.368 0.019  -0.001 -0.082 223 LEU CCC N   
9084  C CA  . LEU C 223 ? 0.292 0.540 0.382 0.019  -0.003 -0.091 223 LEU CCC CA  
9085  C C   . LEU C 223 ? 0.293 0.550 0.387 0.016  -0.001 -0.100 223 LEU CCC C   
9086  O O   . LEU C 223 ? 0.318 0.575 0.423 0.018  -0.003 -0.106 223 LEU CCC O   
9087  C CB  . LEU C 223 ? 0.280 0.533 0.376 0.018  -0.003 -0.093 223 LEU CCC CB  
9088  C CG  . LEU C 223 ? 0.277 0.522 0.372 0.020  -0.005 -0.086 223 LEU CCC CG  
9089  C CD1 . LEU C 223 ? 0.287 0.537 0.387 0.018  -0.005 -0.089 223 LEU CCC CD1 
9090  C CD2 . LEU C 223 ? 0.265 0.504 0.370 0.023  -0.010 -0.084 223 LEU CCC CD2 
9091  N N   . ASN C 224 ? 0.300 0.564 0.385 0.013  0.003  -0.101 224 ASN CCC N   
9092  C CA  . ASN C 224 ? 0.298 0.570 0.384 0.009  0.005  -0.109 224 ASN CCC CA  
9093  C C   . ASN C 224 ? 0.288 0.554 0.373 0.012  0.003  -0.107 224 ASN CCC C   
9094  O O   . ASN C 224 ? 0.325 0.595 0.419 0.012  0.002  -0.115 224 ASN CCC O   
9095  C CB  . ASN C 224 ? 0.290 0.570 0.365 0.004  0.008  -0.108 224 ASN CCC CB  
9096  C CG  . ASN C 224 ? 0.284 0.575 0.361 0.000  0.010  -0.115 224 ASN CCC CG  
9097  O OD1 . ASN C 224 ? 0.324 0.626 0.410 -0.002 0.011  -0.125 224 ASN CCC OD1 
9098  N ND2 . ASN C 224 ? 0.279 0.568 0.347 -0.001 0.011  -0.112 224 ASN CCC ND2 
9099  N N   . GLU C 225 ? 0.297 0.555 0.372 0.014  0.003  -0.098 225 GLU CCC N   
9100  C CA  . GLU C 225 ? 0.305 0.556 0.377 0.016  0.002  -0.096 225 GLU CCC CA  
9101  C C   . GLU C 225 ? 0.289 0.537 0.374 0.019  -0.002 -0.099 225 GLU CCC C   
9102  O O   . GLU C 225 ? 0.317 0.564 0.405 0.020  -0.003 -0.102 225 GLU CCC O   
9103  C CB  . GLU C 225 ? 0.326 0.569 0.387 0.018  0.002  -0.085 225 GLU CCC CB  
9104  C CG  . GLU C 225 ? 0.355 0.601 0.405 0.015  0.004  -0.083 225 GLU CCC CG  
9105  C CD  . GLU C 225 ? 0.390 0.627 0.429 0.017  0.003  -0.074 225 GLU CCC CD  
9106  O OE1 . GLU C 225 ? 0.379 0.614 0.414 0.017  0.004  -0.069 225 GLU CCC OE1 
9107  O OE2 . GLU C 225 ? 0.402 0.635 0.437 0.018  0.003  -0.073 225 GLU CCC OE2 
9108  N N   . LEU C 226 ? 0.263 0.507 0.355 0.021  -0.004 -0.098 226 LEU CCC N   
9109  C CA  . LEU C 226 ? 0.264 0.503 0.368 0.025  -0.009 -0.099 226 LEU CCC CA  
9110  C C   . LEU C 226 ? 0.289 0.535 0.408 0.024  -0.010 -0.111 226 LEU CCC C   
9111  O O   . LEU C 226 ? 0.312 0.554 0.443 0.026  -0.015 -0.113 226 LEU CCC O   
9112  C CB  . LEU C 226 ? 0.251 0.484 0.356 0.027  -0.011 -0.092 226 LEU CCC CB  
9113  C CG  . LEU C 226 ? 0.241 0.465 0.334 0.028  -0.012 -0.081 226 LEU CCC CG  
9114  C CD1 . LEU C 226 ? 0.256 0.476 0.350 0.030  -0.014 -0.075 226 LEU CCC CD1 
9115  C CD2 . LEU C 226 ? 0.242 0.460 0.336 0.031  -0.014 -0.079 226 LEU CCC CD2 
9116  N N   . GLY C 227 ? 0.324 0.581 0.443 0.020  -0.007 -0.118 227 GLY CCC N   
9117  C CA  . GLY C 227 ? 0.322 0.589 0.455 0.019  -0.007 -0.131 227 GLY CCC CA  
9118  C C   . GLY C 227 ? 0.328 0.601 0.469 0.018  -0.007 -0.137 227 GLY CCC C   
9119  O O   . GLY C 227 ? 0.306 0.588 0.460 0.017  -0.008 -0.148 227 GLY CCC O   
9120  N N   . PHE C 228 ? 0.358 0.628 0.493 0.018  -0.007 -0.130 228 PHE CCC N   
9121  C CA  . PHE C 228 ? 0.362 0.638 0.506 0.017  -0.007 -0.135 228 PHE CCC CA  
9122  C C   . PHE C 228 ? 0.352 0.642 0.491 0.012  -0.002 -0.141 228 PHE CCC C   
9123  O O   . PHE C 228 ? 0.362 0.652 0.486 0.009  0.001  -0.135 228 PHE CCC O   
9124  C CB  . PHE C 228 ? 0.379 0.646 0.520 0.019  -0.009 -0.125 228 PHE CCC CB  
9125  C CG  . PHE C 228 ? 0.413 0.668 0.560 0.023  -0.015 -0.120 228 PHE CCC CG  
9126  C CD1 . PHE C 228 ? 0.425 0.680 0.590 0.025  -0.020 -0.127 228 PHE CCC CD1 
9127  C CD2 . PHE C 228 ? 0.429 0.675 0.565 0.024  -0.015 -0.108 228 PHE CCC CD2 
9128  C CE1 . PHE C 228 ? 0.447 0.691 0.618 0.028  -0.026 -0.121 228 PHE CCC CE1 
9129  C CE2 . PHE C 228 ? 0.438 0.675 0.580 0.027  -0.020 -0.103 228 PHE CCC CE2 
9130  C CZ  . PHE C 228 ? 0.431 0.667 0.591 0.029  -0.026 -0.109 228 PHE CCC CZ  
9131  N N   . ASP C 229 ? 0.348 0.648 0.499 0.010  -0.002 -0.151 229 ASP CCC N   
9132  C CA  . ASP C 229 ? 0.344 0.658 0.491 0.005  0.002  -0.158 229 ASP CCC CA  
9133  C C   . ASP C 229 ? 0.337 0.649 0.474 0.004  0.004  -0.149 229 ASP CCC C   
9134  O O   . ASP C 229 ? 0.321 0.627 0.464 0.006  0.001  -0.147 229 ASP CCC O   
9135  C CB  . ASP C 229 ? 0.377 0.702 0.542 0.005  0.001  -0.172 229 ASP CCC CB  
9136  C CG  . ASP C 229 ? 0.400 0.743 0.564 -0.001 0.005  -0.181 229 ASP CCC CG  
9137  O OD1 . ASP C 229 ? 0.430 0.775 0.580 -0.004 0.009  -0.174 229 ASP CCC OD1 
9138  O OD2 . ASP C 229 ? 0.422 0.776 0.599 -0.001 0.005  -0.194 229 ASP CCC OD2 
9139  N N   . THR C 230 ? 0.322 0.635 0.443 0.000  0.007  -0.143 230 THR CCC N   
9140  C CA  . THR C 230 ? 0.319 0.626 0.427 0.000  0.008  -0.132 230 THR CCC CA  
9141  C C   . THR C 230 ? 0.303 0.621 0.403 -0.006 0.012  -0.134 230 THR CCC C   
9142  O O   . THR C 230 ? 0.298 0.625 0.393 -0.010 0.015  -0.136 230 THR CCC O   
9143  C CB  . THR C 230 ? 0.317 0.612 0.414 0.002  0.008  -0.121 230 THR CCC CB  
9144  O OG1 . THR C 230 ? 0.312 0.597 0.418 0.008  0.004  -0.120 230 THR CCC OG1 
9145  C CG2 . THR C 230 ? 0.315 0.604 0.400 0.002  0.009  -0.110 230 THR CCC CG2 
9146  N N   . THR C 231 ? 0.287 0.605 0.385 -0.006 0.012  -0.130 231 THR CCC N   
9147  C CA  . THR C 231 ? 0.293 0.622 0.384 -0.012 0.016  -0.131 231 THR CCC CA  
9148  C C   . THR C 231 ? 0.302 0.623 0.383 -0.011 0.016  -0.120 231 THR CCC C   
9149  O O   . THR C 231 ? 0.325 0.636 0.410 -0.007 0.013  -0.116 231 THR CCC O   
9150  C CB  . THR C 231 ? 0.285 0.627 0.389 -0.014 0.016  -0.143 231 THR CCC CB  
9151  O OG1 . THR C 231 ? 0.299 0.649 0.413 -0.014 0.016  -0.154 231 THR CCC OG1 
9152  C CG2 . THR C 231 ? 0.280 0.635 0.376 -0.021 0.019  -0.145 231 THR CCC CG2 
9153  N N   . VAL C 232 ? 0.294 0.617 0.362 -0.016 0.018  -0.114 232 VAL CCC N   
9154  C CA  . VAL C 232 ? 0.312 0.629 0.371 -0.016 0.018  -0.104 232 VAL CCC CA  
9155  C C   . VAL C 232 ? 0.340 0.668 0.396 -0.021 0.020  -0.107 232 VAL CCC C   
9156  O O   . VAL C 232 ? 0.317 0.656 0.369 -0.027 0.022  -0.110 232 VAL CCC O   
9157  C CB  . VAL C 232 ? 0.308 0.617 0.354 -0.016 0.017  -0.094 232 VAL CCC CB  
9158  C CG1 . VAL C 232 ? 0.334 0.639 0.370 -0.017 0.017  -0.086 232 VAL CCC CG1 
9159  C CG2 . VAL C 232 ? 0.294 0.591 0.341 -0.010 0.015  -0.091 232 VAL CCC CG2 
9160  N N   . ALA C 233 ? 0.349 0.675 0.408 -0.020 0.019  -0.105 233 ALA CCC N   
9161  C CA  . ALA C 233 ? 0.380 0.714 0.435 -0.025 0.020  -0.106 233 ALA CCC CA  
9162  C C   . ALA C 233 ? 0.399 0.726 0.441 -0.026 0.020  -0.094 233 ALA CCC C   
9163  O O   . ALA C 233 ? 0.432 0.747 0.473 -0.021 0.019  -0.087 233 ALA CCC O   
9164  C CB  . ALA C 233 ? 0.391 0.726 0.457 -0.022 0.020  -0.110 233 ALA CCC CB  
9165  N N   . MET C 234 ? 0.415 0.749 0.448 -0.032 0.021  -0.092 234 MET CCC N   
9166  C CA  . MET C 234 ? 0.415 0.743 0.436 -0.033 0.021  -0.081 234 MET CCC CA  
9167  C C   . MET C 234 ? 0.409 0.746 0.426 -0.039 0.021  -0.081 234 MET CCC C   
9168  O O   . MET C 234 ? 0.369 0.720 0.386 -0.046 0.023  -0.086 234 MET CCC O   
9169  C CB  . MET C 234 ? 0.446 0.775 0.461 -0.036 0.020  -0.079 234 MET CCC CB  
9170  C CG  . MET C 234 ? 0.470 0.795 0.474 -0.039 0.019  -0.069 234 MET CCC CG  
9171  S SD  . MET C 234 ? 0.532 0.851 0.529 -0.040 0.017  -0.064 234 MET CCC SD  
9172  C CE  . MET C 234 ? 0.547 0.883 0.546 -0.047 0.020  -0.073 234 MET CCC CE  
9173  N N   . ARG C 235 ? 0.399 0.730 0.415 -0.037 0.021  -0.075 235 ARG CCC N   
9174  C CA  . ARG C 235 ? 0.398 0.736 0.410 -0.042 0.021  -0.074 235 ARG CCC CA  
9175  C C   . ARG C 235 ? 0.399 0.742 0.401 -0.049 0.021  -0.069 235 ARG CCC C   
9176  O O   . ARG C 235 ? 0.407 0.763 0.407 -0.057 0.022  -0.073 235 ARG CCC O   
9177  C CB  . ARG C 235 ? 0.407 0.735 0.419 -0.038 0.020  -0.068 235 ARG CCC CB  
9178  C CG  . ARG C 235 ? 0.431 0.767 0.441 -0.043 0.020  -0.068 235 ARG CCC CG  
9179  C CD  . ARG C 235 ? 0.441 0.768 0.451 -0.039 0.019  -0.062 235 ARG CCC CD  
9180  N NE  . ARG C 235 ? 0.461 0.798 0.473 -0.043 0.020  -0.065 235 ARG CCC NE  
9181  C CZ  . ARG C 235 ? 0.487 0.831 0.491 -0.050 0.020  -0.062 235 ARG CCC CZ  
9182  N NH1 . ARG C 235 ? 0.485 0.825 0.480 -0.053 0.018  -0.055 235 ARG CCC NH1 
9183  N NH2 . ARG C 235 ? 0.532 0.885 0.537 -0.054 0.021  -0.065 235 ARG CCC NH2 
9184  N N   . SER C 236 ? 0.376 0.710 0.372 -0.048 0.019  -0.061 236 SER CCC N   
9185  C CA  . SER C 236 ? 0.373 0.711 0.359 -0.055 0.017  -0.055 236 SER CCC CA  
9186  C C   . SER C 236 ? 0.371 0.703 0.354 -0.054 0.016  -0.053 236 SER CCC C   
9187  O O   . SER C 236 ? 0.372 0.714 0.356 -0.058 0.017  -0.057 236 SER CCC O   
9188  C CB  . SER C 236 ? 0.381 0.714 0.361 -0.056 0.015  -0.047 236 SER CCC CB  
9189  O OG  . SER C 236 ? 0.329 0.647 0.311 -0.048 0.014  -0.042 236 SER CCC OG  
9190  N N   . ILE C 237 ? 0.375 0.694 0.356 -0.049 0.014  -0.045 237 ILE CCC N   
9191  C CA  . ILE C 237 ? 0.348 0.661 0.325 -0.048 0.012  -0.041 237 ILE CCC CA  
9192  C C   . ILE C 237 ? 0.349 0.649 0.330 -0.039 0.011  -0.041 237 ILE CCC C   
9193  O O   . ILE C 237 ? 0.352 0.647 0.337 -0.034 0.012  -0.041 237 ILE CCC O   
9194  C CB  . ILE C 237 ? 0.335 0.644 0.305 -0.051 0.008  -0.031 237 ILE CCC CB  
9195  C CG1 . ILE C 237 ? 0.320 0.618 0.289 -0.046 0.006  -0.026 237 ILE CCC CG1 
9196  C CG2 . ILE C 237 ? 0.317 0.638 0.282 -0.062 0.007  -0.031 237 ILE CCC CG2 
9197  C CD1 . ILE C 237 ? 0.311 0.603 0.275 -0.048 0.002  -0.017 237 ILE CCC CD1 
9198  N N   . PRO C 238 ? 0.340 0.637 0.321 -0.037 0.011  -0.041 238 PRO CCC N   
9199  C CA  . PRO C 238 ? 0.345 0.631 0.328 -0.029 0.010  -0.041 238 PRO CCC CA  
9200  C C   . PRO C 238 ? 0.330 0.605 0.311 -0.025 0.008  -0.033 238 PRO CCC C   
9201  O O   . PRO C 238 ? 0.327 0.601 0.302 -0.028 0.005  -0.028 238 PRO CCC O   
9202  C CB  . PRO C 238 ? 0.341 0.629 0.325 -0.030 0.011  -0.044 238 PRO CCC CB  
9203  C CG  . PRO C 238 ? 0.344 0.639 0.321 -0.039 0.010  -0.041 238 PRO CCC CG  
9204  C CD  . PRO C 238 ? 0.356 0.660 0.333 -0.044 0.011  -0.042 238 PRO CCC CD  
9205  N N   . LEU C 239 ? 0.328 0.595 0.311 -0.018 0.008  -0.032 239 LEU CCC N   
9206  C CA  . LEU C 239 ? 0.325 0.582 0.306 -0.013 0.006  -0.026 239 LEU CCC CA  
9207  C C   . LEU C 239 ? 0.339 0.596 0.315 -0.016 0.003  -0.020 239 LEU CCC C   
9208  O O   . LEU C 239 ? 0.328 0.581 0.301 -0.017 0.000  -0.016 239 LEU CCC O   
9209  C CB  . LEU C 239 ? 0.323 0.575 0.302 -0.012 0.004  -0.025 239 LEU CCC CB  
9210  C CG  . LEU C 239 ? 0.320 0.572 0.303 -0.009 0.006  -0.030 239 LEU CCC CG  
9211  C CD1 . LEU C 239 ? 0.315 0.563 0.296 -0.008 0.004  -0.029 239 LEU CCC CD1 
9212  C CD2 . LEU C 239 ? 0.325 0.573 0.313 -0.002 0.007  -0.031 239 LEU CCC CD2 
9213  N N   . ARG C 240 ? 0.362 0.624 0.340 -0.018 0.005  -0.021 240 ARG CCC N   
9214  C CA  A ARG C 240 ? 0.367 0.628 0.341 -0.021 0.002  -0.016 240 ARG CCC CA  
9215  C CA  B ARG C 240 ? 0.369 0.631 0.343 -0.021 0.002  -0.016 240 ARG CCC CA  
9216  C C   . ARG C 240 ? 0.355 0.607 0.328 -0.016 -0.000 -0.010 240 ARG CCC C   
9217  O O   . ARG C 240 ? 0.374 0.621 0.350 -0.010 0.001  -0.011 240 ARG CCC O   
9218  C CB  A ARG C 240 ? 0.363 0.630 0.340 -0.022 0.005  -0.018 240 ARG CCC CB  
9219  C CB  B ARG C 240 ? 0.369 0.635 0.346 -0.022 0.005  -0.018 240 ARG CCC CB  
9220  C CG  A ARG C 240 ? 0.365 0.634 0.338 -0.027 0.003  -0.014 240 ARG CCC CG  
9221  C CG  B ARG C 240 ? 0.375 0.642 0.349 -0.025 0.003  -0.014 240 ARG CCC CG  
9222  C CD  A ARG C 240 ? 0.347 0.622 0.323 -0.029 0.005  -0.017 240 ARG CCC CD  
9223  C CD  B ARG C 240 ? 0.355 0.617 0.332 -0.020 0.003  -0.012 240 ARG CCC CD  
9224  N NE  A ARG C 240 ? 0.327 0.614 0.302 -0.035 0.007  -0.021 240 ARG CCC NE  
9225  N NE  B ARG C 240 ? 0.341 0.594 0.316 -0.015 0.001  -0.007 240 ARG CCC NE  
9226  C CZ  A ARG C 240 ? 0.316 0.610 0.287 -0.043 0.005  -0.019 240 ARG CCC CZ  
9227  C CZ  B ARG C 240 ? 0.320 0.568 0.299 -0.008 0.002  -0.008 240 ARG CCC CZ  
9228  N NH1 A ARG C 240 ? 0.313 0.602 0.279 -0.045 0.001  -0.012 240 ARG CCC NH1 
9229  N NH1 B ARG C 240 ? 0.309 0.550 0.286 -0.004 -0.001 -0.005 240 ARG CCC NH1 
9230  N NH2 A ARG C 240 ? 0.325 0.630 0.296 -0.049 0.007  -0.024 240 ARG CCC NH2 
9231  N NH2 B ARG C 240 ? 0.317 0.566 0.299 -0.006 0.004  -0.012 240 ARG CCC NH2 
9232  N N   . GLY C 241 ? 0.360 0.610 0.329 -0.019 -0.004 -0.005 241 GLY CCC N   
9233  C CA  . GLY C 241 ? 0.354 0.596 0.323 -0.015 -0.008 -0.001 241 GLY CCC CA  
9234  C C   . GLY C 241 ? 0.378 0.615 0.345 -0.014 -0.010 0.000  241 GLY CCC C   
9235  O O   . GLY C 241 ? 0.440 0.672 0.408 -0.012 -0.014 0.004  241 GLY CCC O   
9236  N N   . PHE C 242 ? 0.374 0.614 0.342 -0.014 -0.008 -0.004 242 PHE CCC N   
9237  C CA  . PHE C 242 ? 0.351 0.586 0.318 -0.012 -0.010 -0.004 242 PHE CCC CA  
9238  C C   . PHE C 242 ? 0.337 0.575 0.300 -0.020 -0.012 -0.001 242 PHE CCC C   
9239  O O   . PHE C 242 ? 0.315 0.561 0.277 -0.027 -0.011 -0.001 242 PHE CCC O   
9240  C CB  . PHE C 242 ? 0.342 0.578 0.312 -0.009 -0.006 -0.009 242 PHE CCC CB  
9241  C CG  . PHE C 242 ? 0.357 0.588 0.329 -0.002 -0.004 -0.011 242 PHE CCC CG  
9242  C CD1 . PHE C 242 ? 0.333 0.566 0.308 -0.000 -0.002 -0.011 242 PHE CCC CD1 
9243  C CD2 . PHE C 242 ? 0.336 0.563 0.310 0.003  -0.004 -0.012 242 PHE CCC CD2 
9244  C CE1 . PHE C 242 ? 0.363 0.592 0.340 0.006  -0.001 -0.012 242 PHE CCC CE1 
9245  C CE2 . PHE C 242 ? 0.333 0.557 0.309 0.009  -0.003 -0.013 242 PHE CCC CE2 
9246  C CZ  . PHE C 242 ? 0.337 0.562 0.315 0.010  -0.001 -0.012 242 PHE CCC CZ  
9247  N N   . ASP C 243 ? 0.319 0.553 0.282 -0.019 -0.016 0.001  243 ASP CCC N   
9248  C CA  . ASP C 243 ? 0.318 0.555 0.278 -0.027 -0.019 0.004  243 ASP CCC CA  
9249  C C   . ASP C 243 ? 0.309 0.556 0.267 -0.033 -0.015 0.000  243 ASP CCC C   
9250  O O   . ASP C 243 ? 0.326 0.575 0.287 -0.030 -0.011 -0.006 243 ASP CCC O   
9251  C CB  . ASP C 243 ? 0.324 0.554 0.284 -0.024 -0.022 0.005  243 ASP CCC CB  
9252  C CG  . ASP C 243 ? 0.345 0.578 0.303 -0.031 -0.026 0.009  243 ASP CCC CG  
9253  O OD1 . ASP C 243 ? 0.352 0.582 0.310 -0.034 -0.031 0.014  243 ASP CCC OD1 
9254  O OD2 . ASP C 243 ? 0.385 0.622 0.341 -0.034 -0.024 0.006  243 ASP CCC OD2 
9255  N N   . ARG C 244 ? 0.295 0.550 0.250 -0.041 -0.017 0.003  244 ARG CCC N   
9256  C CA  . ARG C 244 ? 0.316 0.583 0.270 -0.048 -0.013 -0.002 244 ARG CCC CA  
9257  C C   . ARG C 244 ? 0.294 0.564 0.248 -0.049 -0.012 -0.005 244 ARG CCC C   
9258  O O   . ARG C 244 ? 0.295 0.570 0.252 -0.048 -0.008 -0.012 244 ARG CCC O   
9259  C CB  . ARG C 244 ? 0.353 0.629 0.303 -0.058 -0.016 0.002  244 ARG CCC CB  
9260  C CG  . ARG C 244 ? 0.382 0.658 0.333 -0.058 -0.016 0.004  244 ARG CCC CG  
9261  C CD  . ARG C 244 ? 0.400 0.682 0.353 -0.055 -0.010 -0.003 244 ARG CCC CD  
9262  N NE  . ARG C 244 ? 0.393 0.666 0.351 -0.045 -0.008 -0.006 244 ARG CCC NE  
9263  C CZ  . ARG C 244 ? 0.389 0.663 0.351 -0.041 -0.003 -0.013 244 ARG CCC CZ  
9264  N NH1 . ARG C 244 ? 0.389 0.674 0.352 -0.045 0.000  -0.019 244 ARG CCC NH1 
9265  N NH2 . ARG C 244 ? 0.406 0.672 0.371 -0.032 -0.002 -0.013 244 ARG CCC NH2 
9266  N N   . GLN C 245 ? 0.302 0.567 0.253 -0.051 -0.017 0.000  245 GLN CCC N   
9267  C CA  . GLN C 245 ? 0.303 0.571 0.254 -0.054 -0.017 -0.001 245 GLN CCC CA  
9268  C C   . GLN C 245 ? 0.326 0.590 0.281 -0.045 -0.013 -0.008 245 GLN CCC C   
9269  O O   . GLN C 245 ? 0.330 0.601 0.286 -0.047 -0.010 -0.014 245 GLN CCC O   
9270  C CB  . GLN C 245 ? 0.310 0.570 0.259 -0.055 -0.024 0.006  245 GLN CCC CB  
9271  C CG  . GLN C 245 ? 0.321 0.586 0.269 -0.059 -0.024 0.005  245 GLN CCC CG  
9272  C CD  . GLN C 245 ? 0.336 0.593 0.283 -0.061 -0.031 0.012  245 GLN CCC CD  
9273  O OE1 . GLN C 245 ? 0.368 0.615 0.316 -0.057 -0.035 0.016  245 GLN CCC OE1 
9274  N NE2 . GLN C 245 ? 0.357 0.619 0.302 -0.067 -0.032 0.013  245 GLN CCC NE2 
9275  N N   . CYS C 246 ? 0.305 0.558 0.262 -0.037 -0.014 -0.007 246 CYS CCC N   
9276  C CA  . CYS C 246 ? 0.322 0.570 0.283 -0.029 -0.011 -0.012 246 CYS CCC CA  
9277  C C   . CYS C 246 ? 0.329 0.584 0.294 -0.028 -0.006 -0.018 246 CYS CCC C   
9278  O O   . CYS C 246 ? 0.390 0.647 0.358 -0.026 -0.003 -0.024 246 CYS CCC O   
9279  C CB  . CYS C 246 ? 0.330 0.567 0.292 -0.021 -0.013 -0.010 246 CYS CCC CB  
9280  S SG  . CYS C 246 ? 0.379 0.608 0.340 -0.020 -0.019 -0.004 246 CYS CCC SG  
9281  N N   . SER C 247 ? 0.323 0.579 0.287 -0.029 -0.005 -0.018 247 SER CCC N   
9282  C CA  . SER C 247 ? 0.315 0.577 0.283 -0.027 -0.000 -0.024 247 SER CCC CA  
9283  C C   . SER C 247 ? 0.316 0.590 0.286 -0.034 0.002  -0.030 247 SER CCC C   
9284  O O   . SER C 247 ? 0.315 0.592 0.290 -0.031 0.005  -0.036 247 SER CCC O   
9285  C CB  . SER C 247 ? 0.305 0.568 0.273 -0.028 -0.000 -0.022 247 SER CCC CB  
9286  O OG  . SER C 247 ? 0.267 0.520 0.235 -0.022 -0.003 -0.017 247 SER CCC OG  
9287  N N   . GLU C 248 ? 0.334 0.615 0.300 -0.041 0.001  -0.027 248 GLU CCC N   
9288  C CA  . GLU C 248 ? 0.374 0.668 0.339 -0.048 0.003  -0.033 248 GLU CCC CA  
9289  C C   . GLU C 248 ? 0.354 0.648 0.321 -0.047 0.004  -0.037 248 GLU CCC C   
9290  O O   . GLU C 248 ? 0.321 0.624 0.292 -0.048 0.007  -0.045 248 GLU CCC O   
9291  C CB  . GLU C 248 ? 0.418 0.720 0.377 -0.058 0.001  -0.029 248 GLU CCC CB  
9292  C CG  . GLU C 248 ? 0.445 0.753 0.404 -0.061 0.001  -0.027 248 GLU CCC CG  
9293  C CD  . GLU C 248 ? 0.466 0.778 0.418 -0.070 -0.002 -0.020 248 GLU CCC CD  
9294  O OE1 . GLU C 248 ? 0.502 0.817 0.451 -0.075 -0.005 -0.017 248 GLU CCC OE1 
9295  O OE2 . GLU C 248 ? 0.478 0.790 0.429 -0.071 -0.004 -0.016 248 GLU CCC OE2 
9296  N N   . LYS C 249 ? 0.358 0.642 0.323 -0.044 0.000  -0.032 249 LYS CCC N   
9297  C CA  . LYS C 249 ? 0.360 0.641 0.327 -0.041 0.001  -0.035 249 LYS CCC CA  
9298  C C   . LYS C 249 ? 0.327 0.607 0.302 -0.034 0.004  -0.042 249 LYS CCC C   
9299  O O   . LYS C 249 ? 0.318 0.603 0.296 -0.035 0.006  -0.048 249 LYS CCC O   
9300  C CB  . LYS C 249 ? 0.376 0.646 0.341 -0.038 -0.003 -0.029 249 LYS CCC CB  
9301  C CG  . LYS C 249 ? 0.383 0.652 0.349 -0.036 -0.003 -0.032 249 LYS CCC CG  
9302  C CD  . LYS C 249 ? 0.381 0.640 0.345 -0.034 -0.007 -0.027 249 LYS CCC CD  
9303  C CE  . LYS C 249 ? 0.379 0.638 0.345 -0.032 -0.006 -0.031 249 LYS CCC CE  
9304  N NZ  . LYS C 249 ? 0.379 0.651 0.345 -0.040 -0.004 -0.035 249 LYS CCC NZ  
9305  N N   . ILE C 250 ? 0.299 0.571 0.275 -0.028 0.004  -0.040 250 ILE CCC N   
9306  C CA  . ILE C 250 ? 0.270 0.540 0.253 -0.022 0.007  -0.046 250 ILE CCC CA  
9307  C C   . ILE C 250 ? 0.271 0.552 0.259 -0.025 0.010  -0.054 250 ILE CCC C   
9308  O O   . ILE C 250 ? 0.240 0.522 0.233 -0.023 0.011  -0.060 250 ILE CCC O   
9309  C CB  . ILE C 250 ? 0.255 0.516 0.239 -0.016 0.006  -0.042 250 ILE CCC CB  
9310  C CG1 . ILE C 250 ? 0.249 0.499 0.228 -0.012 0.003  -0.036 250 ILE CCC CG1 
9311  C CG2 . ILE C 250 ? 0.242 0.502 0.233 -0.011 0.008  -0.047 250 ILE CCC CG2 
9312  C CD1 . ILE C 250 ? 0.252 0.496 0.230 -0.008 0.002  -0.031 250 ILE CCC CD1 
9313  N N   . VAL C 251 ? 0.277 0.566 0.263 -0.030 0.011  -0.054 251 VAL CCC N   
9314  C CA  . VAL C 251 ? 0.284 0.585 0.276 -0.034 0.014  -0.062 251 VAL CCC CA  
9315  C C   . VAL C 251 ? 0.296 0.607 0.289 -0.039 0.015  -0.068 251 VAL CCC C   
9316  O O   . VAL C 251 ? 0.283 0.600 0.284 -0.038 0.017  -0.077 251 VAL CCC O   
9317  C CB  . VAL C 251 ? 0.296 0.604 0.285 -0.039 0.014  -0.061 251 VAL CCC CB  
9318  C CG1 . VAL C 251 ? 0.287 0.611 0.281 -0.044 0.017  -0.070 251 VAL CCC CG1 
9319  C CG2 . VAL C 251 ? 0.294 0.593 0.285 -0.033 0.013  -0.057 251 VAL CCC CG2 
9320  N N   . GLU C 252 ? 0.327 0.641 0.313 -0.044 0.013  -0.063 252 GLU CCC N   
9321  C CA  . GLU C 252 ? 0.349 0.672 0.335 -0.049 0.014  -0.067 252 GLU CCC CA  
9322  C C   . GLU C 252 ? 0.344 0.661 0.336 -0.043 0.014  -0.072 252 GLU CCC C   
9323  O O   . GLU C 252 ? 0.294 0.621 0.292 -0.044 0.017  -0.081 252 GLU CCC O   
9324  C CB  . GLU C 252 ? 0.412 0.734 0.389 -0.055 0.011  -0.059 252 GLU CCC CB  
9325  C CG  . GLU C 252 ? 0.480 0.812 0.456 -0.061 0.011  -0.062 252 GLU CCC CG  
9326  C CD  . GLU C 252 ? 0.503 0.829 0.473 -0.063 0.008  -0.055 252 GLU CCC CD  
9327  O OE1 . GLU C 252 ? 0.562 0.897 0.527 -0.071 0.007  -0.053 252 GLU CCC OE1 
9328  O OE2 . GLU C 252 ? 0.611 0.923 0.582 -0.056 0.006  -0.051 252 GLU CCC OE2 
9329  N N   . TYR C 253 ? 0.323 0.625 0.315 -0.036 0.012  -0.067 253 TYR CCC N   
9330  C CA  . TYR C 253 ? 0.307 0.603 0.304 -0.030 0.012  -0.071 253 TYR CCC CA  
9331  C C   . TYR C 253 ? 0.297 0.596 0.304 -0.026 0.014  -0.079 253 TYR CCC C   
9332  O O   . TYR C 253 ? 0.304 0.607 0.318 -0.025 0.015  -0.086 253 TYR CCC O   
9333  C CB  . TYR C 253 ? 0.306 0.588 0.300 -0.024 0.010  -0.063 253 TYR CCC CB  
9334  C CG  . TYR C 253 ? 0.283 0.558 0.281 -0.018 0.009  -0.066 253 TYR CCC CG  
9335  C CD1 . TYR C 253 ? 0.278 0.548 0.283 -0.012 0.010  -0.069 253 TYR CCC CD1 
9336  C CD2 . TYR C 253 ? 0.278 0.553 0.275 -0.020 0.009  -0.067 253 TYR CCC CD2 
9337  C CE1 . TYR C 253 ? 0.290 0.554 0.299 -0.007 0.009  -0.071 253 TYR CCC CE1 
9338  C CE2 . TYR C 253 ? 0.269 0.539 0.270 -0.015 0.008  -0.069 253 TYR CCC CE2 
9339  C CZ  . TYR C 253 ? 0.295 0.559 0.302 -0.008 0.008  -0.071 253 TYR CCC CZ  
9340  O OH  . TYR C 253 ? 0.308 0.566 0.319 -0.004 0.007  -0.073 253 TYR CCC OH  
9341  N N   . MET C 254 ? 0.296 0.591 0.304 -0.023 0.014  -0.077 254 MET CCC N   
9342  C CA  . MET C 254 ? 0.315 0.611 0.333 -0.019 0.015  -0.084 254 MET CCC CA  
9343  C C   . MET C 254 ? 0.316 0.628 0.341 -0.024 0.018  -0.094 254 MET CCC C   
9344  O O   . MET C 254 ? 0.308 0.620 0.343 -0.021 0.018  -0.102 254 MET CCC O   
9345  C CB  . MET C 254 ? 0.322 0.614 0.340 -0.017 0.015  -0.080 254 MET CCC CB  
9346  C CG  . MET C 254 ? 0.316 0.594 0.329 -0.012 0.013  -0.071 254 MET CCC CG  
9347  S SD  . MET C 254 ? 0.316 0.589 0.330 -0.008 0.012  -0.067 254 MET CCC SD  
9348  C CE  . MET C 254 ? 0.324 0.600 0.351 -0.006 0.013  -0.076 254 MET CCC CE  
9349  N N   . LYS C 255 ? 0.319 0.641 0.339 -0.032 0.019  -0.095 255 LYS CCC N   
9350  C CA  . LYS C 255 ? 0.334 0.674 0.359 -0.037 0.021  -0.105 255 LYS CCC CA  
9351  C C   . LYS C 255 ? 0.306 0.650 0.335 -0.038 0.022  -0.111 255 LYS CCC C   
9352  O O   . LYS C 255 ? 0.250 0.602 0.290 -0.037 0.023  -0.121 255 LYS CCC O   
9353  C CB  . LYS C 255 ? 0.393 0.745 0.410 -0.046 0.023  -0.102 255 LYS CCC CB  
9354  C CG  . LYS C 255 ? 0.438 0.795 0.455 -0.048 0.023  -0.103 255 LYS CCC CG  
9355  C CD  . LYS C 255 ? 0.489 0.856 0.497 -0.057 0.024  -0.099 255 LYS CCC CD  
9356  C CE  . LYS C 255 ? 0.549 0.924 0.558 -0.060 0.025  -0.101 255 LYS CCC CE  
9357  N NZ  . LYS C 255 ? 0.569 0.961 0.573 -0.071 0.027  -0.103 255 LYS CCC NZ  
9358  N N   . ALA C 256 ? 0.301 0.639 0.322 -0.039 0.021  -0.104 256 ALA CCC N   
9359  C CA  . ALA C 256 ? 0.284 0.626 0.307 -0.040 0.021  -0.108 256 ALA CCC CA  
9360  C C   . ALA C 256 ? 0.278 0.610 0.311 -0.032 0.020  -0.112 256 ALA CCC C   
9361  O O   . ALA C 256 ? 0.309 0.647 0.347 -0.032 0.020  -0.119 256 ALA CCC O   
9362  C CB  . ALA C 256 ? 0.279 0.616 0.292 -0.042 0.019  -0.099 256 ALA CCC CB  
9363  N N   . THR C 257 ? 0.244 0.565 0.280 -0.025 0.018  -0.109 257 THR CCC N   
9364  C CA  . THR C 257 ? 0.255 0.567 0.300 -0.018 0.017  -0.112 257 THR CCC CA  
9365  C C   . THR C 257 ? 0.257 0.573 0.314 -0.015 0.017  -0.120 257 THR CCC C   
9366  O O   . THR C 257 ? 0.252 0.560 0.317 -0.010 0.015  -0.121 257 THR CCC O   
9367  C CB  . THR C 257 ? 0.259 0.555 0.299 -0.012 0.014  -0.102 257 THR CCC CB  
9368  O OG1 . THR C 257 ? 0.247 0.537 0.282 -0.011 0.014  -0.096 257 THR CCC OG1 
9369  C CG2 . THR C 257 ? 0.256 0.547 0.287 -0.013 0.013  -0.096 257 THR CCC CG2 
9370  N N   . GLY C 258 ? 0.304 0.631 0.363 -0.020 0.018  -0.124 258 GLY CCC N   
9371  C CA  . GLY C 258 ? 0.330 0.663 0.401 -0.019 0.019  -0.134 258 GLY CCC CA  
9372  C C   . GLY C 258 ? 0.342 0.673 0.414 -0.017 0.018  -0.131 258 GLY CCC C   
9373  O O   . GLY C 258 ? 0.337 0.673 0.421 -0.016 0.018  -0.139 258 GLY CCC O   
9374  N N   . THR C 259 ? 0.337 0.660 0.398 -0.017 0.018  -0.121 259 THR CCC N   
9375  C CA  . THR C 259 ? 0.339 0.660 0.400 -0.017 0.018  -0.118 259 THR CCC CA  
9376  C C   . THR C 259 ? 0.357 0.694 0.416 -0.024 0.021  -0.123 259 THR CCC C   
9377  O O   . THR C 259 ? 0.359 0.703 0.409 -0.030 0.022  -0.121 259 THR CCC O   
9378  C CB  . THR C 259 ? 0.321 0.629 0.372 -0.014 0.017  -0.106 259 THR CCC CB  
9379  O OG1 . THR C 259 ? 0.307 0.603 0.361 -0.008 0.014  -0.103 259 THR CCC OG1 
9380  C CG2 . THR C 259 ? 0.316 0.622 0.370 -0.012 0.016  -0.104 259 THR CCC CG2 
9381  N N   . LYS C 260 ? 0.380 0.724 0.448 -0.024 0.021  -0.130 260 LYS CCC N   
9382  C CA  . LYS C 260 ? 0.387 0.747 0.454 -0.031 0.024  -0.136 260 LYS CCC CA  
9383  C C   . LYS C 260 ? 0.396 0.751 0.455 -0.031 0.023  -0.127 260 LYS CCC C   
9384  O O   . LYS C 260 ? 0.410 0.752 0.472 -0.025 0.021  -0.123 260 LYS CCC O   
9385  C CB  . LYS C 260 ? 0.402 0.773 0.484 -0.030 0.024  -0.149 260 LYS CCC CB  
9386  C CG  . LYS C 260 ? 0.410 0.790 0.500 -0.031 0.025  -0.159 260 LYS CCC CG  
9387  C CD  . LYS C 260 ? 0.423 0.809 0.530 -0.029 0.024  -0.173 260 LYS CCC CD  
9388  C CE  . LYS C 260 ? 0.435 0.805 0.551 -0.020 0.019  -0.171 260 LYS CCC CE  
9389  N NZ  . LYS C 260 ? 0.437 0.813 0.572 -0.018 0.018  -0.183 260 LYS CCC NZ  
9390  N N   . PHE C 261 ? 0.386 0.750 0.436 -0.038 0.025  -0.125 261 PHE CCC N   
9391  C CA  . PHE C 261 ? 0.388 0.748 0.430 -0.040 0.025  -0.116 261 PHE CCC CA  
9392  C C   . PHE C 261 ? 0.373 0.749 0.416 -0.046 0.027  -0.123 261 PHE CCC C   
9393  O O   . PHE C 261 ? 0.350 0.741 0.390 -0.053 0.029  -0.127 261 PHE CCC O   
9394  C CB  . PHE C 261 ? 0.359 0.715 0.387 -0.043 0.024  -0.106 261 PHE CCC CB  
9395  C CG  . PHE C 261 ? 0.350 0.689 0.376 -0.037 0.022  -0.098 261 PHE CCC CG  
9396  C CD1 . PHE C 261 ? 0.331 0.667 0.358 -0.035 0.022  -0.100 261 PHE CCC CD1 
9397  C CD2 . PHE C 261 ? 0.326 0.653 0.347 -0.033 0.020  -0.089 261 PHE CCC CD2 
9398  C CE1 . PHE C 261 ? 0.294 0.616 0.319 -0.029 0.020  -0.093 261 PHE CCC CE1 
9399  C CE2 . PHE C 261 ? 0.316 0.629 0.336 -0.027 0.019  -0.083 261 PHE CCC CE2 
9400  C CZ  . PHE C 261 ? 0.311 0.621 0.331 -0.025 0.018  -0.084 261 PHE CCC CZ  
9401  N N   . LEU C 262 ? 0.387 0.761 0.435 -0.043 0.027  -0.124 262 LEU CCC N   
9402  C CA  . LEU C 262 ? 0.400 0.787 0.449 -0.048 0.028  -0.128 262 LEU CCC CA  
9403  C C   . LEU C 262 ? 0.384 0.765 0.421 -0.051 0.027  -0.116 262 LEU CCC C   
9404  O O   . LEU C 262 ? 0.339 0.707 0.376 -0.045 0.026  -0.110 262 LEU CCC O   
9405  C CB  . LEU C 262 ? 0.428 0.813 0.490 -0.043 0.027  -0.135 262 LEU CCC CB  
9406  C CG  . LEU C 262 ? 0.461 0.847 0.537 -0.039 0.026  -0.146 262 LEU CCC CG  
9407  C CD1 . LEU C 262 ? 0.475 0.859 0.564 -0.034 0.025  -0.152 262 LEU CCC CD1 
9408  C CD2 . LEU C 262 ? 0.459 0.864 0.539 -0.044 0.029  -0.157 262 LEU CCC CD2 
9409  N N   . VAL C 263 ? 0.407 0.798 0.434 -0.059 0.029  -0.114 263 VAL CCC N   
9410  C CA  . VAL C 263 ? 0.446 0.831 0.461 -0.062 0.027  -0.102 263 VAL CCC CA  
9411  C C   . VAL C 263 ? 0.461 0.855 0.476 -0.066 0.028  -0.104 263 VAL CCC C   
9412  O O   . VAL C 263 ? 0.455 0.865 0.473 -0.071 0.030  -0.112 263 VAL CCC O   
9413  C CB  . VAL C 263 ? 0.447 0.837 0.452 -0.068 0.027  -0.097 263 VAL CCC CB  
9414  C CG1 . VAL C 263 ? 0.467 0.850 0.462 -0.071 0.024  -0.084 263 VAL CCC CG1 
9415  C CG2 . VAL C 263 ? 0.440 0.822 0.447 -0.064 0.026  -0.097 263 VAL CCC CG2 
9416  N N   . GLY C 264 ? 0.514 0.898 0.526 -0.063 0.026  -0.096 264 GLY CCC N   
9417  C CA  . GLY C 264 ? 0.489 0.879 0.499 -0.066 0.027  -0.095 264 GLY CCC CA  
9418  C C   . GLY C 264 ? 0.494 0.888 0.516 -0.063 0.028  -0.105 264 GLY CCC C   
9419  O O   . GLY C 264 ? 0.475 0.880 0.497 -0.068 0.029  -0.108 264 GLY CCC O   
9420  N N   . VAL C 265 ? 0.476 0.862 0.508 -0.056 0.028  -0.109 265 VAL CCC N   
9421  C CA  . VAL C 265 ? 0.519 0.909 0.564 -0.052 0.028  -0.119 265 VAL CCC CA  
9422  C C   . VAL C 265 ? 0.565 0.938 0.615 -0.043 0.025  -0.115 265 VAL CCC C   
9423  O O   . VAL C 265 ? 0.686 1.047 0.734 -0.039 0.024  -0.108 265 VAL CCC O   
9424  C CB  . VAL C 265 ? 0.594 0.995 0.648 -0.053 0.029  -0.131 265 VAL CCC CB  
9425  C CG1 . VAL C 265 ? 0.632 1.034 0.702 -0.048 0.028  -0.142 265 VAL CCC CG1 
9426  C CG2 . VAL C 265 ? 0.569 0.990 0.618 -0.062 0.032  -0.137 265 VAL CCC CG2 
9427  N N   . VAL C 266 ? 0.532 0.904 0.590 -0.041 0.025  -0.117 266 VAL CCC N   
9428  C CA  . VAL C 266 ? 0.532 0.889 0.596 -0.033 0.022  -0.114 266 VAL CCC CA  
9429  C C   . VAL C 266 ? 0.511 0.874 0.591 -0.031 0.021  -0.125 266 VAL CCC C   
9430  O O   . VAL C 266 ? 0.483 0.859 0.567 -0.035 0.023  -0.134 266 VAL CCC O   
9431  C CB  . VAL C 266 ? 0.562 0.910 0.619 -0.031 0.021  -0.103 266 VAL CCC CB  
9432  C CG1 . VAL C 266 ? 0.614 0.957 0.657 -0.033 0.022  -0.093 266 VAL CCC CG1 
9433  C CG2 . VAL C 266 ? 0.554 0.910 0.611 -0.035 0.022  -0.105 266 VAL CCC CG2 
9434  N N   . PRO C 267 ? 0.489 0.841 0.578 -0.024 0.018  -0.125 267 PRO CCC N   
9435  C CA  . PRO C 267 ? 0.467 0.821 0.572 -0.021 0.016  -0.133 267 PRO CCC CA  
9436  C C   . PRO C 267 ? 0.472 0.828 0.578 -0.023 0.016  -0.132 267 PRO CCC C   
9437  O O   . PRO C 267 ? 0.409 0.758 0.505 -0.022 0.016  -0.121 267 PRO CCC O   
9438  C CB  . PRO C 267 ? 0.481 0.821 0.593 -0.015 0.013  -0.129 267 PRO CCC CB  
9439  C CG  . PRO C 267 ? 0.463 0.796 0.565 -0.014 0.013  -0.121 267 PRO CCC CG  
9440  C CD  . PRO C 267 ? 0.473 0.811 0.560 -0.019 0.017  -0.116 267 PRO CCC CD  
9441  N N   . ILE C 268 ? 0.445 0.813 0.562 -0.024 0.016  -0.143 268 ILE CCC N   
9442  C CA  . ILE C 268 ? 0.448 0.818 0.569 -0.024 0.015  -0.144 268 ILE CCC CA  
9443  C C   . ILE C 268 ? 0.446 0.812 0.584 -0.019 0.011  -0.150 268 ILE CCC C   
9444  O O   . ILE C 268 ? 0.471 0.834 0.613 -0.018 0.010  -0.149 268 ILE CCC O   
9445  C CB  . ILE C 268 ? 0.459 0.846 0.576 -0.031 0.019  -0.151 268 ILE CCC CB  
9446  C CG1 . ILE C 268 ? 0.447 0.849 0.575 -0.033 0.019  -0.167 268 ILE CCC CG1 
9447  C CG2 . ILE C 268 ? 0.456 0.845 0.555 -0.037 0.022  -0.142 268 ILE CCC CG2 
9448  C CD1 . ILE C 268 ? 0.477 0.898 0.603 -0.040 0.023  -0.175 268 ILE CCC CD1 
9449  N N   . ASN C 269 ? 0.435 0.799 0.584 -0.016 0.009  -0.157 269 ASN CCC N   
9450  C CA  . ASN C 269 ? 0.460 0.819 0.628 -0.011 0.004  -0.162 269 ASN CCC CA  
9451  C C   . ASN C 269 ? 0.446 0.798 0.621 -0.008 0.001  -0.163 269 ASN CCC C   
9452  O O   . ASN C 269 ? 0.471 0.829 0.643 -0.009 0.003  -0.167 269 ASN CCC O   
9453  C CB  . ASN C 269 ? 0.477 0.851 0.660 -0.013 0.003  -0.178 269 ASN CCC CB  
9454  C CG  . ASN C 269 ? 0.495 0.862 0.697 -0.008 -0.003 -0.181 269 ASN CCC CG  
9455  O OD1 . ASN C 269 ? 0.493 0.850 0.695 -0.006 -0.005 -0.172 269 ASN CCC OD1 
9456  N ND2 . ASN C 269 ? 0.484 0.857 0.704 -0.006 -0.006 -0.195 269 ASN CCC ND2 
9457  N N   . ILE C 270 ? 0.439 0.778 0.624 -0.003 -0.004 -0.159 270 ILE CCC N   
9458  C CA  . ILE C 270 ? 0.484 0.814 0.675 0.001  -0.008 -0.157 270 ILE CCC CA  
9459  C C   . ILE C 270 ? 0.538 0.865 0.751 0.005  -0.015 -0.163 270 ILE CCC C   
9460  O O   . ILE C 270 ? 0.527 0.845 0.742 0.006  -0.018 -0.156 270 ILE CCC O   
9461  C CB  . ILE C 270 ? 0.467 0.784 0.644 0.003  -0.008 -0.141 270 ILE CCC CB  
9462  C CG1 . ILE C 270 ? 0.449 0.770 0.608 -0.001 -0.002 -0.138 270 ILE CCC CG1 
9463  C CG2 . ILE C 270 ? 0.474 0.780 0.660 0.007  -0.012 -0.138 270 ILE CCC CG2 
9464  C CD1 . ILE C 270 ? 0.436 0.745 0.580 0.001  -0.001 -0.123 270 ILE CCC CD1 
9465  N N   . GLU C 271 ? 0.619 0.951 0.847 0.006  -0.017 -0.175 271 GLU CCC N   
9466  C CA  . GLU C 271 ? 0.677 1.008 0.928 0.009  -0.024 -0.183 271 GLU CCC CA  
9467  C C   . GLU C 271 ? 0.707 1.032 0.968 0.012  -0.029 -0.186 271 GLU CCC C   
9468  O O   . GLU C 271 ? 0.609 0.939 0.864 0.011  -0.025 -0.189 271 GLU CCC O   
9469  C CB  . GLU C 271 ? 0.736 1.082 1.000 0.008  -0.024 -0.199 271 GLU CCC CB  
9470  C CG  . GLU C 271 ? 0.791 1.153 1.046 0.003  -0.017 -0.208 271 GLU CCC CG  
9471  C CD  . GLU C 271 ? 0.788 1.168 1.055 0.001  -0.016 -0.224 271 GLU CCC CD  
9472  O OE1 . GLU C 271 ? 0.744 1.124 1.032 0.004  -0.022 -0.234 271 GLU CCC OE1 
9473  O OE2 . GLU C 271 ? 0.812 1.205 1.068 -0.004 -0.010 -0.228 271 GLU CCC OE2 
9474  N N   . LYS C 272 ? 0.773 1.087 1.050 0.016  -0.037 -0.185 272 LYS CCC N   
9475  C CA  . LYS C 272 ? 0.812 1.122 1.105 0.019  -0.043 -0.189 272 LYS CCC CA  
9476  C C   . LYS C 272 ? 0.841 1.164 1.155 0.020  -0.045 -0.208 272 LYS CCC C   
9477  O O   . LYS C 272 ? 0.839 1.163 1.167 0.021  -0.049 -0.215 272 LYS CCC O   
9478  C CB  . LYS C 272 ? 0.851 1.146 1.153 0.022  -0.051 -0.179 272 LYS CCC CB  
9479  C CG  . LYS C 272 ? 0.919 1.205 1.231 0.025  -0.057 -0.178 272 LYS CCC CG  
9480  C CD  . LYS C 272 ? 0.954 1.226 1.259 0.026  -0.060 -0.162 272 LYS CCC CD  
9481  C CE  . LYS C 272 ? 0.976 1.241 1.289 0.028  -0.065 -0.162 272 LYS CCC CE  
9482  N NZ  . LYS C 272 ? 0.964 1.216 1.267 0.028  -0.068 -0.145 272 LYS CCC NZ  
9483  N N   . VAL C 273 ? 0.885 1.217 1.199 0.019  -0.042 -0.218 273 VAL CCC N   
9484  C CA  . VAL C 273 ? 0.950 1.294 1.284 0.020  -0.044 -0.237 273 VAL CCC CA  
9485  C C   . VAL C 273 ? 0.994 1.330 1.341 0.023  -0.050 -0.238 273 VAL CCC C   
9486  O O   . VAL C 273 ? 0.903 1.241 1.243 0.023  -0.047 -0.238 273 VAL CCC O   
9487  C CB  . VAL C 273 ? 0.931 1.295 1.257 0.015  -0.035 -0.247 273 VAL CCC CB  
9488  C CG1 . VAL C 273 ? 0.910 1.287 1.256 0.016  -0.037 -0.267 273 VAL CCC CG1 
9489  C CG2 . VAL C 273 ? 0.934 1.306 1.250 0.012  -0.030 -0.247 273 VAL CCC CG2 
9490  N N   . ASN C 274 ? 1.023 1.350 1.391 0.027  -0.060 -0.239 274 ASN CCC N   
9491  C CA  . ASN C 274 ? 1.016 1.332 1.398 0.030  -0.068 -0.238 274 ASN CCC CA  
9492  C C   . ASN C 274 ? 0.931 1.233 1.295 0.030  -0.067 -0.219 274 ASN CCC C   
9493  O O   . ASN C 274 ? 0.960 1.252 1.315 0.030  -0.068 -0.206 274 ASN CCC O   
9494  C CB  . ASN C 274 ? 1.051 1.379 1.447 0.031  -0.068 -0.255 274 ASN CCC CB  
9495  C CG  . ASN C 274 ? 1.059 1.401 1.476 0.032  -0.070 -0.274 274 ASN CCC CG  
9496  O OD1 . ASN C 274 ? 1.069 1.428 1.483 0.029  -0.063 -0.287 274 ASN CCC OD1 
9497  N ND2 . ASN C 274 ? 1.030 1.366 1.468 0.035  -0.079 -0.277 274 ASN CCC ND2 
9498  N N   . GLU C 275 ? 0.845 1.146 1.204 0.031  -0.065 -0.218 275 GLU CCC N   
9499  C CA  . GLU C 275 ? 0.774 1.062 1.117 0.031  -0.065 -0.202 275 GLU CCC CA  
9500  C C   . GLU C 275 ? 0.694 0.986 1.010 0.028  -0.054 -0.196 275 GLU CCC C   
9501  O O   . GLU C 275 ? 0.686 0.969 0.987 0.028  -0.053 -0.181 275 GLU CCC O   
9502  C CB  . GLU C 275 ? 0.761 1.043 1.114 0.033  -0.070 -0.204 275 GLU CCC CB  
9503  C CG  . GLU C 275 ? 0.746 1.040 1.099 0.033  -0.065 -0.217 275 GLU CCC CG  
9504  C CD  . GLU C 275 ? 0.725 1.033 1.102 0.034  -0.068 -0.237 275 GLU CCC CD  
9505  O OE1 . GLU C 275 ? 0.699 1.004 1.095 0.036  -0.075 -0.242 275 GLU CCC OE1 
9506  O OE2 . GLU C 275 ? 0.681 1.000 1.057 0.033  -0.063 -0.248 275 GLU CCC OE2 
9507  N N   . ASN C 276 ? 0.613 0.920 0.925 0.025  -0.048 -0.206 276 ASN CCC N   
9508  C CA  . ASN C 276 ? 0.542 0.855 0.830 0.021  -0.038 -0.201 276 ASN CCC CA  
9509  C C   . ASN C 276 ? 0.503 0.817 0.780 0.019  -0.035 -0.194 276 ASN CCC C   
9510  O O   . ASN C 276 ? 0.485 0.797 0.773 0.020  -0.039 -0.196 276 ASN CCC O   
9511  C CB  . ASN C 276 ? 0.517 0.847 0.806 0.019  -0.033 -0.215 276 ASN CCC CB  
9512  C CG  . ASN C 276 ? 0.545 0.874 0.839 0.020  -0.035 -0.220 276 ASN CCC CG  
9513  O OD1 . ASN C 276 ? 0.482 0.799 0.771 0.022  -0.036 -0.209 276 ASN CCC OD1 
9514  N ND2 . ASN C 276 ? 0.537 0.881 0.844 0.020  -0.033 -0.236 276 ASN CCC ND2 
9515  N N   . ILE C 277 ? 0.476 0.791 0.730 0.016  -0.028 -0.186 277 ILE CCC N   
9516  C CA  . ILE C 277 ? 0.481 0.799 0.723 0.013  -0.024 -0.181 277 ILE CCC CA  
9517  C C   . ILE C 277 ? 0.458 0.794 0.693 0.009  -0.017 -0.190 277 ILE CCC C   
9518  O O   . ILE C 277 ? 0.411 0.749 0.633 0.007  -0.012 -0.188 277 ILE CCC O   
9519  C CB  . ILE C 277 ? 0.506 0.813 0.730 0.014  -0.022 -0.163 277 ILE CCC CB  
9520  C CG1 . ILE C 277 ? 0.506 0.798 0.738 0.017  -0.029 -0.155 277 ILE CCC CG1 
9521  C CG2 . ILE C 277 ? 0.481 0.792 0.691 0.011  -0.017 -0.158 277 ILE CCC CG2 
9522  C CD1 . ILE C 277 ? 0.504 0.784 0.720 0.018  -0.028 -0.140 277 ILE CCC CD1 
9523  N N   . LYS C 278 ? 0.449 0.796 0.693 0.007  -0.016 -0.201 278 LYS CCC N   
9524  C CA  . LYS C 278 ? 0.446 0.810 0.683 0.002  -0.010 -0.209 278 LYS CCC CA  
9525  C C   . LYS C 278 ? 0.431 0.792 0.647 -0.001 -0.006 -0.196 278 LYS CCC C   
9526  O O   . LYS C 278 ? 0.426 0.781 0.644 0.000  -0.008 -0.191 278 LYS CCC O   
9527  C CB  . LYS C 278 ? 0.485 0.862 0.740 0.002  -0.012 -0.224 278 LYS CCC CB  
9528  C CG  . LYS C 278 ? 0.499 0.896 0.750 -0.004 -0.006 -0.236 278 LYS CCC CG  
9529  C CD  . LYS C 278 ? 0.531 0.940 0.799 -0.004 -0.008 -0.249 278 LYS CCC CD  
9530  C CE  . LYS C 278 ? 0.562 0.993 0.826 -0.010 -0.002 -0.261 278 LYS CCC CE  
9531  N NZ  . LYS C 278 ? 0.559 1.002 0.841 -0.010 -0.004 -0.276 278 LYS CCC NZ  
9532  N N   . VAL C 279 ? 0.398 0.764 0.598 -0.005 -0.000 -0.192 279 VAL CCC N   
9533  C CA  . VAL C 279 ? 0.366 0.730 0.546 -0.008 0.004  -0.181 279 VAL CCC CA  
9534  C C   . VAL C 279 ? 0.367 0.749 0.543 -0.014 0.008  -0.189 279 VAL CCC C   
9535  O O   . VAL C 279 ? 0.326 0.720 0.502 -0.017 0.011  -0.198 279 VAL CCC O   
9536  C CB  . VAL C 279 ? 0.356 0.710 0.520 -0.008 0.005  -0.168 279 VAL CCC CB  
9537  C CG1 . VAL C 279 ? 0.365 0.720 0.510 -0.012 0.009  -0.159 279 VAL CCC CG1 
9538  C CG2 . VAL C 279 ? 0.350 0.687 0.518 -0.002 0.001  -0.159 279 VAL CCC CG2 
9539  N N   . SER C 280 ? 0.393 0.778 0.565 -0.017 0.009  -0.187 280 SER CCC N   
9540  C CA  . SER C 280 ? 0.408 0.811 0.575 -0.023 0.014  -0.193 280 SER CCC CA  
9541  C C   . SER C 280 ? 0.383 0.783 0.529 -0.027 0.017  -0.180 280 SER CCC C   
9542  O O   . SER C 280 ? 0.359 0.745 0.498 -0.024 0.016  -0.169 280 SER CCC O   
9543  C CB  . SER C 280 ? 0.385 0.795 0.562 -0.023 0.012  -0.201 280 SER CCC CB  
9544  O OG  . SER C 280 ? 0.385 0.799 0.583 -0.020 0.009  -0.215 280 SER CCC OG  
9545  N N   . PHE C 281 ? 0.389 0.799 0.524 -0.033 0.021  -0.182 281 PHE CCC N   
9546  C CA  . PHE C 281 ? 0.408 0.816 0.524 -0.037 0.024  -0.169 281 PHE CCC CA  
9547  C C   . PHE C 281 ? 0.442 0.862 0.550 -0.044 0.026  -0.170 281 PHE CCC C   
9548  O O   . PHE C 281 ? 0.418 0.854 0.534 -0.047 0.027  -0.182 281 PHE CCC O   
9549  C CB  . PHE C 281 ? 0.424 0.835 0.534 -0.039 0.025  -0.169 281 PHE CCC CB  
9550  C CG  . PHE C 281 ? 0.429 0.826 0.542 -0.033 0.023  -0.165 281 PHE CCC CG  
9551  C CD1 . PHE C 281 ? 0.431 0.811 0.534 -0.030 0.022  -0.151 281 PHE CCC CD1 
9552  C CD2 . PHE C 281 ? 0.438 0.838 0.565 -0.030 0.021  -0.176 281 PHE CCC CD2 
9553  C CE1 . PHE C 281 ? 0.435 0.803 0.541 -0.025 0.019  -0.148 281 PHE CCC CE1 
9554  C CE2 . PHE C 281 ? 0.448 0.834 0.578 -0.025 0.019  -0.172 281 PHE CCC CE2 
9555  C CZ  . PHE C 281 ? 0.438 0.809 0.557 -0.022 0.018  -0.158 281 PHE CCC CZ  
9556  N N   . SER C 282 ? 0.468 0.881 0.561 -0.046 0.027  -0.157 282 SER CCC N   
9557  C CA  . SER C 282 ? 0.473 0.894 0.556 -0.052 0.029  -0.153 282 SER CCC CA  
9558  C C   . SER C 282 ? 0.460 0.903 0.540 -0.061 0.032  -0.161 282 SER CCC C   
9559  O O   . SER C 282 ? 0.444 0.897 0.519 -0.066 0.033  -0.162 282 SER CCC O   
9560  C CB  . SER C 282 ? 0.495 0.903 0.564 -0.052 0.028  -0.138 282 SER CCC CB  
9561  O OG  . SER C 282 ? 0.485 0.894 0.544 -0.055 0.029  -0.133 282 SER CCC OG  
9562  N N   . ASP C 283 ? 0.452 0.901 0.533 -0.062 0.033  -0.167 283 ASP CCC N   
9563  C CA  . ASP C 283 ? 0.446 0.916 0.524 -0.071 0.036  -0.175 283 ASP CCC CA  
9564  C C   . ASP C 283 ? 0.424 0.910 0.518 -0.071 0.037  -0.193 283 ASP CCC C   
9565  O O   . ASP C 283 ? 0.404 0.909 0.498 -0.077 0.039  -0.202 283 ASP CCC O   
9566  C CB  . ASP C 283 ? 0.451 0.921 0.520 -0.074 0.037  -0.170 283 ASP CCC CB  
9567  C CG  . ASP C 283 ? 0.443 0.908 0.522 -0.068 0.036  -0.176 283 ASP CCC CG  
9568  O OD1 . ASP C 283 ? 0.414 0.870 0.507 -0.060 0.034  -0.181 283 ASP CCC OD1 
9569  O OD2 . ASP C 283 ? 0.493 0.962 0.567 -0.071 0.037  -0.176 283 ASP CCC OD2 
9570  N N   . GLY C 284 ? 0.430 0.909 0.539 -0.064 0.034  -0.198 284 GLY CCC N   
9571  C CA  . GLY C 284 ? 0.451 0.942 0.578 -0.062 0.034  -0.216 284 GLY CCC CA  
9572  C C   . GLY C 284 ? 0.490 0.982 0.628 -0.058 0.033  -0.224 284 GLY CCC C   
9573  O O   . GLY C 284 ? 0.503 1.006 0.656 -0.057 0.033  -0.239 284 GLY CCC O   
9574  N N   . SER C 285 ? 0.477 0.956 0.606 -0.056 0.033  -0.214 285 SER CCC N   
9575  C CA  . SER C 285 ? 0.472 0.949 0.612 -0.052 0.031  -0.221 285 SER CCC CA  
9576  C C   . SER C 285 ? 0.457 0.915 0.609 -0.043 0.027  -0.219 285 SER CCC C   
9577  O O   . SER C 285 ? 0.480 0.925 0.629 -0.040 0.025  -0.209 285 SER CCC O   
9578  C CB  . SER C 285 ? 0.454 0.927 0.581 -0.054 0.033  -0.212 285 SER CCC CB  
9579  O OG  . SER C 285 ? 0.457 0.909 0.574 -0.050 0.031  -0.197 285 SER CCC OG  
9580  N N   . VAL C 286 ? 0.455 0.913 0.622 -0.038 0.024  -0.229 286 VAL CCC N   
9581  C CA  . VAL C 286 ? 0.456 0.899 0.638 -0.030 0.019  -0.228 286 VAL CCC CA  
9582  C C   . VAL C 286 ? 0.441 0.876 0.625 -0.027 0.018  -0.227 286 VAL CCC C   
9583  O O   . VAL C 286 ? 0.424 0.872 0.606 -0.031 0.021  -0.234 286 VAL CCC O   
9584  C CB  . VAL C 286 ? 0.503 0.955 0.706 -0.028 0.017  -0.244 286 VAL CCC CB  
9585  C CG1 . VAL C 286 ? 0.521 0.961 0.743 -0.020 0.010  -0.247 286 VAL CCC CG1 
9586  C CG2 . VAL C 286 ? 0.521 0.976 0.722 -0.030 0.017  -0.242 286 VAL CCC CG2 
9587  N N   . GLU C 287 ? 0.449 0.865 0.636 -0.020 0.013  -0.219 287 GLU CCC N   
9588  C CA  . GLU C 287 ? 0.474 0.881 0.666 -0.017 0.011  -0.219 287 GLU CCC CA  
9589  C C   . GLU C 287 ? 0.468 0.857 0.670 -0.009 0.005  -0.213 287 GLU CCC C   
9590  O O   . GLU C 287 ? 0.470 0.849 0.667 -0.008 0.004  -0.203 287 GLU CCC O   
9591  C CB  . GLU C 287 ? 0.511 0.915 0.684 -0.019 0.015  -0.208 287 GLU CCC CB  
9592  C CG  . GLU C 287 ? 0.552 0.955 0.729 -0.018 0.014  -0.211 287 GLU CCC CG  
9593  C CD  . GLU C 287 ? 0.571 0.970 0.730 -0.021 0.017  -0.201 287 GLU CCC CD  
9594  O OE1 . GLU C 287 ? 0.591 0.988 0.735 -0.024 0.019  -0.191 287 GLU CCC OE1 
9595  O OE2 . GLU C 287 ? 0.566 0.964 0.727 -0.019 0.016  -0.203 287 GLU CCC OE2 
9596  N N   . GLU C 288 ? 0.465 0.851 0.681 -0.005 0.001  -0.220 288 GLU CCC N   
9597  C CA  . GLU C 288 ? 0.478 0.848 0.706 0.001  -0.005 -0.215 288 GLU CCC CA  
9598  C C   . GLU C 288 ? 0.453 0.809 0.669 0.003  -0.006 -0.202 288 GLU CCC C   
9599  O O   . GLU C 288 ? 0.382 0.742 0.590 0.001  -0.002 -0.203 288 GLU CCC O   
9600  C CB  . GLU C 288 ? 0.530 0.905 0.782 0.004  -0.010 -0.230 288 GLU CCC CB  
9601  C CG  . GLU C 288 ? 0.575 0.962 0.840 0.003  -0.011 -0.242 288 GLU CCC CG  
9602  C CD  . GLU C 288 ? 0.636 1.024 0.927 0.007  -0.018 -0.255 288 GLU CCC CD  
9603  O OE1 . GLU C 288 ? 0.732 1.106 1.032 0.012  -0.023 -0.251 288 GLU CCC OE1 
9604  O OE2 . GLU C 288 ? 0.655 1.058 0.958 0.006  -0.017 -0.269 288 GLU CCC OE2 
9605  N N   . PHE C 289 ? 0.455 0.794 0.669 0.006  -0.009 -0.190 289 PHE CCC N   
9606  C CA  . PHE C 289 ? 0.451 0.776 0.655 0.009  -0.010 -0.177 289 PHE CCC CA  
9607  C C   . PHE C 289 ? 0.458 0.770 0.675 0.014  -0.018 -0.174 289 PHE CCC C   
9608  O O   . PHE C 289 ? 0.495 0.807 0.724 0.015  -0.021 -0.177 289 PHE CCC O   
9609  C CB  . PHE C 289 ? 0.414 0.734 0.598 0.007  -0.006 -0.164 289 PHE CCC CB  
9610  C CG  . PHE C 289 ? 0.392 0.724 0.563 0.002  -0.000 -0.166 289 PHE CCC CG  
9611  C CD1 . PHE C 289 ? 0.383 0.725 0.553 -0.002 0.002  -0.170 289 PHE CCC CD1 
9612  C CD2 . PHE C 289 ? 0.371 0.705 0.530 -0.001 0.003  -0.164 289 PHE CCC CD2 
9613  C CE1 . PHE C 289 ? 0.377 0.731 0.535 -0.008 0.008  -0.171 289 PHE CCC CE1 
9614  C CE2 . PHE C 289 ? 0.361 0.707 0.510 -0.006 0.008  -0.165 289 PHE CCC CE2 
9615  C CZ  . PHE C 289 ? 0.368 0.723 0.515 -0.010 0.010  -0.169 289 PHE CCC CZ  
9616  N N   . GLU C 290 ? 0.439 0.740 0.655 0.016  -0.020 -0.167 290 GLU CCC N   
9617  C CA  . GLU C 290 ? 0.432 0.720 0.657 0.020  -0.027 -0.160 290 GLU CCC CA  
9618  C C   . GLU C 290 ? 0.423 0.701 0.634 0.020  -0.026 -0.145 290 GLU CCC C   
9619  O O   . GLU C 290 ? 0.407 0.678 0.626 0.022  -0.031 -0.141 290 GLU CCC O   
9620  C CB  . GLU C 290 ? 0.490 0.772 0.719 0.022  -0.030 -0.160 290 GLU CCC CB  
9621  C CG  . GLU C 290 ? 0.568 0.839 0.810 0.026  -0.038 -0.155 290 GLU CCC CG  
9622  C CD  . GLU C 290 ? 0.618 0.884 0.867 0.028  -0.042 -0.157 290 GLU CCC CD  
9623  O OE1 . GLU C 290 ? 0.598 0.852 0.849 0.030  -0.047 -0.147 290 GLU CCC OE1 
9624  O OE2 . GLU C 290 ? 0.662 0.936 0.915 0.027  -0.039 -0.167 290 GLU CCC OE2 
9625  N N   . THR C 291 ? 0.373 0.652 0.565 0.018  -0.021 -0.138 291 THR CCC N   
9626  C CA  . THR C 291 ? 0.357 0.628 0.535 0.018  -0.019 -0.124 291 THR CCC CA  
9627  C C   . THR C 291 ? 0.333 0.611 0.496 0.015  -0.013 -0.123 291 THR CCC C   
9628  O O   . THR C 291 ? 0.298 0.583 0.455 0.012  -0.009 -0.128 291 THR CCC O   
9629  C CB  . THR C 291 ? 0.368 0.629 0.537 0.020  -0.020 -0.115 291 THR CCC CB  
9630  O OG1 . THR C 291 ? 0.377 0.632 0.559 0.023  -0.026 -0.116 291 THR CCC OG1 
9631  C CG2 . THR C 291 ? 0.349 0.602 0.504 0.021  -0.019 -0.102 291 THR CCC CG2 
9632  N N   . VAL C 292 ? 0.316 0.591 0.475 0.015  -0.013 -0.116 292 VAL CCC N   
9633  C CA  . VAL C 292 ? 0.328 0.608 0.472 0.012  -0.008 -0.113 292 VAL CCC CA  
9634  C C   . VAL C 292 ? 0.326 0.595 0.458 0.013  -0.008 -0.099 292 VAL CCC C   
9635  O O   . VAL C 292 ? 0.309 0.572 0.446 0.015  -0.011 -0.094 292 VAL CCC O   
9636  C CB  . VAL C 292 ? 0.320 0.608 0.469 0.009  -0.007 -0.119 292 VAL CCC CB  
9637  C CG1 . VAL C 292 ? 0.337 0.629 0.472 0.006  -0.002 -0.114 292 VAL CCC CG1 
9638  C CG2 . VAL C 292 ? 0.311 0.610 0.473 0.008  -0.007 -0.133 292 VAL CCC CG2 
9639  N N   . LEU C 293 ? 0.325 0.594 0.442 0.012  -0.004 -0.094 293 LEU CCC N   
9640  C CA  . LEU C 293 ? 0.333 0.594 0.438 0.013  -0.003 -0.082 293 LEU CCC CA  
9641  C C   . LEU C 293 ? 0.317 0.582 0.411 0.010  0.001  -0.079 293 LEU CCC C   
9642  O O   . LEU C 293 ? 0.290 0.561 0.377 0.008  0.004  -0.082 293 LEU CCC O   
9643  C CB  . LEU C 293 ? 0.354 0.610 0.453 0.015  -0.003 -0.079 293 LEU CCC CB  
9644  C CG  . LEU C 293 ? 0.383 0.631 0.473 0.017  -0.004 -0.068 293 LEU CCC CG  
9645  C CD1 . LEU C 293 ? 0.386 0.628 0.477 0.019  -0.006 -0.065 293 LEU CCC CD1 
9646  C CD2 . LEU C 293 ? 0.379 0.628 0.455 0.015  0.000  -0.063 293 LEU CCC CD2 
9647  N N   . TYR C 294 ? 0.295 0.557 0.386 0.011  0.000  -0.073 294 TYR CCC N   
9648  C CA  . TYR C 294 ? 0.326 0.590 0.405 0.009  0.003  -0.068 294 TYR CCC CA  
9649  C C   . TYR C 294 ? 0.304 0.561 0.371 0.010  0.004  -0.059 294 TYR CCC C   
9650  O O   . TYR C 294 ? 0.285 0.536 0.352 0.013  0.002  -0.053 294 TYR CCC O   
9651  C CB  . TYR C 294 ? 0.324 0.589 0.407 0.009  0.002  -0.066 294 TYR CCC CB  
9652  C CG  . TYR C 294 ? 0.335 0.609 0.423 0.005  0.004  -0.074 294 TYR CCC CG  
9653  C CD1 . TYR C 294 ? 0.338 0.619 0.417 0.002  0.007  -0.075 294 TYR CCC CD1 
9654  C CD2 . TYR C 294 ? 0.358 0.634 0.460 0.006  0.001  -0.082 294 TYR CCC CD2 
9655  C CE1 . TYR C 294 ? 0.331 0.622 0.415 -0.002 0.008  -0.083 294 TYR CCC CE1 
9656  C CE2 . TYR C 294 ? 0.327 0.614 0.435 0.003  0.002  -0.091 294 TYR CCC CE2 
9657  C CZ  . TYR C 294 ? 0.330 0.624 0.428 -0.001 0.006  -0.091 294 TYR CCC CZ  
9658  O OH  . TYR C 294 ? 0.365 0.670 0.468 -0.004 0.007  -0.100 294 TYR CCC OH  
9659  N N   . ALA C 295 ? 0.294 0.554 0.352 0.008  0.007  -0.059 295 ALA CCC N   
9660  C CA  . ALA C 295 ? 0.305 0.560 0.352 0.009  0.007  -0.051 295 ALA CCC CA  
9661  C C   . ALA C 295 ? 0.298 0.557 0.337 0.006  0.009  -0.049 295 ALA CCC C   
9662  O O   . ALA C 295 ? 0.312 0.572 0.343 0.004  0.011  -0.047 295 ALA CCC O   
9663  C CB  . ALA C 295 ? 0.325 0.579 0.369 0.010  0.008  -0.052 295 ALA CCC CB  
9664  N N   . THR C 296 ? 0.296 0.557 0.337 0.005  0.009  -0.048 296 THR CCC N   
9665  C CA  . THR C 296 ? 0.295 0.561 0.330 0.002  0.011  -0.047 296 THR CCC CA  
9666  C C   . THR C 296 ? 0.320 0.580 0.347 0.004  0.011  -0.038 296 THR CCC C   
9667  O O   . THR C 296 ? 0.361 0.622 0.380 0.001  0.011  -0.036 296 THR CCC O   
9668  C CB  . THR C 296 ? 0.273 0.544 0.313 -0.001 0.011  -0.052 296 THR CCC CB  
9669  O OG1 . THR C 296 ? 0.258 0.526 0.307 0.003  0.010  -0.052 296 THR CCC OG1 
9670  C CG2 . THR C 296 ? 0.270 0.550 0.316 -0.004 0.012  -0.061 296 THR CCC CG2 
9671  N N   . GLY C 297 ? 0.325 0.578 0.353 0.008  0.009  -0.034 297 GLY CCC N   
9672  C CA  . GLY C 297 ? 0.316 0.565 0.338 0.010  0.009  -0.027 297 GLY CCC CA  
9673  C C   . GLY C 297 ? 0.316 0.561 0.342 0.013  0.008  -0.024 297 GLY CCC C   
9674  O O   . GLY C 297 ? 0.260 0.505 0.294 0.014  0.007  -0.027 297 GLY CCC O   
9675  N N   . ARG C 298 ? 0.338 0.581 0.360 0.015  0.008  -0.018 298 ARG CCC N   
9676  C CA  . ARG C 298 ? 0.341 0.582 0.365 0.018  0.007  -0.014 298 ARG CCC CA  
9677  C C   . ARG C 298 ? 0.365 0.606 0.386 0.018  0.007  -0.010 298 ARG CCC C   
9678  O O   . ARG C 298 ? 0.424 0.666 0.439 0.017  0.008  -0.009 298 ARG CCC O   
9679  C CB  . ARG C 298 ? 0.335 0.572 0.355 0.021  0.006  -0.011 298 ARG CCC CB  
9680  C CG  . ARG C 298 ? 0.330 0.565 0.353 0.021  0.005  -0.015 298 ARG CCC CG  
9681  C CD  . ARG C 298 ? 0.332 0.565 0.351 0.024  0.005  -0.012 298 ARG CCC CD  
9682  N NE  . ARG C 298 ? 0.329 0.560 0.347 0.026  0.004  -0.008 298 ARG CCC NE  
9683  C CZ  . ARG C 298 ? 0.342 0.572 0.366 0.027  0.002  -0.006 298 ARG CCC CZ  
9684  N NH1 . ARG C 298 ? 0.372 0.601 0.402 0.026  0.001  -0.010 298 ARG CCC NH1 
9685  N NH2 . ARG C 298 ? 0.375 0.606 0.397 0.028  0.002  -0.002 298 ARG CCC NH2 
9686  N N   . ASN C 299 ? 0.394 0.636 0.420 0.018  0.006  -0.008 299 ASN CCC N   
9687  C CA  . ASN C 299 ? 0.372 0.615 0.396 0.018  0.007  -0.004 299 ASN CCC CA  
9688  C C   . ASN C 299 ? 0.391 0.633 0.414 0.021  0.006  0.001  299 ASN CCC C   
9689  O O   . ASN C 299 ? 0.452 0.693 0.478 0.022  0.005  0.002  299 ASN CCC O   
9690  C CB  . ASN C 299 ? 0.379 0.624 0.410 0.017  0.006  -0.005 299 ASN CCC CB  
9691  C CG  . ASN C 299 ? 0.370 0.618 0.403 0.014  0.007  -0.010 299 ASN CCC CG  
9692  O OD1 . ASN C 299 ? 0.353 0.602 0.393 0.013  0.006  -0.014 299 ASN CCC OD1 
9693  N ND2 . ASN C 299 ? 0.375 0.624 0.402 0.012  0.008  -0.010 299 ASN CCC ND2 
9694  N N   . PRO C 300 ? 0.371 0.615 0.389 0.022  0.007  0.004  300 PRO CCC N   
9695  C CA  . PRO C 300 ? 0.373 0.618 0.389 0.024  0.007  0.008  300 PRO CCC CA  
9696  C C   . PRO C 300 ? 0.358 0.604 0.379 0.024  0.005  0.011  300 PRO CCC C   
9697  O O   . PRO C 300 ? 0.392 0.639 0.417 0.022  0.005  0.011  300 PRO CCC O   
9698  C CB  . PRO C 300 ? 0.382 0.628 0.393 0.025  0.008  0.010  300 PRO CCC CB  
9699  C CG  . PRO C 300 ? 0.372 0.618 0.384 0.023  0.008  0.008  300 PRO CCC CG  
9700  C CD  . PRO C 300 ? 0.366 0.610 0.379 0.021  0.008  0.004  300 PRO CCC CD  
9701  N N   . ASP C 301 ? 0.360 0.606 0.382 0.024  0.004  0.014  301 ASP CCC N   
9702  C CA  . ASP C 301 ? 0.365 0.612 0.393 0.023  0.002  0.018  301 ASP CCC CA  
9703  C C   . ASP C 301 ? 0.387 0.639 0.412 0.023  0.003  0.022  301 ASP CCC C   
9704  O O   . ASP C 301 ? 0.359 0.614 0.382 0.024  0.002  0.026  301 ASP CCC O   
9705  C CB  . ASP C 301 ? 0.369 0.615 0.400 0.023  -0.000 0.019  301 ASP CCC CB  
9706  C CG  . ASP C 301 ? 0.385 0.631 0.423 0.021  -0.003 0.023  301 ASP CCC CG  
9707  O OD1 . ASP C 301 ? 0.389 0.635 0.433 0.020  -0.004 0.022  301 ASP CCC OD1 
9708  O OD2 . ASP C 301 ? 0.368 0.615 0.407 0.021  -0.005 0.026  301 ASP CCC OD2 
9709  N N   . VAL C 302 ? 0.413 0.666 0.438 0.023  0.004  0.022  302 VAL CCC N   
9710  C CA  . VAL C 302 ? 0.458 0.717 0.481 0.023  0.005  0.026  302 VAL CCC CA  
9711  C C   . VAL C 302 ? 0.508 0.767 0.535 0.021  0.004  0.028  302 VAL CCC C   
9712  O O   . VAL C 302 ? 0.539 0.804 0.565 0.021  0.004  0.031  302 VAL CCC O   
9713  C CB  . VAL C 302 ? 0.437 0.696 0.455 0.025  0.007  0.023  302 VAL CCC CB  
9714  C CG1 . VAL C 302 ? 0.446 0.704 0.459 0.027  0.008  0.021  302 VAL CCC CG1 
9715  C CG2 . VAL C 302 ? 0.415 0.670 0.433 0.023  0.007  0.020  302 VAL CCC CG2 
9716  N N   . LYS C 303 ? 0.527 0.783 0.561 0.019  0.002  0.027  303 LYS CCC N   
9717  C CA  . LYS C 303 ? 0.592 0.849 0.632 0.017  0.000  0.028  303 LYS CCC CA  
9718  C C   . LYS C 303 ? 0.558 0.819 0.600 0.016  -0.001 0.034  303 LYS CCC C   
9719  O O   . LYS C 303 ? 0.570 0.834 0.613 0.015  -0.001 0.037  303 LYS CCC O   
9720  C CB  . LYS C 303 ? 0.640 0.894 0.687 0.016  -0.001 0.024  303 LYS CCC CB  
9721  C CG  . LYS C 303 ? 0.683 0.935 0.728 0.016  0.001  0.018  303 LYS CCC CG  
9722  C CD  . LYS C 303 ? 0.760 1.010 0.812 0.015  -0.001 0.013  303 LYS CCC CD  
9723  C CE  . LYS C 303 ? 0.792 1.043 0.842 0.014  0.001  0.008  303 LYS CCC CE  
9724  N NZ  . LYS C 303 ? 0.842 1.094 0.901 0.012  -0.000 0.002  303 LYS CCC NZ  
9725  N N   . GLY C 304 ? 0.535 0.796 0.578 0.016  -0.003 0.037  304 GLY CCC N   
9726  C CA  . GLY C 304 ? 0.518 0.783 0.563 0.014  -0.006 0.044  304 GLY CCC CA  
9727  C C   . GLY C 304 ? 0.492 0.764 0.530 0.015  -0.003 0.047  304 GLY CCC C   
9728  O O   . GLY C 304 ? 0.486 0.764 0.525 0.012  -0.005 0.053  304 GLY CCC O   
9729  N N   . LEU C 305 ? 0.476 0.750 0.508 0.017  0.001  0.043  305 LEU CCC N   
9730  C CA  . LEU C 305 ? 0.483 0.763 0.508 0.018  0.003  0.045  305 LEU CCC CA  
9731  C C   . LEU C 305 ? 0.497 0.783 0.522 0.018  0.004  0.047  305 LEU CCC C   
9732  O O   . LEU C 305 ? 0.533 0.827 0.554 0.018  0.005  0.048  305 LEU CCC O   
9733  C CB  . LEU C 305 ? 0.465 0.744 0.485 0.022  0.005  0.039  305 LEU CCC CB  
9734  C CG  . LEU C 305 ? 0.450 0.725 0.468 0.023  0.005  0.038  305 LEU CCC CG  
9735  C CD1 . LEU C 305 ? 0.451 0.724 0.464 0.026  0.007  0.033  305 LEU CCC CD1 
9736  C CD2 . LEU C 305 ? 0.437 0.719 0.454 0.021  0.004  0.042  305 LEU CCC CD2 
9737  N N   . ASN C 306 ? 0.498 0.781 0.527 0.017  0.003  0.046  306 ASN CCC N   
9738  C CA  . ASN C 306 ? 0.526 0.814 0.556 0.016  0.004  0.048  306 ASN CCC CA  
9739  C C   . ASN C 306 ? 0.519 0.809 0.543 0.019  0.007  0.044  306 ASN CCC C   
9740  O O   . ASN C 306 ? 0.509 0.806 0.531 0.019  0.009  0.046  306 ASN CCC O   
9741  C CB  . ASN C 306 ? 0.535 0.830 0.565 0.014  0.003  0.054  306 ASN CCC CB  
9742  C CG  . ASN C 306 ? 0.562 0.861 0.594 0.012  0.003  0.056  306 ASN CCC CG  
9743  O OD1 . ASN C 306 ? 0.583 0.877 0.619 0.012  0.003  0.055  306 ASN CCC OD1 
9744  N ND2 . ASN C 306 ? 0.554 0.863 0.586 0.010  0.004  0.061  306 ASN CCC ND2 
9745  N N   . LEU C 307 ? 0.513 0.797 0.535 0.021  0.008  0.039  307 LEU CCC N   
9746  C CA  . LEU C 307 ? 0.522 0.807 0.540 0.024  0.010  0.036  307 LEU CCC CA  
9747  C C   . LEU C 307 ? 0.545 0.831 0.564 0.024  0.010  0.036  307 LEU CCC C   
9748  O O   . LEU C 307 ? 0.534 0.826 0.552 0.026  0.012  0.035  307 LEU CCC O   
9749  C CB  . LEU C 307 ? 0.487 0.765 0.502 0.025  0.010  0.031  307 LEU CCC CB  
9750  C CG  . LEU C 307 ? 0.476 0.752 0.490 0.026  0.009  0.031  307 LEU CCC CG  
9751  C CD1 . LEU C 307 ? 0.453 0.723 0.465 0.027  0.009  0.027  307 LEU CCC CD1 
9752  C CD2 . LEU C 307 ? 0.473 0.756 0.485 0.028  0.010  0.031  307 LEU CCC CD2 
9753  N N   . ASN C 308 ? 0.573 0.856 0.596 0.022  0.010  0.036  308 ASN CCC N   
9754  C CA  . ASN C 308 ? 0.595 0.878 0.618 0.021  0.010  0.036  308 ASN CCC CA  
9755  C C   . ASN C 308 ? 0.587 0.877 0.611 0.021  0.010  0.039  308 ASN CCC C   
9756  O O   . ASN C 308 ? 0.533 0.826 0.556 0.023  0.011  0.037  308 ASN CCC O   
9757  C CB  . ASN C 308 ? 0.629 0.907 0.656 0.019  0.009  0.036  308 ASN CCC CB  
9758  C CG  . ASN C 308 ? 0.644 0.922 0.672 0.018  0.009  0.035  308 ASN CCC CG  
9759  O OD1 . ASN C 308 ? 0.657 0.938 0.684 0.019  0.010  0.035  308 ASN CCC OD1 
9760  N ND2 . ASN C 308 ? 0.706 0.981 0.737 0.016  0.008  0.033  308 ASN CCC ND2 
9761  N N   . ALA C 309 ? 0.590 0.885 0.617 0.019  0.010  0.043  309 ALA CCC N   
9762  C CA  . ALA C 309 ? 0.567 0.869 0.594 0.018  0.010  0.047  309 ALA CCC CA  
9763  C C   . ALA C 309 ? 0.577 0.888 0.601 0.021  0.012  0.045  309 ALA CCC C   
9764  O O   . ALA C 309 ? 0.566 0.883 0.590 0.021  0.013  0.046  309 ALA CCC O   
9765  C CB  . ALA C 309 ? 0.534 0.839 0.565 0.015  0.008  0.052  309 ALA CCC CB  
9766  N N   . ILE C 310 ? 0.534 0.844 0.555 0.023  0.012  0.043  310 ILE CCC N   
9767  C CA  . ILE C 310 ? 0.524 0.841 0.542 0.025  0.014  0.040  310 ILE CCC CA  
9768  C C   . ILE C 310 ? 0.500 0.815 0.517 0.029  0.014  0.035  310 ILE CCC C   
9769  O O   . ILE C 310 ? 0.497 0.820 0.514 0.031  0.015  0.033  310 ILE CCC O   
9770  C CB  . ILE C 310 ? 0.586 0.904 0.601 0.025  0.014  0.041  310 ILE CCC CB  
9771  C CG1 . ILE C 310 ? 0.610 0.929 0.627 0.021  0.012  0.046  310 ILE CCC CG1 
9772  C CG2 . ILE C 310 ? 0.590 0.918 0.603 0.027  0.015  0.038  310 ILE CCC CG2 
9773  C CD1 . ILE C 310 ? 0.642 0.969 0.661 0.018  0.012  0.051  310 ILE CCC CD1 
9774  N N   . GLY C 311 ? 0.508 0.814 0.525 0.029  0.013  0.034  311 GLY CCC N   
9775  C CA  . GLY C 311 ? 0.496 0.799 0.513 0.031  0.013  0.030  311 GLY CCC CA  
9776  C C   . GLY C 311 ? 0.477 0.775 0.491 0.033  0.012  0.026  311 GLY CCC C   
9777  O O   . GLY C 311 ? 0.497 0.794 0.511 0.036  0.012  0.023  311 GLY CCC O   
9778  N N   . VAL C 312 ? 0.424 0.719 0.437 0.032  0.012  0.027  312 VAL CCC N   
9779  C CA  . VAL C 312 ? 0.463 0.753 0.474 0.034  0.012  0.024  312 VAL CCC CA  
9780  C C   . VAL C 312 ? 0.457 0.738 0.467 0.033  0.011  0.023  312 VAL CCC C   
9781  O O   . VAL C 312 ? 0.444 0.722 0.455 0.030  0.011  0.025  312 VAL CCC O   
9782  C CB  . VAL C 312 ? 0.456 0.746 0.465 0.033  0.012  0.025  312 VAL CCC CB  
9783  C CG1 . VAL C 312 ? 0.456 0.739 0.463 0.035  0.011  0.022  312 VAL CCC CG1 
9784  C CG2 . VAL C 312 ? 0.438 0.738 0.447 0.034  0.013  0.026  312 VAL CCC CG2 
9785  N N   . GLU C 313 ? 0.443 0.721 0.453 0.034  0.009  0.021  313 GLU CCC N   
9786  C CA  . GLU C 313 ? 0.476 0.747 0.485 0.032  0.008  0.020  313 GLU CCC CA  
9787  C C   . GLU C 313 ? 0.466 0.732 0.473 0.031  0.008  0.019  313 GLU CCC C   
9788  O O   . GLU C 313 ? 0.429 0.695 0.435 0.033  0.008  0.018  313 GLU CCC O   
9789  C CB  . GLU C 313 ? 0.533 0.803 0.542 0.034  0.006  0.018  313 GLU CCC CB  
9790  C CG  . GLU C 313 ? 0.611 0.886 0.624 0.035  0.006  0.019  313 GLU CCC CG  
9791  C CD  . GLU C 313 ? 0.654 0.929 0.668 0.032  0.007  0.022  313 GLU CCC CD  
9792  O OE1 . GLU C 313 ? 0.626 0.897 0.639 0.029  0.006  0.023  313 GLU CCC OE1 
9793  O OE2 . GLU C 313 ? 0.693 0.975 0.709 0.032  0.008  0.023  313 GLU CCC OE2 
9794  N N   . VAL C 314 ? 0.495 0.757 0.502 0.028  0.008  0.020  314 VAL CCC N   
9795  C CA  . VAL C 314 ? 0.499 0.758 0.506 0.026  0.008  0.018  314 VAL CCC CA  
9796  C C   . VAL C 314 ? 0.494 0.749 0.499 0.024  0.007  0.017  314 VAL CCC C   
9797  O O   . VAL C 314 ? 0.447 0.704 0.453 0.022  0.006  0.018  314 VAL CCC O   
9798  C CB  . VAL C 314 ? 0.505 0.764 0.514 0.024  0.009  0.019  314 VAL CCC CB  
9799  C CG1 . VAL C 314 ? 0.473 0.736 0.483 0.026  0.009  0.021  314 VAL CCC CG1 
9800  C CG2 . VAL C 314 ? 0.521 0.781 0.533 0.022  0.009  0.020  314 VAL CCC CG2 
9801  N N   . SER C 315 ? 0.465 0.717 0.467 0.023  0.006  0.015  315 SER CCC N   
9802  C CA  . SER C 315 ? 0.441 0.692 0.442 0.019  0.005  0.015  315 SER CCC CA  
9803  C C   . SER C 315 ? 0.444 0.695 0.446 0.016  0.006  0.013  315 SER CCC C   
9804  O O   . SER C 315 ? 0.377 0.630 0.382 0.016  0.007  0.013  315 SER CCC O   
9805  C CB  . SER C 315 ? 0.453 0.701 0.452 0.020  0.004  0.013  315 SER CCC CB  
9806  O OG  . SER C 315 ? 0.445 0.691 0.443 0.019  0.005  0.011  315 SER CCC OG  
9807  N N   . ASP C 316 ? 0.470 0.721 0.471 0.012  0.005  0.012  316 ASP CCC N   
9808  C CA  . ASP C 316 ? 0.521 0.775 0.523 0.008  0.006  0.010  316 ASP CCC CA  
9809  C C   . ASP C 316 ? 0.518 0.771 0.522 0.008  0.007  0.007  316 ASP CCC C   
9810  O O   . ASP C 316 ? 0.532 0.788 0.540 0.007  0.008  0.005  316 ASP CCC O   
9811  C CB  . ASP C 316 ? 0.528 0.784 0.528 0.003  0.005  0.010  316 ASP CCC CB  
9812  C CG  . ASP C 316 ? 0.545 0.801 0.544 0.002  0.003  0.013  316 ASP CCC CG  
9813  O OD1 . ASP C 316 ? 0.479 0.736 0.480 0.004  0.004  0.014  316 ASP CCC OD1 
9814  O OD2 . ASP C 316 ? 0.587 0.843 0.583 -0.001 0.001  0.014  316 ASP CCC OD2 
9815  N N   . SER C 317 ? 0.530 0.781 0.532 0.010  0.007  0.007  317 SER CCC N   
9816  C CA  . SER C 317 ? 0.541 0.791 0.545 0.011  0.008  0.004  317 SER CCC CA  
9817  C C   . SER C 317 ? 0.527 0.777 0.534 0.014  0.009  0.005  317 SER CCC C   
9818  O O   . SER C 317 ? 0.416 0.665 0.426 0.015  0.009  0.003  317 SER CCC O   
9819  C CB  . SER C 317 ? 0.523 0.770 0.523 0.012  0.007  0.004  317 SER CCC CB  
9820  O OG  . SER C 317 ? 0.504 0.749 0.502 0.016  0.007  0.006  317 SER CCC OG  
9821  N N   . GLY C 318 ? 0.489 0.739 0.497 0.016  0.008  0.008  318 GLY CCC N   
9822  C CA  . GLY C 318 ? 0.464 0.715 0.474 0.019  0.009  0.011  318 GLY CCC CA  
9823  C C   . GLY C 318 ? 0.446 0.696 0.454 0.022  0.009  0.012  318 GLY CCC C   
9824  O O   . GLY C 318 ? 0.475 0.727 0.484 0.024  0.009  0.014  318 GLY CCC O   
9825  N N   . LYS C 319 ? 0.438 0.686 0.442 0.023  0.008  0.011  319 LYS CCC N   
9826  C CA  . LYS C 319 ? 0.428 0.676 0.430 0.026  0.008  0.011  319 LYS CCC CA  
9827  C C   . LYS C 319 ? 0.434 0.685 0.435 0.028  0.008  0.013  319 LYS CCC C   
9828  O O   . LYS C 319 ? 0.449 0.701 0.451 0.027  0.007  0.014  319 LYS CCC O   
9829  C CB  . LYS C 319 ? 0.416 0.661 0.415 0.026  0.007  0.009  319 LYS CCC CB  
9830  C CG  . LYS C 319 ? 0.417 0.660 0.416 0.025  0.007  0.007  319 LYS CCC CG  
9831  C CD  . LYS C 319 ? 0.414 0.654 0.410 0.026  0.006  0.005  319 LYS CCC CD  
9832  C CE  . LYS C 319 ? 0.418 0.656 0.414 0.025  0.007  0.003  319 LYS CCC CE  
9833  N NZ  . LYS C 319 ? 0.437 0.673 0.431 0.026  0.006  0.002  319 LYS CCC NZ  
9834  N N   . ILE C 320 ? 0.421 0.674 0.422 0.031  0.008  0.014  320 ILE CCC N   
9835  C CA  . ILE C 320 ? 0.410 0.668 0.412 0.033  0.008  0.014  320 ILE CCC CA  
9836  C C   . ILE C 320 ? 0.394 0.650 0.394 0.035  0.006  0.013  320 ILE CCC C   
9837  O O   . ILE C 320 ? 0.347 0.600 0.346 0.036  0.005  0.011  320 ILE CCC O   
