data_9HNL
# 
_entry.id   9HNL 
# 
_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   9HNL         pdb_00009hnl 10.2210/pdb9hnl/pdb 
WWPDB D_1292140259 ?            ?                   
# 
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 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
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.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HNL 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              essenl@staff.uni-marburg.de 
_pdbx_contact_author.name_first         Lars-Oliver 
_pdbx_contact_author.name_last          Essen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4272-4026 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Po Hsun, W.'       1 0000-0001-7359-934X 
'Maestre-Reyna, M.' 2 0000-0002-9566-7216 
'Essen, L.-O.'      3 0000-0003-4272-4026 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                16084 
_citation.page_last                 16098 
_citation.title                     'Redox-State-Dependent Structural Changes within a Prokaryotic 6-4 Photolyase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.4c18116 
_citation.pdbx_database_id_PubMed   40298610 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, P.H.'        1  ?                   
primary 'Hosokawa, Y.'      2  0000-0001-9559-8567 
primary 'C Soares, J.'      3  0009-0004-8682-8374 
primary 'Emmerich, H.J.'    4  ?                   
primary 'Fuchs, V.'         5  ?                   
primary 'Caramello, N.'     6  ?                   
primary 'Engilberge, S.'    7  ?                   
primary 'Bologna, A.'       8  ?                   
primary 'Rosner, C.J.'      9  ?                   
primary 'Nakamura, M.'      10 ?                   
primary 'Watad, M.'         11 ?                   
primary 'Luo, F.'           12 0000-0003-0631-6236 
primary 'Owada, S.'         13 ?                   
primary 'Tosha, T.'         14 0000-0002-8971-0759 
primary 'Kang, J.'          15 0000-0002-3506-6400 
primary 'Tono, K.'          16 ?                   
primary 'Bessho, Y.'        17 0000-0001-9297-7473 
primary 'Nango, E.'         18 ?                   
primary 'Pierik, A.J.'      19 0000-0002-1509-6370 
primary 'Royant, A.'        20 ?                   
primary 'Tsai, M.D.'        21 0000-0003-1374-0414 
primary 'Yamamoto, J.'      22 ?                   
primary 'Maestre-Reyna, M.' 23 ?                   
primary 'Essen, L.O.'       24 0000-0003-4272-4026 
# 
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 'Cryptochrome/photolyase family protein'                                    58121.285 1   ? ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'                                               785.550   1   ? ? ? ? 
3 non-polymer syn '1-deoxy-1-(6,7-dimethyl-2,4-dioxo-3,4-dihydropteridin-8(2H)-yl)-D-ribitol' 326.305   1   ? ? ? ? 
4 non-polymer syn 'IRON/SULFUR CLUSTER'                                                       351.640   1   ? ? ? ? 
5 water       nat water                                                                       18.015    322 ? ? ? ? 
# 
_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       
;MAGALRLVLGDQLSDNLSALVDADLSRDQVLMVESRVEATAWKHHKQKLVLVWSAMRQFAERLRARGFNVRYVTLEDPDN
TGSIGGELRRALEARAFDRVIRTACGKWGLESHLLSLDLPVPMETREDDRFLCSRAQFAAWAEGRRELRMEFFYREMRRK
TGLLMDGDQPAGGRWNFDAENRRKLPPGLRPPERLRIPPNPTTQTVLEQVSRGFDDHFGEVEGFGWPTNPDEATAILDHF
IADMLPSFGDWQDAMSWRRPFLWHSLISPALNIGLLDPLDICRRAEAAWREGRAPLNAVEGFIRQIIGWREFVRGIYWLK
MPEYAQRNALDAQGKLPGFYWTGQTDMACVADTVRAAHDHAYAHHIQRLMVTGNLAMLLGVHPDAVDDWYMVVFADAYEW
VEMPNTRGMATFADGGIVGSKPYAASGAYIDRMSDYCKGCRYDVKKRLGDDACPFNALYWDFIDRHAQRLAGNGRMMMPL
RTLEKMPDAEREAFRKQARALRVKMGVSG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAGALRLVLGDQLSDNLSALVDADLSRDQVLMVESRVEATAWKHHKQKLVLVWSAMRQFAERLRARGFNVRYVTLEDPDN
TGSIGGELRRALEARAFDRVIRTACGKWGLESHLLSLDLPVPMETREDDRFLCSRAQFAAWAEGRRELRMEFFYREMRRK
TGLLMDGDQPAGGRWNFDAENRRKLPPGLRPPERLRIPPNPTTQTVLEQVSRGFDDHFGEVEGFGWPTNPDEATAILDHF
IADMLPSFGDWQDAMSWRRPFLWHSLISPALNIGLLDPLDICRRAEAAWREGRAPLNAVEGFIRQIIGWREFVRGIYWLK
MPEYAQRNALDAQGKLPGFYWTGQTDMACVADTVRAAHDHAYAHHIQRLMVTGNLAMLLGVHPDAVDDWYMVVFADAYEW
VEMPNTRGMATFADGGIVGSKPYAASGAYIDRMSDYCKGCRYDVKKRLGDDACPFNALYWDFIDRHAQRLAGNGRMMMPL
RTLEKMPDAEREAFRKQARALRVKMGVSG
;
_entity_poly.pdbx_strand_id                 A 
_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 '1-deoxy-1-(6,7-dimethyl-2,4-dioxo-3,4-dihydropteridin-8(2H)-yl)-D-ribitol' DLZ 
4 'IRON/SULFUR CLUSTER'                                                       SF4 
5 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   ALA n 
1 3   GLY n 
1 4   ALA n 
1 5   LEU n 
1 6   ARG n 
1 7   LEU n 
1 8   VAL n 
1 9   LEU n 
1 10  GLY n 
1 11  ASP n 
1 12  GLN n 
1 13  LEU n 
1 14  SER n 
1 15  ASP n 
1 16  ASN n 
1 17  LEU n 
1 18  SER n 
1 19  ALA n 
1 20  LEU n 
1 21  VAL n 
1 22  ASP n 
1 23  ALA n 
1 24  ASP n 
1 25  LEU n 
1 26  SER n 
1 27  ARG n 
1 28  ASP n 
1 29  GLN n 
1 30  VAL n 
1 31  LEU n 
1 32  MET n 
1 33  VAL n 
1 34  GLU n 
1 35  SER n 
1 36  ARG n 
1 37  VAL n 
1 38  GLU n 
1 39  ALA n 
1 40  THR n 
1 41  ALA n 
1 42  TRP n 
1 43  LYS n 
1 44  HIS n 
1 45  HIS n 
1 46  LYS n 
1 47  GLN n 
1 48  LYS n 
1 49  LEU n 
1 50  VAL n 
1 51  LEU n 
1 52  VAL n 
1 53  TRP n 
1 54  SER n 
1 55  ALA n 
1 56  MET n 
1 57  ARG n 
1 58  GLN n 
1 59  PHE n 
1 60  ALA n 
1 61  GLU n 
1 62  ARG n 
1 63  LEU n 
1 64  ARG n 
1 65  ALA n 
1 66  ARG n 
1 67  GLY n 
1 68  PHE n 
1 69  ASN n 
1 70  VAL n 
1 71  ARG n 
1 72  TYR n 
1 73  VAL n 
1 74  THR n 
1 75  LEU n 
1 76  GLU n 
1 77  ASP n 
1 78  PRO n 
1 79  ASP n 
1 80  ASN n 
1 81  THR n 
1 82  GLY n 
1 83  SER n 
1 84  ILE n 
1 85  GLY n 
1 86  GLY n 
1 87  GLU n 
1 88  LEU n 
1 89  ARG n 
1 90  ARG n 
1 91  ALA n 
1 92  LEU n 
1 93  GLU n 
1 94  ALA n 
1 95  ARG n 
1 96  ALA n 
1 97  PHE n 
1 98  ASP n 
1 99  ARG n 
1 100 VAL n 
1 101 ILE n 
1 102 ARG n 
1 103 THR n 
1 104 ALA n 
1 105 CYS n 
1 106 GLY n 
1 107 LYS n 
1 108 TRP n 
1 109 GLY n 
1 110 LEU n 
1 111 GLU n 
1 112 SER n 
1 113 HIS n 
1 114 LEU n 
1 115 LEU n 
1 116 SER n 
1 117 LEU n 
1 118 ASP n 
1 119 LEU n 
1 120 PRO n 
1 121 VAL n 
1 122 PRO n 
1 123 MET n 
1 124 GLU n 
1 125 THR n 
1 126 ARG n 
1 127 GLU n 
1 128 ASP n 
1 129 ASP n 
1 130 ARG n 
1 131 PHE n 
1 132 LEU n 
1 133 CYS n 
1 134 SER n 
1 135 ARG n 
1 136 ALA n 
1 137 GLN n 
1 138 PHE n 
1 139 ALA n 
1 140 ALA n 
1 141 TRP n 
1 142 ALA n 
1 143 GLU n 
1 144 GLY n 
1 145 ARG n 
1 146 ARG n 
1 147 GLU n 
1 148 LEU n 
1 149 ARG n 
1 150 MET n 
1 151 GLU n 
1 152 PHE n 
1 153 PHE n 
1 154 TYR n 
1 155 ARG n 
1 156 GLU n 
1 157 MET n 
1 158 ARG n 
1 159 ARG n 
1 160 LYS n 
1 161 THR n 
1 162 GLY n 
1 163 LEU n 
1 164 LEU n 
1 165 MET n 
1 166 ASP n 
1 167 GLY n 
1 168 ASP n 
1 169 GLN n 
1 170 PRO n 
1 171 ALA n 
1 172 GLY n 
1 173 GLY n 
1 174 ARG n 
1 175 TRP n 
1 176 ASN n 
1 177 PHE n 
1 178 ASP n 
1 179 ALA n 
1 180 GLU n 
1 181 ASN n 
1 182 ARG n 
1 183 ARG n 
1 184 LYS n 
1 185 LEU n 
1 186 PRO n 
1 187 PRO n 
1 188 GLY n 
1 189 LEU n 
1 190 ARG n 
1 191 PRO n 
1 192 PRO n 
1 193 GLU n 
1 194 ARG n 
1 195 LEU n 
1 196 ARG n 
1 197 ILE n 
1 198 PRO n 
1 199 PRO n 
1 200 ASN n 
1 201 PRO n 
1 202 THR n 
1 203 THR n 
1 204 GLN n 
1 205 THR n 
1 206 VAL n 
1 207 LEU n 
1 208 GLU n 
1 209 GLN n 
1 210 VAL n 
1 211 SER n 
1 212 ARG n 
1 213 GLY n 
1 214 PHE n 
1 215 ASP n 
1 216 ASP n 
1 217 HIS n 
1 218 PHE n 
1 219 GLY n 
1 220 GLU n 
1 221 VAL n 
1 222 GLU n 
1 223 GLY n 
1 224 PHE n 
1 225 GLY n 
1 226 TRP n 
1 227 PRO n 
1 228 THR n 
1 229 ASN n 
1 230 PRO n 
1 231 ASP n 
1 232 GLU n 
1 233 ALA n 
1 234 THR n 
1 235 ALA n 
1 236 ILE n 
1 237 LEU n 
1 238 ASP n 
1 239 HIS n 
1 240 PHE n 
1 241 ILE n 
1 242 ALA n 
1 243 ASP n 
1 244 MET n 
1 245 LEU n 
1 246 PRO n 
1 247 SER n 
1 248 PHE n 
1 249 GLY n 
1 250 ASP n 
1 251 TRP n 
1 252 GLN n 
1 253 ASP n 
1 254 ALA n 
1 255 MET n 
1 256 SER n 
1 257 TRP n 
1 258 ARG n 
1 259 ARG n 
1 260 PRO n 
1 261 PHE n 
1 262 LEU n 
1 263 TRP n 
1 264 HIS n 
1 265 SER n 
1 266 LEU n 
1 267 ILE n 
1 268 SER n 
1 269 PRO n 
1 270 ALA n 
1 271 LEU n 
1 272 ASN n 
1 273 ILE n 
1 274 GLY n 
1 275 LEU n 
1 276 LEU n 
1 277 ASP n 
1 278 PRO n 
1 279 LEU n 
1 280 ASP n 
1 281 ILE n 
1 282 CYS n 
1 283 ARG n 
1 284 ARG n 
1 285 ALA n 
1 286 GLU n 
1 287 ALA n 
1 288 ALA n 
1 289 TRP n 
1 290 ARG n 
1 291 GLU n 
1 292 GLY n 
1 293 ARG n 
1 294 ALA n 
1 295 PRO n 
1 296 LEU n 
1 297 ASN n 
1 298 ALA n 
1 299 VAL n 
1 300 GLU n 
1 301 GLY n 
1 302 PHE n 
1 303 ILE n 
1 304 ARG n 
1 305 GLN n 
1 306 ILE n 
1 307 ILE n 
1 308 GLY n 
1 309 TRP n 
1 310 ARG n 
1 311 GLU n 
1 312 PHE n 
1 313 VAL n 
1 314 ARG n 
1 315 GLY n 
1 316 ILE n 
1 317 TYR n 
1 318 TRP n 
1 319 LEU n 
1 320 LYS n 
1 321 MET n 
1 322 PRO n 
1 323 GLU n 
1 324 TYR n 
1 325 ALA n 
1 326 GLN n 
1 327 ARG n 
1 328 ASN n 
1 329 ALA n 
1 330 LEU n 
1 331 ASP n 
1 332 ALA n 
1 333 GLN n 
1 334 GLY n 
1 335 LYS n 
1 336 LEU n 
1 337 PRO n 
1 338 GLY n 
1 339 PHE n 
1 340 TYR n 
1 341 TRP n 
1 342 THR n 
1 343 GLY n 
1 344 GLN n 
1 345 THR n 
1 346 ASP n 
1 347 MET n 
1 348 ALA n 
1 349 CYS n 
1 350 VAL n 
1 351 ALA n 
1 352 ASP n 
1 353 THR n 
1 354 VAL n 
1 355 ARG n 
1 356 ALA n 
1 357 ALA n 
1 358 HIS n 
1 359 ASP n 
1 360 HIS n 
1 361 ALA n 
1 362 TYR n 
1 363 ALA n 
1 364 HIS n 
1 365 HIS n 
1 366 ILE n 
1 367 GLN n 
1 368 ARG n 
1 369 LEU n 
1 370 MET n 
1 371 VAL n 
1 372 THR n 
1 373 GLY n 
1 374 ASN n 
1 375 LEU n 
1 376 ALA n 
1 377 MET n 
1 378 LEU n 
1 379 LEU n 
1 380 GLY n 
1 381 VAL n 
1 382 HIS n 
1 383 PRO n 
1 384 ASP n 
1 385 ALA n 
1 386 VAL n 
1 387 ASP n 
1 388 ASP n 
1 389 TRP n 
1 390 TYR n 
1 391 MET n 
1 392 VAL n 
1 393 VAL n 
1 394 PHE n 
1 395 ALA n 
1 396 ASP n 
1 397 ALA n 
1 398 TYR n 
1 399 GLU n 
1 400 TRP n 
1 401 VAL n 
1 402 GLU n 
1 403 MET n 
1 404 PRO n 
1 405 ASN n 
1 406 THR n 
1 407 ARG n 
1 408 GLY n 
1 409 MET n 
1 410 ALA n 
1 411 THR n 
1 412 PHE n 
1 413 ALA n 
1 414 ASP n 
1 415 GLY n 
1 416 GLY n 
1 417 ILE n 
1 418 VAL n 
1 419 GLY n 
1 420 SER n 
1 421 LYS n 
1 422 PRO n 
1 423 TYR n 
1 424 ALA n 
1 425 ALA n 
1 426 SER n 
1 427 GLY n 
1 428 ALA n 
1 429 TYR n 
1 430 ILE n 
1 431 ASP n 
1 432 ARG n 
1 433 MET n 
1 434 SER n 
1 435 ASP n 
1 436 TYR n 
1 437 CYS n 
1 438 LYS n 
1 439 GLY n 
1 440 CYS n 
1 441 ARG n 
1 442 TYR n 
1 443 ASP n 
1 444 VAL n 
1 445 LYS n 
1 446 LYS n 
1 447 ARG n 
1 448 LEU n 
1 449 GLY n 
1 450 ASP n 
1 451 ASP n 
1 452 ALA n 
1 453 CYS n 
1 454 PRO n 
1 455 PHE n 
1 456 ASN n 
1 457 ALA n 
1 458 LEU n 
1 459 TYR n 
1 460 TRP n 
1 461 ASP n 
1 462 PHE n 
1 463 ILE n 
1 464 ASP n 
1 465 ARG n 
1 466 HIS n 
1 467 ALA n 
1 468 GLN n 
1 469 ARG n 
1 470 LEU n 
1 471 ALA n 
1 472 GLY n 
1 473 ASN n 
1 474 GLY n 
1 475 ARG n 
1 476 MET n 
1 477 MET n 
1 478 MET n 
1 479 PRO n 
1 480 LEU n 
1 481 ARG n 
1 482 THR n 
1 483 LEU n 
1 484 GLU n 
1 485 LYS n 
1 486 MET n 
1 487 PRO n 
1 488 ASP n 
1 489 ALA n 
1 490 GLU n 
1 491 ARG n 
1 492 GLU n 
1 493 ALA n 
1 494 PHE n 
1 495 ARG n 
1 496 LYS n 
1 497 GLN n 
1 498 ALA n 
1 499 ARG n 
1 500 ALA n 
1 501 LEU n 
1 502 ARG n 
1 503 VAL n 
1 504 LYS n 
1 505 MET n 
1 506 GLY n 
1 507 VAL n 
1 508 SER n 
1 509 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                   509 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CC_0646 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Caulobacter vibrioides' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     155892 
_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 B' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     37762 
_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               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              Gold 
_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 
DLZ non-polymer         . '1-deoxy-1-(6,7-dimethyl-2,4-dioxo-3,4-dihydropteridin-8(2H)-yl)-D-ribitol' 
;6,7-dimethyl-8-(1'-D-ribityl) lumazine
;
'C13 H18 N4 O6'     326.305 
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 
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 
SF4 non-polymer         . 'IRON/SULFUR CLUSTER'                                                       ? 'Fe4 S4'            
351.640 
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   1   MET MET A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   GLY 3   3   3   GLY GLY A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   ARG 6   6   6   ARG ARG A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   VAL 8   8   8   VAL VAL A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  MET 32  32  32  MET MET A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  GLU 38  38  38  GLU GLU A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  TRP 42  42  42  TRP TRP A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  HIS 44  44  44  HIS HIS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  GLN 47  47  47  GLN GLN A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  TRP 53  53  53  TRP TRP A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  MET 56  56  56  MET MET A . n 
A 1 57  ARG 57  57  57  ARG ARG A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  ASN 80  80  80  ASN ASN A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ARG 95  95  95  ARG ARG A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  PHE 97  97  97  PHE PHE A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 CYS 105 105 105 CYS CYS A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 TRP 108 108 108 TRP TRP A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 HIS 113 113 113 HIS HIS A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 ASP 118 118 118 ASP ASP A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 MET 123 123 123 MET MET A . n 