9838  C CB  . ILE C 320 ? 0.449 0.712 0.450 0.035  0.009  0.015  320 ILE CCC CB  
9839  C CG1 . ILE C 320 ? 0.459 0.723 0.462 0.033  0.010  0.018  320 ILE CCC CG1 
9840  C CG2 . ILE C 320 ? 0.437 0.705 0.438 0.038  0.009  0.015  320 ILE CCC CG2 
9841  C CD1 . ILE C 320 ? 0.441 0.711 0.444 0.034  0.010  0.020  320 ILE CCC CD1 
9842  N N   . ILE C 321 ? 0.410 0.667 0.411 0.036  0.005  0.013  321 ILE CCC N   
9843  C CA  . ILE C 321 ? 0.445 0.701 0.447 0.037  0.003  0.011  321 ILE CCC CA  
9844  C C   . ILE C 321 ? 0.448 0.708 0.451 0.042  0.003  0.009  321 ILE CCC C   
9845  O O   . ILE C 321 ? 0.531 0.798 0.535 0.043  0.004  0.010  321 ILE CCC O   
9846  C CB  . ILE C 321 ? 0.482 0.738 0.486 0.036  0.002  0.013  321 ILE CCC CB  
9847  C CG1 . ILE C 321 ? 0.508 0.760 0.510 0.031  0.001  0.014  321 ILE CCC CG1 
9848  C CG2 . ILE C 321 ? 0.477 0.732 0.483 0.038  -0.002 0.011  321 ILE CCC CG2 
9849  C CD1 . ILE C 321 ? 0.515 0.768 0.518 0.029  0.001  0.016  321 ILE CCC CD1 
9850  N N   . ALA C 322 ? 0.442 0.701 0.444 0.043  0.002  0.007  322 ALA CCC N   
9851  C CA  . ALA C 322 ? 0.458 0.721 0.461 0.047  0.002  0.004  322 ALA CCC CA  
9852  C C   . ALA C 322 ? 0.438 0.696 0.441 0.049  -0.001 0.001  322 ALA CCC C   
9853  O O   . ALA C 322 ? 0.388 0.646 0.389 0.050  -0.000 0.000  322 ALA CCC O   
9854  C CB  . ALA C 322 ? 0.457 0.725 0.458 0.047  0.005  0.005  322 ALA CCC CB  
9855  N N   . PRO C 323 ? 0.471 0.725 0.476 0.049  -0.004 0.001  323 PRO CCC N   
9856  C CA  . PRO C 323 ? 0.471 0.720 0.477 0.050  -0.008 -0.001 323 PRO CCC CA  
9857  C C   . PRO C 323 ? 0.455 0.707 0.463 0.054  -0.008 -0.005 323 PRO CCC C   
9858  O O   . PRO C 323 ? 0.440 0.687 0.447 0.055  -0.010 -0.006 323 PRO CCC O   
9859  C CB  . PRO C 323 ? 0.469 0.714 0.478 0.049  -0.012 0.000  323 PRO CCC CB  
9860  C CG  . PRO C 323 ? 0.464 0.715 0.476 0.050  -0.011 0.000  323 PRO CCC CG  
9861  C CD  . PRO C 323 ? 0.473 0.727 0.481 0.048  -0.006 0.002  323 PRO CCC CD  
9862  N N   . LYS C 324 ? 0.458 0.718 0.468 0.057  -0.007 -0.008 324 LYS CCC N   
9863  C CA  . LYS C 324 ? 0.480 0.746 0.492 0.062  -0.007 -0.012 324 LYS CCC CA  
9864  C C   . LYS C 324 ? 0.431 0.705 0.439 0.061  -0.002 -0.012 324 LYS CCC C   
9865  O O   . LYS C 324 ? 0.461 0.744 0.471 0.064  -0.001 -0.015 324 LYS CCC O   
9866  C CB  . LYS C 324 ? 0.564 0.834 0.582 0.065  -0.010 -0.016 324 LYS CCC CB  
9867  C CG  . LYS C 324 ? 0.615 0.877 0.637 0.066  -0.015 -0.018 324 LYS CCC CG  
9868  C CD  . LYS C 324 ? 0.686 0.952 0.716 0.071  -0.019 -0.024 324 LYS CCC CD  
9869  C CE  . LYS C 324 ? 0.718 0.977 0.754 0.072  -0.025 -0.025 324 LYS CCC CE  
9870  N NZ  . LYS C 324 ? 0.751 1.014 0.796 0.076  -0.029 -0.030 324 LYS CCC NZ  
9871  N N   . ASP C 325 ? 0.381 0.653 0.385 0.058  0.000  -0.007 325 ASP CCC N   
9872  C CA  . ASP C 325 ? 0.384 0.663 0.386 0.056  0.004  -0.005 325 ASP CCC CA  
9873  C C   . ASP C 325 ? 0.375 0.661 0.378 0.056  0.006  -0.004 325 ASP CCC C   
9874  O O   . ASP C 325 ? 0.365 0.654 0.366 0.053  0.008  -0.000 325 ASP CCC O   
9875  C CB  . ASP C 325 ? 0.418 0.702 0.419 0.059  0.004  -0.008 325 ASP CCC CB  
9876  C CG  . ASP C 325 ? 0.411 0.687 0.410 0.060  0.003  -0.010 325 ASP CCC CG  
9877  O OD1 . ASP C 325 ? 0.369 0.637 0.367 0.058  0.002  -0.008 325 ASP CCC OD1 
9878  O OD2 . ASP C 325 ? 0.446 0.727 0.446 0.063  0.002  -0.014 325 ASP CCC OD2 
9879  N N   . ALA C 326 ? 0.355 0.644 0.361 0.058  0.004  -0.006 326 ALA CCC N   
9880  C CA  . ALA C 326 ? 0.359 0.656 0.368 0.057  0.006  -0.005 326 ALA CCC CA  
9881  C C   . ALA C 326 ? 0.373 0.664 0.382 0.054  0.006  -0.001 326 ALA CCC C   
9882  O O   . ALA C 326 ? 0.362 0.645 0.371 0.054  0.003  -0.001 326 ALA CCC O   
9883  C CB  . ALA C 326 ? 0.349 0.652 0.364 0.061  0.004  -0.011 326 ALA CCC CB  
9884  N N   . THR C 327 ? 0.366 0.660 0.373 0.051  0.008  0.003  327 THR CCC N   
9885  C CA  . THR C 327 ? 0.391 0.680 0.398 0.048  0.008  0.007  327 THR CCC CA  
9886  C C   . THR C 327 ? 0.395 0.689 0.406 0.049  0.007  0.006  327 THR CCC C   
9887  O O   . THR C 327 ? 0.378 0.678 0.392 0.052  0.007  0.002  327 THR CCC O   
9888  C CB  . THR C 327 ? 0.395 0.687 0.401 0.045  0.010  0.012  327 THR CCC CB  
9889  O OG1 . THR C 327 ? 0.401 0.703 0.407 0.045  0.012  0.012  327 THR CCC OG1 
9890  C CG2 . THR C 327 ? 0.379 0.669 0.382 0.044  0.011  0.012  327 THR CCC CG2 
9891  N N   . SER C 328 ? 0.380 0.671 0.392 0.046  0.007  0.009  328 SER CCC N   
9892  C CA  . SER C 328 ? 0.395 0.690 0.411 0.047  0.007  0.009  328 SER CCC CA  
9893  C C   . SER C 328 ? 0.382 0.688 0.398 0.047  0.009  0.009  328 SER CCC C   
9894  O O   . SER C 328 ? 0.398 0.709 0.418 0.049  0.009  0.007  328 SER CCC O   
9895  C CB  . SER C 328 ? 0.399 0.688 0.413 0.043  0.007  0.013  328 SER CCC CB  
9896  O OG  . SER C 328 ? 0.405 0.694 0.418 0.040  0.009  0.016  328 SER CCC OG  
9897  N N   . VAL C 329 ? 0.372 0.683 0.386 0.046  0.011  0.011  329 VAL CCC N   
9898  C CA  . VAL C 329 ? 0.361 0.685 0.375 0.046  0.014  0.011  329 VAL CCC CA  
9899  C C   . VAL C 329 ? 0.361 0.691 0.375 0.049  0.014  0.006  329 VAL CCC C   
9900  O O   . VAL C 329 ? 0.360 0.687 0.371 0.049  0.014  0.007  329 VAL CCC O   
9901  C CB  . VAL C 329 ? 0.359 0.684 0.371 0.042  0.015  0.017  329 VAL CCC CB  
9902  C CG1 . VAL C 329 ? 0.362 0.700 0.373 0.041  0.017  0.018  329 VAL CCC CG1 
9903  C CG2 . VAL C 329 ? 0.340 0.660 0.353 0.039  0.015  0.021  329 VAL CCC CG2 
9904  N N   . PRO C 330 ? 0.378 0.718 0.395 0.052  0.014  0.002  330 PRO CCC N   
9905  C CA  . PRO C 330 ? 0.373 0.718 0.391 0.055  0.014  -0.005 330 PRO CCC CA  
9906  C C   . PRO C 330 ? 0.376 0.731 0.390 0.054  0.016  -0.004 330 PRO CCC C   
9907  O O   . PRO C 330 ? 0.368 0.726 0.383 0.057  0.015  -0.009 330 PRO CCC O   
9908  C CB  . PRO C 330 ? 0.400 0.753 0.424 0.059  0.013  -0.010 330 PRO CCC CB  
9909  C CG  . PRO C 330 ? 0.406 0.763 0.431 0.056  0.014  -0.006 330 PRO CCC CG  
9910  C CD  . PRO C 330 ? 0.393 0.740 0.414 0.052  0.014  0.001  330 PRO CCC CD  
9911  N N   . SER C 331 ? 0.382 0.741 0.393 0.050  0.018  0.002  331 SER CCC N   
9912  C CA  . SER C 331 ? 0.374 0.741 0.381 0.048  0.019  0.004  331 SER CCC CA  
9913  C C   . SER C 331 ? 0.395 0.750 0.399 0.046  0.018  0.008  331 SER CCC C   
9914  O O   . SER C 331 ? 0.384 0.743 0.384 0.044  0.019  0.010  331 SER CCC O   
9915  C CB  . SER C 331 ? 0.357 0.735 0.363 0.044  0.021  0.008  331 SER CCC CB  
9916  O OG  . SER C 331 ? 0.380 0.750 0.386 0.040  0.020  0.015  331 SER CCC OG  
9917  N N   . ILE C 332 ? 0.373 0.714 0.377 0.046  0.017  0.009  332 ILE CCC N   
9918  C CA  . ILE C 332 ? 0.354 0.685 0.356 0.044  0.016  0.013  332 ILE CCC CA  
9919  C C   . ILE C 332 ? 0.346 0.666 0.348 0.047  0.014  0.010  332 ILE CCC C   
9920  O O   . ILE C 332 ? 0.296 0.610 0.300 0.048  0.013  0.008  332 ILE CCC O   
9921  C CB  . ILE C 332 ? 0.346 0.671 0.349 0.040  0.016  0.019  332 ILE CCC CB  
9922  C CG1 . ILE C 332 ? 0.337 0.672 0.340 0.037  0.017  0.023  332 ILE CCC CG1 
9923  C CG2 . ILE C 332 ? 0.353 0.667 0.355 0.039  0.015  0.021  332 ILE CCC CG2 
9924  C CD1 . ILE C 332 ? 0.330 0.660 0.335 0.034  0.016  0.029  332 ILE CCC CD1 
9925  N N   . PHE C 333 ? 0.340 0.658 0.339 0.047  0.014  0.010  333 PHE CCC N   
9926  C CA  . PHE C 333 ? 0.339 0.647 0.337 0.049  0.013  0.006  333 PHE CCC CA  
9927  C C   . PHE C 333 ? 0.342 0.641 0.338 0.046  0.012  0.010  333 PHE CCC C   
9928  O O   . PHE C 333 ? 0.372 0.673 0.369 0.043  0.013  0.015  333 PHE CCC O   
9929  C CB  . PHE C 333 ? 0.348 0.663 0.345 0.052  0.013  0.002  333 PHE CCC CB  
9930  C CG  . PHE C 333 ? 0.354 0.679 0.355 0.055  0.013  -0.003 333 PHE CCC CG  
9931  C CD1 . PHE C 333 ? 0.354 0.692 0.354 0.054  0.015  -0.003 333 PHE CCC CD1 
9932  C CD2 . PHE C 333 ? 0.342 0.663 0.346 0.059  0.011  -0.008 333 PHE CCC CD2 
9933  C CE1 . PHE C 333 ? 0.370 0.718 0.375 0.057  0.015  -0.008 333 PHE CCC CE1 
9934  C CE2 . PHE C 333 ? 0.357 0.687 0.366 0.062  0.011  -0.014 333 PHE CCC CE2 
9935  C CZ  . PHE C 333 ? 0.356 0.699 0.364 0.061  0.013  -0.014 333 PHE CCC CZ  
9936  N N   . ALA C 334 ? 0.309 0.600 0.306 0.047  0.011  0.008  334 ALA CCC N   
9937  C CA  . ALA C 334 ? 0.290 0.571 0.285 0.045  0.010  0.010  334 ALA CCC CA  
9938  C C   . ALA C 334 ? 0.283 0.559 0.277 0.047  0.009  0.007  334 ALA CCC C   
9939  O O   . ALA C 334 ? 0.285 0.560 0.279 0.050  0.008  0.003  334 ALA CCC O   
9940  C CB  . ALA C 334 ? 0.283 0.559 0.279 0.043  0.010  0.012  334 ALA CCC CB  
9941  N N   . VAL C 335 ? 0.283 0.555 0.275 0.046  0.009  0.008  335 VAL CCC N   
9942  C CA  . VAL C 335 ? 0.298 0.564 0.289 0.047  0.008  0.005  335 VAL CCC CA  
9943  C C   . VAL C 335 ? 0.305 0.565 0.296 0.044  0.008  0.007  335 VAL CCC C   
9944  O O   . VAL C 335 ? 0.301 0.562 0.293 0.042  0.008  0.010  335 VAL CCC O   
9945  C CB  . VAL C 335 ? 0.322 0.593 0.312 0.050  0.008  0.003  335 VAL CCC CB  
9946  C CG1 . VAL C 335 ? 0.324 0.602 0.314 0.053  0.008  -0.000 335 VAL CCC CG1 
9947  C CG2 . VAL C 335 ? 0.318 0.593 0.306 0.048  0.009  0.006  335 VAL CCC CG2 
9948  N N   . GLY C 336 ? 0.326 0.580 0.316 0.045  0.007  0.005  336 GLY CCC N   
9949  C CA  . GLY C 336 ? 0.307 0.556 0.297 0.043  0.007  0.006  336 GLY CCC CA  
9950  C C   . GLY C 336 ? 0.322 0.567 0.314 0.040  0.007  0.006  336 GLY CCC C   
9951  O O   . GLY C 336 ? 0.296 0.541 0.288 0.040  0.006  0.005  336 GLY CCC O   
9952  N N   . ASP C 337 ? 0.330 0.572 0.323 0.038  0.007  0.006  337 ASP CCC N   
9953  C CA  . ASP C 337 ? 0.327 0.566 0.322 0.035  0.007  0.005  337 ASP CCC CA  
9954  C C   . ASP C 337 ? 0.340 0.581 0.337 0.033  0.007  0.006  337 ASP CCC C   
9955  O O   . ASP C 337 ? 0.333 0.572 0.330 0.031  0.007  0.005  337 ASP CCC O   
9956  C CB  . ASP C 337 ? 0.342 0.579 0.341 0.033  0.007  0.004  337 ASP CCC CB  
9957  C CG  . ASP C 337 ? 0.363 0.597 0.360 0.034  0.006  0.002  337 ASP CCC CG  
9958  O OD1 . ASP C 337 ? 0.357 0.591 0.352 0.036  0.006  0.001  337 ASP CCC OD1 
9959  O OD2 . ASP C 337 ? 0.384 0.617 0.385 0.033  0.006  0.001  337 ASP CCC OD2 
9960  N N   . ILE C 338 ? 0.341 0.586 0.339 0.034  0.008  0.009  338 ILE CCC N   
9961  C CA  . ILE C 338 ? 0.327 0.574 0.326 0.033  0.008  0.011  338 ILE CCC CA  
9962  C C   . ILE C 338 ? 0.334 0.582 0.331 0.034  0.008  0.010  338 ILE CCC C   
9963  O O   . ILE C 338 ? 0.333 0.582 0.332 0.033  0.008  0.011  338 ILE CCC O   
9964  C CB  . ILE C 338 ? 0.324 0.576 0.325 0.033  0.008  0.014  338 ILE CCC CB  
9965  C CG1 . ILE C 338 ? 0.317 0.575 0.316 0.036  0.009  0.015  338 ILE CCC CG1 
9966  C CG2 . ILE C 338 ? 0.321 0.573 0.326 0.032  0.008  0.015  338 ILE CCC CG2 
9967  C CD1 . ILE C 338 ? 0.318 0.582 0.318 0.035  0.009  0.018  338 ILE CCC CD1 
9968  N N   . VAL C 339 ? 0.351 0.598 0.346 0.036  0.007  0.008  339 VAL CCC N   
9969  C CA  . VAL C 339 ? 0.372 0.620 0.367 0.037  0.006  0.008  339 VAL CCC CA  
9970  C C   . VAL C 339 ? 0.387 0.630 0.380 0.035  0.004  0.007  339 VAL CCC C   
9971  O O   . VAL C 339 ? 0.394 0.633 0.386 0.035  0.004  0.005  339 VAL CCC O   
9972  C CB  . VAL C 339 ? 0.369 0.619 0.363 0.041  0.005  0.006  339 VAL CCC CB  
9973  C CG1 . VAL C 339 ? 0.356 0.606 0.351 0.043  0.003  0.005  339 VAL CCC CG1 
9974  C CG2 . VAL C 339 ? 0.376 0.632 0.370 0.043  0.007  0.007  339 VAL CCC CG2 
9975  N N   . GLU C 340 ? 0.419 0.662 0.413 0.034  0.004  0.008  340 GLU CCC N   
9976  C CA  . GLU C 340 ? 0.455 0.695 0.449 0.031  0.002  0.008  340 GLU CCC CA  
9977  C C   . GLU C 340 ? 0.439 0.676 0.432 0.032  -0.001 0.007  340 GLU CCC C   
9978  O O   . GLU C 340 ? 0.409 0.647 0.403 0.036  -0.002 0.006  340 GLU CCC O   
9979  C CB  . GLU C 340 ? 0.516 0.758 0.511 0.029  0.001  0.009  340 GLU CCC CB  
9980  C CG  . GLU C 340 ? 0.608 0.846 0.601 0.026  -0.001 0.010  340 GLU CCC CG  
9981  C CD  . GLU C 340 ? 0.733 0.973 0.726 0.022  -0.001 0.011  340 GLU CCC CD  
9982  O OE1 . GLU C 340 ? 0.734 0.975 0.729 0.022  -0.003 0.013  340 GLU CCC OE1 
9983  O OE2 . GLU C 340 ? 0.874 1.115 0.867 0.019  0.001  0.010  340 GLU CCC OE2 
9984  N N   . GLY C 341 ? 0.395 0.628 0.385 0.030  -0.002 0.006  341 GLY CCC N   
9985  C CA  . GLY C 341 ? 0.383 0.613 0.374 0.030  -0.006 0.006  341 GLY CCC CA  
9986  C C   . GLY C 341 ? 0.367 0.595 0.357 0.033  -0.006 0.004  341 GLY CCC C   
9987  O O   . GLY C 341 ? 0.353 0.578 0.343 0.034  -0.010 0.004  341 GLY CCC O   
9988  N N   . ARG C 342 ? 0.343 0.572 0.332 0.034  -0.003 0.003  342 ARG CCC N   
9989  C CA  . ARG C 342 ? 0.341 0.569 0.329 0.037  -0.004 0.001  342 ARG CCC CA  
9990  C C   . ARG C 342 ? 0.328 0.555 0.315 0.035  -0.002 0.001  342 ARG CCC C   
9991  O O   . ARG C 342 ? 0.324 0.553 0.311 0.033  0.001  0.001  342 ARG CCC O   
9992  C CB  . ARG C 342 ? 0.316 0.548 0.306 0.041  -0.003 0.000  342 ARG CCC CB  
9993  C CG  . ARG C 342 ? 0.319 0.554 0.308 0.042  0.000  0.001  342 ARG CCC CG  
9994  C CD  . ARG C 342 ? 0.318 0.559 0.308 0.045  0.001  0.000  342 ARG CCC CD  
9995  N NE  . ARG C 342 ? 0.313 0.557 0.305 0.047  0.000  -0.000 342 ARG CCC NE  
9996  C CZ  . ARG C 342 ? 0.332 0.582 0.325 0.050  0.001  -0.002 342 ARG CCC CZ  
9997  N NH1 . ARG C 342 ? 0.325 0.578 0.317 0.052  0.002  -0.003 342 ARG CCC NH1 
9998  N NH2 . ARG C 342 ? 0.327 0.581 0.324 0.052  -0.000 -0.003 342 ARG CCC NH2 
9999  N N   . PRO C 343 ? 0.304 0.528 0.289 0.035  -0.003 -0.001 343 PRO CCC N   
10000 C CA  . PRO C 343 ? 0.290 0.513 0.274 0.034  -0.001 -0.002 343 PRO CCC CA  
10001 C C   . PRO C 343 ? 0.296 0.522 0.282 0.035  0.001  -0.002 343 PRO CCC C   
10002 O O   . PRO C 343 ? 0.291 0.519 0.277 0.039  0.001  -0.002 343 PRO CCC O   
10003 C CB  . PRO C 343 ? 0.298 0.518 0.281 0.035  -0.003 -0.003 343 PRO CCC CB  
10004 C CG  . PRO C 343 ? 0.307 0.526 0.291 0.036  -0.007 -0.002 343 PRO CCC CG  
10005 C CD  . PRO C 343 ? 0.310 0.532 0.295 0.038  -0.006 -0.002 343 PRO CCC CD  
10006 N N   . GLU C 344 ? 0.316 0.542 0.302 0.033  0.003  -0.003 344 GLU CCC N   
10007 C CA  . GLU C 344 ? 0.316 0.544 0.305 0.034  0.004  -0.003 344 GLU CCC CA  
10008 C C   . GLU C 344 ? 0.309 0.535 0.297 0.035  0.004  -0.004 344 GLU CCC C   
10009 O O   . GLU C 344 ? 0.292 0.517 0.282 0.034  0.004  -0.006 344 GLU CCC O   
10010 C CB  . GLU C 344 ? 0.358 0.587 0.350 0.031  0.005  -0.004 344 GLU CCC CB  
10011 C CG  . GLU C 344 ? 0.390 0.621 0.382 0.029  0.006  -0.002 344 GLU CCC CG  
10012 C CD  . GLU C 344 ? 0.421 0.654 0.418 0.026  0.007  -0.004 344 GLU CCC CD  
10013 O OE1 . GLU C 344 ? 0.435 0.668 0.435 0.025  0.007  -0.006 344 GLU CCC OE1 
10014 O OE2 . GLU C 344 ? 0.453 0.688 0.450 0.024  0.007  -0.003 344 GLU CCC OE2 
10015 N N   . LEU C 345 ? 0.295 0.521 0.282 0.039  0.003  -0.004 345 LEU CCC N   
10016 C CA  . LEU C 345 ? 0.318 0.542 0.303 0.040  0.003  -0.005 345 LEU CCC CA  
10017 C C   . LEU C 345 ? 0.314 0.541 0.299 0.043  0.003  -0.004 345 LEU CCC C   
10018 O O   . LEU C 345 ? 0.313 0.543 0.298 0.045  0.003  -0.003 345 LEU CCC O   
10019 C CB  . LEU C 345 ? 0.330 0.550 0.313 0.041  0.001  -0.007 345 LEU CCC CB  
10020 C CG  . LEU C 345 ? 0.327 0.546 0.310 0.037  0.000  -0.007 345 LEU CCC CG  
10021 C CD1 . LEU C 345 ? 0.323 0.538 0.304 0.038  -0.003 -0.008 345 LEU CCC CD1 
10022 C CD2 . LEU C 345 ? 0.331 0.549 0.315 0.035  0.001  -0.009 345 LEU CCC CD2 
10023 N N   . THR C 346 ? 0.321 0.547 0.306 0.044  0.003  -0.005 346 THR CCC N   
10024 C CA  . THR C 346 ? 0.317 0.547 0.302 0.046  0.003  -0.003 346 THR CCC CA  
10025 C C   . THR C 346 ? 0.306 0.540 0.289 0.049  0.003  -0.005 346 THR CCC C   
10026 O O   . THR C 346 ? 0.297 0.535 0.279 0.050  0.003  -0.003 346 THR CCC O   
10027 C CB  . THR C 346 ? 0.321 0.550 0.307 0.045  0.003  -0.003 346 THR CCC CB  
10028 O OG1 . THR C 346 ? 0.340 0.570 0.329 0.043  0.003  -0.001 346 THR CCC OG1 
10029 C CG2 . THR C 346 ? 0.328 0.561 0.312 0.047  0.003  -0.002 346 THR CCC CG2 
10030 N N   . PRO C 347 ? 0.289 0.519 0.270 0.051  0.002  -0.007 347 PRO CCC N   
10031 C CA  . PRO C 347 ? 0.285 0.518 0.265 0.054  0.001  -0.009 347 PRO CCC CA  
10032 C C   . PRO C 347 ? 0.278 0.514 0.259 0.055  0.000  -0.009 347 PRO CCC C   
10033 O O   . PRO C 347 ? 0.265 0.506 0.247 0.057  0.000  -0.011 347 PRO CCC O   
10034 C CB  . PRO C 347 ? 0.276 0.503 0.256 0.055  -0.001 -0.012 347 PRO CCC CB  
10035 C CG  . PRO C 347 ? 0.271 0.494 0.251 0.052  -0.001 -0.011 347 PRO CCC CG  
10036 C CD  . PRO C 347 ? 0.279 0.503 0.260 0.049  0.001  -0.008 347 PRO CCC CD  
10037 N N   . VAL C 348 ? 0.304 0.537 0.286 0.052  0.000  -0.008 348 VAL CCC N   
10038 C CA  . VAL C 348 ? 0.307 0.543 0.291 0.053  -0.000 -0.008 348 VAL CCC CA  
10039 C C   . VAL C 348 ? 0.293 0.534 0.277 0.053  0.002  -0.006 348 VAL CCC C   
10040 O O   . VAL C 348 ? 0.310 0.557 0.295 0.055  0.002  -0.007 348 VAL CCC O   
10041 C CB  . VAL C 348 ? 0.321 0.552 0.305 0.050  -0.001 -0.006 348 VAL CCC CB  
10042 C CG1 . VAL C 348 ? 0.310 0.543 0.296 0.050  -0.001 -0.006 348 VAL CCC CG1 
10043 C CG2 . VAL C 348 ? 0.341 0.566 0.325 0.049  -0.003 -0.008 348 VAL CCC CG2 
10044 N N   . ALA C 349 ? 0.290 0.532 0.274 0.050  0.004  -0.003 349 ALA CCC N   
10045 C CA  . ALA C 349 ? 0.285 0.534 0.270 0.050  0.005  -0.001 349 ALA CCC CA  
10046 C C   . ALA C 349 ? 0.303 0.559 0.286 0.052  0.005  -0.002 349 ALA CCC C   
10047 O O   . ALA C 349 ? 0.345 0.607 0.329 0.053  0.006  -0.002 349 ALA CCC O   
10048 C CB  . ALA C 349 ? 0.278 0.524 0.263 0.047  0.005  0.002  349 ALA CCC CB  
10049 N N   . VAL C 350 ? 0.316 0.571 0.298 0.053  0.005  -0.003 350 VAL CCC N   
10050 C CA  . VAL C 350 ? 0.312 0.574 0.293 0.055  0.005  -0.005 350 VAL CCC CA  
10051 C C   . VAL C 350 ? 0.313 0.578 0.294 0.058  0.005  -0.009 350 VAL CCC C   
10052 O O   . VAL C 350 ? 0.306 0.582 0.287 0.059  0.006  -0.009 350 VAL CCC O   
10053 C CB  . VAL C 350 ? 0.311 0.568 0.289 0.056  0.004  -0.006 350 VAL CCC CB  
10054 C CG1 . VAL C 350 ? 0.301 0.566 0.278 0.058  0.004  -0.008 350 VAL CCC CG1 
10055 C CG2 . VAL C 350 ? 0.321 0.575 0.299 0.052  0.004  -0.002 350 VAL CCC CG2 
10056 N N   . LYS C 351 ? 0.306 0.566 0.288 0.060  0.003  -0.012 351 LYS CCC N   
10057 C CA  . LYS C 351 ? 0.331 0.594 0.315 0.064  0.001  -0.017 351 LYS CCC CA  
10058 C C   . LYS C 351 ? 0.330 0.599 0.317 0.064  0.002  -0.016 351 LYS CCC C   
10059 O O   . LYS C 351 ? 0.332 0.608 0.320 0.067  0.002  -0.020 351 LYS CCC O   
10060 C CB  . LYS C 351 ? 0.339 0.594 0.325 0.066  -0.002 -0.019 351 LYS CCC CB  
10061 C CG  . LYS C 351 ? 0.356 0.615 0.346 0.070  -0.004 -0.025 351 LYS CCC CG  
10062 C CD  . LYS C 351 ? 0.396 0.648 0.389 0.072  -0.008 -0.027 351 LYS CCC CD  
10063 C CE  . LYS C 351 ? 0.396 0.644 0.386 0.072  -0.008 -0.028 351 LYS CCC CE  
10064 N NZ  . LYS C 351 ? 0.396 0.652 0.386 0.075  -0.007 -0.032 351 LYS CCC NZ  
10065 N N   . ALA C 352 ? 0.344 0.609 0.331 0.061  0.002  -0.013 352 ALA CCC N   
10066 C CA  . ALA C 352 ? 0.366 0.635 0.355 0.061  0.003  -0.012 352 ALA CCC CA  
10067 C C   . ALA C 352 ? 0.360 0.640 0.348 0.061  0.005  -0.011 352 ALA CCC C   
10068 O O   . ALA C 352 ? 0.377 0.664 0.367 0.062  0.006  -0.014 352 ALA CCC O   
10069 C CB  . ALA C 352 ? 0.378 0.641 0.367 0.058  0.003  -0.008 352 ALA CCC CB  
10070 N N   . GLY C 353 ? 0.362 0.643 0.347 0.058  0.007  -0.008 353 GLY CCC N   
10071 C CA  . GLY C 353 ? 0.394 0.686 0.378 0.057  0.009  -0.006 353 GLY CCC CA  
10072 C C   . GLY C 353 ? 0.416 0.717 0.399 0.060  0.009  -0.010 353 GLY CCC C   
10073 O O   . GLY C 353 ? 0.437 0.750 0.421 0.059  0.010  -0.011 353 GLY CCC O   
10074 N N   . ILE C 354 ? 0.409 0.707 0.392 0.062  0.008  -0.014 354 ILE CCC N   
10075 C CA  . ILE C 354 ? 0.437 0.745 0.420 0.065  0.008  -0.019 354 ILE CCC CA  
10076 C C   . ILE C 354 ? 0.458 0.770 0.446 0.068  0.007  -0.025 354 ILE CCC C   
10077 O O   . ILE C 354 ? 0.464 0.789 0.453 0.069  0.008  -0.028 354 ILE CCC O   
10078 C CB  . ILE C 354 ? 0.455 0.757 0.437 0.066  0.006  -0.021 354 ILE CCC CB  
10079 C CG1 . ILE C 354 ? 0.447 0.746 0.424 0.063  0.007  -0.016 354 ILE CCC CG1 
10080 C CG2 . ILE C 354 ? 0.460 0.771 0.442 0.070  0.006  -0.028 354 ILE CCC CG2 
10081 C CD1 . ILE C 354 ? 0.449 0.742 0.425 0.064  0.006  -0.018 354 ILE CCC CD1 
10082 N N   . LEU C 355 ? 0.443 0.745 0.434 0.070  0.005  -0.026 355 LEU CCC N   
10083 C CA  . LEU C 355 ? 0.425 0.730 0.422 0.074  0.003  -0.032 355 LEU CCC CA  
10084 C C   . LEU C 355 ? 0.434 0.748 0.432 0.072  0.005  -0.030 355 LEU CCC C   
10085 O O   . LEU C 355 ? 0.392 0.716 0.394 0.075  0.005  -0.036 355 LEU CCC O   
10086 C CB  . LEU C 355 ? 0.425 0.717 0.424 0.074  -0.001 -0.032 355 LEU CCC CB  
10087 C CG  . LEU C 355 ? 0.424 0.708 0.423 0.076  -0.003 -0.033 355 LEU CCC CG  
10088 C CD1 . LEU C 355 ? 0.423 0.697 0.426 0.076  -0.007 -0.034 355 LEU CCC CD1 
10089 C CD2 . LEU C 355 ? 0.410 0.700 0.410 0.079  -0.004 -0.040 355 LEU CCC CD2 
10090 N N   . LEU C 356 ? 0.414 0.725 0.410 0.068  0.006  -0.024 356 LEU CCC N   
10091 C CA  . LEU C 356 ? 0.403 0.721 0.399 0.067  0.008  -0.022 356 LEU CCC CA  
10092 C C   . LEU C 356 ? 0.404 0.738 0.399 0.066  0.011  -0.024 356 LEU CCC C   
10093 O O   . LEU C 356 ? 0.435 0.780 0.434 0.068  0.011  -0.028 356 LEU CCC O   
10094 C CB  . LEU C 356 ? 0.390 0.703 0.384 0.062  0.009  -0.014 356 LEU CCC CB  
10095 C CG  . LEU C 356 ? 0.407 0.727 0.400 0.060  0.011  -0.011 356 LEU CCC CG  
10096 C CD1 . LEU C 356 ? 0.398 0.721 0.396 0.062  0.010  -0.015 356 LEU CCC CD1 
10097 C CD2 . LEU C 356 ? 0.416 0.731 0.408 0.056  0.012  -0.004 356 LEU CCC CD2 
10098 N N   . ALA C 357 ? 0.388 0.725 0.378 0.064  0.012  -0.020 357 ALA CCC N   
10099 C CA  . ALA C 357 ? 0.414 0.766 0.402 0.063  0.014  -0.022 357 ALA CCC CA  
10100 C C   . ALA C 357 ? 0.423 0.785 0.414 0.067  0.013  -0.031 357 ALA CCC C   
10101 O O   . ALA C 357 ? 0.365 0.742 0.358 0.067  0.015  -0.033 357 ALA CCC O   
10102 C CB  . ALA C 357 ? 0.404 0.753 0.387 0.060  0.014  -0.018 357 ALA CCC CB  
10103 N N   . ARG C 358 ? 0.441 0.796 0.435 0.071  0.011  -0.036 358 ARG CCC N   
10104 C CA  . ARG C 358 ? 0.457 0.820 0.456 0.076  0.010  -0.046 358 ARG CCC CA  
10105 C C   . ARG C 358 ? 0.459 0.827 0.465 0.079  0.009  -0.050 358 ARG CCC C   
10106 O O   . ARG C 358 ? 0.459 0.841 0.468 0.081  0.010  -0.057 358 ARG CCC O   
10107 C CB  . ARG C 358 ? 0.479 0.831 0.480 0.080  0.007  -0.049 358 ARG CCC CB  
10108 C CG  . ARG C 358 ? 0.506 0.858 0.501 0.078  0.007  -0.048 358 ARG CCC CG  
10109 C CD  . ARG C 358 ? 0.538 0.878 0.535 0.081  0.004  -0.051 358 ARG CCC CD  
10110 N NE  . ARG C 358 ? 0.563 0.902 0.555 0.079  0.005  -0.048 358 ARG CCC NE  
10111 C CZ  . ARG C 358 ? 0.558 0.886 0.549 0.080  0.003  -0.048 358 ARG CCC CZ  
10112 N NH1 . ARG C 358 ? 0.576 0.893 0.571 0.083  -0.000 -0.050 358 ARG CCC NH1 
10113 N NH2 . ARG C 358 ? 0.512 0.838 0.497 0.078  0.004  -0.045 358 ARG CCC NH2 
10114 N N   . ARG C 359 ? 0.434 0.790 0.442 0.078  0.007  -0.047 359 ARG CCC N   
10115 C CA  . ARG C 359 ? 0.406 0.763 0.420 0.081  0.006  -0.050 359 ARG CCC CA  
10116 C C   . ARG C 359 ? 0.438 0.811 0.452 0.078  0.010  -0.049 359 ARG CCC C   
10117 O O   . ARG C 359 ? 0.451 0.834 0.471 0.081  0.009  -0.056 359 ARG CCC O   
10118 C CB  . ARG C 359 ? 0.390 0.732 0.406 0.080  0.004  -0.045 359 ARG CCC CB  
10119 C CG  . ARG C 359 ? 0.379 0.707 0.397 0.082  -0.000 -0.047 359 ARG CCC CG  
10120 C CD  . ARG C 359 ? 0.351 0.667 0.372 0.081  -0.003 -0.044 359 ARG CCC CD  
10121 N NE  . ARG C 359 ? 0.332 0.644 0.349 0.077  -0.001 -0.036 359 ARG CCC NE  
10122 C CZ  . ARG C 359 ? 0.340 0.643 0.351 0.074  -0.000 -0.030 359 ARG CCC CZ  
10123 N NH1 . ARG C 359 ? 0.343 0.641 0.352 0.074  -0.001 -0.031 359 ARG CCC NH1 
10124 N NH2 . ARG C 359 ? 0.319 0.620 0.327 0.070  0.002  -0.024 359 ARG CCC NH2 
10125 N N   . LEU C 360 ? 0.471 0.845 0.478 0.073  0.012  -0.042 360 LEU CCC N   
10126 C CA  . LEU C 360 ? 0.501 0.889 0.507 0.070  0.015  -0.039 360 LEU CCC CA  
10127 C C   . LEU C 360 ? 0.519 0.926 0.525 0.071  0.017  -0.045 360 LEU CCC C   
10128 O O   . LEU C 360 ? 0.503 0.924 0.511 0.070  0.019  -0.048 360 LEU CCC O   
10129 C CB  . LEU C 360 ? 0.519 0.902 0.518 0.064  0.017  -0.029 360 LEU CCC CB  
10130 C CG  . LEU C 360 ? 0.535 0.902 0.535 0.063  0.016  -0.023 360 LEU CCC CG  
10131 C CD1 . LEU C 360 ? 0.523 0.887 0.518 0.058  0.017  -0.014 360 LEU CCC CD1 
10132 C CD2 . LEU C 360 ? 0.529 0.898 0.534 0.064  0.015  -0.025 360 LEU CCC CD2 
10133 N N   . PHE C 361 ? 0.499 0.907 0.501 0.071  0.017  -0.047 361 PHE CCC N   
10134 C CA  . PHE C 361 ? 0.520 0.948 0.520 0.069  0.020  -0.049 361 PHE CCC CA  
10135 C C   . PHE C 361 ? 0.541 0.975 0.544 0.074  0.019  -0.059 361 PHE CCC C   
10136 O O   . PHE C 361 ? 0.613 1.064 0.613 0.072  0.021  -0.063 361 PHE CCC O   
10137 C CB  . PHE C 361 ? 0.495 0.921 0.486 0.063  0.021  -0.040 361 PHE CCC CB  
10138 C CG  . PHE C 361 ? 0.494 0.917 0.483 0.058  0.022  -0.031 361 PHE CCC CG  
10139 C CD1 . PHE C 361 ? 0.500 0.936 0.490 0.056  0.024  -0.030 361 PHE CCC CD1 
10140 C CD2 . PHE C 361 ? 0.492 0.899 0.478 0.056  0.021  -0.022 361 PHE CCC CD2 
10141 C CE1 . PHE C 361 ? 0.491 0.924 0.480 0.052  0.024  -0.022 361 PHE CCC CE1 
10142 C CE2 . PHE C 361 ? 0.493 0.898 0.478 0.051  0.021  -0.014 361 PHE CCC CE2 
10143 C CZ  . PHE C 361 ? 0.510 0.927 0.496 0.050  0.023  -0.014 361 PHE CCC CZ  
10144 N N   . ALA C 362 ? 0.550 0.970 0.557 0.079  0.015  -0.064 362 ALA CCC N   
10145 C CA  . ALA C 362 ? 0.557 0.981 0.567 0.083  0.014  -0.073 362 ALA CCC CA  
10146 C C   . ALA C 362 ? 0.533 0.951 0.554 0.089  0.010  -0.081 362 ALA CCC C   
10147 O O   . ALA C 362 ? 0.520 0.933 0.545 0.093  0.007  -0.087 362 ALA CCC O   
10148 C CB  . ALA C 362 ? 0.588 1.001 0.593 0.083  0.013  -0.070 362 ALA CCC CB  
10149 N N   . GLY C 363 ? 0.540 0.958 0.566 0.090  0.009  -0.081 363 GLY CCC N   
10150 C CA  . GLY C 363 ? 0.556 0.969 0.592 0.095  0.005  -0.088 363 GLY CCC CA  
10151 C C   . GLY C 363 ? 0.569 0.963 0.608 0.098  0.000  -0.087 363 GLY CCC C   
10152 O O   . GLY C 363 ? 0.574 0.965 0.622 0.102  -0.004 -0.095 363 GLY CCC O   
10153 N N   . SER C 364 ? 0.583 0.962 0.614 0.094  0.001  -0.078 364 SER CCC N   
10154 C CA  . SER C 364 ? 0.552 0.913 0.585 0.095  -0.004 -0.076 364 SER CCC CA  
10155 C C   . SER C 364 ? 0.531 0.881 0.567 0.095  -0.006 -0.072 364 SER CCC C   
10156 O O   . SER C 364 ? 0.536 0.891 0.571 0.092  -0.003 -0.069 364 SER CCC O   
10157 C CB  . SER C 364 ? 0.544 0.896 0.567 0.092  -0.002 -0.068 364 SER CCC CB  
10158 O OG  . SER C 364 ? 0.539 0.873 0.562 0.091  -0.005 -0.064 364 SER CCC OG  
10159 N N   . ASN C 365 ? 0.525 0.861 0.566 0.097  -0.011 -0.073 365 ASN CCC N   
10160 C CA  . ASN C 365 ? 0.580 0.905 0.623 0.095  -0.014 -0.068 365 ASN CCC CA  
10161 C C   . ASN C 365 ? 0.570 0.878 0.610 0.093  -0.017 -0.062 365 ASN CCC C   
10162 O O   . ASN C 365 ? 0.598 0.896 0.641 0.093  -0.021 -0.060 365 ASN CCC O   
10163 C CB  . ASN C 365 ? 0.601 0.929 0.656 0.099  -0.018 -0.075 365 ASN CCC CB  
10164 C CG  . ASN C 365 ? 0.665 0.990 0.720 0.097  -0.018 -0.070 365 ASN CCC CG  
10165 O OD1 . ASN C 365 ? 0.709 1.021 0.765 0.096  -0.022 -0.065 365 ASN CCC OD1 
10166 N ND2 . ASN C 365 ? 0.662 0.999 0.716 0.096  -0.014 -0.070 365 ASN CCC ND2 
10167 N N   . GLU C 366 ? 0.580 0.886 0.612 0.092  -0.014 -0.059 366 GLU CCC N   
10168 C CA  . GLU C 366 ? 0.581 0.873 0.610 0.090  -0.016 -0.055 366 GLU CCC CA  
10169 C C   . GLU C 366 ? 0.533 0.819 0.555 0.085  -0.014 -0.046 366 GLU CCC C   
10170 O O   . GLU C 366 ? 0.479 0.771 0.496 0.082  -0.009 -0.043 366 GLU CCC O   
10171 C CB  . GLU C 366 ? 0.646 0.940 0.672 0.091  -0.015 -0.057 366 GLU CCC CB  
10172 C CG  . GLU C 366 ? 0.675 0.971 0.709 0.096  -0.020 -0.066 366 GLU CCC CG  
10173 C CD  . GLU C 366 ? 0.693 0.984 0.723 0.097  -0.021 -0.066 366 GLU CCC CD  
10174 O OE1 . GLU C 366 ? 0.715 1.016 0.743 0.098  -0.018 -0.070 366 GLU CCC OE1 
10175 O OE2 . GLU C 366 ? 0.702 0.980 0.733 0.095  -0.024 -0.063 366 GLU CCC OE2 
10176 N N   . PHE C 367 ? 0.522 0.796 0.545 0.083  -0.017 -0.042 367 PHE CCC N   
10177 C CA  . PHE C 367 ? 0.490 0.756 0.507 0.078  -0.015 -0.034 367 PHE CCC CA  
10178 C C   . PHE C 367 ? 0.460 0.716 0.474 0.076  -0.017 -0.032 367 PHE CCC C   
10179 O O   . PHE C 367 ? 0.414 0.668 0.432 0.079  -0.021 -0.036 367 PHE CCC O   
10180 C CB  . PHE C 367 ? 0.486 0.748 0.506 0.076  -0.017 -0.032 367 PHE CCC CB  
10181 C CG  . PHE C 367 ? 0.490 0.762 0.512 0.077  -0.015 -0.033 367 PHE CCC CG  
10182 C CD1 . PHE C 367 ? 0.476 0.756 0.505 0.081  -0.017 -0.039 367 PHE CCC CD1 
10183 C CD2 . PHE C 367 ? 0.489 0.763 0.506 0.073  -0.011 -0.028 367 PHE CCC CD2 
10184 C CE1 . PHE C 367 ? 0.442 0.731 0.473 0.081  -0.014 -0.041 367 PHE CCC CE1 
10185 C CE2 . PHE C 367 ? 0.484 0.767 0.503 0.074  -0.008 -0.029 367 PHE CCC CE2 
10186 C CZ  . PHE C 367 ? 0.437 0.728 0.462 0.078  -0.010 -0.035 367 PHE CCC CZ  
10187 N N   . ILE C 368 ? 0.452 0.703 0.460 0.072  -0.015 -0.027 368 ILE CCC N   
10188 C CA  . ILE C 368 ? 0.440 0.682 0.445 0.069  -0.016 -0.024 368 ILE CCC CA  
10189 C C   . ILE C 368 ? 0.412 0.646 0.421 0.068  -0.022 -0.023 368 ILE CCC C   
10190 O O   . ILE C 368 ? 0.338 0.572 0.349 0.068  -0.023 -0.022 368 ILE CCC O   
10191 C CB  . ILE C 368 ? 0.443 0.683 0.442 0.065  -0.012 -0.019 368 ILE CCC CB  
10192 C CG1 . ILE C 368 ? 0.452 0.698 0.448 0.066  -0.008 -0.020 368 ILE CCC CG1 
10193 C CG2 . ILE C 368 ? 0.434 0.665 0.431 0.062  -0.014 -0.017 368 ILE CCC CG2 
10194 C CD1 . ILE C 368 ? 0.455 0.700 0.447 0.062  -0.005 -0.015 368 ILE CCC CD1 
10195 N N   . ASP C 369 ? 0.413 0.641 0.423 0.068  -0.025 -0.024 369 ASP CCC N   
10196 C CA  . ASP C 369 ? 0.413 0.633 0.425 0.066  -0.030 -0.021 369 ASP CCC CA  
10197 C C   . ASP C 369 ? 0.430 0.645 0.435 0.060  -0.028 -0.016 369 ASP CCC C   
10198 O O   . ASP C 369 ? 0.413 0.625 0.414 0.059  -0.027 -0.015 369 ASP CCC O   
10199 C CB  . ASP C 369 ? 0.400 0.616 0.416 0.068  -0.035 -0.024 369 ASP CCC CB  
10200 C CG  . ASP C 369 ? 0.416 0.624 0.436 0.066  -0.042 -0.021 369 ASP CCC CG  
10201 O OD1 . ASP C 369 ? 0.432 0.637 0.450 0.061  -0.042 -0.016 369 ASP CCC OD1 
10202 O OD2 . ASP C 369 ? 0.420 0.624 0.445 0.068  -0.047 -0.024 369 ASP CCC OD2 
10203 N N   . TYR C 370 ? 0.454 0.669 0.458 0.056  -0.027 -0.012 370 TYR CCC N   
10204 C CA  . TYR C 370 ? 0.437 0.651 0.436 0.051  -0.024 -0.008 370 TYR CCC CA  
10205 C C   . TYR C 370 ? 0.488 0.695 0.486 0.047  -0.028 -0.005 370 TYR CCC C   
10206 O O   . TYR C 370 ? 0.462 0.668 0.455 0.042  -0.026 -0.003 370 TYR CCC O   
10207 C CB  . TYR C 370 ? 0.395 0.612 0.393 0.049  -0.022 -0.006 370 TYR CCC CB  
10208 C CG  . TYR C 370 ? 0.398 0.621 0.395 0.051  -0.017 -0.007 370 TYR CCC CG  
10209 C CD1 . TYR C 370 ? 0.389 0.613 0.382 0.050  -0.013 -0.007 370 TYR CCC CD1 
10210 C CD2 . TYR C 370 ? 0.390 0.618 0.391 0.054  -0.017 -0.009 370 TYR CCC CD2 
10211 C CE1 . TYR C 370 ? 0.371 0.602 0.364 0.052  -0.009 -0.007 370 TYR CCC CE1 
10212 C CE2 . TYR C 370 ? 0.398 0.632 0.397 0.056  -0.013 -0.010 370 TYR CCC CE2 
10213 C CZ  . TYR C 370 ? 0.411 0.646 0.406 0.054  -0.009 -0.008 370 TYR CCC CZ  
10214 O OH  . TYR C 370 ? 0.462 0.704 0.457 0.055  -0.005 -0.008 370 TYR CCC OH  
10215 N N   . ASP C 371 ? 0.547 0.751 0.550 0.048  -0.034 -0.006 371 ASP CCC N   
10216 C CA  . ASP C 371 ? 0.554 0.751 0.556 0.044  -0.039 -0.003 371 ASP CCC CA  
10217 C C   . ASP C 371 ? 0.546 0.742 0.544 0.044  -0.037 -0.004 371 ASP CCC C   
10218 O O   . ASP C 371 ? 0.577 0.769 0.573 0.039  -0.039 -0.002 371 ASP CCC O   
10219 C CB  . ASP C 371 ? 0.572 0.765 0.581 0.046  -0.046 -0.004 371 ASP CCC CB  
10220 C CG  . ASP C 371 ? 0.603 0.797 0.616 0.045  -0.049 -0.002 371 ASP CCC CG  
10221 O OD1 . ASP C 371 ? 0.570 0.765 0.579 0.041  -0.047 0.002  371 ASP CCC OD1 
10222 O OD2 . ASP C 371 ? 0.656 0.850 0.677 0.049  -0.054 -0.005 371 ASP CCC OD2 
10223 N N   . PHE C 372 ? 0.505 0.704 0.503 0.049  -0.034 -0.008 372 PHE CCC N   
10224 C CA  . PHE C 372 ? 0.479 0.677 0.475 0.050  -0.033 -0.010 372 PHE CCC CA  
10225 C C   . PHE C 372 ? 0.439 0.640 0.430 0.050  -0.026 -0.011 372 PHE CCC C   
10226 O O   . PHE C 372 ? 0.482 0.686 0.474 0.055  -0.025 -0.014 372 PHE CCC O   
10227 C CB  . PHE C 372 ? 0.497 0.693 0.498 0.055  -0.037 -0.014 372 PHE CCC CB  
10228 C CG  . PHE C 372 ? 0.519 0.709 0.525 0.053  -0.044 -0.012 372 PHE CCC CG  
10229 C CD1 . PHE C 372 ? 0.500 0.685 0.504 0.048  -0.048 -0.009 372 PHE CCC CD1 
10230 C CD2 . PHE C 372 ? 0.536 0.726 0.548 0.056  -0.049 -0.014 372 PHE CCC CD2 
10231 C CE1 . PHE C 372 ? 0.520 0.700 0.529 0.047  -0.055 -0.006 372 PHE CCC CE1 
10232 C CE2 . PHE C 372 ? 0.546 0.730 0.564 0.054  -0.056 -0.012 372 PHE CCC CE2 
10233 C CZ  . PHE C 372 ? 0.524 0.703 0.540 0.050  -0.060 -0.008 372 PHE CCC CZ  
10234 N N   . VAL C 373 ? 0.410 0.613 0.398 0.046  -0.023 -0.009 373 VAL CCC N   
10235 C CA  . VAL C 373 ? 0.390 0.596 0.375 0.046  -0.018 -0.009 373 VAL CCC CA  
10236 C C   . VAL C 373 ? 0.364 0.568 0.347 0.042  -0.017 -0.008 373 VAL CCC C   
10237 O O   . VAL C 373 ? 0.400 0.604 0.381 0.037  -0.017 -0.006 373 VAL CCC O   
10238 C CB  . VAL C 373 ? 0.372 0.582 0.357 0.044  -0.015 -0.007 373 VAL CCC CB  
10239 C CG1 . VAL C 373 ? 0.360 0.573 0.343 0.044  -0.010 -0.008 373 VAL CCC CG1 
10240 C CG2 . VAL C 373 ? 0.370 0.583 0.358 0.048  -0.015 -0.009 373 VAL CCC CG2 
10241 N N   . PRO C 374 ? 0.348 0.550 0.329 0.044  -0.016 -0.010 374 PRO CCC N   
10242 C CA  . PRO C 374 ? 0.351 0.551 0.330 0.040  -0.016 -0.010 374 PRO CCC CA  
10243 C C   . PRO C 374 ? 0.355 0.559 0.333 0.039  -0.011 -0.010 374 PRO CCC C   
10244 O O   . PRO C 374 ? 0.347 0.553 0.326 0.041  -0.009 -0.011 374 PRO CCC O   
10245 C CB  . PRO C 374 ? 0.330 0.529 0.310 0.044  -0.017 -0.012 374 PRO CCC CB  
10246 C CG  . PRO C 374 ? 0.339 0.541 0.320 0.049  -0.016 -0.014 374 PRO CCC CG  
10247 C CD  . PRO C 374 ? 0.348 0.552 0.331 0.049  -0.017 -0.013 374 PRO CCC CD  
10248 N N   . THR C 375 ? 0.366 0.570 0.343 0.035  -0.010 -0.010 375 THR CCC N   
10249 C CA  . THR C 375 ? 0.386 0.593 0.364 0.033  -0.007 -0.012 375 THR CCC CA  
10250 C C   . THR C 375 ? 0.339 0.545 0.316 0.031  -0.006 -0.013 375 THR CCC C   
10251 O O   . THR C 375 ? 0.338 0.542 0.313 0.029  -0.009 -0.013 375 THR CCC O   
10252 C CB  . THR C 375 ? 0.443 0.653 0.421 0.030  -0.005 -0.010 375 THR CCC CB  
10253 O OG1 . THR C 375 ? 0.512 0.725 0.491 0.028  -0.003 -0.012 375 THR CCC OG1 
10254 C CG2 . THR C 375 ? 0.448 0.658 0.424 0.025  -0.008 -0.009 375 THR CCC CG2 
10255 N N   . THR C 376 ? 0.314 0.521 0.292 0.032  -0.004 -0.015 376 THR CCC N   
10256 C CA  . THR C 376 ? 0.309 0.517 0.288 0.029  -0.003 -0.018 376 THR CCC CA  
10257 C C   . THR C 376 ? 0.281 0.492 0.263 0.027  -0.001 -0.020 376 THR CCC C   
10258 O O   . THR C 376 ? 0.251 0.463 0.235 0.029  0.000  -0.019 376 THR CCC O   
10259 C CB  . THR C 376 ? 0.305 0.510 0.284 0.032  -0.004 -0.019 376 THR CCC CB  
10260 O OG1 . THR C 376 ? 0.307 0.508 0.284 0.034  -0.006 -0.018 376 THR CCC OG1 
10261 C CG2 . THR C 376 ? 0.313 0.519 0.293 0.030  -0.003 -0.022 376 THR CCC CG2 
10262 N N   . VAL C 377 ? 0.270 0.484 0.252 0.022  -0.000 -0.022 377 VAL CCC N   
10263 C CA  . VAL C 377 ? 0.262 0.481 0.248 0.020  0.002  -0.025 377 VAL CCC CA  
10264 C C   . VAL C 377 ? 0.265 0.483 0.254 0.021  0.002  -0.029 377 VAL CCC C   
10265 O O   . VAL C 377 ? 0.253 0.470 0.239 0.019  0.001  -0.029 377 VAL CCC O   
10266 C CB  . VAL C 377 ? 0.270 0.494 0.256 0.014  0.002  -0.026 377 VAL CCC CB  
10267 C CG1 . VAL C 377 ? 0.270 0.500 0.260 0.012  0.004  -0.031 377 VAL CCC CG1 
10268 C CG2 . VAL C 377 ? 0.261 0.486 0.244 0.013  0.002  -0.022 377 VAL CCC CG2 
10269 N N   . PHE C 378 ? 0.252 0.470 0.246 0.023  0.003  -0.030 378 PHE CCC N   
10270 C CA  . PHE C 378 ? 0.253 0.470 0.250 0.024  0.003  -0.033 378 PHE CCC CA  
10271 C C   . PHE C 378 ? 0.245 0.467 0.248 0.021  0.004  -0.039 378 PHE CCC C   
10272 O O   . PHE C 378 ? 0.227 0.449 0.235 0.022  0.004  -0.042 378 PHE CCC O   
10273 C CB  . PHE C 378 ? 0.257 0.470 0.256 0.028  0.002  -0.032 378 PHE CCC CB  
10274 C CG  . PHE C 378 ? 0.244 0.453 0.238 0.032  0.001  -0.027 378 PHE CCC CG  
10275 C CD1 . PHE C 378 ? 0.239 0.445 0.231 0.033  -0.000 -0.027 378 PHE CCC CD1 
10276 C CD2 . PHE C 378 ? 0.239 0.449 0.232 0.033  0.001  -0.024 378 PHE CCC CD2 
10277 C CE1 . PHE C 378 ? 0.242 0.446 0.230 0.037  -0.001 -0.024 378 PHE CCC CE1 
10278 C CE2 . PHE C 378 ? 0.241 0.449 0.230 0.036  0.000  -0.021 378 PHE CCC CE2 
10279 C CZ  . PHE C 378 ? 0.244 0.449 0.231 0.038  -0.001 -0.022 378 PHE CCC CZ  
10280 N N   . THR C 379 ? 0.238 0.464 0.237 0.016  0.004  -0.040 379 THR CCC N   
10281 C CA  . THR C 379 ? 0.244 0.477 0.248 0.012  0.006  -0.046 379 THR CCC CA  
10282 C C   . THR C 379 ? 0.237 0.469 0.242 0.013  0.005  -0.049 379 THR CCC C   
10283 O O   . THR C 379 ? 0.229 0.455 0.230 0.015  0.004  -0.046 379 THR CCC O   
10284 C CB  . THR C 379 ? 0.247 0.486 0.247 0.007  0.006  -0.046 379 THR CCC CB  
10285 O OG1 . THR C 379 ? 0.235 0.470 0.228 0.007  0.005  -0.040 379 THR CCC OG1 
10286 C CG2 . THR C 379 ? 0.250 0.492 0.252 0.006  0.008  -0.046 379 THR CCC CG2 
10287 N N   . PRO C 380 ? 0.237 0.475 0.247 0.010  0.006  -0.055 380 PRO CCC N   
10288 C CA  . PRO C 380 ? 0.243 0.480 0.255 0.011  0.006  -0.059 380 PRO CCC CA  
10289 C C   . PRO C 380 ? 0.253 0.488 0.258 0.010  0.005  -0.055 380 PRO CCC C   
10290 O O   . PRO C 380 ? 0.319 0.549 0.325 0.013  0.004  -0.055 380 PRO CCC O   
10291 C CB  . PRO C 380 ? 0.234 0.482 0.253 0.007  0.007  -0.066 380 PRO CCC CB  
10292 C CG  . PRO C 380 ? 0.237 0.487 0.260 0.006  0.008  -0.068 380 PRO CCC CG  
10293 C CD  . PRO C 380 ? 0.241 0.488 0.257 0.007  0.008  -0.061 380 PRO CCC CD  
10294 N N   . ILE C 381 ? 0.266 0.503 0.265 0.006  0.005  -0.052 381 ILE CCC N   
10295 C CA  . ILE C 381 ? 0.271 0.503 0.263 0.006  0.003  -0.046 381 ILE CCC CA  
10296 C C   . ILE C 381 ? 0.259 0.488 0.248 0.008  0.002  -0.041 381 ILE CCC C   
10297 O O   . ILE C 381 ? 0.240 0.473 0.229 0.005  0.003  -0.042 381 ILE CCC O   
10298 C CB  . ILE C 381 ? 0.292 0.529 0.280 0.000  0.002  -0.045 381 ILE CCC CB  
10299 C CG1 . ILE C 381 ? 0.296 0.542 0.283 -0.006 0.004  -0.047 381 ILE CCC CG1 
10300 C CG2 . ILE C 381 ? 0.296 0.536 0.286 -0.001 0.002  -0.050 381 ILE CCC CG2 
10301 C CD1 . ILE C 381 ? 0.314 0.567 0.297 -0.013 0.003  -0.046 381 ILE CCC CD1 
10302 N N   . GLU C 382 ? 0.265 0.486 0.251 0.012  0.000  -0.037 382 GLU CCC N   
10303 C CA  . GLU C 382 ? 0.271 0.488 0.256 0.015  -0.000 -0.033 382 GLU CCC CA  
10304 C C   . GLU C 382 ? 0.255 0.473 0.235 0.012  -0.002 -0.029 382 GLU CCC C   
10305 O O   . GLU C 382 ? 0.271 0.490 0.249 0.009  -0.004 -0.028 382 GLU CCC O   
10306 C CB  . GLU C 382 ? 0.279 0.490 0.264 0.021  -0.001 -0.031 382 GLU CCC CB  
10307 C CG  . GLU C 382 ? 0.290 0.501 0.279 0.024  -0.001 -0.034 382 GLU CCC CG  
10308 C CD  . GLU C 382 ? 0.300 0.505 0.288 0.029  -0.002 -0.032 382 GLU CCC CD  
10309 O OE1 . GLU C 382 ? 0.318 0.520 0.303 0.031  -0.003 -0.029 382 GLU CCC OE1 
10310 O OE2 . GLU C 382 ? 0.307 0.512 0.299 0.031  -0.001 -0.034 382 GLU CCC OE2 
10311 N N   . TYR C 383 ? 0.240 0.456 0.219 0.013  -0.002 -0.026 383 TYR CCC N   
10312 C CA  . TYR C 383 ? 0.256 0.472 0.231 0.011  -0.005 -0.022 383 TYR CCC CA  
10313 C C   . TYR C 383 ? 0.239 0.450 0.214 0.016  -0.006 -0.019 383 TYR CCC C   
10314 O O   . TYR C 383 ? 0.219 0.431 0.196 0.018  -0.005 -0.019 383 TYR CCC O   
10315 C CB  . TYR C 383 ? 0.265 0.488 0.239 0.005  -0.004 -0.022 383 TYR CCC CB  
10316 C CG  . TYR C 383 ? 0.286 0.508 0.258 0.002  -0.007 -0.017 383 TYR CCC CG  
10317 C CD1 . TYR C 383 ? 0.297 0.515 0.267 0.002  -0.010 -0.014 383 TYR CCC CD1 
10318 C CD2 . TYR C 383 ? 0.287 0.513 0.259 0.000  -0.006 -0.016 383 TYR CCC CD2 
10319 C CE1 . TYR C 383 ? 0.300 0.517 0.268 -0.000 -0.014 -0.009 383 TYR CCC CE1 
10320 C CE2 . TYR C 383 ? 0.299 0.523 0.269 -0.002 -0.009 -0.012 383 TYR CCC CE2 
10321 C CZ  . TYR C 383 ? 0.306 0.526 0.274 -0.002 -0.013 -0.008 383 TYR CCC CZ  
10322 O OH  . TYR C 383 ? 0.283 0.501 0.249 -0.005 -0.017 -0.004 383 TYR CCC OH  
10323 N N   . GLY C 384 ? 0.234 0.441 0.208 0.018  -0.010 -0.017 384 GLY CCC N   
10324 C CA  . GLY C 384 ? 0.245 0.447 0.218 0.022  -0.011 -0.015 384 GLY CCC CA  
10325 C C   . GLY C 384 ? 0.251 0.452 0.223 0.020  -0.015 -0.011 384 GLY CCC C   
10326 O O   . GLY C 384 ? 0.254 0.455 0.225 0.016  -0.018 -0.010 384 GLY CCC O   
10327 N N   . HIS C 385 ? 0.244 0.445 0.217 0.022  -0.016 -0.009 385 HIS CCC N   
10328 C CA  . HIS C 385 ? 0.261 0.460 0.234 0.020  -0.021 -0.006 385 HIS CCC CA  
10329 C C   . HIS C 385 ? 0.274 0.470 0.249 0.025  -0.022 -0.006 385 HIS CCC C   
10330 O O   . HIS C 385 ? 0.273 0.472 0.249 0.029  -0.018 -0.007 385 HIS CCC O   
10331 C CB  . HIS C 385 ? 0.253 0.455 0.224 0.013  -0.020 -0.004 385 HIS CCC CB  
10332 C CG  . HIS C 385 ? 0.250 0.456 0.223 0.013  -0.019 -0.003 385 HIS CCC CG  
10333 N ND1 . HIS C 385 ? 0.244 0.453 0.216 0.013  -0.014 -0.005 385 HIS CCC ND1 
10334 C CD2 . HIS C 385 ? 0.249 0.453 0.222 0.014  -0.021 -0.000 385 HIS CCC CD2 
10335 C CE1 . HIS C 385 ? 0.240 0.450 0.213 0.014  -0.014 -0.004 385 HIS CCC CE1 
10336 N NE2 . HIS C 385 ? 0.235 0.442 0.209 0.014  -0.018 -0.001 385 HIS CCC NE2 
10337 N N   . VAL C 386 ? 0.292 0.485 0.269 0.025  -0.027 -0.003 386 VAL CCC N   
10338 C CA  . VAL C 386 ? 0.308 0.500 0.287 0.029  -0.029 -0.003 386 VAL CCC CA  
10339 C C   . VAL C 386 ? 0.334 0.525 0.315 0.024  -0.034 0.001  386 VAL CCC C   
10340 O O   . VAL C 386 ? 0.328 0.516 0.308 0.020  -0.038 0.003  386 VAL CCC O   
10341 C CB  . VAL C 386 ? 0.307 0.497 0.290 0.035  -0.030 -0.006 386 VAL CCC CB  
10342 C CG1 . VAL C 386 ? 0.306 0.491 0.291 0.035  -0.036 -0.005 386 VAL CCC CG1 
10343 C CG2 . VAL C 386 ? 0.307 0.498 0.293 0.040  -0.031 -0.007 386 VAL CCC CG2 
10344 N N   . GLY C 387 ? 0.332 0.523 0.314 0.025  -0.035 0.002  387 GLY CCC N   
10345 C CA  . GLY C 387 ? 0.358 0.548 0.343 0.021  -0.040 0.006  387 GLY CCC CA  
10346 C C   . GLY C 387 ? 0.390 0.583 0.371 0.014  -0.039 0.009  387 GLY CCC C   
10347 O O   . GLY C 387 ? 0.363 0.561 0.341 0.013  -0.033 0.008  387 GLY CCC O   
10348 N N   . LEU C 388 ? 0.419 0.611 0.400 0.008  -0.044 0.014  388 LEU CCC N   
10349 C CA  . LEU C 388 ? 0.426 0.622 0.403 0.000  -0.044 0.017  388 LEU CCC CA  
10350 C C   . LEU C 388 ? 0.427 0.627 0.400 -0.006 -0.042 0.018  388 LEU CCC C   
10351 O O   . LEU C 388 ? 0.381 0.578 0.354 -0.006 -0.045 0.018  388 LEU CCC O   
10352 C CB  . LEU C 388 ? 0.440 0.633 0.420 -0.003 -0.052 0.023  388 LEU CCC CB  
10353 C CG  . LEU C 388 ? 0.451 0.640 0.436 0.003  -0.055 0.022  388 LEU CCC CG  
10354 C CD1 . LEU C 388 ? 0.465 0.650 0.454 -0.001 -0.063 0.028  388 LEU CCC CD1 
10355 C CD2 . LEU C 388 ? 0.433 0.626 0.418 0.005  -0.049 0.020  388 LEU CCC CD2 
10356 N N   . SER C 389 ? 0.425 0.632 0.395 -0.011 -0.038 0.017  389 SER CCC N   
10357 C CA  . SER C 389 ? 0.430 0.643 0.395 -0.019 -0.037 0.018  389 SER CCC CA  
10358 C C   . SER C 389 ? 0.435 0.647 0.400 -0.026 -0.044 0.025  389 SER CCC C   
10359 O O   . SER C 389 ? 0.397 0.604 0.365 -0.025 -0.049 0.028  389 SER CCC O   
10360 C CB  . SER C 389 ? 0.440 0.661 0.403 -0.022 -0.032 0.016  389 SER CCC CB  
10361 O OG  . SER C 389 ? 0.466 0.688 0.430 -0.024 -0.034 0.019  389 SER CCC OG  
10362 N N   . SER C 390 ? 0.436 0.653 0.397 -0.033 -0.045 0.026  390 SER CCC N   
10363 C CA  . SER C 390 ? 0.452 0.671 0.411 -0.042 -0.051 0.033  390 SER CCC CA  
10364 C C   . SER C 390 ? 0.451 0.673 0.410 -0.046 -0.052 0.036  390 SER CCC C   
10365 O O   . SER C 390 ? 0.461 0.679 0.422 -0.048 -0.059 0.042  390 SER CCC O   
10366 C CB  . SER C 390 ? 0.432 0.660 0.387 -0.050 -0.049 0.032  390 SER CCC CB  
10367 O OG  . SER C 390 ? 0.410 0.634 0.366 -0.046 -0.048 0.029  390 SER CCC OG  
10368 N N   . GLU C 391 ? 0.468 0.697 0.424 -0.046 -0.045 0.032  391 GLU CCC N   
10369 C CA  . GLU C 391 ? 0.480 0.714 0.436 -0.050 -0.045 0.034  391 GLU CCC CA  
10370 C C   . GLU C 391 ? 0.508 0.733 0.469 -0.044 -0.049 0.037  391 GLU CCC C   
10371 O O   . GLU C 391 ? 0.527 0.751 0.487 -0.049 -0.055 0.043  391 GLU CCC O   
10372 C CB  . GLU C 391 ? 0.458 0.700 0.411 -0.050 -0.037 0.028  391 GLU CCC CB  
10373 C CG  . GLU C 391 ? 0.479 0.732 0.428 -0.058 -0.034 0.026  391 GLU CCC CG  
10374 C CD  . GLU C 391 ? 0.498 0.751 0.448 -0.055 -0.032 0.022  391 GLU CCC CD  
10375 O OE1 . GLU C 391 ? 0.449 0.695 0.402 -0.046 -0.029 0.018  391 GLU CCC OE1 
10376 O OE2 . GLU C 391 ? 0.495 0.754 0.442 -0.062 -0.033 0.023  391 GLU CCC OE2 
10377 N N   . ALA C 392 ? 0.492 0.711 0.456 -0.035 -0.047 0.032  392 ALA CCC N   
10378 C CA  . ALA C 392 ? 0.484 0.697 0.452 -0.028 -0.050 0.033  392 ALA CCC CA  
10379 C C   . ALA C 392 ? 0.494 0.700 0.467 -0.028 -0.058 0.038  392 ALA CCC C   
10380 O O   . ALA C 392 ? 0.517 0.718 0.494 -0.027 -0.063 0.041  392 ALA CCC O   
10381 C CB  . ALA C 392 ? 0.452 0.663 0.423 -0.019 -0.044 0.027  392 ALA CCC CB  
10382 N N   . ALA C 393 ? 0.480 0.683 0.452 -0.030 -0.061 0.038  393 ALA CCC N   
10383 C CA  . ALA C 393 ? 0.503 0.699 0.480 -0.030 -0.070 0.043  393 ALA CCC CA  
10384 C C   . ALA C 393 ? 0.540 0.737 0.515 -0.040 -0.077 0.050  393 ALA CCC C   
10385 O O   . ALA C 393 ? 0.565 0.756 0.546 -0.039 -0.084 0.054  393 ALA CCC O   
10386 C CB  . ALA C 393 ? 0.475 0.669 0.451 -0.029 -0.070 0.041  393 ALA CCC CB  
10387 N N   . ILE C 394 ? 0.550 0.756 0.519 -0.049 -0.074 0.052  394 ILE CCC N   
10388 C CA  . ILE C 394 ? 0.593 0.803 0.559 -0.060 -0.080 0.060  394 ILE CCC CA  
10389 C C   . ILE C 394 ? 0.591 0.802 0.560 -0.060 -0.081 0.062  394 ILE CCC C   
10390 O O   . ILE C 394 ? 0.588 0.793 0.559 -0.063 -0.090 0.069  394 ILE CCC O   
10391 C CB  . ILE C 394 ? 0.591 0.812 0.549 -0.069 -0.075 0.060  394 ILE CCC CB  
10392 C CG1 . ILE C 394 ? 0.619 0.840 0.577 -0.070 -0.077 0.060  394 ILE CCC CG1 
10393 C CG2 . ILE C 394 ? 0.589 0.818 0.544 -0.080 -0.079 0.067  394 ILE CCC CG2 
10394 C CD1 . ILE C 394 ? 0.626 0.858 0.577 -0.078 -0.072 0.059  394 ILE CCC CD1 
10395 N N   . ALA C 395 ? 0.555 0.769 0.522 -0.055 -0.073 0.057  395 ALA CCC N   
10396 C CA  . ALA C 395 ? 0.557 0.771 0.525 -0.054 -0.074 0.058  395 ALA CCC CA  
10397 C C   . ALA C 395 ? 0.561 0.765 0.538 -0.048 -0.080 0.059  395 ALA CCC C   
10398 O O   . ALA C 395 ? 0.586 0.788 0.565 -0.051 -0.086 0.064  395 ALA CCC O   
10399 C CB  . ALA C 395 ? 0.543 0.762 0.510 -0.049 -0.064 0.051  395 ALA CCC CB  
10400 N N   . LYS C 396 ? 0.591 0.788 0.572 -0.039 -0.080 0.055  396 LYS CCC N   
10401 C CA  . LYS C 396 ? 0.586 0.775 0.576 -0.031 -0.085 0.054  396 LYS CCC CA  
10402 C C   . LYS C 396 ? 0.583 0.765 0.579 -0.034 -0.097 0.060  396 LYS CCC C   
10403 O O   . LYS C 396 ? 0.556 0.734 0.559 -0.033 -0.103 0.062  396 LYS CCC O   
10404 C CB  . LYS C 396 ? 0.616 0.802 0.608 -0.021 -0.080 0.047  396 LYS CCC CB  
10405 C CG  . LYS C 396 ? 0.629 0.809 0.631 -0.013 -0.084 0.044  396 LYS CCC CG  
10406 C CD  . LYS C 396 ? 0.653 0.832 0.656 -0.003 -0.080 0.037  396 LYS CCC CD  
10407 C CE  . LYS C 396 ? 0.701 0.875 0.714 0.005  -0.084 0.033  396 LYS CCC CE  
10408 N NZ  . LYS C 396 ? 0.730 0.906 0.746 0.007  -0.084 0.032  396 LYS CCC NZ  
10409 N N   . TYR C 397 ? 0.612 0.793 0.606 -0.039 -0.100 0.063  397 TYR CCC N   
10410 C CA  . TYR C 397 ? 0.604 0.777 0.604 -0.041 -0.111 0.068  397 TYR CCC CA  
10411 C C   . TYR C 397 ? 0.581 0.758 0.578 -0.053 -0.117 0.077  397 TYR CCC C   
10412 O O   . TYR C 397 ? 0.518 0.689 0.521 -0.057 -0.128 0.083  397 TYR CCC O   
10413 C CB  . TYR C 397 ? 0.614 0.784 0.617 -0.035 -0.111 0.063  397 TYR CCC CB  
10414 C CG  . TYR C 397 ? 0.643 0.809 0.652 -0.023 -0.107 0.055  397 TYR CCC CG  
10415 C CD1 . TYR C 397 ? 0.666 0.825 0.685 -0.017 -0.114 0.054  397 TYR CCC CD1 
10416 C CD2 . TYR C 397 ? 0.679 0.848 0.682 -0.018 -0.097 0.048  397 TYR CCC CD2 
10417 C CE1 . TYR C 397 ? 0.695 0.853 0.719 -0.007 -0.111 0.046  397 TYR CCC CE1 
10418 C CE2 . TYR C 397 ? 0.666 0.834 0.674 -0.007 -0.094 0.041  397 TYR CCC CE2 
10419 C CZ  . TYR C 397 ? 0.679 0.841 0.697 -0.002 -0.101 0.040  397 TYR CCC CZ  
10420 O OH  . TYR C 397 ? 0.672 0.834 0.695 0.008  -0.098 0.033  397 TYR CCC OH  
10421 N N   . GLY C 398 ? 0.573 0.760 0.560 -0.061 -0.111 0.078  398 GLY CCC N   
10422 C CA  . GLY C 398 ? 0.594 0.787 0.575 -0.074 -0.115 0.086  398 GLY CCC CA  
10423 C C   . GLY C 398 ? 0.614 0.810 0.592 -0.077 -0.114 0.086  398 GLY CCC C   
10424 O O   . GLY C 398 ? 0.571 0.759 0.554 -0.070 -0.116 0.083  398 GLY CCC O   
10425 N N   . GLU C 399 ? 0.664 0.870 0.633 -0.087 -0.111 0.089  399 GLU CCC N   
10426 C CA  . GLU C 399 ? 0.703 0.914 0.668 -0.093 -0.110 0.089  399 GLU CCC CA  
10427 C C   . GLU C 399 ? 0.742 0.944 0.712 -0.093 -0.119 0.094  399 GLU CCC C   
10428 O O   . GLU C 399 ? 0.794 0.995 0.763 -0.091 -0.117 0.091  399 GLU CCC O   
10429 C CB  . GLU C 399 ? 0.773 0.997 0.729 -0.106 -0.109 0.094  399 GLU CCC CB  
10430 C CG  . GLU C 399 ? 0.829 1.061 0.780 -0.113 -0.106 0.094  399 GLU CCC CG  
10431 C CD  . GLU C 399 ? 0.896 1.134 0.843 -0.107 -0.094 0.083  399 GLU CCC CD  
10432 O OE1 . GLU C 399 ? 0.926 1.171 0.870 -0.106 -0.087 0.079  399 GLU CCC OE1 
10433 O OE2 . GLU C 399 ? 0.854 1.090 0.801 -0.104 -0.093 0.080  399 GLU CCC OE2 
10434 N N   . ASP C 400 ? 0.750 0.944 0.727 -0.095 -0.131 0.101  400 ASP CCC N   
10435 C CA  . ASP C 400 ? 0.787 0.973 0.770 -0.098 -0.142 0.107  400 ASP CCC CA  
10436 C C   . ASP C 400 ? 0.739 0.914 0.732 -0.085 -0.144 0.102  400 ASP CCC C   
10437 O O   . ASP C 400 ? 0.754 0.922 0.751 -0.086 -0.151 0.104  400 ASP CCC O   
10438 C CB  . ASP C 400 ? 0.852 1.036 0.839 -0.107 -0.154 0.118  400 ASP CCC CB  
10439 C CG  . ASP C 400 ? 0.885 1.079 0.863 -0.122 -0.157 0.127  400 ASP CCC CG  
10440 O OD1 . ASP C 400 ? 0.911 1.118 0.880 -0.126 -0.147 0.123  400 ASP CCC OD1 
10441 O OD2 . ASP C 400 ? 0.998 1.189 0.980 -0.130 -0.169 0.137  400 ASP CCC OD2 
10442 N N   . ASP C 401 ? 0.695 0.866 0.690 -0.075 -0.138 0.094  401 ASP CCC N   
10443 C CA  . ASP C 401 ? 0.722 0.883 0.726 -0.062 -0.140 0.087  401 ASP CCC CA  
10444 C C   . ASP C 401 ? 0.725 0.890 0.725 -0.056 -0.129 0.079  401 ASP CCC C   
10445 O O   . ASP C 401 ? 0.736 0.895 0.741 -0.045 -0.128 0.072  401 ASP CCC O   
10446 C CB  . ASP C 401 ? 0.700 0.858 0.712 -0.055 -0.141 0.085  401 ASP CCC CB  
10447 C CG  . ASP C 401 ? 0.727 0.873 0.750 -0.045 -0.148 0.081  401 ASP CCC CG  
10448 O OD1 . ASP C 401 ? 0.729 0.871 0.758 -0.046 -0.154 0.083  401 ASP CCC OD1 
10449 O OD2 . ASP C 401 ? 0.754 0.899 0.783 -0.037 -0.146 0.076  401 ASP CCC OD2 
10450 N N   . ILE C 402 ? 0.718 0.893 0.708 -0.062 -0.121 0.079  402 ILE CCC N   
10451 C CA  . ILE C 402 ? 0.675 0.853 0.659 -0.056 -0.111 0.070  402 ILE CCC CA  
10452 C C   . ILE C 402 ? 0.684 0.864 0.665 -0.062 -0.112 0.072  402 ILE CCC C   
10453 O O   . ILE C 402 ? 0.721 0.909 0.697 -0.073 -0.114 0.079  402 ILE CCC O   
10454 C CB  . ILE C 402 ? 0.635 0.823 0.612 -0.058 -0.101 0.067  402 ILE CCC CB  
10455 C CG1 . ILE C 402 ? 0.620 0.806 0.602 -0.050 -0.098 0.063  402 ILE CCC CG1 
10456 C CG2 . ILE C 402 ? 0.645 0.839 0.617 -0.056 -0.091 0.060  402 ILE CCC CG2 
10457 C CD1 . ILE C 402 ? 0.605 0.782 0.593 -0.039 -0.098 0.058  402 ILE CCC CD1 
10458 N N   . GLU C 403 ? 0.637 0.813 0.620 -0.054 -0.109 0.067  403 GLU CCC N   
10459 C CA  . GLU C 403 ? 0.606 0.786 0.585 -0.058 -0.107 0.066  403 GLU CCC CA  
10460 C C   . GLU C 403 ? 0.565 0.749 0.541 -0.051 -0.096 0.057  403 GLU CCC C   
10461 O O   . GLU C 403 ? 0.528 0.707 0.507 -0.041 -0.092 0.051  403 GLU CCC O   
10462 C CB  . GLU C 403 ? 0.624 0.794 0.610 -0.056 -0.116 0.068  403 GLU CCC CB  
10463 C CG  . GLU C 403 ? 0.633 0.807 0.616 -0.064 -0.118 0.073  403 GLU CCC CG  
10464 C CD  . GLU C 403 ? 0.639 0.817 0.619 -0.077 -0.126 0.083  403 GLU CCC CD  
10465 O OE1 . GLU C 403 ? 0.604 0.775 0.591 -0.079 -0.136 0.089  403 GLU CCC OE1 
10466 O OE2 . GLU C 403 ? 0.666 0.855 0.638 -0.086 -0.121 0.085  403 GLU CCC OE2 
10467 N N   . GLU C 404 ? 0.561 0.755 0.530 -0.057 -0.090 0.056  404 GLU CCC N   
10468 C CA  . GLU C 404 ? 0.529 0.726 0.495 -0.052 -0.080 0.048  404 GLU CCC CA  
10469 C C   . GLU C 404 ? 0.520 0.717 0.485 -0.054 -0.081 0.048  404 GLU CCC C   
10470 O O   . GLU C 404 ? 0.550 0.753 0.511 -0.063 -0.083 0.052  404 GLU CCC O   
10471 C CB  . GLU C 404 ? 0.536 0.745 0.495 -0.057 -0.072 0.046  404 GLU CCC CB  
10472 C CG  . GLU C 404 ? 0.560 0.769 0.520 -0.056 -0.072 0.047  404 GLU CCC CG  
10473 C CD  . GLU C 404 ? 0.567 0.789 0.522 -0.063 -0.066 0.045  404 GLU CCC CD  
10474 O OE1 . GLU C 404 ? 0.580 0.808 0.533 -0.062 -0.059 0.040  404 GLU CCC OE1 
10475 O OE2 . GLU C 404 ? 0.655 0.880 0.608 -0.069 -0.068 0.050  404 GLU CCC OE2 
10476 N N   . TYR C 405 ? 0.479 0.669 0.447 -0.044 -0.080 0.043  405 TYR CCC N   
10477 C CA  . TYR C 405 ? 0.464 0.653 0.432 -0.044 -0.080 0.041  405 TYR CCC CA  
10478 C C   . TYR C 405 ? 0.463 0.657 0.427 -0.040 -0.070 0.033  405 TYR CCC C   
10479 O O   . TYR C 405 ? 0.484 0.677 0.449 -0.033 -0.065 0.029  405 TYR CCC O   
10480 C CB  . TYR C 405 ? 0.465 0.642 0.439 -0.036 -0.085 0.040  405 TYR CCC CB  
10481 C CG  . TYR C 405 ? 0.483 0.654 0.463 -0.040 -0.097 0.047  405 TYR CCC CG  
10482 C CD1 . TYR C 405 ? 0.486 0.655 0.466 -0.045 -0.103 0.052  405 TYR CCC CD1 
10483 C CD2 . TYR C 405 ? 0.478 0.644 0.462 -0.037 -0.101 0.049  405 TYR CCC CD2 
10484 C CE1 . TYR C 405 ? 0.494 0.657 0.481 -0.048 -0.114 0.059  405 TYR CCC CE1 
10485 C CE2 . TYR C 405 ? 0.481 0.640 0.472 -0.039 -0.112 0.055  405 TYR CCC CE2 
10486 C CZ  . TYR C 405 ? 0.498 0.655 0.490 -0.045 -0.119 0.060  405 TYR CCC CZ  
10487 O OH  . TYR C 405 ? 0.519 0.669 0.518 -0.048 -0.131 0.067  405 TYR CCC OH  
10488 N N   . LEU C 406 ? 0.455 0.657 0.416 -0.045 -0.066 0.032  406 LEU CCC N   
10489 C CA  . LEU C 406 ? 0.428 0.635 0.386 -0.043 -0.057 0.025  406 LEU CCC CA  
10490 C C   . LEU C 406 ? 0.412 0.623 0.369 -0.046 -0.056 0.023  406 LEU CCC C   
10491 O O   . LEU C 406 ? 0.413 0.624 0.369 -0.052 -0.062 0.028  406 LEU CCC O   
10492 C CB  . LEU C 406 ? 0.463 0.680 0.418 -0.047 -0.052 0.024  406 LEU CCC CB  
10493 C CG  . LEU C 406 ? 0.509 0.737 0.459 -0.059 -0.053 0.027  406 LEU CCC CG  
10494 C CD1 . LEU C 406 ? 0.517 0.755 0.465 -0.061 -0.047 0.024  406 LEU CCC CD1 
10495 C CD2 . LEU C 406 ? 0.515 0.741 0.465 -0.066 -0.062 0.036  406 LEU CCC CD2 
10496 N N   . SER C 407 ? 0.383 0.596 0.340 -0.041 -0.049 0.016  407 SER CCC N   
10497 C CA  . SER C 407 ? 0.386 0.602 0.341 -0.042 -0.047 0.013  407 SER CCC CA  
10498 C C   . SER C 407 ? 0.384 0.607 0.339 -0.040 -0.038 0.005  407 SER CCC C   
10499 O O   . SER C 407 ? 0.361 0.581 0.319 -0.032 -0.035 0.002  407 SER CCC O   
10500 C CB  . SER C 407 ? 0.361 0.568 0.320 -0.036 -0.050 0.012  407 SER CCC CB  
10501 O OG  . SER C 407 ? 0.355 0.565 0.312 -0.037 -0.048 0.009  407 SER CCC OG  
10502 N N   . GLU C 408 ? 0.390 0.624 0.343 -0.046 -0.035 0.002  408 GLU CCC N   
10503 C CA  . GLU C 408 ? 0.386 0.627 0.340 -0.044 -0.028 -0.006 408 GLU CCC CA  
10504 C C   . GLU C 408 ? 0.408 0.650 0.364 -0.043 -0.027 -0.009 408 GLU CCC C   
10505 O O   . GLU C 408 ? 0.445 0.691 0.399 -0.050 -0.030 -0.006 408 GLU CCC O   
10506 C CB  . GLU C 408 ? 0.380 0.635 0.332 -0.052 -0.025 -0.007 408 GLU CCC CB  
10507 C CG  . GLU C 408 ? 0.380 0.642 0.335 -0.050 -0.018 -0.016 408 GLU CCC CG  
10508 C CD  . GLU C 408 ? 0.405 0.681 0.359 -0.057 -0.015 -0.018 408 GLU CCC CD  
10509 O OE1 . GLU C 408 ? 0.455 0.739 0.405 -0.067 -0.017 -0.014 408 GLU CCC OE1 
10510 O OE2 . GLU C 408 ? 0.395 0.675 0.352 -0.055 -0.010 -0.024 408 GLU CCC OE2 
10511 N N   . PHE C 409 ? 0.387 0.624 0.345 -0.035 -0.023 -0.015 409 PHE CCC N   
10512 C CA  . PHE C 409 ? 0.356 0.591 0.316 -0.033 -0.023 -0.018 409 PHE CCC CA  
10513 C C   . PHE C 409 ? 0.341 0.576 0.305 -0.026 -0.018 -0.025 409 PHE CCC C   
10514 O O   . PHE C 409 ? 0.359 0.594 0.325 -0.023 -0.015 -0.027 409 PHE CCC O   
10515 C CB  . PHE C 409 ? 0.334 0.558 0.295 -0.028 -0.028 -0.013 409 PHE CCC CB  
10516 C CG  . PHE C 409 ? 0.319 0.533 0.281 -0.020 -0.028 -0.013 409 PHE CCC CG  
10517 C CD1 . PHE C 409 ? 0.304 0.516 0.266 -0.020 -0.030 -0.009 409 PHE CCC CD1 
10518 C CD2 . PHE C 409 ? 0.296 0.505 0.261 -0.012 -0.026 -0.017 409 PHE CCC CD2 
10519 C CE1 . PHE C 409 ? 0.302 0.506 0.265 -0.012 -0.030 -0.010 409 PHE CCC CE1 
10520 C CE2 . PHE C 409 ? 0.296 0.497 0.262 -0.004 -0.026 -0.017 409 PHE CCC CE2 
10521 C CZ  . PHE C 409 ? 0.276 0.476 0.242 -0.005 -0.028 -0.014 409 PHE CCC CZ  
10522 N N   . SER C 410 ? 0.322 0.556 0.288 -0.024 -0.017 -0.028 410 SER CCC N   
10523 C CA  . SER C 410 ? 0.315 0.548 0.286 -0.018 -0.013 -0.035 410 SER CCC CA  
10524 C C   . SER C 410 ? 0.291 0.511 0.262 -0.010 -0.015 -0.033 410 SER CCC C   
10525 O O   . SER C 410 ? 0.290 0.506 0.260 -0.010 -0.019 -0.030 410 SER CCC O   
10526 C CB  . SER C 410 ? 0.316 0.557 0.288 -0.022 -0.010 -0.040 410 SER CCC CB  
10527 O OG  . SER C 410 ? 0.334 0.572 0.311 -0.015 -0.008 -0.046 410 SER CCC OG  
10528 N N   . THR C 411 ? 0.284 0.501 0.258 -0.003 -0.013 -0.036 411 THR CCC N   
10529 C CA  . THR C 411 ? 0.281 0.489 0.256 0.004  -0.014 -0.037 411 THR CCC CA  
10530 C C   . THR C 411 ? 0.288 0.498 0.265 0.003  -0.014 -0.039 411 THR CCC C   
10531 O O   . THR C 411 ? 0.282 0.500 0.261 -0.002 -0.012 -0.043 411 THR CCC O   
10532 C CB  . THR C 411 ? 0.266 0.473 0.244 0.009  -0.011 -0.040 411 THR CCC CB  
10533 O OG1 . THR C 411 ? 0.245 0.452 0.222 0.009  -0.011 -0.037 411 THR CCC OG1 
10534 C CG2 . THR C 411 ? 0.263 0.463 0.243 0.016  -0.012 -0.040 411 THR CCC CG2 
10535 N N   . LEU C 412 ? 0.299 0.501 0.275 0.006  -0.017 -0.038 412 LEU CCC N   
10536 C CA  . LEU C 412 ? 0.337 0.539 0.314 0.006  -0.017 -0.040 412 LEU CCC CA  
10537 C C   . LEU C 412 ? 0.350 0.556 0.332 0.007  -0.014 -0.046 412 LEU CCC C   
10538 O O   . LEU C 412 ? 0.361 0.573 0.344 0.003  -0.013 -0.049 412 LEU CCC O   
10539 C CB  . LEU C 412 ? 0.349 0.541 0.324 0.012  -0.021 -0.037 412 LEU CCC CB  
10540 C CG  . LEU C 412 ? 0.353 0.543 0.330 0.013  -0.022 -0.039 412 LEU CCC CG  
10541 C CD1 . LEU C 412 ? 0.370 0.565 0.346 0.006  -0.023 -0.038 412 LEU CCC CD1 
10542 C CD2 . LEU C 412 ? 0.357 0.538 0.333 0.018  -0.025 -0.037 412 LEU CCC CD2 
10543 N N   . GLU C 413 ? 0.367 0.569 0.351 0.013  -0.012 -0.047 413 GLU CCC N   
10544 C CA  . GLU C 413 ? 0.378 0.581 0.367 0.016  -0.010 -0.053 413 GLU CCC CA  
10545 C C   . GLU C 413 ? 0.356 0.569 0.349 0.011  -0.007 -0.057 413 GLU CCC C   
10546 O O   . GLU C 413 ? 0.375 0.592 0.372 0.010  -0.006 -0.063 413 GLU CCC O   
10547 C CB  . GLU C 413 ? 0.436 0.634 0.426 0.022  -0.010 -0.052 413 GLU CCC CB  
10548 C CG  . GLU C 413 ? 0.457 0.647 0.445 0.027  -0.012 -0.048 413 GLU CCC CG  
10549 C CD  . GLU C 413 ? 0.469 0.657 0.452 0.027  -0.014 -0.043 413 GLU CCC CD  
10550 O OE1 . GLU C 413 ? 0.496 0.685 0.476 0.023  -0.015 -0.041 413 GLU CCC OE1 
10551 O OE2 . GLU C 413 ? 0.522 0.705 0.504 0.032  -0.014 -0.042 413 GLU CCC OE2 
10552 N N   . ILE C 414 ? 0.351 0.568 0.343 0.009  -0.006 -0.055 414 ILE CCC N   
10553 C CA  . ILE C 414 ? 0.336 0.563 0.330 0.004  -0.004 -0.060 414 ILE CCC CA  
10554 C C   . ILE C 414 ? 0.313 0.548 0.306 -0.003 -0.003 -0.062 414 ILE CCC C   
10555 O O   . ILE C 414 ? 0.304 0.547 0.302 -0.006 -0.001 -0.068 414 ILE CCC O   
10556 C CB  . ILE C 414 ? 0.336 0.564 0.328 0.002  -0.003 -0.057 414 ILE CCC CB  
10557 C CG1 . ILE C 414 ? 0.348 0.567 0.340 0.009  -0.004 -0.054 414 ILE CCC CG1 
10558 C CG2 . ILE C 414 ? 0.324 0.563 0.320 -0.002 -0.000 -0.062 414 ILE CCC CG2 
10559 C CD1 . ILE C 414 ? 0.351 0.570 0.349 0.013  -0.002 -0.059 414 ILE CCC CD1 
10560 N N   . ALA C 415 ? 0.304 0.537 0.291 -0.006 -0.006 -0.056 415 ALA CCC N   
10561 C CA  . ALA C 415 ? 0.308 0.549 0.294 -0.013 -0.006 -0.057 415 ALA CCC CA  
10562 C C   . ALA C 415 ? 0.293 0.537 0.283 -0.012 -0.005 -0.063 415 ALA CCC C   
10563 O O   . ALA C 415 ? 0.283 0.537 0.275 -0.018 -0.003 -0.067 415 ALA CCC O   
10564 C CB  . ALA C 415 ? 0.317 0.553 0.296 -0.016 -0.010 -0.049 415 ALA CCC CB  
10565 N N   . ALA C 416 ? 0.304 0.538 0.296 -0.006 -0.007 -0.062 416 ALA CCC N   
10566 C CA  . ALA C 416 ? 0.308 0.542 0.304 -0.004 -0.006 -0.067 416 ALA CCC CA  
10567 C C   . ALA C 416 ? 0.315 0.556 0.320 -0.003 -0.003 -0.075 416 ALA CCC C   
10568 O O   . ALA C 416 ? 0.293 0.539 0.302 -0.004 -0.002 -0.081 416 ALA CCC O   
10569 C CB  . ALA C 416 ? 0.317 0.540 0.313 0.002  -0.009 -0.064 416 ALA CCC CB  
10570 N N   . ALA C 417 ? 0.324 0.564 0.330 -0.001 -0.002 -0.076 417 ALA CCC N   
10571 C CA  . ALA C 417 ? 0.346 0.591 0.361 -0.000 0.000  -0.084 417 ALA CCC CA  
10572 C C   . ALA C 417 ? 0.352 0.612 0.370 -0.007 0.003  -0.090 417 ALA CCC C   
10573 O O   . ALA C 417 ? 0.373 0.640 0.400 -0.007 0.004  -0.098 417 ALA CCC O   
10574 C CB  . ALA C 417 ? 0.363 0.603 0.379 0.004  0.000  -0.082 417 ALA CCC CB  
10575 N N   . HIS C 418 ? 0.359 0.626 0.371 -0.013 0.003  -0.086 418 HIS CCC N   
10576 C CA  . HIS C 418 ? 0.358 0.641 0.371 -0.021 0.006  -0.092 418 HIS CCC CA  
10577 C C   . HIS C 418 ? 0.338 0.625 0.358 -0.019 0.008  -0.098 418 HIS CCC C   
10578 O O   . HIS C 418 ? 0.339 0.637 0.367 -0.021 0.010  -0.107 418 HIS CCC O   
10579 C CB  . HIS C 418 ? 0.398 0.690 0.415 -0.025 0.007  -0.098 418 HIS CCC CB  
10580 C CG  . HIS C 418 ? 0.435 0.724 0.444 -0.028 0.005  -0.092 418 HIS CCC CG  
10581 N ND1 . HIS C 418 ? 0.479 0.776 0.481 -0.036 0.004  -0.088 418 HIS CCC ND1 
10582 C CD2 . HIS C 418 ? 0.478 0.758 0.487 -0.024 0.002  -0.089 418 HIS CCC CD2 
10583 C CE1 . HIS C 418 ? 0.474 0.766 0.472 -0.037 0.002  -0.083 418 HIS CCC CE1 
10584 N NE2 . HIS C 418 ? 0.485 0.767 0.486 -0.030 0.001  -0.084 418 HIS CCC NE2 
10585 N N   . ARG C 419 ? 0.314 0.594 0.331 -0.017 0.007  -0.093 419 ARG CCC N   
10586 C CA  . ARG C 419 ? 0.317 0.601 0.341 -0.015 0.009  -0.097 419 ARG CCC CA  
10587 C C   . ARG C 419 ? 0.332 0.633 0.358 -0.022 0.012  -0.104 419 ARG CCC C   
10588 O O   . ARG C 419 ? 0.295 0.601 0.312 -0.029 0.012  -0.099 419 ARG CCC O   
10589 C CB  . ARG C 419 ? 0.339 0.614 0.358 -0.012 0.008  -0.090 419 ARG CCC CB  
10590 C CG  . ARG C 419 ? 0.338 0.597 0.356 -0.004 0.005  -0.085 419 ARG CCC CG  
10591 C CD  . ARG C 419 ? 0.331 0.585 0.349 -0.000 0.005  -0.081 419 ARG CCC CD  
10592 N NE  . ARG C 419 ? 0.336 0.579 0.355 0.006  0.003  -0.079 419 ARG CCC NE  
10593 C CZ  . ARG C 419 ? 0.324 0.559 0.343 0.011  0.002  -0.075 419 ARG CCC CZ  
10594 N NH1 . ARG C 419 ? 0.321 0.559 0.338 0.009  0.003  -0.073 419 ARG CCC NH1 
10595 N NH2 . ARG C 419 ? 0.280 0.507 0.301 0.016  0.001  -0.073 419 ARG CCC NH2 
10596 N N   . GLU C 420 ? 0.348 0.657 0.384 -0.022 0.013  -0.113 420 GLU CCC N   
10597 C CA  . GLU C 420 ? 0.391 0.717 0.430 -0.028 0.016  -0.122 420 GLU CCC CA  
10598 C C   . GLU C 420 ? 0.378 0.706 0.422 -0.027 0.017  -0.125 420 GLU CCC C   
10599 O O   . GLU C 420 ? 0.333 0.652 0.384 -0.020 0.016  -0.125 420 GLU CCC O   
10600 C CB  . GLU C 420 ? 0.420 0.756 0.470 -0.028 0.017  -0.133 420 GLU CCC CB  
10601 C CG  . GLU C 420 ? 0.468 0.804 0.513 -0.031 0.017  -0.131 420 GLU CCC CG  
10602 C CD  . GLU C 420 ? 0.492 0.843 0.546 -0.034 0.019  -0.142 420 GLU CCC CD  
10603 O OE1 . GLU C 420 ? 0.521 0.888 0.579 -0.040 0.021  -0.150 420 GLU CCC OE1 
10604 O OE2 . GLU C 420 ? 0.528 0.874 0.584 -0.032 0.017  -0.143 420 GLU CCC OE2 
10605 N N   . LYS C 421 ? 0.360 0.702 0.402 -0.034 0.019  -0.127 421 LYS CCC N   
10606 C CA  . LYS C 421 ? 0.379 0.729 0.427 -0.034 0.021  -0.133 421 LYS CCC CA  
10607 C C   . LYS C 421 ? 0.375 0.728 0.438 -0.030 0.021  -0.145 421 LYS CCC C   
10608 O O   . LYS C 421 ? 0.340 0.698 0.408 -0.031 0.021  -0.151 421 LYS CCC O   
10609 C CB  . LYS C 421 ? 0.411 0.779 0.455 -0.043 0.024  -0.137 421 LYS CCC CB  
10610 C CG  . LYS C 421 ? 0.441 0.807 0.473 -0.048 0.023  -0.126 421 LYS CCC CG  
10611 C CD  . LYS C 421 ? 0.469 0.851 0.496 -0.057 0.025  -0.128 421 LYS CCC CD  
10612 C CE  . LYS C 421 ? 0.495 0.872 0.510 -0.060 0.023  -0.116 421 LYS CCC CE  
10613 N NZ  . LYS C 421 ? 0.515 0.908 0.525 -0.070 0.025  -0.116 421 LYS CCC NZ  
10614 N N   . PRO C 422 ? 0.411 0.761 0.482 -0.026 0.020  -0.148 422 PRO CCC N   
10615 C CA  . PRO C 422 ? 0.444 0.800 0.531 -0.023 0.020  -0.161 422 PRO CCC CA  
10616 C C   . PRO C 422 ? 0.441 0.818 0.532 -0.030 0.023  -0.172 422 PRO CCC C   
10617 O O   . PRO C 422 ? 0.413 0.800 0.495 -0.037 0.025  -0.169 422 PRO CCC O   
10618 C CB  . PRO C 422 ? 0.442 0.793 0.535 -0.019 0.018  -0.160 422 PRO CCC CB  
10619 C CG  . PRO C 422 ? 0.454 0.791 0.534 -0.017 0.018  -0.146 422 PRO CCC CG  
10620 C CD  . PRO C 422 ? 0.442 0.783 0.508 -0.024 0.019  -0.141 422 PRO CCC CD  
10621 N N   . GLU C 423 ? 0.489 0.874 0.593 -0.029 0.023  -0.184 423 GLU CCC N   
10622 C CA  . GLU C 423 ? 0.559 0.966 0.667 -0.036 0.026  -0.195 423 GLU CCC CA  
10623 C C   . GLU C 423 ? 0.543 0.966 0.655 -0.040 0.028  -0.202 423 GLU CCC C   
10624 O O   . GLU C 423 ? 0.549 0.990 0.657 -0.048 0.032  -0.207 423 GLU CCC O   
10625 C CB  . GLU C 423 ? 0.626 1.035 0.749 -0.032 0.025  -0.206 423 GLU CCC CB  
10626 C CG  . GLU C 423 ? 0.701 1.134 0.831 -0.038 0.028  -0.219 423 GLU CCC CG  
10627 C CD  . GLU C 423 ? 0.788 1.221 0.929 -0.035 0.027  -0.228 423 GLU CCC CD  
10628 O OE1 . GLU C 423 ? 0.797 1.216 0.933 -0.032 0.024  -0.220 423 GLU CCC OE1 
10629 O OE2 . GLU C 423 ? 0.853 1.302 1.008 -0.036 0.028  -0.243 423 GLU CCC OE2 
10630 N N   . HIS C 424 ? 0.566 0.980 0.682 -0.036 0.027  -0.202 424 HIS CCC N   
10631 C CA  . HIS C 424 ? 0.569 0.997 0.690 -0.039 0.029  -0.209 424 HIS CCC CA  
10632 C C   . HIS C 424 ? 0.542 0.974 0.647 -0.046 0.031  -0.199 424 HIS CCC C   
10633 O O   . HIS C 424 ? 0.543 0.989 0.649 -0.050 0.033  -0.205 424 HIS CCC O   
10634 C CB  . HIS C 424 ? 0.621 1.040 0.754 -0.032 0.026  -0.212 424 HIS CCC CB  
10635 C CG  . HIS C 424 ? 0.634 1.032 0.760 -0.027 0.023  -0.198 424 HIS CCC CG  
10636 N ND1 . HIS C 424 ? 0.644 1.040 0.760 -0.029 0.024  -0.190 424 HIS CCC ND1 
10637 C CD2 . HIS C 424 ? 0.660 1.039 0.788 -0.020 0.019  -0.191 424 HIS CCC CD2 
10638 C CE1 . HIS C 424 ? 0.690 1.068 0.803 -0.023 0.021  -0.179 424 HIS CCC CE1 
10639 N NE2 . HIS C 424 ? 0.692 1.059 0.812 -0.018 0.018  -0.180 424 HIS CCC NE2 
10640 N N   . LEU C 425 ? 0.498 0.919 0.587 -0.047 0.030  -0.186 425 LEU CCC N   
10641 C CA  . LEU C 425 ? 0.516 0.940 0.591 -0.053 0.032  -0.176 425 LEU CCC CA  
10642 C C   . LEU C 425 ? 0.511 0.946 0.576 -0.062 0.033  -0.173 425 LEU CCC C   
10643 O O   . LEU C 425 ? 0.510 0.946 0.562 -0.068 0.034  -0.164 425 LEU CCC O   
10644 C CB  . LEU C 425 ? 0.535 0.937 0.601 -0.048 0.029  -0.162 425 LEU CCC CB  
10645 C CG  . LEU C 425 ? 0.563 0.955 0.636 -0.041 0.028  -0.162 425 LEU CCC CG  
10646 C CD1 . LEU C 425 ? 0.553 0.925 0.621 -0.035 0.025  -0.150 425 LEU CCC CD1 
10647 C CD2 . LEU C 425 ? 0.588 0.991 0.659 -0.046 0.029  -0.163 425 LEU CCC CD2 
10648 N N   . ARG C 426 ? 0.538 0.979 0.608 -0.062 0.034  -0.180 426 ARG CCC N   
10649 C CA  . ARG C 426 ? 0.550 1.002 0.612 -0.070 0.035  -0.178 426 ARG CCC CA  
10650 C C   . ARG C 426 ? 0.611 1.087 0.670 -0.081 0.039  -0.185 426 ARG CCC C   
10651 O O   . ARG C 426 ? 0.589 1.079 0.660 -0.080 0.041  -0.198 426 ARG CCC O   
10652 C CB  . ARG C 426 ? 0.532 0.983 0.601 -0.067 0.035  -0.185 426 ARG CCC CB  
10653 C CG  . ARG C 426 ? 0.496 0.924 0.564 -0.059 0.032  -0.176 426 ARG CCC CG  
10654 C CD  . ARG C 426 ? 0.486 0.906 0.539 -0.062 0.030  -0.162 426 ARG CCC CD  
10655 N NE  . ARG C 426 ? 0.489 0.924 0.538 -0.071 0.032  -0.164 426 ARG CCC NE  
10656 C CZ  . ARG C 426 ? 0.469 0.905 0.520 -0.070 0.032  -0.167 426 ARG CCC CZ  
10657 N NH1 . ARG C 426 ? 0.454 0.877 0.513 -0.062 0.030  -0.169 426 ARG CCC NH1 
10658 N NH2 . ARG C 426 ? 0.470 0.921 0.516 -0.079 0.033  -0.168 426 ARG CCC NH2 
10659 N N   . GLU C 427 ? 0.706 1.188 0.751 -0.089 0.039  -0.175 427 GLU CCC N   
10660 C CA  . GLU C 427 ? 0.743 1.248 0.783 -0.101 0.042  -0.179 427 GLU CCC CA  
10661 C C   . GLU C 427 ? 0.772 1.293 0.809 -0.109 0.043  -0.182 427 GLU CCC C   
10662 O O   . GLU C 427 ? 0.816 1.361 0.853 -0.118 0.046  -0.189 427 GLU CCC O   
10663 C CB  . GLU C 427 ? 0.763 1.263 0.790 -0.106 0.040  -0.165 427 GLU CCC CB  
10664 C CG  . GLU C 427 ? 0.799 1.304 0.827 -0.106 0.041  -0.169 427 GLU CCC CG  
10665 C CD  . GLU C 427 ? 0.792 1.296 0.808 -0.112 0.040  -0.156 427 GLU CCC CD  
10666 O OE1 . GLU C 427 ? 0.829 1.318 0.844 -0.106 0.038  -0.151 427 GLU CCC OE1 
10667 O OE2 . GLU C 427 ? 0.717 1.233 0.722 -0.123 0.040  -0.151 427 GLU CCC OE2 
10668 N N   . ASN C 428 ? 0.744 1.254 0.779 -0.107 0.041  -0.177 428 ASN CCC N   
10669 C CA  . ASN C 428 ? 0.778 1.303 0.809 -0.115 0.042  -0.178 428 ASN CCC CA  
10670 C C   . ASN C 428 ? 0.762 1.271 0.794 -0.108 0.040  -0.174 428 ASN CCC C   
10671 O O   . ASN C 428 ? 0.711 1.202 0.751 -0.098 0.038  -0.175 428 ASN CCC O   
10672 C CB  . ASN C 428 ? 0.839 1.372 0.855 -0.126 0.041  -0.167 428 ASN CCC CB  
10673 C CG  . ASN C 428 ? 0.831 1.342 0.837 -0.124 0.037  -0.150 428 ASN CCC CG  
10674 O OD1 . ASN C 428 ? 0.865 1.357 0.870 -0.117 0.034  -0.143 428 ASN CCC OD1 
10675 N ND2 . ASN C 428 ? 0.825 1.339 0.824 -0.129 0.037  -0.144 428 ASN CCC ND2 
10676 N N   . GLU C 429 ? 0.745 1.260 0.772 -0.115 0.039  -0.170 429 GLU CCC N   
10677 C CA  . GLU C 429 ? 0.755 1.257 0.782 -0.110 0.037  -0.168 429 GLU CCC CA  
10678 C C   . GLU C 429 ? 0.728 1.209 0.744 -0.108 0.033  -0.151 429 GLU CCC C   
10679 O O   . GLU C 429 ? 0.740 1.209 0.755 -0.104 0.031  -0.147 429 GLU CCC O   
10680 C CB  . GLU C 429 ? 0.749 1.271 0.778 -0.118 0.039  -0.174 429 GLU CCC CB  
10681 C CG  . GLU C 429 ? 0.742 1.289 0.781 -0.122 0.044  -0.191 429 GLU CCC CG  
10682 C CD  . GLU C 429 ? 0.709 1.251 0.763 -0.112 0.045  -0.203 429 GLU CCC CD  
10683 O OE1 . GLU C 429 ? 0.668 1.193 0.729 -0.102 0.043  -0.203 429 GLU CCC OE1 
10684 O OE2 . GLU C 429 ? 0.668 1.222 0.727 -0.113 0.047  -0.211 429 GLU CCC OE2 
10685 N N   . MET C 430 ? 0.720 1.197 0.727 -0.111 0.032  -0.141 430 MET CCC N   
10686 C CA  . MET C 430 ? 0.725 1.183 0.721 -0.110 0.027  -0.125 430 MET CCC CA  
10687 C C   . MET C 430 ? 0.664 1.106 0.661 -0.102 0.026  -0.120 430 MET CCC C   
10688 O O   . MET C 430 ? 0.656 1.083 0.645 -0.101 0.022  -0.108 430 MET CCC O   
10689 C CB  . MET C 430 ? 0.795 1.265 0.780 -0.123 0.026  -0.116 430 MET CCC CB  
10690 C CG  . MET C 430 ? 0.833 1.305 0.813 -0.129 0.023  -0.111 430 MET CCC CG  
10691 S SD  . MET C 430 ? 0.869 1.315 0.848 -0.119 0.019  -0.103 430 MET CCC SD  
10692 C CE  . MET C 430 ? 0.937 1.362 0.912 -0.113 0.015  -0.091 430 MET CCC CE  
10693 N N   . ASP C 431 ? 0.567 1.010 0.573 -0.096 0.028  -0.130 431 ASP CCC N   
10694 C CA  . ASP C 431 ? 0.547 0.977 0.555 -0.089 0.027  -0.127 431 ASP CCC CA  
10695 C C   . ASP C 431 ? 0.488 0.899 0.503 -0.077 0.026  -0.128 431 ASP CCC C   
10696 O O   . ASP C 431 ? 0.460 0.864 0.480 -0.071 0.026  -0.130 431 ASP CCC O   
10697 C CB  . ASP C 431 ? 0.586 1.033 0.599 -0.093 0.031  -0.137 431 ASP CCC CB  
10698 C CG  . ASP C 431 ? 0.662 1.099 0.678 -0.086 0.031  -0.137 431 ASP CCC CG  
10699 O OD1 . ASP C 431 ? 0.678 1.099 0.687 -0.083 0.028  -0.125 431 ASP CCC OD1 
10700 O OD2 . ASP C 431 ? 0.718 1.163 0.744 -0.084 0.033  -0.148 431 ASP CCC OD2 
10701 N N   . PHE C 432 ? 0.427 0.831 0.443 -0.074 0.025  -0.127 432 PHE CCC N   
10702 C CA  . PHE C 432 ? 0.404 0.795 0.428 -0.064 0.024  -0.131 432 PHE CCC CA  
10703 C C   . PHE C 432 ? 0.393 0.763 0.414 -0.056 0.021  -0.122 432 PHE CCC C   
10704 O O   . PHE C 432 ? 0.398 0.759 0.427 -0.048 0.021  -0.125 432 PHE CCC O   
10705 C CB  . PHE C 432 ? 0.394 0.787 0.420 -0.065 0.024  -0.134 432 PHE CCC CB  
10706 C CG  . PHE C 432 ? 0.410 0.799 0.425 -0.070 0.021  -0.123 432 PHE CCC CG  
10707 C CD1 . PHE C 432 ? 0.399 0.769 0.409 -0.064 0.018  -0.113 432 PHE CCC CD1 
10708 C CD2 . PHE C 432 ? 0.437 0.844 0.447 -0.081 0.022  -0.123 432 PHE CCC CD2 
10709 C CE1 . PHE C 432 ? 0.411 0.778 0.412 -0.069 0.015  -0.104 432 PHE CCC CE1 
10710 C CE2 . PHE C 432 ? 0.434 0.837 0.434 -0.086 0.019  -0.113 432 PHE CCC CE2 
10711 C CZ  . PHE C 432 ? 0.422 0.804 0.418 -0.079 0.016  -0.103 432 PHE CCC CZ  
10712 N N   . ALA C 433 ? 0.375 0.737 0.385 -0.059 0.019  -0.110 433 ALA CCC N   
10713 C CA  . ALA C 433 ? 0.369 0.711 0.375 -0.052 0.015  -0.100 433 ALA CCC CA  
10714 C C   . ALA C 433 ? 0.362 0.699 0.367 -0.049 0.016  -0.098 433 ALA CCC C   
10715 O O   . ALA C 433 ? 0.392 0.741 0.397 -0.055 0.017  -0.099 433 ALA CCC O   
10716 C CB  . ALA C 433 ? 0.367 0.704 0.362 -0.056 0.012  -0.089 433 ALA CCC CB  
10717 N N   . LEU C 434 ? 0.336 0.659 0.344 -0.040 0.014  -0.095 434 LEU CCC N   
10718 C CA  . LEU C 434 ? 0.332 0.646 0.337 -0.037 0.013  -0.089 434 LEU CCC CA  
10719 C C   . LEU C 434 ? 0.322 0.633 0.316 -0.042 0.011  -0.079 434 LEU CCC C   
10720 O O   . LEU C 434 ? 0.304 0.612 0.293 -0.044 0.009  -0.074 434 LEU CCC O   
10721 C CB  . LEU C 434 ? 0.339 0.637 0.346 -0.028 0.012  -0.086 434 LEU CCC CB  
10722 C CG  . LEU C 434 ? 0.347 0.647 0.366 -0.023 0.013  -0.095 434 LEU CCC CG  
10723 C CD1 . LEU C 434 ? 0.377 0.661 0.397 -0.015 0.011  -0.091 434 LEU CCC CD1 
10724 C CD2 . LEU C 434 ? 0.353 0.664 0.377 -0.026 0.015  -0.102 434 LEU CCC CD2 
10725 N N   . PRO C 435 ? 0.334 0.645 0.325 -0.043 0.010  -0.074 435 PRO CCC N   
10726 C CA  . PRO C 435 ? 0.340 0.645 0.321 -0.046 0.007  -0.064 435 PRO CCC CA  
10727 C C   . PRO C 435 ? 0.336 0.625 0.316 -0.040 0.004  -0.058 435 PRO CCC C   
10728 O O   . PRO C 435 ? 0.305 0.586 0.289 -0.032 0.004  -0.060 435 PRO CCC O   
10729 C CB  . PRO C 435 ? 0.336 0.640 0.316 -0.046 0.007  -0.061 435 PRO CCC CB  
10730 C CG  . PRO C 435 ? 0.340 0.655 0.327 -0.047 0.011  -0.071 435 PRO CCC CG  
10731 C CD  . PRO C 435 ? 0.335 0.651 0.330 -0.043 0.013  -0.079 435 PRO CCC CD  
10732 N N   . LEU C 436 ? 0.354 0.640 0.328 -0.043 0.000  -0.050 436 LEU CCC N   
10733 C CA  . LEU C 436 ? 0.324 0.595 0.295 -0.037 -0.003 -0.044 436 LEU CCC CA  
10734 C C   . LEU C 436 ? 0.300 0.562 0.273 -0.029 -0.003 -0.043 436 LEU CCC C   
10735 O O   . LEU C 436 ? 0.284 0.550 0.257 -0.031 -0.002 -0.043 436 LEU CCC O   
10736 C CB  . LEU C 436 ? 0.335 0.605 0.300 -0.043 -0.008 -0.036 436 LEU CCC CB  
10737 C CG  . LEU C 436 ? 0.347 0.626 0.309 -0.051 -0.009 -0.035 436 LEU CCC CG  
10738 C CD1 . LEU C 436 ? 0.355 0.634 0.312 -0.058 -0.014 -0.026 436 LEU CCC CD1 
10739 C CD2 . LEU C 436 ? 0.346 0.620 0.311 -0.048 -0.010 -0.037 436 LEU CCC CD2 
10740 N N   . ASN C 437 ? 0.272 0.523 0.247 -0.022 -0.004 -0.043 437 ASN CCC N   
10741 C CA  . ASN C 437 ? 0.264 0.510 0.242 -0.015 -0.002 -0.044 437 ASN CCC CA  
10742 C C   . ASN C 437 ? 0.262 0.500 0.236 -0.013 -0.005 -0.037 437 ASN CCC C   
10743 O O   . ASN C 437 ? 0.252 0.487 0.227 -0.009 -0.004 -0.037 437 ASN CCC O   
10744 C CB  . ASN C 437 ? 0.264 0.504 0.247 -0.008 -0.002 -0.048 437 ASN CCC CB  
10745 C CG  . ASN C 437 ? 0.279 0.509 0.259 -0.004 -0.005 -0.044 437 ASN CCC CG  
10746 O OD1 . ASN C 437 ? 0.280 0.510 0.256 -0.008 -0.007 -0.041 437 ASN CCC OD1 
10747 N ND2 . ASN C 437 ? 0.299 0.523 0.282 0.003  -0.005 -0.044 437 ASN CCC ND2 
10748 N N   . CYS C 438 ? 0.261 0.496 0.231 -0.015 -0.009 -0.031 438 CYS CCC N   
10749 C CA  . CYS C 438 ? 0.269 0.495 0.236 -0.012 -0.013 -0.025 438 CYS CCC CA  
10750 C C   . CYS C 438 ? 0.297 0.526 0.261 -0.019 -0.016 -0.020 438 CYS CCC C   
10751 O O   . CYS C 438 ? 0.286 0.521 0.247 -0.026 -0.017 -0.019 438 CYS CCC O   
10752 C CB  . CYS C 438 ? 0.269 0.486 0.236 -0.008 -0.016 -0.023 438 CYS CCC CB  
10753 S SG  . CYS C 438 ? 0.275 0.487 0.245 0.000  -0.014 -0.028 438 CYS CCC SG  
10754 N N   . LEU C 439 ? 0.304 0.529 0.267 -0.017 -0.018 -0.016 439 LEU CCC N   
10755 C CA  . LEU C 439 ? 0.307 0.532 0.268 -0.022 -0.022 -0.010 439 LEU CCC CA  
10756 C C   . LEU C 439 ? 0.301 0.516 0.263 -0.016 -0.025 -0.007 439 LEU CCC C   
10757 O O   . LEU C 439 ? 0.310 0.523 0.273 -0.010 -0.023 -0.009 439 LEU CCC O   
10758 C CB  . LEU C 439 ? 0.320 0.553 0.280 -0.027 -0.019 -0.011 439 LEU CCC CB  
10759 C CG  . LEU C 439 ? 0.320 0.555 0.277 -0.033 -0.024 -0.004 439 LEU CCC CG  
10760 C CD1 . LEU C 439 ? 0.332 0.571 0.287 -0.041 -0.027 -0.001 439 LEU CCC CD1 
10761 C CD2 . LEU C 439 ? 0.323 0.565 0.279 -0.036 -0.020 -0.006 439 LEU CCC CD2 
10762 N N   . ALA C 440 ? 0.314 0.524 0.275 -0.017 -0.031 -0.002 440 ALA CCC N   
10763 C CA  . ALA C 440 ? 0.318 0.519 0.281 -0.012 -0.036 0.001  440 ALA CCC CA  
10764 C C   . ALA C 440 ? 0.342 0.544 0.305 -0.017 -0.041 0.007  440 ALA CCC C   
10765 O O   . ALA C 440 ? 0.329 0.535 0.290 -0.025 -0.044 0.010  440 ALA CCC O   
10766 C CB  . ALA C 440 ? 0.325 0.519 0.290 -0.008 -0.039 0.001  440 ALA CCC CB  
10767 N N   . LYS C 441 ? 0.343 0.542 0.308 -0.014 -0.042 0.008  441 LYS CCC N   
10768 C CA  . LYS C 441 ? 0.357 0.555 0.322 -0.019 -0.047 0.014  441 LYS CCC CA  
10769 C C   . LYS C 441 ? 0.377 0.567 0.345 -0.012 -0.051 0.015  441 LYS CCC C   
10770 O O   . LYS C 441 ? 0.372 0.562 0.342 -0.006 -0.047 0.011  441 LYS CCC O   
10771 C CB  . LYS C 441 ? 0.371 0.577 0.332 -0.024 -0.043 0.014  441 LYS CCC CB  
10772 C CG  . LYS C 441 ? 0.389 0.596 0.350 -0.030 -0.049 0.020  441 LYS CCC CG  
10773 C CD  . LYS C 441 ? 0.399 0.616 0.357 -0.038 -0.046 0.021  441 LYS CCC CD  
10774 C CE  . LYS C 441 ? 0.445 0.665 0.402 -0.034 -0.039 0.017  441 LYS CCC CE  
10775 N NZ  . LYS C 441 ? 0.483 0.714 0.437 -0.043 -0.037 0.017  441 LYS CCC NZ  
10776 N N   . LEU C 442 ? 0.394 0.579 0.365 -0.014 -0.059 0.020  442 LEU CCC N   
10777 C CA  . LEU C 442 ? 0.390 0.569 0.366 -0.010 -0.064 0.022  442 LEU CCC CA  
10778 C C   . LEU C 442 ? 0.426 0.607 0.402 -0.017 -0.068 0.028  442 LEU CCC C   
10779 O O   . LEU C 442 ? 0.381 0.565 0.355 -0.026 -0.072 0.033  442 LEU CCC O   
10780 C CB  . LEU C 442 ? 0.385 0.556 0.367 -0.006 -0.071 0.022  442 LEU CCC CB  
10781 C CG  . LEU C 442 ? 0.366 0.534 0.348 0.001  -0.067 0.016  442 LEU CCC CG  
10782 C CD1 . LEU C 442 ? 0.373 0.534 0.361 0.003  -0.075 0.017  442 LEU CCC CD1 
10783 C CD2 . LEU C 442 ? 0.346 0.515 0.330 0.009  -0.062 0.011  442 LEU CCC CD2 
10784 N N   . VAL C 443 ? 0.462 0.642 0.440 -0.014 -0.068 0.027  443 VAL CCC N   
10785 C CA  . VAL C 443 ? 0.505 0.686 0.484 -0.019 -0.073 0.033  443 VAL CCC CA  
10786 C C   . VAL C 443 ? 0.529 0.701 0.516 -0.014 -0.080 0.034  443 VAL CCC C   
10787 O O   . VAL C 443 ? 0.568 0.737 0.558 -0.005 -0.078 0.029  443 VAL CCC O   
10788 C CB  . VAL C 443 ? 0.506 0.694 0.482 -0.020 -0.066 0.031  443 VAL CCC CB  
10789 C CG1 . VAL C 443 ? 0.488 0.677 0.464 -0.026 -0.070 0.037  443 VAL CCC CG1 
10790 C CG2 . VAL C 443 ? 0.504 0.699 0.474 -0.023 -0.059 0.028  443 VAL CCC CG2 
10791 N N   . VAL C 444 ? 0.545 0.713 0.535 -0.019 -0.089 0.040  444 VAL CCC N   
10792 C CA  . VAL C 444 ? 0.563 0.723 0.563 -0.015 -0.099 0.041  444 VAL CCC CA  
10793 C C   . VAL C 444 ? 0.545 0.704 0.547 -0.021 -0.106 0.048  444 VAL CCC C   
10794 O O   . VAL C 444 ? 0.538 0.702 0.535 -0.030 -0.107 0.054  444 VAL CCC O   
10795 C CB  . VAL C 444 ? 0.570 0.725 0.573 -0.014 -0.104 0.042  444 VAL CCC CB  
10796 C CG1 . VAL C 444 ? 0.570 0.726 0.569 -0.010 -0.097 0.036  444 VAL CCC CG1 
10797 C CG2 . VAL C 444 ? 0.573 0.728 0.573 -0.025 -0.111 0.050  444 VAL CCC CG2 
10798 N N   . VAL C 445 ? 0.550 0.702 0.561 -0.015 -0.112 0.047  445 VAL CCC N   
10799 C CA  . VAL C 445 ? 0.574 0.723 0.590 -0.019 -0.121 0.053  445 VAL CCC CA  
10800 C C   . VAL C 445 ? 0.579 0.720 0.604 -0.021 -0.133 0.057  445 VAL CCC C   
10801 O O   . VAL C 445 ? 0.560 0.695 0.593 -0.013 -0.136 0.052  445 VAL CCC O   
10802 C CB  . VAL C 445 ? 0.555 0.703 0.577 -0.012 -0.119 0.049  445 VAL CCC CB  
10803 C CG1 . VAL C 445 ? 0.577 0.721 0.605 -0.016 -0.129 0.055  445 VAL CCC CG1 
10804 C CG2 . VAL C 445 ? 0.536 0.692 0.550 -0.010 -0.108 0.045  445 VAL CCC CG2 
10805 N N   . LYS C 446 ? 0.596 0.738 0.619 -0.031 -0.140 0.066  446 LYS CCC N   
10806 C CA  . LYS C 446 ? 0.637 0.771 0.667 -0.035 -0.152 0.072  446 LYS CCC CA  
10807 C C   . LYS C 446 ? 0.631 0.756 0.675 -0.029 -0.162 0.071  446 LYS CCC C   
10808 O O   . LYS C 446 ? 0.646 0.765 0.699 -0.024 -0.168 0.069  446 LYS CCC O   
10809 C CB  . LYS C 446 ? 0.674 0.811 0.698 -0.049 -0.157 0.083  446 LYS CCC CB  
10810 C CG  . LYS C 446 ? 0.707 0.854 0.720 -0.054 -0.147 0.082  446 LYS CCC CG  
10811 C CD  . LYS C 446 ? 0.767 0.915 0.777 -0.065 -0.154 0.090  446 LYS CCC CD  
10812 C CE  . LYS C 446 ? 0.826 0.980 0.832 -0.077 -0.158 0.100  446 LYS CCC CE  
10813 N NZ  . LYS C 446 ? 0.862 1.020 0.864 -0.088 -0.163 0.107  446 LYS CCC NZ  
10814 N N   . SER C 447 ? 0.622 0.749 0.668 -0.028 -0.162 0.072  447 SER CCC N   
10815 C CA  . SER C 447 ? 0.621 0.740 0.680 -0.023 -0.172 0.071  447 SER CCC CA  
10816 C C   . SER C 447 ? 0.628 0.745 0.695 -0.010 -0.169 0.060  447 SER CCC C   
10817 O O   . SER C 447 ? 0.640 0.751 0.719 -0.005 -0.176 0.057  447 SER CCC O   
10818 C CB  . SER C 447 ? 0.604 0.726 0.663 -0.027 -0.172 0.075  447 SER CCC CB  
10819 O OG  . SER C 447 ? 0.557 0.686 0.608 -0.023 -0.159 0.069  447 SER CCC OG  
10820 N N   . GLN C 448 ? 0.631 0.751 0.692 -0.005 -0.159 0.053  448 GLN CCC N   
10821 C CA  . GLN C 448 ? 0.641 0.760 0.708 0.007  -0.155 0.042  448 GLN CCC CA  
10822 C C   . GLN C 448 ? 0.629 0.747 0.695 0.009  -0.154 0.039  448 GLN CCC C   
10823 O O   . GLN C 448 ? 0.605 0.726 0.669 0.017  -0.146 0.031  448 GLN CCC O   
10824 C CB  . GLN C 448 ? 0.638 0.765 0.698 0.012  -0.143 0.036  448 GLN CCC CB  
10825 C CG  . GLN C 448 ? 0.646 0.775 0.708 0.010  -0.144 0.039  448 GLN CCC CG  
10826 C CD  . GLN C 448 ? 0.633 0.769 0.688 0.014  -0.132 0.034  448 GLN CCC CD  
10827 O OE1 . GLN C 448 ? 0.625 0.764 0.680 0.022  -0.126 0.026  448 GLN CCC OE1 
10828 N NE2 . GLN C 448 ? 0.642 0.782 0.692 0.008  -0.130 0.038  448 GLN CCC NE2 
10829 N N   . GLY C 449 ? 0.645 0.757 0.713 0.003  -0.163 0.046  449 GLY CCC N   
10830 C CA  . GLY C 449 ? 0.680 0.791 0.748 0.004  -0.164 0.044  449 GLY CCC CA  
10831 C C   . GLY C 449 ? 0.689 0.806 0.743 0.003  -0.151 0.042  449 GLY CCC C   
10832 O O   . GLY C 449 ? 0.729 0.846 0.783 0.009  -0.147 0.036  449 GLY CCC O   
10833 N N   . GLU C 450 ? 0.691 0.815 0.735 -0.005 -0.145 0.047  450 GLU CCC N   
10834 C CA  . GLU C 450 ? 0.669 0.800 0.700 -0.007 -0.133 0.045  450 GLU CCC CA  
10835 C C   . GLU C 450 ? 0.627 0.762 0.658 0.003  -0.124 0.036  450 GLU CCC C   
10836 O O   . GLU C 450 ? 0.592 0.729 0.618 0.006  -0.118 0.032  450 GLU CCC O   
10837 C CB  . GLU C 450 ? 0.691 0.822 0.719 -0.011 -0.134 0.048  450 GLU CCC CB  
10838 C CG  . GLU C 450 ? 0.718 0.849 0.744 -0.023 -0.142 0.058  450 GLU CCC CG  
10839 C CD  . GLU C 450 ? 0.730 0.865 0.750 -0.030 -0.140 0.061  450 GLU CCC CD  
10840 O OE1 . GLU C 450 ? 0.778 0.908 0.800 -0.025 -0.141 0.057  450 GLU CCC OE1 
10841 O OE2 . GLU C 450 ? 0.730 0.872 0.741 -0.039 -0.138 0.066  450 GLU CCC OE2 
10842 N N   . LYS C 451 ? 0.604 0.739 0.638 0.008  -0.123 0.032  451 LYS CCC N   
10843 C CA  . LYS C 451 ? 0.541 0.681 0.574 0.017  -0.113 0.024  451 LYS CCC CA  
10844 C C   . LYS C 451 ? 0.493 0.640 0.514 0.013  -0.103 0.024  451 LYS CCC C   
10845 O O   . LYS C 451 ? 0.490 0.640 0.505 0.005  -0.102 0.030  451 LYS CCC O   
10846 C CB  . LYS C 451 ? 0.559 0.700 0.597 0.021  -0.114 0.022  451 LYS CCC CB  
10847 C CG  . LYS C 451 ? 0.549 0.693 0.587 0.030  -0.106 0.013  451 LYS CCC CG  
10848 C CD  . LYS C 451 ? 0.559 0.706 0.602 0.034  -0.106 0.011  451 LYS CCC CD  
10849 C CE  . LYS C 451 ? 0.565 0.714 0.612 0.044  -0.103 0.002  451 LYS CCC CE  
10850 N NZ  . LYS C 451 ? 0.566 0.715 0.624 0.048  -0.108 -0.001 451 LYS CCC NZ  
10851 N N   . VAL C 452 ? 0.428 0.578 0.445 0.019  -0.095 0.018  452 VAL CCC N   
10852 C CA  . VAL C 452 ? 0.407 0.563 0.415 0.016  -0.085 0.018  452 VAL CCC CA  
10853 C C   . VAL C 452 ? 0.390 0.551 0.396 0.019  -0.080 0.016  452 VAL CCC C   
10854 O O   . VAL C 452 ? 0.395 0.556 0.406 0.026  -0.079 0.011  452 VAL CCC O   
10855 C CB  . VAL C 452 ? 0.399 0.556 0.404 0.021  -0.080 0.013  452 VAL CCC CB  
10856 C CG1 . VAL C 452 ? 0.401 0.564 0.397 0.018  -0.071 0.012  452 VAL CCC CG1 
10857 C CG2 . VAL C 452 ? 0.415 0.567 0.421 0.018  -0.086 0.015  452 VAL CCC CG2 
10858 N N   . VAL C 453 ? 0.370 0.535 0.371 0.012  -0.077 0.020  453 VAL CCC N   
10859 C CA  . VAL C 453 ? 0.362 0.531 0.361 0.013  -0.072 0.019  453 VAL CCC CA  
10860 C C   . VAL C 453 ? 0.330 0.506 0.322 0.011  -0.063 0.017  453 VAL CCC C   
10861 O O   . VAL C 453 ? 0.318 0.498 0.309 0.014  -0.058 0.015  453 VAL CCC O   
10862 C CB  . VAL C 453 ? 0.381 0.550 0.382 0.008  -0.077 0.024  453 VAL CCC CB  
10863 C CG1 . VAL C 453 ? 0.389 0.551 0.399 0.011  -0.087 0.025  453 VAL CCC CG1 
10864 C CG2 . VAL C 453 ? 0.382 0.553 0.378 -0.002 -0.079 0.030  453 VAL CCC CG2 
10865 N N   . GLY C 454 ? 0.320 0.497 0.308 0.008  -0.062 0.017  454 GLY CCC N   
10866 C CA  . GLY C 454 ? 0.313 0.496 0.295 0.006  -0.054 0.015  454 GLY CCC CA  
10867 C C   . GLY C 454 ? 0.318 0.499 0.298 0.007  -0.052 0.013  454 GLY CCC C   
10868 O O   . GLY C 454 ? 0.339 0.519 0.320 0.003  -0.057 0.016  454 GLY CCC O   
10869 N N   . PHE C 455 ? 0.303 0.487 0.282 0.011  -0.046 0.008  455 PHE CCC N   
10870 C CA  . PHE C 455 ? 0.285 0.468 0.262 0.013  -0.044 0.005  455 PHE CCC CA  
10871 C C   . PHE C 455 ? 0.265 0.455 0.239 0.011  -0.037 0.003  455 PHE CCC C   
10872 O O   . PHE C 455 ? 0.259 0.451 0.232 0.013  -0.033 0.001  455 PHE CCC O   
10873 C CB  . PHE C 455 ? 0.280 0.460 0.261 0.021  -0.044 0.001  455 PHE CCC CB  
10874 C CG  . PHE C 455 ? 0.278 0.457 0.256 0.023  -0.041 -0.002 455 PHE CCC CG  
10875 C CD1 . PHE C 455 ? 0.276 0.460 0.252 0.024  -0.034 -0.005 455 PHE CCC CD1 
10876 C CD2 . PHE C 455 ? 0.275 0.450 0.255 0.024  -0.044 -0.002 455 PHE CCC CD2 
10877 C CE1 . PHE C 455 ? 0.277 0.460 0.252 0.026  -0.031 -0.008 455 PHE CCC CE1 
10878 C CE2 . PHE C 455 ? 0.290 0.465 0.268 0.026  -0.041 -0.005 455 PHE CCC CE2 
10879 C CZ  . PHE C 455 ? 0.275 0.454 0.251 0.027  -0.035 -0.008 455 PHE CCC CZ  
10880 N N   . HIS C 456 ? 0.265 0.457 0.236 0.006  -0.035 0.002  456 HIS CCC N   
10881 C CA  . HIS C 456 ? 0.265 0.464 0.234 0.003  -0.029 -0.000 456 HIS CCC CA  
10882 C C   . HIS C 456 ? 0.273 0.471 0.240 0.003  -0.028 -0.003 456 HIS CCC C   
10883 O O   . HIS C 456 ? 0.271 0.469 0.238 -0.000 -0.031 -0.001 456 HIS CCC O   
10884 C CB  . HIS C 456 ? 0.287 0.492 0.253 -0.005 -0.030 0.003  456 HIS CCC CB  
10885 C CG  . HIS C 456 ? 0.303 0.508 0.269 -0.006 -0.032 0.006  456 HIS CCC CG  
10886 N ND1 . HIS C 456 ? 0.304 0.513 0.270 -0.005 -0.027 0.004  456 HIS CCC ND1 
10887 C CD2 . HIS C 456 ? 0.300 0.501 0.268 -0.007 -0.037 0.010  456 HIS CCC CD2 
10888 C CE1 . HIS C 456 ? 0.308 0.515 0.275 -0.005 -0.030 0.007  456 HIS CCC CE1 
10889 N NE2 . HIS C 456 ? 0.297 0.499 0.265 -0.006 -0.036 0.011  456 HIS CCC NE2 
10890 N N   . PHE C 457 ? 0.268 0.468 0.236 0.007  -0.023 -0.007 457 PHE CCC N   
10891 C CA  . PHE C 457 ? 0.257 0.458 0.225 0.007  -0.021 -0.010 457 PHE CCC CA  
10892 C C   . PHE C 457 ? 0.259 0.466 0.227 0.006  -0.016 -0.014 457 PHE CCC C   
10893 O O   . PHE C 457 ? 0.262 0.469 0.232 0.010  -0.013 -0.016 457 PHE CCC O   
10894 C CB  . PHE C 457 ? 0.248 0.443 0.218 0.014  -0.022 -0.012 457 PHE CCC CB  
10895 C CG  . PHE C 457 ? 0.247 0.442 0.216 0.014  -0.021 -0.014 457 PHE CCC CG  
10896 C CD1 . PHE C 457 ? 0.240 0.435 0.209 0.010  -0.024 -0.013 457 PHE CCC CD1 
10897 C CD2 . PHE C 457 ? 0.232 0.428 0.202 0.017  -0.017 -0.018 457 PHE CCC CD2 
10898 C CE1 . PHE C 457 ? 0.233 0.429 0.202 0.009  -0.023 -0.016 457 PHE CCC CE1 
10899 C CE2 . PHE C 457 ? 0.234 0.431 0.205 0.016  -0.016 -0.021 457 PHE CCC CE2 
10900 C CZ  . PHE C 457 ? 0.232 0.429 0.202 0.013  -0.019 -0.020 457 PHE CCC CZ  
10901 N N   . VAL C 458 ? 0.243 0.456 0.211 0.000  -0.015 -0.016 458 VAL CCC N   
10902 C CA  . VAL C 458 ? 0.238 0.457 0.208 -0.001 -0.010 -0.021 458 VAL CCC CA  
10903 C C   . VAL C 458 ? 0.240 0.457 0.211 0.001  -0.010 -0.024 458 VAL CCC C   
10904 O O   . VAL C 458 ? 0.227 0.443 0.195 -0.002 -0.013 -0.022 458 VAL CCC O   
10905 C CB  . VAL C 458 ? 0.257 0.485 0.225 -0.009 -0.009 -0.022 458 VAL CCC CB  
10906 C CG1 . VAL C 458 ? 0.255 0.490 0.227 -0.010 -0.005 -0.028 458 VAL CCC CG1 
10907 C CG2 . VAL C 458 ? 0.254 0.483 0.221 -0.011 -0.010 -0.018 458 VAL CCC CG2 
10908 N N   . GLY C 459 ? 0.243 0.460 0.218 0.006  -0.007 -0.028 459 GLY CCC N   
10909 C CA  . GLY C 459 ? 0.248 0.463 0.224 0.008  -0.007 -0.031 459 GLY CCC CA  
10910 C C   . GLY C 459 ? 0.242 0.452 0.221 0.014  -0.006 -0.032 459 GLY CCC C   
10911 O O   . GLY C 459 ? 0.260 0.469 0.240 0.017  -0.005 -0.032 459 GLY CCC O   
10912 N N   . PRO C 460 ? 0.251 0.458 0.231 0.017  -0.006 -0.034 460 PRO CCC N   
10913 C CA  . PRO C 460 ? 0.253 0.456 0.235 0.023  -0.005 -0.035 460 PRO CCC CA  
10914 C C   . PRO C 460 ? 0.261 0.459 0.241 0.027  -0.007 -0.032 460 PRO CCC C   
10915 O O   . PRO C 460 ? 0.280 0.475 0.257 0.027  -0.009 -0.029 460 PRO CCC O   
10916 C CB  . PRO C 460 ? 0.247 0.449 0.231 0.024  -0.006 -0.038 460 PRO CCC CB  
10917 C CG  . PRO C 460 ? 0.256 0.463 0.240 0.018  -0.006 -0.039 460 PRO CCC CG  
10918 C CD  . PRO C 460 ? 0.254 0.462 0.234 0.014  -0.007 -0.036 460 PRO CCC CD  
10919 N N   . ASN C 461 ? 0.256 0.453 0.238 0.031  -0.006 -0.032 461 ASN CCC N   
10920 C CA  . ASN C 461 ? 0.271 0.464 0.251 0.036  -0.007 -0.029 461 ASN CCC CA  
10921 C C   . ASN C 461 ? 0.269 0.462 0.246 0.035  -0.009 -0.026 461 ASN CCC C   
10922 O O   . ASN C 461 ? 0.255 0.445 0.230 0.037  -0.011 -0.025 461 ASN CCC O   
10923 C CB  . ASN C 461 ? 0.274 0.463 0.252 0.039  -0.009 -0.029 461 ASN CCC CB  
10924 C CG  . ASN C 461 ? 0.291 0.481 0.273 0.038  -0.008 -0.032 461 ASN CCC CG  
10925 O OD1 . ASN C 461 ? 0.291 0.481 0.275 0.040  -0.007 -0.033 461 ASN CCC OD1 
10926 N ND2 . ASN C 461 ? 0.275 0.464 0.257 0.037  -0.009 -0.034 461 ASN CCC ND2 
10927 N N   . ALA C 462 ? 0.252 0.449 0.229 0.031  -0.008 -0.026 462 ALA CCC N   
10928 C CA  . ALA C 462 ? 0.296 0.493 0.271 0.029  -0.010 -0.023 462 ALA CCC CA  
10929 C C   . ALA C 462 ? 0.323 0.518 0.298 0.034  -0.010 -0.021 462 ALA CCC C   
10930 O O   . ALA C 462 ? 0.358 0.551 0.332 0.034  -0.013 -0.019 462 ALA CCC O   
10931 C CB  . ALA C 462 ? 0.280 0.481 0.255 0.024  -0.008 -0.023 462 ALA CCC CB  
10932 N N   . GLY C 463 ? 0.317 0.513 0.294 0.036  -0.008 -0.022 463 GLY CCC N   
10933 C CA  . GLY C 463 ? 0.368 0.564 0.344 0.040  -0.008 -0.020 463 GLY CCC CA  
10934 C C   . GLY C 463 ? 0.361 0.555 0.337 0.045  -0.010 -0.021 463 GLY CCC C   
10935 O O   . GLY C 463 ? 0.364 0.557 0.340 0.047  -0.012 -0.020 463 GLY CCC O   
10936 N N   . GLU C 464 ? 0.366 0.558 0.341 0.045  -0.010 -0.023 464 GLU CCC N   
10937 C CA  . GLU C 464 ? 0.373 0.562 0.347 0.049  -0.012 -0.024 464 GLU CCC CA  
10938 C C   . GLU C 464 ? 0.356 0.542 0.330 0.049  -0.016 -0.023 464 GLU CCC C   
10939 O O   . GLU C 464 ? 0.368 0.553 0.343 0.052  -0.018 -0.024 464 GLU CCC O   
10940 C CB  . GLU C 464 ? 0.374 0.562 0.349 0.049  -0.011 -0.025 464 GLU CCC CB  
10941 C CG  . GLU C 464 ? 0.387 0.578 0.363 0.050  -0.009 -0.025 464 GLU CCC CG  
10942 C CD  . GLU C 464 ? 0.390 0.584 0.366 0.053  -0.008 -0.024 464 GLU CCC CD  
10943 O OE1 . GLU C 464 ? 0.426 0.619 0.400 0.056  -0.010 -0.024 464 GLU CCC OE1 
10944 O OE2 . GLU C 464 ? 0.372 0.568 0.350 0.052  -0.007 -0.023 464 GLU CCC OE2 
10945 N N   . ILE C 465 ? 0.325 0.511 0.299 0.044  -0.016 -0.022 465 ILE CCC N   
10946 C CA  . ILE C 465 ? 0.318 0.501 0.292 0.043  -0.021 -0.021 465 ILE CCC CA  
10947 C C   . ILE C 465 ? 0.324 0.507 0.299 0.043  -0.022 -0.019 465 ILE CCC C   
10948 O O   . ILE C 465 ? 0.343 0.523 0.319 0.045  -0.027 -0.019 465 ILE CCC O   
10949 C CB  . ILE C 465 ? 0.306 0.489 0.279 0.037  -0.021 -0.020 465 ILE CCC CB  
10950 C CG1 . ILE C 465 ? 0.327 0.509 0.300 0.037  -0.020 -0.022 465 ILE CCC CG1 
10951 C CG2 . ILE C 465 ? 0.322 0.503 0.295 0.034  -0.025 -0.017 465 ILE CCC CG2 
10952 C CD1 . ILE C 465 ? 0.304 0.489 0.277 0.031  -0.019 -0.022 465 ILE CCC CD1 
10953 N N   . THR C 466 ? 0.312 0.498 0.287 0.042  -0.020 -0.018 466 THR CCC N   
10954 C CA  . THR C 466 ? 0.322 0.508 0.298 0.041  -0.022 -0.016 466 THR CCC CA  
10955 C C   . THR C 466 ? 0.322 0.509 0.300 0.047  -0.023 -0.018 466 THR CCC C   
10956 O O   . THR C 466 ? 0.306 0.492 0.286 0.047  -0.026 -0.017 466 THR CCC O   
10957 C CB  . THR C 466 ? 0.309 0.500 0.284 0.037  -0.019 -0.015 466 THR CCC CB  
10958 O OG1 . THR C 466 ? 0.347 0.538 0.320 0.032  -0.019 -0.014 466 THR CCC OG1 
10959 C CG2 . THR C 466 ? 0.307 0.498 0.283 0.037  -0.020 -0.013 466 THR CCC CG2 
10960 N N   . GLN C 467 ? 0.311 0.501 0.289 0.050  -0.020 -0.020 467 GLN CCC N   
10961 C CA  . GLN C 467 ? 0.316 0.508 0.295 0.055  -0.020 -0.021 467 GLN CCC CA  
10962 C C   . GLN C 467 ? 0.317 0.506 0.299 0.058  -0.024 -0.023 467 GLN CCC C   
10963 O O   . GLN C 467 ? 0.378 0.569 0.363 0.059  -0.026 -0.023 467 GLN CCC O   
10964 C CB  . GLN C 467 ? 0.300 0.495 0.278 0.058  -0.017 -0.023 467 GLN CCC CB  
10965 C CG  . GLN C 467 ? 0.305 0.505 0.284 0.062  -0.016 -0.024 467 GLN CCC CG  
10966 C CD  . GLN C 467 ? 0.297 0.500 0.275 0.060  -0.014 -0.022 467 GLN CCC CD  
10967 O OE1 . GLN C 467 ? 0.280 0.486 0.257 0.059  -0.011 -0.021 467 GLN CCC OE1 
10968 N NE2 . GLN C 467 ? 0.303 0.506 0.284 0.061  -0.016 -0.022 467 GLN CCC NE2 
10969 N N   . GLY C 468 ? 0.313 0.499 0.295 0.059  -0.026 -0.024 468 GLY CCC N   
10970 C CA  . GLY C 468 ? 0.325 0.509 0.311 0.062  -0.031 -0.026 468 GLY CCC CA  
10971 C C   . GLY C 468 ? 0.329 0.509 0.318 0.059  -0.036 -0.024 468 GLY CCC C   
10972 O O   . GLY C 468 ? 0.329 0.509 0.323 0.062  -0.040 -0.026 468 GLY CCC O   
10973 N N   . PHE C 469 ? 0.343 0.521 0.330 0.054  -0.036 -0.020 469 PHE CCC N   
10974 C CA  . PHE C 469 ? 0.353 0.528 0.342 0.050  -0.041 -0.017 469 PHE CCC CA  
10975 C C   . PHE C 469 ? 0.377 0.553 0.367 0.050  -0.041 -0.016 469 PHE CCC C   
10976 O O   . PHE C 469 ? 0.437 0.611 0.432 0.050  -0.047 -0.015 469 PHE CCC O   
10977 C CB  . PHE C 469 ? 0.357 0.531 0.342 0.043  -0.040 -0.013 469 PHE CCC CB  
10978 C CG  . PHE C 469 ? 0.339 0.509 0.323 0.042  -0.043 -0.014 469 PHE CCC CG  
10979 C CD1 . PHE C 469 ? 0.332 0.497 0.321 0.043  -0.050 -0.013 469 PHE CCC CD1 
10980 C CD2 . PHE C 469 ? 0.331 0.502 0.312 0.041  -0.039 -0.014 469 PHE CCC CD2 
10981 C CE1 . PHE C 469 ? 0.333 0.495 0.322 0.041  -0.053 -0.012 469 PHE CCC CE1 
10982 C CE2 . PHE C 469 ? 0.325 0.493 0.306 0.039  -0.042 -0.014 469 PHE CCC CE2 
10983 C CZ  . PHE C 469 ? 0.325 0.489 0.310 0.040  -0.049 -0.013 469 PHE CCC CZ  
10984 N N   . SER C 470 ? 0.366 0.548 0.354 0.050  -0.036 -0.016 470 SER CCC N   
10985 C CA  . SER C 470 ? 0.352 0.536 0.341 0.051  -0.035 -0.016 470 SER CCC CA  
10986 C C   . SER C 470 ? 0.349 0.533 0.343 0.057  -0.039 -0.019 470 SER CCC C   
10987 O O   . SER C 470 ? 0.362 0.546 0.361 0.056  -0.042 -0.018 470 SER CCC O   
10988 C CB  . SER C 470 ? 0.339 0.528 0.325 0.051  -0.029 -0.016 470 SER CCC CB  
10989 O OG  . SER C 470 ? 0.328 0.520 0.314 0.055  -0.026 -0.019 470 SER CCC OG  
10990 N N   . LEU C 471 ? 0.363 0.549 0.358 0.061  -0.038 -0.023 471 LEU CCC N   
10991 C CA  . LEU C 471 ? 0.368 0.556 0.370 0.067  -0.041 -0.028 471 LEU CCC CA  
10992 C C   . LEU C 471 ? 0.410 0.592 0.417 0.067  -0.049 -0.027 471 LEU CCC C   
10993 O O   . LEU C 471 ? 0.442 0.623 0.455 0.069  -0.053 -0.029 471 LEU CCC O   
10994 C CB  . LEU C 471 ? 0.364 0.556 0.365 0.071  -0.039 -0.032 471 LEU CCC CB  
10995 C CG  . LEU C 471 ? 0.359 0.554 0.366 0.077  -0.042 -0.038 471 LEU CCC CG  
10996 C CD1 . LEU C 471 ? 0.359 0.559 0.369 0.079  -0.041 -0.039 471 LEU CCC CD1 
10997 C CD2 . LEU C 471 ? 0.352 0.551 0.357 0.081  -0.039 -0.042 471 LEU CCC CD2 
10998 N N   . ALA C 472 ? 0.429 0.606 0.435 0.064  -0.051 -0.026 472 ALA CCC N   
10999 C CA  . ALA C 472 ? 0.438 0.607 0.449 0.063  -0.059 -0.024 472 ALA CCC CA  
11000 C C   . ALA C 472 ? 0.461 0.629 0.474 0.059  -0.063 -0.020 472 ALA CCC C   
11001 O O   . ALA C 472 ? 0.469 0.633 0.489 0.060  -0.070 -0.020 472 ALA CCC O   
11002 C CB  . ALA C 472 ? 0.428 0.594 0.436 0.060  -0.060 -0.022 472 ALA CCC CB  
11003 N N   . VAL C 473 ? 0.459 0.629 0.466 0.054  -0.058 -0.015 473 VAL CCC N   
11004 C CA  . VAL C 473 ? 0.472 0.640 0.480 0.049  -0.061 -0.010 473 VAL CCC CA  
11005 C C   . VAL C 473 ? 0.499 0.669 0.512 0.053  -0.063 -0.013 473 VAL CCC C   
11006 O O   . VAL C 473 ? 0.520 0.687 0.539 0.052  -0.069 -0.011 473 VAL CCC O   
11007 C CB  . VAL C 473 ? 0.489 0.660 0.490 0.042  -0.056 -0.006 473 VAL CCC CB  
11008 C CG1 . VAL C 473 ? 0.531 0.702 0.532 0.038  -0.059 -0.002 473 VAL CCC CG1 
11009 C CG2 . VAL C 473 ? 0.479 0.647 0.475 0.037  -0.057 -0.004 473 VAL CCC CG2 
11010 N N   . LYS C 474 ? 0.484 0.660 0.496 0.058  -0.057 -0.017 474 LYS CCC N   
11011 C CA  . LYS C 474 ? 0.481 0.661 0.497 0.062  -0.057 -0.020 474 LYS CCC CA  
11012 C C   . LYS C 474 ? 0.499 0.677 0.525 0.067  -0.064 -0.025 474 LYS CCC C   
11013 O O   . LYS C 474 ? 0.507 0.686 0.540 0.068  -0.068 -0.025 474 LYS CCC O   
11014 C CB  . LYS C 474 ? 0.468 0.656 0.481 0.065  -0.049 -0.024 474 LYS CCC CB  
11015 C CG  . LYS C 474 ? 0.450 0.644 0.467 0.069  -0.048 -0.027 474 LYS CCC CG  
11016 C CD  . LYS C 474 ? 0.432 0.633 0.445 0.071  -0.041 -0.029 474 LYS CCC CD  
11017 C CE  . LYS C 474 ? 0.408 0.615 0.423 0.073  -0.039 -0.030 474 LYS CCC CE  
11018 N NZ  . LYS C 474 ? 0.417 0.631 0.426 0.073  -0.032 -0.031 474 LYS CCC NZ  
11019 N N   . LEU C 475 ? 0.518 0.694 0.547 0.069  -0.066 -0.028 475 LEU CCC N   
11020 C CA  . LEU C 475 ? 0.545 0.718 0.583 0.074  -0.073 -0.033 475 LEU CCC CA  
11021 C C   . LEU C 475 ? 0.561 0.727 0.606 0.071  -0.083 -0.028 475 LEU CCC C   
11022 O O   . LEU C 475 ? 0.635 0.798 0.689 0.075  -0.090 -0.032 475 LEU CCC O   
11023 C CB  . LEU C 475 ? 0.528 0.703 0.566 0.078  -0.072 -0.038 475 LEU CCC CB  
11024 C CG  . LEU C 475 ? 0.547 0.731 0.582 0.082  -0.065 -0.043 475 LEU CCC CG  
11025 C CD1 . LEU C 475 ? 0.556 0.741 0.589 0.085  -0.064 -0.047 475 LEU CCC CD1 
11026 C CD2 . LEU C 475 ? 0.541 0.731 0.583 0.088  -0.066 -0.049 475 LEU CCC CD2 
11027 N N   . GLY C 476 ? 0.546 0.707 0.585 0.063  -0.083 -0.021 476 GLY CCC N   
11028 C CA  . GLY C 476 ? 0.514 0.668 0.557 0.059  -0.092 -0.015 476 GLY CCC CA  
11029 C C   . GLY C 476 ? 0.503 0.652 0.547 0.055  -0.096 -0.012 476 GLY CCC C   
11030 O O   . GLY C 476 ? 0.541 0.683 0.592 0.054  -0.106 -0.010 476 GLY CCC O   
11031 N N   . ALA C 477 ? 0.504 0.654 0.538 0.053  -0.090 -0.011 477 ALA CCC N   
11032 C CA  . ALA C 477 ? 0.517 0.663 0.550 0.049  -0.093 -0.008 477 ALA CCC CA  
11033 C C   . ALA C 477 ? 0.522 0.664 0.553 0.040  -0.099 0.000  477 ALA CCC C   
11034 O O   . ALA C 477 ? 0.508 0.653 0.534 0.036  -0.095 0.004  477 ALA CCC O   
11035 C CB  . ALA C 477 ? 0.513 0.663 0.536 0.048  -0.084 -0.009 477 ALA CCC CB  
11036 N N   . THR C 478 ? 0.500 0.636 0.537 0.038  -0.107 0.003  478 THR CCC N   
11037 C CA  . THR C 478 ? 0.503 0.636 0.539 0.029  -0.113 0.012  478 THR CCC CA  
11038 C C   . THR C 478 ? 0.519 0.653 0.548 0.023  -0.111 0.015  478 THR CCC C   
11039 O O   . THR C 478 ? 0.478 0.613 0.505 0.028  -0.106 0.010  478 THR CCC O   
11040 C CB  . THR C 478 ? 0.523 0.649 0.571 0.030  -0.126 0.014  478 THR CCC CB  
11041 O OG1 . THR C 478 ? 0.532 0.654 0.584 0.034  -0.128 0.010  478 THR CCC OG1 
11042 C CG2 . THR C 478 ? 0.532 0.656 0.590 0.036  -0.130 0.009  478 THR CCC CG2 
11043 N N   . LYS C 479 ? 0.493 0.627 0.517 0.014  -0.114 0.023  479 LYS CCC N   
11044 C CA  . LYS C 479 ? 0.500 0.635 0.519 0.008  -0.112 0.026  479 LYS CCC CA  
11045 C C   . LYS C 479 ? 0.514 0.643 0.538 0.012  -0.118 0.024  479 LYS CCC C   
11046 O O   . LYS C 479 ? 0.499 0.629 0.518 0.012  -0.113 0.022  479 LYS CCC O   
11047 C CB  . LYS C 479 ? 0.486 0.623 0.500 -0.003 -0.116 0.035  479 LYS CCC CB  
11048 C CG  . LYS C 479 ? 0.461 0.602 0.469 -0.010 -0.114 0.038  479 LYS CCC CG  
11049 C CD  . LYS C 479 ? 0.454 0.600 0.454 -0.008 -0.103 0.032  479 LYS CCC CD  
11050 C CE  . LYS C 479 ? 0.427 0.579 0.420 -0.016 -0.100 0.035  479 LYS CCC CE  
11051 N NZ  . LYS C 479 ? 0.424 0.572 0.420 -0.019 -0.107 0.039  479 LYS CCC NZ  
11052 N N   . LYS C 480 ? 0.535 0.657 0.570 0.015  -0.127 0.024  480 LYS CCC N   
11053 C CA  . LYS C 480 ? 0.551 0.667 0.593 0.019  -0.134 0.021  480 LYS CCC CA  
11054 C C   . LYS C 480 ? 0.514 0.632 0.554 0.028  -0.126 0.012  480 LYS CCC C   
11055 O O   . LYS C 480 ? 0.518 0.635 0.556 0.028  -0.125 0.011  480 LYS CCC O   
11056 C CB  . LYS C 480 ? 0.582 0.691 0.638 0.021  -0.146 0.022  480 LYS CCC CB  
11057 C CG  . LYS C 480 ? 0.599 0.701 0.663 0.026  -0.153 0.018  480 LYS CCC CG  
11058 C CD  . LYS C 480 ? 0.642 0.736 0.718 0.023  -0.168 0.023  480 LYS CCC CD  
11059 C CE  . LYS C 480 ? 0.659 0.747 0.748 0.031  -0.175 0.017  480 LYS CCC CE  
11060 N NZ  . LYS C 480 ? 0.686 0.775 0.771 0.033  -0.171 0.013  480 LYS CCC NZ  
11061 N N   . ASP C 481 ? 0.493 0.615 0.534 0.034  -0.121 0.006  481 ASP CCC N   
11062 C CA  . ASP C 481 ? 0.482 0.608 0.521 0.042  -0.113 -0.002 481 ASP CCC CA  
11063 C C   . ASP C 481 ? 0.444 0.574 0.473 0.039  -0.105 -0.002 481 ASP CCC C   
11064 O O   . ASP C 481 ? 0.435 0.565 0.463 0.044  -0.102 -0.006 481 ASP CCC O   
11065 C CB  . ASP C 481 ? 0.476 0.607 0.516 0.047  -0.108 -0.007 481 ASP CCC CB  
11066 C CG  . ASP C 481 ? 0.500 0.628 0.551 0.052  -0.116 -0.009 481 ASP CCC CG  
11067 O OD1 . ASP C 481 ? 0.527 0.650 0.587 0.055  -0.124 -0.012 481 ASP CCC OD1 
11068 O OD2 . ASP C 481 ? 0.524 0.655 0.575 0.053  -0.113 -0.010 481 ASP CCC OD2 
11069 N N   . PHE C 482 ? 0.437 0.570 0.458 0.032  -0.101 0.004  482 PHE CCC N   
11070 C CA  . PHE C 482 ? 0.432 0.570 0.444 0.029  -0.093 0.004  482 PHE CCC CA  
11071 C C   . PHE C 482 ? 0.429 0.564 0.441 0.025  -0.097 0.007  482 PHE CCC C   
11072 O O   . PHE C 482 ? 0.406 0.542 0.414 0.027  -0.092 0.004  482 PHE CCC O   
11073 C CB  . PHE C 482 ? 0.416 0.559 0.421 0.022  -0.089 0.009  482 PHE CCC CB  
11074 C CG  . PHE C 482 ? 0.391 0.540 0.393 0.026  -0.081 0.005  482 PHE CCC CG  
11075 C CD1 . PHE C 482 ? 0.403 0.551 0.409 0.029  -0.082 0.004  482 PHE CCC CD1 
11076 C CD2 . PHE C 482 ? 0.392 0.546 0.388 0.025  -0.072 0.003  482 PHE CCC CD2 
11077 C CE1 . PHE C 482 ? 0.381 0.534 0.384 0.032  -0.075 0.001  482 PHE CCC CE1 
11078 C CE2 . PHE C 482 ? 0.376 0.534 0.369 0.028  -0.065 -0.000 482 PHE CCC CE2 
11079 C CZ  . PHE C 482 ? 0.386 0.544 0.382 0.031  -0.067 -0.001 482 PHE CCC CZ  
11080 N N   . ASP C 483 ? 0.452 0.582 0.467 0.019  -0.106 0.013  483 ASP CCC N   
11081 C CA  . ASP C 483 ? 0.482 0.609 0.498 0.015  -0.111 0.016  483 ASP CCC CA  
11082 C C   . ASP C 483 ? 0.511 0.632 0.532 0.023  -0.114 0.010  483 ASP CCC C   
11083 O O   . ASP C 483 ? 0.571 0.692 0.590 0.021  -0.113 0.011  483 ASP CCC O   
11084 C CB  . ASP C 483 ? 0.482 0.606 0.503 0.007  -0.121 0.024  483 ASP CCC CB  
11085 C CG  . ASP C 483 ? 0.491 0.620 0.505 -0.002 -0.119 0.031  483 ASP CCC CG  
11086 O OD1 . ASP C 483 ? 0.507 0.643 0.512 -0.004 -0.110 0.029  483 ASP CCC OD1 
11087 O OD2 . ASP C 483 ? 0.501 0.628 0.518 -0.008 -0.128 0.038  483 ASP CCC OD2 
11088 N N   . ASP C 484 ? 0.491 0.610 0.521 0.030  -0.117 0.005  484 ASP CCC N   
11089 C CA  . ASP C 484 ? 0.505 0.620 0.541 0.038  -0.120 -0.001 484 ASP CCC CA  
11090 C C   . ASP C 484 ? 0.489 0.609 0.521 0.045  -0.111 -0.008 484 ASP CCC C   
11091 O O   . ASP C 484 ? 0.439 0.557 0.475 0.051  -0.112 -0.014 484 ASP CCC O   
11092 C CB  . ASP C 484 ? 0.542 0.652 0.590 0.043  -0.129 -0.003 484 ASP CCC CB  
11093 C CG  . ASP C 484 ? 0.568 0.673 0.623 0.036  -0.140 0.005  484 ASP CCC CG  
11094 O OD1 . ASP C 484 ? 0.577 0.682 0.627 0.027  -0.141 0.012  484 ASP CCC OD1 
11095 O OD2 . ASP C 484 ? 0.600 0.700 0.665 0.040  -0.148 0.003  484 ASP CCC OD2 
11096 N N   . MET C 485 ? 0.470 0.596 0.493 0.044  -0.102 -0.008 485 MET CCC N   
11097 C CA  . MET C 485 ? 0.457 0.588 0.475 0.049  -0.092 -0.014 485 MET CCC CA  
11098 C C   . MET C 485 ? 0.474 0.604 0.488 0.047  -0.090 -0.014 485 MET CCC C   
11099 O O   . MET C 485 ? 0.438 0.569 0.447 0.039  -0.089 -0.009 485 MET CCC O   
11100 C CB  . MET C 485 ? 0.451 0.588 0.463 0.046  -0.085 -0.013 485 MET CCC CB  
11101 C CG  . MET C 485 ? 0.420 0.562 0.426 0.050  -0.076 -0.017 485 MET CCC CG  
11102 S SD  . MET C 485 ? 0.451 0.600 0.451 0.046  -0.068 -0.015 485 MET CCC SD  
11103 C CE  . MET C 485 ? 0.445 0.593 0.440 0.036  -0.069 -0.008 485 MET CCC CE  
11104 N N   . ILE C 486 ? 0.473 0.603 0.488 0.053  -0.089 -0.020 486 ILE CCC N   
11105 C CA  . ILE C 486 ? 0.461 0.592 0.472 0.052  -0.086 -0.021 486 ILE CCC CA  
11106 C C   . ILE C 486 ? 0.436 0.573 0.439 0.051  -0.076 -0.021 486 ILE CCC C   
11107 O O   . ILE C 486 ? 0.399 0.539 0.400 0.055  -0.071 -0.024 486 ILE CCC O   
11108 C CB  . ILE C 486 ? 0.491 0.619 0.506 0.059  -0.088 -0.027 486 ILE CCC CB  
11109 C CG1 . ILE C 486 ? 0.511 0.633 0.535 0.062  -0.097 -0.028 486 ILE CCC CG1 
11110 C CG2 . ILE C 486 ? 0.526 0.653 0.536 0.057  -0.085 -0.026 486 ILE CCC CG2 
11111 C CD1 . ILE C 486 ? 0.525 0.641 0.552 0.056  -0.105 -0.022 486 ILE CCC CD1 
11112 N N   . GLY C 487 ? 0.425 0.562 0.423 0.045  -0.074 -0.018 487 GLY CCC N   
11113 C CA  . GLY C 487 ? 0.401 0.544 0.393 0.043  -0.066 -0.018 487 GLY CCC CA  
11114 C C   . GLY C 487 ? 0.389 0.533 0.379 0.048  -0.062 -0.023 487 GLY CCC C   
11115 O O   . GLY C 487 ? 0.350 0.489 0.342 0.051  -0.066 -0.025 487 GLY CCC O   
11116 N N   . ILE C 488 ? 0.395 0.543 0.381 0.049  -0.055 -0.025 488 ILE CCC N   
11117 C CA  . ILE C 488 ? 0.404 0.554 0.387 0.051  -0.050 -0.028 488 ILE CCC CA  
11118 C C   . ILE C 488 ? 0.397 0.549 0.377 0.045  -0.048 -0.026 488 ILE CCC C   
11119 O O   . ILE C 488 ? 0.421 0.576 0.399 0.041  -0.045 -0.024 488 ILE CCC O   
11120 C CB  . ILE C 488 ? 0.405 0.559 0.387 0.055  -0.045 -0.030 488 ILE CCC CB  
11121 C CG1 . ILE C 488 ? 0.412 0.566 0.396 0.060  -0.047 -0.032 488 ILE CCC CG1 
11122 C CG2 . ILE C 488 ? 0.381 0.536 0.360 0.058  -0.042 -0.033 488 ILE CCC CG2 
11123 C CD1 . ILE C 488 ? 0.416 0.576 0.399 0.063  -0.042 -0.034 488 ILE CCC CD1 
11124 N N   . HIS C 489 ? 0.414 0.564 0.394 0.045  -0.048 -0.027 489 HIS CCC N   
11125 C CA  . HIS C 489 ? 0.415 0.567 0.393 0.039  -0.046 -0.026 489 HIS CCC CA  
11126 C C   . HIS C 489 ? 0.372 0.525 0.349 0.042  -0.042 -0.029 489 HIS CCC C   
11127 O O   . HIS C 489 ? 0.347 0.497 0.324 0.048  -0.043 -0.032 489 HIS CCC O   
11128 C CB  . HIS C 489 ? 0.447 0.595 0.426 0.036  -0.052 -0.023 489 HIS CCC CB  
11129 C CG  . HIS C 489 ? 0.447 0.599 0.424 0.030  -0.050 -0.022 489 HIS CCC CG  
11130 N ND1 . HIS C 489 ? 0.491 0.649 0.467 0.023  -0.048 -0.020 489 HIS CCC ND1 
11131 C CD2 . HIS C 489 ? 0.461 0.612 0.438 0.028  -0.051 -0.023 489 HIS CCC CD2 
11132 C CE1 . HIS C 489 ? 0.495 0.656 0.469 0.018  -0.047 -0.020 489 HIS CCC CE1 
11133 N NE2 . HIS C 489 ? 0.461 0.618 0.436 0.021  -0.049 -0.022 489 HIS CCC NE2 
11134 N N   . PRO C 490 ? 0.342 0.500 0.317 0.039  -0.038 -0.030 490 PRO CCC N   
11135 C CA  . PRO C 490 ? 0.318 0.480 0.292 0.033  -0.036 -0.028 490 PRO CCC CA  
11136 C C   . PRO C 490 ? 0.311 0.476 0.285 0.035  -0.032 -0.029 490 PRO CCC C   
11137 O O   . PRO C 490 ? 0.312 0.478 0.286 0.038  -0.029 -0.031 490 PRO CCC O   
11138 C CB  . PRO C 490 ? 0.316 0.482 0.290 0.030  -0.033 -0.030 490 PRO CCC CB  
11139 C CG  . PRO C 490 ? 0.332 0.494 0.307 0.034  -0.033 -0.033 490 PRO CCC CG  
11140 C CD  . PRO C 490 ? 0.328 0.486 0.303 0.041  -0.034 -0.033 490 PRO CCC CD  
11141 N N   . THR C 491 ? 0.292 0.458 0.265 0.032  -0.034 -0.026 491 THR CCC N   
11142 C CA  . THR C 491 ? 0.282 0.451 0.255 0.033  -0.030 -0.026 491 THR CCC CA  
11143 C C   . THR C 491 ? 0.267 0.441 0.239 0.026  -0.030 -0.023 491 THR CCC C   
11144 O O   . THR C 491 ? 0.255 0.429 0.227 0.022  -0.033 -0.021 491 THR CCC O   
11145 C CB  . THR C 491 ? 0.277 0.444 0.251 0.038  -0.032 -0.026 491 THR CCC CB  
11146 O OG1 . THR C 491 ? 0.278 0.442 0.253 0.037  -0.037 -0.023 491 THR CCC OG1 
11147 C CG2 . THR C 491 ? 0.273 0.437 0.247 0.044  -0.032 -0.028 491 THR CCC CG2 
11148 N N   . ASP C 492 ? 0.282 0.460 0.254 0.025  -0.027 -0.024 492 ASP CCC N   
11149 C CA  . ASP C 492 ? 0.295 0.477 0.266 0.020  -0.027 -0.021 492 ASP CCC CA  
11150 C C   . ASP C 492 ? 0.300 0.478 0.271 0.021  -0.031 -0.018 492 ASP CCC C   
11151 O O   . ASP C 492 ? 0.318 0.497 0.288 0.016  -0.034 -0.014 492 ASP CCC O   
11152 C CB  . ASP C 492 ? 0.290 0.477 0.261 0.018  -0.022 -0.023 492 ASP CCC CB  
11153 C CG  . ASP C 492 ? 0.303 0.494 0.275 0.016  -0.019 -0.027 492 ASP CCC CG  
11154 O OD1 . ASP C 492 ? 0.338 0.530 0.310 0.013  -0.020 -0.027 492 ASP CCC OD1 
11155 O OD2 . ASP C 492 ? 0.285 0.480 0.259 0.017  -0.015 -0.030 492 ASP CCC OD2 
11156 N N   . ALA C 493 ? 0.294 0.468 0.267 0.028  -0.032 -0.019 493 ALA CCC N   
11157 C CA  . ALA C 493 ? 0.308 0.480 0.282 0.029  -0.035 -0.016 493 ALA CCC CA  
11158 C C   . ALA C 493 ? 0.315 0.482 0.291 0.028  -0.042 -0.014 493 ALA CCC C   
11159 O O   . ALA C 493 ? 0.294 0.459 0.271 0.028  -0.045 -0.012 493 ALA CCC O   
11160 C CB  . ALA C 493 ? 0.311 0.482 0.286 0.037  -0.034 -0.019 493 ALA CCC CB  
11161 N N   . GLU C 494 ? 0.345 0.509 0.320 0.028  -0.043 -0.015 494 GLU CCC N   
11162 C CA  . GLU C 494 ? 0.372 0.531 0.350 0.027  -0.050 -0.012 494 GLU CCC CA  
11163 C C   . GLU C 494 ? 0.364 0.526 0.341 0.019  -0.053 -0.007 494 GLU CCC C   
11164 O O   . GLU C 494 ? 0.343 0.501 0.323 0.017  -0.060 -0.003 494 GLU CCC O   
11165 C CB  . GLU C 494 ? 0.412 0.569 0.390 0.028  -0.051 -0.014 494 GLU CCC CB  
11166 C CG  . GLU C 494 ? 0.452 0.613 0.427 0.022  -0.048 -0.014 494 GLU CCC CG  
11167 C CD  . GLU C 494 ? 0.509 0.668 0.485 0.023  -0.050 -0.015 494 GLU CCC CD  
11168 O OE1 . GLU C 494 ? 0.489 0.642 0.467 0.025  -0.056 -0.013 494 GLU CCC OE1 
11169 O OE2 . GLU C 494 ? 0.558 0.720 0.532 0.023  -0.046 -0.018 494 GLU CCC OE2 
11170 N N   . VAL C 495 ? 0.362 0.530 0.335 0.013  -0.049 -0.006 495 VAL CCC N   
11171 C CA  . VAL C 495 ? 0.356 0.528 0.328 0.005  -0.051 -0.001 495 VAL CCC CA  
11172 C C   . VAL C 495 ? 0.339 0.507 0.314 0.005  -0.057 0.002  495 VAL CCC C   
11173 O O   . VAL C 495 ? 0.323 0.490 0.298 -0.001 -0.063 0.007  495 VAL CCC O   
11174 C CB  . VAL C 495 ? 0.359 0.539 0.327 -0.000 -0.045 -0.003 495 VAL CCC CB  
11175 C CG1 . VAL C 495 ? 0.364 0.546 0.333 0.003  -0.042 -0.004 495 VAL CCC CG1 
11176 C CG2 . VAL C 495 ? 0.351 0.537 0.317 -0.010 -0.048 0.002  495 VAL CCC CG2 
11177 N N   . PHE C 496 ? 0.346 0.512 0.322 0.011  -0.055 -0.000 496 PHE CCC N   
11178 C CA  . PHE C 496 ? 0.351 0.515 0.331 0.012  -0.060 0.003  496 PHE CCC CA  
11179 C C   . PHE C 496 ? 0.352 0.508 0.337 0.014  -0.068 0.005  496 PHE CCC C   
11180 O O   . PHE C 496 ? 0.368 0.522 0.357 0.014  -0.073 0.007  496 PHE CCC O   
11181 C CB  . PHE C 496 ? 0.358 0.522 0.339 0.019  -0.056 -0.001 496 PHE CCC CB  
11182 C CG  . PHE C 496 ? 0.365 0.535 0.341 0.016  -0.050 -0.001 496 PHE CCC CG  
11183 C CD1 . PHE C 496 ? 0.370 0.543 0.347 0.011  -0.051 0.003  496 PHE CCC CD1 
11184 C CD2 . PHE C 496 ? 0.375 0.549 0.350 0.018  -0.043 -0.005 496 PHE CCC CD2 
11185 C CE1 . PHE C 496 ? 0.384 0.563 0.357 0.008  -0.046 0.002  496 PHE CCC CE1 
11186 C CE2 . PHE C 496 ? 0.376 0.556 0.348 0.015  -0.038 -0.006 496 PHE CCC CE2 
11187 C CZ  . PHE C 496 ? 0.394 0.576 0.365 0.010  -0.039 -0.002 496 PHE CCC CZ  
11188 N N   . GLY C 497 ? 0.357 0.510 0.343 0.015  -0.070 0.004  497 GLY CCC N   
11189 C CA  . GLY C 497 ? 0.403 0.550 0.395 0.016  -0.079 0.006  497 GLY CCC CA  
11190 C C   . GLY C 497 ? 0.417 0.563 0.409 0.007  -0.085 0.012  497 GLY CCC C   
11191 O O   . GLY C 497 ? 0.486 0.625 0.482 0.007  -0.093 0.014  497 GLY CCC O   
11192 N N   . ILE C 498 ? 0.403 0.555 0.388 -0.000 -0.081 0.014  498 ILE CCC N   
11193 C CA  . ILE C 498 ? 0.440 0.593 0.423 -0.010 -0.086 0.020  498 ILE CCC CA  
11194 C C   . ILE C 498 ? 0.443 0.605 0.422 -0.019 -0.084 0.024  498 ILE CCC C   
11195 O O   . ILE C 498 ? 0.452 0.620 0.427 -0.027 -0.083 0.027  498 ILE CCC O   
11196 C CB  . ILE C 498 ? 0.467 0.622 0.448 -0.010 -0.082 0.017  498 ILE CCC CB  
11197 C CG1 . ILE C 498 ? 0.473 0.636 0.449 -0.009 -0.072 0.012  498 ILE CCC CG1 
11198 C CG2 . ILE C 498 ? 0.470 0.617 0.456 -0.002 -0.085 0.014  498 ILE CCC CG2 
11199 C CD1 . ILE C 498 ? 0.479 0.646 0.452 -0.013 -0.069 0.011  498 ILE CCC CD1 
11200 N N   . LEU C 499 ? 0.412 0.575 0.391 -0.017 -0.082 0.025  499 LEU CCC N   
11201 C CA  . LEU C 499 ? 0.432 0.602 0.407 -0.026 -0.081 0.029  499 LEU CCC CA  
11202 C C   . LEU C 499 ? 0.445 0.613 0.422 -0.033 -0.091 0.037  499 LEU CCC C   
11203 O O   . LEU C 499 ? 0.475 0.634 0.458 -0.029 -0.098 0.039  499 LEU CCC O   
11204 C CB  . LEU C 499 ? 0.421 0.592 0.396 -0.021 -0.077 0.026  499 LEU CCC CB  
11205 C CG  . LEU C 499 ? 0.405 0.581 0.378 -0.015 -0.067 0.019  499 LEU CCC CG  
11206 C CD1 . LEU C 499 ? 0.398 0.573 0.373 -0.010 -0.065 0.017  499 LEU CCC CD1 
11207 C CD2 . LEU C 499 ? 0.419 0.604 0.386 -0.022 -0.061 0.017  499 LEU CCC CD2 
11208 N N   . GLU C 500 ? 0.456 0.632 0.428 -0.044 -0.091 0.042  500 GLU CCC N   
11209 C CA  . GLU C 500 ? 0.528 0.702 0.503 -0.053 -0.101 0.051  500 GLU CCC CA  
11210 C C   . GLU C 500 ? 0.520 0.705 0.489 -0.064 -0.101 0.056  500 GLU CCC C   
11211 O O   . GLU C 500 ? 0.531 0.713 0.502 -0.070 -0.109 0.064  500 GLU CCC O   
11212 C CB  . GLU C 500 ? 0.586 0.757 0.561 -0.056 -0.106 0.054  500 GLU CCC CB  
11213 C CG  . GLU C 500 ? 0.623 0.803 0.593 -0.059 -0.099 0.050  500 GLU CCC CG  
11214 C CD  . GLU C 500 ? 0.672 0.848 0.644 -0.059 -0.103 0.051  500 GLU CCC CD  
11215 O OE1 . GLU C 500 ? 0.673 0.838 0.651 -0.057 -0.112 0.054  500 GLU CCC OE1 
11216 O OE2 . GLU C 500 ? 0.702 0.884 0.670 -0.061 -0.098 0.047  500 GLU CCC OE2 
11217 N N   . VAL C 501 ? 0.526 0.721 0.488 -0.067 -0.092 0.052  501 VAL CCC N   
11218 C CA  . VAL C 501 ? 0.514 0.722 0.471 -0.078 -0.090 0.056  501 VAL CCC CA  
11219 C C   . VAL C 501 ? 0.540 0.746 0.497 -0.075 -0.089 0.056  501 VAL CCC C   
11220 O O   . VAL C 501 ? 0.557 0.761 0.516 -0.066 -0.083 0.049  501 VAL CCC O   
11221 C CB  . VAL C 501 ? 0.495 0.715 0.446 -0.081 -0.081 0.050  501 VAL CCC CB  
11222 C CG1 . VAL C 501 ? 0.471 0.705 0.417 -0.092 -0.079 0.053  501 VAL CCC CG1 
11223 C CG2 . VAL C 501 ? 0.500 0.721 0.451 -0.083 -0.082 0.050  501 VAL CCC CG2 
11224 N N   . THR C 502 ? 0.570 0.779 0.526 -0.084 -0.095 0.064  502 THR CCC N   
11225 C CA  . THR C 502 ? 0.582 0.791 0.539 -0.083 -0.094 0.064  502 THR CCC CA  
11226 C C   . THR C 502 ? 0.588 0.812 0.538 -0.091 -0.088 0.064  502 THR CCC C   
11227 O O   . THR C 502 ? 0.576 0.810 0.522 -0.101 -0.088 0.066  502 THR CCC O   
11228 C CB  . THR C 502 ? 0.592 0.793 0.554 -0.085 -0.106 0.073  502 THR CCC CB  
11229 O OG1 . THR C 502 ? 0.604 0.813 0.563 -0.099 -0.111 0.082  502 THR CCC OG1 
11230 C CG2 . THR C 502 ? 0.570 0.758 0.540 -0.078 -0.112 0.073  502 THR CCC CG2 
11231 N N   . LYS C 503 ? 0.612 0.839 0.561 -0.088 -0.083 0.060  503 LYS CCC N   
11232 C CA  . LYS C 503 ? 0.645 0.886 0.588 -0.096 -0.078 0.060  503 LYS CCC CA  
11233 C C   . LYS C 503 ? 0.674 0.919 0.615 -0.109 -0.086 0.071  503 LYS CCC C   
11234 O O   . LYS C 503 ? 0.685 0.943 0.621 -0.119 -0.085 0.072  503 LYS CCC O   
11235 C CB  . LYS C 503 ? 0.666 0.907 0.611 -0.091 -0.073 0.056  503 LYS CCC CB  
11236 C CG  . LYS C 503 ? 0.696 0.951 0.635 -0.098 -0.067 0.054  503 LYS CCC CG  
11237 C CD  . LYS C 503 ? 0.719 0.975 0.659 -0.092 -0.061 0.049  503 LYS CCC CD  
11238 C CE  . LYS C 503 ? 0.764 1.035 0.699 -0.098 -0.055 0.045  503 LYS CCC CE  
11239 N NZ  . LYS C 503 ? 0.771 1.042 0.707 -0.091 -0.047 0.037  503 LYS CCC NZ  
11240 N N   . ARG C 504 ? 0.692 0.928 0.638 -0.108 -0.095 0.077  504 ARG CCC N   
11241 C CA  . ARG C 504 ? 0.742 0.979 0.687 -0.120 -0.105 0.088  504 ARG CCC CA  
11242 C C   . ARG C 504 ? 0.760 1.004 0.701 -0.129 -0.108 0.093  504 ARG CCC C   
11243 O O   . ARG C 504 ? 0.773 1.028 0.708 -0.142 -0.110 0.099  504 ARG CCC O   
11244 C CB  . ARG C 504 ? 0.734 0.957 0.687 -0.115 -0.115 0.094  504 ARG CCC CB  
11245 C CG  . ARG C 504 ? 0.731 0.954 0.685 -0.127 -0.127 0.106  504 ARG CCC CG  
11246 C CD  . ARG C 504 ? 0.743 0.952 0.705 -0.123 -0.137 0.111  504 ARG CCC CD  
11247 N NE  . ARG C 504 ? 0.762 0.970 0.725 -0.118 -0.134 0.109  504 ARG CCC NE  
11248 C CZ  . ARG C 504 ? 0.786 0.984 0.756 -0.106 -0.133 0.103  504 ARG CCC CZ  
11249 N NH1 . ARG C 504 ? 0.830 1.017 0.806 -0.097 -0.136 0.099  504 ARG CCC NH1 
11250 N NH2 . ARG C 504 ? 0.806 1.005 0.776 -0.103 -0.130 0.101  504 ARG CCC NH2 
11251 N N   . SER C 505 ? 0.736 0.973 0.681 -0.124 -0.109 0.091  505 SER CCC N   
11252 C CA  . SER C 505 ? 0.736 0.978 0.678 -0.133 -0.113 0.095  505 SER CCC CA  
11253 C C   . SER C 505 ? 0.706 0.967 0.640 -0.142 -0.105 0.092  505 SER CCC C   
11254 O O   . SER C 505 ? 0.718 0.987 0.648 -0.153 -0.108 0.097  505 SER CCC O   
11255 C CB  . SER C 505 ? 0.720 0.952 0.667 -0.124 -0.113 0.091  505 SER CCC CB  
11256 O OG  . SER C 505 ? 0.726 0.964 0.670 -0.119 -0.102 0.081  505 SER CCC OG  
11257 N N   . GLY C 506 ? 0.669 0.937 0.600 -0.138 -0.094 0.083  506 GLY CCC N   
11258 C CA  . GLY C 506 ? 0.667 0.954 0.592 -0.145 -0.086 0.077  506 GLY CCC CA  
11259 C C   . GLY C 506 ? 0.643 0.933 0.567 -0.144 -0.082 0.072  506 GLY CCC C   
11260 O O   . GLY C 506 ? 0.592 0.898 0.511 -0.150 -0.075 0.067  506 GLY CCC O   
11261 N N   . GLU C 507 ? 0.675 0.952 0.604 -0.138 -0.086 0.073  507 GLU CCC N   
11262 C CA  . GLU C 507 ? 0.713 0.992 0.641 -0.136 -0.083 0.069  507 GLU CCC CA  
11263 C C   . GLU C 507 ? 0.673 0.953 0.602 -0.126 -0.072 0.056  507 GLU CCC C   
11264 O O   . GLU C 507 ? 0.650 0.926 0.582 -0.118 -0.069 0.052  507 GLU CCC O   
11265 C CB  . GLU C 507 ? 0.777 1.041 0.711 -0.132 -0.091 0.074  507 GLU CCC CB  
11266 C CG  . GLU C 507 ? 0.862 1.127 0.795 -0.144 -0.102 0.086  507 GLU CCC CG  
11267 C CD  . GLU C 507 ? 0.966 1.215 0.905 -0.140 -0.112 0.091  507 GLU CCC CD  
11268 O OE1 . GLU C 507 ? 1.027 1.262 0.973 -0.130 -0.115 0.090  507 GLU CCC OE1 
11269 O OE2 . GLU C 507 ? 1.014 1.266 0.952 -0.147 -0.116 0.096  507 GLU CCC OE2 
11270 N N   . SER C 508 ? 0.597 0.884 0.525 -0.127 -0.068 0.051  508 SER CCC N   
11271 C CA  . SER C 508 ? 0.580 0.869 0.511 -0.118 -0.058 0.039  508 SER CCC CA  
11272 C C   . SER C 508 ? 0.517 0.788 0.453 -0.104 -0.059 0.037  508 SER CCC C   
11273 O O   . SER C 508 ? 0.479 0.740 0.417 -0.102 -0.065 0.041  508 SER CCC O   
11274 C CB  . SER C 508 ? 0.556 0.855 0.485 -0.122 -0.055 0.035  508 SER CCC CB  
11275 O OG  . SER C 508 ? 0.549 0.848 0.481 -0.113 -0.047 0.024  508 SER CCC OG  
11276 N N   . PHE C 509 ? 0.495 0.762 0.432 -0.095 -0.053 0.030  509 PHE CCC N   
11277 C CA  . PHE C 509 ? 0.492 0.745 0.434 -0.082 -0.053 0.027  509 PHE CCC CA  
11278 C C   . PHE C 509 ? 0.509 0.764 0.454 -0.076 -0.046 0.018  509 PHE CCC C   
11279 O O   . PHE C 509 ? 0.526 0.770 0.473 -0.066 -0.045 0.015  509 PHE CCC O   
11280 C CB  . PHE C 509 ? 0.453 0.701 0.397 -0.077 -0.052 0.027  509 PHE CCC CB  
11281 C CG  . PHE C 509 ? 0.442 0.700 0.384 -0.079 -0.046 0.022  509 PHE CCC CG  
11282 C CD1 . PHE C 509 ? 0.430 0.690 0.374 -0.072 -0.038 0.014  509 PHE CCC CD1 
11283 C CD2 . PHE C 509 ? 0.434 0.701 0.373 -0.088 -0.047 0.027  509 PHE CCC CD2 
11284 C CE1 . PHE C 509 ? 0.439 0.708 0.382 -0.073 -0.033 0.009  509 PHE CCC CE1 
11285 C CE2 . PHE C 509 ? 0.431 0.709 0.369 -0.090 -0.041 0.022  509 PHE CCC CE2 
11286 C CZ  . PHE C 509 ? 0.427 0.705 0.367 -0.082 -0.034 0.012  509 PHE CCC CZ  
11287 N N   . VAL C 510 ? 0.562 0.830 0.504 -0.082 -0.042 0.014  510 VAL CCC N   
11288 C CA  . VAL C 510 ? 0.586 0.855 0.530 -0.078 -0.036 0.005  510 VAL CCC CA  
11289 C C   . VAL C 510 ? 0.611 0.872 0.556 -0.076 -0.040 0.008  510 VAL CCC C   
11290 O O   . VAL C 510 ? 0.540 0.802 0.483 -0.083 -0.047 0.016  510 VAL CCC O   
11291 C CB  . VAL C 510 ? 0.583 0.870 0.525 -0.086 -0.031 -0.000 510 VAL CCC CB  
11292 C CG1 . VAL C 510 ? 0.574 0.864 0.520 -0.082 -0.026 -0.008 510 VAL CCC CG1 
11293 C CG2 . VAL C 510 ? 0.594 0.889 0.537 -0.086 -0.026 -0.004 510 VAL CCC CG2 
11294 N N   . SER C 511 ? 0.650 0.904 0.599 -0.067 -0.038 0.003  511 SER CCC N   
11295 C CA  . SER C 511 ? 0.690 0.938 0.640 -0.064 -0.040 0.003  511 SER CCC CA  
11296 C C   . SER C 511 ? 0.744 0.999 0.695 -0.062 -0.034 -0.006 511 SER CCC C   
11297 O O   . SER C 511 ? 0.676 0.929 0.630 -0.055 -0.029 -0.012 511 SER CCC O   
11298 C CB  . SER C 511 ? 0.711 0.944 0.664 -0.055 -0.044 0.005  511 SER CCC CB  
11299 O OG  . SER C 511 ? 0.697 0.924 0.649 -0.058 -0.051 0.013  511 SER CCC OG  
11300 N N   . SER C 512 ? 0.892 1.154 0.842 -0.069 -0.034 -0.006 512 SER CCC N   
11301 C CA  . SER C 512 ? 0.983 1.256 0.936 -0.070 -0.028 -0.015 512 SER CCC CA  
11302 C C   . SER C 512 ? 1.039 1.302 0.995 -0.062 -0.028 -0.018 512 SER CCC C   
11303 O O   . SER C 512 ? 0.995 1.261 0.954 -0.058 -0.023 -0.026 512 SER CCC O   
11304 C CB  . SER C 512 ? 0.988 1.277 0.938 -0.082 -0.028 -0.014 512 SER CCC CB  
11305 O OG  . SER C 512 ? 1.022 1.320 0.968 -0.089 -0.027 -0.012 512 SER CCC OG  
11306 N N   . GLY C 513 ? 1.061 1.315 1.016 -0.061 -0.034 -0.012 513 GLY CCC N   
11307 C CA  . GLY C 513 ? 1.098 1.341 1.056 -0.053 -0.035 -0.014 513 GLY CCC CA  
11308 C C   . GLY C 513 ? 1.156 1.391 1.117 -0.042 -0.032 -0.018 513 GLY CCC C   
11309 O O   . GLY C 513 ? 1.172 1.403 1.132 -0.040 -0.032 -0.016 513 GLY CCC O   
11310 N N   . GLY C 514 ? 1.088 1.319 1.052 -0.036 -0.029 -0.024 514 GLY CCC N   
11311 C CA  . GLY C 514 ? 1.023 1.248 0.990 -0.027 -0.026 -0.029 514 GLY CCC CA  
11312 C C   . GLY C 514 ? 0.992 1.204 0.960 -0.018 -0.029 -0.027 514 GLY CCC C   
11313 O O   . GLY C 514 ? 0.986 1.196 0.957 -0.013 -0.026 -0.032 514 GLY CCC O   
11314 N N   . CYS C 515 ? 0.969 1.174 0.935 -0.018 -0.034 -0.021 515 CYS CCC N   
11315 C CA  . CYS C 515 ? 0.959 1.152 0.927 -0.009 -0.037 -0.020 515 CYS CCC CA  
11316 C C   . CYS C 515 ? 0.883 1.073 0.851 -0.004 -0.035 -0.021 515 CYS CCC C   
11317 O O   . CYS C 515 ? 0.901 1.083 0.871 0.003  -0.038 -0.020 515 CYS CCC O   
11318 C CB  . CYS C 515 ? 0.962 1.148 0.929 -0.011 -0.044 -0.014 515 CYS CCC CB  
11319 S SG  . CYS C 515 ? 1.034 1.217 1.003 -0.010 -0.047 -0.015 515 CYS CCC SG  
11320 N N   . GLY C 516 ? 0.835 1.032 0.803 -0.006 -0.031 -0.023 516 GLY CCC N   
11321 C CA  . GLY C 516 ? 0.870 1.065 0.839 -0.001 -0.029 -0.023 516 GLY CCC CA  
11322 C C   . GLY C 516 ? 0.873 1.066 0.840 -0.003 -0.033 -0.018 516 GLY CCC C   
11323 O O   . GLY C 516 ? 0.779 0.977 0.744 -0.011 -0.035 -0.014 516 GLY CCC O   
11324 N N   . GLY C 517 ? 0.884 1.071 0.853 0.003  -0.034 -0.017 517 GLY CCC N   
11325 C CA  . GLY C 517 ? 0.879 1.063 0.847 0.003  -0.038 -0.013 517 GLY CCC CA  
11326 C C   . GLY C 517 ? 0.908 1.086 0.877 0.001  -0.045 -0.008 517 GLY CCC C   
11327 O O   . GLY C 517 ? 0.818 0.994 0.787 -0.001 -0.049 -0.004 517 GLY CCC O   
11328 N N   . GLY C 518 ? 0.963 1.137 0.933 0.002  -0.047 -0.009 518 GLY CCC N   
11329 C CA  . GLY C 518 ? 0.962 1.129 0.934 0.003  -0.054 -0.006 518 GLY CCC CA  
11330 C C   . GLY C 518 ? 1.003 1.172 0.974 -0.004 -0.058 -0.002 518 GLY CCC C   
11331 O O   . GLY C 518 ? 0.991 1.168 0.959 -0.012 -0.056 -0.000 518 GLY CCC O   
11332 N N   . LYS C 519 ? 1.034 1.197 1.008 -0.003 -0.063 -0.001 519 LYS CCC N   
11333 C CA  . LYS C 519 ? 1.029 1.194 1.002 -0.008 -0.066 0.001  519 LYS CCC CA  
11334 C C   . LYS C 519 ? 0.959 1.117 0.935 -0.002 -0.067 -0.002 519 LYS CCC C   
11335 O O   . LYS C 519 ? 0.915 1.065 0.894 0.004  -0.071 -0.002 519 LYS CCC O   
11336 C CB  . LYS C 519 ? 1.060 1.225 1.034 -0.017 -0.073 0.009  519 LYS CCC CB  
11337 C CG  . LYS C 519 ? 1.084 1.240 1.062 -0.014 -0.081 0.012  519 LYS CCC CG  
11338 C CD  . LYS C 519 ? 1.115 1.274 1.092 -0.022 -0.085 0.019  519 LYS CCC CD  
11339 C CE  . LYS C 519 ? 1.102 1.253 1.084 -0.024 -0.096 0.025  519 LYS CCC CE  
11340 N NZ  . LYS C 519 ? 1.059 1.204 1.046 -0.018 -0.099 0.025  519 LYS CCC NZ  
11341 N N   . CYS C 520 ? 0.912 1.073 0.886 -0.003 -0.064 -0.005 520 CYS CCC N   
11342 C CA  A CYS C 520 ? 0.930 1.086 0.906 0.001  -0.066 -0.007 520 CYS CCC CA  
11343 C CA  B CYS C 520 ? 0.872 1.028 0.848 0.001  -0.066 -0.007 520 CYS CCC CA  
11344 C C   . CYS C 520 ? 0.900 1.053 0.878 -0.004 -0.074 -0.001 520 CYS CCC C   
11345 O O   . CYS C 520 ? 0.850 0.997 0.830 -0.001 -0.077 -0.003 520 CYS CCC O   
11346 C CB  A CYS C 520 ? 0.908 1.070 0.882 -0.000 -0.059 -0.011 520 CYS CCC CB  
11347 C CB  B CYS C 520 ? 0.774 0.934 0.748 0.001  -0.060 -0.011 520 CYS CCC CB  