A 1 124 GLU 124 124 124 GLU GLU A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 ARG 130 130 130 ARG ARG A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 CYS 133 133 133 CYS CYS A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 GLN 137 137 137 GLN GLN A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 TRP 141 141 141 TRP TRP A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 MET 150 150 150 MET MET A . n 
A 1 151 GLU 151 151 151 GLU GLU A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 ARG 159 159 159 ARG ARG A . n 
A 1 160 LYS 160 160 160 LYS LYS A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 ASP 166 166 166 ASP ASP A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 ASP 168 168 168 ASP ASP A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 ARG 174 174 174 ARG ARG A . n 
A 1 175 TRP 175 175 175 TRP TRP A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 ASP 178 178 178 ASP ASP A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 ASN 181 181 181 ASN ASN A . n 
A 1 182 ARG 182 182 182 ARG ARG A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 PRO 187 187 187 PRO PRO A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 PRO 191 191 191 PRO PRO A . n 
A 1 192 PRO 192 192 192 PRO PRO A . n 
A 1 193 GLU 193 193 193 GLU GLU A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 GLN 204 204 204 GLN GLN A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 GLU 208 208 208 GLU GLU A . n 
A 1 209 GLN 209 209 209 GLN GLN A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 SER 211 211 211 SER SER A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 PHE 214 214 214 PHE PHE A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 HIS 217 217 217 HIS HIS A . n 
A 1 218 PHE 218 218 218 PHE PHE A . n 
A 1 219 GLY 219 219 219 GLY GLY A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 GLY 223 223 223 GLY GLY A . n 
A 1 224 PHE 224 224 224 PHE PHE A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 TRP 226 226 226 TRP TRP A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 GLU 232 232 232 GLU GLU A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 THR 234 234 234 THR THR A . n 
A 1 235 ALA 235 235 235 ALA ALA A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 HIS 239 239 239 HIS HIS A . n 
A 1 240 PHE 240 240 240 PHE PHE A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 ALA 242 242 242 ALA ALA A . n 
A 1 243 ASP 243 243 243 ASP ASP A . n 
A 1 244 MET 244 244 244 MET MET A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 GLY 249 249 249 GLY GLY A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 TRP 251 251 251 TRP TRP A . n 
A 1 252 GLN 252 252 252 GLN GLN A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 ALA 254 254 254 ALA ALA A . n 
A 1 255 MET 255 255 255 MET MET A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 TRP 257 257 257 TRP TRP A . n 
A 1 258 ARG 258 258 258 ARG ARG A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 PRO 260 260 260 PRO PRO A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 TRP 263 263 263 TRP TRP A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 PRO 269 269 269 PRO PRO A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 ASN 272 272 272 ASN ASN A . n 
A 1 273 ILE 273 273 273 ILE ILE A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 ASP 277 277 277 ASP ASP A . n 
A 1 278 PRO 278 278 278 PRO PRO A . n 
A 1 279 LEU 279 279 279 LEU LEU A . n 
A 1 280 ASP 280 280 280 ASP ASP A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 CYS 282 282 282 CYS CYS A . n 
A 1 283 ARG 283 283 283 ARG ARG A . n 
A 1 284 ARG 284 284 284 ARG ARG A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 GLU 286 286 286 GLU GLU A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 TRP 289 289 289 TRP TRP A . n 
A 1 290 ARG 290 290 290 ARG ARG A . n 
A 1 291 GLU 291 291 291 GLU GLU A . n 
A 1 292 GLY 292 292 292 GLY GLY A . n 
A 1 293 ARG 293 293 293 ARG ARG A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 PRO 295 295 295 PRO PRO A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 ASN 297 297 297 ASN ASN A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 GLU 300 300 300 GLU GLU A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 PHE 302 302 302 PHE PHE A . n 
A 1 303 ILE 303 303 303 ILE ILE A . n 
A 1 304 ARG 304 304 304 ARG ARG A . n 
A 1 305 GLN 305 305 305 GLN GLN A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 ILE 307 307 307 ILE ILE A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 TRP 309 309 309 TRP TRP A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 PHE 312 312 312 PHE PHE A . n 
A 1 313 VAL 313 313 313 VAL VAL A . n 
A 1 314 ARG 314 314 314 ARG ARG A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 ILE 316 316 316 ILE ILE A . n 
A 1 317 TYR 317 317 317 TYR TYR A . n 
A 1 318 TRP 318 318 318 TRP TRP A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 LYS 320 320 320 LYS LYS A . n 
A 1 321 MET 321 321 321 MET MET A . n 
A 1 322 PRO 322 322 322 PRO PRO A . n 
A 1 323 GLU 323 323 323 GLU GLU A . n 
A 1 324 TYR 324 324 324 TYR TYR A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 GLN 326 326 326 GLN GLN A . n 
A 1 327 ARG 327 327 327 ARG ARG A . n 
A 1 328 ASN 328 328 328 ASN ASN A . n 
A 1 329 ALA 329 329 329 ALA ALA A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 ASP 331 331 331 ASP ASP A . n 
A 1 332 ALA 332 332 332 ALA ALA A . n 
A 1 333 GLN 333 333 333 GLN GLN A . n 
A 1 334 GLY 334 334 334 GLY GLY A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 LEU 336 336 336 LEU LEU A . n 
A 1 337 PRO 337 337 337 PRO PRO A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 PHE 339 339 339 PHE PHE A . n 
A 1 340 TYR 340 340 340 TYR TYR A . n 
A 1 341 TRP 341 341 341 TRP TRP A . n 
A 1 342 THR 342 342 342 THR THR A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 GLN 344 344 344 GLN GLN A . n 
A 1 345 THR 345 345 345 THR THR A . n 
A 1 346 ASP 346 346 346 ASP ASP A . n 
A 1 347 MET 347 347 347 MET MET A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 CYS 349 349 349 CYS CYS A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 ALA 351 351 351 ALA ALA A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 THR 353 353 353 THR THR A . n 
A 1 354 VAL 354 354 354 VAL VAL A . n 
A 1 355 ARG 355 355 355 ARG ARG A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 HIS 358 358 358 HIS HIS A . n 
A 1 359 ASP 359 359 359 ASP ASP A . n 
A 1 360 HIS 360 360 360 HIS HIS A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 TYR 362 362 362 TYR TYR A . n 
A 1 363 ALA 363 363 363 ALA ALA A . n 
A 1 364 HIS 364 364 364 HIS HIS A . n 
A 1 365 HIS 365 365 365 HIS HIS A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 GLN 367 367 367 GLN GLN A . n 
A 1 368 ARG 368 368 368 ARG ARG A . n 
A 1 369 LEU 369 369 369 LEU LEU A . n 
A 1 370 MET 370 370 370 MET MET A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 THR 372 372 372 THR THR A . n 
A 1 373 GLY 373 373 373 GLY GLY A . n 
A 1 374 ASN 374 374 374 ASN ASN A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 ALA 376 376 376 ALA ALA A . n 
A 1 377 MET 377 377 377 MET MET A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 HIS 382 382 382 HIS HIS A . n 
A 1 383 PRO 383 383 383 PRO PRO A . n 
A 1 384 ASP 384 384 384 ASP ASP A . n 
A 1 385 ALA 385 385 385 ALA ALA A . n 
A 1 386 VAL 386 386 386 VAL VAL A . n 
A 1 387 ASP 387 387 387 ASP ASP A . n 
A 1 388 ASP 388 388 388 ASP ASP A . n 
A 1 389 TRP 389 389 389 TRP TRP A . n 
A 1 390 TYR 390 390 390 TYR TYR A . n 
A 1 391 MET 391 391 391 MET MET A . n 
A 1 392 VAL 392 392 392 VAL VAL A . n 
A 1 393 VAL 393 393 393 VAL VAL A . n 
A 1 394 PHE 394 394 394 PHE PHE A . n 
A 1 395 ALA 395 395 395 ALA ALA A . n 
A 1 396 ASP 396 396 396 ASP ASP A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 TYR 398 398 398 TYR TYR A . n 
A 1 399 GLU 399 399 399 GLU GLU A . n 
A 1 400 TRP 400 400 400 TRP TRP A . n 
A 1 401 VAL 401 401 401 VAL VAL A . n 
A 1 402 GLU 402 402 402 GLU GLU A . n 
A 1 403 MET 403 403 403 MET MET A . n 
A 1 404 PRO 404 404 404 PRO PRO A . n 
A 1 405 ASN 405 405 405 ASN ASN A . n 
A 1 406 THR 406 406 406 THR THR A . n 
A 1 407 ARG 407 407 407 ARG ARG A . n 
A 1 408 GLY 408 408 408 GLY GLY A . n 
A 1 409 MET 409 409 409 MET MET A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 THR 411 411 411 THR THR A . n 
A 1 412 PHE 412 412 412 PHE PHE A . n 
A 1 413 ALA 413 413 413 ALA ALA A . n 
A 1 414 ASP 414 414 414 ASP ASP A . n 
A 1 415 GLY 415 415 415 GLY GLY A . n 
A 1 416 GLY 416 416 416 GLY GLY A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 VAL 418 418 418 VAL VAL A . n 
A 1 419 GLY 419 419 419 GLY GLY A . n 
A 1 420 SER 420 420 420 SER SER A . n 
A 1 421 LYS 421 421 421 LYS LYS A . n 
A 1 422 PRO 422 422 422 PRO PRO A . n 
A 1 423 TYR 423 423 423 TYR TYR A . n 
A 1 424 ALA 424 424 424 ALA ALA A . n 
A 1 425 ALA 425 425 425 ALA ALA A . n 
A 1 426 SER 426 426 426 SER SER A . n 
A 1 427 GLY 427 427 427 GLY GLY A . n 
A 1 428 ALA 428 428 428 ALA ALA A . n 
A 1 429 TYR 429 429 429 TYR TYR A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 ASP 431 431 431 ASP ASP A . n 
A 1 432 ARG 432 432 432 ARG ARG A . n 
A 1 433 MET 433 433 433 MET MET A . n 
A 1 434 SER 434 434 434 SER SER A . n 
A 1 435 ASP 435 435 435 ASP ASP A . n 
A 1 436 TYR 436 436 436 TYR TYR A . n 
A 1 437 CYS 437 437 437 CYS CYS A . n 
A 1 438 LYS 438 438 438 LYS LYS A . n 
A 1 439 GLY 439 439 439 GLY GLY A . n 
A 1 440 CYS 440 440 440 CYS CYS A . n 
A 1 441 ARG 441 441 441 ARG ARG A . n 
A 1 442 TYR 442 442 442 TYR TYR A . n 
A 1 443 ASP 443 443 443 ASP ASP A . n 
A 1 444 VAL 444 444 444 VAL VAL A . n 
A 1 445 LYS 445 445 445 LYS LYS A . n 
A 1 446 LYS 446 446 446 LYS LYS A . n 
A 1 447 ARG 447 447 447 ARG ARG A . n 
A 1 448 LEU 448 448 448 LEU LEU A . n 
A 1 449 GLY 449 449 449 GLY GLY A . n 
A 1 450 ASP 450 450 450 ASP ASP A . n 
A 1 451 ASP 451 451 451 ASP ASP A . n 
A 1 452 ALA 452 452 452 ALA ALA A . n 
A 1 453 CYS 453 453 453 CYS CYS A . n 
A 1 454 PRO 454 454 454 PRO PRO A . n 
A 1 455 PHE 455 455 455 PHE PHE A . n 
A 1 456 ASN 456 456 456 ASN ASN A . n 
A 1 457 ALA 457 457 457 ALA ALA A . n 
A 1 458 LEU 458 458 458 LEU LEU A . n 
A 1 459 TYR 459 459 459 TYR TYR A . n 
A 1 460 TRP 460 460 460 TRP TRP A . n 
A 1 461 ASP 461 461 461 ASP ASP A . n 
A 1 462 PHE 462 462 462 PHE PHE A . n 
A 1 463 ILE 463 463 463 ILE ILE A . n 
A 1 464 ASP 464 464 464 ASP ASP A . n 
A 1 465 ARG 465 465 465 ARG ARG A . n 
A 1 466 HIS 466 466 466 HIS HIS A . n 
A 1 467 ALA 467 467 467 ALA ALA A . n 
A 1 468 GLN 468 468 468 GLN GLN A . n 
A 1 469 ARG 469 469 469 ARG ARG A . n 
A 1 470 LEU 470 470 470 LEU LEU A . n 
A 1 471 ALA 471 471 471 ALA ALA A . n 
A 1 472 GLY 472 472 472 GLY GLY A . n 
A 1 473 ASN 473 473 473 ASN ASN A . n 
A 1 474 GLY 474 474 474 GLY GLY A . n 
A 1 475 ARG 475 475 475 ARG ARG A . n 
A 1 476 MET 476 476 476 MET MET A . n 
A 1 477 MET 477 477 477 MET MET A . n 
A 1 478 MET 478 478 478 MET MET A . n 
A 1 479 PRO 479 479 479 PRO PRO A . n 
A 1 480 LEU 480 480 480 LEU LEU A . n 
A 1 481 ARG 481 481 481 ARG ARG A . n 
A 1 482 THR 482 482 482 THR THR A . n 
A 1 483 LEU 483 483 483 LEU LEU A . n 
A 1 484 GLU 484 484 484 GLU GLU A . n 
A 1 485 LYS 485 485 485 LYS LYS A . n 
A 1 486 MET 486 486 486 MET MET A . n 
A 1 487 PRO 487 487 487 PRO PRO A . n 
A 1 488 ASP 488 488 488 ASP ASP A . n 
A 1 489 ALA 489 489 489 ALA ALA A . n 
A 1 490 GLU 490 490 490 GLU GLU A . n 
A 1 491 ARG 491 491 491 ARG ARG A . n 
A 1 492 GLU 492 492 492 GLU GLU A . n 
A 1 493 ALA 493 493 493 ALA ALA A . n 
A 1 494 PHE 494 494 494 PHE PHE A . n 
A 1 495 ARG 495 495 495 ARG ARG A . n 
A 1 496 LYS 496 496 496 LYS LYS A . n 
A 1 497 GLN 497 497 497 GLN GLN A . n 
A 1 498 ALA 498 498 498 ALA ALA A . n 
A 1 499 ARG 499 499 499 ARG ARG A . n 
A 1 500 ALA 500 500 500 ALA ALA A . n 
A 1 501 LEU 501 501 501 LEU LEU A . n 
A 1 502 ARG 502 502 502 ARG ARG A . n 
A 1 503 VAL 503 503 503 VAL VAL A . n 
A 1 504 LYS 504 504 504 LYS LYS A . n 
A 1 505 MET 505 505 505 MET MET A . n 
A 1 506 GLY 506 506 506 GLY GLY A . n 
A 1 507 VAL 507 507 507 VAL VAL A . n 
A 1 508 SER 508 508 508 SER SER A . n 
A 1 509 GLY 509 509 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 DLZ ? ? DLZ ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FAD ? ? FAD ? ? 'SUBJECT OF INVESTIGATION' ? 
3 SF4 ? ? SF4 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FAD 1   601  552 FAD FAD A . 
C 3 DLZ 1   602  553 DLZ DLZ A . 
D 4 SF4 1   603  554 SF4 SF4 A . 
E 5 HOH 1   701  315 HOH HOH A . 
E 5 HOH 2   702  306 HOH HOH A . 
E 5 HOH 3   703  200 HOH HOH A . 
E 5 HOH 4   704  241 HOH HOH A . 
E 5 HOH 5   705  224 HOH HOH A . 
E 5 HOH 6   706  238 HOH HOH A . 
E 5 HOH 7   707  206 HOH HOH A . 
E 5 HOH 8   708  317 HOH HOH A . 
E 5 HOH 9   709  218 HOH HOH A . 
E 5 HOH 10  710  142 HOH HOH A . 
E 5 HOH 11  711  33  HOH HOH A . 
E 5 HOH 12  712  157 HOH HOH A . 
E 5 HOH 13  713  215 HOH HOH A . 
E 5 HOH 14  714  236 HOH HOH A . 
E 5 HOH 15  715  37  HOH HOH A . 
E 5 HOH 16  716  275 HOH HOH A . 
E 5 HOH 17  717  156 HOH HOH A . 
E 5 HOH 18  718  96  HOH HOH A . 
E 5 HOH 19  719  234 HOH HOH A . 
E 5 HOH 20  720  86  HOH HOH A . 
E 5 HOH 21  721  35  HOH HOH A . 
E 5 HOH 22  722  61  HOH HOH A . 
E 5 HOH 23  723  141 HOH HOH A . 
E 5 HOH 24  724  273 HOH HOH A . 
E 5 HOH 25  725  180 HOH HOH A . 
E 5 HOH 26  726  93  HOH HOH A . 
E 5 HOH 27  727  98  HOH HOH A . 
E 5 HOH 28  728  43  HOH HOH A . 
E 5 HOH 29  729  125 HOH HOH A . 
E 5 HOH 30  730  113 HOH HOH A . 
E 5 HOH 31  731  190 HOH HOH A . 
E 5 HOH 32  732  193 HOH HOH A . 
E 5 HOH 33  733  122 HOH HOH A . 
E 5 HOH 34  734  228 HOH HOH A . 
E 5 HOH 35  735  7   HOH HOH A . 
E 5 HOH 36  736  149 HOH HOH A . 
E 5 HOH 37  737  17  HOH HOH A . 
E 5 HOH 38  738  60  HOH HOH A . 
E 5 HOH 39  739  164 HOH HOH A . 
E 5 HOH 40  740  115 HOH HOH A . 
E 5 HOH 41  741  24  HOH HOH A . 
E 5 HOH 42  742  128 HOH HOH A . 
E 5 HOH 43  743  16  HOH HOH A . 
E 5 HOH 44  744  186 HOH HOH A . 
E 5 HOH 45  745  283 HOH HOH A . 
E 5 HOH 46  746  127 HOH HOH A . 
E 5 HOH 47  747  10  HOH HOH A . 