11348 S SG  A CYS C 520 ? 0.859 1.027 0.831 0.002  -0.051 -0.016 520 CYS CCC SG  
11349 S SG  B CYS C 520 ? 0.685 0.845 0.660 0.010  -0.053 -0.018 520 CYS CCC SG  
11350 N N   . GLY C 521 ? 0.914 1.070 0.891 -0.012 -0.077 0.004  521 GLY CCC N   
11351 C CA  . GLY C 521 ? 0.955 1.107 0.934 -0.018 -0.086 0.011  521 GLY CCC CA  
11352 C C   . GLY C 521 ? 0.959 1.119 0.935 -0.029 -0.087 0.017  521 GLY CCC C   
11353 O O   . GLY C 521 ? 0.937 1.104 0.910 -0.030 -0.082 0.016  521 GLY CCC O   
11354 O OXT . GLY C 521 ? 0.934 1.094 0.911 -0.036 -0.094 0.024  521 GLY CCC OXT 
11355 N N   . LEU D 24  ? 1.428 1.272 1.635 -0.023 -0.129 0.018  24  LEU DDD N   
11356 C CA  . LEU D 24  ? 1.411 1.262 1.602 -0.027 -0.116 0.015  24  LEU DDD CA  
11357 C C   . LEU D 24  ? 1.406 1.258 1.617 -0.027 -0.112 0.008  24  LEU DDD C   
11358 O O   . LEU D 24  ? 1.369 1.219 1.573 -0.034 -0.104 0.013  24  LEU DDD O   
11359 C CB  . LEU D 24  ? 1.408 1.251 1.574 -0.037 -0.111 0.030  24  LEU DDD CB  
11360 C CG  . LEU D 24  ? 1.388 1.234 1.527 -0.037 -0.110 0.034  24  LEU DDD CG  
11361 C CD1 . LEU D 24  ? 1.340 1.200 1.471 -0.031 -0.103 0.021  24  LEU DDD CD1 
11362 C CD2 . LEU D 24  ? 1.370 1.210 1.511 -0.034 -0.121 0.039  24  LEU DDD CD2 
11363 N N   . THR D 25  ? 1.422 1.278 1.659 -0.019 -0.119 -0.003 25  THR DDD N   
11364 C CA  . THR D 25  ? 1.417 1.279 1.674 -0.017 -0.115 -0.015 25  THR DDD CA  
11365 C C   . THR D 25  ? 1.377 1.255 1.623 -0.012 -0.107 -0.027 25  THR DDD C   
11366 O O   . THR D 25  ? 1.277 1.162 1.538 -0.007 -0.105 -0.040 25  THR DDD O   
11367 C CB  . THR D 25  ? 1.444 1.307 1.732 -0.010 -0.125 -0.023 25  THR DDD CB  
11368 O OG1 . THR D 25  ? 1.432 1.300 1.720 -0.002 -0.131 -0.029 25  THR DDD OG1 
11369 C CG2 . THR D 25  ? 1.443 1.290 1.746 -0.016 -0.131 -0.012 25  THR DDD CG2 
11370 N N   . PHE D 26  ? 1.398 1.279 1.618 -0.013 -0.103 -0.023 26  PHE DDD N   
11371 C CA  . PHE D 26  ? 1.378 1.272 1.584 -0.009 -0.095 -0.033 26  PHE DDD CA  
11372 C C   . PHE D 26  ? 1.339 1.230 1.519 -0.017 -0.086 -0.023 26  PHE DDD C   
11373 O O   . PHE D 26  ? 1.305 1.189 1.468 -0.022 -0.087 -0.012 26  PHE DDD O   
11374 C CB  . PHE D 26  ? 1.373 1.276 1.576 -0.001 -0.100 -0.040 26  PHE DDD CB  
11375 C CG  . PHE D 26  ? 1.387 1.293 1.614 0.007  -0.109 -0.049 26  PHE DDD CG  
11376 C CD1 . PHE D 26  ? 1.367 1.280 1.613 0.012  -0.108 -0.062 26  PHE DDD CD1 
11377 C CD2 . PHE D 26  ? 1.434 1.336 1.666 0.010  -0.118 -0.046 26  PHE DDD CD2 
11378 C CE1 . PHE D 26  ? 1.406 1.324 1.675 0.020  -0.117 -0.072 26  PHE DDD CE1 
11379 C CE2 . PHE D 26  ? 1.454 1.359 1.708 0.018  -0.126 -0.056 26  PHE DDD CE2 
11380 C CZ  . PHE D 26  ? 1.428 1.341 1.701 0.022  -0.125 -0.069 26  PHE DDD CZ  
11381 N N   . MET D 27  ? 1.246 1.143 1.423 -0.019 -0.077 -0.029 27  MET DDD N   
11382 C CA  . MET D 27  ? 1.174 1.072 1.328 -0.026 -0.067 -0.023 27  MET DDD CA  
11383 C C   . MET D 27  ? 1.076 0.978 1.209 -0.023 -0.067 -0.022 27  MET DDD C   
11384 O O   . MET D 27  ? 1.000 0.897 1.113 -0.030 -0.064 -0.012 27  MET DDD O   
11385 C CB  . MET D 27  ? 1.182 1.088 1.340 -0.026 -0.058 -0.032 27  MET DDD CB  
11386 C CG  . MET D 27  ? 1.222 1.122 1.397 -0.031 -0.056 -0.031 27  MET DDD CG  
11387 S SD  . MET D 27  ? 1.282 1.193 1.468 -0.028 -0.048 -0.045 27  MET DDD SD  
11388 C CE  . MET D 27  ? 1.253 1.166 1.414 -0.037 -0.036 -0.039 27  MET DDD CE  
11389 N N   . TYR D 28  ? 1.020 0.933 1.158 -0.014 -0.071 -0.032 28  TYR DDD N   
11390 C CA  . TYR D 28  ? 0.950 0.869 1.070 -0.011 -0.070 -0.033 28  TYR DDD CA  
11391 C C   . TYR D 28  ? 0.902 0.822 1.030 -0.004 -0.080 -0.035 28  TYR DDD C   
11392 O O   . TYR D 28  ? 0.853 0.773 1.002 0.001  -0.087 -0.040 28  TYR DDD O   
11393 C CB  . TYR D 28  ? 0.895 0.827 1.012 -0.006 -0.064 -0.044 28  TYR DDD CB  
11394 C CG  . TYR D 28  ? 0.868 0.801 0.976 -0.013 -0.054 -0.042 28  TYR DDD CG  
11395 C CD1 . TYR D 28  ? 0.845 0.777 0.967 -0.015 -0.050 -0.046 28  TYR DDD CD1 
11396 C CD2 . TYR D 28  ? 0.823 0.757 0.910 -0.017 -0.048 -0.038 28  TYR DDD CD2 
11397 C CE1 . TYR D 28  ? 0.797 0.730 0.912 -0.021 -0.041 -0.046 28  TYR DDD CE1 
11398 C CE2 . TYR D 28  ? 0.794 0.728 0.873 -0.023 -0.038 -0.037 28  TYR DDD CE2 
11399 C CZ  . TYR D 28  ? 0.775 0.709 0.869 -0.025 -0.035 -0.041 28  TYR DDD CZ  
11400 O OH  . TYR D 28  ? 0.767 0.703 0.855 -0.031 -0.025 -0.042 28  TYR DDD OH  
11401 N N   . ASP D 29  ? 0.894 0.815 1.005 -0.003 -0.082 -0.031 29  ASP DDD N   
11402 C CA  . ASP D 29  ? 0.883 0.806 0.998 0.004  -0.090 -0.034 29  ASP DDD CA  
11403 C C   . ASP D 29  ? 0.876 0.815 0.996 0.013  -0.088 -0.047 29  ASP DDD C   
11404 O O   . ASP D 29  ? 0.916 0.859 1.050 0.020  -0.095 -0.055 29  ASP DDD O   
11405 C CB  . ASP D 29  ? 0.919 0.837 1.015 0.001  -0.092 -0.024 29  ASP DDD CB  
11406 C CG  . ASP D 29  ? 0.947 0.851 1.041 -0.007 -0.096 -0.011 29  ASP DDD CG  
11407 O OD1 . ASP D 29  ? 0.935 0.833 1.044 -0.005 -0.104 -0.009 29  ASP DDD OD1 
11408 O OD2 . ASP D 29  ? 0.994 0.893 1.070 -0.014 -0.090 -0.002 29  ASP DDD OD2 
11409 N N   . LEU D 30  ? 0.851 0.796 0.958 0.012  -0.080 -0.050 30  LEU DDD N   
11410 C CA  . LEU D 30  ? 0.811 0.770 0.918 0.019  -0.077 -0.061 30  LEU DDD CA  
11411 C C   . LEU D 30  ? 0.776 0.740 0.879 0.016  -0.068 -0.064 30  LEU DDD C   
11412 O O   . LEU D 30  ? 0.713 0.673 0.802 0.010  -0.062 -0.058 30  LEU DDD O   
11413 C CB  . LEU D 30  ? 0.826 0.788 0.916 0.020  -0.078 -0.058 30  LEU DDD CB  
11414 C CG  . LEU D 30  ? 0.827 0.804 0.915 0.027  -0.075 -0.067 30  LEU DDD CG  
11415 C CD1 . LEU D 30  ? 0.821 0.806 0.927 0.035  -0.080 -0.077 30  LEU DDD CD1 
11416 C CD2 . LEU D 30  ? 0.863 0.841 0.933 0.027  -0.074 -0.063 30  LEU DDD CD2 
11417 N N   . VAL D 31  ? 0.746 0.720 0.862 0.022  -0.068 -0.075 31  VAL DDD N   
11418 C CA  . VAL D 31  ? 0.777 0.758 0.891 0.022  -0.061 -0.081 31  VAL DDD CA  
11419 C C   . VAL D 31  ? 0.746 0.741 0.859 0.030  -0.061 -0.089 31  VAL DDD C   
11420 O O   . VAL D 31  ? 0.767 0.767 0.891 0.036  -0.067 -0.096 31  VAL DDD O   
11421 C CB  . VAL D 31  ? 0.801 0.781 0.933 0.021  -0.060 -0.086 31  VAL DDD CB  
11422 C CG1 . VAL D 31  ? 0.763 0.752 0.896 0.023  -0.054 -0.094 31  VAL DDD CG1 
11423 C CG2 . VAL D 31  ? 0.843 0.810 0.976 0.013  -0.058 -0.077 31  VAL DDD CG2 
11424 N N   . VAL D 32  ? 0.718 0.718 0.817 0.029  -0.055 -0.089 32  VAL DDD N   
11425 C CA  . VAL D 32  ? 0.679 0.692 0.774 0.035  -0.054 -0.095 32  VAL DDD CA  
11426 C C   . VAL D 32  ? 0.634 0.654 0.733 0.036  -0.049 -0.102 32  VAL DDD C   
11427 O O   . VAL D 32  ? 0.576 0.591 0.668 0.030  -0.043 -0.098 32  VAL DDD O   
11428 C CB  . VAL D 32  ? 0.685 0.696 0.760 0.033  -0.052 -0.089 32  VAL DDD CB  
11429 C CG1 . VAL D 32  ? 0.699 0.723 0.770 0.039  -0.051 -0.094 32  VAL DDD CG1 
11430 C CG2 . VAL D 32  ? 0.690 0.694 0.761 0.032  -0.057 -0.081 32  VAL DDD CG2 
11431 N N   . ILE D 33  ? 0.634 0.664 0.744 0.043  -0.052 -0.111 33  ILE DDD N   
11432 C CA  . ILE D 33  ? 0.672 0.710 0.785 0.045  -0.048 -0.118 33  ILE DDD CA  
11433 C C   . ILE D 33  ? 0.666 0.715 0.768 0.049  -0.046 -0.120 33  ILE DDD C   
11434 O O   . ILE D 33  ? 0.679 0.737 0.784 0.056  -0.051 -0.125 33  ILE DDD O   
11435 C CB  . ILE D 33  ? 0.672 0.715 0.803 0.049  -0.052 -0.128 33  ILE DDD CB  
11436 C CG1 . ILE D 33  ? 0.707 0.739 0.850 0.045  -0.054 -0.125 33  ILE DDD CG1 
11437 C CG2 . ILE D 33  ? 0.673 0.724 0.808 0.051  -0.048 -0.134 33  ILE DDD CG2 
11438 C CD1 . ILE D 33  ? 0.723 0.759 0.887 0.049  -0.059 -0.135 33  ILE DDD CD1 
11439 N N   . GLY D 34  ? 0.668 0.715 0.758 0.045  -0.040 -0.115 34  GLY DDD N   
11440 C CA  . GLY D 34  ? 0.632 0.689 0.712 0.048  -0.038 -0.116 34  GLY DDD CA  
11441 C C   . GLY D 34  ? 0.633 0.683 0.698 0.043  -0.035 -0.107 34  GLY DDD C   
11442 O O   . GLY D 34  ? 0.696 0.742 0.757 0.042  -0.039 -0.102 34  GLY DDD O   
11443 N N   . GLY D 35  ? 0.599 0.651 0.657 0.040  -0.029 -0.105 35  GLY DDD N   
11444 C CA  . GLY D 35  ? 0.618 0.665 0.660 0.035  -0.026 -0.098 35  GLY DDD CA  
11445 C C   . GLY D 35  ? 0.605 0.661 0.641 0.039  -0.025 -0.098 35  GLY DDD C   
11446 O O   . GLY D 35  ? 0.630 0.686 0.658 0.036  -0.020 -0.096 35  GLY DDD O   
11447 N N   . GLY D 36  ? 0.565 0.628 0.603 0.046  -0.030 -0.102 36  GLY DDD N   
11448 C CA  . GLY D 36  ? 0.588 0.659 0.619 0.049  -0.030 -0.101 36  GLY DDD CA  
11449 C C   . GLY D 36  ? 0.557 0.624 0.581 0.049  -0.033 -0.096 36  GLY DDD C   
11450 O O   . GLY D 36  ? 0.509 0.567 0.531 0.045  -0.034 -0.091 36  GLY DDD O   
11451 N N   . SER D 37  ? 0.569 0.645 0.591 0.054  -0.035 -0.097 37  SER DDD N   
11452 C CA  . SER D 37  ? 0.562 0.635 0.576 0.054  -0.038 -0.092 37  SER DDD CA  
11453 C C   . SER D 37  ? 0.587 0.654 0.606 0.055  -0.043 -0.091 37  SER DDD C   
11454 O O   . SER D 37  ? 0.589 0.647 0.602 0.051  -0.044 -0.086 37  SER DDD O   
11455 C CB  . SER D 37  ? 0.584 0.669 0.597 0.060  -0.038 -0.094 37  SER DDD CB  
11456 O OG  . SER D 37  ? 0.573 0.663 0.582 0.059  -0.034 -0.093 37  SER DDD OG  
11457 N N   . GLY D 38  ? 0.573 0.645 0.604 0.059  -0.047 -0.098 38  GLY DDD N   
11458 C CA  . GLY D 38  ? 0.568 0.635 0.607 0.060  -0.052 -0.099 38  GLY DDD CA  
11459 C C   . GLY D 38  ? 0.556 0.610 0.596 0.054  -0.052 -0.094 38  GLY DDD C   
11460 O O   . GLY D 38  ? 0.537 0.582 0.574 0.051  -0.055 -0.089 38  GLY DDD O   
11461 N N   . GLY D 39  ? 0.580 0.632 0.623 0.051  -0.049 -0.096 39  GLY DDD N   
11462 C CA  . GLY D 39  ? 0.616 0.657 0.663 0.045  -0.048 -0.093 39  GLY DDD CA  
11463 C C   . GLY D 39  ? 0.618 0.649 0.652 0.038  -0.045 -0.084 39  GLY DDD C   
11464 O O   . GLY D 39  ? 0.646 0.668 0.680 0.035  -0.048 -0.079 39  GLY DDD O   
11465 N N   . MET D 40  ? 0.617 0.651 0.640 0.036  -0.039 -0.082 40  MET DDD N   
11466 C CA  . MET D 40  ? 0.652 0.677 0.661 0.029  -0.036 -0.074 40  MET DDD CA  
11467 C C   . MET D 40  ? 0.650 0.672 0.654 0.030  -0.041 -0.069 40  MET DDD C   
11468 O O   . MET D 40  ? 0.682 0.694 0.679 0.024  -0.041 -0.063 40  MET DDD O   
11469 C CB  . MET D 40  ? 0.645 0.676 0.647 0.028  -0.030 -0.075 40  MET DDD CB  
11470 C CG  . MET D 40  ? 0.655 0.687 0.662 0.025  -0.024 -0.078 40  MET DDD CG  
11471 S SD  . MET D 40  ? 0.660 0.695 0.658 0.022  -0.016 -0.078 40  MET DDD SD  
11472 C CE  . MET D 40  ? 0.651 0.697 0.646 0.029  -0.019 -0.079 40  MET DDD CE  
11473 N N   . ALA D 41  ? 0.625 0.654 0.631 0.036  -0.045 -0.072 41  ALA DDD N   
11474 C CA  . ALA D 41  ? 0.649 0.676 0.651 0.037  -0.050 -0.068 41  ALA DDD CA  
11475 C C   . ALA D 41  ? 0.661 0.679 0.670 0.036  -0.056 -0.066 41  ALA DDD C   
11476 O O   . ALA D 41  ? 0.664 0.672 0.666 0.032  -0.058 -0.059 41  ALA DDD O   
11477 C CB  . ALA D 41  ? 0.631 0.668 0.635 0.044  -0.052 -0.073 41  ALA DDD CB  
11478 N N   . ALA D 42  ? 0.634 0.654 0.657 0.040  -0.059 -0.072 42  ALA DDD N   
11479 C CA  . ALA D 42  ? 0.656 0.669 0.690 0.040  -0.065 -0.071 42  ALA DDD CA  
11480 C C   . ALA D 42  ? 0.713 0.713 0.741 0.031  -0.063 -0.063 42  ALA DDD C   
11481 O O   . ALA D 42  ? 0.751 0.742 0.777 0.029  -0.068 -0.057 42  ALA DDD O   
11482 C CB  . ALA D 42  ? 0.635 0.654 0.685 0.044  -0.067 -0.080 42  ALA DDD CB  
11483 N N   . ALA D 43  ? 0.730 0.730 0.755 0.028  -0.056 -0.064 43  ALA DDD N   
11484 C CA  . ALA D 43  ? 0.754 0.744 0.776 0.020  -0.053 -0.058 43  ALA DDD CA  
11485 C C   . ALA D 43  ? 0.824 0.806 0.829 0.014  -0.052 -0.048 43  ALA DDD C   
11486 O O   . ALA D 43  ? 0.875 0.847 0.880 0.009  -0.055 -0.041 43  ALA DDD O   
11487 C CB  . ALA D 43  ? 0.778 0.773 0.801 0.018  -0.045 -0.062 43  ALA DDD CB  
11488 N N   . LYS D 44  ? 0.871 0.858 0.864 0.014  -0.048 -0.048 44  LYS DDD N   
11489 C CA  . LYS D 44  ? 0.851 0.833 0.828 0.008  -0.047 -0.040 44  LYS DDD CA  
11490 C C   . LYS D 44  ? 0.842 0.819 0.819 0.010  -0.056 -0.035 44  LYS DDD C   
11491 O O   . LYS D 44  ? 0.852 0.820 0.819 0.004  -0.057 -0.027 44  LYS DDD O   
11492 C CB  . LYS D 44  ? 0.854 0.843 0.821 0.009  -0.043 -0.042 44  LYS DDD CB  
11493 C CG  . LYS D 44  ? 0.872 0.865 0.836 0.005  -0.034 -0.044 44  LYS DDD CG  
11494 C CD  . LYS D 44  ? 0.862 0.861 0.816 0.006  -0.030 -0.046 44  LYS DDD CD  
11495 C CE  . LYS D 44  ? 0.836 0.846 0.799 0.012  -0.028 -0.053 44  LYS DDD CE  
11496 N NZ  . LYS D 44  ? 0.887 0.902 0.842 0.011  -0.022 -0.054 44  LYS DDD NZ  
11497 N N   . GLU D 45  ? 0.842 0.824 0.829 0.017  -0.061 -0.040 45  GLU DDD N   
11498 C CA  . GLU D 45  ? 0.848 0.826 0.836 0.019  -0.069 -0.037 45  GLU DDD CA  
11499 C C   . GLU D 45  ? 0.839 0.806 0.836 0.017  -0.075 -0.033 45  GLU DDD C   
11500 O O   . GLU D 45  ? 0.869 0.828 0.861 0.014  -0.080 -0.025 45  GLU DDD O   
11501 C CB  . GLU D 45  ? 0.841 0.828 0.839 0.028  -0.073 -0.044 45  GLU DDD CB  
11502 C CG  . GLU D 45  ? 0.871 0.855 0.868 0.029  -0.081 -0.041 45  GLU DDD CG  
11503 C CD  . GLU D 45  ? 0.911 0.895 0.894 0.028  -0.079 -0.036 45  GLU DDD CD  
11504 O OE1 . GLU D 45  ? 0.921 0.907 0.893 0.024  -0.072 -0.035 45  GLU DDD OE1 
11505 O OE2 . GLU D 45  ? 0.936 0.919 0.919 0.030  -0.085 -0.035 45  GLU DDD OE2 
11506 N N   . ALA D 46  ? 0.789 0.757 0.798 0.017  -0.074 -0.037 46  ALA DDD N   
11507 C CA  . ALA D 46  ? 0.797 0.756 0.817 0.015  -0.078 -0.033 46  ALA DDD CA  
11508 C C   . ALA D 46  ? 0.827 0.775 0.834 0.005  -0.076 -0.023 46  ALA DDD C   
11509 O O   . ALA D 46  ? 0.860 0.798 0.866 0.003  -0.082 -0.015 46  ALA DDD O   
11510 C CB  . ALA D 46  ? 0.797 0.759 0.832 0.017  -0.077 -0.041 46  ALA DDD CB  
11511 N N   . ALA D 47  ? 0.853 0.803 0.849 0.001  -0.067 -0.023 47  ALA DDD N   
11512 C CA  . ALA D 47  ? 0.858 0.800 0.841 -0.008 -0.062 -0.014 47  ALA DDD CA  
11513 C C   . ALA D 47  ? 0.894 0.831 0.861 -0.011 -0.066 -0.006 47  ALA DDD C   
11514 O O   . ALA D 47  ? 0.886 0.813 0.844 -0.019 -0.066 0.003  47  ALA DDD O   
11515 C CB  . ALA D 47  ? 0.837 0.785 0.814 -0.011 -0.052 -0.019 47  ALA DDD CB  
11516 N N   . LYS D 48  ? 0.881 0.824 0.844 -0.006 -0.068 -0.009 48  LYS DDD N   
11517 C CA  . LYS D 48  ? 0.916 0.855 0.867 -0.008 -0.072 -0.002 48  LYS DDD CA  
11518 C C   . LYS D 48  ? 0.926 0.854 0.880 -0.010 -0.081 0.006  48  LYS DDD C   
11519 O O   . LYS D 48  ? 0.910 0.831 0.850 -0.015 -0.084 0.014  48  LYS DDD O   
11520 C CB  . LYS D 48  ? 0.908 0.856 0.861 -0.001 -0.075 -0.008 48  LYS DDD CB  
11521 C CG  . LYS D 48  ? 0.922 0.875 0.860 -0.002 -0.070 -0.009 48  LYS DDD CG  
11522 C CD  . LYS D 48  ? 0.940 0.899 0.878 0.005  -0.074 -0.012 48  LYS DDD CD  
11523 C CE  . LYS D 48  ? 0.960 0.913 0.897 0.005  -0.083 -0.006 48  LYS DDD CE  
11524 N NZ  . LYS D 48  ? 0.958 0.917 0.895 0.011  -0.086 -0.009 48  LYS DDD NZ  
11525 N N   . TYR D 49  ? 0.937 0.863 0.910 -0.006 -0.087 0.003  49  TYR DDD N   
11526 C CA  . TYR D 49  ? 0.964 0.881 0.945 -0.006 -0.097 0.009  49  TYR DDD CA  
11527 C C   . TYR D 49  ? 1.003 0.909 0.985 -0.014 -0.096 0.017  49  TYR DDD C   
11528 O O   . TYR D 49  ? 0.985 0.884 0.980 -0.013 -0.104 0.021  49  TYR DDD O   
11529 C CB  . TYR D 49  ? 0.939 0.860 0.939 0.003  -0.103 0.001  49  TYR DDD CB  
11530 C CG  . TYR D 49  ? 0.918 0.848 0.915 0.009  -0.104 -0.004 49  TYR DDD CG  
11531 C CD1 . TYR D 49  ? 0.906 0.832 0.892 0.007  -0.109 0.002  49  TYR DDD CD1 
11532 C CD2 . TYR D 49  ? 0.871 0.814 0.876 0.015  -0.101 -0.015 49  TYR DDD CD2 
11533 C CE1 . TYR D 49  ? 0.884 0.819 0.868 0.013  -0.109 -0.003 49  TYR DDD CE1 
11534 C CE2 . TYR D 49  ? 0.849 0.800 0.850 0.020  -0.101 -0.019 49  TYR DDD CE2 
11535 C CZ  . TYR D 49  ? 0.885 0.832 0.876 0.019  -0.105 -0.013 49  TYR DDD CZ  
11536 O OH  . TYR D 49  ? 0.836 0.791 0.826 0.024  -0.106 -0.018 49  TYR DDD OH  
11537 N N   . GLY D 50  ? 1.035 0.941 1.006 -0.020 -0.087 0.018  50  GLY DDD N   
11538 C CA  . GLY D 50  ? 1.023 0.920 0.993 -0.028 -0.084 0.026  50  GLY DDD CA  
11539 C C   . GLY D 50  ? 1.034 0.933 1.024 -0.026 -0.083 0.020  50  GLY DDD C   
11540 O O   . GLY D 50  ? 1.087 0.978 1.081 -0.032 -0.083 0.026  50  GLY DDD O   
11541 N N   . LYS D 51  ? 0.974 0.882 0.976 -0.018 -0.082 0.008  51  LYS DDD N   
11542 C CA  . LYS D 51  ? 0.959 0.870 0.982 -0.015 -0.082 0.001  51  LYS DDD CA  
11543 C C   . LYS D 51  ? 1.003 0.918 1.023 -0.019 -0.072 -0.002 51  LYS DDD C   
11544 O O   . LYS D 51  ? 1.000 0.920 1.004 -0.021 -0.065 -0.003 51  LYS DDD O   
11545 C CB  . LYS D 51  ? 0.930 0.850 0.968 -0.005 -0.086 -0.010 51  LYS DDD CB  
11546 C CG  . LYS D 51  ? 0.916 0.833 0.959 -0.000 -0.097 -0.008 51  LYS DDD CG  
11547 C CD  . LYS D 51  ? 0.900 0.803 0.948 -0.005 -0.104 0.002  51  LYS DDD CD  
11548 C CE  . LYS D 51  ? 0.898 0.801 0.960 0.001  -0.115 0.001  51  LYS DDD CE  
11549 N NZ  . LYS D 51  ? 0.905 0.795 0.961 -0.003 -0.122 0.013  51  LYS DDD NZ  
11550 N N   . LYS D 52  ? 1.028 0.939 1.062 -0.020 -0.071 -0.003 52  LYS DDD N   
11551 C CA  . LYS D 52  ? 1.043 0.959 1.078 -0.023 -0.061 -0.008 52  LYS DDD CA  
11552 C C   . LYS D 52  ? 1.027 0.955 1.074 -0.015 -0.060 -0.021 52  LYS DDD C   
11553 O O   . LYS D 52  ? 1.011 0.940 1.075 -0.008 -0.066 -0.027 52  LYS DDD O   
11554 C CB  . LYS D 52  ? 1.157 1.064 1.203 -0.029 -0.061 -0.003 52  LYS DDD CB  
11555 C CG  . LYS D 52  ? 1.218 1.125 1.257 -0.036 -0.050 -0.003 52  LYS DDD CG  
11556 C CD  . LYS D 52  ? 1.255 1.158 1.312 -0.040 -0.049 -0.002 52  LYS DDD CD  
11557 C CE  . LYS D 52  ? 1.260 1.167 1.314 -0.044 -0.038 -0.006 52  LYS DDD CE  
11558 N NZ  . LYS D 52  ? 1.269 1.173 1.342 -0.046 -0.037 -0.008 52  LYS DDD NZ  
11559 N N   . VAL D 53  ? 1.023 0.959 1.060 -0.015 -0.052 -0.026 53  VAL DDD N   
11560 C CA  . VAL D 53  ? 0.988 0.937 1.032 -0.006 -0.051 -0.037 53  VAL DDD CA  
11561 C C   . VAL D 53  ? 0.964 0.917 1.008 -0.009 -0.042 -0.042 53  VAL DDD C   
11562 O O   . VAL D 53  ? 0.927 0.878 0.957 -0.016 -0.035 -0.037 53  VAL DDD O   
11563 C CB  . VAL D 53  ? 1.002 0.957 1.033 -0.003 -0.052 -0.038 53  VAL DDD CB  
11564 C CG1 . VAL D 53  ? 0.996 0.963 1.034 0.006  -0.052 -0.049 53  VAL DDD CG1 
11565 C CG2 . VAL D 53  ? 1.019 0.968 1.046 -0.002 -0.060 -0.031 53  VAL DDD CG2 
11566 N N   . ALA D 54  ? 0.929 0.889 0.988 -0.004 -0.042 -0.052 54  ALA DDD N   
11567 C CA  . ALA D 54  ? 0.904 0.871 0.967 -0.004 -0.035 -0.059 54  ALA DDD CA  
11568 C C   . ALA D 54  ? 0.833 0.812 0.898 0.005  -0.036 -0.068 54  ALA DDD C   
11569 O O   . ALA D 54  ? 0.865 0.848 0.939 0.011  -0.043 -0.072 54  ALA DDD O   
11570 C CB  . ALA D 54  ? 0.944 0.908 1.023 -0.005 -0.034 -0.062 54  ALA DDD CB  
11571 N N   . LEU D 55  ? 0.745 0.731 0.803 0.004  -0.029 -0.071 55  LEU DDD N   
11572 C CA  . LEU D 55  ? 0.703 0.702 0.764 0.012  -0.030 -0.079 55  LEU DDD CA  
11573 C C   . LEU D 55  ? 0.665 0.669 0.733 0.012  -0.024 -0.086 55  LEU DDD C   
11574 O O   . LEU D 55  ? 0.648 0.649 0.711 0.005  -0.018 -0.083 55  LEU DDD O   
11575 C CB  . LEU D 55  ? 0.676 0.678 0.720 0.012  -0.028 -0.076 55  LEU DDD CB  
11576 C CG  . LEU D 55  ? 0.654 0.668 0.700 0.020  -0.029 -0.083 55  LEU DDD CG  
11577 C CD1 . LEU D 55  ? 0.676 0.692 0.710 0.022  -0.032 -0.079 55  LEU DDD CD1 
11578 C CD2 . LEU D 55  ? 0.661 0.681 0.705 0.019  -0.022 -0.087 55  LEU DDD CD2 
11579 N N   . PHE D 56  ? 0.627 0.639 0.708 0.019  -0.027 -0.095 56  PHE DDD N   
11580 C CA  . PHE D 56  ? 0.637 0.657 0.726 0.020  -0.024 -0.102 56  PHE DDD CA  
11581 C C   . PHE D 56  ? 0.629 0.660 0.712 0.026  -0.023 -0.106 56  PHE DDD C   
11582 O O   . PHE D 56  ? 0.660 0.695 0.741 0.031  -0.028 -0.107 56  PHE DDD O   
11583 C CB  . PHE D 56  ? 0.655 0.677 0.763 0.024  -0.028 -0.109 56  PHE DDD CB  
11584 C CG  . PHE D 56  ? 0.672 0.683 0.788 0.018  -0.028 -0.106 56  PHE DDD CG  
11585 C CD1 . PHE D 56  ? 0.669 0.677 0.790 0.013  -0.022 -0.106 56  PHE DDD CD1 
11586 C CD2 . PHE D 56  ? 0.662 0.665 0.781 0.018  -0.034 -0.102 56  PHE DDD CD2 
11587 C CE1 . PHE D 56  ? 0.672 0.670 0.799 0.007  -0.021 -0.102 56  PHE DDD CE1 
11588 C CE2 . PHE D 56  ? 0.656 0.650 0.783 0.012  -0.033 -0.097 56  PHE DDD CE2 
11589 C CZ  . PHE D 56  ? 0.666 0.656 0.797 0.007  -0.027 -0.097 56  PHE DDD CZ  
11590 N N   . ASP D 57  ? 0.622 0.656 0.701 0.023  -0.017 -0.107 57  ASP DDD N   
11591 C CA  . ASP D 57  ? 0.577 0.622 0.654 0.028  -0.016 -0.112 57  ASP DDD CA  
11592 C C   . ASP D 57  ? 0.555 0.602 0.639 0.027  -0.012 -0.117 57  ASP DDD C   
11593 O O   . ASP D 57  ? 0.539 0.581 0.621 0.020  -0.006 -0.114 57  ASP DDD O   
11594 C CB  . ASP D 57  ? 0.571 0.616 0.632 0.027  -0.014 -0.107 57  ASP DDD CB  
11595 C CG  . ASP D 57  ? 0.563 0.620 0.623 0.033  -0.015 -0.111 57  ASP DDD CG  
11596 O OD1 . ASP D 57  ? 0.551 0.614 0.615 0.040  -0.021 -0.113 57  ASP DDD OD1 
11597 O OD2 . ASP D 57  ? 0.578 0.638 0.636 0.032  -0.011 -0.111 57  ASP DDD OD2 
11598 N N   . PHE D 58  ? 0.517 0.574 0.611 0.033  -0.014 -0.124 58  PHE DDD N   
11599 C CA  . PHE D 58  ? 0.542 0.604 0.643 0.033  -0.011 -0.130 58  PHE DDD CA  
11600 C C   . PHE D 58  ? 0.538 0.612 0.640 0.040  -0.014 -0.134 58  PHE DDD C   
11601 O O   . PHE D 58  ? 0.526 0.605 0.630 0.046  -0.020 -0.137 58  PHE DDD O   
11602 C CB  . PHE D 58  ? 0.568 0.627 0.684 0.032  -0.011 -0.135 58  PHE DDD CB  
11603 C CG  . PHE D 58  ? 0.567 0.632 0.693 0.031  -0.007 -0.141 58  PHE DDD CG  
11604 C CD1 . PHE D 58  ? 0.574 0.648 0.708 0.038  -0.011 -0.148 58  PHE DDD CD1 
11605 C CD2 . PHE D 58  ? 0.587 0.645 0.712 0.024  0.000  -0.139 58  PHE DDD CD2 
11606 C CE1 . PHE D 58  ? 0.578 0.657 0.721 0.038  -0.008 -0.153 58  PHE DDD CE1 
11607 C CE2 . PHE D 58  ? 0.592 0.654 0.727 0.023  0.004  -0.145 58  PHE DDD CE2 
11608 C CZ  . PHE D 58  ? 0.573 0.646 0.717 0.030  -0.001 -0.152 58  PHE DDD CZ  
11609 N N   . VAL D 59  ? 0.556 0.634 0.656 0.040  -0.010 -0.135 59  VAL DDD N   
11610 C CA  . VAL D 59  ? 0.574 0.663 0.673 0.046  -0.013 -0.138 59  VAL DDD CA  
11611 C C   . VAL D 59  ? 0.575 0.670 0.687 0.049  -0.015 -0.146 59  VAL DDD C   
11612 O O   . VAL D 59  ? 0.547 0.641 0.664 0.046  -0.010 -0.147 59  VAL DDD O   
11613 C CB  . VAL D 59  ? 0.595 0.685 0.683 0.044  -0.009 -0.133 59  VAL DDD CB  
11614 C CG1 . VAL D 59  ? 0.601 0.703 0.689 0.051  -0.012 -0.135 59  VAL DDD CG1 
11615 C CG2 . VAL D 59  ? 0.584 0.668 0.659 0.041  -0.008 -0.126 59  VAL DDD CG2 
11616 N N   . LYS D 60  ? 0.602 0.705 0.721 0.056  -0.021 -0.151 60  LYS DDD N   
11617 C CA  . LYS D 60  ? 0.598 0.709 0.728 0.060  -0.023 -0.159 60  LYS DDD CA  
11618 C C   . LYS D 60  ? 0.565 0.684 0.690 0.063  -0.023 -0.158 60  LYS DDD C   
11619 O O   . LYS D 60  ? 0.545 0.668 0.659 0.065  -0.024 -0.154 60  LYS DDD O   
11620 C CB  . LYS D 60  ? 0.626 0.743 0.763 0.066  -0.030 -0.165 60  LYS DDD CB  
11621 C CG  . LYS D 60  ? 0.629 0.739 0.776 0.064  -0.031 -0.168 60  LYS DDD CG  
11622 C CD  . LYS D 60  ? 0.650 0.766 0.806 0.070  -0.037 -0.175 60  LYS DDD CD  
11623 C CE  . LYS D 60  ? 0.663 0.784 0.811 0.074  -0.041 -0.174 60  LYS DDD CE  
11624 N NZ  . LYS D 60  ? 0.680 0.790 0.821 0.069  -0.039 -0.166 60  LYS DDD NZ  
11625 N N   . PRO D 61  ? 0.574 0.695 0.706 0.062  -0.021 -0.161 61  PRO DDD N   
11626 C CA  . PRO D 61  ? 0.567 0.696 0.696 0.064  -0.022 -0.160 61  PRO DDD CA  
11627 C C   . PRO D 61  ? 0.585 0.725 0.711 0.072  -0.028 -0.162 61  PRO DDD C   
11628 O O   . PRO D 61  ? 0.589 0.734 0.721 0.076  -0.033 -0.168 61  PRO DDD O   
11629 C CB  . PRO D 61  ? 0.547 0.676 0.688 0.063  -0.020 -0.165 61  PRO DDD CB  
11630 C CG  . PRO D 61  ? 0.555 0.675 0.703 0.057  -0.015 -0.167 61  PRO DDD CG  
11631 C CD  . PRO D 61  ? 0.578 0.695 0.723 0.058  -0.018 -0.166 61  PRO DDD CD  
11632 N N   . SER D 62  ? 0.553 0.699 0.670 0.074  -0.028 -0.157 62  SER DDD N   
11633 C CA  . SER D 62  ? 0.550 0.708 0.663 0.080  -0.034 -0.158 62  SER DDD CA  
11634 C C   . SER D 62  ? 0.564 0.729 0.687 0.084  -0.038 -0.165 62  SER DDD C   
11635 O O   . SER D 62  ? 0.532 0.693 0.666 0.082  -0.036 -0.168 62  SER DDD O   
11636 C CB  . SER D 62  ? 0.544 0.704 0.647 0.080  -0.033 -0.150 62  SER DDD CB  
11637 O OG  . SER D 62  ? 0.497 0.657 0.606 0.079  -0.031 -0.150 62  SER DDD OG  
11638 N N   . THR D 63  ? 0.568 0.745 0.688 0.090  -0.044 -0.166 63  THR DDD N   
11639 C CA  . THR D 63  ? 0.578 0.764 0.706 0.095  -0.048 -0.172 63  THR DDD CA  
11640 C C   . THR D 63  ? 0.594 0.779 0.727 0.093  -0.046 -0.170 63  THR DDD C   
11641 O O   . THR D 63  ? 0.591 0.781 0.735 0.095  -0.050 -0.175 63  THR DDD O   
11642 C CB  . THR D 63  ? 0.551 0.750 0.672 0.101  -0.054 -0.173 63  THR DDD CB  
11643 O OG1 . THR D 63  ? 0.539 0.741 0.649 0.101  -0.053 -0.164 63  THR DDD OG1 
11644 C CG2 . THR D 63  ? 0.553 0.754 0.672 0.103  -0.056 -0.177 63  THR DDD CG2 
11645 N N   . GLN D 64  ? 0.630 0.809 0.757 0.089  -0.042 -0.163 64  GLN DDD N   
11646 C CA  . GLN D 64  ? 0.602 0.780 0.735 0.087  -0.040 -0.161 64  GLN DDD CA  
11647 C C   . GLN D 64  ? 0.555 0.721 0.693 0.080  -0.033 -0.161 64  GLN DDD C   
11648 O O   . GLN D 64  ? 0.588 0.753 0.730 0.077  -0.030 -0.158 64  GLN DDD O   
11649 C CB  . GLN D 64  ? 0.616 0.798 0.739 0.088  -0.041 -0.153 64  GLN DDD CB  
11650 C CG  . GLN D 64  ? 0.618 0.813 0.738 0.095  -0.047 -0.153 64  GLN DDD CG  
11651 C CD  . GLN D 64  ? 0.598 0.799 0.729 0.097  -0.052 -0.158 64  GLN DDD CD  
11652 O OE1 . GLN D 64  ? 0.602 0.799 0.742 0.095  -0.050 -0.159 64  GLN DDD OE1 
11653 N NE2 . GLN D 64  ? 0.587 0.799 0.717 0.103  -0.058 -0.162 64  GLN DDD NE2 
11654 N N   . GLY D 65  ? 0.523 0.682 0.663 0.077  -0.030 -0.164 65  GLY DDD N   
11655 C CA  . GLY D 65  ? 0.514 0.663 0.660 0.070  -0.023 -0.164 65  GLY DDD CA  
11656 C C   . GLY D 65  ? 0.504 0.645 0.638 0.065  -0.018 -0.157 65  GLY DDD C   
11657 O O   . GLY D 65  ? 0.487 0.620 0.624 0.059  -0.012 -0.157 65  GLY DDD O   
11658 N N   . THR D 66  ? 0.485 0.629 0.608 0.067  -0.020 -0.151 66  THR DDD N   
11659 C CA  . THR D 66  ? 0.477 0.614 0.589 0.063  -0.015 -0.144 66  THR DDD CA  
11660 C C   . THR D 66  ? 0.470 0.599 0.577 0.059  -0.013 -0.144 66  THR DDD C   
11661 O O   . THR D 66  ? 0.479 0.610 0.586 0.063  -0.017 -0.146 66  THR DDD O   
11662 C CB  . THR D 66  ? 0.483 0.625 0.583 0.066  -0.017 -0.138 66  THR DDD CB  
11663 O OG1 . THR D 66  ? 0.497 0.648 0.602 0.070  -0.021 -0.139 66  THR DDD OG1 
11664 C CG2 . THR D 66  ? 0.479 0.615 0.571 0.061  -0.012 -0.132 66  THR DDD CG2 
11665 N N   . LYS D 67  ? 0.475 0.596 0.580 0.053  -0.007 -0.141 67  LYS DDD N   
11666 C CA  . LYS D 67  ? 0.503 0.615 0.602 0.049  -0.004 -0.139 67  LYS DDD CA  
11667 C C   . LYS D 67  ? 0.464 0.569 0.552 0.044  0.001  -0.133 67  LYS DDD C   
11668 O O   . LYS D 67  ? 0.417 0.525 0.504 0.043  0.003  -0.131 67  LYS DDD O   
11669 C CB  . LYS D 67  ? 0.532 0.639 0.642 0.045  -0.002 -0.144 67  LYS DDD CB  
11670 C CG  . LYS D 67  ? 0.582 0.684 0.696 0.039  0.005  -0.144 67  LYS DDD CG  
11671 C CD  . LYS D 67  ? 0.598 0.695 0.722 0.035  0.008  -0.149 67  LYS DDD CD  
11672 C CE  . LYS D 67  ? 0.620 0.714 0.750 0.029  0.015  -0.151 67  LYS DDD CE  
11673 N NZ  . LYS D 67  ? 0.616 0.713 0.763 0.029  0.015  -0.158 67  LYS DDD NZ  
11674 N N   . TRP D 68  ? 0.451 0.549 0.531 0.040  0.002  -0.129 68  TRP DDD N   
11675 C CA  . TRP D 68  ? 0.433 0.526 0.501 0.036  0.005  -0.123 68  TRP DDD CA  
11676 C C   . TRP D 68  ? 0.429 0.513 0.492 0.031  0.006  -0.120 68  TRP DDD C   
11677 O O   . TRP D 68  ? 0.427 0.508 0.496 0.032  0.005  -0.123 68  TRP DDD O   
11678 C CB  . TRP D 68  ? 0.428 0.527 0.488 0.042  0.000  -0.119 68  TRP DDD CB  
11679 C CG  . TRP D 68  ? 0.433 0.536 0.494 0.047  -0.006 -0.120 68  TRP DDD CG  
11680 C CD1 . TRP D 68  ? 0.447 0.546 0.504 0.047  -0.008 -0.118 68  TRP DDD CD1 
11681 C CD2 . TRP D 68  ? 0.433 0.546 0.500 0.054  -0.011 -0.124 68  TRP DDD CD2 
11682 N NE1 . TRP D 68  ? 0.445 0.549 0.504 0.053  -0.014 -0.122 68  TRP DDD NE1 
11683 C CE2 . TRP D 68  ? 0.422 0.536 0.488 0.057  -0.015 -0.125 68  TRP DDD CE2 
11684 C CE3 . TRP D 68  ? 0.429 0.549 0.502 0.057  -0.012 -0.127 68  TRP DDD CE3 
11685 C CZ2 . TRP D 68  ? 0.412 0.536 0.482 0.064  -0.020 -0.130 68  TRP DDD CZ2 
11686 C CZ3 . TRP D 68  ? 0.429 0.559 0.506 0.063  -0.017 -0.131 68  TRP DDD CZ3 
11687 C CH2 . TRP D 68  ? 0.422 0.554 0.497 0.067  -0.021 -0.132 68  TRP DDD CH2 
11688 N N   . GLY D 69  ? 0.416 0.495 0.467 0.027  0.009  -0.114 69  GLY DDD N   
11689 C CA  . GLY D 69  ? 0.424 0.493 0.468 0.021  0.011  -0.111 69  GLY DDD CA  
11690 C C   . GLY D 69  ? 0.441 0.508 0.480 0.024  0.006  -0.107 69  GLY DDD C   
11691 O O   . GLY D 69  ? 0.453 0.527 0.496 0.031  0.000  -0.109 69  GLY DDD O   
11692 N N   . LEU D 70  ? 0.460 0.519 0.492 0.019  0.007  -0.102 70  LEU DDD N   
11693 C CA  . LEU D 70  ? 0.499 0.554 0.525 0.021  0.002  -0.098 70  LEU DDD CA  
11694 C C   . LEU D 70  ? 0.488 0.549 0.507 0.026  -0.002 -0.096 70  LEU DDD C   
11695 O O   . LEU D 70  ? 0.457 0.519 0.470 0.025  0.001  -0.095 70  LEU DDD O   
11696 C CB  . LEU D 70  ? 0.519 0.563 0.537 0.013  0.005  -0.093 70  LEU DDD CB  
11697 C CG  . LEU D 70  ? 0.573 0.613 0.585 0.014  -0.001 -0.088 70  LEU DDD CG  
11698 C CD1 . LEU D 70  ? 0.565 0.604 0.588 0.018  -0.006 -0.090 70  LEU DDD CD1 
11699 C CD2 . LEU D 70  ? 0.607 0.638 0.608 0.007  0.002  -0.081 70  LEU DDD CD2 
11700 N N   . GLY D 71  ? 0.481 0.542 0.500 0.030  -0.008 -0.096 71  GLY DDD N   
11701 C CA  . GLY D 71  ? 0.471 0.536 0.483 0.034  -0.011 -0.093 71  GLY DDD CA  
11702 C C   . GLY D 71  ? 0.448 0.522 0.466 0.041  -0.016 -0.097 71  GLY DDD C   
11703 O O   . GLY D 71  ? 0.456 0.533 0.470 0.045  -0.019 -0.095 71  GLY DDD O   
11704 N N   . GLY D 72  ? 0.449 0.528 0.477 0.044  -0.016 -0.102 72  GLY DDD N   
11705 C CA  . GLY D 72  ? 0.436 0.523 0.470 0.051  -0.021 -0.107 72  GLY DDD CA  
11706 C C   . GLY D 72  ? 0.427 0.525 0.459 0.056  -0.021 -0.108 72  GLY DDD C   
11707 O O   . GLY D 72  ? 0.456 0.554 0.485 0.053  -0.017 -0.105 72  GLY DDD O   
11708 N N   . THR D 73  ? 0.408 0.515 0.443 0.062  -0.026 -0.111 73  THR DDD N   
11709 C CA  . THR D 73  ? 0.425 0.543 0.459 0.066  -0.026 -0.112 73  THR DDD CA  
11710 C C   . THR D 73  ? 0.412 0.530 0.436 0.065  -0.024 -0.105 73  THR DDD C   
11711 O O   . THR D 73  ? 0.399 0.521 0.422 0.065  -0.022 -0.104 73  THR DDD O   
11712 C CB  . THR D 73  ? 0.422 0.550 0.461 0.073  -0.031 -0.117 73  THR DDD CB  
11713 O OG1 . THR D 73  ? 0.395 0.523 0.443 0.073  -0.032 -0.123 73  THR DDD OG1 
11714 C CG2 . THR D 73  ? 0.425 0.564 0.460 0.077  -0.032 -0.117 73  THR DDD CG2 
11715 N N   . CYS D 74  ? 0.423 0.537 0.441 0.064  -0.025 -0.102 74  CYS DDD N   
11716 C CA  A CYS D 74  ? 0.414 0.529 0.424 0.063  -0.024 -0.096 74  CYS DDD CA  
11717 C CA  B CYS D 74  ? 0.442 0.554 0.451 0.062  -0.024 -0.096 74  CYS DDD CA  
11718 C C   . CYS D 74  ? 0.407 0.516 0.414 0.058  -0.019 -0.093 74  CYS DDD C   
11719 O O   . CYS D 74  ? 0.448 0.563 0.453 0.059  -0.017 -0.091 74  CYS DDD O   
11720 C CB  A CYS D 74  ? 0.420 0.531 0.425 0.063  -0.026 -0.093 74  CYS DDD CB  
11721 C CB  B CYS D 74  ? 0.497 0.601 0.502 0.060  -0.025 -0.092 74  CYS DDD CB  
11722 S SG  A CYS D 74  ? 0.434 0.548 0.431 0.063  -0.025 -0.088 74  CYS DDD SG  
11723 S SG  B CYS D 74  ? 0.554 0.658 0.549 0.059  -0.024 -0.086 74  CYS DDD SG  
11724 N N   . VAL D 75  ? 0.377 0.477 0.384 0.053  -0.016 -0.093 75  VAL DDD N   
11725 C CA  . VAL D 75  ? 0.373 0.468 0.377 0.047  -0.011 -0.091 75  VAL DDD CA  
11726 C C   . VAL D 75  ? 0.333 0.433 0.344 0.048  -0.009 -0.094 75  VAL DDD C   
11727 O O   . VAL D 75  ? 0.309 0.410 0.318 0.046  -0.005 -0.092 75  VAL DDD O   
11728 C CB  . VAL D 75  ? 0.399 0.483 0.402 0.041  -0.009 -0.090 75  VAL DDD CB  
11729 C CG1 . VAL D 75  ? 0.410 0.491 0.412 0.035  -0.003 -0.090 75  VAL DDD CG1 
11730 C CG2 . VAL D 75  ? 0.412 0.490 0.407 0.039  -0.011 -0.086 75  VAL DDD CG2 
11731 N N   . ASN D 76  ? 0.313 0.416 0.332 0.050  -0.010 -0.099 76  ASN DDD N   
11732 C CA  . ASN D 76  ? 0.313 0.420 0.340 0.050  -0.008 -0.102 76  ASN DDD CA  
11733 C C   . ASN D 76  ? 0.322 0.440 0.353 0.056  -0.011 -0.103 76  ASN DDD C   
11734 O O   . ASN D 76  ? 0.360 0.480 0.394 0.056  -0.009 -0.104 76  ASN DDD O   
11735 C CB  . ASN D 76  ? 0.324 0.427 0.359 0.048  -0.008 -0.107 76  ASN DDD CB  
11736 C CG  . ASN D 76  ? 0.320 0.412 0.351 0.042  -0.004 -0.105 76  ASN DDD CG  
11737 O OD1 . ASN D 76  ? 0.314 0.402 0.345 0.037  0.001  -0.104 76  ASN DDD OD1 
11738 N ND2 . ASN D 76  ? 0.327 0.414 0.355 0.041  -0.006 -0.103 76  ASN DDD ND2 
11739 N N   . VAL D 77  ? 0.305 0.429 0.336 0.061  -0.016 -0.105 77  VAL DDD N   
11740 C CA  . VAL D 77  ? 0.305 0.440 0.339 0.067  -0.019 -0.107 77  VAL DDD CA  
11741 C C   . VAL D 77  ? 0.300 0.442 0.329 0.071  -0.022 -0.105 77  VAL DDD C   
11742 O O   . VAL D 77  ? 0.299 0.450 0.330 0.076  -0.026 -0.108 77  VAL DDD O   
11743 C CB  . VAL D 77  ? 0.298 0.435 0.341 0.069  -0.021 -0.114 77  VAL DDD CB  
11744 C CG1 . VAL D 77  ? 0.306 0.440 0.357 0.065  -0.017 -0.116 77  VAL DDD CG1 
11745 C CG2 . VAL D 77  ? 0.305 0.439 0.351 0.069  -0.023 -0.117 77  VAL DDD CG2 
11746 N N   . GLY D 78  ? 0.327 0.465 0.348 0.070  -0.021 -0.100 78  GLY DDD N   
11747 C CA  . GLY D 78  ? 0.320 0.465 0.337 0.074  -0.024 -0.099 78  GLY DDD CA  
11748 C C   . GLY D 78  ? 0.337 0.480 0.347 0.072  -0.022 -0.093 78  GLY DDD C   
11749 O O   . GLY D 78  ? 0.365 0.510 0.375 0.071  -0.020 -0.090 78  GLY DDD O   
11750 N N   . CYS D 79  ? 0.344 0.483 0.349 0.071  -0.023 -0.091 79  CYS DDD N   
11751 C CA  . CYS D 79  ? 0.344 0.484 0.343 0.071  -0.022 -0.085 79  CYS DDD CA  
11752 C C   . CYS D 79  ? 0.341 0.475 0.338 0.066  -0.018 -0.082 79  CYS DDD C   
11753 O O   . CYS D 79  ? 0.345 0.484 0.341 0.067  -0.017 -0.078 79  CYS DDD O   
11754 C CB  . CYS D 79  ? 0.384 0.517 0.379 0.070  -0.024 -0.084 79  CYS DDD CB  
11755 S SG  . CYS D 79  ? 0.431 0.561 0.430 0.071  -0.028 -0.090 79  CYS DDD SG  
11756 N N   . VAL D 80  ? 0.307 0.433 0.306 0.062  -0.016 -0.083 80  VAL DDD N   
11757 C CA  . VAL D 80  ? 0.292 0.411 0.288 0.057  -0.012 -0.080 80  VAL DDD CA  
11758 C C   . VAL D 80  ? 0.265 0.391 0.267 0.058  -0.010 -0.080 80  VAL DDD C   
11759 O O   . VAL D 80  ? 0.239 0.367 0.240 0.058  -0.009 -0.077 80  VAL DDD O   
11760 C CB  . VAL D 80  ? 0.309 0.418 0.304 0.051  -0.009 -0.082 80  VAL DDD CB  
11761 C CG1 . VAL D 80  ? 0.320 0.426 0.315 0.047  -0.004 -0.080 80  VAL DDD CG1 
11762 C CG2 . VAL D 80  ? 0.313 0.416 0.302 0.049  -0.011 -0.080 80  VAL DDD CG2 
11763 N N   . PRO D 81  ? 0.269 0.397 0.278 0.059  -0.010 -0.084 81  PRO DDD N   
11764 C CA  . PRO D 81  ? 0.276 0.410 0.292 0.060  -0.009 -0.084 81  PRO DDD CA  
11765 C C   . PRO D 81  ? 0.292 0.436 0.307 0.065  -0.012 -0.081 81  PRO DDD C   
11766 O O   . PRO D 81  ? 0.279 0.425 0.296 0.065  -0.011 -0.077 81  PRO DDD O   
11767 C CB  . PRO D 81  ? 0.266 0.400 0.288 0.060  -0.010 -0.089 81  PRO DDD CB  
11768 C CG  . PRO D 81  ? 0.271 0.403 0.292 0.061  -0.012 -0.092 81  PRO DDD CG  
11769 C CD  . PRO D 81  ? 0.279 0.404 0.291 0.058  -0.011 -0.089 81  PRO DDD CD  
11770 N N   . LYS D 82  ? 0.278 0.427 0.289 0.069  -0.016 -0.081 82  LYS DDD N   
11771 C CA  . LYS D 82  ? 0.310 0.469 0.319 0.073  -0.018 -0.078 82  LYS DDD CA  
11772 C C   . LYS D 82  ? 0.302 0.461 0.308 0.072  -0.016 -0.072 82  LYS DDD C   
11773 O O   . LYS D 82  ? 0.300 0.464 0.308 0.073  -0.016 -0.068 82  LYS DDD O   
11774 C CB  . LYS D 82  ? 0.333 0.498 0.340 0.077  -0.021 -0.081 82  LYS DDD CB  
11775 C CG  . LYS D 82  ? 0.347 0.523 0.351 0.081  -0.023 -0.078 82  LYS DDD CG  
11776 C CD  . LYS D 82  ? 0.372 0.547 0.370 0.081  -0.023 -0.074 82  LYS DDD CD  
11777 C CE  . LYS D 82  ? 0.382 0.551 0.378 0.080  -0.024 -0.077 82  LYS DDD CE  
11778 N NZ  . LYS D 82  ? 0.375 0.551 0.372 0.084  -0.027 -0.082 82  LYS DDD NZ  
11779 N N   . LYS D 83  ? 0.317 0.468 0.318 0.069  -0.015 -0.072 83  LYS DDD N   
11780 C CA  . LYS D 83  ? 0.304 0.453 0.301 0.067  -0.014 -0.067 83  LYS DDD CA  
11781 C C   . LYS D 83  ? 0.268 0.415 0.270 0.064  -0.010 -0.065 83  LYS DDD C   
11782 O O   . LYS D 83  ? 0.244 0.393 0.246 0.064  -0.010 -0.060 83  LYS DDD O   
11783 C CB  . LYS D 83  ? 0.315 0.456 0.307 0.065  -0.014 -0.067 83  LYS DDD CB  
11784 C CG  . LYS D 83  ? 0.349 0.489 0.338 0.063  -0.013 -0.063 83  LYS DDD CG  
11785 C CD  . LYS D 83  ? 0.336 0.483 0.322 0.067  -0.015 -0.060 83  LYS DDD CD  
11786 C CE  . LYS D 83  ? 0.342 0.489 0.327 0.066  -0.014 -0.056 83  LYS DDD CE  
11787 N NZ  . LYS D 83  ? 0.362 0.507 0.343 0.066  -0.016 -0.056 83  LYS DDD NZ  
11788 N N   . LEU D 84  ? 0.247 0.387 0.252 0.061  -0.008 -0.068 84  LEU DDD N   
11789 C CA  . LEU D 84  ? 0.234 0.373 0.245 0.058  -0.005 -0.067 84  LEU DDD CA  
11790 C C   . LEU D 84  ? 0.245 0.392 0.263 0.061  -0.007 -0.065 84  LEU DDD C   
11791 O O   . LEU D 84  ? 0.235 0.383 0.257 0.060  -0.006 -0.062 84  LEU DDD O   
11792 C CB  . LEU D 84  ? 0.237 0.369 0.251 0.053  -0.002 -0.072 84  LEU DDD CB  
11793 C CG  . LEU D 84  ? 0.240 0.363 0.246 0.049  -0.001 -0.073 84  LEU DDD CG  
11794 C CD1 . LEU D 84  ? 0.243 0.360 0.251 0.045  0.002  -0.078 84  LEU DDD CD1 
11795 C CD2 . LEU D 84  ? 0.253 0.372 0.254 0.047  0.001  -0.070 84  LEU DDD CD2 
11796 N N   . MET D 85  ? 0.242 0.395 0.262 0.065  -0.010 -0.067 85  MET DDD N   
11797 C CA  . MET D 85  ? 0.268 0.429 0.294 0.068  -0.012 -0.065 85  MET DDD CA  
11798 C C   . MET D 85  ? 0.241 0.409 0.263 0.070  -0.013 -0.058 85  MET DDD C   
11799 O O   . MET D 85  ? 0.238 0.409 0.265 0.070  -0.013 -0.054 85  MET DDD O   
11800 C CB  . MET D 85  ? 0.301 0.467 0.328 0.071  -0.015 -0.068 85  MET DDD CB  
11801 C CG  . MET D 85  ? 0.344 0.505 0.376 0.069  -0.014 -0.074 85  MET DDD CG  
11802 S SD  . MET D 85  ? 0.433 0.594 0.476 0.068  -0.013 -0.076 85  MET DDD SD  
11803 C CE  . MET D 85  ? 0.389 0.562 0.433 0.074  -0.019 -0.074 85  MET DDD CE  
11804 N N   . HIS D 86  ? 0.239 0.408 0.254 0.072  -0.014 -0.058 86  HIS DDD N   
11805 C CA  . HIS D 86  ? 0.238 0.414 0.249 0.074  -0.015 -0.052 86  HIS DDD CA  
11806 C C   . HIS D 86  ? 0.236 0.407 0.249 0.070  -0.012 -0.048 86  HIS DDD C   
11807 O O   . HIS D 86  ? 0.246 0.422 0.262 0.072  -0.013 -0.043 86  HIS DDD O   
11808 C CB  . HIS D 86  ? 0.242 0.418 0.245 0.075  -0.016 -0.054 86  HIS DDD CB  
11809 C CG  . HIS D 86  ? 0.264 0.445 0.264 0.077  -0.016 -0.050 86  HIS DDD CG  
11810 N ND1 . HIS D 86  ? 0.273 0.465 0.273 0.080  -0.018 -0.046 86  HIS DDD ND1 
11811 C CD2 . HIS D 86  ? 0.277 0.455 0.273 0.076  -0.016 -0.048 86  HIS DDD CD2 
11812 C CE1 . HIS D 86  ? 0.276 0.471 0.273 0.081  -0.017 -0.042 86  HIS DDD CE1 
11813 N NE2 . HIS D 86  ? 0.289 0.476 0.284 0.078  -0.016 -0.044 86  HIS DDD NE2 
11814 N N   . TYR D 87  ? 0.243 0.404 0.256 0.066  -0.010 -0.051 87  TYR DDD N   
11815 C CA  . TYR D 87  ? 0.237 0.394 0.253 0.063  -0.007 -0.048 87  TYR DDD CA  
11816 C C   . TYR D 87  ? 0.225 0.384 0.251 0.063  -0.007 -0.046 87  TYR DDD C   
11817 O O   . TYR D 87  ? 0.213 0.374 0.242 0.063  -0.007 -0.041 87  TYR DDD O   
11818 C CB  . TYR D 87  ? 0.272 0.419 0.284 0.059  -0.005 -0.052 87  TYR DDD CB  
11819 C CG  . TYR D 87  ? 0.314 0.456 0.327 0.055  -0.003 -0.050 87  TYR DDD CG  
11820 C CD1 . TYR D 87  ? 0.356 0.501 0.366 0.056  -0.003 -0.046 87  TYR DDD CD1 
11821 C CD2 . TYR D 87  ? 0.341 0.479 0.359 0.051  0.000  -0.053 87  TYR DDD CD2 
11822 C CE1 . TYR D 87  ? 0.384 0.526 0.396 0.054  -0.002 -0.045 87  TYR DDD CE1 
11823 C CE2 . TYR D 87  ? 0.349 0.484 0.369 0.049  0.002  -0.052 87  TYR DDD CE2 
11824 C CZ  . TYR D 87  ? 0.379 0.516 0.396 0.050  0.001  -0.048 87  TYR DDD CZ  
11825 O OH  . TYR D 87  ? 0.435 0.569 0.454 0.047  0.003  -0.047 87  TYR DDD OH  
11826 N N   . SER D 88  ? 0.211 0.369 0.242 0.062  -0.007 -0.050 88  SER DDD N   
11827 C CA  . SER D 88  ? 0.212 0.372 0.254 0.062  -0.007 -0.049 88  SER DDD CA  
11828 C C   . SER D 88  ? 0.218 0.388 0.261 0.066  -0.010 -0.042 88  SER DDD C   
11829 O O   . SER D 88  ? 0.218 0.389 0.269 0.066  -0.010 -0.038 88  SER DDD O   
11830 C CB  . SER D 88  ? 0.212 0.371 0.259 0.062  -0.007 -0.054 88  SER DDD CB  
11831 O OG  . SER D 88  ? 0.201 0.362 0.259 0.062  -0.008 -0.053 88  SER DDD OG  
11832 N N   . ALA D 89  ? 0.232 0.408 0.268 0.070  -0.013 -0.041 89  ALA DDD N   
11833 C CA  . ALA D 89  ? 0.260 0.446 0.296 0.073  -0.016 -0.035 89  ALA DDD CA  
11834 C C   . ALA D 89  ? 0.282 0.470 0.317 0.073  -0.014 -0.029 89  ALA DDD C   
11835 O O   . ALA D 89  ? 0.258 0.450 0.299 0.073  -0.015 -0.022 89  ALA DDD O   
11836 C CB  . ALA D 89  ? 0.260 0.452 0.287 0.077  -0.018 -0.037 89  ALA DDD CB  
11837 N N   . LEU D 90  ? 0.290 0.473 0.319 0.071  -0.012 -0.030 90  LEU DDD N   
11838 C CA  . LEU D 90  ? 0.300 0.484 0.328 0.070  -0.011 -0.025 90  LEU DDD CA  
11839 C C   . LEU D 90  ? 0.289 0.468 0.327 0.068  -0.010 -0.023 90  LEU DDD C   
11840 O O   . LEU D 90  ? 0.322 0.505 0.365 0.068  -0.010 -0.017 90  LEU DDD O   
11841 C CB  . LEU D 90  ? 0.293 0.471 0.313 0.069  -0.010 -0.029 90  LEU DDD CB  
11842 C CG  . LEU D 90  ? 0.309 0.492 0.321 0.072  -0.012 -0.031 90  LEU DDD CG  
11843 C CD1 . LEU D 90  ? 0.292 0.469 0.298 0.071  -0.011 -0.034 90  LEU DDD CD1 
11844 C CD2 . LEU D 90  ? 0.317 0.510 0.328 0.075  -0.013 -0.025 90  LEU DDD CD2 
11845 N N   . ILE D 91  ? 0.286 0.459 0.329 0.065  -0.008 -0.028 91  ILE DDD N   
11846 C CA  . ILE D 91  ? 0.271 0.440 0.325 0.062  -0.007 -0.028 91  ILE DDD CA  
11847 C C   . ILE D 91  ? 0.270 0.445 0.333 0.064  -0.009 -0.022 91  ILE DDD C   
11848 O O   . ILE D 91  ? 0.266 0.443 0.338 0.064  -0.009 -0.017 91  ILE DDD O   
11849 C CB  . ILE D 91  ? 0.245 0.406 0.302 0.059  -0.004 -0.035 91  ILE DDD CB  
11850 C CG1 . ILE D 91  ? 0.234 0.388 0.282 0.056  -0.002 -0.039 91  ILE DDD CG1 
11851 C CG2 . ILE D 91  ? 0.239 0.398 0.310 0.056  -0.003 -0.035 91  ILE DDD CG2 
11852 C CD1 . ILE D 91  ? 0.240 0.387 0.289 0.052  0.001  -0.046 91  ILE DDD CD1 
11853 N N   . ALA D 92  ? 0.287 0.466 0.351 0.066  -0.012 -0.023 92  ALA DDD N   
11854 C CA  . ALA D 92  ? 0.311 0.497 0.382 0.069  -0.015 -0.017 92  ALA DDD CA  
11855 C C   . ALA D 92  ? 0.298 0.491 0.367 0.071  -0.016 -0.008 92  ALA DDD C   
11856 O O   . ALA D 92  ? 0.273 0.467 0.352 0.070  -0.017 -0.002 92  ALA DDD O   
11857 C CB  . ALA D 92  ? 0.326 0.515 0.393 0.072  -0.018 -0.020 92  ALA DDD CB  
11858 N N   . SER D 93  ? 0.323 0.519 0.380 0.072  -0.016 -0.008 93  SER DDD N   
11859 C CA  . SER D 93  ? 0.332 0.537 0.386 0.074  -0.017 0.000  93  SER DDD CA  
11860 C C   . SER D 93  ? 0.305 0.506 0.366 0.071  -0.015 0.004  93  SER DDD C   
11861 O O   . SER D 93  ? 0.298 0.504 0.365 0.072  -0.015 0.012  93  SER DDD O   
11862 C CB  . SER D 93  ? 0.347 0.555 0.388 0.076  -0.016 -0.003 93  SER DDD CB  
11863 O OG  . SER D 93  ? 0.419 0.636 0.457 0.077  -0.016 0.004  93  SER DDD OG  
11864 N N   . SER D 94  ? 0.292 0.485 0.352 0.069  -0.012 -0.001 94  SER DDD N   
11865 C CA  . SER D 94  ? 0.291 0.480 0.357 0.066  -0.010 0.001  94  SER DDD CA  
11866 C C   . SER D 94  ? 0.283 0.470 0.364 0.065  -0.010 0.004  94  SER DDD C   
11867 O O   . SER D 94  ? 0.276 0.466 0.365 0.064  -0.010 0.010  94  SER DDD O   
11868 C CB  . SER D 94  ? 0.287 0.468 0.348 0.064  -0.007 -0.007 94  SER DDD CB  
11869 O OG  . SER D 94  ? 0.316 0.491 0.386 0.061  -0.006 -0.008 94  SER DDD OG  
11870 N N   . ILE D 95  ? 0.284 0.469 0.371 0.064  -0.011 -0.000 95  ILE DDD N   
11871 C CA  . ILE D 95  ? 0.275 0.459 0.379 0.063  -0.012 0.001  95  ILE DDD CA  
11872 C C   . ILE D 95  ? 0.281 0.472 0.389 0.066  -0.016 0.011  95  ILE DDD C   
11873 O O   . ILE D 95  ? 0.292 0.483 0.412 0.065  -0.016 0.016  95  ILE DDD O   
11874 C CB  . ILE D 95  ? 0.281 0.459 0.389 0.062  -0.012 -0.006 95  ILE DDD CB  
11875 C CG1 . ILE D 95  ? 0.288 0.458 0.394 0.058  -0.008 -0.015 95  ILE DDD CG1 
11876 C CG2 . ILE D 95  ? 0.283 0.462 0.408 0.062  -0.014 -0.004 95  ILE DDD CG2 
11877 C CD1 . ILE D 95  ? 0.293 0.459 0.403 0.057  -0.007 -0.023 95  ILE DDD CD1 
11878 N N   . HIS D 96  ? 0.300 0.497 0.400 0.069  -0.018 0.013  96  HIS DDD N   
11879 C CA  . HIS D 96  ? 0.316 0.521 0.418 0.071  -0.022 0.023  96  HIS DDD CA  
11880 C C   . HIS D 96  ? 0.308 0.519 0.409 0.071  -0.021 0.031  96  HIS DDD C   
11881 O O   . HIS D 96  ? 0.279 0.491 0.391 0.070  -0.023 0.039  96  HIS DDD O   
11882 C CB  . HIS D 96  ? 0.353 0.565 0.444 0.074  -0.024 0.022  96  HIS DDD CB  
11883 C CG  . HIS D 96  ? 0.428 0.649 0.521 0.076  -0.028 0.031  96  HIS DDD CG  
11884 N ND1 . HIS D 96  ? 0.488 0.719 0.570 0.078  -0.029 0.037  96  HIS DDD ND1 
11885 C CD2 . HIS D 96  ? 0.487 0.709 0.592 0.077  -0.032 0.036  96  HIS DDD CD2 
11886 C CE1 . HIS D 96  ? 0.518 0.755 0.603 0.080  -0.033 0.046  96  HIS DDD CE1 
11887 N NE2 . HIS D 96  ? 0.535 0.767 0.635 0.079  -0.035 0.046  96  HIS DDD NE2 
11888 N N   . HIS D 97  ? 0.315 0.527 0.404 0.071  -0.018 0.029  97  HIS DDD N   
11889 C CA  . HIS D 97  ? 0.318 0.536 0.403 0.072  -0.018 0.037  97  HIS DDD CA  
11890 C C   . HIS D 97  ? 0.330 0.543 0.423 0.069  -0.015 0.038  97  HIS DDD C   
11891 O O   . HIS D 97  ? 0.355 0.574 0.453 0.069  -0.015 0.046  97  HIS DDD O   
11892 C CB  . HIS D 97  ? 0.289 0.513 0.358 0.074  -0.017 0.034  97  HIS DDD CB  
11893 C CG  . HIS D 97  ? 0.306 0.537 0.367 0.076  -0.019 0.035  97  HIS DDD CG  
11894 N ND1 . HIS D 97  ? 0.320 0.561 0.383 0.078  -0.022 0.044  97  HIS DDD ND1 
11895 C CD2 . HIS D 97  ? 0.307 0.539 0.360 0.078  -0.020 0.027  97  HIS DDD CD2 
11896 C CE1 . HIS D 97  ? 0.318 0.565 0.372 0.080  -0.024 0.042  97  HIS DDD CE1 
11897 N NE2 . HIS D 97  ? 0.331 0.572 0.379 0.081  -0.023 0.032  97  HIS DDD NE2 
11898 N N   . ASP D 98  ? 0.331 0.535 0.425 0.067  -0.013 0.029  98  ASP DDD N   
11899 C CA  . ASP D 98  ? 0.314 0.515 0.409 0.065  -0.010 0.028  98  ASP DDD CA  
11900 C C   . ASP D 98  ? 0.302 0.496 0.412 0.062  -0.009 0.026  98  ASP DDD C   
11901 O O   . ASP D 98  ? 0.319 0.512 0.436 0.061  -0.008 0.029  98  ASP DDD O   
11902 C CB  . ASP D 98  ? 0.303 0.500 0.385 0.065  -0.008 0.020  98  ASP DDD CB  
11903 C CG  . ASP D 98  ? 0.290 0.494 0.359 0.067  -0.009 0.021  98  ASP DDD CG  
11904 O OD1 . ASP D 98  ? 0.304 0.517 0.372 0.069  -0.010 0.028  98  ASP DDD OD1 
11905 O OD2 . ASP D 98  ? 0.296 0.496 0.355 0.068  -0.008 0.014  98  ASP DDD OD2 
11906 N N   . ALA D 99  ? 0.292 0.480 0.407 0.061  -0.010 0.020  99  ALA DDD N   
11907 C CA  . ALA D 99  ? 0.306 0.488 0.434 0.058  -0.008 0.015  99  ALA DDD CA  
11908 C C   . ALA D 99  ? 0.338 0.521 0.482 0.057  -0.009 0.022  99  ALA DDD C   
11909 O O   . ALA D 99  ? 0.392 0.572 0.543 0.055  -0.008 0.020  99  ALA DDD O   
11910 C CB  . ALA D 99  ? 0.303 0.481 0.434 0.057  -0.009 0.008  99  ALA DDD CB  
11911 N N   . GLN D 100 ? 0.349 0.537 0.500 0.059  -0.012 0.030  100 GLN DDD N   
11912 C CA  . GLN D 100 ? 0.366 0.556 0.535 0.058  -0.014 0.038  100 GLN DDD CA  
11913 C C   . GLN D 100 ? 0.337 0.529 0.505 0.058  -0.012 0.043  100 GLN DDD C   
11914 O O   . GLN D 100 ? 0.320 0.509 0.501 0.056  -0.011 0.044  100 GLN DDD O   
11915 C CB  . GLN D 100 ? 0.408 0.604 0.580 0.060  -0.018 0.047  100 GLN DDD CB  
11916 C CG  . GLN D 100 ? 0.452 0.651 0.640 0.060  -0.020 0.058  100 GLN DDD CG  
11917 C CD  . GLN D 100 ? 0.533 0.725 0.741 0.058  -0.021 0.054  100 GLN DDD CD  
11918 O OE1 . GLN D 100 ? 0.574 0.763 0.793 0.056  -0.019 0.053  100 GLN DDD OE1 
11919 N NE2 . GLN D 100 ? 0.624 0.814 0.837 0.058  -0.023 0.050  100 GLN DDD NE2 
11920 N N   . MET D 101 ? 0.312 0.510 0.464 0.059  -0.012 0.047  101 MET DDD N   
11921 C CA  . MET D 101 ? 0.307 0.509 0.458 0.059  -0.010 0.053  101 MET DDD CA  
11922 C C   . MET D 101 ? 0.276 0.472 0.428 0.057  -0.008 0.045  101 MET DDD C   
11923 O O   . MET D 101 ? 0.259 0.455 0.419 0.056  -0.007 0.049  101 MET DDD O   
11924 C CB  . MET D 101 ? 0.326 0.536 0.460 0.062  -0.010 0.055  101 MET DDD CB  
11925 C CG  . MET D 101 ? 0.348 0.565 0.479 0.064  -0.012 0.065  101 MET DDD CG  
11926 S SD  . MET D 101 ? 0.408 0.631 0.555 0.062  -0.013 0.079  101 MET DDD SD  
11927 C CE  . MET D 101 ? 0.393 0.620 0.533 0.062  -0.009 0.081  101 MET DDD CE  
11928 N N   . PHE D 102 ? 0.250 0.440 0.395 0.056  -0.006 0.035  102 PHE DDD N   
11929 C CA  . PHE D 102 ? 0.248 0.432 0.391 0.054  -0.004 0.027  102 PHE DDD CA  
11930 C C   . PHE D 102 ? 0.258 0.436 0.416 0.052  -0.004 0.022  102 PHE DDD C   
11931 O O   . PHE D 102 ? 0.266 0.438 0.421 0.050  -0.002 0.014  102 PHE DDD O   
11932 C CB  . PHE D 102 ? 0.239 0.421 0.363 0.055  -0.003 0.020  102 PHE DDD CB  
11933 C CG  . PHE D 102 ? 0.222 0.409 0.335 0.057  -0.003 0.024  102 PHE DDD CG  
11934 C CD1 . PHE D 102 ? 0.233 0.427 0.339 0.060  -0.004 0.029  102 PHE DDD CD1 
11935 C CD2 . PHE D 102 ? 0.219 0.406 0.329 0.057  -0.002 0.023  102 PHE DDD CD2 
11936 C CE1 . PHE D 102 ? 0.240 0.441 0.336 0.062  -0.004 0.032  102 PHE DDD CE1 
11937 C CE2 . PHE D 102 ? 0.220 0.413 0.322 0.058  -0.002 0.027  102 PHE DDD CE2 
11938 C CZ  . PHE D 102 ? 0.233 0.433 0.327 0.061  -0.002 0.031  102 PHE DDD CZ  
11939 N N   . GLY D 103 ? 0.286 0.465 0.459 0.052  -0.006 0.026  103 GLY DDD N   
11940 C CA  . GLY D 103 ? 0.298 0.472 0.489 0.049  -0.006 0.023  103 GLY DDD CA  
11941 C C   . GLY D 103 ? 0.316 0.486 0.511 0.049  -0.006 0.015  103 GLY DDD C   
11942 O O   . GLY D 103 ? 0.330 0.496 0.540 0.046  -0.005 0.010  103 GLY DDD O   
11943 N N   . HIS D 104 ? 0.306 0.477 0.486 0.050  -0.006 0.013  104 HIS DDD N   
11944 C CA  . HIS D 104 ? 0.319 0.485 0.500 0.049  -0.005 0.004  104 HIS DDD CA  
11945 C C   . HIS D 104 ? 0.344 0.515 0.533 0.051  -0.009 0.010  104 HIS DDD C   
11946 O O   . HIS D 104 ? 0.334 0.508 0.509 0.054  -0.010 0.013  104 HIS DDD O   
11947 C CB  . HIS D 104 ? 0.298 0.462 0.460 0.049  -0.003 -0.003 104 HIS DDD CB  
11948 C CG  . HIS D 104 ? 0.291 0.451 0.446 0.047  -0.001 -0.008 104 HIS DDD CG  
11949 N ND1 . HIS D 104 ? 0.289 0.445 0.449 0.043  0.002  -0.017 104 HIS DDD ND1 
11950 C CD2 . HIS D 104 ? 0.294 0.455 0.437 0.047  -0.000 -0.006 104 HIS DDD CD2 
11951 C CE1 . HIS D 104 ? 0.287 0.440 0.438 0.042  0.003  -0.019 104 HIS DDD CE1 
11952 N NE2 . HIS D 104 ? 0.284 0.441 0.426 0.045  0.002  -0.012 104 HIS DDD NE2 
11953 N N   . LYS D 105 ? 0.353 0.523 0.562 0.051  -0.010 0.012  105 LYS DDD N   
11954 C CA  . LYS D 105 ? 0.401 0.573 0.619 0.052  -0.014 0.016  105 LYS DDD CA  
11955 C C   . LYS D 105 ? 0.364 0.533 0.579 0.051  -0.013 0.006  105 LYS DDD C   
11956 O O   . LYS D 105 ? 0.362 0.526 0.585 0.049  -0.010 -0.004 105 LYS DDD O   
11957 C CB  . LYS D 105 ? 0.451 0.624 0.694 0.051  -0.016 0.021  105 LYS DDD CB  
11958 C CG  . LYS D 105 ? 0.514 0.689 0.768 0.053  -0.021 0.026  105 LYS DDD CG  
11959 C CD  . LYS D 105 ? 0.561 0.742 0.805 0.056  -0.024 0.039  105 LYS DDD CD  
11960 C CE  . LYS D 105 ? 0.575 0.759 0.815 0.058  -0.028 0.041  105 LYS DDD CE  
11961 N NZ  . LYS D 105 ? 0.592 0.775 0.856 0.058  -0.032 0.043  105 LYS DDD NZ  
11962 N N   . THR D 106 ? 0.350 0.521 0.554 0.054  -0.014 0.007  106 THR DDD N   
11963 C CA  . THR D 106 ? 0.368 0.536 0.566 0.053  -0.013 -0.003 106 THR DDD CA  
11964 C C   . THR D 106 ? 0.364 0.535 0.569 0.055  -0.017 -0.000 106 THR DDD C   
11965 O O   . THR D 106 ? 0.367 0.543 0.570 0.058  -0.021 0.009  106 THR DDD O   
11966 C CB  . THR D 106 ? 0.344 0.512 0.520 0.054  -0.011 -0.006 106 THR DDD CB  
11967 O OG1 . THR D 106 ? 0.368 0.542 0.536 0.057  -0.014 0.002  106 THR DDD OG1 
11968 C CG2 . THR D 106 ? 0.341 0.508 0.509 0.052  -0.008 -0.007 106 THR DDD CG2 
11969 N N   . SER D 107 ? 0.377 0.544 0.589 0.054  -0.016 -0.009 107 SER DDD N   
11970 C CA  . SER D 107 ? 0.390 0.560 0.604 0.056  -0.019 -0.009 107 SER DDD CA  
11971 C C   . SER D 107 ? 0.398 0.565 0.597 0.055  -0.016 -0.018 107 SER DDD C   
11972 O O   . SER D 107 ? 0.413 0.575 0.610 0.052  -0.011 -0.027 107 SER DDD O   
11973 C CB  . SER D 107 ? 0.382 0.551 0.618 0.056  -0.022 -0.010 107 SER DDD CB  
11974 O OG  . SER D 107 ? 0.398 0.562 0.645 0.053  -0.018 -0.020 107 SER DDD OG  
11975 N N   . SER D 108 ? 0.407 0.577 0.596 0.058  -0.019 -0.017 108 SER DDD N   
11976 C CA  . SER D 108 ? 0.420 0.589 0.594 0.058  -0.016 -0.024 108 SER DDD CA  
11977 C C   . SER D 108 ? 0.393 0.564 0.569 0.061  -0.020 -0.024 108 SER DDD C   
11978 O O   . SER D 108 ? 0.394 0.570 0.574 0.064  -0.025 -0.016 108 SER DDD O   
11979 C CB  . SER D 108 ? 0.448 0.619 0.603 0.059  -0.015 -0.020 108 SER DDD CB  
11980 O OG  . SER D 108 ? 0.495 0.664 0.636 0.059  -0.013 -0.026 108 SER DDD OG  
11981 N N   . SER D 109 ? 0.392 0.560 0.566 0.059  -0.017 -0.034 109 SER DDD N   
11982 C CA  . SER D 109 ? 0.404 0.576 0.575 0.062  -0.021 -0.035 109 SER DDD CA  
11983 C C   . SER D 109 ? 0.386 0.554 0.543 0.061  -0.017 -0.043 109 SER DDD C   
11984 O O   . SER D 109 ? 0.395 0.558 0.552 0.057  -0.012 -0.050 109 SER DDD O   
11985 C CB  . SER D 109 ? 0.421 0.592 0.610 0.062  -0.023 -0.038 109 SER DDD CB  
11986 O OG  . SER D 109 ? 0.440 0.606 0.642 0.058  -0.019 -0.046 109 SER DDD OG  
11987 N N   . PHE D 110 ? 0.380 0.552 0.526 0.064  -0.020 -0.042 110 PHE DDD N   
11988 C CA  . PHE D 110 ? 0.371 0.542 0.504 0.064  -0.017 -0.047 110 PHE DDD CA  
11989 C C   . PHE D 110 ? 0.346 0.514 0.485 0.063  -0.017 -0.056 110 PHE DDD C   
11990 O O   . PHE D 110 ? 0.313 0.485 0.462 0.065  -0.020 -0.055 110 PHE DDD O   
11991 C CB  . PHE D 110 ? 0.355 0.532 0.475 0.068  -0.021 -0.042 110 PHE DDD CB  
11992 C CG  . PHE D 110 ? 0.340 0.516 0.448 0.068  -0.019 -0.048 110 PHE DDD CG  
11993 C CD1 . PHE D 110 ? 0.329 0.498 0.428 0.065  -0.014 -0.052 110 PHE DDD CD1 
11994 C CD2 . PHE D 110 ? 0.323 0.502 0.428 0.071  -0.022 -0.051 110 PHE DDD CD2 
11995 C CE1 . PHE D 110 ? 0.326 0.493 0.415 0.065  -0.013 -0.057 110 PHE DDD CE1 
11996 C CE2 . PHE D 110 ? 0.322 0.499 0.418 0.070  -0.020 -0.057 110 PHE DDD CE2 
11997 C CZ  . PHE D 110 ? 0.326 0.497 0.414 0.067  -0.016 -0.059 110 PHE DDD CZ  
11998 N N   . GLU D 111 ? 0.368 0.531 0.503 0.060  -0.012 -0.063 111 GLU DDD N   
11999 C CA  . GLU D 111 ? 0.371 0.531 0.512 0.058  -0.010 -0.072 111 GLU DDD CA  
12000 C C   . GLU D 111 ? 0.333 0.491 0.459 0.058  -0.009 -0.075 111 GLU DDD C   
12001 O O   . GLU D 111 ? 0.361 0.513 0.479 0.055  -0.004 -0.078 111 GLU DDD O   
12002 C CB  . GLU D 111 ? 0.404 0.558 0.555 0.053  -0.005 -0.078 111 GLU DDD CB  
12003 C CG  . GLU D 111 ? 0.441 0.596 0.607 0.053  -0.006 -0.075 111 GLU DDD CG  
12004 C CD  . GLU D 111 ? 0.479 0.638 0.662 0.056  -0.011 -0.073 111 GLU DDD CD  
12005 O OE1 . GLU D 111 ? 0.499 0.660 0.692 0.056  -0.014 -0.068 111 GLU DDD OE1 
12006 O OE2 . GLU D 111 ? 0.481 0.641 0.665 0.057  -0.013 -0.077 111 GLU DDD OE2 
12007 N N   . TRP D 112 ? 0.322 0.484 0.445 0.062  -0.013 -0.075 112 TRP DDD N   
12008 C CA  . TRP D 112 ? 0.313 0.476 0.425 0.063  -0.013 -0.078 112 TRP DDD CA  
12009 C C   . TRP D 112 ? 0.311 0.466 0.423 0.058  -0.007 -0.085 112 TRP DDD C   
12010 O O   . TRP D 112 ? 0.348 0.499 0.447 0.057  -0.005 -0.086 112 TRP DDD O   
12011 C CB  . TRP D 112 ? 0.299 0.467 0.412 0.068  -0.018 -0.078 112 TRP DDD CB  
12012 C CG  . TRP D 112 ? 0.294 0.463 0.399 0.069  -0.018 -0.083 112 TRP DDD CG  
12013 C CD1 . TRP D 112 ? 0.289 0.454 0.398 0.067  -0.017 -0.091 112 TRP DDD CD1 
12014 C CD2 . TRP D 112 ? 0.281 0.453 0.372 0.071  -0.020 -0.081 112 TRP DDD CD2 
12015 N NE1 . TRP D 112 ? 0.291 0.456 0.390 0.069  -0.018 -0.093 112 TRP DDD NE1 
12016 C CE2 . TRP D 112 ? 0.273 0.443 0.362 0.071  -0.020 -0.087 112 TRP DDD CE2 
12017 C CE3 . TRP D 112 ? 0.275 0.452 0.357 0.073  -0.022 -0.074 112 TRP DDD CE3 
12018 C CZ2 . TRP D 112 ? 0.290 0.462 0.368 0.074  -0.021 -0.087 112 TRP DDD CZ2 
12019 C CZ3 . TRP D 112 ? 0.263 0.442 0.333 0.076  -0.023 -0.074 112 TRP DDD CZ3 
12020 C CH2 . TRP D 112 ? 0.273 0.450 0.342 0.076  -0.023 -0.081 112 TRP DDD CH2 
12021 N N   . GLY D 113 ? 0.293 0.446 0.417 0.056  -0.005 -0.091 113 GLY DDD N   
12022 C CA  . GLY D 113 ? 0.300 0.446 0.425 0.051  0.000  -0.099 113 GLY DDD CA  
12023 C C   . GLY D 113 ? 0.299 0.439 0.416 0.046  0.006  -0.099 113 GLY DDD C   
12024 O O   . GLY D 113 ? 0.312 0.446 0.423 0.043  0.010  -0.103 113 GLY DDD O   
12025 N N   . LYS D 114 ? 0.297 0.438 0.416 0.046  0.006  -0.095 114 LYS DDD N   
12026 C CA  . LYS D 114 ? 0.302 0.438 0.413 0.042  0.011  -0.094 114 LYS DDD CA  
12027 C C   . LYS D 114 ? 0.304 0.439 0.399 0.043  0.010  -0.091 114 LYS DDD C   
12028 O O   . LYS D 114 ? 0.313 0.442 0.399 0.038  0.014  -0.093 114 LYS DDD O   
12029 C CB  . LYS D 114 ? 0.295 0.433 0.413 0.042  0.010  -0.090 114 LYS DDD CB  
12030 C CG  . LYS D 114 ? 0.282 0.416 0.395 0.038  0.015  -0.091 114 LYS DDD CG  
12031 C CD  . LYS D 114 ? 0.288 0.416 0.398 0.032  0.021  -0.098 114 LYS DDD CD  
12032 C CE  . LYS D 114 ? 0.293 0.418 0.403 0.028  0.025  -0.099 114 LYS DDD CE  
12033 N NZ  . LYS D 114 ? 0.306 0.426 0.408 0.022  0.030  -0.105 114 LYS DDD NZ  
12034 N N   . LEU D 115 ? 0.305 0.445 0.395 0.048  0.005  -0.085 115 LEU DDD N   
12035 C CA  . LEU D 115 ? 0.283 0.422 0.358 0.049  0.004  -0.082 115 LEU DDD CA  
12036 C C   . LEU D 115 ? 0.293 0.429 0.362 0.048  0.005  -0.087 115 LEU DDD C   
12037 O O   . LEU D 115 ? 0.289 0.420 0.349 0.046  0.006  -0.087 115 LEU DDD O   
12038 C CB  . LEU D 115 ? 0.269 0.416 0.343 0.055  -0.002 -0.076 115 LEU DDD CB  
12039 C CG  . LEU D 115 ? 0.255 0.404 0.316 0.057  -0.004 -0.074 115 LEU DDD CG  
12040 C CD1 . LEU D 115 ? 0.255 0.400 0.307 0.055  -0.001 -0.071 115 LEU DDD CD1 
12041 C CD2 . LEU D 115 ? 0.254 0.412 0.315 0.063  -0.009 -0.069 115 LEU DDD CD2 
12042 N N   . VAL D 116 ? 0.317 0.456 0.394 0.050  0.003  -0.090 116 VAL DDD N   
12043 C CA  . VAL D 116 ? 0.317 0.453 0.393 0.049  0.004  -0.095 116 VAL DDD CA  
12044 C C   . VAL D 116 ? 0.298 0.425 0.372 0.043  0.010  -0.099 116 VAL DDD C   
12045 O O   . VAL D 116 ? 0.295 0.418 0.360 0.041  0.011  -0.099 116 VAL DDD O   
12046 C CB  . VAL D 116 ? 0.315 0.455 0.403 0.052  0.001  -0.099 116 VAL DDD CB  
12047 C CG1 . VAL D 116 ? 0.332 0.467 0.421 0.049  0.004  -0.106 116 VAL DDD CG1 
12048 C CG2 . VAL D 116 ? 0.333 0.480 0.418 0.058  -0.005 -0.096 116 VAL DDD CG2 
12049 N N   . GLU D 117 ? 0.305 0.431 0.387 0.039  0.013  -0.101 117 GLU DDD N   
12050 C CA  . GLU D 117 ? 0.342 0.462 0.422 0.033  0.020  -0.105 117 GLU DDD CA  
12051 C C   . GLU D 117 ? 0.312 0.428 0.378 0.031  0.021  -0.101 117 GLU DDD C   
12052 O O   . GLU D 117 ? 0.319 0.429 0.377 0.027  0.024  -0.103 117 GLU DDD O   
12053 C CB  . GLU D 117 ? 0.360 0.480 0.454 0.030  0.023  -0.109 117 GLU DDD CB  
12054 C CG  . GLU D 117 ? 0.398 0.514 0.491 0.023  0.030  -0.113 117 GLU DDD CG  
12055 C CD  . GLU D 117 ? 0.446 0.563 0.548 0.021  0.033  -0.115 117 GLU DDD CD  
12056 O OE1 . GLU D 117 ? 0.487 0.602 0.582 0.018  0.035  -0.113 117 GLU DDD OE1 
12057 O OE2 . GLU D 117 ? 0.489 0.609 0.606 0.022  0.032  -0.119 117 GLU DDD OE2 
12058 N N   . THR D 118 ? 0.322 0.440 0.384 0.033  0.019  -0.096 118 THR DDD N   
12059 C CA  . THR D 118 ? 0.341 0.456 0.391 0.032  0.019  -0.092 118 THR DDD CA  
12060 C C   . THR D 118 ? 0.353 0.465 0.392 0.033  0.016  -0.091 118 THR DDD C   
12061 O O   . THR D 118 ? 0.387 0.494 0.417 0.030  0.018  -0.090 118 THR DDD O   
12062 C CB  . THR D 118 ? 0.331 0.450 0.381 0.034  0.017  -0.087 118 THR DDD CB  
12063 O OG1 . THR D 118 ? 0.305 0.423 0.363 0.031  0.020  -0.089 118 THR DDD OG1 
12064 C CG2 . THR D 118 ? 0.330 0.446 0.367 0.034  0.015  -0.083 118 THR DDD CG2 
12065 N N   . LEU D 119 ? 0.380 0.498 0.422 0.038  0.012  -0.090 119 LEU DDD N   
12066 C CA  . LEU D 119 ? 0.405 0.522 0.440 0.040  0.009  -0.090 119 LEU DDD CA  
12067 C C   . LEU D 119 ? 0.413 0.523 0.448 0.036  0.012  -0.094 119 LEU DDD C   
12068 O O   . LEU D 119 ? 0.347 0.451 0.372 0.034  0.013  -0.093 119 LEU DDD O   
12069 C CB  . LEU D 119 ? 0.423 0.546 0.462 0.046  0.004  -0.090 119 LEU DDD CB  
12070 C CG  . LEU D 119 ? 0.451 0.581 0.485 0.051  0.000  -0.085 119 LEU DDD CG  
12071 C CD1 . LEU D 119 ? 0.474 0.606 0.511 0.051  0.001  -0.081 119 LEU DDD CD1 
12072 C CD2 . LEU D 119 ? 0.442 0.580 0.480 0.057  -0.004 -0.086 119 LEU DDD CD2 
12073 N N   . ARG D 120 ? 0.433 0.544 0.478 0.035  0.014  -0.099 120 ARG DDD N   
12074 C CA  . ARG D 120 ? 0.468 0.573 0.514 0.031  0.018  -0.104 120 ARG DDD CA  
12075 C C   . ARG D 120 ? 0.451 0.549 0.489 0.024  0.022  -0.103 120 ARG DDD C   
12076 O O   . ARG D 120 ? 0.423 0.516 0.455 0.022  0.023  -0.103 120 ARG DDD O   
12077 C CB  . ARG D 120 ? 0.573 0.681 0.634 0.030  0.020  -0.109 120 ARG DDD CB  
12078 C CG  . ARG D 120 ? 0.697 0.809 0.765 0.035  0.016  -0.112 120 ARG DDD CG  
12079 C CD  . ARG D 120 ? 0.834 0.947 0.916 0.033  0.018  -0.118 120 ARG DDD CD  
12080 N NE  . ARG D 120 ? 0.898 1.017 0.990 0.036  0.017  -0.118 120 ARG DDD NE  
12081 C CZ  . ARG D 120 ? 0.938 1.057 1.036 0.033  0.020  -0.119 120 ARG DDD CZ  
12082 N NH1 . ARG D 120 ? 0.975 1.088 1.067 0.027  0.026  -0.120 120 ARG DDD NH1 
12083 N NH2 . ARG D 120 ? 0.882 1.006 0.991 0.036  0.018  -0.119 120 ARG DDD NH2 
12084 N N   . ASN D 121 ? 0.450 0.548 0.488 0.022  0.026  -0.102 121 ASN DDD N   
12085 C CA  . ASN D 121 ? 0.477 0.569 0.507 0.015  0.031  -0.102 121 ASN DDD CA  
12086 C C   . ASN D 121 ? 0.430 0.518 0.446 0.015  0.028  -0.097 121 ASN DDD C   
12087 O O   . ASN D 121 ? 0.450 0.533 0.459 0.011  0.030  -0.097 121 ASN DDD O   
12088 C CB  . ASN D 121 ? 0.533 0.627 0.566 0.013  0.034  -0.103 121 ASN DDD CB  
12089 C CG  . ASN D 121 ? 0.574 0.671 0.621 0.012  0.037  -0.109 121 ASN DDD CG  
12090 O OD1 . ASN D 121 ? 0.652 0.750 0.707 0.012  0.037  -0.112 121 ASN DDD OD1 
12091 N ND2 . ASN D 121 ? 0.615 0.714 0.667 0.010  0.039  -0.110 121 ASN DDD ND2 
12092 N N   . HIS D 122 ? 0.380 0.472 0.394 0.020  0.023  -0.093 122 HIS DDD N   
12093 C CA  . HIS D 122 ? 0.393 0.482 0.395 0.021  0.020  -0.088 122 HIS DDD CA  
12094 C C   . HIS D 122 ? 0.379 0.465 0.379 0.022  0.018  -0.089 122 HIS DDD C   
12095 O O   . HIS D 122 ? 0.375 0.454 0.366 0.018  0.018  -0.087 122 HIS DDD O   
12096 C CB  . HIS D 122 ? 0.393 0.487 0.394 0.026  0.016  -0.085 122 HIS DDD CB  
12097 C CG  . HIS D 122 ? 0.416 0.506 0.406 0.026  0.014  -0.081 122 HIS DDD CG  
12098 N ND1 . HIS D 122 ? 0.427 0.514 0.410 0.022  0.015  -0.079 122 HIS DDD ND1 
12099 C CD2 . HIS D 122 ? 0.450 0.540 0.436 0.029  0.009  -0.079 122 HIS DDD CD2 
12100 C CE1 . HIS D 122 ? 0.492 0.576 0.467 0.023  0.012  -0.075 122 HIS DDD CE1 
12101 N NE2 . HIS D 122 ? 0.490 0.575 0.467 0.027  0.008  -0.075 122 HIS DDD NE2 
12102 N N   . ILE D 123 ? 0.389 0.479 0.397 0.026  0.015  -0.091 123 ILE DDD N   