E 5 HOH 48  748  229 HOH HOH A . 
E 5 HOH 49  749  152 HOH HOH A . 
E 5 HOH 50  750  226 HOH HOH A . 
E 5 HOH 51  751  13  HOH HOH A . 
E 5 HOH 52  752  58  HOH HOH A . 
E 5 HOH 53  753  267 HOH HOH A . 
E 5 HOH 54  754  19  HOH HOH A . 
E 5 HOH 55  755  124 HOH HOH A . 
E 5 HOH 56  756  15  HOH HOH A . 
E 5 HOH 57  757  65  HOH HOH A . 
E 5 HOH 58  758  49  HOH HOH A . 
E 5 HOH 59  759  45  HOH HOH A . 
E 5 HOH 60  760  3   HOH HOH A . 
E 5 HOH 61  761  9   HOH HOH A . 
E 5 HOH 62  762  211 HOH HOH A . 
E 5 HOH 63  763  255 HOH HOH A . 
E 5 HOH 64  764  4   HOH HOH A . 
E 5 HOH 65  765  297 HOH HOH A . 
E 5 HOH 66  766  137 HOH HOH A . 
E 5 HOH 67  767  83  HOH HOH A . 
E 5 HOH 68  768  301 HOH HOH A . 
E 5 HOH 69  769  160 HOH HOH A . 
E 5 HOH 70  770  108 HOH HOH A . 
E 5 HOH 71  771  181 HOH HOH A . 
E 5 HOH 72  772  27  HOH HOH A . 
E 5 HOH 73  773  135 HOH HOH A . 
E 5 HOH 74  774  1   HOH HOH A . 
E 5 HOH 75  775  117 HOH HOH A . 
E 5 HOH 76  776  22  HOH HOH A . 
E 5 HOH 77  777  79  HOH HOH A . 
E 5 HOH 78  778  70  HOH HOH A . 
E 5 HOH 79  779  140 HOH HOH A . 
E 5 HOH 80  780  30  HOH HOH A . 
E 5 HOH 81  781  112 HOH HOH A . 
E 5 HOH 82  782  153 HOH HOH A . 
E 5 HOH 83  783  12  HOH HOH A . 
E 5 HOH 84  784  41  HOH HOH A . 
E 5 HOH 85  785  184 HOH HOH A . 
E 5 HOH 86  786  42  HOH HOH A . 
E 5 HOH 87  787  5   HOH HOH A . 
E 5 HOH 88  788  34  HOH HOH A . 
E 5 HOH 89  789  144 HOH HOH A . 
E 5 HOH 90  790  146 HOH HOH A . 
E 5 HOH 91  791  38  HOH HOH A . 
E 5 HOH 92  792  147 HOH HOH A . 
E 5 HOH 93  793  97  HOH HOH A . 
E 5 HOH 94  794  231 HOH HOH A . 
E 5 HOH 95  795  223 HOH HOH A . 
E 5 HOH 96  796  39  HOH HOH A . 
E 5 HOH 97  797  175 HOH HOH A . 
E 5 HOH 98  798  14  HOH HOH A . 
E 5 HOH 99  799  21  HOH HOH A . 
E 5 HOH 100 800  54  HOH HOH A . 
E 5 HOH 101 801  167 HOH HOH A . 
E 5 HOH 102 802  136 HOH HOH A . 
E 5 HOH 103 803  171 HOH HOH A . 
E 5 HOH 104 804  230 HOH HOH A . 
E 5 HOH 105 805  6   HOH HOH A . 
E 5 HOH 106 806  219 HOH HOH A . 
E 5 HOH 107 807  111 HOH HOH A . 
E 5 HOH 108 808  57  HOH HOH A . 
E 5 HOH 109 809  256 HOH HOH A . 
E 5 HOH 110 810  279 HOH HOH A . 
E 5 HOH 111 811  92  HOH HOH A . 
E 5 HOH 112 812  36  HOH HOH A . 
E 5 HOH 113 813  130 HOH HOH A . 
E 5 HOH 114 814  185 HOH HOH A . 
E 5 HOH 115 815  240 HOH HOH A . 
E 5 HOH 116 816  195 HOH HOH A . 
E 5 HOH 117 817  303 HOH HOH A . 
E 5 HOH 118 818  188 HOH HOH A . 
E 5 HOH 119 819  101 HOH HOH A . 
E 5 HOH 120 820  32  HOH HOH A . 
E 5 HOH 121 821  2   HOH HOH A . 
E 5 HOH 122 822  31  HOH HOH A . 
E 5 HOH 123 823  316 HOH HOH A . 
E 5 HOH 124 824  270 HOH HOH A . 
E 5 HOH 125 825  258 HOH HOH A . 
E 5 HOH 126 826  191 HOH HOH A . 
E 5 HOH 127 827  121 HOH HOH A . 
E 5 HOH 128 828  51  HOH HOH A . 
E 5 HOH 129 829  189 HOH HOH A . 
E 5 HOH 130 830  276 HOH HOH A . 
E 5 HOH 131 831  29  HOH HOH A . 
E 5 HOH 132 832  40  HOH HOH A . 
E 5 HOH 133 833  134 HOH HOH A . 
E 5 HOH 134 834  138 HOH HOH A . 
E 5 HOH 135 835  159 HOH HOH A . 
E 5 HOH 136 836  187 HOH HOH A . 
E 5 HOH 137 837  94  HOH HOH A . 
E 5 HOH 138 838  302 HOH HOH A . 
E 5 HOH 139 839  177 HOH HOH A . 
E 5 HOH 140 840  132 HOH HOH A . 
E 5 HOH 141 841  158 HOH HOH A . 
E 5 HOH 142 842  67  HOH HOH A . 
E 5 HOH 143 843  263 HOH HOH A . 
E 5 HOH 144 844  87  HOH HOH A . 
E 5 HOH 145 845  103 HOH HOH A . 
E 5 HOH 146 846  183 HOH HOH A . 
E 5 HOH 147 847  151 HOH HOH A . 
E 5 HOH 148 848  126 HOH HOH A . 
E 5 HOH 149 849  172 HOH HOH A . 
E 5 HOH 150 850  265 HOH HOH A . 
E 5 HOH 151 851  254 HOH HOH A . 
E 5 HOH 152 852  129 HOH HOH A . 
E 5 HOH 153 853  207 HOH HOH A . 
E 5 HOH 154 854  208 HOH HOH A . 
E 5 HOH 155 855  259 HOH HOH A . 
E 5 HOH 156 856  74  HOH HOH A . 
E 5 HOH 157 857  252 HOH HOH A . 
E 5 HOH 158 858  47  HOH HOH A . 
E 5 HOH 159 859  222 HOH HOH A . 
E 5 HOH 160 860  262 HOH HOH A . 
E 5 HOH 161 861  46  HOH HOH A . 
E 5 HOH 162 862  25  HOH HOH A . 
E 5 HOH 163 863  131 HOH HOH A . 
E 5 HOH 164 864  309 HOH HOH A . 
E 5 HOH 165 865  28  HOH HOH A . 
E 5 HOH 166 866  11  HOH HOH A . 
E 5 HOH 167 867  245 HOH HOH A . 
E 5 HOH 168 868  299 HOH HOH A . 
E 5 HOH 169 869  18  HOH HOH A . 
E 5 HOH 170 870  268 HOH HOH A . 
E 5 HOH 171 871  288 HOH HOH A . 
E 5 HOH 172 872  26  HOH HOH A . 
E 5 HOH 173 873  8   HOH HOH A . 
E 5 HOH 174 874  310 HOH HOH A . 
E 5 HOH 175 875  178 HOH HOH A . 
E 5 HOH 176 876  107 HOH HOH A . 
E 5 HOH 177 877  289 HOH HOH A . 
E 5 HOH 178 878  165 HOH HOH A . 
E 5 HOH 179 879  179 HOH HOH A . 
E 5 HOH 180 880  75  HOH HOH A . 
E 5 HOH 181 881  50  HOH HOH A . 
E 5 HOH 182 882  213 HOH HOH A . 
E 5 HOH 183 883  55  HOH HOH A . 
E 5 HOH 184 884  133 HOH HOH A . 
E 5 HOH 185 885  91  HOH HOH A . 
E 5 HOH 186 886  192 HOH HOH A . 
E 5 HOH 187 887  209 HOH HOH A . 
E 5 HOH 188 888  99  HOH HOH A . 
E 5 HOH 189 889  319 HOH HOH A . 
E 5 HOH 190 890  287 HOH HOH A . 
E 5 HOH 191 891  150 HOH HOH A . 
E 5 HOH 192 892  78  HOH HOH A . 
E 5 HOH 193 893  264 HOH HOH A . 
E 5 HOH 194 894  182 HOH HOH A . 
E 5 HOH 195 895  89  HOH HOH A . 
E 5 HOH 196 896  205 HOH HOH A . 
E 5 HOH 197 897  194 HOH HOH A . 
E 5 HOH 198 898  300 HOH HOH A . 
E 5 HOH 199 899  20  HOH HOH A . 
E 5 HOH 200 900  169 HOH HOH A . 
E 5 HOH 201 901  68  HOH HOH A . 
E 5 HOH 202 902  106 HOH HOH A . 
E 5 HOH 203 903  305 HOH HOH A . 
E 5 HOH 204 904  203 HOH HOH A . 
E 5 HOH 205 905  148 HOH HOH A . 
E 5 HOH 206 906  90  HOH HOH A . 
E 5 HOH 207 907  155 HOH HOH A . 
E 5 HOH 208 908  81  HOH HOH A . 
E 5 HOH 209 909  269 HOH HOH A . 
E 5 HOH 210 910  71  HOH HOH A . 
E 5 HOH 211 911  221 HOH HOH A . 
E 5 HOH 212 912  154 HOH HOH A . 
E 5 HOH 213 913  77  HOH HOH A . 
E 5 HOH 214 914  76  HOH HOH A . 
E 5 HOH 215 915  246 HOH HOH A . 
E 5 HOH 216 916  63  HOH HOH A . 
E 5 HOH 217 917  274 HOH HOH A . 
E 5 HOH 218 918  64  HOH HOH A . 
E 5 HOH 219 919  272 HOH HOH A . 
E 5 HOH 220 920  232 HOH HOH A . 
E 5 HOH 221 921  105 HOH HOH A . 
E 5 HOH 222 922  313 HOH HOH A . 
E 5 HOH 223 923  307 HOH HOH A . 
E 5 HOH 224 924  23  HOH HOH A . 
E 5 HOH 225 925  44  HOH HOH A . 
E 5 HOH 226 926  109 HOH HOH A . 
E 5 HOH 227 927  217 HOH HOH A . 
E 5 HOH 228 928  322 HOH HOH A . 
E 5 HOH 229 929  239 HOH HOH A . 
E 5 HOH 230 930  286 HOH HOH A . 
E 5 HOH 231 931  294 HOH HOH A . 
E 5 HOH 232 932  210 HOH HOH A . 
E 5 HOH 233 933  73  HOH HOH A . 
E 5 HOH 234 934  312 HOH HOH A . 
E 5 HOH 235 935  59  HOH HOH A . 
E 5 HOH 236 936  233 HOH HOH A . 
E 5 HOH 237 937  69  HOH HOH A . 
E 5 HOH 238 938  62  HOH HOH A . 
E 5 HOH 239 939  249 HOH HOH A . 
E 5 HOH 240 940  244 HOH HOH A . 
E 5 HOH 241 941  227 HOH HOH A . 
E 5 HOH 242 942  243 HOH HOH A . 
E 5 HOH 243 943  321 HOH HOH A . 
E 5 HOH 244 944  143 HOH HOH A . 
E 5 HOH 245 945  196 HOH HOH A . 
E 5 HOH 246 946  88  HOH HOH A . 
E 5 HOH 247 947  202 HOH HOH A . 
E 5 HOH 248 948  235 HOH HOH A . 
E 5 HOH 249 949  85  HOH HOH A . 
E 5 HOH 250 950  162 HOH HOH A . 
E 5 HOH 251 951  173 HOH HOH A . 
E 5 HOH 252 952  204 HOH HOH A . 
E 5 HOH 253 953  280 HOH HOH A . 
E 5 HOH 254 954  48  HOH HOH A . 
E 5 HOH 255 955  174 HOH HOH A . 
E 5 HOH 256 956  116 HOH HOH A . 
E 5 HOH 257 957  295 HOH HOH A . 
E 5 HOH 258 958  56  HOH HOH A . 
E 5 HOH 259 959  84  HOH HOH A . 
E 5 HOH 260 960  282 HOH HOH A . 
E 5 HOH 261 961  251 HOH HOH A . 
E 5 HOH 262 962  293 HOH HOH A . 
E 5 HOH 263 963  271 HOH HOH A . 
E 5 HOH 264 964  72  HOH HOH A . 
E 5 HOH 265 965  253 HOH HOH A . 
E 5 HOH 266 966  220 HOH HOH A . 
E 5 HOH 267 967  80  HOH HOH A . 
E 5 HOH 268 968  311 HOH HOH A . 
E 5 HOH 269 969  82  HOH HOH A . 
E 5 HOH 270 970  110 HOH HOH A . 
E 5 HOH 271 971  260 HOH HOH A . 
E 5 HOH 272 972  214 HOH HOH A . 
E 5 HOH 273 973  163 HOH HOH A . 
E 5 HOH 274 974  308 HOH HOH A . 
E 5 HOH 275 975  292 HOH HOH A . 
E 5 HOH 276 976  168 HOH HOH A . 
E 5 HOH 277 977  197 HOH HOH A . 
E 5 HOH 278 978  100 HOH HOH A . 
E 5 HOH 279 979  281 HOH HOH A . 
E 5 HOH 280 980  199 HOH HOH A . 
E 5 HOH 281 981  278 HOH HOH A . 
E 5 HOH 282 982  237 HOH HOH A . 
E 5 HOH 283 983  296 HOH HOH A . 
E 5 HOH 284 984  314 HOH HOH A . 
E 5 HOH 285 985  66  HOH HOH A . 
E 5 HOH 286 986  257 HOH HOH A . 
E 5 HOH 287 987  53  HOH HOH A . 
E 5 HOH 288 988  119 HOH HOH A . 
E 5 HOH 289 989  102 HOH HOH A . 
E 5 HOH 290 990  118 HOH HOH A . 
E 5 HOH 291 991  261 HOH HOH A . 
E 5 HOH 292 992  290 HOH HOH A . 
E 5 HOH 293 993  170 HOH HOH A . 
E 5 HOH 294 994  176 HOH HOH A . 
E 5 HOH 295 995  166 HOH HOH A . 
E 5 HOH 296 996  320 HOH HOH A . 
E 5 HOH 297 997  248 HOH HOH A . 
E 5 HOH 298 998  201 HOH HOH A . 
E 5 HOH 299 999  145 HOH HOH A . 
E 5 HOH 300 1000 52  HOH HOH A . 
E 5 HOH 301 1001 123 HOH HOH A . 
E 5 HOH 302 1002 242 HOH HOH A . 
E 5 HOH 303 1003 198 HOH HOH A . 
E 5 HOH 304 1004 285 HOH HOH A . 
E 5 HOH 305 1005 216 HOH HOH A . 
E 5 HOH 306 1006 161 HOH HOH A . 
E 5 HOH 307 1007 284 HOH HOH A . 
E 5 HOH 308 1008 212 HOH HOH A . 
E 5 HOH 309 1009 120 HOH HOH A . 
E 5 HOH 310 1010 266 HOH HOH A . 
E 5 HOH 311 1011 247 HOH HOH A . 
E 5 HOH 312 1012 104 HOH HOH A . 
E 5 HOH 313 1013 277 HOH HOH A . 
E 5 HOH 314 1014 250 HOH HOH A . 
E 5 HOH 315 1015 114 HOH HOH A . 
E 5 HOH 316 1016 304 HOH HOH A . 
E 5 HOH 317 1017 225 HOH HOH A . 
E 5 HOH 318 1018 139 HOH HOH A . 
E 5 HOH 319 1019 95  HOH HOH A . 
E 5 HOH 320 1020 291 HOH HOH A . 
E 5 HOH 321 1021 318 HOH HOH A . 
E 5 HOH 322 1022 298 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 0 A GLU 76  ? CD ? A GLU 76  CD 
2 1 Y 0 A GLU 151 ? CD ? A GLU 151 CD 
3 1 Y 0 A GLU 492 ? CD ? A GLU 492 CD 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HNL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.347 
_cell.length_a_esd                 ? 
_cell.length_b                     102.677 
_cell.length_b_esd                 ? 
_cell.length_c                     103.539 
_cell.length_c_esd                 ? 
_cell.volume                       524611.604 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9HNL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9HNL 
_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             2.26 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.49 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.1 M Tris (pH 8.5)
0.2 M MgCl2
20% (w/v) PEG3350
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-03-26 
_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                    mirror 
_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                        'NSRRC BEAMLINE TPS 05A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'TPS 05A' 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate                          26.75 
_reflns.entry_id                                       9HNL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.2 
_reflns.d_resolution_low                               45.99 
_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                                     27390 
_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                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.5 
_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                              0.2 
_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                                    2.2 
_reflns_shell.d_res_low                                     2.28 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.89 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2689 
_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                                  0.524 
_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                                  1.065 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.31 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9HNL 
_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                            2.20 
_refine.ls_d_res_low                             45.99 
_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                     27335 
_refine.ls_number_reflns_R_free                  1322 
_refine.ls_number_reflns_R_work                  26013 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.59 
_refine.ls_percent_reflns_R_free                 4.84 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1953 
_refine.ls_R_factor_R_free                       0.2375 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1932 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 22.0819 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2360 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        45.99 
_refine_hist.number_atoms_solvent             322 
_refine_hist.number_atoms_total               4484 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4078 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0022 ? 4295 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5298 ? 5835 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0380 ? 596  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0042 ? 756  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 7.9774 ? 583  ? f_dihedral_angle_d ? ? 
# 
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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 2.20 2.29  . . 130 2856 99.97  . . . . 0.2584 . . . . . . . . . . . . . . . 0.2851 
'X-RAY DIFFRACTION' 2.29 2.39  . . 159 2837 99.97  . . . . 0.2467 . . . . . . . . . . . . . . . 0.2918 
'X-RAY DIFFRACTION' 2.39 2.52  . . 152 2845 99.97  . . . . 0.2327 . . . . . . . . . . . . . . . 0.3001 
'X-RAY DIFFRACTION' 2.52 2.68  . . 149 2856 99.97  . . . . 0.2276 . . . . . . . . . . . . . . . 0.2717 
'X-RAY DIFFRACTION' 2.68 2.88  . . 164 2872 100.00 . . . . 0.2195 . . . . . . . . . . . . . . . 0.2458 
'X-RAY DIFFRACTION' 2.88 3.17  . . 133 2891 99.83  . . . . 0.2021 . . . . . . . . . . . . . . . 0.2279 
'X-RAY DIFFRACTION' 3.17 3.63  . . 132 2908 99.80  . . . . 0.1802 . . . . . . . . . . . . . . . 0.2305 
'X-RAY DIFFRACTION' 3.63 4.57  . . 150 2940 99.48  . . . . 0.1511 . . . . . . . . . . . . . . . 0.2083 
'X-RAY DIFFRACTION' 4.58 45.99 . . 153 3008 97.53  . . . . 0.1716 . . . . . . . . . . . . . . . 0.2087 
# 
_struct.entry_id                     9HNL 
_struct.title                        
'Structure of the (6-4) photolyase of Caulobacter crescentus in its oxidized state at room temperture-synchrotron' 
_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        9HNL 
_struct_keywords.text            'DNA repair, photolyase, electron transfer, iron-sulfur cluster, 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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9AAF5_CAUVC 
_struct_ref.pdbx_db_accession          Q9AAF5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAGALRLVLGDQLSDNLSALVDADLSRDQVLMVESRVEATAWKHHKQKLVLVWSAMRQFAERLRARGFNVRYVTLEDPDN
TGSIGGELRRALEARAFDRVIRTACGKWGLESHLLSLDLPVPMETREDDRFLCSRAQFAAWAEGRRELRMEFFYREMRRK
TGLLMDGDQPAGGRWNFDAENRRKLPPGLRPPERLRIPPNPTTQTVLEQVSRGFDDHFGEVEGFGWPTNPDEATAILDHF
IADMLPSFGDWQDAMSWRRPFLWHSLISPALNIGLLDPLDICRRAEAAWREGRAPLNAVEGFIRQIIGWREFVRGIYWLK
MPEYAQRNALDAQGKLPGFYWTGQTDMACVADTVRAAHDHAYAHHIQRLMVTGNLAMLLGVHPDAVDDWYMVVFADAYEW
VEMPNTRGMATFADGGIVGSKPYAASGAYIDRMSDYCKGCRYDVKKRLGDDACPFNALYWDFIDRHAQRLAGNGRMMMPL
RTLEKMPDAEREAFRKQARALRVKMGVSG
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9HNL 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 509 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9AAF5 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  509 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       509 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1590  ? 
1 MORE         -28   ? 
1 'SSA (A^2)'  20510 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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 LEU A 17  ? VAL A 21  ? LEU A 17  VAL A 21  5 ? 5  
HELX_P HELX_P2  AA2 SER A 35  ? TRP A 42  ? SER A 35  TRP A 42  1 ? 8  
HELX_P HELX_P3  AA3 HIS A 45  ? ARG A 66  ? HIS A 45  ARG A 66  1 ? 22 
HELX_P HELX_P4  AA4 SER A 83  ? ARG A 95  ? SER A 83  ARG A 95  1 ? 13 
HELX_P HELX_P5  AA5 LYS A 107 ? SER A 116 ? LYS A 107 SER A 116 1 ? 10 
HELX_P HELX_P6  AA6 SER A 134 ? GLU A 143 ? SER A 134 GLU A 143 1 ? 10 
HELX_P HELX_P7  AA7 ARG A 149 ? GLY A 162 ? ARG A 149 GLY A 162 1 ? 14 
HELX_P HELX_P8  AA8 GLY A 172 ? ARG A 174 ? GLY A 172 ARG A 174 5 ? 3  
HELX_P HELX_P9  AA9 ASN A 200 ? PHE A 214 ? ASN A 200 PHE A 214 1 ? 15 
HELX_P HELX_P10 AB1 ASN A 229 ? MET A 244 ? ASN A 229 MET A 244 1 ? 16 
HELX_P HELX_P11 AB2 LEU A 245 ? PHE A 248 ? LEU A 245 PHE A 248 5 ? 4  
HELX_P HELX_P12 AB3 ILE A 267 ? ASN A 272 ? ILE A 267 ASN A 272 1 ? 6  
HELX_P HELX_P13 AB4 ASP A 277 ? GLU A 291 ? ASP A 277 GLU A 291 1 ? 15 
HELX_P HELX_P14 AB5 PRO A 295 ? GLY A 308 ? PRO A 295 GLY A 308 1 ? 14 
HELX_P HELX_P15 AB6 GLY A 308 ? MET A 321 ? GLY A 308 MET A 321 1 ? 14 
HELX_P HELX_P16 AB7 PRO A 322 ? ARG A 327 ? PRO A 322 ARG A 327 5 ? 6  
HELX_P HELX_P17 AB8 GLY A 338 ? GLY A 343 ? GLY A 338 GLY A 343 1 ? 6  
HELX_P HELX_P18 AB9 MET A 347 ? ALA A 361 ? MET A 347 ALA A 361 1 ? 15 
HELX_P HELX_P19 AC1 HIS A 364 ? VAL A 371 ? HIS A 364 VAL A 371 1 ? 8  
HELX_P HELX_P20 AC2 VAL A 371 ? GLY A 380 ? VAL A 371 GLY A 380 1 ? 10 
HELX_P HELX_P21 AC3 HIS A 382 ? PHE A 394 ? HIS A 382 PHE A 394 1 ? 13 
HELX_P HELX_P22 AC4 TYR A 398 ? ARG A 407 ? TYR A 398 ARG A 407 1 ? 10 
HELX_P HELX_P23 AC5 SER A 426 ? SER A 434 ? SER A 426 SER A 434 1 ? 9  
HELX_P HELX_P24 AC6 CYS A 453 ? HIS A 466 ? CYS A 453 HIS A 466 1 ? 14 
HELX_P HELX_P25 AC7 HIS A 466 ? GLY A 474 ? HIS A 466 GLY A 474 1 ? 9  
HELX_P HELX_P26 AC8 MET A 476 ? LYS A 485 ? MET A 476 LYS A 485 1 ? 10 
HELX_P HELX_P27 AC9 PRO A 487 ? MET A 505 ? PRO A 487 MET A 505 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 349 SG ? ? ? 1_555 D SF4 . FE3 ? ? A CYS 349 A SF4 603 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc2 metalc ? ? A CYS 437 SG ? ? ? 1_555 D SF4 . FE1 ? ? A CYS 437 A SF4 603 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc3 metalc ? ? A CYS 440 SG ? ? ? 1_555 D SF4 . FE4 ? ? A CYS 440 A SF4 603 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc4 metalc ? ? A CYS 453 SG ? ? ? 1_555 D SF4 . FE2 ? ? A CYS 453 A SF4 603 1_555 ? ? ? ? ? ? ? 2.269 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 349 ? A CYS 349 ? 1_555 FE3 ? D SF4 . ? A SF4 603 ? 1_555 S1 ? D SF4 . ? A SF4 603 ? 1_555 115.2 ? 
2  SG ? A CYS 349 ? A CYS 349 ? 1_555 FE3 ? D SF4 . ? A SF4 603 ? 1_555 S2 ? D SF4 . ? A SF4 603 ? 1_555 110.8 ? 
3  S1 ? D SF4 .   ? A SF4 603 ? 1_555 FE3 ? D SF4 . ? A SF4 603 ? 1_555 S2 ? D SF4 . ? A SF4 603 ? 1_555 104.0 ? 
4  SG ? A CYS 349 ? A CYS 349 ? 1_555 FE3 ? D SF4 . ? A SF4 603 ? 1_555 S4 ? D SF4 . ? A SF4 603 ? 1_555 117.1 ? 
5  S1 ? D SF4 .   ? A SF4 603 ? 1_555 FE3 ? D SF4 . ? A SF4 603 ? 1_555 S4 ? D SF4 . ? A SF4 603 ? 1_555 104.1 ? 
6  S2 ? D SF4 .   ? A SF4 603 ? 1_555 FE3 ? D SF4 . ? A SF4 603 ? 1_555 S4 ? D SF4 . ? A SF4 603 ? 1_555 104.3 ? 
7  SG ? A CYS 437 ? A CYS 437 ? 1_555 FE1 ? D SF4 . ? A SF4 603 ? 1_555 S2 ? D SF4 . ? A SF4 603 ? 1_555 117.6 ? 
8  SG ? A CYS 437 ? A CYS 437 ? 1_555 FE1 ? D SF4 . ? A SF4 603 ? 1_555 S3 ? D SF4 . ? A SF4 603 ? 1_555 112.0 ? 
9  S2 ? D SF4 .   ? A SF4 603 ? 1_555 FE1 ? D SF4 . ? A SF4 603 ? 1_555 S3 ? D SF4 . ? A SF4 603 ? 1_555 104.1 ? 
10 SG ? A CYS 437 ? A CYS 437 ? 1_555 FE1 ? D SF4 . ? A SF4 603 ? 1_555 S4 ? D SF4 . ? A SF4 603 ? 1_555 113.5 ? 
11 S2 ? D SF4 .   ? A SF4 603 ? 1_555 FE1 ? D SF4 . ? A SF4 603 ? 1_555 S4 ? D SF4 . ? A SF4 603 ? 1_555 104.1 ? 
12 S3 ? D SF4 .   ? A SF4 603 ? 1_555 FE1 ? D SF4 . ? A SF4 603 ? 1_555 S4 ? D SF4 . ? A SF4 603 ? 1_555 104.2 ? 
13 SG ? A CYS 440 ? A CYS 440 ? 1_555 FE4 ? D SF4 . ? A SF4 603 ? 1_555 S1 ? D SF4 . ? A SF4 603 ? 1_555 116.4 ? 
14 SG ? A CYS 440 ? A CYS 440 ? 1_555 FE4 ? D SF4 . ? A SF4 603 ? 1_555 S2 ? D SF4 . ? A SF4 603 ? 1_555 111.0 ? 
15 S1 ? D SF4 .   ? A SF4 603 ? 1_555 FE4 ? D SF4 . ? A SF4 603 ? 1_555 S2 ? D SF4 . ? A SF4 603 ? 1_555 104.1 ? 
16 SG ? A CYS 440 ? A CYS 440 ? 1_555 FE4 ? D SF4 . ? A SF4 603 ? 1_555 S3 ? D SF4 . ? A SF4 603 ? 1_555 115.9 ? 
17 S1 ? D SF4 .   ? A SF4 603 ? 1_555 FE4 ? D SF4 . ? A SF4 603 ? 1_555 S3 ? D SF4 . ? A SF4 603 ? 1_555 104.0 ? 
18 S2 ? D SF4 .   ? A SF4 603 ? 1_555 FE4 ? D SF4 . ? A SF4 603 ? 1_555 S3 ? D SF4 . ? A SF4 603 ? 1_555 104.1 ? 
19 SG ? A CYS 453 ? A CYS 453 ? 1_555 FE2 ? D SF4 . ? A SF4 603 ? 1_555 S1 ? D SF4 . ? A SF4 603 ? 1_555 122.1 ? 
20 SG ? A CYS 453 ? A CYS 453 ? 1_555 FE2 ? D SF4 . ? A SF4 603 ? 1_555 S3 ? D SF4 . ? A SF4 603 ? 1_555 113.1 ? 
21 S1 ? D SF4 .   ? A SF4 603 ? 1_555 FE2 ? D SF4 . ? A SF4 603 ? 1_555 S3 ? D SF4 . ? A SF4 603 ? 1_555 104.0 ? 
22 SG ? A CYS 453 ? A CYS 453 ? 1_555 FE2 ? D SF4 . ? A SF4 603 ? 1_555 S4 ? D SF4 . ? A SF4 603 ? 1_555 107.5 ? 
23 S1 ? D SF4 .   ? A SF4 603 ? 1_555 FE2 ? D SF4 . ? A SF4 603 ? 1_555 S4 ? D SF4 . ? A SF4 603 ? 1_555 104.1 ? 
24 S3 ? D SF4 .   ? A SF4 603 ? 1_555 FE2 ? D SF4 . ? A SF4 603 ? 1_555 S4 ? D SF4 . ? A SF4 603 ? 1_555 104.3 ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          MET 
_struct_mon_prot_cis.label_seq_id           321 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           MET 
_struct_mon_prot_cis.auth_seq_id            321 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    322 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     322 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       3.30 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 70  ? VAL A 73  ? VAL A 70  VAL A 73  
AA1 2 GLN A 29  ? VAL A 33  ? GLN A 29  VAL A 33  
AA1 3 ALA A 4   ? LEU A 7   ? ALA A 4   LEU A 7   
AA1 4 ARG A 99  ? THR A 103 ? ARG A 99  THR A 103 
AA1 5 MET A 123 ? ARG A 126 ? MET A 123 ARG A 126 
AA2 1 MET A 165 ? ASP A 166 ? MET A 165 ASP A 166 
AA2 2 GLN A 169 ? PRO A 170 ? GLN A 169 PRO A 170 
# 
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 ARG A 71  ? O ARG A 71  N VAL A 30  ? N VAL A 30  
AA1 2 3 O GLN A 29  ? O GLN A 29  N ARG A 6   ? N ARG A 6   
AA1 3 4 N LEU A 5   ? N LEU A 5   O ILE A 101 ? O ILE A 101 
AA1 4 5 N VAL A 100 ? N VAL A 100 O GLU A 124 ? O GLU A 124 
AA2 1 2 N ASP A 166 ? N ASP A 166 O GLN A 169 ? O GLN A 169 
# 
_pdbx_entry_details.entry_id                   9HNL 
_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   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NZ A LYS 43  ? ? OD2 A ASP 216 ? ? 2.08 
2 1 O  A HOH 708 ? ? O   A HOH 726 ? ? 2.15 
# 
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 GLU A 180 ? ? -69.79  -171.42 
2 1 LEU A 262 ? ? 53.81   -125.59 
3 1 VAL A 371 ? ? -103.32 -77.90  
4 1 THR A 406 ? ? -97.31  -61.12  
5 1 SER A 420 ? ? 68.05   -14.50  
6 1 TYR A 423 ? ? -96.28  47.04   
7 1 VAL A 507 ? ? -94.56  -62.54  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 10.1613756885  14.8492828552  32.4237502428 0.23463243136  ? -0.00925566804398 ? -0.0117250214201 
? 0.193615651676 ? 0.0301841188014   ? 0.181998528232 ? 1.10808468907  ? -0.0730729286731 ? -0.0352201419347 ? 1.07480887752 ? 
0.519320780862 ? 1.12941082301  ? -0.00633683994571  ? -0.107874958292 ? 0.0866494002733   ? 0.1189548687     ? 0.0385226390326  ? 
-0.124378988619   ? -0.023526239947  ? 0.107534754156    ? -0.016979745377 ? 
2 'X-RAY DIFFRACTION' ? refined -2.12549161189 -7.07517783624 14.3337958987 0.284837877406 ? -0.0590135265157  ? 0.0763294953176  
? 0.245544960799 ? -0.0185003410873  ? 0.323496060617 ? 1.88994153157  ? -0.716356018784  ? -0.0775267654054 ? 1.29899388369 ? 
0.173915261816 ? 0.656189466755 ? -0.000935937026025 ? 0.263609683546  ? -0.300071659126   ? -0.0929540940954 ? -0.0901931814703 ? 
0.179035556644    ? 0.200456637519   ? -0.0749958447301  ? 0.138684936431  ? 
3 'X-RAY DIFFRACTION' ? refined -1.15413651895 9.49570987898  8.66144915609 0.137498859864 ? -0.0108273593476  ? -0.0109724276883 
? 0.175601609794 ? -0.00405499994341 ? 0.136757299911 ? 0.864131172161 ? 0.0143301282119  ? 0.0735103661021  ? 1.25302176347 ? 
-0.40830403398 ? 1.18127349867  ? -0.0408903354557   ? 0.193830646121  ? -0.00401825456709 ? -0.159243584088  ? 0.00132377176912 ? 
-0.00132376220911 ? 0.00776114699302 ? -0.00386765147004 ? 0.0438142400026 ? 
# 
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 A 1   A 1   ? A 161 A 161 ? ? 
;chain 'A' and (resid 1 through 161 )
;
2 'X-RAY DIFFRACTION' 2 A 162 A 162 ? A 200 A 200 ? ? 
;chain 'A' and (resid 162 through 200 )
;
3 'X-RAY DIFFRACTION' 3 A 201 A 201 ? A 508 A 508 ? ? 