12103 C CA  . ILE D 123 ? 0.410 0.497 0.418 0.027  0.013  -0.092 123 ILE DDD CA  
12104 C C   . ILE D 123 ? 0.415 0.495 0.423 0.021  0.017  -0.094 123 ILE DDD C   
12105 O O   . ILE D 123 ? 0.394 0.469 0.397 0.019  0.016  -0.093 123 ILE DDD O   
12106 C CB  . ILE D 123 ? 0.412 0.507 0.430 0.033  0.009  -0.095 123 ILE DDD CB  
12107 C CG1 . ILE D 123 ? 0.414 0.515 0.429 0.039  0.005  -0.092 123 ILE DDD CG1 
12108 C CG2 . ILE D 123 ? 0.397 0.489 0.418 0.033  0.008  -0.098 123 ILE DDD CG2 
12109 C CD1 . ILE D 123 ? 0.413 0.522 0.436 0.044  0.002  -0.094 123 ILE DDD CD1 
12110 N N   . ARG D 124 ? 0.442 0.522 0.455 0.017  0.022  -0.098 124 ARG DDD N   
12111 C CA  . ARG D 124 ? 0.485 0.560 0.498 0.010  0.028  -0.100 124 ARG DDD CA  
12112 C C   . ARG D 124 ? 0.508 0.575 0.507 0.005  0.029  -0.095 124 ARG DDD C   
12113 O O   . ARG D 124 ? 0.510 0.572 0.505 0.002  0.029  -0.094 124 ARG DDD O   
12114 C CB  . ARG D 124 ? 0.506 0.583 0.527 0.007  0.033  -0.104 124 ARG DDD CB  
12115 C CG  . ARG D 124 ? 0.552 0.625 0.578 0.002  0.038  -0.108 124 ARG DDD CG  
12116 C CD  . ARG D 124 ? 0.600 0.677 0.636 -0.001 0.043  -0.114 124 ARG DDD CD  
12117 N NE  . ARG D 124 ? 0.617 0.700 0.665 0.005  0.040  -0.117 124 ARG DDD NE  
12118 C CZ  . ARG D 124 ? 0.613 0.701 0.664 0.007  0.040  -0.117 124 ARG DDD CZ  
12119 N NH1 . ARG D 124 ? 0.607 0.693 0.651 0.003  0.044  -0.116 124 ARG DDD NH1 
12120 N NH2 . ARG D 124 ? 0.583 0.677 0.645 0.012  0.037  -0.118 124 ARG DDD NH2 
12121 N N   . MET D 125 ? 0.516 0.585 0.509 0.005  0.029  -0.093 125 MET DDD N   
12122 C CA  . MET D 125 ? 0.530 0.593 0.509 0.000  0.030  -0.088 125 MET DDD CA  
12123 C C   . MET D 125 ? 0.504 0.563 0.478 0.003  0.024  -0.084 125 MET DDD C   
12124 O O   . MET D 125 ? 0.507 0.559 0.473 -0.002 0.025  -0.082 125 MET DDD O   
12125 C CB  . MET D 125 ? 0.580 0.646 0.556 0.001  0.030  -0.087 125 MET DDD CB  
12126 C CG  . MET D 125 ? 0.663 0.724 0.625 -0.003 0.030  -0.083 125 MET DDD CG  
12127 S SD  . MET D 125 ? 0.795 0.853 0.749 0.002  0.022  -0.077 125 MET DDD SD  
12128 C CE  . MET D 125 ? 0.798 0.865 0.760 0.010  0.018  -0.077 125 MET DDD CE  
12129 N N   . LEU D 126 ? 0.483 0.546 0.462 0.010  0.019  -0.084 126 LEU DDD N   
12130 C CA  . LEU D 126 ? 0.435 0.496 0.411 0.013  0.013  -0.081 126 LEU DDD CA  
12131 C C   . LEU D 126 ? 0.414 0.470 0.394 0.011  0.013  -0.083 126 LEU DDD C   
12132 O O   . LEU D 126 ? 0.404 0.454 0.379 0.010  0.011  -0.079 126 LEU DDD O   
12133 C CB  . LEU D 126 ? 0.435 0.503 0.416 0.021  0.008  -0.082 126 LEU DDD CB  
12134 C CG  . LEU D 126 ? 0.448 0.519 0.423 0.023  0.006  -0.078 126 LEU DDD CG  
12135 C CD1 . LEU D 126 ? 0.468 0.548 0.450 0.030  0.003  -0.079 126 LEU DDD CD1 
12136 C CD2 . LEU D 126 ? 0.434 0.500 0.400 0.022  0.003  -0.074 126 LEU DDD CD2 
12137 N N   . ASN D 127 ? 0.405 0.464 0.395 0.011  0.016  -0.088 127 ASN DDD N   
12138 C CA  . ASN D 127 ? 0.432 0.487 0.427 0.009  0.016  -0.089 127 ASN DDD CA  
12139 C C   . ASN D 127 ? 0.424 0.470 0.410 0.001  0.020  -0.086 127 ASN DDD C   
12140 O O   . ASN D 127 ? 0.423 0.463 0.407 -0.000 0.017  -0.083 127 ASN DDD O   
12141 C CB  . ASN D 127 ? 0.420 0.479 0.428 0.009  0.020  -0.095 127 ASN DDD CB  
12142 C CG  . ASN D 127 ? 0.401 0.469 0.417 0.017  0.016  -0.099 127 ASN DDD CG  
12143 O OD1 . ASN D 127 ? 0.389 0.461 0.412 0.017  0.018  -0.102 127 ASN DDD OD1 
12144 N ND2 . ASN D 127 ? 0.412 0.482 0.429 0.022  0.010  -0.098 127 ASN DDD ND2 
12145 N N   . PHE D 128 ? 0.452 0.498 0.433 -0.004 0.026  -0.086 128 PHE DDD N   
12146 C CA  . PHE D 128 ? 0.492 0.531 0.464 -0.012 0.030  -0.083 128 PHE DDD CA  
12147 C C   . PHE D 128 ? 0.512 0.545 0.471 -0.013 0.026  -0.076 128 PHE DDD C   
12148 O O   . PHE D 128 ? 0.539 0.565 0.493 -0.017 0.025  -0.072 128 PHE DDD O   
12149 C CB  . PHE D 128 ? 0.486 0.527 0.455 -0.017 0.037  -0.086 128 PHE DDD CB  
12150 C CG  . PHE D 128 ? 0.487 0.531 0.469 -0.019 0.042  -0.091 128 PHE DDD CG  
12151 C CD1 . PHE D 128 ? 0.495 0.533 0.478 -0.024 0.045  -0.091 128 PHE DDD CD1 
12152 C CD2 . PHE D 128 ? 0.493 0.543 0.484 -0.017 0.045  -0.097 128 PHE DDD CD2 
12153 C CE1 . PHE D 128 ? 0.502 0.543 0.497 -0.026 0.050  -0.097 128 PHE DDD CE1 
12154 C CE2 . PHE D 128 ? 0.488 0.540 0.491 -0.019 0.049  -0.103 128 PHE DDD CE2 
12155 C CZ  . PHE D 128 ? 0.490 0.538 0.495 -0.023 0.052  -0.103 128 PHE DDD CZ  
12156 N N   . SER D 129 ? 0.503 0.540 0.459 -0.009 0.023  -0.075 129 SER DDD N   
12157 C CA  . SER D 129 ? 0.552 0.584 0.497 -0.008 0.018  -0.069 129 SER DDD CA  
12158 C C   . SER D 129 ? 0.596 0.624 0.544 -0.006 0.012  -0.066 129 SER DDD C   
12159 O O   . SER D 129 ? 0.656 0.677 0.595 -0.010 0.009  -0.061 129 SER DDD O   
12160 C CB  . SER D 129 ? 0.536 0.574 0.480 -0.003 0.015  -0.069 129 SER DDD CB  
12161 O OG  . SER D 129 ? 0.571 0.606 0.506 -0.003 0.011  -0.064 129 SER DDD OG  
12162 N N   . TYR D 130 ? 0.629 0.661 0.588 -0.001 0.009  -0.070 130 TYR DDD N   
12163 C CA  . TYR D 130 ? 0.658 0.687 0.622 0.002  0.003  -0.069 130 TYR DDD CA  
12164 C C   . TYR D 130 ? 0.668 0.689 0.633 -0.004 0.005  -0.067 130 TYR DDD C   
12165 O O   . TYR D 130 ? 0.663 0.678 0.626 -0.005 0.001  -0.063 130 TYR DDD O   
12166 C CB  . TYR D 130 ? 0.675 0.711 0.650 0.010  -0.000 -0.074 130 TYR DDD CB  
12167 C CG  . TYR D 130 ? 0.693 0.735 0.666 0.016  -0.005 -0.073 130 TYR DDD CG  
12168 C CD1 . TYR D 130 ? 0.701 0.739 0.669 0.017  -0.010 -0.069 130 TYR DDD CD1 
12169 C CD2 . TYR D 130 ? 0.715 0.766 0.692 0.020  -0.003 -0.076 130 TYR DDD CD2 
12170 C CE1 . TYR D 130 ? 0.727 0.771 0.693 0.022  -0.013 -0.068 130 TYR DDD CE1 
12171 C CE2 . TYR D 130 ? 0.721 0.777 0.695 0.025  -0.007 -0.075 130 TYR DDD CE2 
12172 C CZ  . TYR D 130 ? 0.728 0.781 0.698 0.026  -0.012 -0.072 130 TYR DDD CZ  
12173 O OH  . TYR D 130 ? 0.785 0.843 0.753 0.031  -0.015 -0.071 130 TYR DDD OH  
12174 N N   . ARG D 131 ? 0.666 0.688 0.635 -0.007 0.012  -0.071 131 ARG DDD N   
12175 C CA  . ARG D 131 ? 0.742 0.757 0.713 -0.014 0.015  -0.069 131 ARG DDD CA  
12176 C C   . ARG D 131 ? 0.751 0.758 0.708 -0.020 0.015  -0.062 131 ARG DDD C   
12177 O O   . ARG D 131 ? 0.784 0.784 0.740 -0.023 0.013  -0.057 131 ARG DDD O   
12178 C CB  . ARG D 131 ? 0.752 0.770 0.727 -0.018 0.023  -0.074 131 ARG DDD CB  
12179 C CG  . ARG D 131 ? 0.758 0.779 0.749 -0.015 0.023  -0.079 131 ARG DDD CG  
12180 C CD  . ARG D 131 ? 0.780 0.806 0.778 -0.017 0.030  -0.085 131 ARG DDD CD  
12181 N NE  . ARG D 131 ? 0.788 0.809 0.780 -0.026 0.037  -0.084 131 ARG DDD NE  
12182 C CZ  . ARG D 131 ? 0.799 0.823 0.798 -0.029 0.044  -0.089 131 ARG DDD CZ  
12183 N NH1 . ARG D 131 ? 0.783 0.815 0.795 -0.024 0.044  -0.096 131 ARG DDD NH1 
12184 N NH2 . ARG D 131 ? 0.808 0.828 0.801 -0.038 0.051  -0.088 131 ARG DDD NH2 
12185 N N   . THR D 132 ? 0.767 0.776 0.713 -0.023 0.018  -0.060 132 THR DDD N   
12186 C CA  . THR D 132 ? 0.811 0.814 0.741 -0.029 0.019  -0.054 132 THR DDD CA  
12187 C C   . THR D 132 ? 0.820 0.817 0.746 -0.026 0.010  -0.048 132 THR DDD C   
12188 O O   . THR D 132 ? 0.918 0.908 0.838 -0.031 0.008  -0.042 132 THR DDD O   
12189 C CB  . THR D 132 ? 0.842 0.848 0.763 -0.032 0.023  -0.055 132 THR DDD CB  
12190 O OG1 . THR D 132 ? 0.916 0.926 0.842 -0.036 0.031  -0.060 132 THR DDD OG1 
12191 C CG2 . THR D 132 ? 0.810 0.811 0.715 -0.038 0.023  -0.049 132 THR DDD CG2 
12192 N N   . GLY D 133 ? 0.787 0.790 0.718 -0.018 0.005  -0.050 133 GLY DDD N   
12193 C CA  . GLY D 133 ? 0.800 0.799 0.729 -0.014 -0.003 -0.046 133 GLY DDD CA  
12194 C C   . GLY D 133 ? 0.834 0.827 0.770 -0.015 -0.008 -0.043 133 GLY DDD C   
12195 O O   . GLY D 133 ? 0.793 0.779 0.723 -0.016 -0.013 -0.037 133 GLY DDD O   
12196 N N   . LEU D 134 ? 0.830 0.825 0.778 -0.013 -0.006 -0.048 134 LEU DDD N   
12197 C CA  . LEU D 134 ? 0.815 0.804 0.773 -0.014 -0.009 -0.047 134 LEU DDD CA  
12198 C C   . LEU D 134 ? 0.869 0.849 0.819 -0.023 -0.006 -0.040 134 LEU DDD C   
12199 O O   . LEU D 134 ? 0.919 0.891 0.868 -0.024 -0.011 -0.034 134 LEU DDD O   
12200 C CB  . LEU D 134 ? 0.782 0.777 0.754 -0.010 -0.007 -0.054 134 LEU DDD CB  
12201 C CG  . LEU D 134 ? 0.761 0.764 0.744 -0.001 -0.012 -0.060 134 LEU DDD CG  
12202 C CD1 . LEU D 134 ? 0.757 0.765 0.754 0.001  -0.010 -0.067 134 LEU DDD CD1 
12203 C CD2 . LEU D 134 ? 0.742 0.742 0.728 0.003  -0.020 -0.058 134 LEU DDD CD2 
12204 N N   . ARG D 135 ? 0.921 0.902 0.866 -0.029 0.002  -0.041 135 ARG DDD N   
12205 C CA  . ARG D 135 ? 1.005 0.979 0.942 -0.038 0.006  -0.035 135 ARG DDD CA  
12206 C C   . ARG D 135 ? 1.007 0.974 0.928 -0.042 0.003  -0.027 135 ARG DDD C   
12207 O O   . ARG D 135 ? 0.955 0.914 0.874 -0.046 -0.001 -0.019 135 ARG DDD O   
12208 C CB  . ARG D 135 ? 1.050 1.027 0.984 -0.043 0.016  -0.039 135 ARG DDD CB  
12209 C CG  . ARG D 135 ? 1.115 1.086 1.047 -0.052 0.022  -0.036 135 ARG DDD CG  
12210 C CD  . ARG D 135 ? 1.139 1.116 1.073 -0.057 0.032  -0.041 135 ARG DDD CD  
12211 N NE  . ARG D 135 ? 1.157 1.138 1.078 -0.058 0.035  -0.042 135 ARG DDD NE  
12212 C CZ  . ARG D 135 ? 1.159 1.149 1.085 -0.053 0.037  -0.050 135 ARG DDD CZ  
12213 N NH1 . ARG D 135 ? 1.150 1.145 1.091 -0.047 0.035  -0.056 135 ARG DDD NH1 
12214 N NH2 . ARG D 135 ? 1.171 1.165 1.086 -0.055 0.040  -0.050 135 ARG DDD NH2 
12215 N N   . VAL D 136 ? 0.951 0.922 0.862 -0.040 0.003  -0.027 136 VAL DDD N   
12216 C CA  . VAL D 136 ? 0.941 0.908 0.837 -0.043 -0.001 -0.020 136 VAL DDD CA  
12217 C C   . VAL D 136 ? 0.965 0.927 0.867 -0.038 -0.011 -0.016 136 VAL DDD C   
12218 O O   . VAL D 136 ? 0.989 0.943 0.882 -0.043 -0.015 -0.007 136 VAL DDD O   
12219 C CB  . VAL D 136 ? 0.936 0.910 0.825 -0.041 0.000  -0.023 136 VAL DDD CB  
12220 C CG1 . VAL D 136 ? 0.907 0.878 0.786 -0.040 -0.007 -0.017 136 VAL DDD CG1 
12221 C CG2 . VAL D 136 ? 0.920 0.896 0.800 -0.047 0.009  -0.026 136 VAL DDD CG2 
12222 N N   . GLY D 137 ? 0.957 0.923 0.873 -0.030 -0.016 -0.021 137 GLY DDD N   
12223 C CA  . GLY D 137 ? 0.930 0.893 0.853 -0.025 -0.025 -0.019 137 GLY DDD CA  
12224 C C   . GLY D 137 ? 0.915 0.871 0.849 -0.027 -0.028 -0.016 137 GLY DDD C   
12225 O O   . GLY D 137 ? 0.850 0.802 0.792 -0.022 -0.036 -0.015 137 GLY DDD O   
12226 N N   . ASN D 138 ? 0.974 0.926 0.906 -0.033 -0.022 -0.015 138 ASN DDD N   
12227 C CA  . ASN D 138 ? 0.951 0.895 0.891 -0.037 -0.023 -0.010 138 ASN DDD CA  
12228 C C   . ASN D 138 ? 0.896 0.843 0.856 -0.030 -0.026 -0.018 138 ASN DDD C   
12229 O O   . ASN D 138 ? 0.866 0.807 0.836 -0.030 -0.032 -0.014 138 ASN DDD O   
12230 C CB  . ASN D 138 ? 0.981 0.915 0.913 -0.041 -0.029 0.000  138 ASN DDD CB  
12231 C CG  . ASN D 138 ? 0.986 0.912 0.925 -0.047 -0.029 0.006  138 ASN DDD CG  
12232 O OD1 . ASN D 138 ? 0.937 0.863 0.876 -0.052 -0.021 0.005  138 ASN DDD OD1 
12233 N ND2 . ASN D 138 ? 0.971 0.889 0.916 -0.046 -0.038 0.012  138 ASN DDD ND2 
12234 N N   . VAL D 139 ? 0.921 0.878 0.888 -0.026 -0.022 -0.027 139 VAL DDD N   
12235 C CA  . VAL D 139 ? 0.862 0.824 0.848 -0.019 -0.024 -0.035 139 VAL DDD CA  
12236 C C   . VAL D 139 ? 0.857 0.821 0.848 -0.023 -0.016 -0.039 139 VAL DDD C   
12237 O O   . VAL D 139 ? 0.837 0.805 0.818 -0.026 -0.009 -0.040 139 VAL DDD O   
12238 C CB  . VAL D 139 ? 0.840 0.812 0.830 -0.010 -0.026 -0.042 139 VAL DDD CB  
12239 C CG1 . VAL D 139 ? 0.832 0.810 0.840 -0.004 -0.028 -0.051 139 VAL DDD CG1 
12240 C CG2 . VAL D 139 ? 0.847 0.819 0.832 -0.007 -0.033 -0.039 139 VAL DDD CG2 
12241 N N   . GLU D 140 ? 0.839 0.800 0.845 -0.024 -0.017 -0.040 140 GLU DDD N   
12242 C CA  . GLU D 140 ? 0.874 0.837 0.888 -0.027 -0.010 -0.045 140 GLU DDD CA  
12243 C C   . GLU D 140 ? 0.846 0.819 0.871 -0.019 -0.009 -0.055 140 GLU DDD C   
12244 O O   . GLU D 140 ? 0.801 0.777 0.840 -0.013 -0.015 -0.060 140 GLU DDD O   
12245 C CB  . GLU D 140 ? 0.924 0.878 0.949 -0.030 -0.012 -0.041 140 GLU DDD CB  
12246 C CG  . GLU D 140 ? 0.943 0.898 0.975 -0.036 -0.004 -0.044 140 GLU DDD CG  
12247 C CD  . GLU D 140 ? 0.964 0.908 1.002 -0.042 -0.005 -0.037 140 GLU DDD CD  
12248 O OE1 . GLU D 140 ? 0.921 0.862 0.972 -0.037 -0.013 -0.037 140 GLU DDD OE1 
12249 O OE2 . GLU D 140 ? 0.964 0.903 0.993 -0.051 0.001  -0.030 140 GLU DDD OE2 
12250 N N   . TYR D 141 ? 0.848 0.828 0.867 -0.020 -0.003 -0.059 141 TYR DDD N   
12251 C CA  . TYR D 141 ? 0.805 0.796 0.833 -0.013 -0.002 -0.069 141 TYR DDD CA  
12252 C C   . TYR D 141 ? 0.776 0.767 0.816 -0.015 0.003  -0.074 141 TYR DDD C   
12253 O O   . TYR D 141 ? 0.765 0.753 0.801 -0.023 0.009  -0.071 141 TYR DDD O   
12254 C CB  . TYR D 141 ? 0.811 0.808 0.827 -0.013 0.003  -0.070 141 TYR DDD CB  
12255 C CG  . TYR D 141 ? 0.793 0.799 0.816 -0.008 0.005  -0.078 141 TYR DDD CG  
12256 C CD1 . TYR D 141 ? 0.766 0.779 0.802 -0.000 -0.000 -0.084 141 TYR DDD CD1 
12257 C CD2 . TYR D 141 ? 0.735 0.745 0.755 -0.012 0.012  -0.081 141 TYR DDD CD2 
12258 C CE1 . TYR D 141 ? 0.711 0.733 0.753 0.004  0.001  -0.092 141 TYR DDD CE1 
12259 C CE2 . TYR D 141 ? 0.701 0.720 0.729 -0.007 0.014  -0.088 141 TYR DDD CE2 
12260 C CZ  . TYR D 141 ? 0.697 0.722 0.736 0.001  0.008  -0.093 141 TYR DDD CZ  
12261 O OH  . TYR D 141 ? 0.626 0.660 0.673 0.005  0.009  -0.100 141 TYR DDD OH  
12262 N N   . ILE D 142 ? 0.796 0.793 0.852 -0.009 -0.001 -0.081 142 ILE DDD N   
12263 C CA  . ILE D 142 ? 0.768 0.767 0.839 -0.010 0.003  -0.088 142 ILE DDD CA  
12264 C C   . ILE D 142 ? 0.736 0.746 0.813 -0.002 0.002  -0.097 142 ILE DDD C   
12265 O O   . ILE D 142 ? 0.701 0.716 0.783 0.005  -0.005 -0.100 142 ILE DDD O   
12266 C CB  . ILE D 142 ? 0.826 0.820 0.912 -0.009 -0.002 -0.088 142 ILE DDD CB  
12267 C CG1 . ILE D 142 ? 0.834 0.816 0.912 -0.017 -0.002 -0.078 142 ILE DDD CG1 
12268 C CG2 . ILE D 142 ? 0.821 0.818 0.923 -0.009 0.001  -0.096 142 ILE DDD CG2 
12269 C CD1 . ILE D 142 ? 0.835 0.811 0.927 -0.016 -0.008 -0.077 142 ILE DDD CD1 
12270 N N   . ASN D 143 ? 0.672 0.687 0.750 -0.004 0.008  -0.101 143 ASN DDD N   
12271 C CA  . ASN D 143 ? 0.639 0.664 0.723 0.002  0.008  -0.108 143 ASN DDD CA  
12272 C C   . ASN D 143 ? 0.625 0.653 0.728 0.005  0.006  -0.116 143 ASN DDD C   
12273 O O   . ASN D 143 ? 0.620 0.649 0.730 0.002  0.012  -0.120 143 ASN DDD O   
12274 C CB  . ASN D 143 ? 0.637 0.665 0.714 -0.002 0.015  -0.109 143 ASN DDD CB  
12275 C CG  . ASN D 143 ? 0.604 0.643 0.686 0.005  0.014  -0.115 143 ASN DDD CG  
12276 O OD1 . ASN D 143 ? 0.585 0.630 0.670 0.012  0.008  -0.118 143 ASN DDD OD1 
12277 N ND2 . ASN D 143 ? 0.592 0.633 0.673 0.001  0.021  -0.117 143 ASN DDD ND2 
12278 N N   . ALA D 144 ? 0.613 0.642 0.724 0.010  -0.001 -0.118 144 ALA DDD N   
12279 C CA  . ALA D 144 ? 0.609 0.642 0.738 0.014  -0.004 -0.126 144 ALA DDD CA  
12280 C C   . ALA D 144 ? 0.646 0.684 0.780 0.023  -0.013 -0.130 144 ALA DDD C   
12281 O O   . ALA D 144 ? 0.651 0.687 0.775 0.024  -0.016 -0.125 144 ALA DDD O   
12282 C CB  . ALA D 144 ? 0.629 0.653 0.768 0.008  -0.002 -0.124 144 ALA DDD CB  
12283 N N   . LEU D 145 ? 0.655 0.701 0.802 0.028  -0.016 -0.139 145 LEU DDD N   
12284 C CA  . LEU D 145 ? 0.671 0.723 0.825 0.036  -0.024 -0.145 145 LEU DDD CA  
12285 C C   . LEU D 145 ? 0.692 0.736 0.856 0.035  -0.027 -0.144 145 LEU DDD C   
12286 O O   . LEU D 145 ? 0.685 0.724 0.861 0.030  -0.025 -0.144 145 LEU DDD O   
12287 C CB  . LEU D 145 ? 0.687 0.750 0.854 0.042  -0.026 -0.155 145 LEU DDD CB  
12288 C CG  . LEU D 145 ? 0.684 0.757 0.843 0.046  -0.025 -0.157 145 LEU DDD CG  
12289 C CD1 . LEU D 145 ? 0.710 0.792 0.881 0.051  -0.027 -0.167 145 LEU DDD CD1 
12290 C CD2 . LEU D 145 ? 0.677 0.755 0.824 0.050  -0.029 -0.155 145 LEU DDD CD2 
12291 N N   . ALA D 146 ? 0.724 0.768 0.885 0.038  -0.033 -0.142 146 ALA DDD N   
12292 C CA  . ALA D 146 ? 0.742 0.779 0.913 0.038  -0.038 -0.141 146 ALA DDD CA  
12293 C C   . ALA D 146 ? 0.801 0.847 0.985 0.046  -0.045 -0.151 146 ALA DDD C   
12294 O O   . ALA D 146 ? 0.794 0.851 0.973 0.052  -0.046 -0.156 146 ALA DDD O   
12295 C CB  . ALA D 146 ? 0.748 0.778 0.906 0.035  -0.039 -0.131 146 ALA DDD CB  
12296 N N   . LYS D 147 ? 0.826 0.868 1.028 0.046  -0.049 -0.154 147 LYS DDD N   
12297 C CA  . LYS D 147 ? 0.863 0.913 1.078 0.054  -0.057 -0.164 147 LYS DDD CA  
12298 C C   . LYS D 147 ? 0.879 0.920 1.104 0.053  -0.062 -0.161 147 LYS DDD C   
12299 O O   . LYS D 147 ? 0.868 0.896 1.093 0.046  -0.059 -0.152 147 LYS DDD O   
12300 C CB  . LYS D 147 ? 0.873 0.931 1.103 0.057  -0.057 -0.175 147 LYS DDD CB  
12301 C CG  . LYS D 147 ? 0.930 0.980 1.175 0.052  -0.055 -0.175 147 LYS DDD CG  
12302 C CD  . LYS D 147 ? 0.937 0.994 1.203 0.057  -0.059 -0.187 147 LYS DDD CD  
12303 C CE  . LYS D 147 ? 0.916 0.980 1.184 0.058  -0.055 -0.193 147 LYS DDD CE  
12304 N NZ  . LYS D 147 ? 0.884 0.958 1.170 0.064  -0.061 -0.206 147 LYS DDD NZ  
12305 N N   . LEU D 148 ? 0.918 0.965 1.152 0.059  -0.069 -0.168 148 LEU DDD N   
12306 C CA  . LEU D 148 ? 0.967 1.007 1.214 0.059  -0.075 -0.167 148 LEU DDD CA  
12307 C C   . LEU D 148 ? 1.020 1.057 1.290 0.059  -0.077 -0.173 148 LEU DDD C   
12308 O O   . LEU D 148 ? 1.089 1.136 1.368 0.063  -0.077 -0.184 148 LEU DDD O   
12309 C CB  . LEU D 148 ? 0.927 0.976 1.175 0.067  -0.081 -0.173 148 LEU DDD CB  
12310 C CG  . LEU D 148 ? 0.930 0.981 1.158 0.068  -0.079 -0.167 148 LEU DDD CG  
12311 C CD1 . LEU D 148 ? 0.955 1.018 1.186 0.075  -0.085 -0.175 148 LEU DDD CD1 
12312 C CD2 . LEU D 148 ? 0.935 0.973 1.154 0.061  -0.079 -0.154 148 LEU DDD CD2 
12313 N N   . ILE D 149 ? 1.092 1.115 1.370 0.053  -0.078 -0.166 149 ILE DDD N   
12314 C CA  . ILE D 149 ? 1.196 1.216 1.499 0.052  -0.081 -0.171 149 ILE DDD CA  
12315 C C   . ILE D 149 ? 1.172 1.192 1.490 0.057  -0.089 -0.175 149 ILE DDD C   
12316 O O   . ILE D 149 ? 1.215 1.240 1.552 0.062  -0.094 -0.187 149 ILE DDD O   
12317 C CB  . ILE D 149 ? 1.266 1.271 1.569 0.043  -0.076 -0.160 149 ILE DDD CB  
12318 C CG1 . ILE D 149 ? 1.243 1.250 1.536 0.039  -0.067 -0.160 149 ILE DDD CG1 
12319 C CG2 . ILE D 149 ? 1.306 1.304 1.633 0.041  -0.080 -0.162 149 ILE DDD CG2 
12320 C CD1 . ILE D 149 ? 1.228 1.246 1.536 0.044  -0.067 -0.173 149 ILE DDD CD1 
12321 N N   . ASP D 150 ? 1.138 1.151 1.447 0.056  -0.092 -0.167 150 ASP DDD N   
12322 C CA  . ASP D 150 ? 1.115 1.127 1.437 0.060  -0.100 -0.170 150 ASP DDD CA  
12323 C C   . ASP D 150 ? 1.050 1.059 1.354 0.060  -0.102 -0.161 150 ASP DDD C   
12324 O O   . ASP D 150 ? 1.081 1.089 1.364 0.056  -0.096 -0.153 150 ASP DDD O   
12325 C CB  . ASP D 150 ? 1.178 1.178 1.522 0.056  -0.104 -0.168 150 ASP DDD CB  
12326 C CG  . ASP D 150 ? 1.231 1.215 1.567 0.047  -0.102 -0.152 150 ASP DDD CG  
12327 O OD1 . ASP D 150 ? 1.284 1.264 1.602 0.045  -0.101 -0.142 150 ASP DDD OD1 
12328 O OD2 . ASP D 150 ? 1.229 1.204 1.579 0.042  -0.101 -0.149 150 ASP DDD OD2 
12329 N N   . PRO D 151 ? 1.020 1.029 1.334 0.063  -0.109 -0.163 151 PRO DDD N   
12330 C CA  . PRO D 151 ? 0.992 0.999 1.290 0.063  -0.110 -0.156 151 PRO DDD CA  
12331 C C   . PRO D 151 ? 0.955 0.948 1.234 0.055  -0.107 -0.139 151 PRO DDD C   
12332 O O   . PRO D 151 ? 0.916 0.910 1.180 0.055  -0.107 -0.134 151 PRO DDD O   
12333 C CB  . PRO D 151 ? 1.009 1.014 1.326 0.067  -0.120 -0.159 151 PRO DDD CB  
12334 C CG  . PRO D 151 ? 1.014 1.028 1.354 0.073  -0.123 -0.175 151 PRO DDD CG  
12335 C CD  . PRO D 151 ? 1.017 1.028 1.357 0.068  -0.116 -0.173 151 PRO DDD CD  
12336 N N   . HIS D 152 ? 0.998 0.981 1.279 0.048  -0.103 -0.132 152 HIS DDD N   
12337 C CA  . HIS D 152 ? 1.033 1.003 1.296 0.039  -0.099 -0.116 152 HIS DDD CA  
12338 C C   . HIS D 152 ? 1.038 1.006 1.292 0.033  -0.090 -0.113 152 HIS DDD C   
12339 O O   . HIS D 152 ? 1.068 1.025 1.309 0.025  -0.087 -0.100 152 HIS DDD O   
12340 C CB  . HIS D 152 ? 1.020 0.976 1.296 0.035  -0.105 -0.108 152 HIS DDD CB  
12341 C CG  . HIS D 152 ? 1.033 0.989 1.315 0.040  -0.114 -0.109 152 HIS DDD CG  
12342 N ND1 . HIS D 152 ? 1.067 1.022 1.330 0.040  -0.115 -0.102 152 HIS DDD ND1 
12343 C CD2 . HIS D 152 ? 1.024 0.981 1.329 0.045  -0.122 -0.116 152 HIS DDD CD2 
12344 C CE1 . HIS D 152 ? 1.037 0.992 1.312 0.045  -0.123 -0.106 152 HIS DDD CE1 
12345 N NE2 . HIS D 152 ? 1.048 1.005 1.349 0.048  -0.128 -0.114 152 HIS DDD NE2 
12346 N N   . SER D 153 ? 1.021 0.999 1.280 0.036  -0.086 -0.123 153 SER DDD N   
12347 C CA  . SER D 153 ? 1.110 1.086 1.364 0.030  -0.078 -0.121 153 SER DDD CA  
12348 C C   . SER D 153 ? 1.048 1.037 1.292 0.034  -0.073 -0.128 153 SER DDD C   
12349 O O   . SER D 153 ? 1.101 1.101 1.352 0.042  -0.076 -0.139 153 SER DDD O   
12350 C CB  . SER D 153 ? 1.151 1.123 1.428 0.028  -0.079 -0.124 153 SER DDD CB  
12351 O OG  . SER D 153 ? 1.173 1.134 1.462 0.026  -0.085 -0.118 153 SER DDD OG  
12352 N N   . VAL D 154 ? 1.010 0.998 1.238 0.028  -0.065 -0.122 154 VAL DDD N   
12353 C CA  . VAL D 154 ? 0.974 0.972 1.191 0.031  -0.059 -0.128 154 VAL DDD CA  
12354 C C   . VAL D 154 ? 0.929 0.924 1.149 0.025  -0.052 -0.127 154 VAL DDD C   
12355 O O   . VAL D 154 ? 0.901 0.885 1.119 0.017  -0.049 -0.117 154 VAL DDD O   
12356 C CB  . VAL D 154 ? 0.977 0.977 1.172 0.031  -0.057 -0.122 154 VAL DDD CB  
12357 C CG1 . VAL D 154 ? 1.012 1.002 1.192 0.022  -0.051 -0.109 154 VAL DDD CG1 
12358 C CG2 . VAL D 154 ? 1.014 1.027 1.202 0.035  -0.054 -0.129 154 VAL DDD CG2 
12359 N N   . GLU D 155 ? 0.921 0.926 1.145 0.028  -0.049 -0.136 155 GLU DDD N   
12360 C CA  . GLU D 155 ? 0.958 0.961 1.186 0.023  -0.042 -0.137 155 GLU DDD CA  
12361 C C   . GLU D 155 ? 0.930 0.941 1.143 0.023  -0.036 -0.137 155 GLU DDD C   
12362 O O   . GLU D 155 ? 0.965 0.986 1.173 0.030  -0.039 -0.143 155 GLU DDD O   
12363 C CB  . GLU D 155 ? 1.002 1.012 1.253 0.028  -0.046 -0.149 155 GLU DDD CB  
12364 C CG  . GLU D 155 ? 1.055 1.064 1.315 0.023  -0.039 -0.152 155 GLU DDD CG  
12365 C CD  . GLU D 155 ? 1.080 1.094 1.364 0.028  -0.043 -0.163 155 GLU DDD CD  
12366 O OE1 . GLU D 155 ? 1.131 1.157 1.419 0.036  -0.048 -0.173 155 GLU DDD OE1 
12367 O OE2 . GLU D 155 ? 1.063 1.070 1.362 0.023  -0.042 -0.162 155 GLU DDD OE2 
12368 N N   . TYR D 156 ? 0.879 0.884 1.085 0.015  -0.028 -0.132 156 TYR DDD N   
12369 C CA  . TYR D 156 ? 0.845 0.856 1.040 0.014  -0.022 -0.133 156 TYR DDD CA  
12370 C C   . TYR D 156 ? 0.847 0.855 1.050 0.008  -0.015 -0.134 156 TYR DDD C   
12371 O O   . TYR D 156 ? 0.777 0.776 0.987 0.002  -0.013 -0.129 156 TYR DDD O   
12372 C CB  . TYR D 156 ? 0.823 0.832 0.997 0.011  -0.019 -0.124 156 TYR DDD CB  
12373 C CG  . TYR D 156 ? 0.791 0.788 0.956 0.002  -0.014 -0.114 156 TYR DDD CG  
12374 C CD1 . TYR D 156 ? 0.788 0.775 0.953 -0.001 -0.018 -0.107 156 TYR DDD CD1 
12375 C CD2 . TYR D 156 ? 0.790 0.785 0.946 -0.005 -0.005 -0.111 156 TYR DDD CD2 
12376 C CE1 . TYR D 156 ? 0.784 0.761 0.940 -0.010 -0.014 -0.096 156 TYR DDD CE1 
12377 C CE2 . TYR D 156 ? 0.795 0.780 0.942 -0.014 -0.001 -0.101 156 TYR DDD CE2 
12378 C CZ  . TYR D 156 ? 0.790 0.767 0.937 -0.017 -0.005 -0.093 156 TYR DDD CZ  
12379 O OH  . TYR D 156 ? 0.777 0.744 0.914 -0.026 -0.001 -0.083 156 TYR DDD OH  
12380 N N   . GLU D 157 ? 0.878 0.895 1.082 0.010  -0.011 -0.141 157 GLU DDD N   
12381 C CA  . GLU D 157 ? 0.925 0.940 1.134 0.004  -0.003 -0.142 157 GLU DDD CA  
12382 C C   . GLU D 157 ? 0.948 0.959 1.140 -0.004 0.004  -0.134 157 GLU DDD C   
12383 O O   . GLU D 157 ? 0.965 0.977 1.140 -0.002 0.004  -0.130 157 GLU DDD O   
12384 C CB  . GLU D 157 ? 0.931 0.959 1.147 0.010  -0.003 -0.152 157 GLU DDD CB  
12385 C CG  . GLU D 157 ? 0.964 0.995 1.201 0.014  -0.007 -0.162 157 GLU DDD CG  
12386 C CD  . GLU D 157 ? 0.995 1.034 1.241 0.015  -0.004 -0.170 157 GLU DDD CD  
12387 O OE1 . GLU D 157 ? 0.880 0.920 1.116 0.011  0.003  -0.168 157 GLU DDD OE1 
12388 O OE2 . GLU D 157 ? 1.070 1.115 1.333 0.020  -0.008 -0.180 157 GLU DDD OE2 
12389 N N   . ASP D 158 ? 1.005 1.010 1.201 -0.012 0.011  -0.131 158 ASP DDD N   
12390 C CA  . ASP D 158 ? 1.021 1.021 1.201 -0.021 0.020  -0.123 158 ASP DDD CA  
12391 C C   . ASP D 158 ? 0.988 0.987 1.179 -0.027 0.028  -0.127 158 ASP DDD C   
12392 O O   . ASP D 158 ? 0.954 0.947 1.156 -0.031 0.029  -0.124 158 ASP DDD O   
12393 C CB  . ASP D 158 ? 1.051 1.041 1.220 -0.026 0.019  -0.112 158 ASP DDD CB  
12394 C CG  . ASP D 158 ? 1.117 1.101 1.270 -0.035 0.027  -0.104 158 ASP DDD CG  
12395 O OD1 . ASP D 158 ? 1.143 1.132 1.286 -0.036 0.032  -0.105 158 ASP DDD OD1 
12396 O OD2 . ASP D 158 ? 1.149 1.125 1.302 -0.042 0.028  -0.096 158 ASP DDD OD2 
12397 N N   . ASN D 159 ? 1.016 1.022 1.206 -0.027 0.033  -0.132 159 ASN DDD N   
12398 C CA  . ASN D 159 ? 1.103 1.112 1.308 -0.031 0.040  -0.138 159 ASN DDD CA  
12399 C C   . ASN D 159 ? 1.138 1.148 1.365 -0.026 0.034  -0.146 159 ASN DDD C   
12400 O O   . ASN D 159 ? 1.135 1.141 1.376 -0.031 0.038  -0.147 159 ASN DDD O   
12401 C CB  . ASN D 159 ? 1.149 1.149 1.349 -0.042 0.048  -0.131 159 ASN DDD CB  
12402 C CG  . ASN D 159 ? 1.187 1.187 1.367 -0.047 0.055  -0.126 159 ASN DDD CG  
12403 O OD1 . ASN D 159 ? 1.187 1.192 1.367 -0.049 0.061  -0.130 159 ASN DDD OD1 
12404 N ND2 . ASN D 159 ? 1.217 1.211 1.380 -0.050 0.053  -0.116 159 ASN DDD ND2 
12405 N N   . GLY D 160 ? 1.136 1.152 1.366 -0.016 0.025  -0.152 160 GLY DDD N   
12406 C CA  . GLY D 160 ? 1.134 1.155 1.386 -0.010 0.019  -0.160 160 GLY DDD CA  
12407 C C   . GLY D 160 ? 1.157 1.168 1.419 -0.013 0.017  -0.157 160 GLY DDD C   
12408 O O   . GLY D 160 ? 1.082 1.094 1.365 -0.013 0.016  -0.163 160 GLY DDD O   
12409 N N   . GLN D 161 ? 1.188 1.192 1.438 -0.016 0.016  -0.147 161 GLN DDD N   
12410 C CA  . GLN D 161 ? 1.167 1.161 1.425 -0.020 0.013  -0.142 161 GLN DDD CA  
12411 C C   . GLN D 161 ? 1.118 1.111 1.368 -0.015 0.005  -0.138 161 GLN DDD C   
12412 O O   . GLN D 161 ? 1.118 1.107 1.349 -0.018 0.006  -0.129 161 GLN DDD O   
12413 C CB  . GLN D 161 ? 1.231 1.216 1.483 -0.031 0.021  -0.132 161 GLN DDD CB  
12414 C CG  . GLN D 161 ? 1.313 1.299 1.579 -0.036 0.029  -0.136 161 GLN DDD CG  
12415 C CD  . GLN D 161 ? 1.384 1.366 1.635 -0.046 0.040  -0.129 161 GLN DDD CD  
12416 O OE1 . GLN D 161 ? 1.419 1.403 1.650 -0.047 0.042  -0.125 161 GLN DDD OE1 
12417 N NE2 . GLN D 161 ? 1.404 1.382 1.664 -0.054 0.047  -0.128 161 GLN DDD NE2 
12418 N N   . LYS D 162 ? 1.062 1.058 1.327 -0.007 -0.003 -0.145 162 LYS DDD N   
12419 C CA  . LYS D 162 ? 1.011 1.005 1.273 -0.002 -0.012 -0.142 162 LYS DDD CA  
12420 C C   . LYS D 162 ? 0.989 0.972 1.242 -0.009 -0.011 -0.129 162 LYS DDD C   
12421 O O   . LYS D 162 ? 0.931 0.905 1.192 -0.017 -0.007 -0.125 162 LYS DDD O   
12422 C CB  . LYS D 162 ? 1.000 0.997 1.286 0.004  -0.020 -0.151 162 LYS DDD CB  
12423 C CG  . LYS D 162 ? 0.979 0.989 1.276 0.011  -0.022 -0.165 162 LYS DDD CG  
12424 C CD  . LYS D 162 ? 0.954 0.974 1.237 0.018  -0.024 -0.168 162 LYS DDD CD  
12425 C CE  . LYS D 162 ? 0.946 0.977 1.238 0.025  -0.026 -0.180 162 LYS DDD CE  
12426 N NZ  . LYS D 162 ? 0.916 0.958 1.198 0.033  -0.031 -0.184 162 LYS DDD NZ  
12427 N N   . LYS D 163 ? 0.981 0.962 1.217 -0.008 -0.014 -0.123 163 LYS DDD N   
12428 C CA  . LYS D 163 ? 1.023 0.993 1.250 -0.013 -0.016 -0.111 163 LYS DDD CA  
12429 C C   . LYS D 163 ? 1.010 0.981 1.239 -0.005 -0.025 -0.113 163 LYS DDD C   
12430 O O   . LYS D 163 ? 1.081 1.063 1.307 0.002  -0.028 -0.120 163 LYS DDD O   
12431 C CB  . LYS D 163 ? 1.062 1.028 1.265 -0.019 -0.009 -0.102 163 LYS DDD CB  
12432 C CG  . LYS D 163 ? 1.073 1.038 1.274 -0.028 0.001  -0.100 163 LYS DDD CG  
12433 C CD  . LYS D 163 ? 1.086 1.044 1.266 -0.036 0.007  -0.088 163 LYS DDD CD  
12434 C CE  . LYS D 163 ? 1.109 1.065 1.289 -0.046 0.017  -0.086 163 LYS DDD CE  
12435 N NZ  . LYS D 163 ? 1.099 1.048 1.259 -0.054 0.022  -0.075 163 LYS DDD NZ  
12436 N N   . THR D 164 ? 0.982 0.945 1.217 -0.007 -0.030 -0.106 164 THR DDD N   
12437 C CA  . THR D 164 ? 0.942 0.905 1.181 -0.001 -0.040 -0.107 164 THR DDD CA  
12438 C C   . THR D 164 ? 0.939 0.892 1.162 -0.006 -0.041 -0.094 164 THR DDD C   
12439 O O   . THR D 164 ? 0.883 0.826 1.104 -0.015 -0.037 -0.084 164 THR DDD O   
12440 C CB  . THR D 164 ? 0.937 0.899 1.202 0.003  -0.047 -0.114 164 THR DDD CB  
12441 O OG1 . THR D 164 ? 0.875 0.848 1.152 0.008  -0.046 -0.127 164 THR DDD OG1 
12442 C CG2 . THR D 164 ? 0.929 0.891 1.200 0.009  -0.056 -0.116 164 THR DDD CG2 
12443 N N   . ILE D 165 ? 0.960 0.915 1.172 -0.002 -0.046 -0.092 165 ILE DDD N   
12444 C CA  . ILE D 165 ? 0.980 0.926 1.177 -0.006 -0.048 -0.080 165 ILE DDD CA  
12445 C C   . ILE D 165 ? 0.913 0.861 1.118 0.001  -0.058 -0.083 165 ILE DDD C   
12446 O O   . ILE D 165 ? 0.833 0.792 1.046 0.010  -0.061 -0.094 165 ILE DDD O   
12447 C CB  . ILE D 165 ? 1.008 0.956 1.180 -0.009 -0.041 -0.075 165 ILE DDD CB  
12448 C CG1 . ILE D 165 ? 1.015 0.976 1.181 -0.001 -0.043 -0.083 165 ILE DDD CG1 
12449 C CG2 . ILE D 165 ? 1.034 0.981 1.201 -0.016 -0.032 -0.073 165 ILE DDD CG2 
12450 C CD1 . ILE D 165 ? 1.021 0.983 1.163 -0.003 -0.039 -0.077 165 ILE DDD CD1 
12451 N N   . THR D 166 ? 0.889 0.826 1.090 -0.002 -0.063 -0.073 166 THR DDD N   
12452 C CA  . THR D 166 ? 0.933 0.869 1.145 0.004  -0.073 -0.075 166 THR DDD CA  
12453 C C   . THR D 166 ? 0.898 0.834 1.092 0.005  -0.075 -0.068 166 THR DDD C   
12454 O O   . THR D 166 ? 0.930 0.859 1.105 -0.002 -0.071 -0.057 166 THR DDD O   
12455 C CB  . THR D 166 ? 0.953 0.878 1.184 0.000  -0.078 -0.069 166 THR DDD CB  
12456 O OG1 . THR D 166 ? 0.995 0.908 1.210 -0.009 -0.074 -0.054 166 THR DDD OG1 
12457 C CG2 . THR D 166 ? 0.938 0.864 1.191 0.001  -0.077 -0.077 166 THR DDD CG2 
12458 N N   . SER D 167 ? 0.865 0.807 1.064 0.013  -0.082 -0.075 167 SER DDD N   
12459 C CA  . SER D 167 ? 0.926 0.868 1.109 0.015  -0.085 -0.070 167 SER DDD CA  
12460 C C   . SER D 167 ? 0.942 0.884 1.140 0.021  -0.095 -0.073 167 SER DDD C   
12461 O O   . SER D 167 ? 0.912 0.861 1.130 0.027  -0.099 -0.084 167 SER DDD O   
12462 C CB  . SER D 167 ? 0.937 0.891 1.105 0.019  -0.080 -0.076 167 SER DDD CB  
12463 O OG  . SER D 167 ? 0.987 0.938 1.135 0.016  -0.079 -0.067 167 SER DDD OG  
12464 N N   . ARG D 168 ? 0.994 0.929 1.182 0.019  -0.099 -0.064 168 ARG DDD N   
12465 C CA  . ARG D 168 ? 1.018 0.954 1.217 0.025  -0.109 -0.067 168 ARG DDD CA  
12466 C C   . ARG D 168 ? 0.986 0.937 1.186 0.034  -0.109 -0.080 168 ARG DDD C   
12467 O O   . ARG D 168 ? 0.901 0.858 1.120 0.041  -0.114 -0.090 168 ARG DDD O   
12468 C CB  . ARG D 168 ? 1.060 0.987 1.246 0.021  -0.113 -0.055 168 ARG DDD CB  
12469 C CG  . ARG D 168 ? 1.078 1.001 1.276 0.026  -0.123 -0.055 168 ARG DDD CG  
12470 C CD  . ARG D 168 ? 1.107 1.018 1.293 0.020  -0.127 -0.041 168 ARG DDD CD  
12471 N NE  . ARG D 168 ? 1.104 1.014 1.296 0.024  -0.136 -0.040 168 ARG DDD NE  
12472 C CZ  . ARG D 168 ? 1.141 1.045 1.318 0.022  -0.139 -0.031 168 ARG DDD CZ  
12473 N NH1 . ARG D 168 ? 1.119 1.018 1.273 0.015  -0.133 -0.020 168 ARG DDD NH1 
12474 N NH2 . ARG D 168 ? 1.179 1.083 1.365 0.026  -0.148 -0.032 168 ARG DDD NH2 
12475 N N   . TYR D 169 ? 1.001 0.959 1.181 0.034  -0.102 -0.080 169 TYR DDD N   
12476 C CA  . TYR D 169 ? 0.986 0.959 1.163 0.041  -0.101 -0.090 169 TYR DDD CA  
12477 C C   . TYR D 169 ? 0.927 0.907 1.094 0.041  -0.092 -0.094 169 TYR DDD C   
12478 O O   . TYR D 169 ? 0.943 0.918 1.098 0.034  -0.086 -0.087 169 TYR DDD O   
12479 C CB  . TYR D 169 ? 0.982 0.955 1.144 0.042  -0.103 -0.084 169 TYR DDD CB  
12480 C CG  . TYR D 169 ? 0.981 0.946 1.152 0.043  -0.112 -0.081 169 TYR DDD CG  
12481 C CD1 . TYR D 169 ? 0.967 0.938 1.159 0.050  -0.119 -0.091 169 TYR DDD CD1 
12482 C CD2 . TYR D 169 ? 1.026 0.980 1.187 0.038  -0.114 -0.068 169 TYR DDD CD2 
12483 C CE1 . TYR D 169 ? 0.971 0.936 1.174 0.051  -0.127 -0.088 169 TYR DDD CE1 
12484 C CE2 . TYR D 169 ? 1.020 0.967 1.190 0.039  -0.123 -0.065 169 TYR DDD CE2 
12485 C CZ  . TYR D 169 ? 1.000 0.952 1.192 0.046  -0.130 -0.075 169 TYR DDD CZ  
12486 O OH  . TYR D 169 ? 0.936 0.882 1.139 0.047  -0.139 -0.072 169 TYR DDD OH  
12487 N N   . ILE D 170 ? 0.879 0.873 1.052 0.047  -0.092 -0.106 170 ILE DDD N   
12488 C CA  . ILE D 170 ? 0.865 0.869 1.031 0.048  -0.084 -0.110 170 ILE DDD CA  
12489 C C   . ILE D 170 ? 0.833 0.849 0.990 0.054  -0.084 -0.115 170 ILE DDD C   
12490 O O   . ILE D 170 ? 0.873 0.895 1.039 0.060  -0.090 -0.121 170 ILE DDD O   
12491 C CB  . ILE D 170 ? 0.879 0.887 1.062 0.050  -0.084 -0.120 170 ILE DDD CB  
12492 C CG1 . ILE D 170 ? 0.915 0.911 1.107 0.044  -0.083 -0.114 170 ILE DDD CG1 
12493 C CG2 . ILE D 170 ? 0.865 0.883 1.040 0.052  -0.077 -0.125 170 ILE DDD CG2 
12494 C CD1 . ILE D 170 ? 0.946 0.945 1.158 0.046  -0.084 -0.123 170 ILE DDD CD1 
12495 N N   . LEU D 171 ? 0.799 0.818 0.938 0.052  -0.078 -0.112 171 LEU DDD N   
12496 C CA  . LEU D 171 ? 0.769 0.800 0.899 0.057  -0.077 -0.116 171 LEU DDD CA  
12497 C C   . LEU D 171 ? 0.716 0.757 0.844 0.059  -0.071 -0.122 171 LEU DDD C   
12498 O O   . LEU D 171 ? 0.738 0.774 0.859 0.054  -0.066 -0.118 171 LEU DDD O   
12499 C CB  . LEU D 171 ? 0.780 0.807 0.891 0.054  -0.074 -0.106 171 LEU DDD CB  
12500 C CG  . LEU D 171 ? 0.741 0.778 0.841 0.058  -0.072 -0.109 171 LEU DDD CG  
12501 C CD1 . LEU D 171 ? 0.726 0.774 0.835 0.065  -0.077 -0.116 171 LEU DDD CD1 
12502 C CD2 . LEU D 171 ? 0.751 0.784 0.834 0.054  -0.070 -0.099 171 LEU DDD CD2 
12503 N N   . LEU D 172 ? 0.675 0.729 0.810 0.066  -0.073 -0.132 172 LEU DDD N   
12504 C CA  . LEU D 172 ? 0.655 0.720 0.787 0.069  -0.069 -0.138 172 LEU DDD CA  
12505 C C   . LEU D 172 ? 0.622 0.694 0.739 0.071  -0.067 -0.135 172 LEU DDD C   
12506 O O   . LEU D 172 ? 0.544 0.621 0.659 0.075  -0.070 -0.136 172 LEU DDD O   
12507 C CB  . LEU D 172 ? 0.670 0.746 0.818 0.076  -0.074 -0.150 172 LEU DDD CB  
12508 C CG  . LEU D 172 ? 0.695 0.764 0.861 0.075  -0.077 -0.153 172 LEU DDD CG  
12509 C CD1 . LEU D 172 ? 0.710 0.791 0.891 0.082  -0.082 -0.166 172 LEU DDD CD1 
12510 C CD2 . LEU D 172 ? 0.682 0.743 0.850 0.069  -0.073 -0.150 172 LEU DDD CD2 
12511 N N   . ALA D 173 ? 0.614 0.687 0.720 0.068  -0.061 -0.131 173 ALA DDD N   
12512 C CA  . ALA D 173 ? 0.585 0.665 0.678 0.069  -0.058 -0.129 173 ALA DDD CA  
12513 C C   . ALA D 173 ? 0.528 0.612 0.617 0.068  -0.052 -0.130 173 ALA DDD C   
12514 O O   . ALA D 173 ? 0.524 0.604 0.602 0.063  -0.048 -0.124 173 ALA DDD O   
12515 C CB  . ALA D 173 ? 0.609 0.680 0.689 0.064  -0.056 -0.119 173 ALA DDD CB  
12516 N N   . THR D 174 ? 0.522 0.614 0.621 0.072  -0.054 -0.138 174 THR DDD N   
12517 C CA  . THR D 174 ? 0.518 0.614 0.619 0.071  -0.050 -0.141 174 THR DDD CA  
12518 C C   . THR D 174 ? 0.510 0.617 0.602 0.075  -0.048 -0.142 174 THR DDD C   
12519 O O   . THR D 174 ? 0.550 0.660 0.641 0.074  -0.045 -0.143 174 THR DDD O   
12520 C CB  . THR D 174 ? 0.492 0.590 0.608 0.073  -0.052 -0.149 174 THR DDD CB  
12521 O OG1 . THR D 174 ? 0.463 0.570 0.586 0.080  -0.058 -0.157 174 THR DDD OG1 
12522 C CG2 . THR D 174 ? 0.503 0.588 0.627 0.068  -0.052 -0.147 174 THR DDD CG2 
12523 N N   . GLY D 175 ? 0.515 0.628 0.601 0.078  -0.051 -0.142 175 GLY DDD N   
12524 C CA  . GLY D 175 ? 0.491 0.616 0.570 0.082  -0.050 -0.141 175 GLY DDD CA  
12525 C C   . GLY D 175 ? 0.469 0.606 0.554 0.087  -0.052 -0.150 175 GLY DDD C   
12526 O O   . GLY D 175 ? 0.467 0.605 0.564 0.089  -0.054 -0.157 175 GLY DDD O   
12527 N N   . GLY D 176 ? 0.429 0.576 0.507 0.090  -0.050 -0.149 176 GLY DDD N   
12528 C CA  . GLY D 176 ? 0.429 0.588 0.511 0.094  -0.052 -0.155 176 GLY DDD CA  
12529 C C   . GLY D 176 ? 0.424 0.582 0.504 0.092  -0.049 -0.153 176 GLY DDD C   
12530 O O   . GLY D 176 ? 0.422 0.569 0.499 0.086  -0.044 -0.147 176 GLY DDD O   
12531 N N   . ARG D 177 ? 0.430 0.598 0.514 0.096  -0.050 -0.158 177 ARG DDD N   
12532 C CA  . ARG D 177 ? 0.443 0.615 0.525 0.095  -0.048 -0.156 177 ARG DDD CA  
12533 C C   . ARG D 177 ? 0.421 0.607 0.498 0.100  -0.051 -0.158 177 ARG DDD C   
12534 O O   . ARG D 177 ? 0.391 0.587 0.470 0.105  -0.055 -0.163 177 ARG DDD O   
12535 C CB  . ARG D 177 ? 0.455 0.621 0.548 0.093  -0.048 -0.161 177 ARG DDD CB  
12536 C CG  . ARG D 177 ? 0.483 0.634 0.579 0.087  -0.044 -0.158 177 ARG DDD CG  
12537 C CD  . ARG D 177 ? 0.473 0.617 0.559 0.081  -0.039 -0.149 177 ARG DDD CD  
12538 N NE  . ARG D 177 ? 0.491 0.637 0.579 0.080  -0.036 -0.149 177 ARG DDD NE  
12539 C CZ  . ARG D 177 ? 0.498 0.637 0.593 0.077  -0.034 -0.151 177 ARG DDD CZ  
12540 N NH1 . ARG D 177 ? 0.506 0.637 0.608 0.073  -0.033 -0.152 177 ARG DDD NH1 
12541 N NH2 . ARG D 177 ? 0.516 0.658 0.614 0.076  -0.032 -0.151 177 ARG DDD NH2 
12542 N N   . PRO D 178 ? 0.450 0.640 0.523 0.100  -0.049 -0.154 178 PRO DDD N   
12543 C CA  . PRO D 178 ? 0.465 0.668 0.533 0.105  -0.052 -0.154 178 PRO DDD CA  
12544 C C   . PRO D 178 ? 0.499 0.712 0.575 0.109  -0.057 -0.164 178 PRO DDD C   
12545 O O   . PRO D 178 ? 0.464 0.673 0.550 0.108  -0.057 -0.169 178 PRO DDD O   
12546 C CB  . PRO D 178 ? 0.437 0.639 0.503 0.103  -0.050 -0.149 178 PRO DDD CB  
12547 C CG  . PRO D 178 ? 0.431 0.619 0.496 0.097  -0.045 -0.143 178 PRO DDD CG  
12548 C CD  . PRO D 178 ? 0.434 0.614 0.506 0.095  -0.045 -0.148 178 PRO DDD CD  
12549 N N   . SER D 179 ? 0.561 0.788 0.633 0.114  -0.060 -0.167 179 SER DDD N   
12550 C CA  . SER D 179 ? 0.610 0.848 0.688 0.119  -0.065 -0.177 179 SER DDD CA  
12551 C C   . SER D 179 ? 0.603 0.852 0.676 0.122  -0.067 -0.175 179 SER DDD C   
12552 O O   . SER D 179 ? 0.570 0.824 0.632 0.122  -0.066 -0.168 179 SER DDD O   
12553 C CB  . SER D 179 ? 0.630 0.876 0.707 0.123  -0.067 -0.183 179 SER DDD CB  
12554 O OG  . SER D 179 ? 0.759 1.015 0.845 0.127  -0.072 -0.193 179 SER DDD OG  
12555 N N   . ILE D 180 ? 0.620 0.871 0.701 0.123  -0.069 -0.180 180 ILE DDD N   
12556 C CA  . ILE D 180 ? 0.660 0.922 0.740 0.126  -0.073 -0.180 180 ILE DDD CA  
12557 C C   . ILE D 180 ? 0.695 0.970 0.780 0.131  -0.078 -0.191 180 ILE DDD C   
12558 O O   . ILE D 180 ? 0.754 1.025 0.850 0.131  -0.080 -0.200 180 ILE DDD O   
12559 C CB  . ILE D 180 ? 0.667 0.921 0.754 0.123  -0.071 -0.178 180 ILE DDD CB  
12560 C CG1 . ILE D 180 ? 0.669 0.910 0.752 0.117  -0.066 -0.169 180 ILE DDD CG1 
12561 C CG2 . ILE D 180 ? 0.665 0.929 0.750 0.126  -0.076 -0.178 180 ILE DDD CG2 
12562 C CD1 . ILE D 180 ? 0.677 0.910 0.768 0.114  -0.064 -0.167 180 ILE DDD CD1 
12563 N N   . PRO D 181 ? 0.640 0.930 0.715 0.135  -0.081 -0.192 181 PRO DDD N   
12564 C CA  . PRO D 181 ? 0.653 0.956 0.731 0.140  -0.087 -0.202 181 PRO DDD CA  
12565 C C   . PRO D 181 ? 0.649 0.953 0.740 0.141  -0.090 -0.209 181 PRO DDD C   
12566 O O   . PRO D 181 ? 0.576 0.879 0.665 0.141  -0.092 -0.204 181 PRO DDD O   
12567 C CB  . PRO D 181 ? 0.644 0.963 0.709 0.143  -0.089 -0.198 181 PRO DDD CB  
12568 C CG  . PRO D 181 ? 0.663 0.976 0.721 0.139  -0.085 -0.185 181 PRO DDD CG  
12569 C CD  . PRO D 181 ? 0.635 0.930 0.697 0.135  -0.080 -0.181 181 PRO DDD CD  
12570 N N   . GLU D 182 ? 0.713 1.015 0.815 0.142  -0.093 -0.220 182 GLU DDD N   
12571 C CA  . GLU D 182 ? 0.842 1.145 0.958 0.144  -0.096 -0.229 182 GLU DDD CA  
12572 C C   . GLU D 182 ? 0.829 1.149 0.941 0.149  -0.103 -0.234 182 GLU DDD C   
12573 O O   . GLU D 182 ? 0.843 1.164 0.963 0.150  -0.106 -0.237 182 GLU DDD O   
12574 C CB  . GLU D 182 ? 0.918 1.214 1.048 0.143  -0.097 -0.238 182 GLU DDD CB  
12575 C CG  . GLU D 182 ? 0.981 1.259 1.116 0.138  -0.091 -0.233 182 GLU DDD CG  
12576 C CD  . GLU D 182 ? 1.013 1.284 1.152 0.136  -0.089 -0.235 182 GLU DDD CD  
12577 O OE1 . GLU D 182 ? 0.967 1.247 1.104 0.140  -0.091 -0.240 182 GLU DDD OE1 
12578 O OE2 . GLU D 182 ? 1.042 1.297 1.186 0.131  -0.085 -0.231 182 GLU DDD OE2 
12579 N N   . THR D 183 ? 0.802 1.136 0.902 0.152  -0.104 -0.234 183 THR DDD N   
12580 C CA  . THR D 183 ? 0.790 1.142 0.883 0.157  -0.110 -0.238 183 THR DDD CA  
12581 C C   . THR D 183 ? 0.799 1.154 0.884 0.156  -0.111 -0.228 183 THR DDD C   
12582 O O   . THR D 183 ? 0.789 1.154 0.874 0.160  -0.117 -0.233 183 THR DDD O   
12583 C CB  . THR D 183 ? 0.770 1.136 0.853 0.159  -0.109 -0.241 183 THR DDD CB  
12584 O OG1 . THR D 183 ? 0.748 1.110 0.817 0.157  -0.105 -0.229 183 THR DDD OG1 
12585 C CG2 . THR D 183 ? 0.771 1.133 0.864 0.160  -0.109 -0.251 183 THR DDD CG2 
12586 N N   . VAL D 184 ? 0.768 1.114 0.846 0.153  -0.106 -0.216 184 VAL DDD N   
12587 C CA  . VAL D 184 ? 0.726 1.074 0.796 0.152  -0.107 -0.205 184 VAL DDD CA  
12588 C C   . VAL D 184 ? 0.741 1.079 0.824 0.150  -0.108 -0.205 184 VAL DDD C   
12589 O O   . VAL D 184 ? 0.801 1.124 0.892 0.146  -0.103 -0.202 184 VAL DDD O   
12590 C CB  . VAL D 184 ? 0.662 1.006 0.721 0.149  -0.102 -0.192 184 VAL DDD CB  
12591 C CG1 . VAL D 184 ? 0.621 0.964 0.676 0.148  -0.103 -0.181 184 VAL DDD CG1 
12592 C CG2 . VAL D 184 ? 0.645 1.001 0.691 0.151  -0.101 -0.192 184 VAL DDD CG2 
12593 N N   . PRO D 185 ? 0.726 1.072 0.812 0.153  -0.114 -0.208 185 PRO DDD N   
12594 C CA  . PRO D 185 ? 0.678 1.015 0.777 0.151  -0.116 -0.208 185 PRO DDD CA  
12595 C C   . PRO D 185 ? 0.650 0.977 0.749 0.147  -0.112 -0.196 185 PRO DDD C   
12596 O O   . PRO D 185 ? 0.606 0.938 0.693 0.147  -0.112 -0.186 185 PRO DDD O   
12597 C CB  . PRO D 185 ? 0.688 1.039 0.788 0.156  -0.124 -0.212 185 PRO DDD CB  
12598 C CG  . PRO D 185 ? 0.709 1.075 0.798 0.160  -0.127 -0.218 185 PRO DDD CG  
12599 C CD  . PRO D 185 ? 0.712 1.076 0.789 0.158  -0.121 -0.211 185 PRO DDD CD  
12600 N N   . GLY D 186 ? 0.654 0.966 0.765 0.143  -0.108 -0.196 186 GLY DDD N   
12601 C CA  . GLY D 186 ? 0.665 0.965 0.778 0.139  -0.104 -0.187 186 GLY DDD CA  
12602 C C   . GLY D 186 ? 0.653 0.943 0.760 0.135  -0.096 -0.180 186 GLY DDD C   
12603 O O   . GLY D 186 ? 0.650 0.929 0.762 0.130  -0.092 -0.175 186 GLY DDD O   
12604 N N   . ALA D 187 ? 0.637 0.931 0.735 0.136  -0.095 -0.182 187 ALA DDD N   
12605 C CA  . ALA D 187 ? 0.632 0.919 0.723 0.132  -0.088 -0.175 187 ALA DDD CA  
12606 C C   . ALA D 187 ? 0.621 0.891 0.721 0.127  -0.083 -0.176 187 ALA DDD C   
12607 O O   . ALA D 187 ? 0.589 0.850 0.687 0.123  -0.078 -0.168 187 ALA DDD O   
12608 C CB  . ALA D 187 ? 0.606 0.900 0.688 0.135  -0.089 -0.180 187 ALA DDD CB  
12609 N N   . ILE D 188 ? 0.643 0.910 0.754 0.127  -0.083 -0.186 188 ILE DDD N   
12610 C CA  . ILE D 188 ? 0.656 0.908 0.776 0.123  -0.078 -0.187 188 ILE DDD CA  
12611 C C   . ILE D 188 ? 0.676 0.919 0.803 0.119  -0.076 -0.183 188 ILE DDD C   
12612 O O   . ILE D 188 ? 0.676 0.908 0.804 0.114  -0.070 -0.179 188 ILE DDD O   
12613 C CB  . ILE D 188 ? 0.691 0.942 0.821 0.124  -0.080 -0.198 188 ILE DDD CB  
12614 C CG1 . ILE D 188 ? 0.704 0.958 0.829 0.126  -0.080 -0.201 188 ILE DDD CG1 
12615 C CG2 . ILE D 188 ? 0.698 0.936 0.841 0.119  -0.076 -0.201 188 ILE DDD CG2 
12616 C CD1 . ILE D 188 ? 0.699 0.957 0.834 0.128  -0.084 -0.213 188 ILE DDD CD1 
12617 N N   . GLN D 189 ? 0.682 0.932 0.814 0.122  -0.080 -0.185 189 GLN DDD N   
12618 C CA  . GLN D 189 ? 0.664 0.908 0.808 0.119  -0.079 -0.185 189 GLN DDD CA  
12619 C C   . GLN D 189 ? 0.654 0.894 0.790 0.116  -0.076 -0.174 189 GLN DDD C   
12620 O O   . GLN D 189 ? 0.662 0.892 0.806 0.112  -0.071 -0.172 189 GLN DDD O   
12621 C CB  . GLN D 189 ? 0.657 0.909 0.809 0.123  -0.086 -0.191 189 GLN DDD CB  
12622 C CG  . GLN D 189 ? 0.664 0.909 0.832 0.120  -0.085 -0.194 189 GLN DDD CG  
12623 C CD  . GLN D 189 ? 0.674 0.927 0.850 0.124  -0.092 -0.198 189 GLN DDD CD  
12624 O OE1 . GLN D 189 ? 0.622 0.886 0.797 0.129  -0.098 -0.203 189 GLN DDD OE1 
12625 N NE2 . GLN D 189 ? 0.672 0.921 0.858 0.122  -0.091 -0.196 189 GLN DDD NE2 
12626 N N   . TYR D 190 ? 0.608 0.858 0.733 0.119  -0.079 -0.167 190 TYR DDD N   
12627 C CA  . TYR D 190 ? 0.600 0.850 0.721 0.118  -0.078 -0.157 190 TYR DDD CA  
12628 C C   . TYR D 190 ? 0.531 0.777 0.639 0.116  -0.074 -0.149 190 TYR DDD C   
12629 O O   . TYR D 190 ? 0.488 0.730 0.597 0.113  -0.071 -0.142 190 TYR DDD O   
12630 C CB  . TYR D 190 ? 0.621 0.883 0.739 0.123  -0.086 -0.155 190 TYR DDD CB  
12631 C CG  . TYR D 190 ? 0.653 0.918 0.784 0.125  -0.091 -0.162 190 TYR DDD CG  
12632 C CD1 . TYR D 190 ? 0.646 0.901 0.791 0.121  -0.089 -0.163 190 TYR DDD CD1 
12633 C CD2 . TYR D 190 ? 0.701 0.977 0.832 0.130  -0.098 -0.168 190 TYR DDD CD2 
12634 C CE1 . TYR D 190 ? 0.676 0.933 0.834 0.123  -0.093 -0.169 190 TYR DDD CE1 
12635 C CE2 . TYR D 190 ? 0.715 0.993 0.859 0.131  -0.103 -0.175 190 TYR DDD CE2 
12636 C CZ  . TYR D 190 ? 0.700 0.969 0.858 0.128  -0.101 -0.175 190 TYR DDD CZ  
12637 O OH  . TYR D 190 ? 0.685 0.956 0.857 0.130  -0.106 -0.182 190 TYR DDD OH  
12638 N N   . SER D 191 ? 0.479 0.727 0.579 0.116  -0.072 -0.151 191 SER DDD N   
12639 C CA  . SER D 191 ? 0.480 0.726 0.568 0.115  -0.068 -0.143 191 SER DDD CA  
12640 C C   . SER D 191 ? 0.441 0.673 0.531 0.110  -0.062 -0.143 191 SER DDD C   
12641 O O   . SER D 191 ? 0.459 0.685 0.557 0.108  -0.061 -0.150 191 SER DDD O   
12642 C CB  . SER D 191 ? 0.471 0.726 0.549 0.118  -0.071 -0.146 191 SER DDD CB  
12643 O OG  . SER D 191 ? 0.536 0.804 0.612 0.123  -0.077 -0.149 191 SER DDD OG  
12644 N N   . ILE D 192 ? 0.427 0.655 0.510 0.107  -0.058 -0.135 192 ILE DDD N   
12645 C CA  . ILE D 192 ? 0.415 0.631 0.497 0.102  -0.052 -0.134 192 ILE DDD CA  
12646 C C   . ILE D 192 ? 0.408 0.625 0.480 0.103  -0.051 -0.133 192 ILE DDD C   
12647 O O   . ILE D 192 ? 0.402 0.630 0.467 0.107  -0.055 -0.133 192 ILE DDD O   
12648 C CB  . ILE D 192 ? 0.393 0.601 0.476 0.098  -0.048 -0.127 192 ILE DDD CB  
12649 C CG1 . ILE D 192 ? 0.414 0.629 0.488 0.099  -0.049 -0.118 192 ILE DDD CG1 
12650 C CG2 . ILE D 192 ? 0.405 0.611 0.500 0.097  -0.048 -0.129 192 ILE DDD CG2 
12651 C CD1 . ILE D 192 ? 0.393 0.601 0.467 0.095  -0.044 -0.111 192 ILE DDD CD1 
12652 N N   . THR D 193 ? 0.411 0.619 0.481 0.099  -0.047 -0.132 193 THR DDD N   
12653 C CA  . THR D 193 ? 0.409 0.616 0.470 0.100  -0.046 -0.130 193 THR DDD CA  
12654 C C   . THR D 193 ? 0.411 0.609 0.468 0.095  -0.041 -0.124 193 THR DDD C   
12655 O O   . THR D 193 ? 0.445 0.638 0.506 0.092  -0.038 -0.121 193 THR DDD O   
12656 C CB  . THR D 193 ? 0.417 0.622 0.483 0.100  -0.047 -0.138 193 THR DDD CB  
12657 O OG1 . THR D 193 ? 0.394 0.586 0.466 0.095  -0.043 -0.139 193 THR DDD OG1 
12658 C CG2 . THR D 193 ? 0.438 0.652 0.510 0.105  -0.052 -0.146 193 THR DDD CG2 
12659 N N   . SER D 194 ? 0.392 0.587 0.442 0.094  -0.040 -0.122 194 SER DDD N   
12660 C CA  . SER D 194 ? 0.380 0.566 0.426 0.090  -0.035 -0.116 194 SER DDD CA  
12661 C C   . SER D 194 ? 0.377 0.550 0.427 0.085  -0.032 -0.118 194 SER DDD C   
12662 O O   . SER D 194 ? 0.376 0.542 0.424 0.080  -0.028 -0.113 194 SER DDD O   
12663 C CB  . SER D 194 ? 0.347 0.534 0.385 0.091  -0.036 -0.115 194 SER DDD CB  
12664 O OG  . SER D 194 ? 0.379 0.566 0.420 0.093  -0.038 -0.121 194 SER DDD OG  
12665 N N   . ASP D 195 ? 0.393 0.565 0.451 0.085  -0.033 -0.125 195 ASP DDD N   
12666 C CA  . ASP D 195 ? 0.418 0.579 0.483 0.080  -0.029 -0.127 195 ASP DDD CA  
12667 C C   . ASP D 195 ? 0.411 0.571 0.481 0.077  -0.026 -0.125 195 ASP DDD C   
12668 O O   . ASP D 195 ? 0.412 0.563 0.484 0.072  -0.022 -0.125 195 ASP DDD O   
12669 C CB  . ASP D 195 ? 0.440 0.602 0.514 0.081  -0.032 -0.135 195 ASP DDD CB  
12670 C CG  . ASP D 195 ? 0.451 0.610 0.523 0.082  -0.033 -0.137 195 ASP DDD CG  
12671 O OD1 . ASP D 195 ? 0.437 0.595 0.500 0.082  -0.033 -0.132 195 ASP DDD OD1 
12672 O OD2 . ASP D 195 ? 0.508 0.666 0.588 0.083  -0.035 -0.143 195 ASP DDD OD2 
12673 N N   . ASP D 196 ? 0.406 0.574 0.476 0.081  -0.029 -0.124 196 ASP DDD N   
12674 C CA  . ASP D 196 ? 0.412 0.579 0.490 0.079  -0.027 -0.123 196 ASP DDD CA  
12675 C C   . ASP D 196 ? 0.420 0.588 0.493 0.078  -0.026 -0.116 196 ASP DDD C   
12676 O O   . ASP D 196 ? 0.404 0.568 0.484 0.075  -0.023 -0.115 196 ASP DDD O   
12677 C CB  . ASP D 196 ? 0.419 0.595 0.506 0.083  -0.032 -0.128 196 ASP DDD CB  
12678 C CG  . ASP D 196 ? 0.395 0.571 0.487 0.085  -0.034 -0.135 196 ASP DDD CG  
12679 O OD1 . ASP D 196 ? 0.389 0.557 0.486 0.081  -0.031 -0.139 196 ASP DDD OD1 
12680 O OD2 . ASP D 196 ? 0.398 0.583 0.487 0.090  -0.039 -0.138 196 ASP DDD OD2 
12681 N N   . ILE D 197 ? 0.394 0.568 0.459 0.081  -0.028 -0.111 197 ILE DDD N   
12682 C CA  . ILE D 197 ? 0.377 0.555 0.439 0.082  -0.028 -0.104 197 ILE DDD CA  
12683 C C   . ILE D 197 ? 0.371 0.541 0.432 0.076  -0.023 -0.100 197 ILE DDD C   
12684 O O   . ILE D 197 ? 0.390 0.560 0.455 0.076  -0.022 -0.097 197 ILE DDD O   
12685 C CB  . ILE D 197 ? 0.362 0.549 0.415 0.086  -0.031 -0.100 197 ILE DDD CB  
12686 C CG1 . ILE D 197 ? 0.364 0.556 0.415 0.086  -0.031 -0.093 197 ILE DDD CG1 
12687 C CG2 . ILE D 197 ? 0.345 0.527 0.390 0.084  -0.029 -0.100 197 ILE DDD CG2 
12688 C CD1 . ILE D 197 ? 0.353 0.549 0.412 0.087  -0.034 -0.092 197 ILE DDD CD1 
12689 N N   . PHE D 198 ? 0.363 0.524 0.420 0.073  -0.019 -0.102 198 PHE DDD N   
12690 C CA  . PHE D 198 ? 0.379 0.532 0.433 0.068  -0.015 -0.098 198 PHE DDD CA  
12691 C C   . PHE D 198 ? 0.449 0.597 0.512 0.064  -0.011 -0.101 198 PHE DDD C   
12692 O O   . PHE D 198 ? 0.490 0.633 0.553 0.060  -0.007 -0.099 198 PHE DDD O   
12693 C CB  . PHE D 198 ? 0.353 0.500 0.398 0.066  -0.013 -0.097 198 PHE DDD CB  
12694 C CG  . PHE D 198 ? 0.329 0.483 0.368 0.070  -0.017 -0.095 198 PHE DDD CG  
12695 C CD1 . PHE D 198 ? 0.311 0.471 0.346 0.072  -0.018 -0.089 198 PHE DDD CD1 
12696 C CD2 . PHE D 198 ? 0.339 0.494 0.376 0.072  -0.019 -0.099 198 PHE DDD CD2 
12697 C CE1 . PHE D 198 ? 0.312 0.478 0.341 0.076  -0.021 -0.088 198 PHE DDD CE1 
12698 C CE2 . PHE D 198 ? 0.346 0.506 0.376 0.076  -0.022 -0.097 198 PHE DDD CE2 
12699 C CZ  . PHE D 198 ? 0.326 0.493 0.352 0.078  -0.023 -0.092 198 PHE DDD CZ  
12700 N N   . PHE D 199 ? 0.494 0.643 0.566 0.064  -0.012 -0.107 199 PHE DDD N   
12701 C CA  . PHE D 199 ? 0.493 0.636 0.574 0.060  -0.008 -0.111 199 PHE DDD CA  
12702 C C   . PHE D 199 ? 0.469 0.617 0.562 0.062  -0.010 -0.114 199 PHE DDD C   
12703 O O   . PHE D 199 ? 0.471 0.616 0.574 0.059  -0.007 -0.118 199 PHE DDD O   
12704 C CB  . PHE D 199 ? 0.537 0.675 0.619 0.057  -0.006 -0.116 199 PHE DDD CB  
12705 C CG  . PHE D 199 ? 0.601 0.733 0.672 0.055  -0.004 -0.113 199 PHE DDD CG  
12706 C CD1 . PHE D 199 ? 0.660 0.787 0.725 0.051  -0.000 -0.110 199 PHE DDD CD1 
12707 C CD2 . PHE D 199 ? 0.625 0.757 0.691 0.057  -0.007 -0.115 199 PHE DDD CD2 
12708 C CE1 . PHE D 199 ? 0.676 0.797 0.730 0.049  0.001  -0.107 199 PHE DDD CE1 
12709 C CE2 . PHE D 199 ? 0.629 0.756 0.686 0.055  -0.006 -0.112 199 PHE DDD CE2 
12710 C CZ  . PHE D 199 ? 0.662 0.784 0.713 0.051  -0.002 -0.108 199 PHE DDD CZ  
12711 N N   . LEU D 200 ? 0.455 0.613 0.549 0.067  -0.016 -0.111 200 LEU DDD N   
12712 C CA  . LEU D 200 ? 0.488 0.651 0.594 0.070  -0.019 -0.113 200 LEU DDD CA  
12713 C C   . LEU D 200 ? 0.481 0.638 0.595 0.065  -0.014 -0.113 200 LEU DDD C   
12714 O O   . LEU D 200 ? 0.498 0.654 0.609 0.063  -0.012 -0.108 200 LEU DDD O   
12715 C CB  . LEU D 200 ? 0.493 0.664 0.595 0.075  -0.024 -0.107 200 LEU DDD CB  
12716 C CG  . LEU D 200 ? 0.508 0.686 0.603 0.080  -0.029 -0.108 200 LEU DDD CG  
12717 C CD1 . LEU D 200 ? 0.515 0.703 0.608 0.084  -0.034 -0.102 200 LEU DDD CD1 
12718 C CD2 . LEU D 200 ? 0.499 0.678 0.602 0.081  -0.031 -0.116 200 LEU DDD CD2 
12719 N N   . SER D 201 ? 0.483 0.639 0.610 0.064  -0.013 -0.119 201 SER DDD N   
12720 C CA  . SER D 201 ? 0.554 0.707 0.693 0.060  -0.010 -0.121 201 SER DDD CA  
12721 C C   . SER D 201 ? 0.576 0.735 0.720 0.063  -0.014 -0.115 201 SER DDD C   
12722 O O   . SER D 201 ? 0.625 0.781 0.774 0.060  -0.011 -0.114 201 SER DDD O   
12723 C CB  . SER D 201 ? 0.569 0.720 0.721 0.058  -0.008 -0.129 201 SER DDD CB  
12724 O OG  . SER D 201 ? 0.577 0.735 0.735 0.063  -0.015 -0.131 201 SER DDD OG  
12725 N N   . LYS D 202 ? 0.600 0.767 0.742 0.069  -0.021 -0.112 202 LYS DDD N   
12726 C CA  . LYS D 202 ? 0.643 0.815 0.788 0.072  -0.026 -0.106 202 LYS DDD CA  
12727 C C   . LYS D 202 ? 0.554 0.731 0.685 0.075  -0.029 -0.098 202 LYS DDD C   
12728 O O   . LYS D 202 ? 0.498 0.677 0.619 0.077  -0.029 -0.099 202 LYS DDD O   
12729 C CB  . LYS D 202 ? 0.800 0.978 0.957 0.076  -0.032 -0.109 202 LYS DDD CB  
12730 C CG  . LYS D 202 ? 0.944 1.128 1.108 0.079  -0.037 -0.103 202 LYS DDD CG  
12731 C CD  . LYS D 202 ? 1.064 1.255 1.234 0.083  -0.044 -0.104 202 LYS DDD CD  
12732 C CE  . LYS D 202 ? 1.120 1.316 1.296 0.086  -0.051 -0.097 202 LYS DDD CE  
12733 N NZ  . LYS D 202 ? 1.154 1.355 1.316 0.088  -0.053 -0.088 202 LYS DDD NZ  
12734 N N   . SER D 203 ? 0.496 0.676 0.628 0.076  -0.030 -0.091 203 SER DDD N   
12735 C CA  . SER D 203 ? 0.492 0.678 0.612 0.079  -0.033 -0.083 203 SER DDD CA  
12736 C C   . SER D 203 ? 0.491 0.686 0.607 0.084  -0.039 -0.083 203 SER DDD C   
12737 O O   . SER D 203 ? 0.437 0.635 0.563 0.086  -0.043 -0.086 203 SER DDD O   
12738 C CB  . SER D 203 ? 0.485 0.672 0.609 0.078  -0.033 -0.075 203 SER DDD CB  
12739 O OG  . SER D 203 ? 0.535 0.727 0.669 0.081  -0.039 -0.073 203 SER DDD OG  
12740 N N   . PRO D 204 ? 0.462 0.662 0.565 0.086  -0.041 -0.081 204 PRO DDD N   
12741 C CA  . PRO D 204 ? 0.462 0.671 0.560 0.091  -0.046 -0.082 204 PRO DDD CA  
12742 C C   . PRO D 204 ? 0.473 0.691 0.571 0.095  -0.052 -0.076 204 PRO DDD C   
12743 O O   . PRO D 204 ? 0.452 0.678 0.548 0.099  -0.057 -0.078 204 PRO DDD O   
12744 C CB  . PRO D 204 ? 0.487 0.697 0.570 0.092  -0.044 -0.081 204 PRO DDD CB  
12745 C CG  . PRO D 204 ? 0.487 0.693 0.567 0.089  -0.040 -0.075 204 PRO DDD CG  
12746 C CD  . PRO D 204 ? 0.481 0.678 0.573 0.085  -0.037 -0.077 204 PRO DDD CD  
12747 N N   . GLY D 205 ? 0.467 0.685 0.570 0.094  -0.052 -0.068 205 GLY DDD N   
12748 C CA  . GLY D 205 ? 0.442 0.668 0.545 0.097  -0.058 -0.059 205 GLY DDD CA  
12749 C C   . GLY D 205 ? 0.438 0.674 0.526 0.100  -0.060 -0.056 205 GLY DDD C   
12750 O O   . GLY D 205 ? 0.377 0.612 0.454 0.099  -0.057 -0.057 205 GLY DDD O   
12751 N N   . LYS D 206 ? 0.463 0.709 0.550 0.104  -0.067 -0.052 206 LYS DDD N   
12752 C CA  . LYS D 206 ? 0.460 0.718 0.533 0.107  -0.070 -0.049 206 LYS DDD CA  
12753 C C   . LYS D 206 ? 0.442 0.701 0.508 0.108  -0.069 -0.058 206 LYS DDD C   
12754 O O   . LYS D 206 ? 0.464 0.721 0.536 0.109  -0.071 -0.067 206 LYS DDD O   
12755 C CB  . LYS D 206 ? 0.480 0.747 0.555 0.110  -0.078 -0.044 206 LYS DDD CB  
12756 C CG  . LYS D 206 ? 0.500 0.781 0.561 0.114  -0.081 -0.043 206 LYS DDD CG  
12757 C CD  . LYS D 206 ? 0.521 0.811 0.581 0.117  -0.089 -0.035 206 LYS DDD CD  
12758 C CE  . LYS D 206 ? 0.537 0.841 0.581 0.120  -0.091 -0.032 206 LYS DDD CE  
12759 N NZ  . LYS D 206 ? 0.573 0.888 0.616 0.123  -0.099 -0.028 206 LYS DDD NZ  
12760 N N   . THR D 207 ? 0.409 0.671 0.464 0.108  -0.066 -0.058 207 THR DDD N   
12761 C CA  . THR D 207 ? 0.388 0.648 0.437 0.109  -0.063 -0.067 207 THR DDD CA  
12762 C C   . THR D 207 ? 0.378 0.651 0.415 0.113  -0.066 -0.067 207 THR DDD C   
12763 O O   . THR D 207 ? 0.338 0.617 0.366 0.113  -0.065 -0.059 207 THR DDD O   
12764 C CB  . THR D 207 ? 0.379 0.628 0.428 0.105  -0.057 -0.068 207 THR DDD CB  
12765 O OG1 . THR D 207 ? 0.398 0.636 0.458 0.102  -0.055 -0.070 207 THR DDD OG1 
12766 C CG2 . THR D 207 ? 0.377 0.625 0.421 0.106  -0.055 -0.077 207 THR DDD CG2 
12767 N N   . LEU D 208 ? 0.399 0.676 0.435 0.115  -0.068 -0.076 208 LEU DDD N   
12768 C CA  . LEU D 208 ? 0.417 0.705 0.441 0.118  -0.069 -0.080 208 LEU DDD CA  
12769 C C   . LEU D 208 ? 0.422 0.703 0.446 0.117  -0.065 -0.087 208 LEU DDD C   
12770 O O   . LEU D 208 ? 0.410 0.682 0.442 0.116  -0.064 -0.095 208 LEU DDD O   
12771 C CB  . LEU D 208 ? 0.428 0.727 0.453 0.122  -0.075 -0.085 208 LEU DDD CB  
12772 C CG  . LEU D 208 ? 0.438 0.748 0.453 0.126  -0.076 -0.091 208 LEU DDD CG  
12773 C CD1 . LEU D 208 ? 0.434 0.755 0.437 0.126  -0.076 -0.083 208 LEU DDD CD1 
12774 C CD2 . LEU D 208 ? 0.465 0.783 0.483 0.129  -0.082 -0.099 208 LEU DDD CD2 
12775 N N   . VAL D 209 ? 0.417 0.701 0.432 0.117  -0.062 -0.085 209 VAL DDD N   
12776 C CA  . VAL D 209 ? 0.419 0.698 0.433 0.116  -0.059 -0.092 209 VAL DDD CA  
12777 C C   . VAL D 209 ? 0.436 0.728 0.442 0.121  -0.062 -0.098 209 VAL DDD C   
12778 O O   . VAL D 209 ? 0.448 0.752 0.446 0.122  -0.062 -0.092 209 VAL DDD O   
12779 C CB  . VAL D 209 ? 0.392 0.663 0.402 0.113  -0.054 -0.086 209 VAL DDD CB  
12780 C CG1 . VAL D 209 ? 0.381 0.648 0.390 0.113  -0.051 -0.093 209 VAL DDD CG1 
12781 C CG2 . VAL D 209 ? 0.400 0.659 0.418 0.109  -0.051 -0.082 209 VAL DDD CG2 
12782 N N   . ILE D 210 ? 0.434 0.727 0.445 0.122  -0.063 -0.108 210 ILE DDD N   
12783 C CA  . ILE D 210 ? 0.444 0.749 0.450 0.126  -0.066 -0.116 210 ILE DDD CA  
12784 C C   . ILE D 210 ? 0.439 0.738 0.444 0.125  -0.062 -0.119 210 ILE DDD C   
12785 O O   . ILE D 210 ? 0.454 0.741 0.466 0.123  -0.060 -0.123 210 ILE DDD O   
12786 C CB  . ILE D 210 ? 0.464 0.773 0.476 0.129  -0.070 -0.126 210 ILE DDD CB  
12787 C CG1 . ILE D 210 ? 0.450 0.762 0.464 0.130  -0.074 -0.122 210 ILE DDD CG1 
12788 C CG2 . ILE D 210 ? 0.468 0.791 0.475 0.133  -0.073 -0.134 210 ILE DDD CG2 
12789 C CD1 . ILE D 210 ? 0.450 0.750 0.477 0.127  -0.074 -0.124 210 ILE DDD CD1 
12790 N N   . GLY D 211 ? 0.423 0.732 0.420 0.126  -0.061 -0.117 211 GLY DDD N   
12791 C CA  . GLY D 211 ? 0.428 0.734 0.424 0.126  -0.058 -0.120 211 GLY DDD CA  
12792 C C   . GLY D 211 ? 0.440 0.744 0.429 0.123  -0.054 -0.110 211 GLY DDD C   
12793 O O   . GLY D 211 ? 0.439 0.734 0.430 0.120  -0.052 -0.102 211 GLY DDD O   
12794 N N   . ALA D 212 ? 0.442 0.757 0.426 0.125  -0.053 -0.110 212 ALA DDD N   
12795 C CA  . ALA D 212 ? 0.431 0.745 0.410 0.123  -0.049 -0.102 212 ALA DDD CA  
12796 C C   . ALA D 212 ? 0.403 0.709 0.385 0.122  -0.047 -0.107 212 ALA DDD C   
12797 O O   . ALA D 212 ? 0.384 0.693 0.361 0.122  -0.045 -0.104 212 ALA DDD O   
12798 C CB  . ALA D 212 ? 0.462 0.792 0.431 0.125  -0.050 -0.099 212 ALA DDD CB  
12799 N N   . SER D 213 ? 0.390 0.686 0.378 0.121  -0.049 -0.114 213 SER DDD N   
12800 C CA  . SER D 213 ? 0.407 0.690 0.400 0.119  -0.047 -0.116 213 SER DDD CA  
12801 C C   . SER D 213 ? 0.388 0.659 0.380 0.115  -0.044 -0.106 213 SER DDD C   
12802 O O   . SER D 213 ? 0.376 0.646 0.366 0.114  -0.043 -0.099 213 SER DDD O   
12803 C CB  . SER D 213 ? 0.416 0.690 0.418 0.119  -0.049 -0.123 213 SER DDD CB  
12804 O OG  . SER D 213 ? 0.378 0.646 0.382 0.117  -0.049 -0.119 213 SER DDD OG  
12805 N N   . TYR D 214 ? 0.388 0.649 0.381 0.113  -0.042 -0.106 214 TYR DDD N   
12806 C CA  . TYR D 214 ? 0.402 0.652 0.394 0.109  -0.039 -0.098 214 TYR DDD CA  
12807 C C   . TYR D 214 ? 0.396 0.636 0.391 0.106  -0.038 -0.096 214 TYR DDD C   
12808 O O   . TYR D 214 ? 0.417 0.654 0.411 0.103  -0.036 -0.088 214 TYR DDD O   
12809 C CB  . TYR D 214 ? 0.410 0.652 0.403 0.107  -0.038 -0.099 214 TYR DDD CB  
12810 C CG  . TYR D 214 ? 0.437 0.665 0.436 0.105  -0.039 -0.103 214 TYR DDD CG  
12811 C CD1 . TYR D 214 ? 0.461 0.676 0.459 0.100  -0.036 -0.098 214 TYR DDD CD1 
12812 C CD2 . TYR D 214 ? 0.437 0.665 0.440 0.107  -0.041 -0.111 214 TYR DDD CD2 
12813 C CE1 . TYR D 214 ? 0.469 0.671 0.471 0.098  -0.037 -0.100 214 TYR DDD CE1 
12814 C CE2 . TYR D 214 ? 0.456 0.671 0.464 0.104  -0.042 -0.114 214 TYR DDD CE2 
12815 C CZ  . TYR D 214 ? 0.493 0.696 0.500 0.099  -0.039 -0.108 214 TYR DDD CZ  
12816 O OH  . TYR D 214 ? 0.578 0.768 0.589 0.096  -0.039 -0.109 214 TYR DDD OH  
12817 N N   . ILE D 215 ? 0.369 0.605 0.370 0.106  -0.040 -0.102 215 ILE DDD N   
12818 C CA  . ILE D 215 ? 0.365 0.592 0.370 0.103  -0.039 -0.101 215 ILE DDD CA  
12819 C C   . ILE D 215 ? 0.357 0.592 0.361 0.104  -0.040 -0.096 215 ILE DDD C   
12820 O O   . ILE D 215 ? 0.333 0.562 0.338 0.101  -0.038 -0.090 215 ILE DDD O   
12821 C CB  . ILE D 215 ? 0.382 0.604 0.395 0.103  -0.041 -0.108 215 ILE DDD CB  
12822 C CG1 . ILE D 215 ? 0.374 0.585 0.388 0.101  -0.040 -0.111 215 ILE DDD CG1 
12823 C CG2 . ILE D 215 ? 0.420 0.635 0.437 0.101  -0.040 -0.108 215 ILE DDD CG2 
12824 C CD1 . ILE D 215 ? 0.387 0.597 0.408 0.102  -0.043 -0.119 215 ILE DDD CD1 
12825 N N   . GLY D 216 ? 0.335 0.583 0.338 0.108  -0.043 -0.099 216 GLY DDD N   
12826 C CA  . GLY D 216 ? 0.333 0.591 0.334 0.110  -0.044 -0.095 216 GLY DDD CA  
12827 C C   . GLY D 216 ? 0.337 0.596 0.334 0.108  -0.042 -0.085 216 GLY DDD C   
12828 O O   . GLY D 216 ? 0.337 0.593 0.336 0.107  -0.042 -0.080 216 GLY DDD O   
12829 N N   . LEU D 217 ? 0.357 0.620 0.348 0.109  -0.041 -0.083 217 LEU DDD N   
12830 C CA  . LEU D 217 ? 0.373 0.638 0.359 0.108  -0.038 -0.073 217 LEU DDD CA  
12831 C C   . LEU D 217 ? 0.354 0.606 0.345 0.103  -0.036 -0.069 217 LEU DDD C   
12832 O O   . LEU D 217 ? 0.352 0.604 0.344 0.102  -0.035 -0.061 217 LEU DDD O   
12833 C CB  . LEU D 217 ? 0.387 0.660 0.369 0.109  -0.037 -0.073 217 LEU DDD CB  
12834 C CG  . LEU D 217 ? 0.412 0.701 0.388 0.113  -0.039 -0.076 217 LEU DDD CG  
12835 C CD1 . LEU D 217 ? 0.443 0.739 0.414 0.113  -0.037 -0.073 217 LEU DDD CD1 
12836 C CD2 . LEU D 217 ? 0.431 0.729 0.405 0.114  -0.041 -0.072 217 LEU DDD CD2 
12837 N N   . GLU D 218 ? 0.337 0.578 0.330 0.101  -0.034 -0.073 218 GLU DDD N   
12838 C CA  . GLU D 218 ? 0.335 0.562 0.331 0.097  -0.031 -0.069 218 GLU DDD CA  
12839 C C   . GLU D 218 ? 0.315 0.539 0.317 0.095  -0.031 -0.068 218 GLU DDD C   
12840 O O   . GLU D 218 ? 0.277 0.497 0.281 0.093  -0.030 -0.062 218 GLU DDD O   
12841 C CB  . GLU D 218 ? 0.330 0.546 0.326 0.095  -0.030 -0.074 218 GLU DDD CB  
12842 C CG  . GLU D 218 ? 0.332 0.549 0.325 0.095  -0.030 -0.075 218 GLU DDD CG  
12843 C CD  . GLU D 218 ? 0.342 0.548 0.336 0.093  -0.029 -0.079 218 GLU DDD CD  
12844 O OE1 . GLU D 218 ? 0.350 0.551 0.348 0.092  -0.030 -0.084 218 GLU DDD OE1 
12845 O OE2 . GLU D 218 ? 0.359 0.562 0.350 0.092  -0.029 -0.078 218 GLU DDD OE2 
12846 N N   . THR D 219 ? 0.309 0.534 0.314 0.097  -0.034 -0.074 219 THR DDD N   
12847 C CA  . THR D 219 ? 0.329 0.551 0.341 0.096  -0.034 -0.074 219 THR DDD CA  
12848 C C   . THR D 219 ? 0.344 0.574 0.356 0.097  -0.036 -0.068 219 THR DDD C   
12849 O O   . THR D 219 ? 0.369 0.594 0.387 0.095  -0.035 -0.064 219 THR DDD O   
12850 C CB  . THR D 219 ? 0.329 0.551 0.345 0.098  -0.037 -0.083 219 THR DDD CB  
12851 O OG1 . THR D 219 ? 0.291 0.506 0.306 0.096  -0.035 -0.088 219 THR DDD OG1 
12852 C CG2 . THR D 219 ? 0.337 0.556 0.362 0.096  -0.037 -0.084 219 THR DDD CG2 
12853 N N   . ALA D 220 ? 0.357 0.599 0.364 0.101  -0.039 -0.066 220 ALA DDD N   
12854 C CA  . ALA D 220 ? 0.356 0.607 0.363 0.102  -0.041 -0.059 220 ALA DDD CA  
12855 C C   . ALA D 220 ? 0.328 0.576 0.335 0.100  -0.038 -0.050 220 ALA DDD C   
12856 O O   . ALA D 220 ? 0.296 0.543 0.307 0.099  -0.038 -0.044 220 ALA DDD O   
12857 C CB  . ALA D 220 ? 0.342 0.607 0.341 0.106  -0.044 -0.060 220 ALA DDD CB  