;chain 'A' and (resid 201 through 508 )
;
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     GLY 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      509 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    GLY 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     509 
# 
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  
DLZ C7     C  N N 88  
DLZ C7A    C  N N 89  
DLZ C5A    C  N N 90  
DLZ C6     C  N N 91  
DLZ N5     N  N N 92  
DLZ C4A    C  N N 93  
DLZ C4     C  N N 94  
DLZ O4     O  N N 95  
DLZ N3     N  N N 96  
DLZ C2     C  N N 97  
DLZ O2     O  N N 98  
DLZ N1     N  N N 99  
DLZ C8     C  N N 100 
DLZ N8     N  N N 101 
DLZ "C1'"  C  N N 102 
DLZ "C2'"  C  N S 103 
DLZ "O2'"  O  N N 104 
DLZ "C3'"  C  N S 105 
DLZ "O3'"  O  N N 106 
DLZ "C4'"  C  N R 107 
DLZ "O4'"  O  N N 108 
DLZ "C5'"  C  N N 109 
DLZ "O5'"  O  N N 110 
DLZ H7     H  N N 111 
DLZ H7A    H  N N 112 
DLZ H7B    H  N N 113 
DLZ H6     H  N N 114 
DLZ H6A    H  N N 115 
DLZ H6B    H  N N 116 
DLZ HN3    H  N N 117 
DLZ "H1'"  H  N N 118 
DLZ "H1'A" H  N N 119 
DLZ "H2'"  H  N N 120 
DLZ "HO2'" H  N N 121 
DLZ "H3'"  H  N N 122 
DLZ "HO3'" H  N N 123 
DLZ "H4'"  H  N N 124 
DLZ "HO4'" H  N N 125 
DLZ "H5'"  H  N N 126 
DLZ "H5'A" H  N N 127 
DLZ "HO5'" H  N N 128 
FAD PA     P  N R 129 
FAD O1A    O  N N 130 
FAD O2A    O  N N 131 
FAD O5B    O  N N 132 
FAD C5B    C  N N 133 
FAD C4B    C  N R 134 
FAD O4B    O  N N 135 
FAD C3B    C  N S 136 
FAD O3B    O  N N 137 
FAD C2B    C  N R 138 
FAD O2B    O  N N 139 
FAD C1B    C  N R 140 
FAD N9A    N  Y N 141 
FAD C8A    C  Y N 142 
FAD N7A    N  Y N 143 
FAD C5A    C  Y N 144 
FAD C6A    C  Y N 145 
FAD N6A    N  N N 146 
FAD N1A    N  Y N 147 
FAD C2A    C  Y N 148 
FAD N3A    N  Y N 149 
FAD C4A    C  Y N 150 
FAD N1     N  N N 151 
FAD C2     C  N N 152 
FAD O2     O  N N 153 
FAD N3     N  N N 154 
FAD C4     C  N N 155 
FAD O4     O  N N 156 
FAD C4X    C  N N 157 
FAD N5     N  N N 158 
FAD C5X    C  Y N 159 
FAD C6     C  Y N 160 
FAD C7     C  Y N 161 
FAD C7M    C  N N 162 
FAD C8     C  Y N 163 
FAD C8M    C  N N 164 
FAD C9     C  Y N 165 
FAD C9A    C  Y N 166 
FAD N10    N  N N 167 
FAD C10    C  N N 168 
FAD "C1'"  C  N N 169 
FAD "C2'"  C  N S 170 
FAD "O2'"  O  N N 171 
FAD "C3'"  C  N S 172 
FAD "O3'"  O  N N 173 
FAD "C4'"  C  N R 174 
FAD "O4'"  O  N N 175 
FAD "C5'"  C  N N 176 
FAD "O5'"  O  N N 177 
FAD P      P  N R 178 
FAD O1P    O  N N 179 
FAD O2P    O  N N 180 
FAD O3P    O  N N 181 
FAD HOA2   H  N N 182 
FAD H51A   H  N N 183 
FAD H52A   H  N N 184 
FAD H4B    H  N N 185 
FAD H3B    H  N N 186 
FAD HO3A   H  N N 187 
FAD H2B    H  N N 188 
FAD HO2A   H  N N 189 
FAD H1B    H  N N 190 
FAD H8A    H  N N 191 
FAD H61A   H  N N 192 
FAD H62A   H  N N 193 
FAD H2A    H  N N 194 
FAD HN3    H  N N 195 
FAD H6     H  N N 196 
FAD HM71   H  N N 197 
FAD HM72   H  N N 198 
FAD HM73   H  N N 199 
FAD HM81   H  N N 200 
FAD HM82   H  N N 201 
FAD HM83   H  N N 202 
FAD H9     H  N N 203 
FAD "H1'1" H  N N 204 
FAD "H1'2" H  N N 205 
FAD "H2'"  H  N N 206 
FAD "HO2'" H  N N 207 
FAD "H3'"  H  N N 208 
FAD "HO3'" H  N N 209 
FAD "H4'"  H  N N 210 
FAD "HO4'" H  N N 211 
FAD "H5'1" H  N N 212 
FAD "H5'2" H  N N 213 
FAD HOP2   H  N N 214 
GLN N      N  N N 215 
GLN CA     C  N S 216 
GLN C      C  N N 217 
GLN O      O  N N 218 
GLN CB     C  N N 219 
GLN CG     C  N N 220 
GLN CD     C  N N 221 
GLN OE1    O  N N 222 
GLN NE2    N  N N 223 
GLN OXT    O  N N 224 
GLN H      H  N N 225 
GLN H2     H  N N 226 
GLN HA     H  N N 227 
GLN HB2    H  N N 228 
GLN HB3    H  N N 229 
GLN HG2    H  N N 230 
GLN HG3    H  N N 231 
GLN HE21   H  N N 232 
GLN HE22   H  N N 233 
GLN HXT    H  N N 234 
GLU N      N  N N 235 
GLU CA     C  N S 236 
GLU C      C  N N 237 
GLU O      O  N N 238 
GLU CB     C  N N 239 
GLU CG     C  N N 240 
GLU CD     C  N N 241 
GLU OE1    O  N N 242 
GLU OE2    O  N N 243 
GLU OXT    O  N N 244 
GLU H      H  N N 245 
GLU H2     H  N N 246 
GLU HA     H  N N 247 
GLU HB2    H  N N 248 
GLU HB3    H  N N 249 
GLU HG2    H  N N 250 
GLU HG3    H  N N 251 
GLU HE2    H  N N 252 
GLU HXT    H  N N 253 
GLY N      N  N N 254 
GLY CA     C  N N 255 
GLY C      C  N N 256 
GLY O      O  N N 257 
GLY OXT    O  N N 258 
GLY H      H  N N 259 
GLY H2     H  N N 260 
GLY HA2    H  N N 261 
GLY HA3    H  N N 262 
GLY HXT    H  N N 263 
HIS N      N  N N 264 
HIS CA     C  N S 265 
HIS C      C  N N 266 
HIS O      O  N N 267 
HIS CB     C  N N 268 
HIS CG     C  Y N 269 
HIS ND1    N  Y N 270 
HIS CD2    C  Y N 271 
HIS CE1    C  Y N 272 
HIS NE2    N  Y N 273 
HIS OXT    O  N N 274 
HIS H      H  N N 275 
HIS H2     H  N N 276 
HIS HA     H  N N 277 
HIS HB2    H  N N 278 
HIS HB3    H  N N 279 
HIS HD1    H  N N 280 
HIS HD2    H  N N 281 
HIS HE1    H  N N 282 
HIS HE2    H  N N 283 
HIS HXT    H  N N 284 
HOH O      O  N N 285 
HOH H1     H  N N 286 
HOH H2     H  N N 287 
ILE N      N  N N 288 
ILE CA     C  N S 289 
ILE C      C  N N 290 
ILE O      O  N N 291 
ILE CB     C  N S 292 
ILE CG1    C  N N 293 
ILE CG2    C  N N 294 
ILE CD1    C  N N 295 
ILE OXT    O  N N 296 
ILE H      H  N N 297 
ILE H2     H  N N 298 
ILE HA     H  N N 299 
ILE HB     H  N N 300 
ILE HG12   H  N N 301 
ILE HG13   H  N N 302 
ILE HG21   H  N N 303 
ILE HG22   H  N N 304 
ILE HG23   H  N N 305 
ILE HD11   H  N N 306 
ILE HD12   H  N N 307 
ILE HD13   H  N N 308 
ILE HXT    H  N N 309 
LEU N      N  N N 310 
LEU CA     C  N S 311 
LEU C      C  N N 312 
LEU O      O  N N 313 
LEU CB     C  N N 314 
LEU CG     C  N N 315 
LEU CD1    C  N N 316 
LEU CD2    C  N N 317 
LEU OXT    O  N N 318 
LEU H      H  N N 319 
LEU H2     H  N N 320 
LEU HA     H  N N 321 
LEU HB2    H  N N 322 
LEU HB3    H  N N 323 
LEU HG     H  N N 324 
LEU HD11   H  N N 325 
LEU HD12   H  N N 326 
LEU HD13   H  N N 327 
LEU HD21   H  N N 328 
LEU HD22   H  N N 329 
LEU HD23   H  N N 330 
LEU HXT    H  N N 331 
LYS N      N  N N 332 
LYS CA     C  N S 333 
LYS C      C  N N 334 
LYS O      O  N N 335 
LYS CB     C  N N 336 
LYS CG     C  N N 337 
LYS CD     C  N N 338 
LYS CE     C  N N 339 
LYS NZ     N  N N 340 
LYS OXT    O  N N 341 
LYS H      H  N N 342 
LYS H2     H  N N 343 
LYS HA     H  N N 344 
LYS HB2    H  N N 345 
LYS HB3    H  N N 346 
LYS HG2    H  N N 347 
LYS HG3    H  N N 348 
LYS HD2    H  N N 349 
LYS HD3    H  N N 350 
LYS HE2    H  N N 351 
LYS HE3    H  N N 352 
LYS HZ1    H  N N 353 
LYS HZ2    H  N N 354 
LYS HZ3    H  N N 355 
LYS HXT    H  N N 356 
MET N      N  N N 357 
MET CA     C  N S 358 
MET C      C  N N 359 
MET O      O  N N 360 
MET CB     C  N N 361 
MET CG     C  N N 362 
MET SD     S  N N 363 
MET CE     C  N N 364 
MET OXT    O  N N 365 
MET H      H  N N 366 
MET H2     H  N N 367 
MET HA     H  N N 368 
MET HB2    H  N N 369 
MET HB3    H  N N 370 
MET HG2    H  N N 371 
MET HG3    H  N N 372 
MET HE1    H  N N 373 
MET HE2    H  N N 374 
MET HE3    H  N N 375 
MET HXT    H  N N 376 
PHE N      N  N N 377 
PHE CA     C  N S 378 
PHE C      C  N N 379 
PHE O      O  N N 380 
PHE CB     C  N N 381 
PHE CG     C  Y N 382 
PHE CD1    C  Y N 383 
PHE CD2    C  Y N 384 
PHE CE1    C  Y N 385 
PHE CE2    C  Y N 386 
PHE CZ     C  Y N 387 
PHE OXT    O  N N 388 
PHE H      H  N N 389 
PHE H2     H  N N 390 
PHE HA     H  N N 391 
PHE HB2    H  N N 392 
PHE HB3    H  N N 393 
PHE HD1    H  N N 394 
PHE HD2    H  N N 395 
PHE HE1    H  N N 396 
PHE HE2    H  N N 397 
PHE HZ     H  N N 398 
PHE HXT    H  N N 399 
PRO N      N  N N 400 
PRO CA     C  N S 401 
PRO C      C  N N 402 
PRO O      O  N N 403 
PRO CB     C  N N 404 
PRO CG     C  N N 405 
PRO CD     C  N N 406 
PRO OXT    O  N N 407 
PRO H      H  N N 408 
PRO HA     H  N N 409 
PRO HB2    H  N N 410 
PRO HB3    H  N N 411 
PRO HG2    H  N N 412 
PRO HG3    H  N N 413 
PRO HD2    H  N N 414 
PRO HD3    H  N N 415 
PRO HXT    H  N N 416 
SER N      N  N N 417 
SER CA     C  N S 418 
SER C      C  N N 419 
SER O      O  N N 420 
SER CB     C  N N 421 
SER OG     O  N N 422 
SER OXT    O  N N 423 
SER H      H  N N 424 
SER H2     H  N N 425 
SER HA     H  N N 426 
SER HB2    H  N N 427 
SER HB3    H  N N 428 
SER HG     H  N N 429 
SER HXT    H  N N 430 
SF4 FE1    FE N N 431 
SF4 FE2    FE N N 432 
SF4 FE3    FE N N 433 
SF4 FE4    FE N N 434 
SF4 S1     S  N N 435 
SF4 S2     S  N N 436 
SF4 S3     S  N N 437 
SF4 S4     S  N N 438 
THR N      N  N N 439 
THR CA     C  N S 440 
THR C      C  N N 441 
THR O      O  N N 442 
THR CB     C  N R 443 
THR OG1    O  N N 444 
THR CG2    C  N N 445 
THR OXT    O  N N 446 
THR H      H  N N 447 
THR H2     H  N N 448 
THR HA     H  N N 449 
THR HB     H  N N 450 
THR HG1    H  N N 451 
THR HG21   H  N N 452 
THR HG22   H  N N 453 
THR HG23   H  N N 454 
THR HXT    H  N N 455 
TRP N      N  N N 456 
TRP CA     C  N S 457 
TRP C      C  N N 458 
TRP O      O  N N 459 
TRP CB     C  N N 460 
TRP CG     C  Y N 461 
TRP CD1    C  Y N 462 
TRP CD2    C  Y N 463 
TRP NE1    N  Y N 464 
TRP CE2    C  Y N 465 
TRP CE3    C  Y N 466 
TRP CZ2    C  Y N 467 
TRP CZ3    C  Y N 468 
TRP CH2    C  Y N 469 
TRP OXT    O  N N 470 
TRP H      H  N N 471 
TRP H2     H  N N 472 
TRP HA     H  N N 473 
TRP HB2    H  N N 474 
TRP HB3    H  N N 475 
TRP HD1    H  N N 476 
TRP HE1    H  N N 477 
TRP HE3    H  N N 478 
TRP HZ2    H  N N 479 
TRP HZ3    H  N N 480 
TRP HH2    H  N N 481 
TRP HXT    H  N N 482 
TYR N      N  N N 483 
TYR CA     C  N S 484 
TYR C      C  N N 485 
TYR O      O  N N 486 
TYR CB     C  N N 487 
TYR CG     C  Y N 488 
TYR CD1    C  Y N 489 
TYR CD2    C  Y N 490 
TYR CE1    C  Y N 491 
TYR CE2    C  Y N 492 
TYR CZ     C  Y N 493 
TYR OH     O  N N 494 
TYR OXT    O  N N 495 
TYR H      H  N N 496 
TYR H2     H  N N 497 
TYR HA     H  N N 498 
TYR HB2    H  N N 499 
TYR HB3    H  N N 500 
TYR HD1    H  N N 501 
TYR HD2    H  N N 502 
TYR HE1    H  N N 503 
TYR HE2    H  N N 504 
TYR HH     H  N N 505 
TYR HXT    H  N N 506 
VAL N      N  N N 507 
VAL CA     C  N S 508 
VAL C      C  N N 509 
VAL O      O  N N 510 
VAL CB     C  N N 511 
VAL CG1    C  N N 512 
VAL CG2    C  N N 513 
VAL OXT    O  N N 514 
VAL H      H  N N 515 
VAL H2     H  N N 516 
VAL HA     H  N N 517 
VAL HB     H  N N 518 
VAL HG11   H  N N 519 
VAL HG12   H  N N 520 
VAL HG13   H  N N 521 
VAL HG21   H  N N 522 
VAL HG22   H  N N 523 
VAL HG23   H  N N 524 
VAL HXT    H  N N 525 
# 
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  
DLZ C7    C7A    sing N N 83  
DLZ C7A   C5A    doub N N 84  
DLZ C7A   N8     sing N N 85  
DLZ C5A   C6     sing N N 86  
DLZ C5A   N5     sing N N 87  
DLZ N5    C4A    doub N N 88  
DLZ C4A   C4     sing N N 89  
DLZ C4A   C8     sing N N 90  
DLZ C4    O4     doub N N 91  
DLZ C4    N3     sing N N 92  
DLZ N3    C2     sing N N 93  
DLZ C2    O2     doub N N 94  
DLZ C2    N1     sing N N 95  
DLZ N1    C8     doub N N 96  
DLZ C8    N8     sing N N 97  
DLZ N8    "C1'"  sing N N 98  
DLZ "C1'" "C2'"  sing N N 99  
DLZ "C2'" "O2'"  sing N N 100 
DLZ "C2'" "C3'"  sing N N 101 
DLZ "C3'" "O3'"  sing N N 102 
DLZ "C3'" "C4'"  sing N N 103 
DLZ "C4'" "O4'"  sing N N 104 
DLZ "C4'" "C5'"  sing N N 105 
DLZ "C5'" "O5'"  sing N N 106 
DLZ C7    H7     sing N N 107 
DLZ C7    H7A    sing N N 108 
DLZ C7    H7B    sing N N 109 
DLZ C6    H6     sing N N 110 
DLZ C6    H6A    sing N N 111 
DLZ C6    H6B    sing N N 112 
DLZ N3    HN3    sing N N 113 
DLZ "C1'" "H1'"  sing N N 114 
DLZ "C1'" "H1'A" sing N N 115 
DLZ "C2'" "H2'"  sing N N 116 
DLZ "O2'" "HO2'" sing N N 117 
DLZ "C3'" "H3'"  sing N N 118 
DLZ "O3'" "HO3'" sing N N 119 
DLZ "C4'" "H4'"  sing N N 120 
DLZ "O4'" "HO4'" sing N N 121 
DLZ "C5'" "H5'"  sing N N 122 
DLZ "C5'" "H5'A" sing N N 123 
DLZ "O5'" "HO5'" sing N N 124 
FAD PA    O1A    doub N N 125 
FAD PA    O2A    sing N N 126 
FAD PA    O5B    sing N N 127 
FAD PA    O3P    sing N N 128 
FAD O2A   HOA2   sing N N 129 
FAD O5B   C5B    sing N N 130 
FAD C5B   C4B    sing N N 131 
FAD C5B   H51A   sing N N 132 
FAD C5B   H52A   sing N N 133 
FAD C4B   O4B    sing N N 134 
FAD C4B   C3B    sing N N 135 
FAD C4B   H4B    sing N N 136 
FAD O4B   C1B    sing N N 137 
FAD C3B   O3B    sing N N 138 
FAD C3B   C2B    sing N N 139 
FAD C3B   H3B    sing N N 140 
FAD O3B   HO3A   sing N N 141 
FAD C2B   O2B    sing N N 142 
FAD C2B   C1B    sing N N 143 
FAD C2B   H2B    sing N N 144 
FAD O2B   HO2A   sing N N 145 
FAD C1B   N9A    sing N N 146 
FAD C1B   H1B    sing N N 147 
FAD N9A   C8A    sing Y N 148 
FAD N9A   C4A    sing Y N 149 
FAD C8A   N7A    doub Y N 150 
FAD C8A   H8A    sing N N 151 
FAD N7A   C5A    sing Y N 152 
FAD C5A   C6A    sing Y N 153 
FAD C5A   C4A    doub Y N 154 
FAD C6A   N6A    sing N N 155 
FAD C6A   N1A    doub Y N 156 
FAD N6A   H61A   sing N N 157 
FAD N6A   H62A   sing N N 158 
FAD N1A   C2A    sing Y N 159 
FAD C2A   N3A    doub Y N 160 
FAD C2A   H2A    sing N N 161 
FAD N3A   C4A    sing Y N 162 
FAD N1    C2     sing N N 163 
FAD N1    C10    doub N N 164 
FAD C2    O2     doub N N 165 
FAD C2    N3     sing N N 166 
FAD N3    C4     sing N N 167 
FAD N3    HN3    sing N N 168 
FAD C4    O4     doub N N 169 
FAD C4    C4X    sing N N 170 
FAD C4X   N5     doub N N 171 
FAD C4X   C10    sing N N 172 
FAD N5    C5X    sing N N 173 
FAD C5X   C6     doub Y N 174 
FAD C5X   C9A    sing Y N 175 
FAD C6    C7     sing Y N 176 
FAD C6    H6     sing N N 177 
FAD C7    C7M    sing N N 178 
FAD C7    C8     doub Y N 179 
FAD C7M   HM71   sing N N 180 
FAD C7M   HM72   sing N N 181 
FAD C7M   HM73   sing N N 182 
FAD C8    C8M    sing N N 183 
FAD C8    C9     sing Y N 184 
FAD C8M   HM81   sing N N 185 
FAD C8M   HM82   sing N N 186 
FAD C8M   HM83   sing N N 187 
FAD C9    C9A    doub Y N 188 
FAD C9    H9     sing N N 189 
FAD C9A   N10    sing N N 190 
FAD N10   C10    sing N N 191 
FAD N10   "C1'"  sing N N 192 
FAD "C1'" "C2'"  sing N N 193 
FAD "C1'" "H1'1" sing N N 194 
FAD "C1'" "H1'2" sing N N 195 
FAD "C2'" "O2'"  sing N N 196 
FAD "C2'" "C3'"  sing N N 197 
FAD "C2'" "H2'"  sing N N 198 
FAD "O2'" "HO2'" sing N N 199 
FAD "C3'" "O3'"  sing N N 200 
FAD "C3'" "C4'"  sing N N 201 
FAD "C3'" "H3'"  sing N N 202 
FAD "O3'" "HO3'" sing N N 203 
FAD "C4'" "O4'"  sing N N 204 
FAD "C4'" "C5'"  sing N N 205 
FAD "C4'" "H4'"  sing N N 206 
FAD "O4'" "HO4'" sing N N 207 
FAD "C5'" "O5'"  sing N N 208 
FAD "C5'" "H5'1" sing N N 209 
FAD "C5'" "H5'2" sing N N 210 
FAD "O5'" P      sing N N 211 
FAD P     O1P    doub N N 212 
FAD P     O2P    sing N N 213 
FAD P     O3P    sing N N 214 
FAD O2P   HOP2   sing N N 215 
GLN N     CA     sing N N 216 
GLN N     H      sing N N 217 
GLN N     H2     sing N N 218 
GLN CA    C      sing N N 219 
GLN CA    CB     sing N N 220 
GLN CA    HA     sing N N 221 
GLN C     O      doub N N 222 
GLN C     OXT    sing N N 223 
GLN CB    CG     sing N N 224 
GLN CB    HB2    sing N N 225 
GLN CB    HB3    sing N N 226 
GLN CG    CD     sing N N 227 
GLN CG    HG2    sing N N 228 
GLN CG    HG3    sing N N 229 
GLN CD    OE1    doub N N 230 
GLN CD    NE2    sing N N 231 
GLN NE2   HE21   sing N N 232 
GLN NE2   HE22   sing N N 233 
GLN OXT   HXT    sing N N 234 
GLU N     CA     sing N N 235 
GLU N     H      sing N N 236 
GLU N     H2     sing N N 237 
GLU CA    C      sing N N 238 
GLU CA    CB     sing N N 239 
GLU CA    HA     sing N N 240 
GLU C     O      doub N N 241 
GLU C     OXT    sing N N 242 
GLU CB    CG     sing N N 243 
GLU CB    HB2    sing N N 244 
GLU CB    HB3    sing N N 245 
GLU CG    CD     sing N N 246 
GLU CG    HG2    sing N N 247 
GLU CG    HG3    sing N N 248 
GLU CD    OE1    doub N N 249 
GLU CD    OE2    sing N N 250 
GLU OE2   HE2    sing N N 251 
GLU OXT   HXT    sing N N 252 
GLY N     CA     sing N N 253 
GLY N     H      sing N N 254 
GLY N     H2     sing N N 255 
GLY CA    C      sing N N 256 
GLY CA    HA2    sing N N 257 
GLY CA    HA3    sing N N 258 
GLY C     O      doub N N 259 
GLY C     OXT    sing N N 260 
GLY OXT   HXT    sing N N 261 
HIS N     CA     sing N N 262 
HIS N     H      sing N N 263 
HIS N     H2     sing N N 264 
HIS CA    C      sing N N 265 
HIS CA    CB     sing N N 266 
HIS CA    HA     sing N N 267 
HIS C     O      doub N N 268 
HIS C     OXT    sing N N 269 
HIS CB    CG     sing N N 270 
HIS CB    HB2    sing N N 271 
HIS CB    HB3    sing N N 272 
HIS CG    ND1    sing Y N 273 
HIS CG    CD2    doub Y N 274 
HIS ND1   CE1    doub Y N 275 
HIS ND1   HD1    sing N N 276 
HIS CD2   NE2    sing Y N 277 
HIS CD2   HD2    sing N N 278 
HIS CE1   NE2    sing Y N 279 
HIS CE1   HE1    sing N N 280 
HIS NE2   HE2    sing N N 281 
HIS OXT   HXT    sing N N 282 
HOH O     H1     sing N N 283 
HOH O     H2     sing N N 284 
ILE N     CA     sing N N 285 
ILE N     H      sing N N 286 
ILE N     H2     sing N N 287 
ILE CA    C      sing N N 288 
ILE CA    CB     sing N N 289 
ILE CA    HA     sing N N 290 
ILE C     O      doub N N 291 
ILE C     OXT    sing N N 292 
ILE CB    CG1    sing N N 293 
ILE CB    CG2    sing N N 294 
ILE CB    HB     sing N N 295 
ILE CG1   CD1    sing N N 296 
ILE CG1   HG12   sing N N 297 
ILE CG1   HG13   sing N N 298 
ILE CG2   HG21   sing N N 299 
ILE CG2   HG22   sing N N 300 
ILE CG2   HG23   sing N N 301 
ILE CD1   HD11   sing N N 302 
ILE CD1   HD12   sing N N 303 
ILE CD1   HD13   sing N N 304 
ILE OXT   HXT    sing N N 305 
LEU N     CA     sing N N 306 
LEU N     H      sing N N 307 
LEU N     H2     sing N N 308 
LEU CA    C      sing N N 309 
LEU CA    CB     sing N N 310 
LEU CA    HA     sing N N 311 
LEU C     O      doub N N 312 
LEU C     OXT    sing N N 313 
LEU CB    CG     sing N N 314 
LEU CB    HB2    sing N N 315 
LEU CB    HB3    sing N N 316 
LEU CG    CD1    sing N N 317 
LEU CG    CD2    sing N N 318 
LEU CG    HG     sing N N 319 
LEU CD1   HD11   sing N N 320 
LEU CD1   HD12   sing N N 321 
LEU CD1   HD13   sing N N 322 
LEU CD2   HD21   sing N N 323 
LEU CD2   HD22   sing N N 324 
LEU CD2   HD23   sing N N 325 
LEU OXT   HXT    sing N N 326 
LYS N     CA     sing N N 327 
LYS N     H      sing N N 328 
LYS N     H2     sing N N 329 
LYS CA    C      sing N N 330 
LYS CA    CB     sing N N 331 
LYS CA    HA     sing N N 332 
LYS C     O      doub N N 333 
LYS C     OXT    sing N N 334 
LYS CB    CG     sing N N 335 
LYS CB    HB2    sing N N 336 
LYS CB    HB3    sing N N 337 
LYS CG    CD     sing N N 338 
LYS CG    HG2    sing N N 339 
LYS CG    HG3    sing N N 340 
LYS CD    CE     sing N N 341 
LYS CD    HD2    sing N N 342 
LYS CD    HD3    sing N N 343 
LYS CE    NZ     sing N N 344 
LYS CE    HE2    sing N N 345 
LYS CE    HE3    sing N N 346 
LYS NZ    HZ1    sing N N 347 
LYS NZ    HZ2    sing N N 348 
LYS NZ    HZ3    sing N N 349 
LYS OXT   HXT    sing N N 350 
MET N     CA     sing N N 351 
MET N     H      sing N N 352 
MET N     H2     sing N N 353 
MET CA    C      sing N N 354 
MET CA    CB     sing N N 355 
MET CA    HA     sing N N 356 
MET C     O      doub N N 357 
MET C     OXT    sing N N 358 
MET CB    CG     sing N N 359 
MET CB    HB2    sing N N 360 
MET CB    HB3    sing N N 361 
MET CG    SD     sing N N 362 
MET CG    HG2    sing N N 363 
MET CG    HG3    sing N N 364 
MET SD    CE     sing N N 365 
MET CE    HE1    sing N N 366 
MET CE    HE2    sing N N 367 
MET CE    HE3    sing N N 368 
MET OXT   HXT    sing N N 369 
PHE N     CA     sing N N 370 
PHE N     H      sing N N 371 
PHE N     H2     sing N N 372 
PHE CA    C      sing N N 373 
PHE CA    CB     sing N N 374 
PHE CA    HA     sing N N 375 
PHE C     O      doub N N 376 
PHE C     OXT    sing N N 377 
PHE CB    CG     sing N N 378 
PHE CB    HB2    sing N N 379 
PHE CB    HB3    sing N N 380 
PHE CG    CD1    doub Y N 381 
PHE CG    CD2    sing Y N 382 
PHE CD1   CE1    sing Y N 383 
PHE CD1   HD1    sing N N 384 
PHE CD2   CE2    doub Y N 385 
PHE CD2   HD2    sing N N 386 
PHE CE1   CZ     doub Y N 387 
PHE CE1   HE1    sing N N 388 
PHE CE2   CZ     sing Y N 389 
PHE CE2   HE2    sing N N 390 
PHE CZ    HZ     sing N N 391 
PHE OXT   HXT    sing N N 392 
PRO N     CA     sing N N 393 
PRO N     CD     sing N N 394 
PRO N     H      sing N N 395 
PRO CA    C      sing N N 396 
PRO CA    CB     sing N N 397 
PRO CA    HA     sing N N 398 
PRO C     O      doub N N 399 
PRO C     OXT    sing N N 400 
PRO CB    CG     sing N N 401 
PRO CB    HB2    sing N N 402 
PRO CB    HB3    sing N N 403 
PRO CG    CD     sing N N 404 
PRO CG    HG2    sing N N 405 
PRO CG    HG3    sing N N 406 
PRO CD    HD2    sing N N 407 
PRO CD    HD3    sing N N 408 
PRO OXT   HXT    sing N N 409 
SER N     CA     sing N N 410 
SER N     H      sing N N 411 
SER N     H2     sing N N 412 
SER CA    C      sing N N 413 
SER CA    CB     sing N N 414 
SER CA    HA     sing N N 415 
SER C     O      doub N N 416 
SER C     OXT    sing N N 417 
SER CB    OG     sing N N 418 
SER CB    HB2    sing N N 419 
SER CB    HB3    sing N N 420 
SER OG    HG     sing N N 421 
SER OXT   HXT    sing N N 422 
SF4 FE1   S2     sing N N 423 
SF4 FE1   S3     sing N N 424 
SF4 FE1   S4     sing N N 425 
SF4 FE2   S1     sing N N 426 
SF4 FE2   S3     sing N N 427 
SF4 FE2   S4     sing N N 428 
SF4 FE3   S1     sing N N 429 
SF4 FE3   S2     sing N N 430 
SF4 FE3   S4     sing N N 431 
SF4 FE4   S1     sing N N 432 
SF4 FE4   S2     sing N N 433 
SF4 FE4   S3     sing N N 434 
THR N     CA     sing N N 435 
THR N     H      sing N N 436 
THR N     H2     sing N N 437 
THR CA    C      sing N N 438 
THR CA    CB     sing N N 439 
THR CA    HA     sing N N 440 
THR C     O      doub N N 441 
THR C     OXT    sing N N 442 
THR CB    OG1    sing N N 443 
THR CB    CG2    sing N N 444 
THR CB    HB     sing N N 445 
THR OG1   HG1    sing N N 446 
THR CG2   HG21   sing N N 447 
THR CG2   HG22   sing N N 448 
THR CG2   HG23   sing N N 449 
THR OXT   HXT    sing N N 450 
TRP N     CA     sing N N 451 
TRP N     H      sing N N 452 
TRP N     H2     sing N N 453 
TRP CA    C      sing N N 454 
TRP CA    CB     sing N N 455 
TRP CA    HA     sing N N 456 
TRP C     O      doub N N 457 
TRP C     OXT    sing N N 458 
TRP CB    CG     sing N N 459 
TRP CB    HB2    sing N N 460 
TRP CB    HB3    sing N N 461 
TRP CG    CD1    doub Y N 462 
TRP CG    CD2    sing Y N 463 
TRP CD1   NE1    sing Y N 464 
TRP CD1   HD1    sing N N 465 
TRP CD2   CE2    doub Y N 466 
TRP CD2   CE3    sing Y N 467 
TRP NE1   CE2    sing Y N 468 
TRP NE1   HE1    sing N N 469 
TRP CE2   CZ2    sing Y N 470 
TRP CE3   CZ3    doub Y N 471 
TRP CE3   HE3    sing N N 472 
TRP CZ2   CH2    doub Y N 473 
TRP CZ2   HZ2    sing N N 474 
TRP CZ3   CH2    sing Y N 475 
TRP CZ3   HZ3    sing N N 476 
TRP CH2   HH2    sing N N 477 
TRP OXT   HXT    sing N N 478 
TYR N     CA     sing N N 479 
TYR N     H      sing N N 480 
TYR N     H2     sing N N 481 
TYR CA    C      sing N N 482 
TYR CA    CB     sing N N 483 
TYR CA    HA     sing N N 484 
TYR C     O      doub N N 485 
TYR C     OXT    sing N N 486 
TYR CB    CG     sing N N 487 
TYR CB    HB2    sing N N 488 
TYR CB    HB3    sing N N 489 
TYR CG    CD1    doub Y N 490 
TYR CG    CD2    sing Y N 491 
TYR CD1   CE1    sing Y N 492 
TYR CD1   HD1    sing N N 493 
TYR CD2   CE2    doub Y N 494 
TYR CD2   HD2    sing N N 495 
TYR CE1   CZ     doub Y N 496 
TYR CE1   HE1    sing N N 497 
TYR CE2   CZ     sing Y N 498 
TYR CE2   HE2    sing N N 499 
TYR CZ    OH     sing N N 500 
TYR OH    HH     sing N N 501 
TYR OXT   HXT    sing N N 502 
VAL N     CA     sing N N 503 
VAL N     H      sing N N 504 
VAL N     H2     sing N N 505 
VAL CA    C      sing N N 506 
VAL CA    CB     sing N N 507 
VAL CA    HA     sing N N 508 
VAL C     O      doub N N 509 
VAL C     OXT    sing N N 510 
VAL CB    CG1    sing N N 511 
VAL CB    CG2    sing N N 512 
VAL CB    HB     sing N N 513 
VAL CG1   HG11   sing N N 514 
VAL CG1   HG12   sing N N 515 
VAL CG1   HG13   sing N N 516 
VAL CG2   HG21   sing N N 517 
VAL CG2   HG22   sing N N 518 
VAL CG2   HG23   sing N N 519 
VAL OXT   HXT    sing N N 520 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           ES152/18 
_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   8A1H 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9HNL 
_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]   0.020265 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009739 
_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]   0.009658 
_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.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
FE ? ? 20.90327 4.99816 ? ? 2.55100  38.46870 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135  5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . MET A 1 1   ? 22.57691  18.40841  53.08073  1.000 94.74598  ? 1    MET A N     1 
ATOM   2    C  CA    . MET A 1 1   ? 21.51829  17.41082  52.97731  1.000 94.02551  ? 1    MET A CA    1 
ATOM   3    C  C     . MET A 1 1   ? 20.13985  18.07307  52.93074  1.000 93.55458  ? 1    MET A C     1 
ATOM   4    O  O     . MET A 1 1   ? 19.17148  17.57173  53.50156  1.000 93.32046  ? 1    MET A O     1 
ATOM   5    C  CB    . MET A 1 1   ? 21.61020  16.41638  54.14204  1.000 96.18484  ? 1    MET A CB    1 
ATOM   6    C  CG    . MET A 1 1   ? 21.35255  17.00924  55.52468  1.000 96.77107  ? 1    MET A CG    1 
ATOM   7    S  SD    . MET A 1 1   ? 22.63985  18.14080  56.08452  1.000 97.72210  ? 1    MET A SD    1 
ATOM   8    C  CE    . MET A 1 1   ? 21.94824  18.68573  57.64493  1.000 98.20889  ? 1    MET A CE    1 
ATOM   9    N  N     . ALA A 1 2   ? 20.05654  19.20076  52.22153  1.000 44.49720  ? 2    ALA A N     1 
ATOM   10   C  CA    . ALA A 1 2   ? 18.80895  19.95312  52.16057  1.000 44.36940  ? 2    ALA A CA    1 
ATOM   11   C  C     . ALA A 1 2   ? 17.74198  19.26080  51.32060  1.000 42.97065  ? 2    ALA A C     1 
ATOM   12   O  O     . ALA A 1 2   ? 16.55246  19.54006  51.50508  1.000 43.00094  ? 2    ALA A O     1 
ATOM   13   C  CB    . ALA A 1 2   ? 19.06888  21.35797  51.61530  1.000 43.30716  ? 2    ALA A CB    1 
ATOM   14   N  N     . GLY A 1 3   ? 18.12926  18.37914  50.41071  1.000 29.48676  ? 3    GLY A N     1 