12858 N N   . GLY D 221 ? 0.336 0.581 0.337 0.099  -0.035 -0.050 221 GLY DDD N   
12859 C CA  . GLY D 221 ? 0.353 0.596 0.355 0.096  -0.032 -0.043 221 GLY DDD CA  
12860 C C   . GLY D 221 ? 0.342 0.573 0.352 0.092  -0.030 -0.041 221 GLY DDD C   
12861 O O   . GLY D 221 ? 0.357 0.589 0.371 0.091  -0.030 -0.033 221 GLY DDD O   
12862 N N   . PHE D 222 ? 0.325 0.546 0.338 0.090  -0.029 -0.047 222 PHE DDD N   
12863 C CA  . PHE D 222 ? 0.324 0.535 0.345 0.087  -0.027 -0.046 222 PHE DDD CA  
12864 C C   . PHE D 222 ? 0.324 0.536 0.352 0.087  -0.029 -0.046 222 PHE DDD C   
12865 O O   . PHE D 222 ? 0.311 0.520 0.347 0.085  -0.028 -0.041 222 PHE DDD O   
12866 C CB  . PHE D 222 ? 0.305 0.506 0.325 0.083  -0.024 -0.052 222 PHE DDD CB  
12867 C CG  . PHE D 222 ? 0.298 0.495 0.320 0.084  -0.025 -0.060 222 PHE DDD CG  
12868 C CD1 . PHE D 222 ? 0.317 0.512 0.346 0.083  -0.025 -0.063 222 PHE DDD CD1 
12869 C CD2 . PHE D 222 ? 0.306 0.501 0.322 0.084  -0.025 -0.065 222 PHE DDD CD2 
12870 C CE1 . PHE D 222 ? 0.321 0.513 0.352 0.083  -0.026 -0.070 222 PHE DDD CE1 
12871 C CE2 . PHE D 222 ? 0.306 0.498 0.325 0.084  -0.025 -0.072 222 PHE DDD CE2 
12872 C CZ  . PHE D 222 ? 0.332 0.523 0.358 0.084  -0.026 -0.074 222 PHE DDD CZ  
12873 N N   . LEU D 223 ? 0.321 0.540 0.350 0.090  -0.032 -0.049 223 LEU DDD N   
12874 C CA  . LEU D 223 ? 0.333 0.553 0.370 0.091  -0.035 -0.048 223 LEU DDD CA  
12875 C C   . LEU D 223 ? 0.332 0.559 0.371 0.092  -0.037 -0.039 223 LEU DDD C   
12876 O O   . LEU D 223 ? 0.300 0.524 0.349 0.090  -0.037 -0.036 223 LEU DDD O   
12877 C CB  . LEU D 223 ? 0.339 0.564 0.376 0.094  -0.039 -0.055 223 LEU DDD CB  
12878 C CG  . LEU D 223 ? 0.351 0.569 0.391 0.092  -0.037 -0.064 223 LEU DDD CG  
12879 C CD1 . LEU D 223 ? 0.372 0.596 0.413 0.096  -0.041 -0.070 223 LEU DDD CD1 
12880 C CD2 . LEU D 223 ? 0.356 0.563 0.405 0.088  -0.034 -0.065 223 LEU DDD CD2 
12881 N N   . ASN D 224 ? 0.348 0.584 0.378 0.094  -0.038 -0.034 224 ASN DDD N   
12882 C CA  . ASN D 224 ? 0.361 0.604 0.392 0.094  -0.039 -0.024 224 ASN DDD CA  
12883 C C   . ASN D 224 ? 0.369 0.605 0.405 0.091  -0.036 -0.019 224 ASN DDD C   
12884 O O   . ASN D 224 ? 0.384 0.618 0.428 0.090  -0.037 -0.013 224 ASN DDD O   
12885 C CB  . ASN D 224 ? 0.357 0.612 0.376 0.097  -0.040 -0.021 224 ASN DDD CB  
12886 C CG  . ASN D 224 ? 0.345 0.606 0.364 0.097  -0.041 -0.009 224 ASN DDD CG  
12887 O OD1 . ASN D 224 ? 0.317 0.584 0.338 0.099  -0.046 -0.005 224 ASN DDD OD1 
12888 N ND2 . ASN D 224 ? 0.366 0.627 0.383 0.095  -0.038 -0.004 224 ASN DDD ND2 
12889 N N   . GLU D 225 ? 0.382 0.611 0.414 0.089  -0.032 -0.021 225 GLU DDD N   
12890 C CA  . GLU D 225 ? 0.399 0.621 0.436 0.085  -0.028 -0.018 225 GLU DDD CA  
12891 C C   . GLU D 225 ? 0.382 0.596 0.431 0.083  -0.028 -0.020 225 GLU DDD C   
12892 O O   . GLU D 225 ? 0.413 0.624 0.470 0.081  -0.027 -0.015 225 GLU DDD O   
12893 C CB  . GLU D 225 ? 0.436 0.653 0.467 0.084  -0.025 -0.022 225 GLU DDD CB  
12894 C CG  . GLU D 225 ? 0.486 0.709 0.511 0.084  -0.024 -0.016 225 GLU DDD CG  
12895 C CD  . GLU D 225 ? 0.522 0.739 0.540 0.083  -0.021 -0.020 225 GLU DDD CD  
12896 O OE1 . GLU D 225 ? 0.531 0.748 0.543 0.084  -0.021 -0.026 225 GLU DDD OE1 
12897 O OE2 . GLU D 225 ? 0.631 0.845 0.652 0.081  -0.019 -0.016 225 GLU DDD OE2 
12898 N N   . LEU D 226 ? 0.342 0.553 0.394 0.083  -0.029 -0.027 226 LEU DDD N   
12899 C CA  . LEU D 226 ? 0.338 0.540 0.401 0.080  -0.028 -0.031 226 LEU DDD CA  
12900 C C   . LEU D 226 ? 0.372 0.579 0.445 0.082  -0.032 -0.027 226 LEU DDD C   
12901 O O   . LEU D 226 ? 0.356 0.558 0.441 0.080  -0.032 -0.031 226 LEU DDD O   
12902 C CB  . LEU D 226 ? 0.315 0.512 0.377 0.079  -0.026 -0.040 226 LEU DDD CB  
12903 C CG  . LEU D 226 ? 0.311 0.501 0.367 0.076  -0.022 -0.044 226 LEU DDD CG  
12904 C CD1 . LEU D 226 ? 0.326 0.510 0.381 0.075  -0.021 -0.053 226 LEU DDD CD1 
12905 C CD2 . LEU D 226 ? 0.305 0.488 0.367 0.072  -0.018 -0.043 226 LEU DDD CD2 
12906 N N   . GLY D 227 ? 0.407 0.623 0.475 0.085  -0.036 -0.021 227 GLY DDD N   
12907 C CA  . GLY D 227 ? 0.405 0.627 0.482 0.087  -0.040 -0.015 227 GLY DDD CA  
12908 C C   . GLY D 227 ? 0.404 0.631 0.481 0.090  -0.045 -0.018 227 GLY DDD C   
12909 O O   . GLY D 227 ? 0.401 0.632 0.485 0.091  -0.050 -0.013 227 GLY DDD O   
12910 N N   . PHE D 228 ? 0.375 0.603 0.444 0.091  -0.045 -0.026 228 PHE DDD N   
12911 C CA  . PHE D 228 ? 0.367 0.601 0.436 0.094  -0.049 -0.030 228 PHE DDD CA  
12912 C C   . PHE D 228 ? 0.367 0.613 0.425 0.098  -0.053 -0.025 228 PHE DDD C   
12913 O O   . PHE D 228 ? 0.383 0.633 0.431 0.098  -0.051 -0.022 228 PHE DDD O   
12914 C CB  . PHE D 228 ? 0.359 0.588 0.426 0.094  -0.047 -0.041 228 PHE DDD CB  
12915 C CG  . PHE D 228 ? 0.366 0.583 0.443 0.090  -0.043 -0.046 228 PHE DDD CG  
12916 C CD1 . PHE D 228 ? 0.366 0.580 0.456 0.089  -0.045 -0.048 228 PHE DDD CD1 
12917 C CD2 . PHE D 228 ? 0.376 0.585 0.450 0.086  -0.037 -0.049 228 PHE DDD CD2 
12918 C CE1 . PHE D 228 ? 0.363 0.568 0.463 0.085  -0.041 -0.052 228 PHE DDD CE1 
12919 C CE2 . PHE D 228 ? 0.372 0.571 0.453 0.083  -0.034 -0.054 228 PHE DDD CE2 
12920 C CZ  . PHE D 228 ? 0.380 0.577 0.475 0.082  -0.035 -0.055 228 PHE DDD CZ  
12921 N N   . ASP D 229 ? 0.379 0.632 0.440 0.101  -0.059 -0.024 229 ASP DDD N   
12922 C CA  . ASP D 229 ? 0.385 0.651 0.436 0.104  -0.063 -0.020 229 ASP DDD CA  
12923 C C   . ASP D 229 ? 0.367 0.637 0.408 0.106  -0.062 -0.030 229 ASP DDD C   
12924 O O   . ASP D 229 ? 0.379 0.646 0.424 0.107  -0.063 -0.038 229 ASP DDD O   
12925 C CB  . ASP D 229 ? 0.424 0.695 0.481 0.106  -0.070 -0.017 229 ASP DDD CB  
12926 C CG  . ASP D 229 ? 0.465 0.750 0.511 0.110  -0.075 -0.013 229 ASP DDD CG  
12927 O OD1 . ASP D 229 ? 0.492 0.784 0.526 0.112  -0.074 -0.016 229 ASP DDD OD1 
12928 O OD2 . ASP D 229 ? 0.496 0.786 0.547 0.111  -0.081 -0.007 229 ASP DDD OD2 
12929 N N   . THR D 230 ? 0.338 0.613 0.367 0.107  -0.060 -0.028 230 THR DDD N   
12930 C CA  . THR D 230 ? 0.350 0.626 0.371 0.108  -0.058 -0.037 230 THR DDD CA  
12931 C C   . THR D 230 ? 0.362 0.653 0.371 0.111  -0.060 -0.036 230 THR DDD C   
12932 O O   . THR D 230 ? 0.349 0.647 0.353 0.111  -0.060 -0.027 230 THR DDD O   
12933 C CB  . THR D 230 ? 0.363 0.630 0.383 0.105  -0.052 -0.037 230 THR DDD CB  
12934 O OG1 . THR D 230 ? 0.374 0.629 0.406 0.102  -0.050 -0.039 230 THR DDD OG1 
12935 C CG2 . THR D 230 ? 0.365 0.634 0.378 0.106  -0.050 -0.045 230 THR DDD CG2 
12936 N N   . THR D 231 ? 0.360 0.655 0.366 0.114  -0.062 -0.045 231 THR DDD N   
12937 C CA  . THR D 231 ? 0.370 0.680 0.365 0.117  -0.065 -0.047 231 THR DDD CA  
12938 C C   . THR D 231 ? 0.376 0.685 0.369 0.118  -0.063 -0.058 231 THR DDD C   
12939 O O   . THR D 231 ? 0.365 0.665 0.366 0.118  -0.063 -0.066 231 THR DDD O   
12940 C CB  . THR D 231 ? 0.417 0.736 0.414 0.120  -0.071 -0.047 231 THR DDD CB  
12941 O OG1 . THR D 231 ? 0.430 0.748 0.430 0.119  -0.073 -0.036 231 THR DDD OG1 
12942 C CG2 . THR D 231 ? 0.439 0.774 0.424 0.124  -0.074 -0.049 231 THR DDD CG2 
12943 N N   . VAL D 232 ? 0.394 0.712 0.377 0.119  -0.061 -0.059 232 VAL DDD N   
12944 C CA  . VAL D 232 ? 0.409 0.728 0.390 0.121  -0.060 -0.069 232 VAL DDD CA  
12945 C C   . VAL D 232 ? 0.438 0.774 0.413 0.125  -0.064 -0.074 232 VAL DDD C   
12946 O O   . VAL D 232 ? 0.418 0.765 0.383 0.126  -0.064 -0.068 232 VAL DDD O   
12947 C CB  . VAL D 232 ? 0.406 0.722 0.384 0.119  -0.055 -0.068 232 VAL DDD CB  
12948 C CG1 . VAL D 232 ? 0.406 0.727 0.381 0.121  -0.054 -0.078 232 VAL DDD CG1 
12949 C CG2 . VAL D 232 ? 0.393 0.693 0.377 0.115  -0.051 -0.064 232 VAL DDD CG2 
12950 N N   . ALA D 233 ? 0.457 0.794 0.436 0.127  -0.066 -0.085 233 ALA DDD N   
12951 C CA  . ALA D 233 ? 0.482 0.833 0.455 0.131  -0.070 -0.093 233 ALA DDD CA  
12952 C C   . ALA D 233 ? 0.517 0.869 0.488 0.132  -0.067 -0.101 233 ALA DDD C   
12953 O O   . ALA D 233 ? 0.507 0.849 0.486 0.131  -0.066 -0.109 233 ALA DDD O   
12954 C CB  . ALA D 233 ? 0.507 0.858 0.488 0.133  -0.075 -0.102 233 ALA DDD CB  
12955 N N   . MET D 234 ? 0.564 0.928 0.526 0.133  -0.065 -0.098 234 MET DDD N   
12956 C CA  . MET D 234 ? 0.563 0.931 0.523 0.133  -0.062 -0.105 234 MET DDD CA  
12957 C C   . MET D 234 ? 0.622 1.007 0.577 0.138  -0.065 -0.114 234 MET DDD C   
12958 O O   . MET D 234 ? 0.643 1.042 0.588 0.139  -0.067 -0.109 234 MET DDD O   
12959 C CB  . MET D 234 ? 0.559 0.928 0.512 0.131  -0.058 -0.095 234 MET DDD CB  
12960 C CG  . MET D 234 ? 0.558 0.934 0.508 0.132  -0.055 -0.100 234 MET DDD CG  
12961 S SD  . MET D 234 ? 0.575 0.946 0.522 0.129  -0.049 -0.089 234 MET DDD SD  
12962 C CE  . MET D 234 ? 0.609 0.992 0.546 0.128  -0.050 -0.076 234 MET DDD CE  
12963 N N   . ARG D 235 ? 0.663 1.046 0.624 0.139  -0.067 -0.127 235 ARG DDD N   
12964 C CA  . ARG D 235 ? 0.692 1.092 0.650 0.144  -0.070 -0.138 235 ARG DDD CA  
12965 C C   . ARG D 235 ? 0.693 1.108 0.642 0.144  -0.067 -0.137 235 ARG DDD C   
12966 O O   . ARG D 235 ? 0.732 1.164 0.673 0.147  -0.069 -0.139 235 ARG DDD O   
12967 C CB  . ARG D 235 ? 0.706 1.100 0.676 0.145  -0.071 -0.151 235 ARG DDD CB  
12968 C CG  . ARG D 235 ? 0.733 1.144 0.702 0.150  -0.075 -0.163 235 ARG DDD CG  
12969 C CD  . ARG D 235 ? 0.768 1.175 0.749 0.152  -0.079 -0.177 235 ARG DDD CD  
12970 N NE  . ARG D 235 ? 0.827 1.252 0.803 0.156  -0.083 -0.186 235 ARG DDD NE  
12971 C CZ  . ARG D 235 ? 0.872 1.313 0.845 0.158  -0.082 -0.194 235 ARG DDD CZ  
12972 N NH1 . ARG D 235 ? 0.860 1.299 0.832 0.157  -0.078 -0.194 235 ARG DDD NH1 
12973 N NH2 . ARG D 235 ? 0.884 1.341 0.853 0.162  -0.086 -0.203 235 ARG DDD NH2 
12974 N N   . SER D 236 ? 0.684 1.093 0.634 0.142  -0.062 -0.134 236 SER DDD N   
12975 C CA  . SER D 236 ? 0.635 1.057 0.577 0.143  -0.059 -0.134 236 SER DDD CA  
12976 C C   . SER D 236 ? 0.634 1.048 0.574 0.139  -0.054 -0.123 236 SER DDD C   
12977 O O   . SER D 236 ? 0.637 1.056 0.569 0.138  -0.053 -0.112 236 SER DDD O   
12978 C CB  . SER D 236 ? 0.590 1.019 0.537 0.145  -0.059 -0.148 236 SER DDD CB  
12979 O OG  . SER D 236 ? 0.517 0.929 0.475 0.145  -0.059 -0.153 236 SER DDD OG  
12980 N N   . ILE D 237 ? 0.645 1.047 0.593 0.138  -0.052 -0.125 237 ILE DDD N   
12981 C CA  . ILE D 237 ? 0.646 1.042 0.592 0.135  -0.047 -0.117 237 ILE DDD CA  
12982 C C   . ILE D 237 ? 0.621 0.996 0.575 0.132  -0.046 -0.113 237 ILE DDD C   
12983 O O   . ILE D 237 ? 0.598 0.963 0.559 0.132  -0.049 -0.120 237 ILE DDD O   
12984 C CB  . ILE D 237 ? 0.672 1.077 0.619 0.136  -0.044 -0.124 237 ILE DDD CB  
12985 C CG1 . ILE D 237 ? 0.695 1.091 0.652 0.138  -0.046 -0.137 237 ILE DDD CG1 
12986 C CG2 . ILE D 237 ? 0.663 1.090 0.600 0.139  -0.044 -0.128 237 ILE DDD CG2 
12987 C CD1 . ILE D 237 ? 0.702 1.104 0.663 0.139  -0.044 -0.143 237 ILE DDD CD1 
12988 N N   . PRO D 238 ? 0.611 0.978 0.563 0.129  -0.043 -0.102 238 PRO DDD N   
12989 C CA  . PRO D 238 ? 0.591 0.938 0.550 0.126  -0.042 -0.099 238 PRO DDD CA  
12990 C C   . PRO D 238 ? 0.547 0.887 0.512 0.125  -0.041 -0.104 238 PRO DDD C   
12991 O O   . PRO D 238 ? 0.531 0.878 0.494 0.126  -0.039 -0.106 238 PRO DDD O   
12992 C CB  . PRO D 238 ? 0.598 0.944 0.553 0.123  -0.039 -0.086 238 PRO DDD CB  
12993 C CG  . PRO D 238 ? 0.605 0.968 0.552 0.124  -0.037 -0.084 238 PRO DDD CG  
12994 C CD  . PRO D 238 ? 0.621 0.998 0.565 0.128  -0.040 -0.093 238 PRO DDD CD  
12995 N N   . LEU D 239 ? 0.552 0.876 0.524 0.124  -0.042 -0.107 239 LEU DDD N   
12996 C CA  . LEU D 239 ? 0.557 0.870 0.534 0.123  -0.041 -0.111 239 LEU DDD CA  
12997 C C   . LEU D 239 ? 0.577 0.901 0.556 0.126  -0.042 -0.121 239 LEU DDD C   
12998 O O   . LEU D 239 ? 0.547 0.873 0.526 0.126  -0.040 -0.121 239 LEU DDD O   
12999 C CB  . LEU D 239 ? 0.545 0.852 0.520 0.120  -0.037 -0.102 239 LEU DDD CB  
13000 C CG  . LEU D 239 ? 0.523 0.820 0.497 0.116  -0.036 -0.092 239 LEU DDD CG  
13001 C CD1 . LEU D 239 ? 0.517 0.809 0.490 0.113  -0.033 -0.084 239 LEU DDD CD1 
13002 C CD2 . LEU D 239 ? 0.521 0.804 0.501 0.114  -0.038 -0.095 239 LEU DDD CD2 
13003 N N   . ARG D 240 ? 0.636 0.967 0.618 0.129  -0.045 -0.130 240 ARG DDD N   
13004 C CA  . ARG D 240 ? 0.685 1.027 0.670 0.132  -0.047 -0.141 240 ARG DDD CA  
13005 C C   . ARG D 240 ? 0.646 0.976 0.639 0.131  -0.047 -0.145 240 ARG DDD C   
13006 O O   . ARG D 240 ? 0.591 0.905 0.589 0.129  -0.048 -0.144 240 ARG DDD O   
13007 C CB  . ARG D 240 ? 0.785 1.132 0.774 0.135  -0.050 -0.151 240 ARG DDD CB  
13008 C CG  . ARG D 240 ? 0.893 1.254 0.886 0.139  -0.052 -0.163 240 ARG DDD CG  
13009 C CD  . ARG D 240 ? 0.997 1.356 0.998 0.141  -0.056 -0.173 240 ARG DDD CD  
13010 N NE  . ARG D 240 ? 1.050 1.389 1.057 0.138  -0.057 -0.169 240 ARG DDD NE  
13011 C CZ  . ARG D 240 ? 1.071 1.395 1.085 0.136  -0.057 -0.169 240 ARG DDD CZ  
13012 N NH1 . ARG D 240 ? 1.109 1.437 1.127 0.137  -0.057 -0.174 240 ARG DDD NH1 
13013 N NH2 . ARG D 240 ? 1.019 1.327 1.037 0.133  -0.057 -0.165 240 ARG DDD NH2 
13014 N N   . GLY D 241 ? 0.601 0.940 0.596 0.133  -0.045 -0.148 241 GLY DDD N   
13015 C CA  . GLY D 241 ? 0.565 0.894 0.567 0.132  -0.046 -0.152 241 GLY DDD CA  
13016 C C   . GLY D 241 ? 0.565 0.889 0.564 0.129  -0.043 -0.142 241 GLY DDD C   
13017 O O   . GLY D 241 ? 0.626 0.949 0.629 0.129  -0.042 -0.145 241 GLY DDD O   
13018 N N   . PHE D 242 ? 0.580 0.901 0.571 0.127  -0.040 -0.132 242 PHE DDD N   
13019 C CA  . PHE D 242 ? 0.576 0.891 0.563 0.124  -0.037 -0.122 242 PHE DDD CA  
13020 C C   . PHE D 242 ? 0.522 0.853 0.504 0.125  -0.034 -0.120 242 PHE DDD C   
13021 O O   . PHE D 242 ? 0.543 0.890 0.521 0.127  -0.034 -0.124 242 PHE DDD O   
13022 C CB  . PHE D 242 ? 0.622 0.927 0.606 0.120  -0.036 -0.112 242 PHE DDD CB  
13023 C CG  . PHE D 242 ? 0.646 0.933 0.634 0.118  -0.038 -0.112 242 PHE DDD CG  
13024 C CD1 . PHE D 242 ? 0.634 0.919 0.627 0.120  -0.041 -0.120 242 PHE DDD CD1 
13025 C CD2 . PHE D 242 ? 0.665 0.938 0.653 0.114  -0.036 -0.105 242 PHE DDD CD2 
13026 C CE1 . PHE D 242 ? 0.667 0.936 0.664 0.117  -0.042 -0.119 242 PHE DDD CE1 
13027 C CE2 . PHE D 242 ? 0.643 0.901 0.634 0.112  -0.037 -0.105 242 PHE DDD CE2 
13028 C CZ  . PHE D 242 ? 0.643 0.899 0.638 0.113  -0.040 -0.112 242 PHE DDD CZ  
13029 N N   . ASP D 243 ? 0.475 0.804 0.457 0.123  -0.031 -0.115 243 ASP DDD N   
13030 C CA  . ASP D 243 ? 0.450 0.794 0.428 0.124  -0.028 -0.112 243 ASP DDD CA  
13031 C C   . ASP D 243 ? 0.441 0.795 0.409 0.123  -0.026 -0.105 243 ASP DDD C   
13032 O O   . ASP D 243 ? 0.414 0.759 0.381 0.121  -0.026 -0.097 243 ASP DDD O   
13033 C CB  . ASP D 243 ? 0.436 0.771 0.414 0.121  -0.025 -0.104 243 ASP DDD CB  
13034 C CG  . ASP D 243 ? 0.434 0.783 0.410 0.121  -0.021 -0.100 243 ASP DDD CG  
13035 O OD1 . ASP D 243 ? 0.423 0.782 0.403 0.123  -0.021 -0.108 243 ASP DDD OD1 
13036 O OD2 . ASP D 243 ? 0.435 0.785 0.405 0.119  -0.019 -0.090 243 ASP DDD OD2 
13037 N N   . ARG D 244 ? 0.430 0.803 0.395 0.126  -0.025 -0.108 244 ARG DDD N   
13038 C CA  . ARG D 244 ? 0.433 0.818 0.389 0.126  -0.024 -0.103 244 ARG DDD CA  
13039 C C   . ARG D 244 ? 0.409 0.791 0.361 0.122  -0.021 -0.089 244 ARG DDD C   
13040 O O   . ARG D 244 ? 0.441 0.818 0.389 0.121  -0.022 -0.082 244 ARG DDD O   
13041 C CB  . ARG D 244 ? 0.455 0.860 0.406 0.128  -0.023 -0.110 244 ARG DDD CB  
13042 C CG  . ARG D 244 ? 0.465 0.876 0.421 0.132  -0.027 -0.124 244 ARG DDD CG  
13043 C CD  . ARG D 244 ? 0.480 0.886 0.433 0.133  -0.031 -0.124 244 ARG DDD CD  
13044 N NE  . ARG D 244 ? 0.486 0.873 0.446 0.131  -0.033 -0.123 244 ARG DDD NE  
13045 C CZ  . ARG D 244 ? 0.489 0.865 0.449 0.130  -0.035 -0.117 244 ARG DDD CZ  
13046 N NH1 . ARG D 244 ? 0.504 0.887 0.456 0.130  -0.035 -0.111 244 ARG DDD NH1 
13047 N NH2 . ARG D 244 ? 0.494 0.852 0.460 0.128  -0.036 -0.118 244 ARG DDD NH2 
13048 N N   . GLN D 245 ? 0.380 0.764 0.333 0.121  -0.017 -0.086 245 GLN DDD N   
13049 C CA  . GLN D 245 ? 0.365 0.748 0.315 0.118  -0.014 -0.073 245 GLN DDD CA  
13050 C C   . GLN D 245 ? 0.366 0.730 0.318 0.116  -0.016 -0.066 245 GLN DDD C   
13051 O O   . GLN D 245 ? 0.378 0.743 0.327 0.114  -0.015 -0.057 245 GLN DDD O   
13052 C CB  . GLN D 245 ? 0.351 0.736 0.305 0.117  -0.011 -0.073 245 GLN DDD CB  
13053 C CG  . GLN D 245 ? 0.359 0.746 0.310 0.114  -0.007 -0.060 245 GLN DDD CG  
13054 C CD  . GLN D 245 ? 0.370 0.760 0.325 0.113  -0.003 -0.060 245 GLN DDD CD  
13055 O OE1 . GLN D 245 ? 0.400 0.786 0.362 0.115  -0.004 -0.069 245 GLN DDD OE1 
13056 N NE2 . GLN D 245 ? 0.370 0.766 0.323 0.111  0.000  -0.051 245 GLN DDD NE2 
13057 N N   . CYS D 246 ? 0.357 0.706 0.316 0.115  -0.018 -0.071 246 CYS DDD N   
13058 C CA  . CYS D 246 ? 0.372 0.704 0.334 0.112  -0.019 -0.065 246 CYS DDD CA  
13059 C C   . CYS D 246 ? 0.399 0.729 0.359 0.113  -0.021 -0.065 246 CYS DDD C   
13060 O O   . CYS D 246 ? 0.454 0.777 0.413 0.111  -0.021 -0.057 246 CYS DDD O   
13061 C CB  . CYS D 246 ? 0.363 0.681 0.331 0.112  -0.020 -0.071 246 CYS DDD CB  
13062 S SG  . CYS D 246 ? 0.343 0.659 0.314 0.111  -0.018 -0.070 246 CYS DDD SG  
13063 N N   . SER D 247 ? 0.401 0.736 0.360 0.116  -0.024 -0.075 247 SER DDD N   
13064 C CA  . SER D 247 ? 0.403 0.736 0.361 0.117  -0.027 -0.076 247 SER DDD CA  
13065 C C   . SER D 247 ? 0.412 0.754 0.364 0.116  -0.026 -0.067 247 SER DDD C   
13066 O O   . SER D 247 ? 0.365 0.701 0.318 0.115  -0.028 -0.062 247 SER DDD O   
13067 C CB  . SER D 247 ? 0.408 0.747 0.368 0.120  -0.030 -0.087 247 SER DDD CB  
13068 O OG  . SER D 247 ? 0.405 0.734 0.372 0.120  -0.031 -0.094 247 SER DDD OG  
13069 N N   . GLU D 248 ? 0.446 0.803 0.393 0.117  -0.024 -0.064 248 GLU DDD N   
13070 C CA  . GLU D 248 ? 0.476 0.845 0.417 0.117  -0.024 -0.055 248 GLU DDD CA  
13071 C C   . GLU D 248 ? 0.444 0.805 0.386 0.113  -0.022 -0.043 248 GLU DDD C   
13072 O O   . GLU D 248 ? 0.456 0.817 0.397 0.112  -0.023 -0.035 248 GLU DDD O   
13073 C CB  . GLU D 248 ? 0.511 0.900 0.445 0.118  -0.022 -0.058 248 GLU DDD CB  
13074 C CG  . GLU D 248 ? 0.544 0.943 0.476 0.122  -0.025 -0.069 248 GLU DDD CG  
13075 C CD  . GLU D 248 ? 0.566 0.983 0.493 0.124  -0.022 -0.075 248 GLU DDD CD  
13076 O OE1 . GLU D 248 ? 0.574 0.999 0.496 0.122  -0.018 -0.067 248 GLU DDD OE1 
13077 O OE2 . GLU D 248 ? 0.612 1.036 0.540 0.127  -0.024 -0.087 248 GLU DDD OE2 
13078 N N   . LYS D 249 ? 0.411 0.766 0.358 0.111  -0.019 -0.041 249 LYS DDD N   
13079 C CA  . LYS D 249 ? 0.409 0.753 0.359 0.108  -0.017 -0.031 249 LYS DDD CA  
13080 C C   . LYS D 249 ? 0.393 0.723 0.348 0.107  -0.020 -0.029 249 LYS DDD C   
13081 O O   . LYS D 249 ? 0.377 0.706 0.333 0.105  -0.020 -0.020 249 LYS DDD O   
13082 C CB  . LYS D 249 ? 0.399 0.736 0.354 0.106  -0.014 -0.031 249 LYS DDD CB  
13083 C CG  . LYS D 249 ? 0.400 0.730 0.359 0.103  -0.013 -0.020 249 LYS DDD CG  
13084 C CD  . LYS D 249 ? 0.405 0.727 0.369 0.101  -0.010 -0.020 249 LYS DDD CD  
13085 C CE  . LYS D 249 ? 0.421 0.737 0.390 0.098  -0.009 -0.009 249 LYS DDD CE  
13086 N NZ  . LYS D 249 ? 0.429 0.757 0.395 0.098  -0.008 0.000  249 LYS DDD NZ  
13087 N N   . ILE D 250 ? 0.370 0.691 0.327 0.108  -0.022 -0.038 250 ILE DDD N   
13088 C CA  . ILE D 250 ? 0.390 0.698 0.352 0.106  -0.024 -0.038 250 ILE DDD CA  
13089 C C   . ILE D 250 ? 0.378 0.694 0.338 0.107  -0.026 -0.034 250 ILE DDD C   
13090 O O   . ILE D 250 ? 0.359 0.668 0.322 0.105  -0.027 -0.026 250 ILE DDD O   
13091 C CB  . ILE D 250 ? 0.400 0.699 0.365 0.107  -0.025 -0.048 250 ILE DDD CB  
13092 C CG1 . ILE D 250 ? 0.412 0.702 0.380 0.105  -0.023 -0.049 250 ILE DDD CG1 
13093 C CG2 . ILE D 250 ? 0.394 0.683 0.363 0.106  -0.027 -0.048 250 ILE DDD CG2 
13094 C CD1 . ILE D 250 ? 0.442 0.728 0.411 0.107  -0.025 -0.059 250 ILE DDD CD1 
13095 N N   . VAL D 251 ? 0.392 0.719 0.346 0.110  -0.028 -0.039 251 VAL DDD N   
13096 C CA  . VAL D 251 ? 0.395 0.730 0.347 0.112  -0.031 -0.036 251 VAL DDD CA  
13097 C C   . VAL D 251 ? 0.413 0.754 0.362 0.110  -0.030 -0.024 251 VAL DDD C   
13098 O O   . VAL D 251 ? 0.412 0.750 0.364 0.109  -0.033 -0.018 251 VAL DDD O   
13099 C CB  . VAL D 251 ? 0.399 0.748 0.345 0.115  -0.034 -0.045 251 VAL DDD CB  
13100 C CG1 . VAL D 251 ? 0.401 0.761 0.342 0.117  -0.037 -0.041 251 VAL DDD CG1 
13101 C CG2 . VAL D 251 ? 0.379 0.720 0.330 0.117  -0.035 -0.057 251 VAL DDD CG2 
13102 N N   . GLU D 252 ? 0.440 0.790 0.386 0.110  -0.027 -0.020 252 GLU DDD N   
13103 C CA  . GLU D 252 ? 0.492 0.846 0.437 0.108  -0.025 -0.007 252 GLU DDD CA  
13104 C C   . GLU D 252 ? 0.473 0.813 0.427 0.105  -0.025 0.000  252 GLU DDD C   
13105 O O   . GLU D 252 ? 0.457 0.797 0.412 0.104  -0.027 0.009  252 GLU DDD O   
13106 C CB  . GLU D 252 ? 0.544 0.906 0.485 0.107  -0.021 -0.005 252 GLU DDD CB  
13107 C CG  . GLU D 252 ? 0.602 0.971 0.543 0.105  -0.019 0.008  252 GLU DDD CG  
13108 C CD  . GLU D 252 ? 0.678 1.051 0.618 0.104  -0.014 0.009  252 GLU DDD CD  
13109 O OE1 . GLU D 252 ? 0.696 1.081 0.629 0.105  -0.012 0.003  252 GLU DDD OE1 
13110 O OE2 . GLU D 252 ? 0.694 1.059 0.641 0.101  -0.012 0.015  252 GLU DDD OE2 
13111 N N   . TYR D 253 ? 0.454 0.780 0.413 0.103  -0.024 -0.004 253 TYR DDD N   
13112 C CA  . TYR D 253 ? 0.406 0.718 0.374 0.100  -0.023 0.001  253 TYR DDD CA  
13113 C C   . TYR D 253 ? 0.390 0.696 0.362 0.100  -0.027 -0.000 253 TYR DDD C   
13114 O O   . TYR D 253 ? 0.365 0.667 0.343 0.099  -0.028 0.007  253 TYR DDD O   
13115 C CB  . TYR D 253 ? 0.412 0.713 0.384 0.099  -0.021 -0.004 253 TYR DDD CB  
13116 C CG  . TYR D 253 ? 0.412 0.700 0.393 0.095  -0.020 0.001  253 TYR DDD CG  
13117 C CD1 . TYR D 253 ? 0.406 0.682 0.392 0.094  -0.021 -0.003 253 TYR DDD CD1 
13118 C CD2 . TYR D 253 ? 0.391 0.678 0.375 0.093  -0.017 0.009  253 TYR DDD CD2 
13119 C CE1 . TYR D 253 ? 0.403 0.669 0.397 0.091  -0.020 0.001  253 TYR DDD CE1 
13120 C CE2 . TYR D 253 ? 0.398 0.675 0.391 0.090  -0.017 0.013  253 TYR DDD CE2 
13121 C CZ  . TYR D 253 ? 0.402 0.668 0.400 0.089  -0.018 0.008  253 TYR DDD CZ  
13122 O OH  . TYR D 253 ? 0.399 0.655 0.405 0.087  -0.017 0.011  253 TYR DDD OH  
13123 N N   . MET D 254 ? 0.373 0.678 0.344 0.102  -0.029 -0.010 254 MET DDD N   
13124 C CA  . MET D 254 ? 0.389 0.688 0.365 0.103  -0.032 -0.012 254 MET DDD CA  
13125 C C   . MET D 254 ? 0.406 0.714 0.380 0.104  -0.036 -0.005 254 MET DDD C   
13126 O O   . MET D 254 ? 0.398 0.699 0.379 0.103  -0.038 -0.002 254 MET DDD O   
13127 C CB  . MET D 254 ? 0.382 0.680 0.355 0.105  -0.034 -0.024 254 MET DDD CB  
13128 C CG  . MET D 254 ? 0.375 0.663 0.351 0.104  -0.031 -0.031 254 MET DDD CG  
13129 S SD  . MET D 254 ? 0.381 0.665 0.357 0.106  -0.034 -0.044 254 MET DDD SD  
13130 C CE  . MET D 254 ? 0.374 0.652 0.357 0.105  -0.037 -0.043 254 MET DDD CE  
13131 N N   . LYS D 255 ? 0.422 0.745 0.387 0.106  -0.036 -0.003 255 LYS DDD N   
13132 C CA  . LYS D 255 ? 0.456 0.790 0.419 0.107  -0.039 0.005  255 LYS DDD CA  
13133 C C   . LYS D 255 ? 0.417 0.747 0.385 0.104  -0.038 0.018  255 LYS DDD C   
13134 O O   . LYS D 255 ? 0.443 0.772 0.416 0.104  -0.042 0.023  255 LYS DDD O   
13135 C CB  . LYS D 255 ? 0.541 0.891 0.492 0.109  -0.039 0.006  255 LYS DDD CB  
13136 C CG  . LYS D 255 ? 0.591 0.950 0.535 0.112  -0.043 -0.004 255 LYS DDD CG  
13137 C CD  . LYS D 255 ? 0.681 1.058 0.615 0.114  -0.041 -0.005 255 LYS DDD CD  
13138 C CE  . LYS D 255 ? 0.730 1.118 0.658 0.117  -0.044 -0.015 255 LYS DDD CE  
13139 N NZ  . LYS D 255 ? 0.738 1.139 0.657 0.119  -0.041 -0.020 255 LYS DDD NZ  
13140 N N   . ALA D 256 ? 0.387 0.714 0.356 0.102  -0.034 0.022  256 ALA DDD N   
13141 C CA  . ALA D 256 ? 0.371 0.696 0.346 0.099  -0.033 0.033  256 ALA DDD CA  
13142 C C   . ALA D 256 ? 0.370 0.680 0.358 0.097  -0.034 0.034  256 ALA DDD C   
13143 O O   . ALA D 256 ? 0.358 0.666 0.354 0.095  -0.034 0.043  256 ALA DDD O   
13144 C CB  . ALA D 256 ? 0.361 0.688 0.335 0.097  -0.028 0.036  256 ALA DDD CB  
13145 N N   . THR D 257 ? 0.359 0.659 0.350 0.097  -0.034 0.023  257 THR DDD N   
13146 C CA  . THR D 257 ? 0.363 0.649 0.365 0.095  -0.034 0.022  257 THR DDD CA  
13147 C C   . THR D 257 ? 0.358 0.643 0.364 0.097  -0.039 0.019  257 THR DDD C   
13148 O O   . THR D 257 ? 0.354 0.629 0.371 0.095  -0.039 0.016  257 THR DDD O   
13149 C CB  . THR D 257 ? 0.367 0.642 0.372 0.094  -0.031 0.014  257 THR DDD CB  
13150 O OG1 . THR D 257 ? 0.361 0.637 0.359 0.096  -0.031 0.004  257 THR DDD OG1 
13151 C CG2 . THR D 257 ? 0.367 0.641 0.372 0.092  -0.027 0.019  257 THR DDD CG2 
13152 N N   . GLY D 258 ? 0.351 0.647 0.350 0.100  -0.042 0.018  258 GLY DDD N   
13153 C CA  . GLY D 258 ? 0.337 0.633 0.340 0.101  -0.047 0.017  258 GLY DDD CA  
13154 C C   . GLY D 258 ? 0.350 0.648 0.348 0.104  -0.049 0.006  258 GLY DDD C   
13155 O O   . GLY D 258 ? 0.352 0.652 0.355 0.105  -0.054 0.004  258 GLY DDD O   
13156 N N   . THR D 259 ? 0.388 0.687 0.380 0.105  -0.046 -0.003 259 THR DDD N   
13157 C CA  . THR D 259 ? 0.403 0.705 0.392 0.107  -0.049 -0.013 259 THR DDD CA  
13158 C C   . THR D 259 ? 0.418 0.736 0.397 0.110  -0.052 -0.012 259 THR DDD C   
13159 O O   . THR D 259 ? 0.423 0.750 0.394 0.111  -0.050 -0.007 259 THR DDD O   
13160 C CB  . THR D 259 ? 0.405 0.700 0.392 0.107  -0.045 -0.022 259 THR DDD CB  
13161 O OG1 . THR D 259 ? 0.400 0.682 0.396 0.103  -0.042 -0.022 259 THR DDD OG1 
13162 C CG2 . THR D 259 ? 0.399 0.696 0.385 0.109  -0.047 -0.034 259 THR DDD CG2 
13163 N N   . LYS D 260 ? 0.426 0.748 0.406 0.113  -0.057 -0.016 260 LYS DDD N   
13164 C CA  . LYS D 260 ? 0.479 0.817 0.449 0.116  -0.060 -0.016 260 LYS DDD CA  
13165 C C   . LYS D 260 ? 0.498 0.840 0.463 0.118  -0.060 -0.029 260 LYS DDD C   
13166 O O   . LYS D 260 ? 0.463 0.795 0.435 0.118  -0.060 -0.037 260 LYS DDD O   
13167 C CB  . LYS D 260 ? 0.475 0.815 0.449 0.117  -0.067 -0.013 260 LYS DDD CB  
13168 C CG  . LYS D 260 ? 0.488 0.828 0.465 0.115  -0.068 0.001  260 LYS DDD CG  
13169 C CD  . LYS D 260 ? 0.503 0.839 0.490 0.116  -0.074 0.004  260 LYS DDD CD  
13170 C CE  . LYS D 260 ? 0.507 0.828 0.508 0.114  -0.073 -0.003 260 LYS DDD CE  
13171 N NZ  . LYS D 260 ? 0.520 0.840 0.529 0.116  -0.079 -0.004 260 LYS DDD NZ  
13172 N N   . PHE D 261 ? 0.519 0.876 0.474 0.120  -0.060 -0.029 261 PHE DDD N   
13173 C CA  . PHE D 261 ? 0.555 0.919 0.504 0.123  -0.060 -0.042 261 PHE DDD CA  
13174 C C   . PHE D 261 ? 0.539 0.919 0.481 0.126  -0.065 -0.044 261 PHE DDD C   
13175 O O   . PHE D 261 ? 0.524 0.916 0.456 0.126  -0.065 -0.036 261 PHE DDD O   
13176 C CB  . PHE D 261 ? 0.588 0.956 0.532 0.122  -0.055 -0.042 261 PHE DDD CB  
13177 C CG  . PHE D 261 ? 0.604 0.956 0.555 0.120  -0.051 -0.043 261 PHE DDD CG  
13178 C CD1 . PHE D 261 ? 0.591 0.934 0.546 0.116  -0.048 -0.033 261 PHE DDD CD1 
13179 C CD2 . PHE D 261 ? 0.597 0.942 0.551 0.120  -0.049 -0.054 261 PHE DDD CD2 
13180 C CE1 . PHE D 261 ? 0.580 0.910 0.541 0.114  -0.044 -0.034 261 PHE DDD CE1 
13181 C CE2 . PHE D 261 ? 0.616 0.947 0.576 0.118  -0.046 -0.054 261 PHE DDD CE2 
13182 C CZ  . PHE D 261 ? 0.596 0.921 0.559 0.114  -0.043 -0.044 261 PHE DDD CZ  
13183 N N   . LEU D 262 ? 0.517 0.897 0.462 0.129  -0.068 -0.055 262 LEU DDD N   
13184 C CA  . LEU D 262 ? 0.514 0.910 0.452 0.133  -0.073 -0.061 262 LEU DDD CA  
13185 C C   . LEU D 262 ? 0.516 0.919 0.451 0.134  -0.070 -0.073 262 LEU DDD C   
13186 O O   . LEU D 262 ? 0.483 0.877 0.426 0.135  -0.070 -0.083 262 LEU DDD O   
13187 C CB  . LEU D 262 ? 0.470 0.861 0.416 0.134  -0.078 -0.068 262 LEU DDD CB  
13188 C CG  . LEU D 262 ? 0.460 0.840 0.415 0.132  -0.080 -0.059 262 LEU DDD CG  
13189 C CD1 . LEU D 262 ? 0.479 0.854 0.443 0.134  -0.085 -0.067 262 LEU DDD CD1 
13190 C CD2 . LEU D 262 ? 0.455 0.844 0.402 0.132  -0.083 -0.046 262 LEU DDD CD2 
13191 N N   . VAL D 263 ? 0.544 0.961 0.467 0.135  -0.069 -0.071 263 VAL DDD N   
13192 C CA  . VAL D 263 ? 0.578 1.004 0.498 0.137  -0.066 -0.081 263 VAL DDD CA  
13193 C C   . VAL D 263 ? 0.594 1.034 0.510 0.141  -0.070 -0.092 263 VAL DDD C   
13194 O O   . VAL D 263 ? 0.617 1.069 0.525 0.142  -0.074 -0.088 263 VAL DDD O   
13195 C CB  . VAL D 263 ? 0.575 1.010 0.486 0.135  -0.061 -0.073 263 VAL DDD CB  
13196 C CG1 . VAL D 263 ? 0.566 1.008 0.475 0.136  -0.057 -0.083 263 VAL DDD CG1 
13197 C CG2 . VAL D 263 ? 0.581 1.002 0.496 0.131  -0.057 -0.061 263 VAL DDD CG2 
13198 N N   . GLY D 264 ? 0.607 1.045 0.530 0.143  -0.070 -0.106 264 GLY DDD N   
13199 C CA  . GLY D 264 ? 0.625 1.076 0.546 0.147  -0.074 -0.119 264 GLY DDD CA  
13200 C C   . GLY D 264 ? 0.636 1.084 0.562 0.148  -0.080 -0.122 264 GLY DDD C   
13201 O O   . GLY D 264 ? 0.627 1.088 0.549 0.151  -0.085 -0.130 264 GLY DDD O   
13202 N N   . VAL D 265 ? 0.634 1.065 0.569 0.146  -0.081 -0.116 265 VAL DDD N   
13203 C CA  . VAL D 265 ? 0.646 1.073 0.587 0.147  -0.086 -0.116 265 VAL DDD CA  
13204 C C   . VAL D 265 ? 0.653 1.060 0.608 0.146  -0.085 -0.122 265 VAL DDD C   
13205 O O   . VAL D 265 ? 0.709 1.104 0.668 0.142  -0.081 -0.116 265 VAL DDD O   
13206 C CB  . VAL D 265 ? 0.651 1.077 0.587 0.145  -0.088 -0.101 265 VAL DDD CB  
13207 C CG1 . VAL D 265 ? 0.657 1.076 0.602 0.146  -0.093 -0.102 265 VAL DDD CG1 
13208 C CG2 . VAL D 265 ? 0.675 1.120 0.597 0.146  -0.090 -0.095 265 VAL DDD CG2 
13209 N N   . VAL D 266 ? 0.651 1.058 0.614 0.148  -0.090 -0.132 266 VAL DDD N   
13210 C CA  . VAL D 266 ? 0.659 1.049 0.637 0.146  -0.089 -0.137 266 VAL DDD CA  
13211 C C   . VAL D 266 ? 0.620 1.009 0.604 0.148  -0.095 -0.139 266 VAL DDD C   
13212 O O   . VAL D 266 ? 0.646 1.049 0.625 0.151  -0.100 -0.140 266 VAL DDD O   
13213 C CB  . VAL D 266 ? 0.723 1.111 0.706 0.148  -0.088 -0.150 266 VAL DDD CB  
13214 C CG1 . VAL D 266 ? 0.739 1.127 0.717 0.146  -0.082 -0.147 266 VAL DDD CG1 
13215 C CG2 . VAL D 266 ? 0.725 1.128 0.708 0.152  -0.093 -0.162 266 VAL DDD CG2 
13216 N N   . PRO D 267 ? 0.599 0.972 0.596 0.145  -0.094 -0.139 267 PRO DDD N   
13217 C CA  . PRO D 267 ? 0.588 0.959 0.593 0.147  -0.099 -0.143 267 PRO DDD CA  
13218 C C   . PRO D 267 ? 0.581 0.960 0.590 0.151  -0.104 -0.157 267 PRO DDD C   
13219 O O   . PRO D 267 ? 0.568 0.946 0.580 0.151  -0.101 -0.166 267 PRO DDD O   
13220 C CB  . PRO D 267 ? 0.570 0.922 0.587 0.143  -0.096 -0.142 267 PRO DDD CB  
13221 C CG  . PRO D 267 ? 0.589 0.933 0.602 0.140  -0.090 -0.134 267 PRO DDD CG  
13222 C CD  . PRO D 267 ? 0.580 0.936 0.582 0.141  -0.088 -0.136 267 PRO DDD CD  
13223 N N   . ILE D 268 ? 0.583 0.972 0.593 0.153  -0.110 -0.160 268 ILE DDD N   
13224 C CA  . ILE D 268 ? 0.596 0.992 0.613 0.157  -0.115 -0.174 268 ILE DDD CA  
13225 C C   . ILE D 268 ? 0.580 0.967 0.611 0.157  -0.119 -0.176 268 ILE DDD C   
13226 O O   . ILE D 268 ? 0.597 0.985 0.637 0.159  -0.122 -0.189 268 ILE DDD O   
13227 C CB  . ILE D 268 ? 0.610 1.027 0.615 0.161  -0.121 -0.176 268 ILE DDD CB  
13228 C CG1 . ILE D 268 ? 0.628 1.050 0.625 0.161  -0.125 -0.165 268 ILE DDD CG1 
13229 C CG2 . ILE D 268 ? 0.603 1.030 0.596 0.162  -0.117 -0.177 268 ILE DDD CG2 
13230 C CD1 . ILE D 268 ? 0.680 1.124 0.665 0.165  -0.131 -0.167 268 ILE DDD CD1 
13231 N N   . ASN D 269 ? 0.544 0.921 0.577 0.154  -0.118 -0.166 269 ASN DDD N   
13232 C CA  . ASN D 269 ? 0.558 0.927 0.607 0.154  -0.121 -0.168 269 ASN DDD CA  
13233 C C   . ASN D 269 ? 0.545 0.899 0.598 0.149  -0.117 -0.158 269 ASN DDD C   
13234 O O   . ASN D 269 ? 0.571 0.927 0.614 0.148  -0.115 -0.146 269 ASN DDD O   
13235 C CB  . ASN D 269 ? 0.578 0.958 0.626 0.157  -0.129 -0.170 269 ASN DDD CB  
13236 C CG  . ASN D 269 ? 0.552 0.924 0.617 0.157  -0.133 -0.175 269 ASN DDD CG  
13237 O OD1 . ASN D 269 ? 0.574 0.943 0.643 0.156  -0.136 -0.168 269 ASN DDD OD1 
13238 N ND2 . ASN D 269 ? 0.530 0.897 0.607 0.158  -0.132 -0.188 269 ASN DDD ND2 
13239 N N   . ILE D 270 ? 0.530 0.870 0.597 0.147  -0.115 -0.162 270 ILE DDD N   
13240 C CA  . ILE D 270 ? 0.566 0.892 0.640 0.142  -0.110 -0.154 270 ILE DDD CA  
13241 C C   . ILE D 270 ? 0.587 0.907 0.677 0.142  -0.113 -0.158 270 ILE DDD C   
13242 O O   . ILE D 270 ? 0.618 0.934 0.719 0.142  -0.113 -0.169 270 ILE DDD O   
13243 C CB  . ILE D 270 ? 0.530 0.844 0.604 0.138  -0.102 -0.154 270 ILE DDD CB  
13244 C CG1 . ILE D 270 ? 0.537 0.857 0.596 0.139  -0.099 -0.148 270 ILE DDD CG1 
13245 C CG2 . ILE D 270 ? 0.513 0.812 0.596 0.134  -0.097 -0.149 270 ILE DDD CG2 
13246 C CD1 . ILE D 270 ? 0.506 0.817 0.564 0.136  -0.093 -0.149 270 ILE DDD CD1 
13247 N N   . GLU D 271 ? 0.616 0.937 0.709 0.142  -0.117 -0.150 271 GLU DDD N   
13248 C CA  . GLU D 271 ? 0.659 0.975 0.767 0.142  -0.120 -0.154 271 GLU DDD CA  
13249 C C   . GLU D 271 ? 0.655 0.960 0.771 0.138  -0.117 -0.145 271 GLU DDD C   
13250 O O   . GLU D 271 ? 0.627 0.932 0.734 0.136  -0.115 -0.135 271 GLU DDD O   
13251 C CB  . GLU D 271 ? 0.709 1.038 0.815 0.146  -0.130 -0.153 271 GLU DDD CB  
13252 C CG  . GLU D 271 ? 0.794 1.136 0.895 0.151  -0.135 -0.162 271 GLU DDD CG  
13253 C CD  . GLU D 271 ? 0.852 1.210 0.945 0.155  -0.144 -0.159 271 GLU DDD CD  
13254 O OE1 . GLU D 271 ? 0.880 1.240 0.966 0.154  -0.145 -0.146 271 GLU DDD OE1 
13255 O OE2 . GLU D 271 ? 0.844 1.212 0.938 0.159  -0.150 -0.168 271 GLU DDD OE2 
13256 N N   . LYS D 272 ? 0.690 0.986 0.823 0.136  -0.116 -0.150 272 LYS DDD N   
13257 C CA  . LYS D 272 ? 0.734 1.021 0.877 0.132  -0.114 -0.144 272 LYS DDD CA  
13258 C C   . LYS D 272 ? 0.746 1.039 0.893 0.135  -0.122 -0.139 272 LYS DDD C   
13259 O O   . LYS D 272 ? 0.711 1.008 0.868 0.138  -0.128 -0.147 272 LYS DDD O   
13260 C CB  . LYS D 272 ? 0.762 1.036 0.921 0.129  -0.109 -0.152 272 LYS DDD CB  
13261 C CG  . LYS D 272 ? 0.814 1.078 0.981 0.124  -0.103 -0.146 272 LYS DDD CG  
13262 C CD  . LYS D 272 ? 0.858 1.115 1.014 0.120  -0.095 -0.141 272 LYS DDD CD  
13263 C CE  . LYS D 272 ? 0.875 1.118 1.040 0.115  -0.087 -0.142 272 LYS DDD CE  
13264 N NZ  . LYS D 272 ? 0.875 1.113 1.048 0.113  -0.084 -0.152 272 LYS DDD NZ  
13265 N N   . VAL D 273 ? 0.771 1.067 0.912 0.135  -0.123 -0.127 273 VAL DDD N   
13266 C CA  . VAL D 273 ? 0.827 1.127 0.974 0.137  -0.131 -0.121 273 VAL DDD CA  
13267 C C   . VAL D 273 ? 0.815 1.103 0.975 0.132  -0.127 -0.116 273 VAL DDD C   
13268 O O   . VAL D 273 ? 0.766 1.051 0.920 0.130  -0.124 -0.106 273 VAL DDD O   
13269 C CB  . VAL D 273 ? 0.865 1.177 0.996 0.139  -0.136 -0.110 273 VAL DDD CB  
13270 C CG1 . VAL D 273 ? 0.890 1.205 1.027 0.140  -0.143 -0.102 273 VAL DDD CG1 
13271 C CG2 . VAL D 273 ? 0.880 1.205 0.999 0.143  -0.141 -0.117 273 VAL DDD CG2 
13272 N N   . ASN D 274 ? 0.831 1.113 1.009 0.131  -0.127 -0.124 274 ASN DDD N   
13273 C CA  . ASN D 274 ? 0.831 1.101 1.025 0.127  -0.123 -0.123 274 ASN DDD CA  
13274 C C   . ASN D 274 ? 0.809 1.070 0.999 0.123  -0.112 -0.124 274 ASN DDD C   
13275 O O   . ASN D 274 ? 0.801 1.060 0.990 0.122  -0.108 -0.133 274 ASN DDD O   
13276 C CB  . ASN D 274 ? 0.833 1.105 1.031 0.127  -0.127 -0.111 274 ASN DDD CB  
13277 C CG  . ASN D 274 ? 0.848 1.128 1.053 0.132  -0.138 -0.111 274 ASN DDD CG  
13278 O OD1 . ASN D 274 ? 0.859 1.148 1.053 0.134  -0.145 -0.102 274 ASN DDD OD1 
13279 N ND2 . ASN D 274 ? 0.806 1.083 1.029 0.132  -0.140 -0.120 274 ASN DDD ND2 
13280 N N   . GLU D 275 ? 0.819 1.075 1.006 0.120  -0.107 -0.116 275 GLU DDD N   
13281 C CA  . GLU D 275 ? 0.857 1.104 1.040 0.115  -0.097 -0.116 275 GLU DDD CA  
13282 C C   . GLU D 275 ? 0.758 1.009 0.921 0.116  -0.096 -0.110 275 GLU DDD C   
13283 O O   . GLU D 275 ? 0.733 0.978 0.890 0.113  -0.088 -0.111 275 GLU DDD O   
13284 C CB  . GLU D 275 ? 0.927 1.165 1.121 0.111  -0.093 -0.112 275 GLU DDD CB  
13285 C CG  . GLU D 275 ? 1.006 1.248 1.198 0.112  -0.097 -0.100 275 GLU DDD CG  
13286 C CD  . GLU D 275 ? 1.036 1.283 1.240 0.115  -0.106 -0.097 275 GLU DDD CD  
13287 O OE1 . GLU D 275 ? 1.051 1.298 1.268 0.116  -0.110 -0.105 275 GLU DDD OE1 
13288 O OE2 . GLU D 275 ? 1.042 1.293 1.242 0.116  -0.110 -0.086 275 GLU DDD OE2 
13289 N N   . ASN D 276 ? 0.673 0.936 0.826 0.120  -0.102 -0.104 276 ASN DDD N   
13290 C CA  . ASN D 276 ? 0.674 0.942 0.807 0.121  -0.101 -0.098 276 ASN DDD CA  
13291 C C   . ASN D 276 ? 0.647 0.922 0.771 0.124  -0.103 -0.106 276 ASN DDD C   
13292 O O   . ASN D 276 ? 0.609 0.885 0.743 0.125  -0.106 -0.115 276 ASN DDD O   
13293 C CB  . ASN D 276 ? 0.695 0.971 0.821 0.123  -0.106 -0.086 276 ASN DDD CB  
13294 C CG  . ASN D 276 ? 0.687 0.957 0.820 0.120  -0.104 -0.077 276 ASN DDD CG  
13295 O OD1 . ASN D 276 ? 0.707 0.967 0.842 0.116  -0.096 -0.078 276 ASN DDD OD1 
13296 N ND2 . ASN D 276 ? 0.654 0.929 0.789 0.121  -0.110 -0.068 276 ASN DDD ND2 
13297 N N   . ILE D 277 ? 0.621 0.901 0.729 0.124  -0.100 -0.104 277 ILE DDD N   
13298 C CA  . ILE D 277 ? 0.616 0.904 0.716 0.128  -0.102 -0.111 277 ILE DDD CA  
13299 C C   . ILE D 277 ? 0.614 0.916 0.700 0.131  -0.107 -0.105 277 ILE DDD C   
13300 O O   . ILE D 277 ? 0.577 0.880 0.651 0.130  -0.104 -0.097 277 ILE DDD O   
13301 C CB  . ILE D 277 ? 0.607 0.887 0.702 0.125  -0.094 -0.116 277 ILE DDD CB  
13302 C CG1 . ILE D 277 ? 0.617 0.884 0.726 0.121  -0.090 -0.123 277 ILE DDD CG1 
13303 C CG2 . ILE D 277 ? 0.586 0.875 0.673 0.128  -0.096 -0.123 277 ILE DDD CG2 
13304 C CD1 . ILE D 277 ? 0.600 0.857 0.706 0.117  -0.082 -0.123 277 ILE DDD CD1 
13305 N N   . LYS D 278 ? 0.599 0.911 0.685 0.135  -0.114 -0.109 278 LYS DDD N   
13306 C CA  . LYS D 278 ? 0.562 0.889 0.633 0.139  -0.120 -0.105 278 LYS DDD CA  
13307 C C   . LYS D 278 ? 0.518 0.851 0.578 0.140  -0.117 -0.113 278 LYS DDD C   
13308 O O   . LYS D 278 ? 0.459 0.791 0.526 0.141  -0.117 -0.125 278 LYS DDD O   
13309 C CB  . LYS D 278 ? 0.592 0.928 0.668 0.142  -0.129 -0.108 278 LYS DDD CB  
13310 C CG  . LYS D 278 ? 0.630 0.983 0.692 0.146  -0.135 -0.102 278 LYS DDD CG  
13311 C CD  . LYS D 278 ? 0.647 1.007 0.714 0.149  -0.145 -0.105 278 LYS DDD CD  
13312 C CE  . LYS D 278 ? 0.689 1.066 0.739 0.153  -0.151 -0.102 278 LYS DDD CE  
13313 N NZ  . LYS D 278 ? 0.713 1.099 0.768 0.157  -0.161 -0.106 278 LYS DDD NZ  
13314 N N   . VAL D 279 ? 0.511 0.849 0.558 0.140  -0.114 -0.107 279 VAL DDD N   
13315 C CA  . VAL D 279 ? 0.505 0.851 0.542 0.141  -0.111 -0.113 279 VAL DDD CA  
13316 C C   . VAL D 279 ? 0.498 0.862 0.522 0.145  -0.117 -0.112 279 VAL DDD C   
13317 O O   . VAL D 279 ? 0.504 0.873 0.519 0.145  -0.118 -0.100 279 VAL DDD O   
13318 C CB  . VAL D 279 ? 0.495 0.833 0.527 0.138  -0.103 -0.109 279 VAL DDD CB  
13319 C CG1 . VAL D 279 ? 0.503 0.849 0.523 0.140  -0.101 -0.114 279 VAL DDD CG1 
13320 C CG2 . VAL D 279 ? 0.490 0.811 0.534 0.134  -0.098 -0.112 279 VAL DDD CG2 
13321 N N   . SER D 280 ? 0.489 0.861 0.510 0.148  -0.120 -0.123 280 SER DDD N   
13322 C CA  . SER D 280 ? 0.509 0.900 0.516 0.152  -0.124 -0.123 280 SER DDD CA  
13323 C C   . SER D 280 ? 0.502 0.898 0.499 0.152  -0.119 -0.127 280 SER DDD C   
13324 O O   . SER D 280 ? 0.498 0.888 0.503 0.152  -0.116 -0.137 280 SER DDD O   
13325 C CB  . SER D 280 ? 0.503 0.902 0.515 0.156  -0.132 -0.133 280 SER DDD CB  
13326 O OG  . SER D 280 ? 0.466 0.863 0.486 0.156  -0.137 -0.127 280 SER DDD OG  
13327 N N   . PHE D 281 ? 0.524 0.931 0.507 0.152  -0.118 -0.119 281 PHE DDD N   
13328 C CA  . PHE D 281 ? 0.569 0.980 0.543 0.152  -0.112 -0.121 281 PHE DDD CA  
13329 C C   . PHE D 281 ? 0.588 1.019 0.552 0.156  -0.116 -0.129 281 PHE DDD C   
13330 O O   . PHE D 281 ? 0.599 1.041 0.559 0.158  -0.122 -0.129 281 PHE DDD O   
13331 C CB  . PHE D 281 ? 0.590 1.001 0.555 0.149  -0.108 -0.106 281 PHE DDD CB  
13332 C CG  . PHE D 281 ? 0.582 0.975 0.557 0.145  -0.103 -0.100 281 PHE DDD CG  
13333 C CD1 . PHE D 281 ? 0.571 0.954 0.550 0.143  -0.097 -0.104 281 PHE DDD CD1 
13334 C CD2 . PHE D 281 ? 0.570 0.955 0.550 0.143  -0.105 -0.090 281 PHE DDD CD2 
13335 C CE1 . PHE D 281 ? 0.572 0.938 0.558 0.139  -0.093 -0.099 281 PHE DDD CE1 
13336 C CE2 . PHE D 281 ? 0.590 0.959 0.579 0.139  -0.101 -0.085 281 PHE DDD CE2 
13337 C CZ  . PHE D 281 ? 0.572 0.932 0.564 0.137  -0.094 -0.089 281 PHE DDD CZ  
13338 N N   . SER D 282 ? 0.608 1.042 0.568 0.156  -0.111 -0.136 282 SER DDD N   
13339 C CA  . SER D 282 ? 0.635 1.087 0.588 0.159  -0.113 -0.147 282 SER DDD CA  
13340 C C   . SER D 282 ? 0.672 1.143 0.609 0.160  -0.115 -0.140 282 SER DDD C   
13341 O O   . SER D 282 ? 0.720 1.206 0.650 0.164  -0.118 -0.149 282 SER DDD O   
13342 C CB  . SER D 282 ? 0.628 1.078 0.583 0.159  -0.107 -0.154 282 SER DDD CB  
13343 O OG  . SER D 282 ? 0.631 1.081 0.576 0.156  -0.102 -0.143 282 SER DDD OG  
13344 N N   . ASP D 283 ? 0.684 1.153 0.614 0.158  -0.114 -0.124 283 ASP DDD N   
13345 C CA  . ASP D 283 ? 0.678 1.163 0.592 0.158  -0.116 -0.115 283 ASP DDD CA  
13346 C C   . ASP D 283 ? 0.674 1.162 0.588 0.159  -0.124 -0.109 283 ASP DDD C   
13347 O O   . ASP D 283 ? 0.659 1.158 0.560 0.159  -0.126 -0.098 283 ASP DDD O   
13348 C CB  . ASP D 283 ? 0.660 1.142 0.567 0.154  -0.109 -0.101 283 ASP DDD CB  
13349 C CG  . ASP D 283 ? 0.644 1.110 0.559 0.151  -0.109 -0.088 283 ASP DDD CG  
13350 O OD1 . ASP D 283 ? 0.595 1.048 0.522 0.151  -0.112 -0.091 283 ASP DDD OD1 
13351 O OD2 . ASP D 283 ? 0.633 1.098 0.541 0.148  -0.105 -0.075 283 ASP DDD OD2 
13352 N N   . GLY D 284 ? 0.665 1.143 0.592 0.160  -0.128 -0.115 284 GLY DDD N   
13353 C CA  . GLY D 284 ? 0.685 1.164 0.615 0.162  -0.136 -0.111 284 GLY DDD CA  
13354 C C   . GLY D 284 ? 0.685 1.151 0.620 0.158  -0.136 -0.095 284 GLY DDD C   
13355 O O   . GLY D 284 ? 0.729 1.195 0.667 0.159  -0.143 -0.091 284 GLY DDD O   
13356 N N   . SER D 285 ? 0.663 1.119 0.600 0.155  -0.128 -0.088 285 SER DDD N   
13357 C CA  . SER D 285 ? 0.660 1.102 0.604 0.151  -0.128 -0.074 285 SER DDD CA  
13358 C C   . SER D 285 ? 0.645 1.070 0.608 0.151  -0.127 -0.080 285 SER DDD C   
13359 O O   . SER D 285 ? 0.628 1.048 0.597 0.152  -0.125 -0.093 285 SER DDD O   
13360 C CB  . SER D 285 ? 0.646 1.086 0.584 0.148  -0.120 -0.064 285 SER DDD CB  
13361 O OG  . SER D 285 ? 0.603 1.031 0.547 0.147  -0.113 -0.071 285 SER DDD OG  
13362 N N   . VAL D 286 ? 0.661 1.076 0.633 0.149  -0.130 -0.071 286 VAL DDD N   
13363 C CA  . VAL D 286 ? 0.650 1.049 0.640 0.148  -0.130 -0.075 286 VAL DDD CA  
13364 C C   . VAL D 286 ? 0.644 1.030 0.641 0.144  -0.125 -0.064 286 VAL DDD C   
13365 O O   . VAL D 286 ? 0.634 1.024 0.622 0.142  -0.125 -0.051 286 VAL DDD O   
13366 C CB  . VAL D 286 ? 0.622 1.024 0.618 0.150  -0.139 -0.077 286 VAL DDD CB  
13367 C CG1 . VAL D 286 ? 0.613 0.999 0.629 0.149  -0.139 -0.079 286 VAL DDD CG1 
13368 C CG2 . VAL D 286 ? 0.626 1.040 0.618 0.154  -0.143 -0.091 286 VAL DDD CG2 
13369 N N   . GLU D 287 ? 0.631 1.001 0.641 0.141  -0.121 -0.069 287 GLU DDD N   
13370 C CA  . GLU D 287 ? 0.617 0.974 0.634 0.137  -0.116 -0.059 287 GLU DDD CA  
13371 C C   . GLU D 287 ? 0.579 0.920 0.613 0.135  -0.114 -0.067 287 GLU DDD C   
13372 O O   . GLU D 287 ? 0.591 0.930 0.627 0.136  -0.112 -0.079 287 GLU DDD O   
13373 C CB  . GLU D 287 ? 0.635 0.991 0.642 0.135  -0.109 -0.054 287 GLU DDD CB  
13374 C CG  . GLU D 287 ? 0.650 0.998 0.662 0.131  -0.106 -0.042 287 GLU DDD CG  
13375 C CD  . GLU D 287 ? 0.666 1.015 0.668 0.129  -0.100 -0.036 287 GLU DDD CD  
13376 O OE1 . GLU D 287 ? 0.680 1.038 0.670 0.131  -0.098 -0.040 287 GLU DDD OE1 
13377 O OE2 . GLU D 287 ? 0.669 1.010 0.676 0.126  -0.097 -0.027 287 GLU DDD OE2 
13378 N N   . GLU D 288 ? 0.546 0.878 0.591 0.133  -0.114 -0.061 288 GLU DDD N   
13379 C CA  . GLU D 288 ? 0.540 0.857 0.601 0.131  -0.111 -0.067 288 GLU DDD CA  
13380 C C   . GLU D 288 ? 0.507 0.814 0.569 0.126  -0.102 -0.065 288 GLU DDD C   
13381 O O   . GLU D 288 ? 0.473 0.781 0.529 0.125  -0.100 -0.054 288 GLU DDD O   
13382 C CB  . GLU D 288 ? 0.556 0.871 0.631 0.130  -0.116 -0.061 288 GLU DDD CB  
13383 C CG  . GLU D 288 ? 0.580 0.902 0.659 0.134  -0.125 -0.066 288 GLU DDD CG  
13384 C CD  . GLU D 288 ? 0.599 0.914 0.697 0.133  -0.129 -0.065 288 GLU DDD CD  
13385 O OE1 . GLU D 288 ? 0.586 0.889 0.695 0.130  -0.123 -0.065 288 GLU DDD OE1 
13386 O OE2 . GLU D 288 ? 0.589 0.910 0.690 0.136  -0.137 -0.066 288 GLU DDD OE2 
13387 N N   . PHE D 289 ? 0.494 0.791 0.563 0.125  -0.098 -0.074 289 PHE DDD N   
13388 C CA  . PHE D 289 ? 0.490 0.775 0.560 0.120  -0.090 -0.073 289 PHE DDD CA  
13389 C C   . PHE D 289 ? 0.466 0.739 0.552 0.118  -0.087 -0.080 289 PHE DDD C   
13390 O O   . PHE D 289 ? 0.427 0.701 0.521 0.120  -0.091 -0.088 289 PHE DDD O   
13391 C CB  . PHE D 289 ? 0.493 0.780 0.553 0.120  -0.085 -0.078 289 PHE DDD CB  
13392 C CG  . PHE D 289 ? 0.511 0.810 0.555 0.123  -0.087 -0.073 289 PHE DDD CG  
13393 C CD1 . PHE D 289 ? 0.516 0.828 0.555 0.127  -0.092 -0.078 289 PHE DDD CD1 
13394 C CD2 . PHE D 289 ? 0.503 0.803 0.539 0.121  -0.083 -0.064 289 PHE DDD CD2 
13395 C CE1 . PHE D 289 ? 0.534 0.858 0.558 0.129  -0.093 -0.075 289 PHE DDD CE1 
13396 C CE2 . PHE D 289 ? 0.502 0.815 0.525 0.124  -0.085 -0.060 289 PHE DDD CE2 
13397 C CZ  . PHE D 289 ? 0.520 0.845 0.536 0.127  -0.089 -0.066 289 PHE DDD CZ  
13398 N N   . GLU D 290 ? 0.490 0.753 0.581 0.114  -0.081 -0.077 290 GLU DDD N   
13399 C CA  . GLU D 290 ? 0.480 0.730 0.584 0.110  -0.077 -0.084 290 GLU DDD CA  
13400 C C   . GLU D 290 ? 0.455 0.701 0.555 0.109  -0.073 -0.093 290 GLU DDD C   
13401 O O   . GLU D 290 ? 0.451 0.692 0.561 0.108  -0.072 -0.101 290 GLU DDD O   
13402 C CB  . GLU D 290 ? 0.496 0.738 0.606 0.107  -0.073 -0.078 290 GLU DDD CB  
13403 C CG  . GLU D 290 ? 0.549 0.782 0.675 0.103  -0.070 -0.084 290 GLU DDD CG  
13404 C CD  . GLU D 290 ? 0.590 0.815 0.725 0.100  -0.067 -0.079 290 GLU DDD CD  
13405 O OE1 . GLU D 290 ? 0.609 0.826 0.751 0.096  -0.061 -0.085 290 GLU DDD OE1 
13406 O OE2 . GLU D 290 ? 0.615 0.844 0.750 0.101  -0.070 -0.070 290 GLU DDD OE2 
13407 N N   . THR D 291 ? 0.416 0.664 0.503 0.109  -0.070 -0.090 291 THR DDD N   
13408 C CA  . THR D 291 ? 0.403 0.647 0.486 0.108  -0.065 -0.097 291 THR DDD CA  
13409 C C   . THR D 291 ? 0.402 0.656 0.472 0.112  -0.068 -0.098 291 THR DDD C   
13410 O O   . THR D 291 ? 0.387 0.648 0.448 0.113  -0.069 -0.090 291 THR DDD O   
13411 C CB  . THR D 291 ? 0.387 0.620 0.468 0.103  -0.059 -0.094 291 THR DDD CB  
13412 O OG1 . THR D 291 ? 0.385 0.610 0.478 0.100  -0.056 -0.093 291 THR DDD OG1 
13413 C CG2 . THR D 291 ? 0.377 0.604 0.454 0.102  -0.054 -0.100 291 THR DDD CG2 
13414 N N   . VAL D 292 ? 0.390 0.644 0.460 0.113  -0.068 -0.107 292 VAL DDD N   
13415 C CA  . VAL D 292 ? 0.398 0.660 0.457 0.116  -0.069 -0.110 292 VAL DDD CA  
13416 C C   . VAL D 292 ? 0.380 0.634 0.439 0.114  -0.065 -0.115 292 VAL DDD C   
13417 O O   . VAL D 292 ? 0.340 0.587 0.409 0.112  -0.064 -0.122 292 VAL DDD O   
13418 C CB  . VAL D 292 ? 0.424 0.698 0.484 0.121  -0.076 -0.117 292 VAL DDD CB  
13419 C CG1 . VAL D 292 ? 0.435 0.717 0.485 0.124  -0.076 -0.121 292 VAL DDD CG1 
13420 C CG2 . VAL D 292 ? 0.443 0.726 0.503 0.123  -0.081 -0.110 292 VAL DDD CG2 
13421 N N   . LEU D 293 ? 0.401 0.656 0.450 0.113  -0.062 -0.112 293 LEU DDD N   
13422 C CA  . LEU D 293 ? 0.411 0.657 0.459 0.111  -0.058 -0.115 293 LEU DDD CA  
13423 C C   . LEU D 293 ? 0.421 0.676 0.462 0.114  -0.059 -0.119 293 LEU DDD C   
13424 O O   . LEU D 293 ? 0.421 0.686 0.453 0.116  -0.060 -0.114 293 LEU DDD O   
13425 C CB  . LEU D 293 ? 0.448 0.687 0.492 0.107  -0.053 -0.107 293 LEU DDD CB  
13426 C CG  . LEU D 293 ? 0.458 0.686 0.501 0.104  -0.048 -0.109 293 LEU DDD CG  
13427 C CD1 . LEU D 293 ? 0.450 0.667 0.494 0.099  -0.044 -0.103 293 LEU DDD CD1 
13428 C CD2 . LEU D 293 ? 0.457 0.690 0.493 0.106  -0.048 -0.110 293 LEU DDD CD2 
13429 N N   . TYR D 294 ? 0.439 0.692 0.485 0.115  -0.060 -0.128 294 TYR DDD N   
13430 C CA  . TYR D 294 ? 0.463 0.723 0.504 0.118  -0.062 -0.134 294 TYR DDD CA  
13431 C C   . TYR D 294 ? 0.462 0.715 0.500 0.115  -0.058 -0.132 294 TYR DDD C   
13432 O O   . TYR D 294 ? 0.433 0.673 0.477 0.112  -0.055 -0.134 294 TYR DDD O   
13433 C CB  . TYR D 294 ? 0.492 0.755 0.542 0.120  -0.065 -0.145 294 TYR DDD CB  
13434 C CG  . TYR D 294 ? 0.503 0.780 0.552 0.125  -0.071 -0.149 294 TYR DDD CG  
13435 C CD1 . TYR D 294 ? 0.534 0.825 0.575 0.129  -0.073 -0.152 294 TYR DDD CD1 
13436 C CD2 . TYR D 294 ? 0.490 0.768 0.545 0.126  -0.073 -0.150 294 TYR DDD CD2 
13437 C CE1 . TYR D 294 ? 0.526 0.831 0.565 0.133  -0.078 -0.155 294 TYR DDD CE1 
13438 C CE2 . TYR D 294 ? 0.499 0.791 0.552 0.130  -0.079 -0.153 294 TYR DDD CE2 
13439 C CZ  . TYR D 294 ? 0.528 0.834 0.573 0.134  -0.081 -0.155 294 TYR DDD CZ  
13440 O OH  . TYR D 294 ? 0.534 0.853 0.576 0.138  -0.087 -0.158 294 TYR DDD OH  
13441 N N   . ALA D 295 ? 0.472 0.731 0.500 0.117  -0.057 -0.128 295 ALA DDD N   
13442 C CA  . ALA D 295 ? 0.467 0.720 0.492 0.115  -0.054 -0.127 295 ALA DDD CA  
13443 C C   . ALA D 295 ? 0.465 0.731 0.487 0.119  -0.056 -0.133 295 ALA DDD C   
13444 O O   . ALA D 295 ? 0.440 0.710 0.454 0.120  -0.055 -0.130 295 ALA DDD O   
13445 C CB  . ALA D 295 ? 0.477 0.728 0.496 0.112  -0.050 -0.117 295 ALA DDD CB  
13446 N N   . THR D 296 ? 0.486 0.756 0.514 0.122  -0.060 -0.143 296 THR DDD N   
13447 C CA  . THR D 296 ? 0.501 0.784 0.527 0.126  -0.063 -0.150 296 THR DDD CA  
13448 C C   . THR D 296 ? 0.528 0.806 0.559 0.126  -0.062 -0.156 296 THR DDD C   
13449 O O   . THR D 296 ? 0.623 0.912 0.652 0.129  -0.063 -0.161 296 THR DDD O   
13450 C CB  . THR D 296 ? 0.493 0.786 0.523 0.130  -0.067 -0.158 296 THR DDD CB  
13451 O OG1 . THR D 296 ? 0.470 0.753 0.510 0.128  -0.068 -0.161 296 THR DDD OG1 
13452 C CG2 . THR D 296 ? 0.496 0.800 0.518 0.131  -0.069 -0.152 296 THR DDD CG2 
13453 N N   . GLY D 297 ? 0.487 0.749 0.524 0.122  -0.060 -0.155 297 GLY DDD N   
13454 C CA  . GLY D 297 ? 0.458 0.712 0.499 0.121  -0.060 -0.159 297 GLY DDD CA  
13455 C C   . GLY D 297 ? 0.448 0.687 0.498 0.118  -0.059 -0.160 297 GLY DDD C   
13456 O O   . GLY D 297 ? 0.438 0.674 0.490 0.116  -0.058 -0.157 297 GLY DDD O   
13457 N N   . ARG D 298 ? 0.434 0.667 0.490 0.117  -0.059 -0.164 298 ARG DDD N   
13458 C CA  . ARG D 298 ? 0.428 0.646 0.492 0.113  -0.058 -0.164 298 ARG DDD CA  
13459 C C   . ARG D 298 ? 0.453 0.672 0.528 0.115  -0.062 -0.174 298 ARG DDD C   
13460 O O   . ARG D 298 ? 0.418 0.642 0.492 0.118  -0.064 -0.176 298 ARG DDD O   
13461 C CB  . ARG D 298 ? 0.398 0.603 0.457 0.108  -0.055 -0.155 298 ARG DDD CB  
13462 C CG  . ARG D 298 ? 0.384 0.588 0.435 0.105  -0.051 -0.147 298 ARG DDD CG  
13463 C CD  . ARG D 298 ? 0.387 0.580 0.431 0.101  -0.048 -0.139 298 ARG DDD CD  
13464 N NE  . ARG D 298 ? 0.376 0.555 0.424 0.097  -0.046 -0.138 298 ARG DDD NE  
13465 C CZ  . ARG D 298 ? 0.350 0.521 0.400 0.092  -0.043 -0.135 298 ARG DDD CZ  
13466 N NH1 . ARG D 298 ? 0.345 0.519 0.393 0.092  -0.041 -0.133 298 ARG DDD NH1 
13467 N NH2 . ARG D 298 ? 0.345 0.504 0.398 0.088  -0.042 -0.134 298 ARG DDD NH2 
13468 N N   . ASN D 299 ? 0.482 0.696 0.567 0.114  -0.063 -0.179 299 ASN DDD N   
13469 C CA  . ASN D 299 ? 0.524 0.734 0.621 0.115  -0.066 -0.187 299 ASN DDD CA  
13470 C C   . ASN D 299 ? 0.531 0.725 0.632 0.110  -0.064 -0.182 299 ASN DDD C   
13471 O O   . ASN D 299 ? 0.588 0.773 0.687 0.106  -0.060 -0.176 299 ASN DDD O   
13472 C CB  . ASN D 299 ? 0.572 0.788 0.681 0.118  -0.069 -0.196 299 ASN DDD CB  
13473 C CG  . ASN D 299 ? 0.602 0.835 0.707 0.123  -0.072 -0.201 299 ASN DDD CG  
13474 O OD1 . ASN D 299 ? 0.674 0.911 0.780 0.124  -0.072 -0.202 299 ASN DDD OD1 
13475 N ND2 . ASN D 299 ? 0.634 0.877 0.735 0.127  -0.074 -0.204 299 ASN DDD ND2 
13476 N N   . PRO D 300 ? 0.499 0.689 0.607 0.110  -0.066 -0.185 300 PRO DDD N   
13477 C CA  . PRO D 300 ? 0.503 0.677 0.615 0.105  -0.065 -0.181 300 PRO DDD CA  
13478 C C   . PRO D 300 ? 0.543 0.710 0.666 0.103  -0.064 -0.183 300 PRO DDD C   
13479 O O   . PRO D 300 ? 0.523 0.696 0.656 0.106  -0.068 -0.193 300 PRO DDD O   
13480 C CB  . PRO D 300 ? 0.498 0.671 0.617 0.108  -0.069 -0.186 300 PRO DDD CB  
13481 C CG  . PRO D 300 ? 0.502 0.692 0.627 0.114  -0.073 -0.196 300 PRO DDD CG  
13482 C CD  . PRO D 300 ? 0.493 0.693 0.604 0.115  -0.070 -0.193 300 PRO DDD CD  
13483 N N   . ASP D 301 ? 0.592 0.746 0.711 0.097  -0.060 -0.176 301 ASP DDD N   
13484 C CA  . ASP D 301 ? 0.613 0.760 0.742 0.093  -0.059 -0.177 301 ASP DDD CA  
13485 C C   . ASP D 301 ? 0.659 0.796 0.799 0.091  -0.061 -0.180 301 ASP DDD C   
13486 O O   . ASP D 301 ? 0.674 0.798 0.812 0.086  -0.058 -0.172 301 ASP DDD O   
13487 C CB  . ASP D 301 ? 0.604 0.742 0.724 0.087  -0.053 -0.169 301 ASP DDD CB  
13488 C CG  . ASP D 301 ? 0.593 0.725 0.723 0.084  -0.051 -0.171 301 ASP DDD CG  
13489 O OD1 . ASP D 301 ? 0.596 0.735 0.738 0.087  -0.054 -0.180 301 ASP DDD OD1 
13490 O OD2 . ASP D 301 ? 0.545 0.666 0.671 0.078  -0.046 -0.165 301 ASP DDD OD2 
13491 N N   . VAL D 302 ? 0.704 0.848 0.856 0.096  -0.066 -0.189 302 VAL DDD N   
13492 C CA  . VAL D 302 ? 0.733 0.870 0.899 0.095  -0.069 -0.192 302 VAL DDD CA  
13493 C C   . VAL D 302 ? 0.703 0.841 0.886 0.096  -0.071 -0.201 302 VAL DDD C   
13494 O O   . VAL D 302 ? 0.747 0.878 0.943 0.095  -0.074 -0.204 302 VAL DDD O   
13495 C CB  . VAL D 302 ? 0.703 0.846 0.871 0.100  -0.074 -0.196 302 VAL DDD CB  
13496 C CG1 . VAL D 302 ? 0.696 0.834 0.849 0.098  -0.072 -0.186 302 VAL DDD CG1 
13497 C CG2 . VAL D 302 ? 0.686 0.846 0.855 0.107  -0.077 -0.206 302 VAL DDD CG2 
13498 N N   . LYS D 303 ? 0.669 0.815 0.852 0.098  -0.071 -0.206 303 LYS DDD N   
13499 C CA  . LYS D 303 ? 0.720 0.871 0.920 0.101  -0.074 -0.216 303 LYS DDD CA  
13500 C C   . LYS D 303 ? 0.726 0.863 0.936 0.095  -0.071 -0.213 303 LYS DDD C   
13501 O O   . LYS D 303 ? 0.723 0.859 0.951 0.096  -0.074 -0.220 303 LYS DDD O   
13502 C CB  . LYS D 303 ? 0.736 0.899 0.932 0.105  -0.074 -0.221 303 LYS DDD CB  
13503 C CG  . LYS D 303 ? 0.756 0.934 0.943 0.111  -0.077 -0.224 303 LYS DDD CG  
13504 C CD  . LYS D 303 ? 0.781 0.974 0.967 0.115  -0.079 -0.231 303 LYS DDD CD  
13505 C CE  . LYS D 303 ? 0.801 1.007 0.973 0.120  -0.080 -0.230 303 LYS DDD CE  
13506 N NZ  . LYS D 303 ? 0.796 1.018 0.970 0.125  -0.084 -0.239 303 LYS DDD NZ  
13507 N N   . GLY D 304 ? 0.731 0.858 0.932 0.088  -0.065 -0.203 304 GLY DDD N   
13508 C CA  . GLY D 304 ? 0.731 0.844 0.940 0.082  -0.062 -0.199 304 GLY DDD CA  
13509 C C   . GLY D 304 ? 0.705 0.807 0.919 0.079  -0.064 -0.195 304 GLY DDD C   
13510 O O   . GLY D 304 ? 0.666 0.757 0.888 0.073  -0.061 -0.192 304 GLY DDD O   
13511 N N   . LEU D 305 ? 0.729 0.833 0.939 0.082  -0.067 -0.195 305 LEU DDD N   
13512 C CA  . LEU D 305 ? 0.735 0.827 0.946 0.078  -0.069 -0.188 305 LEU DDD CA  
13513 C C   . LEU D 305 ? 0.791 0.881 1.024 0.080  -0.074 -0.195 305 LEU DDD C   
13514 O O   . LEU D 305 ? 0.817 0.896 1.054 0.076  -0.075 -0.189 305 LEU DDD O   
13515 C CB  . LEU D 305 ? 0.716 0.813 0.916 0.081  -0.071 -0.185 305 LEU DDD CB  
13516 C CG  . LEU D 305 ? 0.746 0.840 0.925 0.078  -0.066 -0.175 305 LEU DDD CG  
13517 C CD1 . LEU D 305 ? 0.794 0.893 0.963 0.081  -0.068 -0.173 305 LEU DDD CD1 
13518 C CD2 . LEU D 305 ? 0.746 0.826 0.920 0.070  -0.061 -0.165 305 LEU DDD CD2 
13519 N N   . ASN D 306 ? 0.811 0.913 1.057 0.086  -0.078 -0.207 306 ASN DDD N   
13520 C CA  . ASN D 306 ? 0.806 0.906 1.074 0.088  -0.083 -0.216 306 ASN DDD CA  
13521 C C   . ASN D 306 ? 0.809 0.911 1.080 0.092  -0.089 -0.218 306 ASN DDD C   
13522 O O   . ASN D 306 ? 0.802 0.895 1.087 0.090  -0.092 -0.217 306 ASN DDD O   
13523 C CB  . ASN D 306 ? 0.841 0.927 1.119 0.081  -0.081 -0.211 306 ASN DDD CB  
13524 C CG  . ASN D 306 ? 0.818 0.905 1.121 0.083  -0.086 -0.221 306 ASN DDD CG  
13525 O OD1 . ASN D 306 ? 0.745 0.844 1.057 0.089  -0.089 -0.233 306 ASN DDD OD1 
13526 N ND2 . ASN D 306 ? 0.854 0.927 1.168 0.078  -0.086 -0.215 306 ASN DDD ND2 
13527 N N   . LEU D 307 ? 0.831 0.944 1.090 0.096  -0.090 -0.219 307 LEU DDD N   
13528 C CA  . LEU D 307 ? 0.844 0.960 1.104 0.100  -0.094 -0.220 307 LEU DDD CA  
13529 C C   . LEU D 307 ? 0.822 0.944 1.103 0.105  -0.101 -0.234 307 LEU DDD C   
13530 O O   . LEU D 307 ? 0.799 0.916 1.090 0.105  -0.105 -0.234 307 LEU DDD O   
13531 C CB  . LEU D 307 ? 0.851 0.978 1.093 0.103  -0.093 -0.220 307 LEU DDD CB  
13532 C CG  . LEU D 307 ? 0.853 0.974 1.074 0.098  -0.087 -0.207 307 LEU DDD CG  
13533 C CD1 . LEU D 307 ? 0.852 0.985 1.058 0.103  -0.086 -0.208 307 LEU DDD CD1 
13534 C CD2 . LEU D 307 ? 0.864 0.968 1.081 0.093  -0.086 -0.196 307 LEU DDD CD2 
13535 N N   . ASN D 308 ? 0.858 0.993 1.145 0.110  -0.102 -0.245 308 ASN DDD N   
13536 C CA  . ASN D 308 ? 0.858 1.003 1.165 0.116  -0.108 -0.260 308 ASN DDD CA  
13537 C C   . ASN D 308 ? 0.844 0.977 1.174 0.113  -0.111 -0.261 308 ASN DDD C   
13538 O O   . ASN D 308 ? 0.851 0.985 1.193 0.116  -0.117 -0.266 308 ASN DDD O   
13539 C CB  . ASN D 308 ? 0.875 1.033 1.185 0.120  -0.108 -0.271 308 ASN DDD CB  
13540 C CG  . ASN D 308 ? 0.902 1.075 1.228 0.127  -0.114 -0.287 308 ASN DDD CG  
13541 O OD1 . ASN D 308 ? 0.904 1.074 1.245 0.128  -0.119 -0.291 308 ASN DDD OD1 
13542 N ND2 . ASN D 308 ? 0.917 1.106 1.240 0.131  -0.115 -0.296 308 ASN DDD ND2 
13543 N N   . ALA D 309 ? 0.821 0.942 1.154 0.107  -0.108 -0.255 309 ALA DDD N   
13544 C CA  . ALA D 309 ? 0.818 0.927 1.173 0.104  -0.111 -0.255 309 ALA DDD CA  
13545 C C   . ALA D 309 ? 0.804 0.900 1.159 0.100  -0.113 -0.245 309 ALA DDD C   
13546 O O   . ALA D 309 ? 0.785 0.874 1.161 0.100  -0.118 -0.247 309 ALA DDD O   
13547 C CB  . ALA D 309 ? 0.793 0.895 1.148 0.098  -0.106 -0.250 309 ALA DDD CB  
13548 N N   . ILE D 310 ? 0.804 0.896 1.138 0.098  -0.110 -0.234 310 ILE DDD N   
13549 C CA  . ILE D 310 ? 0.819 0.897 1.151 0.094  -0.111 -0.223 310 ILE DDD CA  
13550 C C   . ILE D 310 ? 0.789 0.874 1.126 0.099  -0.117 -0.229 310 ILE DDD C   
13551 O O   . ILE D 310 ? 0.754 0.829 1.097 0.097  -0.121 -0.223 310 ILE DDD O   
13552 C CB  . ILE D 310 ? 0.859 0.928 1.167 0.087  -0.105 -0.208 310 ILE DDD CB  
13553 C CG1 . ILE D 310 ? 0.903 0.968 1.208 0.082  -0.099 -0.203 310 ILE DDD CG1 
13554 C CG2 . ILE D 310 ? 0.837 0.893 1.142 0.083  -0.107 -0.197 310 ILE DDD CG2 
13555 C CD1 . ILE D 310 ? 0.919 0.975 1.245 0.079  -0.100 -0.205 310 ILE DDD CD1 
13556 N N   . GLY D 311 ? 0.770 0.872 1.104 0.106  -0.118 -0.240 311 GLY DDD N   
13557 C CA  . GLY D 311 ? 0.768 0.880 1.105 0.112  -0.123 -0.247 311 GLY DDD CA  
13558 C C   . GLY D 311 ? 0.746 0.860 1.060 0.112  -0.120 -0.239 311 GLY DDD C   
13559 O O   . GLY D 311 ? 0.701 0.817 1.018 0.114  -0.123 -0.240 311 GLY DDD O   
13560 N N   . VAL D 312 ? 0.729 0.844 1.023 0.109  -0.113 -0.231 312 VAL DDD N   
13561 C CA  . VAL D 312 ? 0.729 0.847 1.000 0.109  -0.110 -0.224 312 VAL DDD CA  
13562 C C   . VAL D 312 ? 0.716 0.854 0.983 0.116  -0.110 -0.235 312 VAL DDD C   
13563 O O   . VAL D 312 ? 0.742 0.887 1.004 0.117  -0.107 -0.239 312 VAL DDD O   
13564 C CB  . VAL D 312 ? 0.731 0.840 0.982 0.103  -0.103 -0.211 312 VAL DDD CB  
13565 C CG1 . VAL D 312 ? 0.729 0.845 0.960 0.104  -0.100 -0.207 312 VAL DDD CG1 
13566 C CG2 . VAL D 312 ? 0.731 0.822 0.983 0.096  -0.103 -0.199 312 VAL DDD CG2 
13567 N N   . GLU D 313 ? 0.750 0.896 1.017 0.120  -0.113 -0.240 313 GLU DDD N   
13568 C CA  . GLU D 313 ? 0.805 0.971 1.071 0.127  -0.113 -0.251 313 GLU DDD CA  
13569 C C   . GLU D 313 ? 0.785 0.958 1.027 0.126  -0.107 -0.245 313 GLU DDD C   
13570 O O   . GLU D 313 ? 0.767 0.931 0.994 0.122  -0.104 -0.233 313 GLU DDD O   
13571 C CB  . GLU D 313 ? 0.868 1.040 1.141 0.131  -0.118 -0.257 313 GLU DDD CB  
13572 C CG  . GLU D 313 ? 0.930 1.100 1.229 0.133  -0.124 -0.266 313 GLU DDD CG  
13573 C CD  . GLU D 313 ? 0.955 1.135 1.264 0.138  -0.128 -0.276 313 GLU DDD CD  
13574 O OE1 . GLU D 313 ? 0.968 1.160 1.293 0.143  -0.132 -0.291 313 GLU DDD OE1 
13575 O OE2 . GLU D 313 ? 0.996 1.173 1.296 0.137  -0.128 -0.269 313 GLU DDD OE2 
13576 N N   . VAL D 314 ? 0.740 0.928 0.978 0.130  -0.106 -0.253 314 VAL DDD N   
13577 C CA  . VAL D 314 ? 0.752 0.948 0.969 0.130  -0.102 -0.248 314 VAL DDD CA  
13578 C C   . VAL D 314 ? 0.709 0.925 0.924 0.136  -0.103 -0.258 314 VAL DDD C   
13579 O O   . VAL D 314 ? 0.727 0.951 0.956 0.140  -0.107 -0.270 314 VAL DDD O   
13580 C CB  . VAL D 314 ? 0.806 1.000 1.019 0.128  -0.098 -0.246 314 VAL DDD CB  
13581 C CG1 . VAL D 314 ? 0.808 0.982 1.023 0.121  -0.096 -0.236 314 VAL DDD CG1 
13582 C CG2 . VAL D 314 ? 0.801 1.006 1.028 0.132  -0.102 -0.259 314 VAL DDD CG2 
13583 N N   . SER D 315 ? 0.737 0.960 0.934 0.137  -0.099 -0.252 315 SER DDD N   
13584 C CA  . SER D 315 ? 0.743 0.985 0.934 0.142  -0.099 -0.260 315 SER DDD CA  
13585 C C   . SER D 315 ? 0.701 0.955 0.888 0.144  -0.099 -0.265 315 SER DDD C   
13586 O O   . SER D 315 ? 0.653 0.900 0.844 0.142  -0.098 -0.263 315 SER DDD O   
13587 C CB  . SER D 315 ? 0.777 1.021 0.951 0.141  -0.095 -0.250 315 SER DDD CB  
13588 O OG  . SER D 315 ? 0.808 1.049 0.966 0.138  -0.091 -0.241 315 SER DDD OG  
13589 N N   . ASP D 316 ? 0.751 1.024 0.932 0.149  -0.099 -0.272 316 ASP DDD N   
13590 C CA  . ASP D 316 ? 0.775 1.062 0.951 0.151  -0.099 -0.277 316 ASP DDD CA  
13591 C C   . ASP D 316 ? 0.821 1.101 0.981 0.147  -0.095 -0.264 316 ASP DDD C   
13592 O O   . ASP D 316 ? 0.790 1.074 0.950 0.148  -0.095 -0.267 316 ASP DDD O   
13593 C CB  . ASP D 316 ? 0.781 1.089 0.951 0.156  -0.099 -0.285 316 ASP DDD CB  
13594 C CG  . ASP D 316 ? 0.816 1.133 1.002 0.161  -0.104 -0.301 316 ASP DDD CG  
13595 O OD1 . ASP D 316 ? 0.795 1.108 0.998 0.161  -0.108 -0.309 316 ASP DDD OD1 
13596 O OD2 . ASP D 316 ? 0.815 1.144 0.999 0.163  -0.103 -0.305 316 ASP DDD OD2 
13597 N N   . SER D 317 ? 0.874 1.145 1.023 0.144  -0.091 -0.252 317 SER DDD N   
13598 C CA  . SER D 317 ? 0.857 1.121 0.992 0.140  -0.087 -0.240 317 SER DDD CA  
13599 C C   . SER D 317 ? 0.831 1.077 0.972 0.135  -0.086 -0.234 317 SER DDD C   
13600 O O   . SER D 317 ? 0.822 1.063 0.954 0.132  -0.082 -0.226 317 SER DDD O   
13601 C CB  . SER D 317 ? 0.816 1.079 0.938 0.138  -0.083 -0.229 317 SER DDD CB  
13602 O OG  . SER D 317 ? 0.833 1.082 0.959 0.135  -0.083 -0.225 317 SER DDD OG  
13603 N N   . GLY D 318 ? 0.817 1.055 0.974 0.134  -0.089 -0.239 318 GLY DDD N   
13604 C CA  . GLY D 318 ? 0.784 1.005 0.948 0.129  -0.087 -0.234 318 GLY DDD CA  
13605 C C   . GLY D 318 ? 0.772 0.978 0.931 0.125  -0.085 -0.223 318 GLY DDD C   
13606 O O   . GLY D 318 ? 0.756 0.947 0.919 0.120  -0.084 -0.218 318 GLY DDD O   
13607 N N   . LYS D 319 ? 0.767 0.976 0.917 0.126  -0.085 -0.220 319 LYS DDD N   
13608 C CA  . LYS D 319 ? 0.798 0.993 0.943 0.121  -0.083 -0.210 319 LYS DDD CA  
13609 C C   . LYS D 319 ? 0.801 0.989 0.962 0.121  -0.087 -0.214 319 LYS DDD C   
13610 O O   . LYS D 319 ? 0.883 1.080 1.056 0.126  -0.091 -0.225 319 LYS DDD O   
13611 C CB  . LYS D 319 ? 0.813 1.015 0.945 0.122  -0.081 -0.205 319 LYS DDD CB  
13612 C CG  . LYS D 319 ? 0.814 1.019 0.930 0.120  -0.076 -0.197 319 LYS DDD CG  