ATOM   15   C  CA    . GLY A 1 3   ? 17.18975  17.65384  49.58076  1.000 28.86294  ? 3    GLY A CA    1 
ATOM   16   C  C     . GLY A 1 3   ? 17.25654  18.08802  48.12496  1.000 28.99107  ? 3    GLY A C     1 
ATOM   17   O  O     . GLY A 1 3   ? 17.93029  19.04922  47.75203  1.000 28.80471  ? 3    GLY A O     1 
ATOM   18   N  N     . ALA A 1 4   ? 16.52166  17.34855  47.29748  1.000 26.05458  ? 4    ALA A N     1 
ATOM   19   C  CA    . ALA A 1 4   ? 16.50438  17.55844  45.85781  1.000 25.58033  ? 4    ALA A CA    1 
ATOM   20   C  C     . ALA A 1 4   ? 15.10435  17.93287  45.39270  1.000 24.60352  ? 4    ALA A C     1 
ATOM   21   O  O     . ALA A 1 4   ? 14.10705  17.41741  45.90867  1.000 24.39054  ? 4    ALA A O     1 
ATOM   22   C  CB    . ALA A 1 4   ? 16.98047  16.30673  45.10969  1.000 25.02495  ? 4    ALA A CB    1 
ATOM   23   N  N     . LEU A 1 5   ? 15.04016  18.83506  44.41685  1.000 27.19434  ? 5    LEU A N     1 
ATOM   24   C  CA    . LEU A 1 5   ? 13.79732  19.18885  43.74368  1.000 26.43578  ? 5    LEU A CA    1 
ATOM   25   C  C     . LEU A 1 5   ? 13.69093  18.35872  42.47009  1.000 26.57175  ? 5    LEU A C     1 
ATOM   26   O  O     . LEU A 1 5   ? 14.56600  18.43392  41.60067  1.000 26.71016  ? 5    LEU A O     1 
ATOM   27   C  CB    . LEU A 1 5   ? 13.75318  20.68232  43.42467  1.000 26.84195  ? 5    LEU A CB    1 
ATOM   28   C  CG    . LEU A 1 5   ? 12.54150  21.17840  42.63316  1.000 26.89234  ? 5    LEU A CG    1 
ATOM   29   C  CD1   . LEU A 1 5   ? 11.27167  21.06389  43.46212  1.000 25.99317  ? 5    LEU A CD1   1 
ATOM   30   C  CD2   . LEU A 1 5   ? 12.75662  22.61106  42.17171  1.000 26.64443  ? 5    LEU A CD2   1 
ATOM   31   N  N     . ARG A 1 6   ? 12.62625  17.57042  42.36196  1.000 21.10563  ? 6    ARG A N     1 
ATOM   32   C  CA    . ARG A 1 6   ? 12.47781  16.59263  41.28974  1.000 20.31679  ? 6    ARG A CA    1 
ATOM   33   C  C     . ARG A 1 6   ? 11.35775  17.03721  40.35742  1.000 19.50526  ? 6    ARG A C     1 
ATOM   34   O  O     . ARG A 1 6   ? 10.18883  17.07968  40.75458  1.000 19.17811  ? 6    ARG A O     1 
ATOM   35   C  CB    . ARG A 1 6   ? 12.21507  15.20398  41.86817  1.000 20.12442  ? 6    ARG A CB    1 
ATOM   36   C  CG    . ARG A 1 6   ? 13.40289  14.66766  42.65385  1.000 20.91655  ? 6    ARG A CG    1 
ATOM   37   C  CD    . ARG A 1 6   ? 13.10253  13.35690  43.35171  1.000 21.24555  ? 6    ARG A CD    1 
ATOM   38   N  NE    . ARG A 1 6   ? 14.19277  12.98571  44.24560  1.000 22.19188  ? 6    ARG A NE    1 
ATOM   39   C  CZ    . ARG A 1 6   ? 15.24156  12.25739  43.88793  1.000 22.41172  ? 6    ARG A CZ    1 
ATOM   40   N  NH1   . ARG A 1 6   ? 15.36353  11.77565  42.66172  1.000 21.74731  ? 6    ARG A NH1   1 
ATOM   41   N  NH2   . ARG A 1 6   ? 16.19295  12.00794  44.78265  1.000 23.40933  ? 6    ARG A NH2   1 
ATOM   42   N  N     . LEU A 1 7   ? 11.72098  17.35777  39.11800  1.000 22.01434  ? 7    LEU A N     1 
ATOM   43   C  CA    . LEU A 1 7   ? 10.77580  17.83816  38.11907  1.000 21.45124  ? 7    LEU A CA    1 
ATOM   44   C  C     . LEU A 1 7   ? 10.10609  16.66537  37.41133  1.000 20.30269  ? 7    LEU A C     1 
ATOM   45   O  O     . LEU A 1 7   ? 10.77543  15.70502  37.01669  1.000 20.18185  ? 7    LEU A O     1 
ATOM   46   C  CB    . LEU A 1 7   ? 11.49167  18.72661  37.10187  1.000 22.00755  ? 7    LEU A CB    1 
ATOM   47   C  CG    . LEU A 1 7   ? 10.65387  19.32919  35.97403  1.000 22.34905  ? 7    LEU A CG    1 
ATOM   48   C  CD1   . LEU A 1 7   ? 9.63386   20.31943  36.52287  1.000 21.69422  ? 7    LEU A CD1   1 
ATOM   49   C  CD2   . LEU A 1 7   ? 11.55966  19.99491  34.95191  1.000 22.02078  ? 7    LEU A CD2   1 
ATOM   50   N  N     . VAL A 1 8   ? 8.78696   16.75032  37.24954  1.000 20.03837  ? 8    VAL A N     1 
ATOM   51   C  CA    . VAL A 1 8   ? 8.00548   15.75615  36.52004  1.000 18.82110  ? 8    VAL A CA    1 
ATOM   52   C  C     . VAL A 1 8   ? 7.15707   16.49195  35.49206  1.000 18.42329  ? 8    VAL A C     1 
ATOM   53   O  O     . VAL A 1 8   ? 6.34400   17.34987  35.85595  1.000 18.90078  ? 8    VAL A O     1 
ATOM   54   C  CB    . VAL A 1 8   ? 7.11473   14.91763  37.45225  1.000 18.36262  ? 8    VAL A CB    1 
ATOM   55   C  CG1   . VAL A 1 8   ? 6.15883   14.05451  36.63721  1.000 16.90598  ? 8    VAL A CG1   1 
ATOM   56   C  CG2   . VAL A 1 8   ? 7.96658   14.06040  38.37853  1.000 18.39235  ? 8    VAL A CG2   1 
ATOM   57   N  N     . LEU A 1 9   ? 7.33995   16.15797  34.21760  1.000 18.85285  ? 9    LEU A N     1 
ATOM   58   C  CA    . LEU A 1 9   ? 6.62321   16.82324  33.14122  1.000 18.04802  ? 9    LEU A CA    1 
ATOM   59   C  C     . LEU A 1 9   ? 5.34158   16.06966  32.78836  1.000 17.02600  ? 9    LEU A C     1 
ATOM   60   O  O     . LEU A 1 9   ? 5.06261   14.98229  33.29867  1.000 17.07975  ? 9    LEU A O     1 
ATOM   61   C  CB    . LEU A 1 9   ? 7.51888   16.96690  31.91262  1.000 17.86472  ? 9    LEU A CB    1 
ATOM   62   C  CG    . LEU A 1 9   ? 8.73720   17.86555  32.12841  1.000 19.61281  ? 9    LEU A CG    1 
ATOM   63   C  CD1   . LEU A 1 9   ? 9.54628   17.99295  30.85015  1.000 19.12575  ? 9    LEU A CD1   1 
ATOM   64   C  CD2   . LEU A 1 9   ? 8.31345   19.23547  32.64398  1.000 19.67818  ? 9    LEU A CD2   1 
ATOM   65   N  N     . GLY A 1 10  ? 4.55971   16.66864  31.88666  1.000 17.82264  ? 10   GLY A N     1 
ATOM   66   C  CA    . GLY A 1 10  ? 3.23450   16.16237  31.57140  1.000 17.69269  ? 10   GLY A CA    1 
ATOM   67   C  C     . GLY A 1 10  ? 3.21916   14.80099  30.90803  1.000 17.39278  ? 10   GLY A C     1 
ATOM   68   O  O     . GLY A 1 10  ? 2.19669   14.10880  30.96120  1.000 17.08386  ? 10   GLY A O     1 
ATOM   69   N  N     . ASP A 1 11  ? 4.32282   14.39946  30.27687  1.000 22.79841  ? 11   ASP A N     1 
ATOM   70   C  CA    . ASP A 1 11  ? 4.42249   13.09099  29.64398  1.000 22.20291  ? 11   ASP A CA    1 
ATOM   71   C  C     . ASP A 1 11  ? 5.33179   12.14491  30.41952  1.000 22.65357  ? 11   ASP A C     1 
ATOM   72   O  O     . ASP A 1 11  ? 5.83730   11.17009  29.85413  1.000 22.61807  ? 11   ASP A O     1 
ATOM   73   C  CB    . ASP A 1 11  ? 4.90595   13.23183  28.20022  1.000 22.88305  ? 11   ASP A CB    1 
ATOM   74   C  CG    . ASP A 1 11  ? 6.31802   13.77405  28.10654  1.000 24.08686  ? 11   ASP A CG    1 
ATOM   75   O  OD1   . ASP A 1 11  ? 6.77031   14.43823  29.06320  1.000 24.08557  ? 11   ASP A OD1   1 
ATOM   76   O  OD2   . ASP A 1 11  ? 6.97580   13.54022  27.07079  1.000 24.24825  ? 11   ASP A OD2   1 
ATOM   77   N  N     . GLN A 1 12  ? 5.54110   12.40995  31.70799  1.000 16.74381  ? 12   GLN A N     1 
ATOM   78   C  CA    . GLN A 1 12  ? 6.44283   11.62897  32.54492  1.000 16.87221  ? 12   GLN A CA    1 
ATOM   79   C  C     . GLN A 1 12  ? 5.71423   11.03588  33.74719  1.000 17.08464  ? 12   GLN A C     1 
ATOM   80   O  O     . GLN A 1 12  ? 6.28957   10.90369  34.82867  1.000 17.75327  ? 12   GLN A O     1 
ATOM   81   C  CB    . GLN A 1 12  ? 7.61857   12.49276  32.99745  1.000 17.56694  ? 12   GLN A CB    1 
ATOM   82   C  CG    . GLN A 1 12  ? 8.37379   13.13828  31.84795  1.000 18.13999  ? 12   GLN A CG    1 
ATOM   83   C  CD    . GLN A 1 12  ? 9.63723   13.83917  32.29835  1.000 19.47126  ? 12   GLN A CD    1 
ATOM   84   O  OE1   . GLN A 1 12  ? 9.68665   14.41607  33.38385  1.000 19.70529  ? 12   GLN A OE1   1 
ATOM   85   N  NE2   . GLN A 1 12  ? 10.67016  13.79066  31.46456  1.000 19.83258  ? 12   GLN A NE2   1 
ATOM   86   N  N     . LEU A 1 13  ? 4.44799   10.66224  33.56483  1.000 16.64553  ? 13   LEU A N     1 
ATOM   87   C  CA    . LEU A 1 13  ? 3.57932   10.27352  34.67754  1.000 17.19827  ? 13   LEU A CA    1 
ATOM   88   C  C     . LEU A 1 13  ? 3.68884   8.76864   34.92923  1.000 17.30889  ? 13   LEU A C     1 
ATOM   89   O  O     . LEU A 1 13  ? 2.75217   7.99097   34.73542  1.000 17.03773  ? 13   LEU A O     1 
ATOM   90   C  CB    . LEU A 1 13  ? 2.14611   10.70073  34.39291  1.000 16.76208  ? 13   LEU A CB    1 
ATOM   91   C  CG    . LEU A 1 13  ? 2.05725   12.11443  33.80914  1.000 17.36398  ? 13   LEU A CG    1 
ATOM   92   C  CD1   . LEU A 1 13  ? 0.63447   12.45897  33.42463  1.000 16.81828  ? 13   LEU A CD1   1 
ATOM   93   C  CD2   . LEU A 1 13  ? 2.61170   13.14418  34.78882  1.000 17.49753  ? 13   LEU A CD2   1 
ATOM   94   N  N     . SER A 1 14  ? 4.87292   8.36999   35.38802  1.000 21.24305  ? 14   SER A N     1 
ATOM   95   C  CA    . SER A 1 14  ? 5.17468   6.98093   35.69725  1.000 21.44344  ? 14   SER A CA    1 
ATOM   96   C  C     . SER A 1 14  ? 5.88281   6.90560   37.04063  1.000 21.81593  ? 14   SER A C     1 
ATOM   97   O  O     . SER A 1 14  ? 6.70898   7.76461   37.36237  1.000 22.10820  ? 14   SER A O     1 
ATOM   98   C  CB    . SER A 1 14  ? 6.05013   6.34954   34.61051  1.000 21.06257  ? 14   SER A CB    1 
ATOM   99   O  OG    . SER A 1 14  ? 5.69855   6.83649   33.32805  1.000 21.52886  ? 14   SER A OG    1 
ATOM   100  N  N     . ASP A 1 15  ? 5.55520   5.87361   37.82414  1.000 36.73501  ? 15   ASP A N     1 
ATOM   101  C  CA    . ASP A 1 15  ? 6.21744   5.68963   39.11187  1.000 37.20420  ? 15   ASP A CA    1 
ATOM   102  C  C     . ASP A 1 15  ? 7.70064   5.38629   38.94367  1.000 38.29781  ? 15   ASP A C     1 
ATOM   103  O  O     . ASP A 1 15  ? 8.51100   5.77214   39.79419  1.000 38.88146  ? 15   ASP A O     1 
ATOM   104  C  CB    . ASP A 1 15  ? 5.54056   4.56982   39.90445  1.000 38.24442  ? 15   ASP A CB    1 
ATOM   105  C  CG    . ASP A 1 15  ? 4.03482   4.73656   39.98771  1.000 38.24750  ? 15   ASP A CG    1 
ATOM   106  O  OD1   . ASP A 1 15  ? 3.32913   3.71424   40.12449  1.000 38.93900  ? 15   ASP A OD1   1 
ATOM   107  O  OD2   . ASP A 1 15  ? 3.55624   5.88789   39.92216  1.000 37.65559  ? 15   ASP A OD2   1 
ATOM   108  N  N     . ASN A 1 16  ? 8.07435   4.70699   37.85894  1.000 36.15251  ? 16   ASN A N     1 
ATOM   109  C  CA    . ASN A 1 16  ? 9.45518   4.32099   37.60719  1.000 36.75153  ? 16   ASN A CA    1 
ATOM   110  C  C     . ASN A 1 16  ? 10.24061  5.38426   36.84546  1.000 36.71693  ? 16   ASN A C     1 
ATOM   111  O  O     . ASN A 1 16  ? 11.28161  5.06775   36.25817  1.000 37.65470  ? 16   ASN A O     1 
ATOM   112  C  CB    . ASN A 1 16  ? 9.50041   2.98810   36.85303  1.000 36.60206  ? 16   ASN A CB    1 
ATOM   113  C  CG    . ASN A 1 16  ? 8.75356   3.03359   35.52993  1.000 36.70315  ? 16   ASN A CG    1 
ATOM   114  O  OD1   . ASN A 1 16  ? 8.19493   4.06094   35.15001  1.000 36.91379  ? 16   ASN A OD1   1 
ATOM   115  N  ND2   . ASN A 1 16  ? 8.74364   1.91187   34.82034  1.000 37.82049  ? 16   ASN A ND2   1 
ATOM   116  N  N     . LEU A 1 17  ? 9.76519   6.62813   36.83615  1.000 18.41766  ? 17   LEU A N     1 
ATOM   117  C  CA    . LEU A 1 17  ? 10.50727  7.70485   36.19361  1.000 18.59409  ? 17   LEU A CA    1 
ATOM   118  C  C     . LEU A 1 17  ? 11.87072  7.87595   36.85316  1.000 19.27369  ? 17   LEU A C     1 
ATOM   119  O  O     . LEU A 1 17  ? 11.98826  7.87988   38.08172  1.000 19.66431  ? 17   LEU A O     1 
ATOM   120  C  CB    . LEU A 1 17  ? 9.71626   9.01043   36.26665  1.000 18.19448  ? 17   LEU A CB    1 
ATOM   121  C  CG    . LEU A 1 17  ? 10.25917  10.16761  35.42915  1.000 18.63939  ? 17   LEU A CG    1 
ATOM   122  C  CD1   . LEU A 1 17  ? 9.97031   9.94117   33.95422  1.000 17.83754  ? 17   LEU A CD1   1 
ATOM   123  C  CD2   . LEU A 1 17  ? 9.66826   11.48560  35.90007  1.000 18.26652  ? 17   LEU A CD2   1 
ATOM   124  N  N     . SER A 1 18  ? 12.90804  8.01733   36.02189  1.000 24.18729  ? 18   SER A N     1 
ATOM   125  C  CA    . SER A 1 18  ? 14.27430  8.06389   36.53593  1.000 25.61934  ? 18   SER A CA    1 
ATOM   126  C  C     . SER A 1 18  ? 14.48458  9.22827   37.49624  1.000 26.34592  ? 18   SER A C     1 
ATOM   127  O  O     . SER A 1 18  ? 15.31572  9.13622   38.40732  1.000 26.99830  ? 18   SER A O     1 
ATOM   128  C  CB    . SER A 1 18  ? 15.26776  8.14422   35.37602  1.000 26.00441  ? 18   SER A CB    1 
ATOM   129  O  OG    . SER A 1 18  ? 14.93690  9.20303   34.49363  1.000 26.57687  ? 18   SER A OG    1 
ATOM   130  N  N     . ALA A 1 19  ? 13.74228  10.32419  37.31809  1.000 21.49274  ? 19   ALA A N     1 
ATOM   131  C  CA    . ALA A 1 19  ? 13.87259  11.46753  38.21440  1.000 21.74443  ? 19   ALA A CA    1 
ATOM   132  C  C     . ALA A 1 19  ? 13.35108  11.17480  39.61567  1.000 21.73117  ? 19   ALA A C     1 
ATOM   133  O  O     . ALA A 1 19  ? 13.71310  11.88842  40.55733  1.000 22.13975  ? 19   ALA A O     1 
ATOM   134  C  CB    . ALA A 1 19  ? 13.14190  12.67945  37.63238  1.000 21.73215  ? 19   ALA A CB    1 
ATOM   135  N  N     . LEU A 1 20  ? 12.51707  10.14791  39.77711  1.000 26.88118  ? 20   LEU A N     1 
ATOM   136  C  CA    . LEU A 1 20  ? 11.94442  9.79513   41.06994  1.000 26.05120  ? 20   LEU A CA    1 
ATOM   137  C  C     . LEU A 1 20  ? 12.66825  8.63931   41.74857  1.000 27.21029  ? 20   LEU A C     1 
ATOM   138  O  O     . LEU A 1 20  ? 12.33193  8.29920   42.88795  1.000 27.21021  ? 20   LEU A O     1 