13613 C CD  . LYS D 319 ? 0.794 1.000 0.898 0.120  -0.074 -0.190 319 LYS DDD CD  
13614 C CE  . LYS D 319 ? 0.749 0.956 0.838 0.118  -0.069 -0.181 319 LYS DDD CE  
13615 N NZ  . LYS D 319 ? 0.752 0.960 0.831 0.117  -0.067 -0.174 319 LYS DDD NZ  
13616 N N   . ILE D 320 ? 0.776 0.947 0.937 0.116  -0.086 -0.205 320 ILE DDD N   
13617 C CA  . ILE D 320 ? 0.748 0.909 0.922 0.115  -0.091 -0.206 320 ILE DDD CA  
13618 C C   . ILE D 320 ? 0.730 0.897 0.905 0.118  -0.093 -0.208 320 ILE DDD C   
13619 O O   . ILE D 320 ? 0.697 0.865 0.858 0.117  -0.091 -0.202 320 ILE DDD O   
13620 C CB  . ILE D 320 ? 0.741 0.884 0.913 0.108  -0.089 -0.195 320 ILE DDD CB  
13621 C CG1 . ILE D 320 ? 0.742 0.879 0.914 0.105  -0.086 -0.194 320 ILE DDD CG1 
13622 C CG2 . ILE D 320 ? 0.776 0.908 0.961 0.107  -0.094 -0.194 320 ILE DDD CG2 
13623 C CD1 . ILE D 320 ? 0.782 0.903 0.950 0.098  -0.083 -0.183 320 ILE DDD CD1 
13624 N N   . ILE D 321 ? 0.749 0.919 0.941 0.121  -0.099 -0.217 321 ILE DDD N   
13625 C CA  . ILE D 321 ? 0.756 0.929 0.952 0.124  -0.102 -0.220 321 ILE DDD CA  
13626 C C   . ILE D 321 ? 0.756 0.911 0.954 0.120  -0.104 -0.210 321 ILE DDD C   
13627 O O   . ILE D 321 ? 0.801 0.945 1.012 0.117  -0.107 -0.210 321 ILE DDD O   
13628 C CB  . ILE D 321 ? 0.745 0.930 0.959 0.130  -0.107 -0.236 321 ILE DDD CB  
13629 C CG1 . ILE D 321 ? 0.707 0.912 0.916 0.135  -0.105 -0.245 321 ILE DDD CG1 
13630 C CG2 . ILE D 321 ? 0.763 0.949 0.987 0.132  -0.111 -0.239 321 ILE DDD CG2 
13631 C CD1 . ILE D 321 ? 0.717 0.933 0.943 0.140  -0.109 -0.260 321 ILE DDD CD1 
13632 N N   . ALA D 322 ? 0.716 0.869 0.901 0.118  -0.102 -0.202 322 ALA DDD N   
13633 C CA  . ALA D 322 ? 0.756 0.892 0.939 0.113  -0.103 -0.191 322 ALA DDD CA  
13634 C C   . ALA D 322 ? 0.730 0.870 0.902 0.114  -0.102 -0.187 322 ALA DDD C   
13635 O O   . ALA D 322 ? 0.696 0.829 0.853 0.110  -0.099 -0.176 322 ALA DDD O   
13636 C CB  . ALA D 322 ? 0.771 0.894 0.945 0.107  -0.100 -0.181 322 ALA DDD CB  
13637 N N   . PRO D 323 ? 0.698 0.849 0.878 0.119  -0.105 -0.195 323 PRO DDD N   
13638 C CA  . PRO D 323 ? 0.677 0.833 0.847 0.120  -0.104 -0.192 323 PRO DDD CA  
13639 C C   . PRO D 323 ? 0.683 0.823 0.848 0.115  -0.105 -0.180 323 PRO DDD C   
13640 O O   . PRO D 323 ? 0.692 0.834 0.845 0.115  -0.103 -0.175 323 PRO DDD O   
13641 C CB  . PRO D 323 ? 0.692 0.861 0.876 0.126  -0.107 -0.205 323 PRO DDD CB  
13642 C CG  . PRO D 323 ? 0.690 0.857 0.894 0.127  -0.112 -0.213 323 PRO DDD CG  
13643 C CD  . PRO D 323 ? 0.682 0.841 0.880 0.124  -0.110 -0.209 323 PRO DDD CD  
13644 N N   . LYS D 324 ? 0.675 0.800 0.850 0.112  -0.109 -0.177 324 LYS DDD N   
13645 C CA  . LYS D 324 ? 0.669 0.779 0.840 0.108  -0.112 -0.166 324 LYS DDD CA  
13646 C C   . LYS D 324 ? 0.632 0.728 0.796 0.101  -0.109 -0.156 324 LYS DDD C   
13647 O O   . LYS D 324 ? 0.567 0.649 0.733 0.097  -0.113 -0.149 324 LYS DDD O   
13648 C CB  . LYS D 324 ? 0.723 0.827 0.913 0.109  -0.120 -0.170 324 LYS DDD CB  
13649 C CG  . LYS D 324 ? 0.754 0.871 0.951 0.115  -0.122 -0.178 324 LYS DDD CG  
13650 C CD  . LYS D 324 ? 0.769 0.884 0.952 0.113  -0.121 -0.170 324 LYS DDD CD  
13651 C CE  . LYS D 324 ? 0.769 0.902 0.951 0.118  -0.118 -0.177 324 LYS DDD CE  
13652 N NZ  . LYS D 324 ? 0.743 0.875 0.904 0.116  -0.113 -0.168 324 LYS DDD NZ  
13653 N N   . ASP D 325 ? 0.667 0.767 0.823 0.100  -0.104 -0.157 325 ASP DDD N   
13654 C CA  . ASP D 325 ? 0.679 0.767 0.828 0.095  -0.101 -0.150 325 ASP DDD CA  
13655 C C   . ASP D 325 ? 0.679 0.762 0.846 0.094  -0.104 -0.154 325 ASP DDD C   
13656 O O   . ASP D 325 ? 0.699 0.777 0.863 0.091  -0.101 -0.152 325 ASP DDD O   
13657 C CB  . ASP D 325 ? 0.705 0.780 0.841 0.089  -0.099 -0.137 325 ASP DDD CB  
13658 C CG  . ASP D 325 ? 0.722 0.803 0.843 0.089  -0.096 -0.133 325 ASP DDD CG  
13659 O OD1 . ASP D 325 ? 0.723 0.818 0.840 0.093  -0.093 -0.138 325 ASP DDD OD1 
13660 O OD2 . ASP D 325 ? 0.750 0.822 0.864 0.086  -0.098 -0.125 325 ASP DDD OD2 
13661 N N   . ALA D 326 ? 0.723 0.805 0.907 0.097  -0.111 -0.160 326 ALA DDD N   
13662 C CA  . ALA D 326 ? 0.743 0.820 0.947 0.097  -0.115 -0.164 326 ALA DDD CA  
13663 C C   . ALA D 326 ? 0.761 0.852 0.974 0.102  -0.115 -0.177 326 ALA DDD C   
13664 O O   . ALA D 326 ? 0.764 0.870 0.982 0.108  -0.116 -0.187 326 ALA DDD O   
13665 C CB  . ALA D 326 ? 0.736 0.807 0.954 0.098  -0.123 -0.165 326 ALA DDD CB  
13666 N N   . THR D 327 ? 0.755 0.843 0.973 0.100  -0.113 -0.178 327 THR DDD N   
13667 C CA  . THR D 327 ? 0.749 0.848 0.978 0.104  -0.113 -0.191 327 THR DDD CA  
13668 C C   . THR D 327 ? 0.736 0.836 0.990 0.108  -0.120 -0.200 327 THR DDD C   
13669 O O   . THR D 327 ? 0.698 0.788 0.959 0.106  -0.125 -0.196 327 THR DDD O   
13670 C CB  . THR D 327 ? 0.750 0.845 0.976 0.101  -0.108 -0.189 327 THR DDD CB  
13671 O OG1 . THR D 327 ? 0.685 0.766 0.924 0.096  -0.111 -0.184 327 THR DDD OG1 
13672 C CG2 . THR D 327 ? 0.725 0.818 0.930 0.096  -0.101 -0.179 327 THR DDD CG2 
13673 N N   . SER D 328 ? 0.748 0.858 1.015 0.112  -0.121 -0.212 328 SER DDD N   
13674 C CA  . SER D 328 ? 0.726 0.837 1.019 0.115  -0.128 -0.223 328 SER DDD CA  
13675 C C   . SER D 328 ? 0.731 0.823 1.034 0.110  -0.130 -0.215 328 SER DDD C   
13676 O O   . SER D 328 ? 0.745 0.835 1.071 0.111  -0.137 -0.221 328 SER DDD O   
13677 C CB  . SER D 328 ? 0.718 0.844 1.018 0.120  -0.127 -0.237 328 SER DDD CB  
13678 O OG  . SER D 328 ? 0.690 0.815 0.980 0.117  -0.122 -0.234 328 SER DDD OG  
13679 N N   . VAL D 329 ? 0.734 0.816 1.024 0.103  -0.126 -0.204 329 VAL DDD N   
13680 C CA  . VAL D 329 ? 0.751 0.815 1.049 0.097  -0.127 -0.194 329 VAL DDD CA  
13681 C C   . VAL D 329 ? 0.743 0.794 1.026 0.092  -0.127 -0.180 329 VAL DDD C   
13682 O O   . VAL D 329 ? 0.756 0.806 1.018 0.089  -0.121 -0.172 329 VAL DDD O   
13683 C CB  . VAL D 329 ? 0.758 0.819 1.051 0.093  -0.121 -0.192 329 VAL DDD CB  
13684 C CG1 . VAL D 329 ? 0.760 0.803 1.057 0.085  -0.121 -0.181 329 VAL DDD CG1 
13685 C CG2 . VAL D 329 ? 0.755 0.828 1.065 0.098  -0.123 -0.207 329 VAL DDD CG2 
13686 N N   . PRO D 330 ? 0.771 0.812 1.067 0.091  -0.133 -0.176 330 PRO DDD N   
13687 C CA  . PRO D 330 ? 0.777 0.809 1.060 0.088  -0.135 -0.164 330 PRO DDD CA  
13688 C C   . PRO D 330 ? 0.770 0.788 1.035 0.079  -0.130 -0.148 330 PRO DDD C   
13689 O O   . PRO D 330 ? 0.800 0.813 1.051 0.077  -0.131 -0.140 330 PRO DDD O   
13690 C CB  . PRO D 330 ? 0.799 0.826 1.104 0.089  -0.144 -0.166 330 PRO DDD CB  
13691 C CG  . PRO D 330 ? 0.789 0.813 1.117 0.090  -0.146 -0.173 330 PRO DDD CG  
13692 C CD  . PRO D 330 ? 0.775 0.812 1.097 0.092  -0.140 -0.182 330 PRO DDD CD  
13693 N N   . SER D 331 ? 0.738 0.751 1.003 0.075  -0.126 -0.146 331 SER DDD N   
13694 C CA  . SER D 331 ? 0.751 0.753 0.999 0.067  -0.121 -0.132 331 SER DDD CA  
13695 C C   . SER D 331 ? 0.740 0.750 0.967 0.066  -0.112 -0.132 331 SER DDD C   
13696 O O   . SER D 331 ? 0.702 0.705 0.913 0.060  -0.107 -0.122 331 SER DDD O   
13697 C CB  . SER D 331 ? 0.729 0.721 0.989 0.062  -0.120 -0.129 331 SER DDD CB  
13698 O OG  . SER D 331 ? 0.686 0.687 0.956 0.065  -0.118 -0.140 331 SER DDD OG  
13699 N N   . ILE D 332 ? 0.759 0.784 0.987 0.073  -0.111 -0.144 332 ILE DDD N   
13700 C CA  . ILE D 332 ? 0.759 0.794 0.972 0.074  -0.104 -0.146 332 ILE DDD CA  
13701 C C   . ILE D 332 ? 0.763 0.809 0.965 0.078  -0.104 -0.148 332 ILE DDD C   
13702 O O   . ILE D 332 ? 0.696 0.752 0.908 0.085  -0.108 -0.158 332 ILE DDD O   
13703 C CB  . ILE D 332 ? 0.778 0.822 1.002 0.077  -0.102 -0.156 332 ILE DDD CB  
13704 C CG1 . ILE D 332 ? 0.773 0.806 1.008 0.071  -0.101 -0.153 332 ILE DDD CG1 
13705 C CG2 . ILE D 332 ? 0.748 0.803 0.956 0.078  -0.096 -0.159 332 ILE DDD CG2 
13706 C CD1 . ILE D 332 ? 0.761 0.801 1.007 0.073  -0.099 -0.163 332 ILE DDD CD1 
13707 N N   . PHE D 333 ? 0.759 0.803 0.940 0.075  -0.099 -0.139 333 PHE DDD N   
13708 C CA  . PHE D 333 ? 0.743 0.795 0.911 0.078  -0.097 -0.139 333 PHE DDD CA  
13709 C C   . PHE D 333 ? 0.710 0.772 0.866 0.079  -0.091 -0.142 333 PHE DDD C   
13710 O O   . PHE D 333 ? 0.642 0.702 0.799 0.076  -0.087 -0.142 333 PHE DDD O   
13711 C CB  . PHE D 333 ? 0.770 0.811 0.926 0.073  -0.098 -0.127 333 PHE DDD CB  
13712 C CG  . PHE D 333 ? 0.779 0.812 0.948 0.073  -0.106 -0.126 333 PHE DDD CG  
13713 C CD1 . PHE D 333 ? 0.793 0.812 0.970 0.068  -0.108 -0.120 333 PHE DDD CD1 
13714 C CD2 . PHE D 333 ? 0.778 0.816 0.952 0.078  -0.111 -0.130 333 PHE DDD CD2 
13715 C CE1 . PHE D 333 ? 0.798 0.809 0.987 0.068  -0.115 -0.118 333 PHE DDD CE1 
13716 C CE2 . PHE D 333 ? 0.815 0.845 1.003 0.078  -0.118 -0.128 333 PHE DDD CE2 
13717 C CZ  . PHE D 333 ? 0.812 0.828 1.007 0.073  -0.121 -0.122 333 PHE DDD CZ  
13718 N N   . ALA D 334 ? 0.666 0.739 0.813 0.083  -0.089 -0.144 334 ALA DDD N   
13719 C CA  . ALA D 334 ? 0.624 0.707 0.759 0.084  -0.084 -0.145 334 ALA DDD CA  
13720 C C   . ALA D 334 ? 0.624 0.711 0.745 0.085  -0.082 -0.141 334 ALA DDD C   
13721 O O   . ALA D 334 ? 0.597 0.685 0.721 0.087  -0.086 -0.142 334 ALA DDD O   
13722 C CB  . ALA D 334 ? 0.569 0.666 0.715 0.090  -0.085 -0.157 334 ALA DDD CB  
13723 N N   . VAL D 335 ? 0.611 0.699 0.718 0.082  -0.076 -0.136 335 VAL DDD N   
13724 C CA  . VAL D 335 ? 0.580 0.673 0.672 0.083  -0.074 -0.132 335 VAL DDD CA  
13725 C C   . VAL D 335 ? 0.542 0.643 0.626 0.083  -0.068 -0.133 335 VAL DDD C   
13726 O O   . VAL D 335 ? 0.526 0.628 0.616 0.083  -0.067 -0.136 335 VAL DDD O   
13727 C CB  . VAL D 335 ? 0.581 0.662 0.663 0.077  -0.073 -0.121 335 VAL DDD CB  
13728 C CG1 . VAL D 335 ? 0.590 0.663 0.680 0.077  -0.079 -0.119 335 VAL DDD CG1 
13729 C CG2 . VAL D 335 ? 0.578 0.650 0.653 0.071  -0.068 -0.115 335 VAL DDD CG2 
13730 N N   . GLY D 336 ? 0.528 0.637 0.603 0.085  -0.066 -0.130 336 GLY DDD N   
13731 C CA  . GLY D 336 ? 0.531 0.648 0.597 0.085  -0.061 -0.130 336 GLY DDD CA  
13732 C C   . GLY D 336 ? 0.534 0.666 0.606 0.091  -0.062 -0.139 336 GLY DDD C   
13733 O O   . GLY D 336 ? 0.544 0.682 0.624 0.096  -0.066 -0.146 336 GLY DDD O   
13734 N N   . ASP D 337 ? 0.538 0.674 0.606 0.091  -0.059 -0.139 337 ASP DDD N   
13735 C CA  . ASP D 337 ? 0.544 0.696 0.613 0.096  -0.059 -0.146 337 ASP DDD CA  
13736 C C   . ASP D 337 ? 0.536 0.693 0.619 0.100  -0.063 -0.156 337 ASP DDD C   
13737 O O   . ASP D 337 ? 0.586 0.757 0.670 0.105  -0.064 -0.162 337 ASP DDD O   
13738 C CB  . ASP D 337 ? 0.529 0.684 0.593 0.095  -0.055 -0.143 337 ASP DDD CB  
13739 C CG  . ASP D 337 ? 0.541 0.695 0.593 0.093  -0.051 -0.135 337 ASP DDD CG  
13740 O OD1 . ASP D 337 ? 0.543 0.695 0.589 0.092  -0.052 -0.131 337 ASP DDD OD1 
13741 O OD2 . ASP D 337 ? 0.511 0.666 0.558 0.092  -0.048 -0.133 337 ASP DDD OD2 
13742 N N   . ILE D 338 ? 0.532 0.678 0.624 0.098  -0.065 -0.157 338 ILE DDD N   
13743 C CA  . ILE D 338 ? 0.542 0.692 0.649 0.101  -0.069 -0.167 338 ILE DDD CA  
13744 C C   . ILE D 338 ? 0.585 0.741 0.700 0.105  -0.073 -0.173 338 ILE DDD C   
13745 O O   . ILE D 338 ? 0.555 0.717 0.683 0.108  -0.077 -0.183 338 ILE DDD O   
13746 C CB  . ILE D 338 ? 0.539 0.677 0.654 0.096  -0.068 -0.166 338 ILE DDD CB  
13747 C CG1 . ILE D 338 ? 0.564 0.688 0.681 0.092  -0.070 -0.160 338 ILE DDD CG1 
13748 C CG2 . ILE D 338 ? 0.539 0.672 0.646 0.092  -0.063 -0.160 338 ILE DDD CG2 
13749 C CD1 . ILE D 338 ? 0.577 0.687 0.701 0.087  -0.069 -0.157 338 ILE DDD CD1 
13750 N N   . VAL D 339 ? 0.604 0.757 0.713 0.104  -0.074 -0.168 339 VAL DDD N   
13751 C CA  . VAL D 339 ? 0.626 0.783 0.745 0.108  -0.079 -0.174 339 VAL DDD CA  
13752 C C   . VAL D 339 ? 0.647 0.822 0.763 0.114  -0.079 -0.180 339 VAL DDD C   
13753 O O   . VAL D 339 ? 0.631 0.809 0.733 0.113  -0.075 -0.175 339 VAL DDD O   
13754 C CB  . VAL D 339 ? 0.638 0.783 0.755 0.105  -0.080 -0.167 339 VAL DDD CB  
13755 C CG1 . VAL D 339 ? 0.624 0.773 0.753 0.109  -0.085 -0.174 339 VAL DDD CG1 
13756 C CG2 . VAL D 339 ? 0.638 0.766 0.757 0.099  -0.080 -0.160 339 VAL DDD CG2 
13757 N N   . GLU D 340 ? 0.711 0.895 0.838 0.118  -0.082 -0.192 340 GLU DDD N   
13758 C CA  . GLU D 340 ? 0.725 0.928 0.851 0.124  -0.083 -0.199 340 GLU DDD CA  
13759 C C   . GLU D 340 ? 0.638 0.842 0.760 0.124  -0.083 -0.196 340 GLU DDD C   
13760 O O   . GLU D 340 ? 0.642 0.835 0.771 0.123  -0.086 -0.195 340 GLU DDD O   
13761 C CB  . GLU D 340 ? 0.802 1.014 0.942 0.129  -0.087 -0.213 340 GLU DDD CB  
13762 C CG  . GLU D 340 ? 0.849 1.080 0.989 0.134  -0.087 -0.220 340 GLU DDD CG  
13763 C CD  . GLU D 340 ? 0.953 1.199 1.098 0.138  -0.089 -0.233 340 GLU DDD CD  
13764 O OE1 . GLU D 340 ? 1.027 1.280 1.185 0.142  -0.093 -0.244 340 GLU DDD OE1 
13765 O OE2 . GLU D 340 ? 1.032 1.284 1.168 0.138  -0.087 -0.231 340 GLU DDD OE2 
13766 N N   . GLY D 341 ? 0.618 0.834 0.728 0.126  -0.080 -0.195 341 GLY DDD N   
13767 C CA  . GLY D 341 ? 0.617 0.839 0.725 0.128  -0.080 -0.195 341 GLY DDD CA  
13768 C C   . GLY D 341 ? 0.586 0.797 0.685 0.124  -0.077 -0.183 341 GLY DDD C   
13769 O O   . GLY D 341 ? 0.589 0.802 0.688 0.124  -0.078 -0.182 341 GLY DDD O   
13770 N N   . ARG D 342 ? 0.583 0.783 0.673 0.119  -0.075 -0.174 342 ARG DDD N   
13771 C CA  . ARG D 342 ? 0.596 0.787 0.676 0.115  -0.072 -0.162 342 ARG DDD CA  
13772 C C   . ARG D 342 ? 0.568 0.760 0.634 0.113  -0.067 -0.156 342 ARG DDD C   
13773 O O   . ARG D 342 ? 0.518 0.712 0.585 0.113  -0.066 -0.158 342 ARG DDD O   
13774 C CB  . ARG D 342 ? 0.578 0.750 0.661 0.111  -0.074 -0.157 342 ARG DDD CB  
13775 C CG  . ARG D 342 ? 0.574 0.736 0.657 0.107  -0.073 -0.155 342 ARG DDD CG  
13776 C CD  . ARG D 342 ? 0.573 0.718 0.658 0.102  -0.075 -0.148 342 ARG DDD CD  
13777 N NE  . ARG D 342 ? 0.553 0.694 0.652 0.104  -0.080 -0.153 342 ARG DDD NE  
13778 C CZ  . ARG D 342 ? 0.540 0.667 0.644 0.100  -0.083 -0.149 342 ARG DDD CZ  
13779 N NH1 . ARG D 342 ? 0.543 0.658 0.637 0.095  -0.081 -0.139 342 ARG DDD NH1 
13780 N NH2 . ARG D 342 ? 0.563 0.689 0.682 0.102  -0.089 -0.154 342 ARG DDD NH2 
13781 N N   . PRO D 343 ? 0.549 0.741 0.605 0.111  -0.064 -0.148 343 PRO DDD N   
13782 C CA  . PRO D 343 ? 0.532 0.726 0.578 0.109  -0.060 -0.142 343 PRO DDD CA  
13783 C C   . PRO D 343 ? 0.499 0.680 0.543 0.105  -0.058 -0.137 343 PRO DDD C   
13784 O O   . PRO D 343 ? 0.457 0.626 0.504 0.102  -0.059 -0.134 343 PRO DDD O   
13785 C CB  . PRO D 343 ? 0.552 0.744 0.589 0.108  -0.058 -0.134 343 PRO DDD CB  
13786 C CG  . PRO D 343 ? 0.573 0.768 0.618 0.111  -0.061 -0.139 343 PRO DDD CG  
13787 C CD  . PRO D 343 ? 0.557 0.746 0.613 0.111  -0.065 -0.145 343 PRO DDD CD  
13788 N N   . GLU D 344 ? 0.512 0.698 0.552 0.105  -0.056 -0.137 344 GLU DDD N   
13789 C CA  . GLU D 344 ? 0.545 0.720 0.584 0.101  -0.054 -0.133 344 GLU DDD CA  
13790 C C   . GLU D 344 ? 0.504 0.674 0.534 0.097  -0.050 -0.124 344 GLU DDD C   
13791 O O   . GLU D 344 ? 0.528 0.702 0.553 0.097  -0.047 -0.121 344 GLU DDD O   
13792 C CB  . GLU D 344 ? 0.609 0.794 0.650 0.103  -0.053 -0.137 344 GLU DDD CB  
13793 C CG  . GLU D 344 ? 0.649 0.840 0.700 0.107  -0.057 -0.148 344 GLU DDD CG  
13794 C CD  . GLU D 344 ? 0.703 0.906 0.755 0.110  -0.057 -0.152 344 GLU DDD CD  
13795 O OE1 . GLU D 344 ? 0.681 0.883 0.728 0.108  -0.054 -0.148 344 GLU DDD OE1 
13796 O OE2 . GLU D 344 ? 0.747 0.960 0.805 0.115  -0.060 -0.161 344 GLU DDD OE2 
13797 N N   . LEU D 345 ? 0.457 0.617 0.484 0.094  -0.050 -0.119 345 LEU DDD N   
13798 C CA  . LEU D 345 ? 0.425 0.578 0.443 0.090  -0.047 -0.110 345 LEU DDD CA  
13799 C C   . LEU D 345 ? 0.418 0.555 0.435 0.085  -0.047 -0.107 345 LEU DDD C   
13800 O O   . LEU D 345 ? 0.387 0.519 0.411 0.085  -0.050 -0.109 345 LEU DDD O   
13801 C CB  . LEU D 345 ? 0.429 0.587 0.444 0.092  -0.048 -0.108 345 LEU DDD CB  
13802 C CG  . LEU D 345 ? 0.410 0.584 0.425 0.096  -0.047 -0.111 345 LEU DDD CG  
13803 C CD1 . LEU D 345 ? 0.397 0.575 0.410 0.098  -0.048 -0.110 345 LEU DDD CD1 
13804 C CD2 . LEU D 345 ? 0.408 0.586 0.416 0.095  -0.043 -0.106 345 LEU DDD CD2 
13805 N N   . THR D 346 ? 0.410 0.541 0.420 0.080  -0.043 -0.100 346 THR DDD N   
13806 C CA  . THR D 346 ? 0.406 0.523 0.414 0.075  -0.042 -0.097 346 THR DDD CA  
13807 C C   . THR D 346 ? 0.404 0.514 0.411 0.073  -0.045 -0.094 346 THR DDD C   
13808 O O   . THR D 346 ? 0.399 0.500 0.409 0.071  -0.048 -0.094 346 THR DDD O   
13809 C CB  . THR D 346 ? 0.418 0.532 0.420 0.071  -0.037 -0.092 346 THR DDD CB  
13810 O OG1 . THR D 346 ? 0.405 0.521 0.411 0.070  -0.035 -0.095 346 THR DDD OG1 
13811 C CG2 . THR D 346 ? 0.428 0.530 0.424 0.065  -0.036 -0.086 346 THR DDD CG2 
13812 N N   . PRO D 347 ? 0.415 0.529 0.417 0.074  -0.045 -0.091 347 PRO DDD N   
13813 C CA  . PRO D 347 ? 0.419 0.526 0.420 0.074  -0.049 -0.088 347 PRO DDD CA  
13814 C C   . PRO D 347 ? 0.468 0.575 0.479 0.077  -0.054 -0.093 347 PRO DDD C   
13815 O O   . PRO D 347 ? 0.513 0.610 0.525 0.074  -0.057 -0.091 347 PRO DDD O   
13816 C CB  . PRO D 347 ? 0.403 0.517 0.400 0.075  -0.048 -0.086 347 PRO DDD CB  
13817 C CG  . PRO D 347 ? 0.400 0.518 0.392 0.075  -0.043 -0.084 347 PRO DDD CG  
13818 C CD  . PRO D 347 ? 0.412 0.535 0.410 0.076  -0.043 -0.089 347 PRO DDD CD  
13819 N N   . VAL D 348 ? 0.504 0.621 0.522 0.081  -0.055 -0.100 348 VAL DDD N   
13820 C CA  . VAL D 348 ? 0.517 0.635 0.546 0.085  -0.060 -0.107 348 VAL DDD CA  
13821 C C   . VAL D 348 ? 0.540 0.648 0.574 0.082  -0.061 -0.107 348 VAL DDD C   
13822 O O   . VAL D 348 ? 0.517 0.618 0.557 0.081  -0.066 -0.107 348 VAL DDD O   
13823 C CB  . VAL D 348 ? 0.520 0.653 0.554 0.091  -0.060 -0.114 348 VAL DDD CB  
13824 C CG1 . VAL D 348 ? 0.544 0.680 0.591 0.094  -0.065 -0.122 348 VAL DDD CG1 
13825 C CG2 . VAL D 348 ? 0.538 0.682 0.568 0.093  -0.059 -0.113 348 VAL DDD CG2 
13826 N N   . ALA D 349 ? 0.535 0.643 0.567 0.080  -0.058 -0.107 349 ALA DDD N   
13827 C CA  . ALA D 349 ? 0.563 0.661 0.600 0.076  -0.058 -0.107 349 ALA DDD CA  
13828 C C   . ALA D 349 ? 0.581 0.665 0.612 0.070  -0.058 -0.099 349 ALA DDD C   
13829 O O   . ALA D 349 ? 0.561 0.637 0.599 0.069  -0.062 -0.099 349 ALA DDD O   
13830 C CB  . ALA D 349 ? 0.587 0.687 0.620 0.074  -0.053 -0.107 349 ALA DDD CB  
13831 N N   . VAL D 350 ? 0.627 0.707 0.646 0.067  -0.055 -0.093 350 VAL DDD N   
13832 C CA  . VAL D 350 ? 0.619 0.688 0.631 0.061  -0.055 -0.085 350 VAL DDD CA  
13833 C C   . VAL D 350 ? 0.611 0.675 0.627 0.062  -0.061 -0.084 350 VAL DDD C   
13834 O O   . VAL D 350 ? 0.659 0.712 0.677 0.059  -0.064 -0.081 350 VAL DDD O   
13835 C CB  . VAL D 350 ? 0.653 0.722 0.653 0.059  -0.051 -0.080 350 VAL DDD CB  
13836 C CG1 . VAL D 350 ? 0.675 0.733 0.667 0.053  -0.052 -0.073 350 VAL DDD CG1 
13837 C CG2 . VAL D 350 ? 0.696 0.767 0.693 0.056  -0.045 -0.081 350 VAL DDD CG2 
13838 N N   . LYS D 351 ? 0.592 0.663 0.609 0.067  -0.064 -0.086 351 LYS DDD N   
13839 C CA  . LYS D 351 ? 0.629 0.696 0.651 0.068  -0.070 -0.085 351 LYS DDD CA  
13840 C C   . LYS D 351 ? 0.643 0.708 0.678 0.070  -0.075 -0.090 351 LYS DDD C   
13841 O O   . LYS D 351 ? 0.636 0.692 0.675 0.068  -0.080 -0.087 351 LYS DDD O   
13842 C CB  . LYS D 351 ? 0.609 0.685 0.630 0.072  -0.071 -0.087 351 LYS DDD CB  
13843 C CG  . LYS D 351 ? 0.632 0.702 0.657 0.073  -0.077 -0.085 351 LYS DDD CG  
13844 C CD  . LYS D 351 ? 0.672 0.751 0.697 0.076  -0.078 -0.086 351 LYS DDD CD  
13845 C CE  . LYS D 351 ? 0.673 0.750 0.685 0.074  -0.075 -0.080 351 LYS DDD CE  
13846 N NZ  . LYS D 351 ? 0.668 0.731 0.674 0.069  -0.078 -0.073 351 LYS DDD NZ  
13847 N N   . ALA D 352 ? 0.659 0.732 0.702 0.074  -0.074 -0.097 352 ALA DDD N   
13848 C CA  . ALA D 352 ? 0.693 0.766 0.751 0.076  -0.079 -0.103 352 ALA DDD CA  
13849 C C   . ALA D 352 ? 0.712 0.771 0.770 0.070  -0.079 -0.098 352 ALA DDD C   
13850 O O   . ALA D 352 ? 0.742 0.794 0.810 0.070  -0.084 -0.098 352 ALA DDD O   
13851 C CB  . ALA D 352 ? 0.656 0.741 0.722 0.081  -0.077 -0.112 352 ALA DDD CB  
13852 N N   . GLY D 353 ? 0.696 0.751 0.745 0.066  -0.073 -0.094 353 GLY DDD N   
13853 C CA  . GLY D 353 ? 0.693 0.737 0.741 0.060  -0.072 -0.089 353 GLY DDD CA  
13854 C C   . GLY D 353 ? 0.702 0.734 0.744 0.055  -0.075 -0.080 353 GLY DDD C   
13855 O O   . GLY D 353 ? 0.657 0.679 0.705 0.052  -0.079 -0.077 353 GLY DDD O   
13856 N N   . ILE D 354 ? 0.715 0.747 0.745 0.054  -0.074 -0.076 354 ILE DDD N   
13857 C CA  . ILE D 354 ? 0.714 0.735 0.737 0.050  -0.078 -0.068 354 ILE DDD CA  
13858 C C   . ILE D 354 ? 0.707 0.726 0.742 0.054  -0.086 -0.069 354 ILE DDD C   
13859 O O   . ILE D 354 ? 0.650 0.658 0.687 0.050  -0.090 -0.063 354 ILE DDD O   
13860 C CB  . ILE D 354 ? 0.738 0.762 0.747 0.050  -0.075 -0.064 354 ILE DDD CB  
13861 C CG1 . ILE D 354 ? 0.744 0.769 0.742 0.046  -0.067 -0.062 354 ILE DDD CG1 
13862 C CG2 . ILE D 354 ? 0.755 0.770 0.758 0.046  -0.080 -0.057 354 ILE DDD CG2 
13863 C CD1 . ILE D 354 ? 0.717 0.747 0.705 0.045  -0.064 -0.060 354 ILE DDD CD1 
13864 N N   . LEU D 355 ? 0.691 0.721 0.735 0.060  -0.089 -0.076 355 LEU DDD N   
13865 C CA  . LEU D 355 ? 0.677 0.705 0.733 0.064  -0.097 -0.079 355 LEU DDD CA  
13866 C C   . LEU D 355 ? 0.690 0.712 0.761 0.064  -0.100 -0.081 355 LEU DDD C   
13867 O O   . LEU D 355 ? 0.729 0.743 0.808 0.063  -0.107 -0.078 355 LEU DDD O   
13868 C CB  . LEU D 355 ? 0.624 0.666 0.687 0.071  -0.097 -0.087 355 LEU DDD CB  
13869 C CG  . LEU D 355 ? 0.595 0.642 0.647 0.071  -0.095 -0.084 355 LEU DDD CG  
13870 C CD1 . LEU D 355 ? 0.558 0.618 0.619 0.078  -0.097 -0.092 355 LEU DDD CD1 
13871 C CD2 . LEU D 355 ? 0.623 0.658 0.667 0.067  -0.099 -0.076 355 LEU DDD CD2 
13872 N N   . LEU D 356 ? 0.735 0.763 0.811 0.064  -0.097 -0.086 356 LEU DDD N   
13873 C CA  . LEU D 356 ? 0.816 0.839 0.906 0.064  -0.099 -0.089 356 LEU DDD CA  
13874 C C   . LEU D 356 ? 0.851 0.857 0.936 0.056  -0.101 -0.078 356 LEU DDD C   
13875 O O   . LEU D 356 ? 0.968 0.967 1.064 0.056  -0.107 -0.076 356 LEU DDD O   
13876 C CB  . LEU D 356 ? 0.793 0.823 0.886 0.065  -0.094 -0.096 356 LEU DDD CB  
13877 C CG  . LEU D 356 ? 0.815 0.839 0.921 0.064  -0.096 -0.098 356 LEU DDD CG  
13878 C CD1 . LEU D 356 ? 0.854 0.880 0.980 0.068  -0.103 -0.105 356 LEU DDD CD1 
13879 C CD2 . LEU D 356 ? 0.803 0.835 0.910 0.064  -0.090 -0.104 356 LEU DDD CD2 
13880 N N   . ALA D 357 ? 0.829 0.832 0.898 0.051  -0.094 -0.072 357 ALA DDD N   
13881 C CA  . ALA D 357 ? 0.848 0.836 0.908 0.043  -0.094 -0.061 357 ALA DDD CA  
13882 C C   . ALA D 357 ? 0.827 0.807 0.888 0.042  -0.102 -0.055 357 ALA DDD C   
13883 O O   . ALA D 357 ? 0.758 0.727 0.824 0.039  -0.107 -0.050 357 ALA DDD O   
13884 C CB  . ALA D 357 ? 0.848 0.836 0.889 0.038  -0.087 -0.057 357 ALA DDD CB  
13885 N N   . ARG D 358 ? 0.807 0.792 0.863 0.046  -0.104 -0.056 358 ARG DDD N   
13886 C CA  . ARG D 358 ? 0.840 0.818 0.896 0.045  -0.112 -0.050 358 ARG DDD CA  
13887 C C   . ARG D 358 ? 0.862 0.838 0.939 0.049  -0.120 -0.054 358 ARG DDD C   
13888 O O   . ARG D 358 ? 0.894 0.859 0.974 0.046  -0.127 -0.047 358 ARG DDD O   
13889 C CB  . ARG D 358 ? 0.836 0.822 0.885 0.049  -0.111 -0.051 358 ARG DDD CB  
13890 C CG  . ARG D 358 ? 0.834 0.818 0.861 0.044  -0.105 -0.045 358 ARG DDD CG  
13891 C CD  . ARG D 358 ? 0.835 0.827 0.856 0.047  -0.105 -0.047 358 ARG DDD CD  
13892 N NE  . ARG D 358 ? 0.834 0.826 0.838 0.043  -0.098 -0.043 358 ARG DDD NE  
13893 C CZ  . ARG D 358 ? 0.835 0.835 0.832 0.045  -0.095 -0.044 358 ARG DDD CZ  
13894 N NH1 . ARG D 358 ? 0.838 0.846 0.843 0.051  -0.097 -0.050 358 ARG DDD NH1 
13895 N NH2 . ARG D 358 ? 0.827 0.827 0.810 0.040  -0.088 -0.041 358 ARG DDD NH2 
13896 N N   . ARG D 359 ? 0.839 0.826 0.930 0.056  -0.120 -0.065 359 ARG DDD N   
13897 C CA  . ARG D 359 ? 0.861 0.849 0.974 0.060  -0.128 -0.071 359 ARG DDD CA  
13898 C C   . ARG D 359 ? 0.891 0.867 1.013 0.056  -0.131 -0.067 359 ARG DDD C   
13899 O O   . ARG D 359 ? 0.933 0.901 1.068 0.057  -0.139 -0.066 359 ARG DDD O   
13900 C CB  . ARG D 359 ? 0.866 0.868 0.990 0.068  -0.126 -0.085 359 ARG DDD CB  
13901 C CG  . ARG D 359 ? 0.868 0.881 0.988 0.072  -0.126 -0.089 359 ARG DDD CG  
13902 C CD  . ARG D 359 ? 0.874 0.901 1.009 0.080  -0.127 -0.102 359 ARG DDD CD  
13903 N NE  . ARG D 359 ? 0.885 0.920 1.024 0.081  -0.122 -0.109 359 ARG DDD NE  
13904 C CZ  . ARG D 359 ? 0.956 1.000 1.083 0.081  -0.114 -0.110 359 ARG DDD CZ  
13905 N NH1 . ARG D 359 ? 0.947 0.993 1.058 0.080  -0.110 -0.106 359 ARG DDD NH1 
13906 N NH2 . ARG D 359 ? 0.938 0.987 1.069 0.082  -0.111 -0.117 359 ARG DDD NH2 
13907 N N   . LEU D 360 ? 0.911 0.886 1.027 0.052  -0.124 -0.066 360 LEU DDD N   
13908 C CA  . LEU D 360 ? 0.948 0.913 1.073 0.048  -0.125 -0.063 360 LEU DDD CA  
13909 C C   . LEU D 360 ? 0.965 0.915 1.081 0.041  -0.128 -0.049 360 LEU DDD C   
13910 O O   . LEU D 360 ? 1.000 0.940 1.129 0.039  -0.134 -0.046 360 LEU DDD O   
13911 C CB  . LEU D 360 ? 0.958 0.928 1.078 0.046  -0.116 -0.066 360 LEU DDD CB  
13912 C CG  . LEU D 360 ? 0.968 0.951 1.100 0.053  -0.114 -0.079 360 LEU DDD CG  
13913 C CD1 . LEU D 360 ? 0.972 0.959 1.099 0.050  -0.106 -0.081 360 LEU DDD CD1 
13914 C CD2 . LEU D 360 ? 0.978 0.961 1.134 0.057  -0.122 -0.087 360 LEU DDD CD2 
13915 N N   . PHE D 361 ? 0.960 0.908 1.056 0.037  -0.125 -0.041 361 PHE DDD N   
13916 C CA  . PHE D 361 ? 0.969 0.903 1.050 0.028  -0.125 -0.028 361 PHE DDD CA  
13917 C C   . PHE D 361 ? 0.992 0.922 1.061 0.027  -0.129 -0.020 361 PHE DDD C   
13918 O O   . PHE D 361 ? 1.052 0.971 1.111 0.020  -0.130 -0.009 361 PHE DDD O   
13919 C CB  . PHE D 361 ? 0.942 0.878 1.008 0.023  -0.115 -0.026 361 PHE DDD CB  
13920 C CG  . PHE D 361 ? 0.936 0.875 1.014 0.023  -0.110 -0.032 361 PHE DDD CG  
13921 C CD1 . PHE D 361 ? 0.937 0.867 1.029 0.021  -0.114 -0.030 361 PHE DDD CD1 
13922 C CD2 . PHE D 361 ? 0.915 0.865 0.989 0.025  -0.102 -0.040 361 PHE DDD CD2 
13923 C CE1 . PHE D 361 ? 0.897 0.831 1.001 0.021  -0.110 -0.036 361 PHE DDD CE1 
13924 C CE2 . PHE D 361 ? 0.844 0.797 0.929 0.026  -0.099 -0.046 361 PHE DDD CE2 
13925 C CZ  . PHE D 361 ? 0.856 0.800 0.955 0.024  -0.102 -0.044 361 PHE DDD CZ  
13926 N N   . ALA D 362 ? 0.977 0.915 1.047 0.033  -0.132 -0.026 362 ALA DDD N   
13927 C CA  . ALA D 362 ? 0.981 0.915 1.039 0.032  -0.136 -0.020 362 ALA DDD CA  
13928 C C   . ALA D 362 ? 0.955 0.893 1.029 0.039  -0.144 -0.025 362 ALA DDD C   
13929 O O   . ALA D 362 ? 0.927 0.867 0.994 0.040  -0.147 -0.024 362 ALA DDD O   
13930 C CB  . ALA D 362 ? 1.005 0.947 1.045 0.031  -0.128 -0.020 362 ALA DDD CB  
13931 N N   . GLY D 363 ? 0.967 0.906 1.063 0.043  -0.149 -0.032 363 GLY DDD N   
13932 C CA  . GLY D 363 ? 0.939 0.880 1.053 0.049  -0.158 -0.037 363 GLY DDD CA  
13933 C C   . GLY D 363 ? 0.943 0.898 1.056 0.055  -0.155 -0.046 363 GLY DDD C   
13934 O O   . GLY D 363 ? 0.952 0.908 1.075 0.059  -0.162 -0.048 363 GLY DDD O   
13935 N N   . SER D 364 ? 0.946 0.912 1.048 0.056  -0.146 -0.051 364 SER DDD N   
13936 C CA  . SER D 364 ? 0.953 0.933 1.054 0.062  -0.143 -0.059 364 SER DDD CA  
13937 C C   . SER D 364 ? 0.940 0.931 1.062 0.069  -0.144 -0.072 364 SER DDD C   
13938 O O   . SER D 364 ? 0.899 0.887 1.032 0.069  -0.145 -0.075 364 SER DDD O   
13939 C CB  . SER D 364 ? 0.978 0.964 1.060 0.060  -0.133 -0.058 364 SER DDD CB  
13940 O OG  . SER D 364 ? 0.998 0.999 1.081 0.066  -0.129 -0.067 364 SER DDD OG  
13941 N N   . ASN D 365 ? 0.999 1.001 1.126 0.075  -0.145 -0.080 365 ASN DDD N   
13942 C CA  . ASN D 365 ? 1.056 1.071 1.200 0.082  -0.145 -0.093 365 ASN DDD CA  
13943 C C   . ASN D 365 ? 1.013 1.043 1.148 0.085  -0.138 -0.099 365 ASN DDD C   
13944 O O   . ASN D 365 ? 0.970 1.012 1.117 0.091  -0.138 -0.110 365 ASN DDD O   
13945 C CB  . ASN D 365 ? 1.124 1.138 1.289 0.086  -0.154 -0.098 365 ASN DDD CB  
13946 C CG  . ASN D 365 ? 1.191 1.212 1.375 0.090  -0.155 -0.110 365 ASN DDD CG  
13947 O OD1 . ASN D 365 ? 1.169 1.205 1.362 0.096  -0.153 -0.121 365 ASN DDD OD1 
13948 N ND2 . ASN D 365 ? 1.266 1.278 1.456 0.087  -0.156 -0.107 365 ASN DDD ND2 
13949 N N   . GLU D 366 ? 1.005 1.035 1.120 0.082  -0.131 -0.093 366 GLU DDD N   
13950 C CA  . GLU D 366 ? 0.968 1.010 1.073 0.084  -0.125 -0.096 366 GLU DDD CA  
13951 C C   . GLU D 366 ? 0.899 0.952 1.004 0.085  -0.118 -0.102 366 GLU DDD C   
13952 O O   . GLU D 366 ? 0.871 0.917 0.970 0.081  -0.115 -0.098 366 GLU DDD O   
13953 C CB  . GLU D 366 ? 0.976 1.013 1.062 0.080  -0.122 -0.086 366 GLU DDD CB  
13954 C CG  . GLU D 366 ? 0.966 0.999 1.054 0.080  -0.128 -0.083 366 GLU DDD CG  
13955 C CD  . GLU D 366 ? 0.993 1.020 1.063 0.076  -0.126 -0.074 366 GLU DDD CD  
13956 O OE1 . GLU D 366 ? 1.080 1.094 1.143 0.070  -0.129 -0.065 366 GLU DDD OE1 
13957 O OE2 . GLU D 366 ? 0.993 1.029 1.056 0.077  -0.121 -0.076 366 GLU DDD OE2 
13958 N N   . PHE D 367 ? 0.864 0.931 0.973 0.091  -0.116 -0.111 367 PHE DDD N   
13959 C CA  . PHE D 367 ? 0.803 0.882 0.909 0.093  -0.109 -0.118 367 PHE DDD CA  
13960 C C   . PHE D 367 ? 0.765 0.854 0.858 0.094  -0.104 -0.116 367 PHE DDD C   
13961 O O   . PHE D 367 ? 0.818 0.906 0.908 0.094  -0.105 -0.114 367 PHE DDD O   
13962 C CB  . PHE D 367 ? 0.783 0.873 0.907 0.099  -0.112 -0.130 367 PHE DDD CB  
13963 C CG  . PHE D 367 ? 0.787 0.869 0.926 0.098  -0.117 -0.132 367 PHE DDD CG  
13964 C CD1 . PHE D 367 ? 0.773 0.845 0.923 0.098  -0.125 -0.130 367 PHE DDD CD1 
13965 C CD2 . PHE D 367 ? 0.776 0.858 0.916 0.098  -0.114 -0.135 367 PHE DDD CD2 
13966 C CE1 . PHE D 367 ? 0.756 0.820 0.920 0.097  -0.130 -0.131 367 PHE DDD CE1 
13967 C CE2 . PHE D 367 ? 0.773 0.847 0.927 0.097  -0.119 -0.136 367 PHE DDD CE2 
13968 C CZ  . PHE D 367 ? 0.779 0.843 0.945 0.096  -0.126 -0.134 367 PHE DDD CZ  
13969 N N   . ILE D 368 ? 0.710 0.807 0.796 0.094  -0.097 -0.118 368 ILE DDD N   
13970 C CA  . ILE D 368 ? 0.631 0.739 0.707 0.096  -0.092 -0.118 368 ILE DDD CA  
13971 C C   . ILE D 368 ? 0.607 0.729 0.692 0.101  -0.093 -0.126 368 ILE DDD C   
13972 O O   . ILE D 368 ? 0.584 0.710 0.683 0.105  -0.096 -0.135 368 ILE DDD O   
13973 C CB  . ILE D 368 ? 0.622 0.735 0.690 0.095  -0.086 -0.119 368 ILE DDD CB  
13974 C CG1 . ILE D 368 ? 0.597 0.697 0.655 0.089  -0.083 -0.110 368 ILE DDD CG1 
13975 C CG2 . ILE D 368 ? 0.639 0.766 0.701 0.098  -0.081 -0.120 368 ILE DDD CG2 
13976 C CD1 . ILE D 368 ? 0.582 0.687 0.637 0.088  -0.078 -0.112 368 ILE DDD CD1 
13977 N N   . ASP D 369 ? 0.585 0.713 0.664 0.102  -0.091 -0.124 369 ASP DDD N   
13978 C CA  . ASP D 369 ? 0.610 0.754 0.694 0.107  -0.090 -0.132 369 ASP DDD CA  
13979 C C   . ASP D 369 ? 0.622 0.779 0.699 0.109  -0.084 -0.134 369 ASP DDD C   
13980 O O   . ASP D 369 ? 0.681 0.839 0.745 0.107  -0.079 -0.128 369 ASP DDD O   
13981 C CB  . ASP D 369 ? 0.616 0.760 0.698 0.107  -0.091 -0.129 369 ASP DDD CB  
13982 C CG  . ASP D 369 ? 0.652 0.811 0.742 0.112  -0.090 -0.137 369 ASP DDD CG  
13983 O OD1 . ASP D 369 ? 0.681 0.854 0.775 0.116  -0.088 -0.144 369 ASP DDD OD1 
13984 O OD2 . ASP D 369 ? 0.666 0.825 0.758 0.113  -0.092 -0.135 369 ASP DDD OD2 
13985 N N   . TYR D 370 ? 0.616 0.782 0.700 0.112  -0.084 -0.143 370 TYR DDD N   
13986 C CA  . TYR D 370 ? 0.628 0.804 0.705 0.113  -0.078 -0.145 370 TYR DDD CA  
13987 C C   . TYR D 370 ? 0.637 0.829 0.710 0.116  -0.075 -0.147 370 TYR DDD C   
13988 O O   . TYR D 370 ? 0.686 0.888 0.753 0.117  -0.071 -0.148 370 TYR DDD O   
13989 C CB  . TYR D 370 ? 0.650 0.830 0.737 0.116  -0.080 -0.153 370 TYR DDD CB  
13990 C CG  . TYR D 370 ? 0.658 0.824 0.745 0.112  -0.082 -0.150 370 TYR DDD CG  
13991 C CD1 . TYR D 370 ? 0.671 0.833 0.747 0.109  -0.077 -0.144 370 TYR DDD CD1 
13992 C CD2 . TYR D 370 ? 0.650 0.806 0.748 0.111  -0.087 -0.152 370 TYR DDD CD2 
13993 C CE1 . TYR D 370 ? 0.696 0.845 0.772 0.105  -0.078 -0.140 370 TYR DDD CE1 
13994 C CE2 . TYR D 370 ? 0.673 0.816 0.773 0.108  -0.088 -0.148 370 TYR DDD CE2 
13995 C CZ  . TYR D 370 ? 0.711 0.850 0.799 0.104  -0.083 -0.142 370 TYR DDD CZ  
13996 O OH  . TYR D 370 ? 0.707 0.834 0.795 0.100  -0.084 -0.138 370 TYR DDD OH  
13997 N N   . ASP D 371 ? 0.602 0.796 0.679 0.117  -0.077 -0.148 371 ASP DDD N   
13998 C CA  . ASP D 371 ? 0.576 0.786 0.650 0.120  -0.073 -0.150 371 ASP DDD CA  
13999 C C   . ASP D 371 ? 0.512 0.719 0.573 0.116  -0.068 -0.139 371 ASP DDD C   
14000 O O   . ASP D 371 ? 0.487 0.706 0.543 0.118  -0.064 -0.139 371 ASP DDD O   
14001 C CB  . ASP D 371 ? 0.622 0.835 0.707 0.122  -0.076 -0.155 371 ASP DDD CB  
14002 C CG  . ASP D 371 ? 0.625 0.844 0.726 0.126  -0.080 -0.167 371 ASP DDD CG  
14003 O OD1 . ASP D 371 ? 0.645 0.874 0.745 0.128  -0.079 -0.173 371 ASP DDD OD1 
14004 O OD2 . ASP D 371 ? 0.652 0.866 0.765 0.127  -0.086 -0.170 371 ASP DDD OD2 
14005 N N   . PHE D 372 ? 0.499 0.690 0.554 0.112  -0.069 -0.131 372 PHE DDD N   
14006 C CA  . PHE D 372 ? 0.473 0.660 0.517 0.109  -0.065 -0.121 372 PHE DDD CA  
14007 C C   . PHE D 372 ? 0.453 0.630 0.488 0.105  -0.063 -0.115 372 PHE DDD C   
14008 O O   . PHE D 372 ? 0.469 0.633 0.500 0.101  -0.064 -0.109 372 PHE DDD O   
14009 C CB  . PHE D 372 ? 0.499 0.678 0.545 0.107  -0.068 -0.118 372 PHE DDD CB  
14010 C CG  . PHE D 372 ? 0.502 0.692 0.557 0.111  -0.070 -0.124 372 PHE DDD CG  
14011 C CD1 . PHE D 372 ? 0.508 0.711 0.559 0.113  -0.065 -0.124 372 PHE DDD CD1 
14012 C CD2 . PHE D 372 ? 0.516 0.704 0.583 0.113  -0.075 -0.130 372 PHE DDD CD2 
14013 C CE1 . PHE D 372 ? 0.540 0.754 0.600 0.116  -0.065 -0.129 372 PHE DDD CE1 
14014 C CE2 . PHE D 372 ? 0.525 0.724 0.602 0.117  -0.076 -0.137 372 PHE DDD CE2 
14015 C CZ  . PHE D 372 ? 0.522 0.734 0.595 0.118  -0.071 -0.136 372 PHE DDD CZ  
14016 N N   . VAL D 373 ? 0.406 0.591 0.439 0.106  -0.060 -0.118 373 VAL DDD N   
14017 C CA  . VAL D 373 ? 0.397 0.575 0.423 0.103  -0.058 -0.113 373 VAL DDD CA  
14018 C C   . VAL D 373 ? 0.357 0.543 0.375 0.103  -0.053 -0.109 373 VAL DDD C   
14019 O O   . VAL D 373 ? 0.330 0.529 0.349 0.106  -0.051 -0.113 373 VAL DDD O   
14020 C CB  . VAL D 373 ? 0.415 0.593 0.446 0.104  -0.060 -0.119 373 VAL DDD CB  
14021 C CG1 . VAL D 373 ? 0.434 0.608 0.459 0.101  -0.057 -0.115 373 VAL DDD CG1 
14022 C CG2 . VAL D 373 ? 0.420 0.589 0.461 0.104  -0.065 -0.122 373 VAL DDD CG2 
14023 N N   . PRO D 374 ? 0.362 0.542 0.373 0.099  -0.050 -0.101 374 PRO DDD N   
14024 C CA  . PRO D 374 ? 0.364 0.552 0.369 0.099  -0.046 -0.096 374 PRO DDD CA  
14025 C C   . PRO D 374 ? 0.380 0.565 0.381 0.097  -0.044 -0.095 374 PRO DDD C   
14026 O O   . PRO D 374 ? 0.380 0.557 0.382 0.095  -0.045 -0.096 374 PRO DDD O   
14027 C CB  . PRO D 374 ? 0.351 0.530 0.351 0.095  -0.045 -0.089 374 PRO DDD CB  
14028 C CG  . PRO D 374 ? 0.359 0.523 0.359 0.092  -0.048 -0.088 374 PRO DDD CG  
14029 C CD  . PRO D 374 ? 0.373 0.538 0.381 0.095  -0.052 -0.096 374 PRO DDD CD  
14030 N N   . THR D 375 ? 0.373 0.568 0.371 0.098  -0.040 -0.093 375 THR DDD N   
14031 C CA  . THR D 375 ? 0.411 0.606 0.406 0.097  -0.039 -0.092 375 THR DDD CA  
14032 C C   . THR D 375 ? 0.395 0.595 0.385 0.096  -0.035 -0.085 375 THR DDD C   
14033 O O   . THR D 375 ? 0.371 0.579 0.361 0.098  -0.034 -0.084 375 THR DDD O   
14034 C CB  . THR D 375 ? 0.463 0.668 0.462 0.101  -0.040 -0.099 375 THR DDD CB  
14035 O OG1 . THR D 375 ? 0.537 0.744 0.533 0.101  -0.038 -0.098 375 THR DDD OG1 
14036 C CG2 . THR D 375 ? 0.462 0.682 0.462 0.105  -0.040 -0.103 375 THR DDD CG2 
14037 N N   . THR D 376 ? 0.340 0.535 0.328 0.094  -0.033 -0.082 376 THR DDD N   
14038 C CA  . THR D 376 ? 0.347 0.547 0.332 0.093  -0.030 -0.076 376 THR DDD CA  
14039 C C   . THR D 376 ? 0.349 0.553 0.334 0.094  -0.030 -0.077 376 THR DDD C   
14040 O O   . THR D 376 ? 0.352 0.547 0.339 0.092  -0.030 -0.079 376 THR DDD O   
14041 C CB  . THR D 376 ? 0.346 0.538 0.329 0.089  -0.028 -0.069 376 THR DDD CB  
14042 O OG1 . THR D 376 ? 0.320 0.511 0.302 0.089  -0.028 -0.068 376 THR DDD OG1 
14043 C CG2 . THR D 376 ? 0.352 0.548 0.334 0.088  -0.025 -0.064 376 THR DDD CG2 
14044 N N   . VAL D 377 ? 0.333 0.549 0.317 0.096  -0.029 -0.075 377 VAL DDD N   
14045 C CA  . VAL D 377 ? 0.337 0.557 0.322 0.097  -0.029 -0.074 377 VAL DDD CA  
14046 C C   . VAL D 377 ? 0.333 0.549 0.317 0.094  -0.026 -0.067 377 VAL DDD C   
14047 O O   . VAL D 377 ? 0.331 0.552 0.313 0.094  -0.025 -0.061 377 VAL DDD O   
14048 C CB  . VAL D 377 ? 0.338 0.573 0.321 0.101  -0.030 -0.077 377 VAL DDD CB  
14049 C CG1 . VAL D 377 ? 0.347 0.588 0.329 0.102  -0.030 -0.075 377 VAL DDD CG1 
14050 C CG2 . VAL D 377 ? 0.350 0.589 0.335 0.104  -0.033 -0.086 377 VAL DDD CG2 
14051 N N   . PHE D 378 ? 0.343 0.551 0.329 0.091  -0.026 -0.066 378 PHE DDD N   
14052 C CA  . PHE D 378 ? 0.348 0.551 0.335 0.088  -0.023 -0.060 378 PHE DDD CA  
14053 C C   . PHE D 378 ? 0.328 0.540 0.317 0.090  -0.024 -0.057 378 PHE DDD C   
14054 O O   . PHE D 378 ? 0.355 0.563 0.347 0.088  -0.023 -0.056 378 PHE DDD O   
14055 C CB  . PHE D 378 ? 0.340 0.531 0.330 0.084  -0.022 -0.061 378 PHE DDD CB  
14056 C CG  . PHE D 378 ? 0.359 0.541 0.346 0.082  -0.022 -0.063 378 PHE DDD CG  
14057 C CD1 . PHE D 378 ? 0.366 0.545 0.352 0.080  -0.020 -0.058 378 PHE DDD CD1 
14058 C CD2 . PHE D 378 ? 0.368 0.547 0.355 0.083  -0.024 -0.068 378 PHE DDD CD2 
14059 C CE1 . PHE D 378 ? 0.373 0.544 0.356 0.078  -0.021 -0.059 378 PHE DDD CE1 
14060 C CE2 . PHE D 378 ? 0.369 0.540 0.354 0.081  -0.025 -0.069 378 PHE DDD CE2 
14061 C CZ  . PHE D 378 ? 0.385 0.552 0.367 0.079  -0.023 -0.064 378 PHE DDD CZ  
14062 N N   . THR D 379 ? 0.303 0.528 0.289 0.093  -0.024 -0.054 379 THR DDD N   
14063 C CA  . THR D 379 ? 0.303 0.537 0.289 0.094  -0.025 -0.049 379 THR DDD CA  
14064 C C   . THR D 379 ? 0.318 0.549 0.306 0.092  -0.023 -0.041 379 THR DDD C   
14065 O O   . THR D 379 ? 0.335 0.560 0.324 0.089  -0.021 -0.040 379 THR DDD O   
14066 C CB  . THR D 379 ? 0.311 0.559 0.293 0.098  -0.026 -0.051 379 THR DDD CB  
14067 O OG1 . THR D 379 ? 0.291 0.540 0.270 0.098  -0.025 -0.053 379 THR DDD OG1 
14068 C CG2 . THR D 379 ? 0.318 0.570 0.300 0.101  -0.029 -0.058 379 THR DDD CG2 
14069 N N   . PRO D 380 ? 0.334 0.570 0.324 0.092  -0.023 -0.035 380 PRO DDD N   
14070 C CA  . PRO D 380 ? 0.340 0.574 0.335 0.089  -0.021 -0.028 380 PRO DDD CA  
14071 C C   . PRO D 380 ? 0.346 0.581 0.339 0.089  -0.019 -0.024 380 PRO DDD C   
14072 O O   . PRO D 380 ? 0.357 0.585 0.354 0.086  -0.017 -0.021 380 PRO DDD O   
14073 C CB  . PRO D 380 ? 0.346 0.588 0.342 0.091  -0.023 -0.022 380 PRO DDD CB  
14074 C CG  . PRO D 380 ? 0.342 0.587 0.338 0.093  -0.026 -0.028 380 PRO DDD CG  
14075 C CD  . PRO D 380 ? 0.343 0.588 0.333 0.095  -0.026 -0.036 380 PRO DDD CD  
14076 N N   . ILE D 381 ? 0.338 0.582 0.326 0.091  -0.019 -0.025 381 ILE DDD N   
14077 C CA  . ILE D 381 ? 0.331 0.575 0.316 0.091  -0.018 -0.025 381 ILE DDD CA  
14078 C C   . ILE D 381 ? 0.308 0.550 0.291 0.092  -0.019 -0.034 381 ILE DDD C   
14079 O O   . ILE D 381 ? 0.332 0.580 0.312 0.095  -0.021 -0.038 381 ILE DDD O   
14080 C CB  . ILE D 381 ? 0.353 0.610 0.337 0.092  -0.016 -0.020 381 ILE DDD CB  
14081 C CG1 . ILE D 381 ? 0.364 0.633 0.342 0.095  -0.018 -0.021 381 ILE DDD CG1 
14082 C CG2 . ILE D 381 ? 0.362 0.618 0.350 0.090  -0.015 -0.010 381 ILE DDD CG2 
14083 C CD1 . ILE D 381 ? 0.404 0.686 0.379 0.096  -0.016 -0.016 381 ILE DDD CD1 
14084 N N   . GLU D 382 ? 0.307 0.540 0.290 0.091  -0.018 -0.037 382 GLU DDD N   
14085 C CA  . GLU D 382 ? 0.303 0.531 0.285 0.091  -0.020 -0.045 382 GLU DDD CA  
14086 C C   . GLU D 382 ? 0.287 0.524 0.266 0.094  -0.020 -0.048 382 GLU DDD C   
14087 O O   . GLU D 382 ? 0.306 0.550 0.284 0.095  -0.019 -0.044 382 GLU DDD O   
14088 C CB  . GLU D 382 ? 0.305 0.519 0.288 0.088  -0.019 -0.046 382 GLU DDD CB  
14089 C CG  . GLU D 382 ? 0.319 0.525 0.305 0.085  -0.018 -0.042 382 GLU DDD CG  
14090 C CD  . GLU D 382 ? 0.340 0.532 0.326 0.081  -0.017 -0.044 382 GLU DDD CD  
14091 O OE1 . GLU D 382 ? 0.325 0.515 0.309 0.081  -0.018 -0.045 382 GLU DDD OE1 
14092 O OE2 . GLU D 382 ? 0.352 0.538 0.341 0.078  -0.016 -0.043 382 GLU DDD OE2 
14093 N N   . TYR D 383 ? 0.282 0.518 0.261 0.096  -0.023 -0.056 383 TYR DDD N   
14094 C CA  . TYR D 383 ? 0.304 0.548 0.282 0.099  -0.023 -0.060 383 TYR DDD CA  
14095 C C   . TYR D 383 ? 0.298 0.533 0.278 0.098  -0.025 -0.066 383 TYR DDD C   
14096 O O   . TYR D 383 ? 0.288 0.518 0.269 0.098  -0.027 -0.071 383 TYR DDD O   
14097 C CB  . TYR D 383 ? 0.313 0.571 0.289 0.102  -0.024 -0.063 383 TYR DDD CB  
14098 C CG  . TYR D 383 ? 0.323 0.591 0.300 0.105  -0.025 -0.070 383 TYR DDD CG  
14099 C CD1 . TYR D 383 ? 0.321 0.591 0.299 0.105  -0.024 -0.070 383 TYR DDD CD1 
14100 C CD2 . TYR D 383 ? 0.330 0.603 0.307 0.108  -0.027 -0.078 383 TYR DDD CD2 
14101 C CE1 . TYR D 383 ? 0.335 0.612 0.315 0.108  -0.025 -0.077 383 TYR DDD CE1 
14102 C CE2 . TYR D 383 ? 0.341 0.622 0.320 0.111  -0.028 -0.086 383 TYR DDD CE2 
14103 C CZ  . TYR D 383 ? 0.342 0.626 0.323 0.111  -0.027 -0.085 383 TYR DDD CZ  
14104 O OH  . TYR D 383 ? 0.353 0.644 0.337 0.113  -0.028 -0.092 383 TYR DDD OH  
14105 N N   . GLY D 384 ? 0.293 0.526 0.275 0.098  -0.025 -0.065 384 GLY DDD N   
14106 C CA  . GLY D 384 ? 0.307 0.531 0.291 0.097  -0.027 -0.070 384 GLY DDD CA  
14107 C C   . GLY D 384 ? 0.316 0.549 0.302 0.100  -0.028 -0.075 384 GLY DDD C   
14108 O O   . GLY D 384 ? 0.314 0.556 0.299 0.101  -0.026 -0.072 384 GLY DDD O   
14109 N N   . HIS D 385 ? 0.329 0.559 0.318 0.102  -0.032 -0.082 385 HIS DDD N   
14110 C CA  . HIS D 385 ? 0.395 0.634 0.389 0.105  -0.033 -0.088 385 HIS DDD CA  
14111 C C   . HIS D 385 ? 0.406 0.635 0.405 0.105  -0.037 -0.093 385 HIS DDD C   
14112 O O   . HIS D 385 ? 0.400 0.618 0.398 0.103  -0.039 -0.093 385 HIS DDD O   
14113 C CB  . HIS D 385 ? 0.439 0.694 0.432 0.109  -0.032 -0.093 385 HIS DDD CB  
14114 C CG  . HIS D 385 ? 0.479 0.734 0.475 0.111  -0.035 -0.101 385 HIS DDD CG  
14115 N ND1 . HIS D 385 ? 0.541 0.800 0.544 0.114  -0.038 -0.110 385 HIS DDD ND1 
14116 C CD2 . HIS D 385 ? 0.486 0.737 0.481 0.110  -0.036 -0.102 385 HIS DDD CD2 
14117 C CE1 . HIS D 385 ? 0.539 0.796 0.544 0.115  -0.041 -0.116 385 HIS DDD CE1 
14118 N NE2 . HIS D 385 ? 0.480 0.733 0.481 0.113  -0.039 -0.111 385 HIS DDD NE2 
14119 N N   . VAL D 386 ? 0.377 0.610 0.381 0.107  -0.039 -0.098 386 VAL DDD N   
14120 C CA  . VAL D 386 ? 0.360 0.588 0.371 0.108  -0.043 -0.105 386 VAL DDD CA  
14121 C C   . VAL D 386 ? 0.398 0.640 0.416 0.112  -0.044 -0.112 386 VAL DDD C   
14122 O O   . VAL D 386 ? 0.422 0.675 0.438 0.113  -0.040 -0.110 386 VAL DDD O   
14123 C CB  . VAL D 386 ? 0.345 0.558 0.357 0.106  -0.046 -0.101 386 VAL DDD CB  
14124 C CG1 . VAL D 386 ? 0.345 0.562 0.359 0.106  -0.045 -0.099 386 VAL DDD CG1 
14125 C CG2 . VAL D 386 ? 0.332 0.537 0.352 0.106  -0.051 -0.107 386 VAL DDD CG2 
14126 N N   . GLY D 387 ? 0.402 0.645 0.427 0.115  -0.047 -0.120 387 GLY DDD N   
14127 C CA  . GLY D 387 ? 0.440 0.696 0.472 0.119  -0.048 -0.129 387 GLY DDD CA  
14128 C C   . GLY D 387 ? 0.461 0.733 0.489 0.121  -0.045 -0.133 387 GLY DDD C   
14129 O O   . GLY D 387 ? 0.464 0.735 0.487 0.120  -0.044 -0.131 387 GLY DDD O   
14130 N N   . LEU D 388 ? 0.506 0.794 0.537 0.124  -0.043 -0.137 388 LEU DDD N   
14131 C CA  . LEU D 388 ? 0.536 0.842 0.564 0.127  -0.041 -0.144 388 LEU DDD CA  
14132 C C   . LEU D 388 ? 0.525 0.840 0.543 0.125  -0.036 -0.136 388 LEU DDD C   
14133 O O   . LEU D 388 ? 0.469 0.783 0.485 0.123  -0.033 -0.129 388 LEU DDD O   
14134 C CB  . LEU D 388 ? 0.588 0.906 0.626 0.130  -0.042 -0.154 388 LEU DDD CB  
14135 C CG  . LEU D 388 ? 0.612 0.922 0.663 0.131  -0.047 -0.162 388 LEU DDD CG  
14136 C CD1 . LEU D 388 ? 0.613 0.935 0.674 0.134  -0.047 -0.171 388 LEU DDD CD1 
14137 C CD2 . LEU D 388 ? 0.603 0.908 0.657 0.132  -0.051 -0.167 388 LEU DDD CD2 
14138 N N   . SER D 389 ? 0.572 0.895 0.584 0.127  -0.035 -0.137 389 SER DDD N   
14139 C CA  . SER D 389 ? 0.560 0.898 0.563 0.126  -0.031 -0.132 389 SER DDD CA  
14140 C C   . SER D 389 ? 0.572 0.926 0.577 0.128  -0.028 -0.137 389 SER DDD C   
14141 O O   . SER D 389 ? 0.563 0.919 0.577 0.130  -0.030 -0.146 389 SER DDD O   
14142 C CB  . SER D 389 ? 0.590 0.934 0.589 0.128  -0.032 -0.135 389 SER DDD CB  
14143 O OG  . SER D 389 ? 0.606 0.958 0.611 0.131  -0.034 -0.147 389 SER DDD OG  
14144 N N   . SER D 390 ? 0.586 0.952 0.583 0.127  -0.024 -0.130 390 SER DDD N   
14145 C CA  . SER D 390 ? 0.596 0.981 0.593 0.129  -0.020 -0.134 390 SER DDD CA  
14146 C C   . SER D 390 ? 0.628 1.026 0.628 0.133  -0.022 -0.148 390 SER DDD C   
14147 O O   . SER D 390 ? 0.661 1.067 0.668 0.135  -0.022 -0.157 390 SER DDD O   
14148 C CB  . SER D 390 ? 0.590 0.984 0.576 0.127  -0.015 -0.124 390 SER DDD CB  
14149 O OG  . SER D 390 ? 0.584 0.968 0.569 0.124  -0.014 -0.113 390 SER DDD OG  
14150 N N   . GLU D 391 ? 0.639 1.036 0.634 0.134  -0.024 -0.149 391 GLU DDD N   
14151 C CA  . GLU D 391 ? 0.633 1.044 0.631 0.137  -0.026 -0.162 391 GLU DDD CA  
14152 C C   . GLU D 391 ? 0.660 1.064 0.671 0.139  -0.030 -0.173 391 GLU DDD C   
14153 O O   . GLU D 391 ? 0.694 1.112 0.712 0.142  -0.030 -0.185 391 GLU DDD O   
14154 C CB  . GLU D 391 ? 0.615 1.025 0.606 0.138  -0.028 -0.160 391 GLU DDD CB  
14155 C CG  . GLU D 391 ? 0.611 1.032 0.589 0.136  -0.025 -0.151 391 GLU DDD CG  
14156 C CD  . GLU D 391 ? 0.619 1.028 0.591 0.132  -0.023 -0.136 391 GLU DDD CD  
14157 O OE1 . GLU D 391 ? 0.532 0.923 0.508 0.131  -0.025 -0.131 391 GLU DDD OE1 
14158 O OE2 . GLU D 391 ? 0.561 0.982 0.527 0.131  -0.019 -0.128 391 GLU DDD OE2 
14159 N N   . ALA D 392 ? 0.649 1.034 0.666 0.138  -0.034 -0.171 392 ALA DDD N   
14160 C CA  . ALA D 392 ? 0.637 1.013 0.668 0.140  -0.039 -0.180 392 ALA DDD CA  
14161 C C   . ALA D 392 ? 0.634 1.012 0.672 0.140  -0.037 -0.183 392 ALA DDD C   
14162 O O   . ALA D 392 ? 0.626 1.007 0.677 0.143  -0.040 -0.194 392 ALA DDD O   
14163 C CB  . ALA D 392 ? 0.593 0.948 0.627 0.138  -0.042 -0.175 392 ALA DDD CB  
14164 N N   . ALA D 393 ? 0.641 1.020 0.674 0.138  -0.033 -0.174 393 ALA DDD N   
14165 C CA  . ALA D 393 ? 0.616 0.997 0.657 0.138  -0.032 -0.175 393 ALA DDD CA  
14166 C C   . ALA D 393 ? 0.611 1.014 0.653 0.140  -0.029 -0.185 393 ALA DDD C   
14167 O O   . ALA D 393 ? 0.556 0.963 0.611 0.142  -0.031 -0.195 393 ALA DDD O   
14168 C CB  . ALA D 393 ? 0.588 0.962 0.621 0.134  -0.029 -0.162 393 ALA DDD CB  
14169 N N   . ILE D 394 ? 0.632 1.050 0.663 0.140  -0.025 -0.182 394 ILE DDD N   
14170 C CA  . ILE D 394 ? 0.686 1.128 0.717 0.142  -0.021 -0.191 394 ILE DDD CA  
14171 C C   . ILE D 394 ? 0.693 1.141 0.733 0.146  -0.025 -0.207 394 ILE DDD C   
14172 O O   . ILE D 394 ? 0.595 1.054 0.645 0.148  -0.024 -0.218 394 ILE DDD O   
14173 C CB  . ILE D 394 ? 0.708 1.163 0.723 0.141  -0.016 -0.183 394 ILE DDD CB  
14174 C CG1 . ILE D 394 ? 0.697 1.149 0.706 0.137  -0.012 -0.170 394 ILE DDD CG1 
14175 C CG2 . ILE D 394 ? 0.735 1.214 0.747 0.143  -0.014 -0.194 394 ILE DDD CG2 
14176 C CD1 . ILE D 394 ? 0.695 1.157 0.689 0.135  -0.008 -0.160 394 ILE DDD CD1 
14177 N N   . ALA D 395 ? 0.758 1.199 0.798 0.147  -0.029 -0.209 395 ALA DDD N   
14178 C CA  . ALA D 395 ? 0.773 1.217 0.822 0.151  -0.034 -0.223 395 ALA DDD CA  
14179 C C   . ALA D 395 ? 0.794 1.230 0.861 0.152  -0.038 -0.232 395 ALA DDD C   
14180 O O   . ALA D 395 ? 0.887 1.336 0.966 0.155  -0.039 -0.246 395 ALA DDD O   
14181 C CB  . ALA D 395 ? 0.734 1.168 0.780 0.151  -0.038 -0.221 395 ALA DDD CB  
14182 N N   . LYS D 396 ? 0.745 1.161 0.816 0.150  -0.040 -0.223 396 LYS DDD N   
14183 C CA  . LYS D 396 ? 0.730 1.135 0.818 0.151  -0.045 -0.229 396 LYS DDD CA  
14184 C C   . LYS D 396 ? 0.705 1.119 0.802 0.152  -0.043 -0.234 396 LYS DDD C   
14185 O O   . LYS D 396 ? 0.711 1.127 0.824 0.154  -0.046 -0.246 396 LYS DDD O   
14186 C CB  . LYS D 396 ? 0.708 1.088 0.795 0.148  -0.048 -0.218 396 LYS DDD CB  
14187 C CG  . LYS D 396 ? 0.713 1.080 0.817 0.148  -0.054 -0.223 396 LYS DDD CG  
14188 C CD  . LYS D 396 ? 0.717 1.061 0.817 0.145  -0.057 -0.210 396 LYS DDD CD  
14189 C CE  . LYS D 396 ? 0.723 1.053 0.837 0.145  -0.062 -0.212 396 LYS DDD CE  
14190 N NZ  . LYS D 396 ? 0.708 1.034 0.836 0.147  -0.068 -0.222 396 LYS DDD NZ  
14191 N N   . TYR D 397 ? 0.672 1.091 0.760 0.149  -0.037 -0.225 397 TYR DDD N   
14192 C CA  . TYR D 397 ? 0.673 1.098 0.769 0.149  -0.035 -0.228 397 TYR DDD CA  
14193 C C   . TYR D 397 ? 0.665 1.115 0.757 0.150  -0.028 -0.233 397 TYR DDD C   
14194 O O   . TYR D 397 ? 0.669 1.127 0.770 0.151  -0.026 -0.239 397 TYR DDD O   
14195 C CB  . TYR D 397 ? 0.653 1.063 0.745 0.146  -0.034 -0.214 397 TYR DDD CB  
14196 C CG  . TYR D 397 ? 0.629 1.015 0.726 0.145  -0.041 -0.210 397 TYR DDD CG  
14197 C CD1 . TYR D 397 ? 0.634 1.014 0.749 0.146  -0.046 -0.217 397 TYR DDD CD1 
14198 C CD2 . TYR D 397 ? 0.597 0.968 0.684 0.142  -0.042 -0.199 397 TYR DDD CD2 
14199 C CE1 . TYR D 397 ? 0.619 0.977 0.738 0.145  -0.052 -0.212 397 TYR DDD CE1 
14200 C CE2 . TYR D 397 ? 0.577 0.928 0.669 0.141  -0.047 -0.195 397 TYR DDD CE2 
14201 C CZ  . TYR D 397 ? 0.610 0.954 0.717 0.142  -0.053 -0.201 397 TYR DDD CZ  
14202 O OH  . TYR D 397 ? 0.598 0.922 0.709 0.141  -0.058 -0.196 397 TYR DDD OH  
14203 N N   . GLY D 398 ? 0.685 1.147 0.763 0.150  -0.025 -0.231 398 GLY DDD N   
14204 C CA  . GLY D 398 ? 0.683 1.169 0.753 0.150  -0.018 -0.233 398 GLY DDD CA  
14205 C C   . GLY D 398 ? 0.686 1.171 0.742 0.146  -0.012 -0.218 398 GLY DDD C   
14206 O O   . GLY D 398 ? 0.673 1.144 0.733 0.144  -0.013 -0.211 398 GLY DDD O   
14207 N N   . GLU D 399 ? 0.802 1.303 0.845 0.145  -0.007 -0.215 399 GLU DDD N   
14208 C CA  . GLU D 399 ? 0.861 1.365 0.890 0.142  -0.001 -0.200 399 GLU DDD CA  
14209 C C   . GLU D 399 ? 0.847 1.350 0.884 0.140  0.002  -0.197 399 GLU DDD C   
14210 O O   . GLU D 399 ? 0.862 1.356 0.893 0.137  0.004  -0.183 399 GLU DDD O   
14211 C CB  . GLU D 399 ? 0.954 1.481 0.970 0.142  0.004  -0.201 399 GLU DDD CB  
14212 C CG  . GLU D 399 ? 1.013 1.544 1.016 0.138  0.009  -0.185 399 GLU DDD CG  
14213 C CD  . GLU D 399 ? 1.097 1.612 1.090 0.136  0.006  -0.172 399 GLU DDD CD  
14214 O OE1 . GLU D 399 ? 1.143 1.659 1.130 0.138  0.003  -0.175 399 GLU DDD OE1 
14215 O OE2 . GLU D 399 ? 1.140 1.644 1.130 0.133  0.008  -0.159 399 GLU DDD OE2 
14216 N N   . ASP D 400 ? 0.823 1.337 0.873 0.142  0.003  -0.209 400 ASP DDD N   
14217 C CA  . ASP D 400 ? 0.810 1.326 0.867 0.140  0.007  -0.208 400 ASP DDD CA  
14218 C C   . ASP D 400 ? 0.745 1.240 0.814 0.140  0.002  -0.205 400 ASP DDD C   
14219 O O   . ASP D 400 ? 0.751 1.244 0.824 0.138  0.004  -0.200 400 ASP DDD O   
14220 C CB  . ASP D 400 ? 0.833 1.372 0.899 0.142  0.011  -0.222 400 ASP DDD CB  
14221 C CG  . ASP D 400 ? 0.855 1.415 0.907 0.140  0.019  -0.217 400 ASP DDD CG  
14222 O OD1 . ASP D 400 ? 0.865 1.427 0.901 0.139  0.020  -0.209 400 ASP DDD OD1 
14223 O OD2 . ASP D 400 ? 0.833 1.406 0.890 0.139  0.025  -0.220 400 ASP DDD OD2 
14224 N N   . ASP D 401 ? 0.686 1.165 0.761 0.142  -0.006 -0.209 401 ASP DDD N   
14225 C CA  . ASP D 401 ? 0.686 1.144 0.772 0.141  -0.011 -0.206 401 ASP DDD CA  
14226 C C   . ASP D 401 ? 0.658 1.097 0.732 0.138  -0.013 -0.191 401 ASP DDD C   
14227 O O   . ASP D 401 ? 0.653 1.073 0.732 0.138  -0.018 -0.187 401 ASP DDD O   
14228 C CB  . ASP D 401 ? 0.669 1.121 0.768 0.145  -0.018 -0.219 401 ASP DDD CB  
14229 C CG  . ASP D 401 ? 0.669 1.106 0.784 0.145  -0.023 -0.220 401 ASP DDD CG  
14230 O OD1 . ASP D 401 ? 0.642 1.080 0.759 0.143  -0.020 -0.214 401 ASP DDD OD1 
14231 O OD2 . ASP D 401 ? 0.659 1.085 0.784 0.147  -0.030 -0.226 401 ASP DDD OD2 
14232 N N   . ILE D 402 ? 0.610 1.055 0.668 0.137  -0.009 -0.182 402 ILE DDD N   
14233 C CA  . ILE D 402 ? 0.584 1.014 0.632 0.134  -0.009 -0.168 402 ILE DDD CA  
14234 C C   . ILE D 402 ? 0.556 0.989 0.595 0.130  -0.003 -0.155 402 ILE DDD C   
14235 O O   . ILE D 402 ? 0.508 0.960 0.541 0.130  0.002  -0.155 402 ILE DDD O   
14236 C CB  . ILE D 402 ? 0.609 1.040 0.646 0.134  -0.011 -0.168 402 ILE DDD CB  
14237 C CG1 . ILE D 402 ? 0.619 1.041 0.665 0.137  -0.017 -0.177 402 ILE DDD CG1 
14238 C CG2 . ILE D 402 ? 0.594 1.015 0.620 0.131  -0.010 -0.153 402 ILE DDD CG2 
14239 C CD1 . ILE D 402 ? 0.621 1.021 0.676 0.136  -0.023 -0.175 402 ILE DDD CD1 
14240 N N   . GLU D 403 ? 0.552 0.969 0.592 0.128  -0.005 -0.145 403 GLU DDD N   
14241 C CA  . GLU D 403 ? 0.612 1.029 0.644 0.124  -0.000 -0.132 403 GLU DDD CA  
14242 C C   . GLU D 403 ? 0.572 0.973 0.595 0.122  -0.003 -0.122 403 GLU DDD C   
14243 O O   . GLU D 403 ? 0.562 0.946 0.589 0.123  -0.008 -0.123 403 GLU DDD O   
14244 C CB  . GLU D 403 ? 0.657 1.071 0.697 0.123  0.001  -0.129 403 GLU DDD CB  
14245 C CG  . GLU D 403 ? 0.702 1.126 0.737 0.120  0.008  -0.120 403 GLU DDD CG  
14246 C CD  . GLU D 403 ? 0.731 1.178 0.765 0.121  0.014  -0.126 403 GLU DDD CD  
14247 O OE1 . GLU D 403 ? 0.764 1.219 0.808 0.123  0.015  -0.135 403 GLU DDD OE1 
14248 O OE2 . GLU D 403 ? 0.736 1.195 0.759 0.120  0.018  -0.120 403 GLU DDD OE2 
14249 N N   . GLU D 404 ? 0.562 0.968 0.575 0.121  0.001  -0.113 404 GLU DDD N   
14250 C CA  . GLU D 404 ? 0.538 0.931 0.544 0.118  -0.001 -0.102 404 GLU DDD CA  
14251 C C   . GLU D 404 ? 0.501 0.891 0.505 0.115  0.003  -0.091 404 GLU DDD C   
14252 O O   . GLU D 404 ? 0.467 0.871 0.466 0.114  0.008  -0.086 404 GLU DDD O   
14253 C CB  . GLU D 404 ? 0.604 1.003 0.599 0.119  -0.001 -0.102 404 GLU DDD CB  
14254 C CG  . GLU D 404 ? 0.646 1.050 0.643 0.123  -0.004 -0.114 404 GLU DDD CG  
14255 C CD  . GLU D 404 ? 0.672 1.087 0.660 0.124  -0.004 -0.115 404 GLU DDD CD  
14256 O OE1 . GLU D 404 ? 0.633 1.043 0.614 0.122  -0.004 -0.105 404 GLU DDD OE1 
14257 O OE2 . GLU D 404 ? 0.724 1.153 0.713 0.127  -0.004 -0.126 404 GLU DDD OE2 
14258 N N   . TYR D 405 ? 0.497 0.870 0.505 0.113  0.000  -0.086 405 TYR DDD N   
14259 C CA  . TYR D 405 ? 0.460 0.828 0.468 0.110  0.003  -0.075 405 TYR DDD CA  
14260 C C   . TYR D 405 ? 0.446 0.802 0.447 0.108  0.001  -0.067 405 TYR DDD C   
14261 O O   . TYR D 405 ? 0.425 0.770 0.425 0.109  -0.003 -0.070 405 TYR DDD O   
14262 C CB  . TYR D 405 ? 0.449 0.805 0.466 0.109  0.001  -0.076 405 TYR DDD CB  
14263 C CG  . TYR D 405 ? 0.446 0.811 0.472 0.111  0.002  -0.083 405 TYR DDD CG  
14264 C CD1 . TYR D 405 ? 0.443 0.817 0.472 0.109  0.007  -0.079 405 TYR DDD CD1 
14265 C CD2 . TYR D 405 ? 0.444 0.810 0.476 0.114  -0.001 -0.095 405 TYR DDD CD2 
14266 C CE1 . TYR D 405 ? 0.453 0.836 0.491 0.110  0.009  -0.086 405 TYR DDD CE1 
14267 C CE2 . TYR D 405 ? 0.475 0.850 0.517 0.115  -0.000 -0.102 405 TYR DDD CE2 
14268 C CZ  . TYR D 405 ? 0.468 0.852 0.513 0.113  0.005  -0.098 405 TYR DDD CZ  
14269 O OH  . TYR D 405 ? 0.481 0.873 0.536 0.115  0.006  -0.105 405 TYR DDD OH  
14270 N N   . LEU D 406 ? 0.425 0.785 0.421 0.106  0.005  -0.056 406 LEU DDD N   
14271 C CA  . LEU D 406 ? 0.433 0.785 0.424 0.104  0.004  -0.049 406 LEU DDD CA  
14272 C C   . LEU D 406 ? 0.438 0.791 0.429 0.101  0.007  -0.037 406 LEU DDD C   
14273 O O   . LEU D 406 ? 0.410 0.772 0.404 0.100  0.011  -0.034 406 LEU DDD O   
14274 C CB  . LEU D 406 ? 0.428 0.789 0.412 0.106  0.003  -0.052 406 LEU DDD CB  
14275 C CG  . LEU D 406 ? 0.438 0.818 0.415 0.107  0.007  -0.049 406 LEU DDD CG  
14276 C CD1 . LEU D 406 ? 0.430 0.814 0.400 0.108  0.005  -0.051 406 LEU DDD CD1 
14277 C CD2 . LEU D 406 ? 0.441 0.836 0.421 0.108  0.010  -0.055 406 LEU DDD CD2 
14278 N N   . SER D 407 ? 0.422 0.762 0.411 0.100  0.005  -0.031 407 SER DDD N   
14279 C CA  . SER D 407 ? 0.433 0.771 0.424 0.097  0.007  -0.020 407 SER DDD CA  
14280 C C   . SER D 407 ? 0.432 0.764 0.419 0.096  0.005  -0.015 407 SER DDD C   
14281 O O   . SER D 407 ? 0.446 0.767 0.431 0.097  0.002  -0.021 407 SER DDD O   
14282 C CB  . SER D 407 ? 0.412 0.739 0.411 0.095  0.007  -0.018 407 SER DDD CB  
14283 O OG  . SER D 407 ? 0.412 0.737 0.413 0.092  0.009  -0.007 407 SER DDD OG  
14284 N N   . GLU D 408 ? 0.433 0.771 0.416 0.095  0.007  -0.007 408 GLU DDD N   
14285 C CA  . GLU D 408 ? 0.432 0.765 0.413 0.094  0.005  -0.001 408 GLU DDD CA  
14286 C C   . GLU D 408 ? 0.416 0.743 0.404 0.091  0.006  0.009  408 GLU DDD C   
14287 O O   . GLU D 408 ? 0.393 0.729 0.383 0.090  0.010  0.015  408 GLU DDD O   
14288 C CB  . GLU D 408 ? 0.467 0.814 0.440 0.095  0.005  0.001  408 GLU DDD CB  
14289 C CG  . GLU D 408 ? 0.496 0.837 0.467 0.095  0.002  0.004  408 GLU DDD CG  
14290 C CD  . GLU D 408 ? 0.528 0.883 0.490 0.097  0.002  0.004  408 GLU DDD CD  
14291 O OE1 . GLU D 408 ? 0.595 0.966 0.554 0.098  0.005  0.007  408 GLU DDD OE1 
14292 O OE2 . GLU D 408 ? 0.588 0.940 0.548 0.099  -0.002 0.002  408 GLU DDD OE2 
14293 N N   . PHE D 409 ? 0.400 0.713 0.391 0.090  0.004  0.010  409 PHE DDD N   
14294 C CA  . PHE D 409 ? 0.361 0.667 0.360 0.087  0.005  0.018  409 PHE DDD CA  
14295 C C   . PHE D 409 ? 0.357 0.650 0.357 0.086  0.002  0.019  409 PHE DDD C   
14296 O O   . PHE D 409 ? 0.325 0.614 0.320 0.087  -0.000 0.013  409 PHE DDD O   
14297 C CB  . PHE D 409 ? 0.356 0.654 0.360 0.086  0.006  0.015  409 PHE DDD CB  
14298 C CG  . PHE D 409 ? 0.332 0.619 0.335 0.086  0.003  0.005  409 PHE DDD CG  
14299 C CD1 . PHE D 409 ? 0.320 0.611 0.318 0.089  0.002  -0.003 409 PHE DDD CD1 
14300 C CD2 . PHE D 409 ? 0.329 0.602 0.336 0.084  0.001  0.005  409 PHE DDD CD2 
14301 C CE1 . PHE D 409 ? 0.333 0.613 0.330 0.090  -0.001 -0.011 409 PHE DDD CE1 
14302 C CE2 . PHE D 409 ? 0.322 0.585 0.327 0.085  -0.002 -0.003 409 PHE DDD CE2 
14303 C CZ  . PHE D 409 ? 0.346 0.613 0.346 0.087  -0.003 -0.010 409 PHE DDD CZ  
14304 N N   . SER D 410 ? 0.334 0.621 0.342 0.083  0.003  0.025  410 SER DDD N   
14305 C CA  . SER D 410 ? 0.320 0.595 0.332 0.081  0.001  0.026  410 SER DDD CA  
14306 C C   . SER D 410 ? 0.316 0.578 0.332 0.080  0.000  0.022  410 SER DDD C   
14307 O O   . SER D 410 ? 0.313 0.575 0.334 0.079  0.002  0.023  410 SER DDD O   
14308 C CB  . SER D 410 ? 0.317 0.594 0.334 0.080  0.001  0.036  410 SER DDD CB  
14309 O OG  . SER D 410 ? 0.319 0.586 0.343 0.078  -0.000 0.036  410 SER DDD OG  
14310 N N   . THR D 411 ? 0.317 0.569 0.333 0.079  -0.002 0.016  411 THR DDD N   
14311 C CA  . THR D 411 ? 0.306 0.545 0.327 0.077  -0.002 0.014  411 THR DDD CA  
14312 C C   . THR D 411 ? 0.290 0.529 0.320 0.075  -0.001 0.022  411 THR DDD C   
14313 O O   . THR D 411 ? 0.280 0.525 0.314 0.075  -0.000 0.028  411 THR DDD O   
14314 C CB  . THR D 411 ? 0.318 0.548 0.336 0.076  -0.004 0.009  411 THR DDD CB  
14315 O OG1 . THR D 411 ? 0.304 0.535 0.314 0.079  -0.005 0.003  411 THR DDD OG1 
14316 C CG2 . THR D 411 ? 0.328 0.546 0.350 0.074  -0.004 0.006  411 THR DDD CG2 
14317 N N   . LEU D 412 ? 0.303 0.535 0.338 0.073  -0.000 0.021  412 LEU DDD N   
14318 C CA  . LEU D 412 ? 0.324 0.555 0.371 0.071  0.001  0.027  412 LEU DDD CA  
14319 C C   . LEU D 412 ? 0.327 0.554 0.380 0.069  0.000  0.029  412 LEU DDD C   
14320 O O   . LEU D 412 ? 0.366 0.597 0.426 0.069  0.001  0.037  412 LEU DDD O   
14321 C CB  . LEU D 412 ? 0.348 0.571 0.398 0.069  0.001  0.022  412 LEU DDD CB  
14322 C CG  . LEU D 412 ? 0.356 0.575 0.418 0.066  0.002  0.025  412 LEU DDD CG  
14323 C CD1 . LEU D 412 ? 0.367 0.596 0.436 0.067  0.004  0.034  412 LEU DDD CD1 
14324 C CD2 . LEU D 412 ? 0.328 0.540 0.391 0.065  0.001  0.020  412 LEU DDD CD2 
14325 N N   . GLU D 413 ? 0.329 0.547 0.380 0.068  -0.001 0.023  413 GLU DDD N   
14326 C CA  . GLU D 413 ? 0.329 0.541 0.386 0.067  -0.002 0.024  413 GLU DDD CA  
14327 C C   . GLU D 413 ? 0.313 0.532 0.370 0.068  -0.002 0.029  413 GLU DDD C   
14328 O O   . GLU D 413 ? 0.279 0.498 0.345 0.067  -0.003 0.034  413 GLU DDD O   
14329 C CB  . GLU D 413 ? 0.360 0.562 0.411 0.066  -0.003 0.015  413 GLU DDD CB  
14330 C CG  . GLU D 413 ? 0.405 0.600 0.455 0.064  -0.002 0.010  413 GLU DDD CG  
14331 C CD  . GLU D 413 ? 0.417 0.612 0.456 0.066  -0.003 0.005  413 GLU DDD CD  
14332 O OE1 . GLU D 413 ? 0.468 0.671 0.505 0.068  -0.003 0.008  413 GLU DDD OE1 
14333 O OE2 . GLU D 413 ? 0.429 0.617 0.462 0.065  -0.004 -0.001 413 GLU DDD OE2 
14334 N N   . ILE D 414 ? 0.300 0.524 0.346 0.071  -0.003 0.027  414 ILE DDD N   
14335 C CA  . ILE D 414 ? 0.299 0.531 0.343 0.073  -0.004 0.031  414 ILE DDD CA  
14336 C C   . ILE D 414 ? 0.285 0.526 0.333 0.073  -0.003 0.041  414 ILE DDD C   
14337 O O   . ILE D 414 ? 0.279 0.524 0.333 0.072  -0.004 0.048  414 ILE DDD O   
14338 C CB  . ILE D 414 ? 0.320 0.557 0.352 0.075  -0.005 0.026  414 ILE DDD CB  
14339 C CG1 . ILE D 414 ? 0.323 0.549 0.351 0.075  -0.006 0.016  414 ILE DDD CG1 
14340 C CG2 . ILE D 414 ? 0.323 0.567 0.353 0.077  -0.007 0.029  414 ILE DDD CG2 
14341 C CD1 . ILE D 414 ? 0.316 0.535 0.348 0.074  -0.007 0.014  414 ILE DDD CD1 
14342 N N   . ALA D 415 ? 0.295 0.542 0.342 0.073  -0.001 0.043  415 ALA DDD N   
14343 C CA  . ALA D 415 ? 0.299 0.555 0.350 0.072  0.000  0.052  415 ALA DDD CA  
14344 C C   . ALA D 415 ? 0.320 0.571 0.385 0.070  -0.000 0.059  415 ALA DDD C   
14345 O O   . ALA D 415 ? 0.311 0.569 0.380 0.070  -0.001 0.068  415 ALA DDD O   
14346 C CB  . ALA D 415 ? 0.303 0.563 0.353 0.072  0.003  0.052  415 ALA DDD CB  
14347 N N   . ALA D 416 ? 0.314 0.555 0.387 0.068  -0.000 0.055  416 ALA DDD N   
14348 C CA  . ALA D 416 ? 0.324 0.561 0.413 0.066  -0.000 0.060  416 ALA DDD CA  
14349 C C   . ALA D 416 ? 0.344 0.578 0.438 0.066  -0.003 0.062  416 ALA DDD C   
14350 O O   . ALA D 416 ? 0.372 0.604 0.478 0.064  -0.003 0.068  416 ALA DDD O   
14351 C CB  . ALA D 416 ? 0.328 0.554 0.421 0.064  0.000  0.053  416 ALA DDD CB  
14352 N N   . ALA D 417 ? 0.339 0.571 0.423 0.067  -0.004 0.056  417 ALA DDD N   
14353 C CA  . ALA D 417 ? 0.349 0.579 0.438 0.067  -0.007 0.056  417 ALA DDD CA  
14354 C C   . ALA D 417 ? 0.374 0.614 0.462 0.069  -0.008 0.066  417 ALA DDD C   
14355 O O   . ALA D 417 ? 0.375 0.612 0.471 0.068  -0.011 0.070  417 ALA DDD O   
14356 C CB  . ALA D 417 ? 0.336 0.561 0.414 0.068  -0.007 0.046  417 ALA DDD CB  
14357 N N   . HIS D 418 ? 0.415 0.664 0.493 0.070  -0.007 0.070  418 HIS DDD N   
14358 C CA  . HIS D 418 ? 0.405 0.665 0.480 0.071  -0.009 0.080  418 HIS DDD CA  
14359 C C   . HIS D 418 ? 0.406 0.665 0.477 0.073  -0.012 0.076  418 HIS DDD C   
14360 O O   . HIS D 418 ? 0.414 0.674 0.492 0.073  -0.015 0.083  418 HIS DDD O   
14361 C CB  . HIS D 418 ? 0.415 0.677 0.505 0.069  -0.009 0.091  418 HIS DDD CB  
14362 C CG  . HIS D 418 ? 0.440 0.705 0.533 0.068  -0.006 0.096  418 HIS DDD CG  
14363 N ND1 . HIS D 418 ? 0.446 0.723 0.531 0.068  -0.004 0.102  418 HIS DDD ND1 
14364 C CD2 . HIS D 418 ? 0.459 0.717 0.563 0.066  -0.004 0.095  418 HIS DDD CD2 
14365 C CE1 . HIS D 418 ? 0.441 0.717 0.532 0.067  -0.001 0.104  418 HIS DDD CE1 
14366 N NE2 . HIS D 418 ? 0.425 0.691 0.528 0.065  -0.001 0.100  418 HIS DDD NE2 
14367 N N   . ARG D 419 ? 0.396 0.654 0.456 0.075  -0.012 0.067  419 ARG DDD N   
14368 C CA  . ARG D 419 ? 0.415 0.673 0.469 0.077  -0.015 0.062  419 ARG DDD CA  
14369 C C   . ARG D 419 ? 0.467 0.737 0.515 0.079  -0.017 0.070  419 ARG DDD C   
14370 O O   . ARG D 419 ? 0.511 0.791 0.550 0.079  -0.015 0.073  419 ARG DDD O   
14371 C CB  . ARG D 419 ? 0.388 0.644 0.431 0.078  -0.014 0.051  419 ARG DDD CB  
14372 C CG  . ARG D 419 ? 0.364 0.608 0.411 0.076  -0.013 0.042  419 ARG DDD CG  
14373 C CD  . ARG D 419 ? 0.359 0.600 0.398 0.078  -0.013 0.032  419 ARG DDD CD  
14374 N NE  . ARG D 419 ? 0.345 0.573 0.388 0.075  -0.012 0.025  419 ARG DDD NE  
14375 C CZ  . ARG D 419 ? 0.354 0.576 0.392 0.076  -0.012 0.017  419 ARG DDD CZ  
14376 N NH1 . ARG D 419 ? 0.346 0.574 0.375 0.078  -0.013 0.013  419 ARG DDD NH1 
14377 N NH2 . ARG D 419 ? 0.369 0.580 0.411 0.073  -0.011 0.011  419 ARG DDD NH2 
14378 N N   . GLU D 420 ? 0.487 0.757 0.541 0.079  -0.021 0.073  420 GLU DDD N   
14379 C CA  . GLU D 420 ? 0.573 0.854 0.623 0.080  -0.024 0.082  420 GLU DDD CA  
14380 C C   . GLU D 420 ? 0.551 0.834 0.592 0.083  -0.027 0.075  420 GLU DDD C   
14381 O O   . GLU D 420 ? 0.521 0.795 0.567 0.083  -0.028 0.067  420 GLU DDD O   
14382 C CB  . GLU D 420 ? 0.631 0.910 0.695 0.079  -0.027 0.092  420 GLU DDD CB  
14383 C CG  . GLU D 420 ? 0.661 0.939 0.733 0.076  -0.024 0.101  420 GLU DDD CG  
14384 C CD  . GLU D 420 ? 0.692 0.961 0.783 0.074  -0.026 0.105  420 GLU DDD CD  
14385 O OE1 . GLU D 420 ? 0.708 0.975 0.807 0.074  -0.030 0.107  420 GLU DDD OE1 
14386 O OE2 . GLU D 420 ? 0.715 0.979 0.814 0.072  -0.022 0.104  420 GLU DDD OE2 
14387 N N   . LYS D 421 ? 0.566 0.862 0.596 0.085  -0.029 0.079  421 LYS DDD N   
14388 C CA  . LYS D 421 ? 0.579 0.880 0.603 0.088  -0.033 0.075  421 LYS DDD CA  
14389 C C   . LYS D 421 ? 0.577 0.871 0.612 0.087  -0.037 0.078  421 LYS DDD C   
14390 O O   . LYS D 421 ? 0.573 0.865 0.619 0.086  -0.038 0.088  421 LYS DDD O   
14391 C CB  . LYS D 421 ? 0.578 0.894 0.589 0.089  -0.034 0.082  421 LYS DDD CB  
14392 C CG  . LYS D 421 ? 0.609 0.935 0.607 0.091  -0.031 0.076  421 LYS DDD CG  
14393 C CD  . LYS D 421 ? 0.631 0.972 0.617 0.092  -0.033 0.081  421 LYS DDD CD  
14394 C CE  . LYS D 421 ? 0.642 0.993 0.615 0.095  -0.031 0.071  421 LYS DDD CE  
14395 N NZ  . LYS D 421 ? 0.657 1.019 0.621 0.094  -0.027 0.075  421 LYS DDD NZ  
14396 N N   . PRO D 422 ? 0.586 0.877 0.621 0.089  -0.040 0.070  422 PRO DDD N   
14397 C CA  . PRO D 422 ? 0.635 0.923 0.681 0.089  -0.045 0.073  422 PRO DDD CA  
14398 C C   . PRO D 422 ? 0.692 0.991 0.734 0.090  -0.049 0.086  422 PRO DDD C   
14399 O O   . PRO D 422 ? 0.650 0.961 0.678 0.092  -0.049 0.087  422 PRO DDD O   
14400 C CB  . PRO D 422 ? 0.626 0.911 0.668 0.091  -0.047 0.062  422 PRO DDD CB  
14401 C CG  . PRO D 422 ? 0.607 0.890 0.640 0.092  -0.043 0.052  422 PRO DDD CG  
14402 C CD  . PRO D 422 ? 0.586 0.876 0.611 0.091  -0.039 0.058  422 PRO DDD CD  
14403 N N   . GLU D 423 ? 0.742 1.038 0.797 0.089  -0.053 0.095  423 GLU DDD N   
14404 C CA  . GLU D 423 ? 0.781 1.088 0.834 0.089  -0.056 0.109  423 GLU DDD CA  
14405 C C   . GLU D 423 ? 0.767 1.084 0.808 0.092  -0.061 0.109  423 GLU DDD C   
14406 O O   . GLU D 423 ? 0.712 1.041 0.745 0.092  -0.063 0.120  423 GLU DDD O   
14407 C CB  . GLU D 423 ? 0.849 1.148 0.920 0.087  -0.058 0.119  423 GLU DDD CB  
14408 C CG  . GLU D 423 ? 0.903 1.202 0.984 0.087  -0.066 0.125  423 GLU DDD CG  
14409 C CD  . GLU D 423 ? 0.925 1.220 1.025 0.085  -0.067 0.137  423 GLU DDD CD  
14410 O OE1 . GLU D 423 ? 0.850 1.145 0.957 0.085  -0.074 0.145  423 GLU DDD OE1 
14411 O OE2 . GLU D 423 ? 0.908 1.197 1.015 0.082  -0.062 0.137  423 GLU DDD OE2 
14412 N N   . HIS D 424 ? 0.776 1.091 0.815 0.094  -0.063 0.098  424 HIS DDD N   
14413 C CA  . HIS D 424 ? 0.854 1.179 0.881 0.097  -0.068 0.096  424 HIS DDD CA  
14414 C C   . HIS D 424 ? 0.878 1.216 0.886 0.099  -0.065 0.093  424 HIS DDD C   
14415 O O   . HIS D 424 ? 0.867 1.215 0.864 0.101  -0.068 0.093  424 HIS DDD O   
14416 C CB  . HIS D 424 ? 0.857 1.175 0.889 0.099  -0.071 0.085  424 HIS DDD CB  
14417 C CG  . HIS D 424 ? 0.896 1.208 0.928 0.099  -0.067 0.071  424 HIS DDD CG  
14418 N ND1 . HIS D 424 ? 0.932 1.249 0.949 0.101  -0.065 0.062  424 HIS DDD ND1 
14419 C CD2 . HIS D 424 ? 0.891 1.189 0.933 0.098  -0.064 0.064  424 HIS DDD CD2 
14420 C CE1 . HIS D 424 ? 0.883 1.191 0.903 0.101  -0.061 0.050  424 HIS DDD CE1 
14421 N NE2 . HIS D 424 ? 0.873 1.169 0.908 0.099  -0.060 0.051  424 HIS DDD NE2 
14422 N N   . LEU D 425 ? 0.827 1.163 0.832 0.097  -0.058 0.090  425 LEU DDD N   
14423 C CA  . LEU D 425 ? 0.863 1.210 0.851 0.098  -0.054 0.086  425 LEU DDD CA  
14424 C C   . LEU D 425 ? 0.880 1.236 0.864 0.096  -0.051 0.097  425 LEU DDD C   
14425 O O   . LEU D 425 ? 0.822 1.187 0.794 0.097  -0.047 0.094  425 LEU DDD O   
14426 C CB  . LEU D 425 ? 0.872 1.211 0.859 0.099  -0.050 0.072  425 LEU DDD CB  
14427 C CG  . LEU D 425 ? 0.893 1.227 0.881 0.101  -0.053 0.060  425 LEU DDD CG  
14428 C CD1 . LEU D 425 ? 0.892 1.216 0.884 0.100  -0.048 0.049  425 LEU DDD CD1 
14429 C CD2 . LEU D 425 ? 0.928 1.276 0.903 0.104  -0.055 0.055  425 LEU DDD CD2 
14430 N N   . ARG D 426 ? 0.923 1.275 0.917 0.094  -0.052 0.109  426 ARG DDD N   
14431 C CA  . ARG D 426 ? 0.973 1.331 0.965 0.091  -0.048 0.121  426 ARG DDD CA  
14432 C C   . ARG D 426 ? 1.050 1.425 1.029 0.092  -0.051 0.130  426 ARG DDD C   
14433 O O   . ARG D 426 ? 1.043 1.420 1.022 0.093  -0.057 0.134  426 ARG DDD O   
14434 C CB  . ARG D 426 ? 0.941 1.289 0.952 0.088  -0.049 0.131  426 ARG DDD CB  
14435 C CG  . ARG D 426 ? 0.902 1.236 0.925 0.087  -0.046 0.124  426 ARG DDD CG  
14436 C CD  . ARG D 426 ? 0.874 1.209 0.892 0.086  -0.039 0.122  426 ARG DDD CD  
14437 N NE  . ARG D 426 ? 0.850 1.192 0.870 0.083  -0.038 0.136  426 ARG DDD NE  
14438 C CZ  . ARG D 426 ? 0.844 1.180 0.879 0.081  -0.037 0.145  426 ARG DDD CZ  
14439 N NH1 . ARG D 426 ? 0.781 1.102 0.831 0.080  -0.038 0.141  426 ARG DDD NH1 
14440 N NH2 . ARG D 426 ? 0.870 1.213 0.905 0.078  -0.036 0.158  426 ARG DDD NH2 
14441 N N   . GLU D 427 ? 1.123 1.509 1.091 0.091  -0.046 0.133  427 GLU DDD N   
14442 C CA  . GLU D 427 ? 1.160 1.565 1.113 0.091  -0.047 0.140  427 GLU DDD CA  
14443 C C   . GLU D 427 ? 1.183 1.592 1.139 0.088  -0.045 0.158  427 GLU DDD C   
14444 O O   . GLU D 427 ? 1.249 1.671 1.195 0.087  -0.048 0.168  427 GLU DDD O   
14445 C CB  . GLU D 427 ? 1.188 1.603 1.125 0.093  -0.042 0.130  427 GLU DDD CB  
14446 C CG  . GLU D 427 ? 1.192 1.616 1.118 0.096  -0.047 0.120  427 GLU DDD CG  
14447 C CD  . GLU D 427 ? 1.182 1.619 1.093 0.098  -0.043 0.110  427 GLU DDD CD  
14448 O OE1 . GLU D 427 ? 1.165 1.599 1.075 0.101  -0.043 0.095  427 GLU DDD OE1 
14449 O OE2 . GLU D 427 ? 1.080 1.531 0.982 0.097  -0.039 0.116  427 GLU DDD OE2 
14450 N N   . ASN D 428 ? 1.145 1.544 1.114 0.085  -0.042 0.161  428 ASN DDD N   
14451 C CA  . ASN D 428 ? 1.143 1.546 1.117 0.081  -0.040 0.178  428 ASN DDD CA  
14452 C C   . ASN D 428 ? 1.133 1.520 1.126 0.079  -0.037 0.179  428 ASN DDD C   
14453 O O   . ASN D 428 ? 1.150 1.524 1.152 0.081  -0.039 0.169  428 ASN DDD O   
14454 C CB  . ASN D 428 ? 1.173 1.591 1.132 0.080  -0.034 0.180  428 ASN DDD CB  
14455 C CG  . ASN D 428 ? 1.231 1.649 1.186 0.081  -0.028 0.166  428 ASN DDD CG  
14456 O OD1 . ASN D 428 ? 1.221 1.627 1.187 0.081  -0.025 0.161  428 ASN DDD OD1 
14457 N ND2 . ASN D 428 ? 1.268 1.700 1.207 0.083  -0.026 0.158  428 ASN DDD ND2 
14458 N N   . GLU D 429 ? 1.125 1.514 1.123 0.076  -0.034 0.190  429 GLU DDD N   
14459 C CA  . GLU D 429 ? 1.130 1.507 1.148 0.074  -0.031 0.192  429 GLU DDD CA  
14460 C C   . GLU D 429 ? 1.128 1.503 1.144 0.073  -0.024 0.182  429 GLU DDD C   
14461 O O   . GLU D 429 ? 1.121 1.486 1.152 0.071  -0.022 0.182  429 GLU DDD O   
14462 C CB  . GLU D 429 ? 1.145 1.524 1.173 0.070  -0.032 0.210  429 GLU DDD CB  
14463 C CG  . GLU D 429 ? 1.161 1.542 1.188 0.070  -0.040 0.221  429 GLU DDD CG  
14464 C CD  . GLU D 429 ? 1.137 1.508 1.171 0.073  -0.046 0.214  429 GLU DDD CD  
14465 O OE1 . GLU D 429 ? 1.091 1.449 1.142 0.073  -0.046 0.208  429 GLU DDD OE1 
14466 O OE2 . GLU D 429 ? 1.129 1.508 1.152 0.075  -0.051 0.213  429 GLU DDD OE2 
14467 N N   . MET D 430 ? 1.106 1.490 1.106 0.075  -0.021 0.173  430 MET DDD N   
14468 C CA  . MET D 430 ? 1.075 1.460 1.072 0.075  -0.014 0.163  430 MET DDD CA  
14469 C C   . MET D 430 ? 0.995 1.376 0.984 0.078  -0.015 0.146  430 MET DDD C   
14470 O O   . MET D 430 ? 1.000 1.382 0.986 0.079  -0.010 0.137  430 MET DDD O   
14471 C CB  . MET D 430 ? 1.084 1.486 1.068 0.074  -0.010 0.169  430 MET DDD CB  
14472 C CG  . MET D 430 ? 1.127 1.531 1.114 0.072  -0.003 0.167  430 MET DDD CG  
14473 S SD  . MET D 430 ? 1.117 1.543 1.091 0.070  0.003  0.177  430 MET DDD SD  
14474 C CE  . MET D 430 ? 1.092 1.523 1.059 0.072  0.009  0.160  430 MET DDD CE  
14475 N N   . ASP D 431 ? 0.872 1.249 0.860 0.081  -0.020 0.142  431 ASP DDD N   
14476 C CA  . ASP D 431 ? 0.793 1.167 0.776 0.084  -0.022 0.126  431 ASP DDD CA  
14477 C C   . ASP D 431 ? 0.744 1.100 0.740 0.084  -0.023 0.120  431 ASP DDD C   
14478 O O   . ASP D 431 ? 0.712 1.063 0.706 0.086  -0.026 0.110  431 ASP DDD O   
14479 C CB  . ASP D 431 ? 0.785 1.168 0.756 0.086  -0.026 0.127  431 ASP DDD CB  
14480 C CG  . ASP D 431 ? 0.748 1.127 0.715 0.089  -0.029 0.113  431 ASP DDD CG  
14481 O OD1 . ASP D 431 ? 0.795 1.172 0.759 0.091  -0.026 0.101  431 ASP DDD OD1 
14482 O OD2 . ASP D 431 ? 0.647 1.026 0.615 0.091  -0.035 0.115  431 ASP DDD OD2 
14483 N N   . PHE D 432 ? 0.645 0.991 0.655 0.081  -0.022 0.124  432 PHE DDD N   
14484 C CA  . PHE D 432 ? 0.604 0.934 0.628 0.080  -0.024 0.121  432 PHE DDD CA  
14485 C C   . PHE D 432 ? 0.573 0.894 0.596 0.082  -0.022 0.106  432 PHE DDD C   
14486 O O   . PHE D 432 ? 0.519 0.831 0.547 0.082  -0.024 0.099  432 PHE DDD O   
14487 C CB  . PHE D 432 ? 0.615 0.940 0.655 0.077  -0.022 0.131  432 PHE DDD CB  
14488 C CG  . PHE D 432 ? 0.623 0.951 0.662 0.075  -0.017 0.133  432 PHE DDD CG  
14489 C CD1 . PHE D 432 ? 0.602 0.921 0.646 0.075  -0.013 0.124  432 PHE DDD CD1 
14490 C CD2 . PHE D 432 ? 0.657 0.997 0.692 0.074  -0.015 0.145  432 PHE DDD CD2 
14491 C CE1 . PHE D 432 ? 0.593 0.915 0.638 0.073  -0.009 0.126  432 PHE DDD CE1 
14492 C CE2 . PHE D 432 ? 0.662 1.006 0.698 0.072  -0.010 0.146  432 PHE DDD CE2 
14493 C CZ  . PHE D 432 ? 0.639 0.973 0.680 0.072  -0.007 0.137  432 PHE DDD CZ  
14494 N N   . ALA D 433 ? 0.536 0.861 0.553 0.082  -0.017 0.101  433 ALA DDD N   
14495 C CA  . ALA D 433 ? 0.485 0.801 0.502 0.082  -0.015 0.089  433 ALA DDD CA  
14496 C C   . ALA D 433 ? 0.473 0.790 0.480 0.085  -0.016 0.078  433 ALA DDD C   
14497 O O   . ALA D 433 ? 0.459 0.788 0.455 0.087  -0.018 0.078  433 ALA DDD O   
14498 C CB  . ALA D 433 ? 0.480 0.801 0.493 0.081  -0.010 0.089  433 ALA DDD CB  
14499 N N   . LEU D 434 ? 0.445 0.750 0.455 0.085  -0.016 0.068  434 LEU DDD N   
14500 C CA  . LEU D 434 ? 0.414 0.719 0.415 0.087  -0.016 0.055  434 LEU DDD CA  
14501 C C   . LEU D 434 ? 0.403 0.716 0.396 0.088  -0.013 0.052  434 LEU DDD C   
14502 O O   . LEU D 434 ? 0.416 0.730 0.412 0.086  -0.010 0.057  434 LEU DDD O   
14503 C CB  . LEU D 434 ? 0.393 0.683 0.401 0.086  -0.016 0.047  434 LEU DDD CB  
14504 C CG  . LEU D 434 ? 0.393 0.676 0.409 0.086  -0.020 0.048  434 LEU DDD CG  
14505 C CD1 . LEU D 434 ? 0.400 0.669 0.419 0.085  -0.019 0.038  434 LEU DDD CD1 
14506 C CD2 . LEU D 434 ? 0.410 0.700 0.420 0.088  -0.023 0.048  434 LEU DDD CD2 
14507 N N   . PRO D 435 ? 0.398 0.717 0.381 0.091  -0.013 0.044  435 PRO DDD N   
14508 C CA  . PRO D 435 ? 0.398 0.724 0.376 0.091  -0.010 0.039  435 PRO DDD CA  
14509 C C   . PRO D 435 ? 0.415 0.729 0.400 0.090  -0.008 0.035  435 PRO DDD C   
14510 O O   . PRO D 435 ? 0.401 0.702 0.392 0.089  -0.009 0.032  435 PRO DDD O   
14511 C CB  . PRO D 435 ? 0.389 0.718 0.359 0.094  -0.012 0.028  435 PRO DDD CB  
14512 C CG  . PRO D 435 ? 0.393 0.726 0.361 0.096  -0.016 0.031  435 PRO DDD CG  
14513 C CD  . PRO D 435 ? 0.412 0.733 0.391 0.093  -0.017 0.038  435 PRO DDD CD  
14514 N N   . LEU D 436 ? 0.415 0.734 0.399 0.089  -0.005 0.035  436 LEU DDD N   
14515 C CA  . LEU D 436 ? 0.400 0.710 0.388 0.088  -0.003 0.030  436 LEU DDD CA  
14516 C C   . LEU D 436 ? 0.385 0.685 0.371 0.090  -0.005 0.019  436 LEU DDD C   
14517 O O   . LEU D 436 ? 0.379 0.685 0.359 0.092  -0.007 0.013  436 LEU DDD O   
14518 C CB  . LEU D 436 ? 0.407 0.727 0.392 0.089  0.000  0.028  436 LEU DDD CB  
14519 C CG  . LEU D 436 ? 0.406 0.736 0.393 0.087  0.003  0.039  436 LEU DDD CG  
14520 C CD1 . LEU D 436 ? 0.404 0.746 0.387 0.088  0.006  0.036  436 LEU DDD CD1 
14521 C CD2 . LEU D 436 ? 0.405 0.726 0.403 0.084  0.004  0.046  436 LEU DDD CD2 
14522 N N   . ASN D 437 ? 0.351 0.637 0.343 0.088  -0.006 0.016  437 ASN DDD N   
14523 C CA  . ASN D 437 ? 0.326 0.602 0.316 0.088  -0.008 0.008  437 ASN DDD CA  
14524 C C   . ASN D 437 ? 0.299 0.575 0.286 0.090  -0.008 -0.001 437 ASN DDD C   
14525 O O   . ASN D 437 ? 0.286 0.556 0.270 0.091  -0.010 -0.008 437 ASN DDD O   
14526 C CB  . ASN D 437 ? 0.333 0.595 0.331 0.086  -0.008 0.009  437 ASN DDD CB  
14527 C CG  . ASN D 437 ? 0.336 0.591 0.338 0.084  -0.007 0.009  437 ASN DDD CG  
14528 O OD1 . ASN D 437 ? 0.308 0.569 0.311 0.083  -0.005 0.013  437 ASN DDD OD1 
14529 N ND2 . ASN D 437 ? 0.356 0.599 0.361 0.082  -0.007 0.005  437 ASN DDD ND2 
14530 N N   . CYS D 438 ? 0.302 0.583 0.289 0.090  -0.006 -0.001 438 CYS DDD N   
14531 C CA  . CYS D 438 ? 0.312 0.590 0.298 0.091  -0.006 -0.009 438 CYS DDD CA  
14532 C C   . CYS D 438 ? 0.325 0.617 0.307 0.094  -0.005 -0.012 438 CYS DDD C   
14533 O O   . CYS D 438 ? 0.321 0.624 0.302 0.093  -0.003 -0.006 438 CYS DDD O   
14534 C CB  . CYS D 438 ? 0.322 0.592 0.313 0.089  -0.005 -0.008 438 CYS DDD CB  
14535 S SG  . CYS D 438 ? 0.325 0.578 0.321 0.086  -0.006 -0.007 438 CYS DDD SG  
14536 N N   . LEU D 439 ? 0.333 0.625 0.314 0.096  -0.007 -0.021 439 LEU DDD N   
14537 C CA  . LEU D 439 ? 0.328 0.632 0.306 0.098  -0.006 -0.026 439 LEU DDD CA  
14538 C C   . LEU D 439 ? 0.320 0.616 0.301 0.099  -0.008 -0.035 439 LEU DDD C   
14539 O O   . LEU D 439 ? 0.308 0.596 0.288 0.099  -0.011 -0.040 439 LEU DDD O   
14540 C CB  . LEU D 439 ? 0.341 0.655 0.313 0.101  -0.007 -0.030 439 LEU DDD CB  
14541 C CG  . LEU D 439 ? 0.339 0.667 0.310 0.103  -0.006 -0.037 439 LEU DDD CG  
14542 C CD1 . LEU D 439 ? 0.340 0.680 0.310 0.102  -0.002 -0.031 439 LEU DDD CD1 
14543 C CD2 . LEU D 439 ? 0.360 0.696 0.325 0.106  -0.008 -0.043 439 LEU DDD CD2 
14544 N N   . ALA D 440 ? 0.320 0.620 0.305 0.099  -0.006 -0.035 440 ALA DDD N   
14545 C CA  . ALA D 440 ? 0.334 0.627 0.322 0.100  -0.008 -0.043 440 ALA DDD CA  
14546 C C   . ALA D 440 ? 0.357 0.664 0.345 0.102  -0.007 -0.050 440 ALA DDD C   
14547 O O   . ALA D 440 ? 0.345 0.665 0.333 0.103  -0.004 -0.046 440 ALA DDD O   
14548 C CB  . ALA D 440 ? 0.319 0.605 0.313 0.097  -0.007 -0.039 440 ALA DDD CB  
14549 N N   . LYS D 441 ? 0.373 0.678 0.363 0.105  -0.011 -0.059 441 LYS DDD N   
14550 C CA  . LYS D 441 ? 0.394 0.711 0.386 0.108  -0.010 -0.067 441 LYS DDD CA  
14551 C C   . LYS D 441 ? 0.394 0.703 0.392 0.109  -0.014 -0.076 441 LYS DDD C   
14552 O O   . LYS D 441 ? 0.405 0.703 0.403 0.109  -0.018 -0.078 441 LYS DDD O   
14553 C CB  . LYS D 441 ? 0.414 0.742 0.400 0.110  -0.010 -0.071 441 LYS DDD CB  
14554 C CG  . LYS D 441 ? 0.414 0.756 0.403 0.113  -0.010 -0.081 441 LYS DDD CG  
14555 C CD  . LYS D 441 ? 0.442 0.799 0.424 0.115  -0.009 -0.082 441 LYS DDD CD  
14556 C CE  . LYS D 441 ? 0.454 0.806 0.433 0.116  -0.012 -0.085 441 LYS DDD CE  
14557 N NZ  . LYS D 441 ? 0.451 0.819 0.424 0.118  -0.011 -0.087 441 LYS DDD NZ  
14558 N N   . LEU D 442 ? 0.404 0.719 0.408 0.110  -0.013 -0.080 442 LEU DDD N   
14559 C CA  . LEU D 442 ? 0.416 0.729 0.428 0.112  -0.017 -0.089 442 LEU DDD CA  
14560 C C   . LEU D 442 ? 0.441 0.770 0.455 0.115  -0.016 -0.098 442 LEU DDD C   
14561 O O   . LEU D 442 ? 0.462 0.807 0.475 0.116  -0.012 -0.097 442 LEU DDD O   
14562 C CB  . LEU D 442 ? 0.416 0.724 0.435 0.111  -0.017 -0.087 442 LEU DDD CB  
14563 C CG  . LEU D 442 ? 0.418 0.709 0.435 0.108  -0.019 -0.080 442 LEU DDD CG  
14564 C CD1 . LEU D 442 ? 0.411 0.700 0.435 0.107  -0.018 -0.078 442 LEU DDD CD1 
14565 C CD2 . LEU D 442 ? 0.404 0.679 0.420 0.107  -0.024 -0.082 442 LEU DDD CD2 
14566 N N   . VAL D 443 ? 0.460 0.786 0.477 0.118  -0.020 -0.107 443 VAL DDD N   
14567 C CA  . VAL D 443 ? 0.453 0.794 0.475 0.121  -0.020 -0.118 443 VAL DDD CA  
14568 C C   . VAL D 443 ? 0.454 0.790 0.488 0.122  -0.024 -0.125 443 VAL DDD C   
14569 O O   . VAL D 443 ? 0.433 0.753 0.470 0.122  -0.029 -0.126 443 VAL DDD O   
14570 C CB  . VAL D 443 ? 0.438 0.781 0.457 0.123  -0.022 -0.123 443 VAL DDD CB  
14571 C CG1 . VAL D 443 ? 0.441 0.801 0.465 0.126  -0.022 -0.135 443 VAL DDD CG1 
14572 C CG2 . VAL D 443 ? 0.422 0.766 0.430 0.121  -0.020 -0.115 443 VAL DDD CG2 
14573 N N   . VAL D 444 ? 0.453 0.802 0.493 0.124  -0.021 -0.130 444 VAL DDD N   
14574 C CA  . VAL D 444 ? 0.444 0.790 0.498 0.125  -0.024 -0.136 444 VAL DDD CA  
14575 C C   . VAL D 444 ? 0.450 0.811 0.511 0.128  -0.024 -0.149 444 VAL DDD C   
14576 O O   . VAL D 444 ? 0.428 0.807 0.484 0.129  -0.019 -0.152 444 VAL DDD O   
14577 C CB  . VAL D 444 ? 0.463 0.807 0.518 0.123  -0.021 -0.130 444 VAL DDD CB  
14578 C CG1 . VAL D 444 ? 0.473 0.803 0.519 0.119  -0.021 -0.117 444 VAL DDD CG1 
14579 C CG2 . VAL D 444 ? 0.445 0.809 0.499 0.123  -0.015 -0.130 444 VAL DDD CG2 
14580 N N   . VAL D 445 ? 0.479 0.835 0.553 0.130  -0.029 -0.158 445 VAL DDD N   
14581 C CA  . VAL D 445 ? 0.496 0.866 0.582 0.134  -0.029 -0.171 445 VAL DDD CA  
14582 C C   . VAL D 445 ? 0.516 0.892 0.611 0.134  -0.027 -0.173 445 VAL DDD C   
14583 O O   . VAL D 445 ? 0.522 0.885 0.624 0.133  -0.031 -0.170 445 VAL DDD O   
14584 C CB  . VAL D 445 ? 0.499 0.860 0.596 0.136  -0.036 -0.180 445 VAL DDD CB  
14585 C CG1 . VAL D 445 ? 0.518 0.894 0.628 0.140  -0.037 -0.195 445 VAL DDD CG1 
14586 C CG2 . VAL D 445 ? 0.496 0.851 0.583 0.136  -0.038 -0.178 445 VAL DDD CG2 
14587 N N   . LYS D 446 ? 0.550 0.946 0.645 0.135  -0.021 -0.177 446 LYS DDD N   
14588 C CA  . LYS D 446 ? 0.612 1.018 0.716 0.134  -0.017 -0.179 446 LYS DDD CA  
14589 C C   . LYS D 446 ? 0.631 1.033 0.753 0.137  -0.023 -0.190 446 LYS DDD C   
14590 O O   . LYS D 446 ? 0.640 1.035 0.770 0.136  -0.024 -0.187 446 LYS DDD O   
14591 C CB  . LYS D 446 ? 0.587 1.016 0.686 0.135  -0.010 -0.182 446 LYS DDD CB  
14592 C CG  . LYS D 446 ? 0.591 1.024 0.672 0.132  -0.005 -0.171 446 LYS DDD CG  
14593 C CD  . LYS D 446 ? 0.578 1.025 0.656 0.130  0.003  -0.165 446 LYS DDD CD  
14594 C CE  . LYS D 446 ? 0.572 1.043 0.649 0.131  0.009  -0.174 446 LYS DDD CE  
14595 N NZ  . LYS D 446 ? 0.559 1.042 0.629 0.128  0.017  -0.166 446 LYS DDD NZ  
14596 N N   . SER D 447 ? 0.647 1.053 0.777 0.140  -0.027 -0.201 447 SER DDD N   
14597 C CA  . SER D 447 ? 0.670 1.074 0.819 0.143  -0.032 -0.213 447 SER DDD CA  
14598 C C   . SER D 447 ? 0.682 1.063 0.837 0.142  -0.040 -0.208 447 SER DDD C   
14599 O O   . SER D 447 ? 0.659 1.035 0.830 0.144  -0.046 -0.216 447 SER DDD O   
14600 C CB  . SER D 447 ? 0.689 1.104 0.845 0.146  -0.034 -0.227 447 SER DDD CB  
14601 O OG  . SER D 447 ? 0.741 1.145 0.889 0.146  -0.037 -0.224 447 SER DDD OG  
14602 N N   . GLN D 448 ? 0.710 1.075 0.852 0.139  -0.041 -0.195 448 GLN DDD N   
14603 C CA  . GLN D 448 ? 0.718 1.060 0.862 0.138  -0.049 -0.189 448 GLN DDD CA  
14604 C C   . GLN D 448 ? 0.696 1.031 0.833 0.134  -0.046 -0.176 448 GLN DDD C   
14605 O O   . GLN D 448 ? 0.718 1.035 0.847 0.132  -0.050 -0.167 448 GLN DDD O   
14606 C CB  . GLN D 448 ? 0.711 1.041 0.848 0.137  -0.053 -0.186 448 GLN DDD CB  
14607 C CG  . GLN D 448 ? 0.739 1.077 0.886 0.141  -0.055 -0.199 448 GLN DDD CG  
14608 C CD  . GLN D 448 ? 0.762 1.089 0.903 0.140  -0.059 -0.197 448 GLN DDD CD  
14609 O OE1 . GLN D 448 ? 0.810 1.126 0.938 0.137  -0.058 -0.186 448 GLN DDD OE1 
14610 N NE2 . GLN D 448 ? 0.729 1.060 0.880 0.143  -0.062 -0.208 448 GLN DDD NE2 
14611 N N   . GLY D 449 ? 0.684 1.031 0.822 0.134  -0.041 -0.176 449 GLY DDD N   
14612 C CA  . GLY D 449 ? 0.652 0.994 0.785 0.131  -0.038 -0.165 449 GLY DDD CA  
14613 C C   . GLY D 449 ? 0.631 0.968 0.747 0.128  -0.035 -0.154 449 GLY DDD C   
14614 O O   . GLY D 449 ? 0.608 0.930 0.719 0.125  -0.037 -0.145 449 GLY DDD O   
14615 N N   . GLU D 450 ? 0.594 0.941 0.700 0.128  -0.030 -0.155 450 GLU DDD N   
14616 C CA  . GLU D 450 ? 0.580 0.925 0.671 0.126  -0.027 -0.145 450 GLU DDD CA  
14617 C C   . GLU D 450 ? 0.548 0.872 0.635 0.124  -0.033 -0.140 450 GLU DDD C   
14618 O O   . GLU D 450 ? 0.555 0.869 0.633 0.121  -0.032 -0.130 450 GLU DDD O   
14619 C CB  . GLU D 450 ? 0.576 0.924 0.661 0.123  -0.022 -0.136 450 GLU DDD CB  
14620 C CG  . GLU D 450 ? 0.586 0.956 0.672 0.124  -0.015 -0.139 450 GLU DDD CG  
14621 C CD  . GLU D 450 ? 0.581 0.956 0.658 0.121  -0.008 -0.128 450 GLU DDD CD  
14622 O OE1 . GLU D 450 ? 0.564 0.929 0.643 0.118  -0.008 -0.121 450 GLU DDD OE1 
14623 O OE2 . GLU D 450 ? 0.574 0.963 0.643 0.121  -0.003 -0.127 450 GLU DDD OE2 
14624 N N   . LYS D 451 ? 0.529 0.846 0.622 0.127  -0.039 -0.148 451 LYS DDD N   
14625 C CA  . LYS D 451 ? 0.557 0.855 0.645 0.125  -0.045 -0.143 451 LYS DDD CA  
14626 C C   . LYS D 451 ? 0.519 0.818 0.593 0.124  -0.041 -0.137 451 LYS DDD C   
14627 O O   . LYS D 451 ? 0.470 0.784 0.542 0.125  -0.037 -0.142 451 LYS DDD O   
14628 C CB  . LYS D 451 ? 0.607 0.900 0.705 0.128  -0.051 -0.152 451 LYS DDD CB  
14629 C CG  . LYS D 451 ? 0.621 0.895 0.717 0.126  -0.057 -0.147 451 LYS DDD CG  
14630 C CD  . LYS D 451 ? 0.658 0.927 0.764 0.128  -0.063 -0.156 451 LYS DDD CD  
14631 C CE  . LYS D 451 ? 0.695 0.945 0.806 0.127  -0.071 -0.153 451 LYS DDD CE  
14632 N NZ  . LYS D 451 ? 0.694 0.943 0.820 0.130  -0.077 -0.162 451 LYS DDD NZ  
14633 N N   . VAL D 452 ? 0.477 0.761 0.543 0.120  -0.042 -0.128 452 VAL DDD N   
14634 C CA  . VAL D 452 ? 0.485 0.770 0.539 0.119  -0.039 -0.123 452 VAL DDD CA  
14635 C C   . VAL D 452 ? 0.471 0.750 0.525 0.120  -0.043 -0.129 452 VAL DDD C   
14636 O O   . VAL D 452 ? 0.505 0.770 0.564 0.120  -0.049 -0.129 452 VAL DDD O   
14637 C CB  . VAL D 452 ? 0.495 0.766 0.540 0.115  -0.038 -0.112 452 VAL DDD CB  
14638 C CG1 . VAL D 452 ? 0.504 0.775 0.539 0.114  -0.036 -0.107 452 VAL DDD CG1 
14639 C CG2 . VAL D 452 ? 0.484 0.761 0.531 0.114  -0.035 -0.107 452 VAL DDD CG2 
14640 N N   . VAL D 453 ? 0.469 0.761 0.521 0.122  -0.041 -0.133 453 VAL DDD N   
14641 C CA  . VAL D 453 ? 0.470 0.759 0.524 0.124  -0.044 -0.139 453 VAL DDD CA  
14642 C C   . VAL D 453 ? 0.450 0.737 0.492 0.122  -0.042 -0.133 453 VAL DDD C   
14643 O O   . VAL D 453 ? 0.492 0.773 0.534 0.123  -0.045 -0.136 453 VAL DDD O   
14644 C CB  . VAL D 453 ? 0.464 0.769 0.526 0.128  -0.044 -0.151 453 VAL DDD CB  
14645 C CG1 . VAL D 453 ? 0.440 0.745 0.515 0.130  -0.048 -0.158 453 VAL DDD CG1 
14646 C CG2 . VAL D 453 ? 0.477 0.801 0.532 0.129  -0.038 -0.152 453 VAL DDD CG2 
14647 N N   . GLY D 454 ? 0.413 0.705 0.447 0.120  -0.037 -0.125 454 GLY DDD N   
14648 C CA  . GLY D 454 ? 0.436 0.727 0.459 0.119  -0.035 -0.119 454 GLY DDD CA  
14649 C C   . GLY D 454 ? 0.435 0.720 0.452 0.115  -0.032 -0.108 454 GLY DDD C   
14650 O O   . GLY D 454 ? 0.501 0.795 0.518 0.115  -0.028 -0.105 454 GLY DDD O   
14651 N N   . PHE D 455 ? 0.400 0.671 0.412 0.113  -0.033 -0.102 455 PHE DDD N   
14652 C CA  . PHE D 455 ? 0.359 0.624 0.365 0.109  -0.030 -0.091 455 PHE DDD CA  
14653 C C   . PHE D 455 ? 0.353 0.618 0.353 0.108  -0.028 -0.087 455 PHE DDD C   
14654 O O   . PHE D 455 ? 0.359 0.617 0.358 0.108  -0.031 -0.091 455 PHE DDD O   
14655 C CB  . PHE D 455 ? 0.344 0.592 0.353 0.107  -0.033 -0.089 455 PHE DDD CB  
14656 C CG  . PHE D 455 ? 0.338 0.578 0.341 0.103  -0.031 -0.079 455 PHE DDD CG  
14657 C CD1 . PHE D 455 ? 0.332 0.566 0.330 0.101  -0.030 -0.076 455 PHE DDD CD1 
14658 C CD2 . PHE D 455 ? 0.326 0.565 0.330 0.102  -0.029 -0.075 455 PHE DDD CD2 
14659 C CE1 . PHE D 455 ? 0.323 0.551 0.318 0.098  -0.028 -0.068 455 PHE DDD CE1 
14660 C CE2 . PHE D 455 ? 0.338 0.570 0.339 0.098  -0.027 -0.067 455 PHE DDD CE2 
14661 C CZ  . PHE D 455 ? 0.346 0.573 0.342 0.096  -0.027 -0.064 455 PHE DDD CZ  
14662 N N   . HIS D 456 ? 0.326 0.597 0.321 0.107  -0.024 -0.080 456 HIS DDD N   
14663 C CA  . HIS D 456 ? 0.323 0.597 0.312 0.107  -0.023 -0.076 456 HIS DDD CA  
14664 C C   . HIS D 456 ? 0.313 0.584 0.300 0.104  -0.020 -0.066 456 HIS DDD C   
14665 O O   . HIS D 456 ? 0.317 0.594 0.305 0.103  -0.017 -0.063 456 HIS DDD O   
14666 C CB  . HIS D 456 ? 0.348 0.640 0.335 0.110  -0.021 -0.080 456 HIS DDD CB  
14667 C CG  . HIS D 456 ? 0.364 0.661 0.354 0.113  -0.024 -0.090 456 HIS DDD CG  
14668 N ND1 . HIS D 456 ? 0.371 0.667 0.361 0.114  -0.026 -0.095 456 HIS DDD ND1 
14669 C CD2 . HIS D 456 ? 0.379 0.682 0.375 0.115  -0.025 -0.098 456 HIS DDD CD2 
14670 C CE1 . HIS D 456 ? 0.358 0.658 0.352 0.117  -0.029 -0.105 456 HIS DDD CE1 
14671 N NE2 . HIS D 456 ? 0.376 0.681 0.375 0.117  -0.028 -0.107 456 HIS DDD NE2 
14672 N N   . PHE D 457 ? 0.302 0.564 0.287 0.102  -0.020 -0.063 457 PHE DDD N   
14673 C CA  . PHE D 457 ? 0.311 0.568 0.294 0.099  -0.018 -0.054 457 PHE DDD CA  
14674 C C   . PHE D 457 ? 0.311 0.567 0.291 0.098  -0.018 -0.051 457 PHE DDD C   
14675 O O   . PHE D 457 ? 0.333 0.581 0.314 0.097  -0.020 -0.054 457 PHE DDD O   
14676 C CB  . PHE D 457 ? 0.300 0.544 0.286 0.096  -0.019 -0.051 457 PHE DDD CB  
14677 C CG  . PHE D 457 ? 0.292 0.533 0.278 0.093  -0.016 -0.043 457 PHE DDD CG  
14678 C CD1 . PHE D 457 ? 0.285 0.534 0.274 0.093  -0.014 -0.038 457 PHE DDD CD1 
14679 C CD2 . PHE D 457 ? 0.286 0.518 0.271 0.090  -0.016 -0.040 457 PHE DDD CD2 
14680 C CE1 . PHE D 457 ? 0.286 0.532 0.276 0.090  -0.012 -0.031 457 PHE DDD CE1 
14681 C CE2 . PHE D 457 ? 0.292 0.522 0.279 0.088  -0.014 -0.033 457 PHE DDD CE2 
14682 C CZ  . PHE D 457 ? 0.276 0.513 0.265 0.088  -0.012 -0.028 457 PHE DDD CZ  
14683 N N   . VAL D 458 ? 0.303 0.569 0.282 0.098  -0.016 -0.045 458 VAL DDD N   
14684 C CA  . VAL D 458 ? 0.296 0.562 0.273 0.097  -0.015 -0.040 458 VAL DDD CA  
14685 C C   . VAL D 458 ? 0.280 0.539 0.260 0.094  -0.014 -0.032 458 VAL DDD C   
14686 O O   . VAL D 458 ? 0.246 0.511 0.228 0.094  -0.011 -0.028 458 VAL DDD O   
14687 C CB  . VAL D 458 ? 0.306 0.588 0.280 0.100  -0.015 -0.039 458 VAL DDD CB  
14688 C CG1 . VAL D 458 ? 0.313 0.594 0.286 0.099  -0.015 -0.034 458 VAL DDD CG1 
14689 C CG2 . VAL D 458 ? 0.316 0.604 0.287 0.103  -0.017 -0.048 458 VAL DDD CG2 
14690 N N   . GLY D 459 ? 0.292 0.541 0.274 0.092  -0.014 -0.031 459 GLY DDD N   
14691 C CA  . GLY D 459 ? 0.312 0.554 0.298 0.089  -0.013 -0.024 459 GLY DDD CA  
14692 C C   . GLY D 459 ? 0.290 0.519 0.278 0.086  -0.013 -0.026 459 GLY DDD C   
14693 O O   . GLY D 459 ? 0.289 0.513 0.275 0.087  -0.015 -0.032 459 GLY DDD O   
14694 N N   . PRO D 460 ? 0.279 0.500 0.270 0.083  -0.012 -0.022 460 PRO DDD N   
14695 C CA  . PRO D 460 ? 0.272 0.480 0.264 0.080  -0.012 -0.024 460 PRO DDD CA  
14696 C C   . PRO D 460 ? 0.277 0.477 0.266 0.079  -0.013 -0.029 460 PRO DDD C   
14697 O O   . PRO D 460 ? 0.274 0.477 0.263 0.080  -0.014 -0.030 460 PRO DDD O   
14698 C CB  . PRO D 460 ? 0.277 0.482 0.275 0.077  -0.011 -0.018 460 PRO DDD CB  
14699 C CG  . PRO D 460 ? 0.292 0.508 0.293 0.079  -0.010 -0.012 460 PRO DDD CG  
14700 C CD  . PRO D 460 ? 0.289 0.515 0.285 0.082  -0.010 -0.014 460 PRO DDD CD  
14701 N N   . ASN D 461 ? 0.301 0.492 0.289 0.078  -0.014 -0.033 461 ASN DDD N   
14702 C CA  . ASN D 461 ? 0.308 0.489 0.293 0.076  -0.015 -0.037 461 ASN DDD CA  
14703 C C   . ASN D 461 ? 0.320 0.507 0.304 0.079  -0.018 -0.041 461 ASN DDD C   
14704 O O   . ASN D 461 ? 0.305 0.488 0.288 0.079  -0.019 -0.041 461 ASN DDD O   
14705 C CB  . ASN D 461 ? 0.301 0.476 0.288 0.073  -0.014 -0.034 461 ASN DDD CB  
14706 C CG  . ASN D 461 ? 0.313 0.486 0.304 0.071  -0.012 -0.031 461 ASN DDD CG  
14707 O OD1 . ASN D 461 ? 0.352 0.521 0.343 0.069  -0.012 -0.033 461 ASN DDD OD1 
14708 N ND2 . ASN D 461 ? 0.297 0.475 0.293 0.071  -0.011 -0.026 461 ASN DDD ND2 
14709 N N   . ALA D 462 ? 0.303 0.498 0.286 0.082  -0.018 -0.043 462 ALA DDD N   
14710 C CA  . ALA D 462 ? 0.323 0.524 0.305 0.086  -0.020 -0.047 462 ALA DDD CA  
14711 C C   . ALA D 462 ? 0.312 0.505 0.293 0.085  -0.023 -0.052 462 ALA DDD C   
14712 O O   . ALA D 462 ? 0.320 0.514 0.302 0.086  -0.024 -0.055 462 ALA DDD O   
14713 C CB  . ALA D 462 ? 0.326 0.540 0.308 0.089  -0.020 -0.049 462 ALA DDD CB  
14714 N N   . GLY D 463 ? 0.315 0.499 0.295 0.083  -0.023 -0.054 463 GLY DDD N   
14715 C CA  . GLY D 463 ? 0.332 0.506 0.311 0.082  -0.026 -0.058 463 GLY DDD CA  
14716 C C   . GLY D 463 ? 0.351 0.516 0.328 0.079  -0.026 -0.056 463 GLY DDD C   
14717 O O   . GLY D 463 ? 0.361 0.523 0.339 0.080  -0.029 -0.058 463 GLY DDD O   
14718 N N   . GLU D 464 ? 0.368 0.530 0.345 0.076  -0.024 -0.051 464 GLU DDD N   
14719 C CA  . GLU D 464 ? 0.372 0.527 0.348 0.073  -0.024 -0.049 464 GLU DDD CA  
14720 C C   . GLU D 464 ? 0.350 0.511 0.328 0.076  -0.026 -0.049 464 GLU DDD C   
14721 O O   . GLU D 464 ? 0.353 0.509 0.331 0.075  -0.028 -0.049 464 GLU DDD O   
14722 C CB  . GLU D 464 ? 0.369 0.521 0.345 0.070  -0.021 -0.045 464 GLU DDD CB  
14723 C CG  . GLU D 464 ? 0.363 0.511 0.338 0.068  -0.019 -0.046 464 GLU DDD CG  
14724 C CD  . GLU D 464 ? 0.400 0.537 0.371 0.065  -0.020 -0.048 464 GLU DDD CD  
14725 O OE1 . GLU D 464 ? 0.427 0.559 0.395 0.064  -0.023 -0.049 464 GLU DDD OE1 
14726 O OE2 . GLU D 464 ? 0.366 0.499 0.337 0.063  -0.019 -0.050 464 GLU DDD OE2 
14727 N N   . ILE D 465 ? 0.341 0.514 0.321 0.079  -0.024 -0.048 465 ILE DDD N   
14728 C CA  . ILE D 465 ? 0.315 0.495 0.299 0.081  -0.025 -0.048 465 ILE DDD CA  
14729 C C   . ILE D 465 ? 0.307 0.489 0.292 0.084  -0.028 -0.054 465 ILE DDD C   
14730 O O   . ILE D 465 ? 0.296 0.477 0.283 0.085  -0.030 -0.055 465 ILE DDD O   
14731 C CB  . ILE D 465 ? 0.317 0.510 0.303 0.083  -0.022 -0.045 465 ILE DDD CB  
14732 C CG1 . ILE D 465 ? 0.322 0.513 0.310 0.081  -0.019 -0.039 465 ILE DDD CG1 
14733 C CG2 . ILE D 465 ? 0.320 0.523 0.309 0.086  -0.022 -0.046 465 ILE DDD CG2 
14734 C CD1 . ILE D 465 ? 0.315 0.516 0.304 0.082  -0.016 -0.034 465 ILE DDD CD1 
14735 N N   . THR D 466 ? 0.289 0.472 0.273 0.086  -0.029 -0.057 466 THR DDD N   
14736 C CA  . THR D 466 ? 0.304 0.492 0.291 0.089  -0.032 -0.063 466 THR DDD CA  
14737 C C   . THR D 466 ? 0.324 0.500 0.311 0.088  -0.036 -0.066 466 THR DDD C   
14738 O O   . THR D 466 ? 0.356 0.535 0.348 0.090  -0.039 -0.070 466 THR DDD O   
14739 C CB  . THR D 466 ? 0.298 0.493 0.285 0.091  -0.031 -0.067 466 THR DDD CB  
14740 O OG1 . THR D 466 ? 0.294 0.501 0.280 0.093  -0.028 -0.065 466 THR DDD OG1 
14741 C CG2 . THR D 466 ? 0.288 0.486 0.279 0.094  -0.035 -0.074 466 THR DDD CG2 
14742 N N   . GLN D 467 ? 0.321 0.486 0.305 0.084  -0.036 -0.064 467 GLN DDD N   
14743 C CA  . GLN D 467 ? 0.328 0.480 0.311 0.082  -0.040 -0.065 467 GLN DDD CA  
14744 C C   . GLN D 467 ? 0.318 0.470 0.305 0.083  -0.043 -0.066 467 GLN DDD C   
14745 O O   . GLN D 467 ? 0.307 0.459 0.298 0.085  -0.047 -0.070 467 GLN DDD O   
14746 C CB  . GLN D 467 ? 0.329 0.470 0.306 0.077  -0.039 -0.061 467 GLN DDD CB  
14747 C CG  . GLN D 467 ? 0.337 0.466 0.313 0.075  -0.043 -0.062 467 GLN DDD CG  
14748 C CD  . GLN D 467 ? 0.334 0.464 0.313 0.077  -0.044 -0.067 467 GLN DDD CD  
14749 O OE1 . GLN D 467 ? 0.351 0.479 0.328 0.075  -0.041 -0.067 467 GLN DDD OE1 
14750 N NE2 . GLN D 467 ? 0.336 0.468 0.320 0.080  -0.047 -0.071 467 GLN DDD NE2 
14751 N N   . GLY D 468 ? 0.327 0.479 0.312 0.082  -0.042 -0.062 468 GLY DDD N   
14752 C CA  . GLY D 468 ? 0.342 0.492 0.330 0.082  -0.045 -0.062 468 GLY DDD CA  
14753 C C   . GLY D 468 ? 0.352 0.513 0.348 0.087  -0.046 -0.066 468 GLY DDD C   
14754 O O   . GLY D 468 ? 0.370 0.528 0.370 0.088  -0.051 -0.069 468 GLY DDD O   
14755 N N   . PHE D 469 ? 0.366 0.539 0.363 0.089  -0.042 -0.066 469 PHE DDD N   
14756 C CA  . PHE D 469 ? 0.350 0.535 0.353 0.093  -0.042 -0.071 469 PHE DDD CA  
14757 C C   . PHE D 469 ? 0.380 0.566 0.387 0.095  -0.045 -0.077 469 PHE DDD C   
14758 O O   . PHE D 469 ? 0.377 0.568 0.391 0.098  -0.048 -0.082 469 PHE DDD O   
14759 C CB  . PHE D 469 ? 0.324 0.522 0.325 0.094  -0.037 -0.069 469 PHE DDD CB  
14760 C CG  . PHE D 469 ? 0.300 0.501 0.302 0.092  -0.034 -0.063 469 PHE DDD CG  
14761 C CD1 . PHE D 469 ? 0.285 0.489 0.293 0.094  -0.035 -0.064 469 PHE DDD CD1 
14762 C CD2 . PHE D 469 ? 0.283 0.484 0.281 0.090  -0.030 -0.057 469 PHE DDD CD2 
14763 C CE1 . PHE D 469 ? 0.276 0.483 0.285 0.092  -0.032 -0.060 469 PHE DDD CE1 
14764 C CE2 . PHE D 469 ? 0.278 0.482 0.278 0.089  -0.028 -0.053 469 PHE DDD CE2 
14765 C CZ  . PHE D 469 ? 0.285 0.492 0.291 0.090  -0.029 -0.054 469 PHE DDD CZ  
14766 N N   . SER D 470 ? 0.392 0.574 0.396 0.094  -0.046 -0.078 470 SER DDD N   
14767 C CA  . SER D 470 ? 0.401 0.581 0.409 0.096  -0.049 -0.085 470 SER DDD CA  
14768 C C   . SER D 470 ? 0.400 0.572 0.413 0.096  -0.055 -0.086 470 SER DDD C   
14769 O O   . SER D 470 ? 0.414 0.591 0.436 0.099  -0.058 -0.093 470 SER DDD O   
14770 C CB  . SER D 470 ? 0.381 0.556 0.385 0.095  -0.048 -0.084 470 SER DDD CB  
14771 O OG  . SER D 470 ? 0.390 0.550 0.390 0.091  -0.050 -0.081 470 SER DDD OG  
14772 N N   . LEU D 471 ? 0.427 0.586 0.436 0.093  -0.056 -0.081 471 LEU DDD N   
14773 C CA  . LEU D 471 ? 0.428 0.577 0.441 0.092  -0.062 -0.082 471 LEU DDD CA  
14774 C C   . LEU D 471 ? 0.441 0.598 0.462 0.095  -0.064 -0.084 471 LEU DDD C   
14775 O O   . LEU D 471 ? 0.431 0.588 0.460 0.097  -0.069 -0.089 471 LEU DDD O   
14776 C CB  . LEU D 471 ? 0.431 0.568 0.437 0.087  -0.063 -0.075 471 LEU DDD CB  
14777 C CG  . LEU D 471 ? 0.426 0.553 0.435 0.086  -0.070 -0.074 471 LEU DDD CG  
14778 C CD1 . LEU D 471 ? 0.429 0.551 0.443 0.088  -0.074 -0.078 471 LEU DDD CD1 
14779 C CD2 . LEU D 471 ? 0.428 0.542 0.427 0.081  -0.070 -0.067 471 LEU DDD CD2 
14780 N N   . ALA D 472 ? 0.456 0.621 0.475 0.095  -0.060 -0.082 472 ALA DDD N   
14781 C CA  . ALA D 472 ? 0.451 0.624 0.477 0.097  -0.060 -0.084 472 ALA DDD CA  
14782 C C   . ALA D 472 ? 0.454 0.640 0.488 0.102  -0.060 -0.092 472 ALA DDD C   
14783 O O   . ALA D 472 ? 0.441 0.629 0.485 0.104  -0.063 -0.097 472 ALA DDD O   
14784 C CB  . ALA D 472 ? 0.444 0.623 0.467 0.096  -0.055 -0.079 472 ALA DDD CB  
14785 N N   . VAL D 473 ? 0.444 0.637 0.475 0.103  -0.056 -0.093 473 VAL DDD N   
14786 C CA  . VAL D 473 ? 0.472 0.679 0.510 0.107  -0.056 -0.102 473 VAL DDD CA  
14787 C C   . VAL D 473 ? 0.494 0.694 0.540 0.108  -0.062 -0.108 473 VAL DDD C   
14788 O O   . VAL D 473 ? 0.485 0.693 0.541 0.112  -0.064 -0.115 473 VAL DDD O   
14789 C CB  . VAL D 473 ? 0.485 0.702 0.517 0.108  -0.051 -0.102 473 VAL DDD CB  
14790 C CG1 . VAL D 473 ? 0.506 0.734 0.544 0.112  -0.051 -0.111 473 VAL DDD CG1 
14791 C CG2 . VAL D 473 ? 0.504 0.730 0.531 0.107  -0.045 -0.096 473 VAL DDD CG2 
14792 N N   . LYS D 474 ? 0.515 0.701 0.557 0.106  -0.065 -0.105 474 LYS DDD N   
14793 C CA  . LYS D 474 ? 0.535 0.714 0.585 0.107  -0.071 -0.109 474 LYS DDD CA  
14794 C C   . LYS D 474 ? 0.526 0.700 0.585 0.108  -0.076 -0.111 474 LYS DDD C   
14795 O O   . LYS D 474 ? 0.519 0.695 0.590 0.110  -0.081 -0.118 474 LYS DDD O   
14796 C CB  . LYS D 474 ? 0.532 0.697 0.576 0.103  -0.072 -0.104 474 LYS DDD CB  
14797 C CG  . LYS D 474 ? 0.552 0.707 0.603 0.103  -0.078 -0.108 474 LYS DDD CG  
14798 C CD  . LYS D 474 ? 0.535 0.675 0.579 0.099  -0.080 -0.101 474 LYS DDD CD  
14799 C CE  . LYS D 474 ? 0.525 0.658 0.576 0.099  -0.085 -0.105 474 LYS DDD CE  
14800 N NZ  . LYS D 474 ? 0.541 0.663 0.583 0.095  -0.083 -0.099 474 LYS DDD NZ  
14801 N N   . LEU D 475 ? 0.515 0.685 0.570 0.105  -0.076 -0.105 475 LEU DDD N   
14802 C CA  . LEU D 475 ? 0.526 0.691 0.589 0.106  -0.081 -0.105 475 LEU DDD CA  
14803 C C   . LEU D 475 ? 0.515 0.695 0.588 0.109  -0.080 -0.111 475 LEU DDD C   
14804 O O   . LEU D 475 ? 0.520 0.697 0.601 0.110  -0.085 -0.112 475 LEU DDD O   
14805 C CB  . LEU D 475 ? 0.540 0.695 0.594 0.102  -0.082 -0.096 475 LEU DDD CB  
14806 C CG  . LEU D 475 ? 0.552 0.691 0.597 0.097  -0.084 -0.090 475 LEU DDD CG  
14807 C CD1 . LEU D 475 ? 0.554 0.685 0.590 0.094  -0.084 -0.083 475 LEU DDD CD1 
14808 C CD2 . LEU D 475 ? 0.545 0.674 0.597 0.098  -0.092 -0.092 475 LEU DDD CD2 
14809 N N   . GLY D 476 ? 0.514 0.708 0.586 0.112  -0.074 -0.115 476 GLY DDD N   
14810 C CA  . GLY D 476 ? 0.523 0.734 0.606 0.115  -0.072 -0.123 476 GLY DDD CA  
14811 C C   . GLY D 476 ? 0.516 0.734 0.595 0.115  -0.067 -0.119 476 GLY DDD C   
14812 O O   . GLY D 476 ? 0.512 0.738 0.601 0.117  -0.067 -0.123 476 GLY DDD O   
14813 N N   . ALA D 477 ? 0.491 0.708 0.558 0.112  -0.062 -0.111 477 ALA DDD N   
14814 C CA  . ALA D 477 ? 0.450 0.674 0.514 0.111  -0.057 -0.106 477 ALA DDD CA  
14815 C C   . ALA D 477 ? 0.416 0.659 0.484 0.114  -0.052 -0.112 477 ALA DDD C   
14816 O O   . ALA D 477 ? 0.404 0.655 0.470 0.115  -0.050 -0.116 477 ALA DDD O   
14817 C CB  . ALA D 477 ? 0.447 0.665 0.498 0.107  -0.053 -0.098 477 ALA DDD CB  
14818 N N   . THR D 478 ? 0.387 0.637 0.460 0.114  -0.050 -0.112 478 THR DDD N   
14819 C CA  . THR D 478 ? 0.388 0.658 0.466 0.116  -0.044 -0.116 478 THR DDD CA  
14820 C C   . THR D 478 ? 0.404 0.680 0.474 0.114  -0.038 -0.108 478 THR DDD C   
14821 O O   . THR D 478 ? 0.443 0.708 0.507 0.111  -0.038 -0.100 478 THR DDD O   
14822 C CB  . THR D 478 ? 0.360 0.635 0.452 0.118  -0.046 -0.122 478 THR DDD CB  
14823 O OG1 . THR D 478 ? 0.327 0.594 0.418 0.115  -0.047 -0.115 478 THR DDD OG1 
14824 C CG2 . THR D 478 ? 0.348 0.617 0.450 0.120  -0.053 -0.130 478 THR DDD CG2 
14825 N N   . LYS D 479 ? 0.415 0.708 0.484 0.115  -0.032 -0.110 479 LYS DDD N   
14826 C CA  . LYS D 479 ? 0.417 0.717 0.480 0.113  -0.025 -0.102 479 LYS DDD CA  
14827 C C   . LYS D 479 ? 0.425 0.719 0.493 0.111  -0.026 -0.097 479 LYS DDD C   
14828 O O   . LYS D 479 ? 0.439 0.728 0.501 0.108  -0.023 -0.089 479 LYS DDD O   
14829 C CB  . LYS D 479 ? 0.408 0.728 0.470 0.114  -0.019 -0.105 479 LYS DDD CB  
14830 C CG  . LYS D 479 ? 0.419 0.746 0.475 0.112  -0.013 -0.096 479 LYS DDD CG  
14831 C CD  . LYS D 479 ? 0.443 0.760 0.489 0.109  -0.013 -0.087 479 LYS DDD CD  
14832 C CE  . LYS D 479 ? 0.471 0.798 0.511 0.108  -0.007 -0.079 479 LYS DDD CE  
14833 N NZ  . LYS D 479 ? 0.474 0.806 0.520 0.106  -0.003 -0.075 479 LYS DDD NZ  
14834 N N   . LYS D 480 ? 0.453 0.747 0.533 0.112  -0.029 -0.103 480 LYS DDD N   
14835 C CA  . LYS D 480 ? 0.450 0.738 0.536 0.111  -0.030 -0.100 480 LYS DDD CA  
14836 C C   . LYS D 480 ? 0.435 0.705 0.515 0.108  -0.034 -0.093 480 LYS DDD C   
14837 O O   . LYS D 480 ? 0.436 0.702 0.513 0.106  -0.032 -0.086 480 LYS DDD O   
14838 C CB  . LYS D 480 ? 0.458 0.749 0.558 0.113  -0.034 -0.109 480 LYS DDD CB  
14839 C CG  . LYS D 480 ? 0.476 0.758 0.584 0.112  -0.037 -0.106 480 LYS DDD CG  
14840 C CD  . LYS D 480 ? 0.492 0.785 0.615 0.114  -0.037 -0.114 480 LYS DDD CD  
14841 C CE  . LYS D 480 ? 0.480 0.763 0.612 0.114  -0.042 -0.113 480 LYS DDD CE  
14842 N NZ  . LYS D 480 ? 0.458 0.733 0.584 0.110  -0.041 -0.104 480 LYS DDD NZ  
14843 N N   . ASP D 481 ? 0.452 0.710 0.529 0.108  -0.040 -0.095 481 ASP DDD N   
14844 C CA  . ASP D 481 ? 0.448 0.688 0.517 0.106  -0.044 -0.089 481 ASP DDD CA  
14845 C C   . ASP D 481 ? 0.413 0.653 0.472 0.103  -0.039 -0.081 481 ASP DDD C   
14846 O O   . ASP D 481 ? 0.398 0.629 0.454 0.100  -0.040 -0.075 481 ASP DDD O   
14847 C CB  . ASP D 481 ? 0.468 0.699 0.535 0.106  -0.049 -0.092 481 ASP DDD CB  
14848 C CG  . ASP D 481 ? 0.471 0.699 0.549 0.109  -0.056 -0.099 481 ASP DDD CG  
14849 O OD1 . ASP D 481 ? 0.489 0.715 0.574 0.109  -0.058 -0.099 481 ASP DDD OD1 
14850 O OD2 . ASP D 481 ? 0.481 0.708 0.561 0.111  -0.059 -0.105 481 ASP DDD OD2 
14851 N N   . PHE D 482 ? 0.391 0.642 0.446 0.104  -0.034 -0.081 482 PHE DDD N   
14852 C CA  . PHE D 482 ? 0.376 0.627 0.422 0.101  -0.029 -0.074 482 PHE DDD CA  
14853 C C   . PHE D 482 ? 0.377 0.634 0.425 0.100  -0.025 -0.068 482 PHE DDD C   
14854 O O   . PHE D 482 ? 0.372 0.622 0.416 0.097  -0.024 -0.061 482 PHE DDD O   
14855 C CB  . PHE D 482 ? 0.350 0.612 0.391 0.103  -0.026 -0.076 482 PHE DDD CB  
14856 C CG  . PHE D 482 ? 0.347 0.600 0.382 0.103  -0.030 -0.077 482 PHE DDD CG  
14857 C CD1 . PHE D 482 ? 0.342 0.591 0.380 0.105  -0.034 -0.085 482 PHE DDD CD1 
14858 C CD2 . PHE D 482 ? 0.343 0.590 0.369 0.101  -0.028 -0.072 482 PHE DDD CD2 
14859 C CE1 . PHE D 482 ? 0.353 0.595 0.387 0.105  -0.037 -0.086 482 PHE DDD CE1 
14860 C CE2 . PHE D 482 ? 0.334 0.574 0.356 0.101  -0.030 -0.073 482 PHE DDD CE2 
14861 C CZ  . PHE D 482 ? 0.325 0.562 0.350 0.103  -0.035 -0.080 482 PHE DDD CZ  
14862 N N   . ASP D 483 ? 0.387 0.656 0.443 0.101  -0.023 -0.071 483 ASP DDD N   
14863 C CA  . ASP D 483 ? 0.397 0.673 0.458 0.100  -0.018 -0.066 483 ASP DDD CA  
14864 C C   . ASP D 483 ? 0.386 0.650 0.452 0.098  -0.022 -0.064 483 ASP DDD C   
14865 O O   . ASP D 483 ? 0.380 0.645 0.448 0.096  -0.019 -0.058 483 ASP DDD O   
14866 C CB  . ASP D 483 ? 0.427 0.719 0.496 0.102  -0.015 -0.071 483 ASP DDD CB  
14867 C CG  . ASP D 483 ? 0.442 0.749 0.506 0.103  -0.010 -0.072 483 ASP DDD CG  
14868 O OD1 . ASP D 483 ? 0.462 0.768 0.517 0.102  -0.009 -0.068 483 ASP DDD OD1 
14869 O OD2 . ASP D 483 ? 0.505 0.825 0.575 0.105  -0.008 -0.079 483 ASP DDD OD2 
14870 N N   . ASP D 484 ? 0.362 0.616 0.431 0.099  -0.028 -0.069 484 ASP DDD N   
14871 C CA  . ASP D 484 ? 0.363 0.606 0.437 0.098  -0.033 -0.067 484 ASP DDD CA  
14872 C C   . ASP D 484 ? 0.362 0.590 0.426 0.095  -0.036 -0.063 484 ASP DDD C   
14873 O O   . ASP D 484 ? 0.370 0.587 0.436 0.093  -0.040 -0.062 484 ASP DDD O   
14874 C CB  . ASP D 484 ? 0.375 0.616 0.458 0.100  -0.039 -0.075 484 ASP DDD CB  
14875 C CG  . ASP D 484 ? 0.371 0.626 0.464 0.103  -0.036 -0.081 484 ASP DDD CG  
14876 O OD1 . ASP D 484 ? 0.315 0.584 0.409 0.102  -0.029 -0.079 484 ASP DDD OD1 
14877 O OD2 . ASP D 484 ? 0.384 0.637 0.484 0.105  -0.041 -0.087 484 ASP DDD OD2 
14878 N N   . MET D 485 ? 0.353 0.579 0.408 0.094  -0.034 -0.061 485 MET DDD N   
14879 C CA  . MET D 485 ? 0.356 0.569 0.402 0.092  -0.036 -0.057 485 MET DDD CA  
14880 C C   . MET D 485 ? 0.341 0.554 0.386 0.089  -0.032 -0.050 485 MET DDD C   
14881 O O   . MET D 485 ? 0.347 0.570 0.393 0.089  -0.027 -0.047 485 MET DDD O   
14882 C CB  . MET D 485 ? 0.378 0.591 0.416 0.092  -0.035 -0.058 485 MET DDD CB  
14883 C CG  . MET D 485 ? 0.409 0.612 0.439 0.089  -0.035 -0.053 485 MET DDD CG  
14884 S SD  . MET D 485 ? 0.435 0.640 0.457 0.089  -0.033 -0.053 485 MET DDD SD  
14885 C CE  . MET D 485 ? 0.450 0.672 0.474 0.092  -0.027 -0.053 485 MET DDD CE  
14886 N N   . ILE D 486 ? 0.331 0.533 0.375 0.086  -0.035 -0.048 486 ILE DDD N   
14887 C CA  . ILE D 486 ? 0.339 0.539 0.383 0.084  -0.032 -0.042 486 ILE DDD CA  
14888 C C   . ILE D 486 ? 0.358 0.555 0.393 0.082  -0.030 -0.039 486 ILE DDD C   
14889 O O   . ILE D 486 ? 0.347 0.536 0.375 0.081  -0.032 -0.041 486 ILE DDD O   
14890 C CB  . ILE D 486 ? 0.339 0.529 0.385 0.082  -0.036 -0.042 486 ILE DDD CB  
14891 C CG1 . ILE D 486 ? 0.348 0.541 0.403 0.083  -0.039 -0.045 486 ILE DDD CG1 
14892 C CG2 . ILE D 486 ? 0.334 0.523 0.382 0.079  -0.033 -0.037 486 ILE DDD CG2 
14893 C CD1 . ILE D 486 ? 0.333 0.537 0.398 0.084  -0.035 -0.044 486 ILE DDD CD1 
14894 N N   . GLY D 487 ? 0.364 0.569 0.402 0.081  -0.024 -0.034 487 GLY DDD N   
14895 C CA  . GLY D 487 ? 0.341 0.544 0.372 0.080  -0.021 -0.031 487 GLY DDD CA  
14896 C C   . GLY D 487 ? 0.348 0.541 0.378 0.077  -0.022 -0.028 487 GLY DDD C   
14897 O O   . GLY D 487 ? 0.340 0.529 0.375 0.075  -0.024 -0.028 487 GLY DDD O   
14898 N N   . ILE D 488 ? 0.318 0.506 0.341 0.075  -0.022 -0.028 488 ILE DDD N   
14899 C CA  . ILE D 488 ? 0.333 0.513 0.355 0.072  -0.021 -0.025 488 ILE DDD CA  
14900 C C   . ILE D 488 ? 0.308 0.496 0.334 0.072  -0.017 -0.020 488 ILE DDD C   
14901 O O   . ILE D 488 ? 0.301 0.495 0.324 0.073  -0.015 -0.019 488 ILE DDD O   
14902 C CB  . ILE D 488 ? 0.333 0.504 0.346 0.070  -0.023 -0.028 488 ILE DDD CB  
14903 C CG1 . ILE D 488 ? 0.331 0.495 0.340 0.071  -0.028 -0.032 488 ILE DDD CG1 
14904 C CG2 . ILE D 488 ? 0.319 0.483 0.332 0.067  -0.022 -0.026 488 ILE DDD CG2 
14905 C CD1 . ILE D 488 ? 0.332 0.487 0.332 0.069  -0.030 -0.034 488 ILE DDD CD1 
14906 N N   . HIS D 489 ? 0.302 0.490 0.335 0.070  -0.015 -0.017 489 HIS DDD N   
14907 C CA  . HIS D 489 ? 0.301 0.496 0.340 0.069  -0.011 -0.011 489 HIS DDD CA  
14908 C C   . HIS D 489 ? 0.304 0.492 0.345 0.066  -0.011 -0.010 489 HIS DDD C   
14909 O O   . HIS D 489 ? 0.305 0.484 0.346 0.065  -0.013 -0.012 489 HIS DDD O   
14910 C CB  . HIS D 489 ? 0.328 0.530 0.376 0.070  -0.009 -0.008 489 HIS DDD CB  
14911 C CG  . HIS D 489 ? 0.362 0.571 0.416 0.069  -0.005 -0.001 489 HIS DDD CG  
14912 N ND1 . HIS D 489 ? 0.381 0.599 0.433 0.071  -0.003 0.002  489 HIS DDD ND1 
14913 C CD2 . HIS D 489 ? 0.379 0.590 0.444 0.068  -0.004 0.004  489 HIS DDD CD2 
14914 C CE1 . HIS D 489 ? 0.408 0.632 0.467 0.070  -0.000 0.009  489 HIS DDD CE1 
14915 N NE2 . HIS D 489 ? 0.388 0.608 0.455 0.068  -0.000 0.010  489 HIS DDD NE2 
14916 N N   . PRO D 490 ? 0.302 0.492 0.344 0.066  -0.008 -0.006 490 PRO DDD N   
14917 C CA  . PRO D 490 ? 0.328 0.526 0.367 0.068  -0.006 -0.003 490 PRO DDD CA  
14918 C C   . PRO D 490 ? 0.332 0.527 0.361 0.069  -0.008 -0.007 490 PRO DDD C   
14919 O O   . PRO D 490 ? 0.351 0.538 0.378 0.067  -0.008 -0.009 490 PRO DDD O   
14920 C CB  . PRO D 490 ? 0.313 0.514 0.359 0.067  -0.004 0.003  490 PRO DDD CB  
14921 C CG  . PRO D 490 ? 0.312 0.505 0.365 0.064  -0.004 0.002  490 PRO DDD CG  
14922 C CD  . PRO D 490 ? 0.300 0.484 0.346 0.063  -0.007 -0.005 490 PRO DDD CD  
14923 N N   . THR D 491 ? 0.302 0.503 0.326 0.072  -0.008 -0.010 491 THR DDD N   
14924 C CA  . THR D 491 ? 0.301 0.500 0.317 0.073  -0.010 -0.013 491 THR DDD CA  
14925 C C   . THR D 491 ? 0.294 0.505 0.309 0.076  -0.008 -0.011 491 THR DDD C   
14926 O O   . THR D 491 ? 0.285 0.505 0.305 0.077  -0.006 -0.008 491 THR DDD O   
14927 C CB  . THR D 491 ? 0.308 0.500 0.318 0.073  -0.013 -0.019 491 THR DDD CB  
14928 O OG1 . THR D 491 ? 0.302 0.500 0.314 0.076  -0.014 -0.021 491 THR DDD OG1 
14929 C CG2 . THR D 491 ? 0.318 0.499 0.329 0.070  -0.015 -0.021 491 THR DDD CG2 
14930 N N   . ASP D 492 ? 0.306 0.518 0.316 0.077  -0.009 -0.014 492 ASP DDD N   
14931 C CA  . ASP D 492 ? 0.318 0.541 0.324 0.080  -0.008 -0.014 492 ASP DDD CA  
14932 C C   . ASP D 492 ? 0.325 0.550 0.330 0.082  -0.010 -0.021 492 ASP DDD C   
14933 O O   . ASP D 492 ? 0.350 0.585 0.354 0.084  -0.009 -0.021 492 ASP DDD O   
14934 C CB  . ASP D 492 ? 0.314 0.537 0.316 0.081  -0.008 -0.015 492 ASP DDD CB  
14935 C CG  . ASP D 492 ? 0.346 0.570 0.352 0.079  -0.007 -0.008 492 ASP DDD CG  
14936 O OD1 . ASP D 492 ? 0.370 0.599 0.382 0.078  -0.005 -0.003 492 ASP DDD OD1 
14937 O OD2 . ASP D 492 ? 0.399 0.619 0.404 0.079  -0.007 -0.009 492 ASP DDD OD2 
14938 N N   . ALA D 493 ? 0.313 0.526 0.315 0.081  -0.013 -0.025 493 ALA DDD N   
14939 C CA  . ALA D 493 ? 0.323 0.536 0.324 0.083  -0.016 -0.031 493 ALA DDD CA  
14940 C C   . ALA D 493 ? 0.338 0.556 0.344 0.084  -0.016 -0.032 493 ALA DDD C   
14941 O O   . ALA D 493 ? 0.346 0.567 0.353 0.086  -0.017 -0.037 493 ALA DDD O   
14942 C CB  . ALA D 493 ? 0.318 0.518 0.316 0.082  -0.019 -0.035 493 ALA DDD CB  
14943 N N   . GLU D 494 ? 0.342 0.560 0.353 0.082  -0.014 -0.027 494 GLU DDD N   
14944 C CA  . GLU D 494 ? 0.353 0.576 0.371 0.083  -0.013 -0.027 494 GLU DDD CA  
14945 C C   . GLU D 494 ? 0.333 0.571 0.352 0.085  -0.010 -0.026 494 GLU DDD C   
14946 O O   . GLU D 494 ? 0.313 0.557 0.336 0.087  -0.010 -0.029 494 GLU DDD O   
14947 C CB  . GLU D 494 ? 0.356 0.576 0.379 0.080  -0.012 -0.021 494 GLU DDD CB  
14948 C CG  . GLU D 494 ? 0.386 0.613 0.412 0.079  -0.008 -0.015 494 GLU DDD CG  
14949 C CD  . GLU D 494 ? 0.387 0.611 0.421 0.077  -0.007 -0.010 494 GLU DDD CD  
14950 O OE1 . GLU D 494 ? 0.406 0.630 0.445 0.077  -0.007 -0.011 494 GLU DDD OE1 
14951 O OE2 . GLU D 494 ? 0.440 0.661 0.475 0.075  -0.005 -0.005 494 GLU DDD OE2 
14952 N N   . VAL D 495 ? 0.333 0.578 0.348 0.086  -0.008 -0.024 495 VAL DDD N   
14953 C CA  . VAL D 495 ? 0.333 0.594 0.348 0.088  -0.005 -0.024 495 VAL DDD CA  
14954 C C   . VAL D 495 ? 0.335 0.600 0.350 0.091  -0.007 -0.032 495 VAL DDD C   
14955 O O   . VAL D 495 ? 0.326 0.602 0.345 0.092  -0.005 -0.033 495 VAL DDD O   
14956 C CB  . VAL D 495 ? 0.344 0.610 0.353 0.089  -0.004 -0.021 495 VAL DDD CB  
14957 C CG1 . VAL D 495 ? 0.355 0.619 0.359 0.091  -0.007 -0.028 495 VAL DDD CG1 
14958 C CG2 . VAL D 495 ? 0.360 0.643 0.369 0.090  0.000  -0.018 495 VAL DDD CG2 
14959 N N   . PHE D 496 ? 0.329 0.585 0.342 0.092  -0.011 -0.038 496 PHE DDD N   
14960 C CA  . PHE D 496 ? 0.332 0.590 0.347 0.095  -0.014 -0.047 496 PHE DDD CA  
14961 C C   . PHE D 496 ? 0.340 0.599 0.362 0.095  -0.015 -0.049 496 PHE DDD C   
14962 O O   . PHE D 496 ? 0.356 0.619 0.382 0.097  -0.017 -0.056 496 PHE DDD O   
14963 C CB  . PHE D 496 ? 0.319 0.565 0.331 0.095  -0.018 -0.051 496 PHE DDD CB  
14964 C CG  . PHE D 496 ? 0.320 0.569 0.326 0.096  -0.018 -0.052 496 PHE DDD CG  
14965 C CD1 . PHE D 496 ? 0.314 0.575 0.319 0.099  -0.017 -0.057 496 PHE DDD CD1 
14966 C CD2 . PHE D 496 ? 0.306 0.548 0.307 0.094  -0.018 -0.048 496 PHE DDD CD2 
14967 C CE1 . PHE D 496 ? 0.316 0.581 0.316 0.100  -0.017 -0.058 496 PHE DDD CE1 
14968 C CE2 . PHE D 496 ? 0.312 0.557 0.308 0.095  -0.017 -0.049 496 PHE DDD CE2 
14969 C CZ  . PHE D 496 ? 0.309 0.566 0.305 0.098  -0.017 -0.054 496 PHE DDD CZ  
14970 N N   . GLY D 497 ? 0.347 0.603 0.373 0.093  -0.013 -0.043 497 GLY DDD N   
14971 C CA  . GLY D 497 ? 0.353 0.611 0.388 0.093  -0.014 -0.045 497 GLY DDD CA  
14972 C C   . GLY D 497 ? 0.367 0.639 0.406 0.093  -0.009 -0.043 497 GLY DDD C   
14973 O O   . GLY D 497 ? 0.425 0.700 0.471 0.094  -0.009 -0.045 497 GLY DDD O   
14974 N N   . ILE D 498 ? 0.385 0.667 0.420 0.093  -0.004 -0.038 498 ILE DDD N   
14975 C CA  . ILE D 498 ? 0.391 0.687 0.429 0.093  0.001  -0.034 498 ILE DDD CA  
14976 C C   . ILE D 498 ? 0.362 0.673 0.395 0.094  0.004  -0.034 498 ILE DDD C   
14977 O O   . ILE D 498 ? 0.330 0.650 0.362 0.093  0.009  -0.028 498 ILE DDD O   
14978 C CB  . ILE D 498 ? 0.405 0.698 0.446 0.090  0.003  -0.024 498 ILE DDD CB  
14979 C CG1 . ILE D 498 ? 0.428 0.715 0.462 0.088  0.003  -0.020 498 ILE DDD CG1 
14980 C CG2 . ILE D 498 ? 0.408 0.689 0.456 0.088  0.001  -0.024 498 ILE DDD CG2 
14981 C CD1 . ILE D 498 ? 0.443 0.731 0.479 0.086  0.006  -0.010 498 ILE DDD CD1 
14982 N N   . LEU D 499 ? 0.373 0.683 0.401 0.097  0.002  -0.042 499 LEU DDD N   
14983 C CA  . LEU D 499 ? 0.439 0.764 0.462 0.099  0.004  -0.044 499 LEU DDD CA  
14984 C C   . LEU D 499 ? 0.501 0.842 0.530 0.100  0.007  -0.048 499 LEU DDD C   
14985 O O   . LEU D 499 ? 0.561 0.898 0.596 0.101  0.005  -0.055 499 LEU DDD O   
14986 C CB  . LEU D 499 ? 0.428 0.748 0.446 0.101  -0.000 -0.051 499 LEU DDD CB  
14987 C CG  . LEU D 499 ? 0.410 0.717 0.423 0.099  -0.003 -0.047 499 LEU DDD CG  
14988 C CD1 . LEU D 499 ? 0.405 0.707 0.416 0.101  -0.007 -0.055 499 LEU DDD CD1 
14989 C CD2 . LEU D 499 ? 0.405 0.719 0.412 0.099  0.000  -0.040 499 LEU DDD CD2 
14990 N N   . GLU D 500 ? 0.545 0.901 0.570 0.099  0.013  -0.044 500 GLU DDD N   
14991 C CA  . GLU D 500 ? 0.576 0.947 0.606 0.100  0.017  -0.048 500 GLU DDD CA  
14992 C C   . GLU D 500 ? 0.585 0.975 0.608 0.101  0.021  -0.049 500 GLU DDD C   
14993 O O   . GLU D 500 ? 0.684 1.087 0.710 0.103  0.023  -0.056 500 GLU DDD O   
14994 C CB  . GLU D 500 ? 0.584 0.957 0.621 0.097  0.021  -0.040 500 GLU DDD CB  
14995 C CG  . GLU D 500 ? 0.606 0.978 0.639 0.095  0.023  -0.028 500 GLU DDD CG  
14996 C CD  . GLU D 500 ? 0.671 1.043 0.713 0.092  0.026  -0.021 500 GLU DDD CD  
14997 O OE1 . GLU D 500 ? 0.605 0.971 0.656 0.092  0.025  -0.026 500 GLU DDD OE1 
14998 O OE2 . GLU D 500 ? 0.758 1.137 0.799 0.089  0.030  -0.011 500 GLU DDD OE2 
14999 N N   . VAL D 501 ? 0.558 0.948 0.571 0.101  0.021  -0.043 501 VAL DDD N   
15000 C CA  . VAL D 501 ? 0.561 0.969 0.566 0.101  0.024  -0.042 501 VAL DDD CA  
15001 C C   . VAL D 501 ? 0.539 0.949 0.541 0.105  0.021  -0.054 501 VAL DDD C   
15002 O O   . VAL D 501 ? 0.524 0.920 0.526 0.106  0.016  -0.056 501 VAL DDD O   
15003 C CB  . VAL D 501 ? 0.589 0.997 0.586 0.099  0.025  -0.031 501 VAL DDD CB  
15004 C CG1 . VAL D 501 ? 0.595 1.021 0.582 0.100  0.028  -0.030 501 VAL DDD CG1 
15005 C CG2 . VAL D 501 ? 0.586 0.990 0.588 0.096  0.028  -0.019 501 VAL DDD CG2 
15006 N N   . THR D 502 ? 0.539 0.966 0.539 0.107  0.023  -0.061 502 THR DDD N   
15007 C CA  . THR D 502 ? 0.536 0.967 0.535 0.110  0.020  -0.074 502 THR DDD CA  
15008 C C   . THR D 502 ? 0.538 0.982 0.525 0.110  0.022  -0.071 502 THR DDD C   
15009 O O   . THR D 502 ? 0.542 0.996 0.523 0.108  0.026  -0.062 502 THR DDD O   
15010 C CB  . THR D 502 ? 0.528 0.968 0.535 0.112  0.021  -0.085 502 THR DDD CB  
15011 O OG1 . THR D 502 ? 0.566 1.028 0.570 0.111  0.028  -0.085 502 THR DDD OG1 
15012 C CG2 . THR D 502 ? 0.499 0.928 0.518 0.111  0.020  -0.086 502 THR DDD CG2 
15013 N N   . LYS D 503 ? 0.555 0.997 0.538 0.113  0.018  -0.078 503 LYS DDD N   
15014 C CA  . LYS D 503 ? 0.602 1.057 0.574 0.114  0.019  -0.079 503 LYS DDD CA  
15015 C C   . LYS D 503 ? 0.599 1.077 0.570 0.114  0.024  -0.084 503 LYS DDD C   
15016 O O   . LYS D 503 ? 0.607 1.098 0.570 0.112  0.028  -0.075 503 LYS DDD O   
15017 C CB  . LYS D 503 ? 0.638 1.088 0.609 0.117  0.013  -0.088 503 LYS DDD CB  
15018 C CG  . LYS D 503 ? 0.648 1.111 0.609 0.118  0.013  -0.089 503 LYS DDD CG  
15019 C CD  . LYS D 503 ? 0.647 1.109 0.609 0.122  0.008  -0.102 503 LYS DDD CD  
15020 C CE  . LYS D 503 ? 0.668 1.150 0.622 0.124  0.009  -0.107 503 LYS DDD CE  
15021 N NZ  . LYS D 503 ? 0.644 1.124 0.588 0.123  0.007  -0.100 503 LYS DDD NZ  
15022 N N   . ARG D 504 ? 0.633 1.115 0.613 0.116  0.024  -0.096 504 ARG DDD N   
15023 C CA  . ARG D 504 ? 0.643 1.147 0.624 0.117  0.029  -0.104 504 ARG DDD CA  
15024 C C   . ARG D 504 ? 0.626 1.139 0.603 0.113  0.036  -0.092 504 ARG DDD C   
15025 O O   . ARG D 504 ? 0.604 1.137 0.573 0.113  0.040  -0.092 504 ARG DDD O   
15026 C CB  . ARG D 504 ? 0.653 1.155 0.648 0.119  0.028  -0.117 504 ARG DDD CB  
15027 C CG  . ARG D 504 ? 0.660 1.183 0.658 0.119  0.034  -0.123 504 ARG DDD CG  
15028 C CD  . ARG D 504 ? 0.657 1.182 0.670 0.122  0.033  -0.138 504 ARG DDD CD  
15029 N NE  . ARG D 504 ? 0.637 1.161 0.653 0.126  0.027  -0.150 504 ARG DDD NE  
15030 C CZ  . ARG D 504 ? 0.634 1.141 0.660 0.128  0.021  -0.156 504 ARG DDD CZ  
15031 N NH1 . ARG D 504 ? 0.636 1.127 0.670 0.126  0.019  -0.151 504 ARG DDD NH1 
15032 N NH2 . ARG D 504 ? 0.642 1.148 0.670 0.131  0.016  -0.167 504 ARG DDD NH2 
15033 N N   . SER D 505 ? 0.603 1.103 0.586 0.111  0.036  -0.083 505 SER DDD N   
15034 C CA  . SER D 505 ? 0.589 1.097 0.572 0.107  0.043  -0.072 505 SER DDD CA  
15035 C C   . SER D 505 ? 0.618 1.135 0.587 0.105  0.045  -0.060 505 SER DDD C   
15036 O O   . SER D 505 ? 0.682 1.212 0.648 0.102  0.051  -0.053 505 SER DDD O   
15037 C CB  . SER D 505 ? 0.606 1.096 0.597 0.105  0.042  -0.064 505 SER DDD CB  
15038 O OG  . SER D 505 ? 0.564 1.041 0.550 0.104  0.039  -0.052 505 SER DDD OG  
15039 N N   . GLY D 506 ? 0.601 1.111 0.562 0.106  0.040  -0.058 506 GLY DDD N   
15040 C CA  . GLY D 506 ? 0.598 1.115 0.546 0.105  0.041  -0.047 506 GLY DDD CA  
15041 C C   . GLY D 506 ? 0.593 1.102 0.542 0.101  0.043  -0.031 506 GLY DDD C   
15042 O O   . GLY D 506 ? 0.585 1.099 0.525 0.099  0.043  -0.020 506 GLY DDD O   
15043 N N   . GLU D 507 ? 0.587 1.085 0.547 0.099  0.044  -0.028 507 GLU DDD N   
15044 C CA  . GLU D 507 ? 0.607 1.095 0.571 0.096  0.045  -0.014 507 GLU DDD CA  
15045 C C   . GLU D 507 ? 0.573 1.044 0.536 0.096  0.039  -0.009 507 GLU DDD C   
15046 O O   . GLU D 507 ? 0.497 0.960 0.457 0.099  0.034  -0.017 507 GLU DDD O   
15047 C CB  . GLU D 507 ? 0.651 1.132 0.628 0.095  0.046  -0.016 507 GLU DDD CB  
15048 C CG  . GLU D 507 ? 0.698 1.197 0.679 0.094  0.053  -0.018 507 GLU DDD CG  
15049 C CD  . GLU D 507 ? 0.742 1.233 0.736 0.093  0.054  -0.022 507 GLU DDD CD  
15050 O OE1 . GLU D 507 ? 0.787 1.264 0.789 0.096  0.049  -0.030 507 GLU DDD OE1 
15051 O OE2 . GLU D 507 ? 0.762 1.263 0.762 0.091  0.060  -0.017 507 GLU DDD OE2 
15052 N N   . SER D 508 ? 0.585 1.049 0.548 0.093  0.039  0.005  508 SER DDD N   
15053 C CA  . SER D 508 ? 0.603 1.051 0.566 0.093  0.034  0.011  508 SER DDD CA  
15054 C C   . SER D 508 ? 0.601 1.029 0.573 0.094  0.031  0.005  508 SER DDD C   
15055 O O   . SER D 508 ? 0.558 0.983 0.540 0.092  0.032  0.005  508 SER DDD O   
15056 C CB  . SER D 508 ? 0.597 1.043 0.561 0.089  0.036  0.027  508 SER DDD CB  
15057 O OG  . SER D 508 ? 0.560 0.991 0.526 0.089  0.031  0.032  508 SER DDD OG  
15058 N N   . PHE D 509 ? 0.637 1.055 0.607 0.095  0.025  0.000  509 PHE DDD N   
15059 C CA  . PHE D 509 ? 0.668 1.067 0.644 0.096  0.021  -0.005 509 PHE DDD CA  
15060 C C   . PHE D 509 ? 0.613 0.998 0.592 0.094  0.019  0.004  509 PHE DDD C   
15061 O O   . PHE D 509 ? 0.503 0.872 0.486 0.094  0.016  0.002  509 PHE DDD O   
15062 C CB  . PHE D 509 ? 0.710 1.106 0.684 0.099  0.018  -0.018 509 PHE DDD CB  
15063 C CG  . PHE D 509 ? 0.739 1.140 0.704 0.101  0.015  -0.019 509 PHE DDD CG  
15064 C CD1 . PHE D 509 ? 0.768 1.158 0.732 0.101  0.012  -0.015 509 PHE DDD CD1 
15065 C CD2 . PHE D 509 ? 0.744 1.163 0.702 0.103  0.017  -0.025 509 PHE DDD CD2 
15066 C CE1 . PHE D 509 ? 0.778 1.173 0.734 0.102  0.009  -0.016 509 PHE DDD CE1 
15067 C CE2 . PHE D 509 ? 0.773 1.197 0.723 0.105  0.014  -0.026 509 PHE DDD CE2 
15068 C CZ  . PHE D 509 ? 0.799 1.211 0.748 0.104  0.010  -0.022 509 PHE DDD CZ  
15069 N N   . VAL D 510 ? 0.648 1.039 0.624 0.092  0.020  0.015  510 VAL DDD N   
15070 C CA  . VAL D 510 ? 0.689 1.067 0.668 0.090  0.019  0.025  510 VAL DDD CA  
15071 C C   . VAL D 510 ? 0.714 1.086 0.704 0.087  0.021  0.030  510 VAL DDD C   
15072 O O   . VAL D 510 ? 0.742 1.125 0.734 0.086  0.025  0.032  510 VAL DDD O   
15073 C CB  . VAL D 510 ? 0.692 1.079 0.666 0.089  0.019  0.035  510 VAL DDD CB  
15074 C CG1 . VAL D 510 ? 0.684 1.060 0.664 0.086  0.018  0.046  510 VAL DDD CG1 
15075 C CG2 . VAL D 510 ? 0.703 1.093 0.667 0.092  0.015  0.029  510 VAL DDD CG2 
15076 N N   . SER D 511 ? 0.759 1.115 0.755 0.086  0.019  0.031  511 SER DDD N   
15077 C CA  . SER D 511 ? 0.823 1.172 0.829 0.083  0.020  0.038  511 SER DDD CA  
15078 C C   . SER D 511 ? 0.929 1.271 0.939 0.081  0.018  0.047  511 SER DDD C   
15079 O O   . SER D 511 ? 0.856 1.188 0.864 0.082  0.015  0.043  511 SER DDD O   
15080 C CB  . SER D 511 ? 0.824 1.162 0.837 0.083  0.019  0.031  511 SER DDD CB  
15081 O OG  . SER D 511 ? 0.797 1.142 0.808 0.085  0.020  0.022  511 SER DDD OG  
15082 N N   . SER D 512 ? 1.082 1.429 1.098 0.079  0.021  0.058  512 SER DDD N   
15083 C CA  . SER D 512 ? 1.134 1.476 1.153 0.077  0.019  0.068  512 SER DDD CA  
15084 C C   . SER D 512 ? 1.128 1.457 1.160 0.075  0.018  0.070  512 SER DDD C   
15085 O O   . SER D 512 ? 1.107 1.427 1.142 0.074  0.015  0.073  512 SER DDD O   
15086 C CB  . SER D 512 ? 1.172 1.528 1.190 0.076  0.022  0.080  512 SER DDD CB  
15087 O OG  . SER D 512 ? 1.197 1.565 1.202 0.078  0.021  0.078  512 SER DDD OG  
15088 N N   . GLY D 513 ? 1.126 1.452 1.165 0.074  0.020  0.069  513 GLY DDD N   
15089 C CA  . GLY D 513 ? 1.087 1.400 1.137 0.072  0.019  0.069  513 GLY DDD CA  
15090 C C   . GLY D 513 ? 1.046 1.346 1.094 0.073  0.015  0.060  513 GLY DDD C   
15091 O O   . GLY D 513 ? 1.069 1.369 1.108 0.075  0.014  0.051  513 GLY DDD O   
15092 N N   . GLY D 514 ? 0.974 1.262 1.031 0.071  0.014  0.061  514 GLY DDD N   
15093 C CA  . GLY D 514 ? 0.938 1.214 0.994 0.072  0.010  0.054  514 GLY DDD CA  
15094 C C   . GLY D 514 ? 0.854 1.120 0.914 0.071  0.010  0.047  514 GLY DDD C   
15095 O O   . GLY D 514 ? 0.773 1.028 0.839 0.069  0.008  0.047  514 GLY DDD O   
15096 N N   . CYS D 515 ? 0.813 1.081 0.870 0.072  0.011  0.042  515 CYS DDD N   
15097 C CA  . CYS D 515 ? 0.806 1.065 0.865 0.072  0.009  0.035  515 CYS DDD CA  
15098 C C   . CYS D 515 ? 0.730 0.982 0.780 0.073  0.006  0.026  515 CYS DDD C   
15099 O O   . CYS D 515 ? 0.748 0.992 0.797 0.073  0.004  0.020  515 CYS DDD O   
15100 C CB  . CYS D 515 ? 0.789 1.055 0.851 0.072  0.011  0.033  515 CYS DDD CB  
15101 S SG  . CYS D 515 ? 0.905 1.187 0.970 0.072  0.016  0.042  515 CYS DDD SG  
15102 N N   . GLY D 516 ? 0.702 0.956 0.744 0.074  0.005  0.026  516 GLY DDD N   
15103 C CA  . GLY D 516 ? 0.682 0.931 0.715 0.076  0.003  0.018  516 GLY DDD CA  
15104 C C   . GLY D 516 ? 0.652 0.908 0.680 0.078  0.003  0.013  516 GLY DDD C   
15105 O O   . GLY D 516 ? 0.599 0.867 0.625 0.079  0.005  0.015  516 GLY DDD O   
15106 N N   . GLY D 517 ? 0.676 0.924 0.700 0.079  0.000  0.005  517 GLY DDD N   
15107 C CA  . GLY D 517 ? 0.722 0.975 0.742 0.081  -0.000 -0.002 517 GLY DDD CA  
15108 C C   . GLY D 517 ? 0.691 0.949 0.717 0.081  0.001  -0.002 517 GLY DDD C   
15109 O O   . GLY D 517 ? 0.677 0.942 0.701 0.084  0.001  -0.007 517 GLY DDD O   
15110 N N   . GLY D 518 ? 0.725 0.979 0.758 0.079  0.002  0.002  518 GLY DDD N   
15111 C CA  . GLY D 518 ? 0.778 1.033 0.818 0.079  0.002  0.000  518 GLY DDD CA  
15112 C C   . GLY D 518 ? 0.743 1.008 0.790 0.078  0.006  0.007  518 GLY DDD C   
15113 O O   . GLY D 518 ? 0.846 1.122 0.890 0.079  0.009  0.011  518 GLY DDD O   
15114 N N   . LYS D 519 ? 0.637 0.899 0.693 0.077  0.006  0.008  519 LYS DDD N   
15115 C CA  . LYS D 519 ? 0.575 0.843 0.640 0.075  0.009  0.015  519 LYS DDD CA  
15116 C C   . LYS D 519 ? 0.551 0.808 0.624 0.073  0.008  0.015  519 LYS DDD C   
15117 O O   . LYS D 519 ? 0.470 0.717 0.542 0.073  0.004  0.009  519 LYS DDD O   
15118 C CB  . LYS D 519 ? 0.563 0.842 0.631 0.077  0.012  0.013  519 LYS DDD CB  
15119 C CG  . LYS D 519 ? 0.538 0.832 0.601 0.078  0.015  0.014  519 LYS DDD CG  
15120 C CD  . LYS D 519 ? 0.522 0.828 0.591 0.077  0.020  0.023  519 LYS DDD CD  
15121 C CE  . LYS D 519 ? 0.516 0.836 0.576 0.078  0.024  0.025  519 LYS DDD CE  
15122 N NZ  . LYS D 519 ? 0.500 0.828 0.563 0.076  0.027  0.036  519 LYS DDD NZ  
# 