ATOM   139  C  CB    . LEU A 1 20  ? 10.46019  9.45021   40.91063  1.000 24.90017  ? 20   LEU A CB    1 
ATOM   140  C  CG    . LEU A 1 20  ? 9.58550   10.55878  40.31991  1.000 25.09344  ? 20   LEU A CG    1 
ATOM   141  C  CD1   . LEU A 1 20  ? 8.20906   10.02588  39.94897  1.000 23.95182  ? 20   LEU A CD1   1 
ATOM   142  C  CD2   . LEU A 1 20  ? 9.47242   11.72689  41.28790  1.000 25.33626  ? 20   LEU A CD2   1 
ATOM   143  N  N     . VAL A 1 21  ? 13.65076  8.03128   41.08204  1.000 36.03058  ? 21   VAL A N     1 
ATOM   144  C  CA    . VAL A 1 21  ? 14.38170  6.91388   41.66619  1.000 37.29991  ? 21   VAL A CA    1 
ATOM   145  C  C     . VAL A 1 21  ? 15.26124  7.41322   42.80566  1.000 38.38230  ? 21   VAL A C     1 
ATOM   146  O  O     . VAL A 1 21  ? 15.89855  8.47196   42.70625  1.000 38.83744  ? 21   VAL A O     1 
ATOM   147  C  CB    . VAL A 1 21  ? 15.21071  6.20113   40.58197  1.000 36.81385  ? 21   VAL A CB    1 
ATOM   148  C  CG1   . VAL A 1 21  ? 16.33174  5.37287   41.20014  1.000 37.04039  ? 21   VAL A CG1   1 
ATOM   149  C  CG2   . VAL A 1 21  ? 14.31243  5.32926   39.71772  1.000 35.48876  ? 21   VAL A CG2   1 
ATOM   150  N  N     . ASP A 1 22  ? 15.28446  6.65477   43.90621  1.000 48.92635  ? 22   ASP A N     1 
ATOM   151  C  CA    . ASP A 1 22  ? 16.14360  6.93914   45.05771  1.000 49.42612  ? 22   ASP A CA    1 
ATOM   152  C  C     . ASP A 1 22  ? 15.78319  8.26533   45.72239  1.000 50.01935  ? 22   ASP A C     1 
ATOM   153  O  O     . ASP A 1 22  ? 16.65338  8.97049   46.23916  1.000 51.08222  ? 22   ASP A O     1 
ATOM   154  C  CB    . ASP A 1 22  ? 17.62648  6.92457   44.66617  1.000 50.75459  ? 22   ASP A CB    1 
ATOM   155  C  CG    . ASP A 1 22  ? 18.24546  5.53987   44.75247  1.000 52.20829  ? 22   ASP A CG    1 
ATOM   156  O  OD1   . ASP A 1 22  ? 17.49378  4.54340   44.81278  1.000 51.92936  ? 22   ASP A OD1   1 
ATOM   157  O  OD2   . ASP A 1 22  ? 19.49149  5.44984   44.75656  1.000 53.46902  ? 22   ASP A OD2   1 
ATOM   158  N  N     . ALA A 1 23  ? 14.49997  8.61355   45.71886  1.000 30.96610  ? 23   ALA A N     1 
ATOM   159  C  CA    . ALA A 1 23  ? 14.05112  9.85415   46.33210  1.000 31.31478  ? 23   ALA A CA    1 
ATOM   160  C  C     . ALA A 1 23  ? 14.05518  9.74017   47.85088  1.000 31.86454  ? 23   ALA A C     1 
ATOM   161  O  O     . ALA A 1 23  ? 13.75132  8.68328   48.41153  1.000 31.49537  ? 23   ALA A O     1 
ATOM   162  C  CB    . ALA A 1 23  ? 12.64975  10.21478  45.84160  1.000 29.81492  ? 23   ALA A CB    1 
ATOM   163  N  N     . ASP A 1 24  ? 14.40602  10.83961  48.51418  1.000 34.47975  ? 24   ASP A N     1 
ATOM   164  C  CA    . ASP A 1 24  ? 14.34690  10.94416  49.97054  1.000 34.50095  ? 24   ASP A CA    1 
ATOM   165  C  C     . ASP A 1 24  ? 13.03935  11.65321  50.30902  1.000 34.86836  ? 24   ASP A C     1 
ATOM   166  O  O     . ASP A 1 24  ? 12.93385  12.87582  50.18746  1.000 34.12160  ? 24   ASP A O     1 
ATOM   167  C  CB    . ASP A 1 24  ? 15.56234  11.69118  50.51161  1.000 35.83780  ? 24   ASP A CB    1 
ATOM   168  C  CG    . ASP A 1 24  ? 15.59919  11.73688  52.03052  1.000 37.29458  ? 24   ASP A CG    1 
ATOM   169  O  OD1   . ASP A 1 24  ? 14.67787  11.19528  52.67755  1.000 37.17458  ? 24   ASP A OD1   1 
ATOM   170  O  OD2   . ASP A 1 24  ? 16.56607  12.30413  52.58051  1.000 38.05775  ? 24   ASP A OD2   1 
ATOM   171  N  N     . LEU A 1 25  ? 12.04215  10.87607  50.74068  1.000 33.87641  ? 25   LEU A N     1 
ATOM   172  C  CA    . LEU A 1 25  ? 10.69660  11.41435  50.92078  1.000 33.82939  ? 25   LEU A CA    1 
ATOM   173  C  C     . LEU A 1 25  ? 10.64125  12.47570  52.01217  1.000 34.50568  ? 25   LEU A C     1 
ATOM   174  O  O     . LEU A 1 25  ? 9.75319   13.33593  51.99407  1.000 34.57230  ? 25   LEU A O     1 
ATOM   175  C  CB    . LEU A 1 25  ? 9.72240   10.27985  51.23815  1.000 33.66555  ? 25   LEU A CB    1 
ATOM   176  C  CG    . LEU A 1 25  ? 8.88359   9.72685   50.08471  1.000 33.13118  ? 25   LEU A CG    1 
ATOM   177  C  CD1   . LEU A 1 25  ? 9.75079   9.41855   48.87487  1.000 32.84791  ? 25   LEU A CD1   1 
ATOM   178  C  CD2   . LEU A 1 25  ? 8.13996   8.48062   50.53927  1.000 32.77796  ? 25   LEU A CD2   1 
ATOM   179  N  N     . SER A 1 26  ? 11.57262  12.43827  52.96400  1.000 35.67138  ? 26   SER A N     1 
ATOM   180  C  CA    . SER A 1 26  ? 11.55428  13.38013  54.07489  1.000 36.75214  ? 26   SER A CA    1 
ATOM   181  C  C     . SER A 1 26  ? 12.22856  14.70836  53.75194  1.000 37.02417  ? 26   SER A C     1 
ATOM   182  O  O     . SER A 1 26  ? 12.10845  15.64999  54.54366  1.000 37.54450  ? 26   SER A O     1 
ATOM   183  C  CB    . SER A 1 26  ? 12.21950  12.75186  55.30340  1.000 38.07925  ? 26   SER A CB    1 
ATOM   184  O  OG    . SER A 1 26  ? 13.56267  12.38920  55.03089  1.000 37.88469  ? 26   SER A OG    1 
ATOM   185  N  N     . ARG A 1 27  ? 12.92579  14.81519  52.62072  1.000 34.42172  ? 27   ARG A N     1 
ATOM   186  C  CA    . ARG A 1 27  ? 13.63006  16.04862  52.28924  1.000 34.21160  ? 27   ARG A CA    1 
ATOM   187  C  C     . ARG A 1 27  ? 13.27807  16.55558  50.89644  1.000 33.63995  ? 27   ARG A C     1 
ATOM   188  O  O     . ARG A 1 27  ? 13.34084  17.76166  50.63904  1.000 34.68231  ? 27   ARG A O     1 
ATOM   189  C  CB    . ARG A 1 27  ? 15.14461  15.84855  52.39088  1.000 35.98910  ? 27   ARG A CB    1 
ATOM   190  C  CG    . ARG A 1 27  ? 15.63044  15.32281  53.72954  1.000 35.95642  ? 27   ARG A CG    1 
ATOM   191  C  CD    . ARG A 1 27  ? 17.14017  15.15372  53.72847  1.000 37.07069  ? 27   ARG A CD    1 
ATOM   192  N  NE    . ARG A 1 27  ? 17.74091  15.50547  55.00919  1.000 37.52066  ? 27   ARG A NE    1 
ATOM   193  C  CZ    . ARG A 1 27  ? 18.10958  14.62448  55.92861  1.000 38.32662  ? 27   ARG A CZ    1 
ATOM   194  N  NH1   . ARG A 1 27  ? 17.94402  13.32479  55.74529  1.000 38.41074  ? 27   ARG A NH1   1 
ATOM   195  N  NH2   . ARG A 1 27  ? 18.65975  15.05802  57.05961  1.000 38.92301  ? 27   ARG A NH2   1 
ATOM   196  N  N     . ASP A 1 28  ? 12.91219  15.65179  49.99255  1.000 31.90070  ? 28   ASP A N     1 
ATOM   197  C  CA    . ASP A 1 28  ? 12.72642  16.02738  48.59972  1.000 31.70684  ? 28   ASP A CA    1 
ATOM   198  C  C     . ASP A 1 28  ? 11.33455  16.60560  48.35828  1.000 30.76624  ? 28   ASP A C     1 
ATOM   199  O  O     . ASP A 1 28  ? 10.41310  16.45660  49.16608  1.000 30.99542  ? 28   ASP A O     1 
ATOM   200  C  CB    . ASP A 1 28  ? 12.94570  14.82659  47.67814  1.000 30.48431  ? 28   ASP A CB    1 
ATOM   201  C  CG    . ASP A 1 28  ? 14.38607  14.35791  47.66120  1.000 31.76002  ? 28   ASP A CG    1 
ATOM   202  O  OD1   . ASP A 1 28  ? 15.23872  15.01912  48.29049  1.000 32.32016  ? 28   ASP A OD1   1 
ATOM   203  O  OD2   . ASP A 1 28  ? 14.66576  13.32805  47.01096  1.000 31.64648  ? 28   ASP A OD2   1 
ATOM   204  N  N     . GLN A 1 29  ? 11.19664  17.27323  47.21516  1.000 23.99740  ? 29   GLN A N     1 
ATOM   205  C  CA    . GLN A 1 29  ? 9.92447   17.80484  46.75358  1.000 23.87021  ? 29   GLN A CA    1 
ATOM   206  C  C     . GLN A 1 29  ? 9.78245   17.51675  45.26678  1.000 23.28346  ? 29   GLN A C     1 
ATOM   207  O  O     . GLN A 1 29  ? 10.76377  17.56840  44.51963  1.000 23.36024  ? 29   GLN A O     1 
ATOM   208  C  CB    . GLN A 1 29  ? 9.81336   19.31502  47.01053  1.000 24.24575  ? 29   GLN A CB    1 
ATOM   209  C  CG    . GLN A 1 29  ? 8.40422   19.87321  46.85178  1.000 24.09432  ? 29   GLN A CG    1 
ATOM   210  C  CD    . GLN A 1 29  ? 8.32024   21.36296  47.15125  1.000 24.89909  ? 29   GLN A CD    1 
ATOM   211  O  OE1   . GLN A 1 29  ? 7.64355   21.78315  48.09059  1.000 24.91697  ? 29   GLN A OE1   1 
ATOM   212  N  NE2   . GLN A 1 29  ? 9.00508   22.16784  46.34752  1.000 24.44946  ? 29   GLN A NE2   1 
ATOM   213  N  N     . VAL A 1 30  ? 8.56027   17.20498  44.84631  1.000 23.21453  ? 30   VAL A N     1 
ATOM   214  C  CA    . VAL A 1 30  ? 8.23716   16.98317  43.44233  1.000 22.53738  ? 30   VAL A CA    1 
ATOM   215  C  C     . VAL A 1 30  ? 7.55002   18.23148  42.90825  1.000 22.80088  ? 30   VAL A C     1 
ATOM   216  O  O     . VAL A 1 30  ? 6.59481   18.73174  43.51628  1.000 22.76797  ? 30   VAL A O     1 
ATOM   217  C  CB    . VAL A 1 30  ? 7.34488   15.74238  43.26324  1.000 21.92845  ? 30   VAL A CB    1 
ATOM   218  C  CG1   . VAL A 1 30  ? 6.78727   15.68669  41.84783  1.000 21.31105  ? 30   VAL A CG1   1 
ATOM   219  C  CG2   . VAL A 1 30  ? 8.12329   14.47484  43.58371  1.000 21.77222  ? 30   VAL A CG2   1 
ATOM   220  N  N     . LEU A 1 31  ? 8.03841   18.74147  41.78082  1.000 19.51219  ? 31   LEU A N     1 
ATOM   221  C  CA    . LEU A 1 31  ? 7.45771   19.90325  41.12163  1.000 19.32521  ? 31   LEU A CA    1 
ATOM   222  C  C     . LEU A 1 31  ? 6.73152   19.46096  39.85952  1.000 18.58523  ? 31   LEU A C     1 
ATOM   223  O  O     . LEU A 1 31  ? 7.31336   18.77806  39.00968  1.000 18.16458  ? 31   LEU A O     1 
ATOM   224  C  CB    . LEU A 1 31  ? 8.53167   20.93810  40.77536  1.000 19.56049  ? 31   LEU A CB    1 
ATOM   225  C  CG    . LEU A 1 31  ? 8.06097   22.16360  39.98558  1.000 19.57857  ? 31   LEU A CG    1 
ATOM   226  C  CD1   . LEU A 1 31  ? 7.06930   22.98903  40.79435  1.000 19.94281  ? 31   LEU A CD1   1 
ATOM   227  C  CD2   . LEU A 1 31  ? 9.24503   23.01820  39.54793  1.000 19.88377  ? 31   LEU A CD2   1 
ATOM   228  N  N     . MET A 1 32  ? 5.46137   19.84353  39.74748  1.000 21.06156  ? 32   MET A N     1 
ATOM   229  C  CA    . MET A 1 32  ? 4.66971   19.62819  38.54394  1.000 20.39024  ? 32   MET A CA    1 
ATOM   230  C  C     . MET A 1 32  ? 3.96468   20.92993  38.19923  1.000 21.08457  ? 32   MET A C     1 
ATOM   231  O  O     . MET A 1 32  ? 3.35749   21.55914  39.07170  1.000 21.33568  ? 32   MET A O     1 
ATOM   232  C  CB    . MET A 1 32  ? 3.65041   18.49871  38.72897  1.000 19.35334  ? 32   MET A CB    1 
ATOM   233  C  CG    . MET A 1 32  ? 4.27103   17.11509  38.83587  1.000 18.47511  ? 32   MET A CG    1 
ATOM   234  S  SD    . MET A 1 32  ? 3.08288   15.85935  39.34587  1.000 18.14567  ? 32   MET A SD    1 
ATOM   235  C  CE    . MET A 1 32  ? 2.30204   15.50216  37.77773  1.000 17.30258  ? 32   MET A CE    1 
ATOM   236  N  N     . VAL A 1 33  ? 4.04703   21.33205  36.93366  1.000 17.81943  ? 33   VAL A N     1 
ATOM   237  C  CA    . VAL A 1 33  ? 3.57841   22.63963  36.49264  1.000 18.10006  ? 33   VAL A CA    1 
ATOM   238  C  C     . VAL A 1 33  ? 2.58452   22.45935  35.35610  1.000 17.76609  ? 33   VAL A C     1 
ATOM   239  O  O     . VAL A 1 33  ? 2.87981   21.77798  34.36730  1.000 17.30106  ? 33   VAL A O     1 
ATOM   240  C  CB    . VAL A 1 33  ? 4.74504   23.53755  36.03976  1.000 18.31363  ? 33   VAL A CB    1 
ATOM   241  C  CG1   . VAL A 1 33  ? 4.23269   24.91598  35.64160  1.000 18.75724  ? 33   VAL A CG1   1 
ATOM   242  C  CG2   . VAL A 1 33  ? 5.79074   23.63783  37.13688  1.000 18.71196  ? 33   VAL A CG2   1 
ATOM   243  N  N     . GLU A 1 34  ? 1.41016   23.06886  35.49900  1.000 22.95068  ? 34   GLU A N     1 
ATOM   244  C  CA    . GLU A 1 34  ? 0.47210   23.22155  34.39093  1.000 23.22386  ? 34   GLU A CA    1 
ATOM   245  C  C     . GLU A 1 34  ? 0.88551   24.48962  33.65321  1.000 23.23405  ? 34   GLU A C     1 
ATOM   246  O  O     . GLU A 1 34  ? 0.54779   25.60329  34.06317  1.000 23.57896  ? 34   GLU A O     1 
ATOM   247  C  CB    . GLU A 1 34  ? -0.96585  23.27282  34.89614  1.000 23.83424  ? 34   GLU A CB    1 
ATOM   248  C  CG    . GLU A 1 34  ? -1.38926  22.00041  35.62195  1.000 23.85531  ? 34   GLU A CG    1 
ATOM   249  C  CD    . GLU A 1 34  ? -2.87886  21.93821  35.91298  1.000 25.22651  ? 34   GLU A CD    1 
ATOM   250  O  OE1   . GLU A 1 34  ? -3.56070  22.97719  35.79509  1.000 25.93729  ? 34   GLU A OE1   1 
ATOM   251  O  OE2   . GLU A 1 34  ? -3.36888  20.84199  36.26154  1.000 24.41949  ? 34   GLU A OE2   1 
ATOM   252  N  N     . SER A 1 35  ? 1.63857   24.31664  32.57043  1.000 19.54155  ? 35   SER A N     1 
ATOM   253  C  CA    . SER A 1 35  ? 2.35539   25.40433  31.91880  1.000 19.05830  ? 35   SER A CA    1 
ATOM   254  C  C     . SER A 1 35  ? 1.61298   25.87052  30.67398  1.000 19.30286  ? 35   SER A C     1 
ATOM   255  O  O     . SER A 1 35  ? 1.30511   25.06452  29.78959  1.000 18.79895  ? 35   SER A O     1 
ATOM   256  C  CB    . SER A 1 35  ? 3.77037   24.95949  31.54663  1.000 18.55687  ? 35   SER A CB    1 
ATOM   257  O  OG    . SER A 1 35  ? 4.35551   25.85264  30.61796  1.000 18.57561  ? 35   SER A OG    1 
ATOM   258  N  N     . ARG A 1 36  ? 1.34133   27.17530  30.60247  1.000 25.76359  ? 36   ARG A N     1 
ATOM   259  C  CA    . ARG A 1 36  ? 0.70656   27.74331  29.42072  1.000 25.22496  ? 36   ARG A CA    1 
ATOM   260  C  C     . ARG A 1 36  ? 1.68670   27.94631  28.27286  1.000 25.21249  ? 36   ARG A C     1 
ATOM   261  O  O     . ARG A 1 36  ? 1.25583   28.04089  27.11778  1.000 24.99778  ? 36   ARG A O     1 
ATOM   262  C  CB    . ARG A 1 36  ? 0.02579   29.06784  29.77192  1.000 26.85961  ? 36   ARG A CB    1 
ATOM   263  C  CG    . ARG A 1 36  ? -1.25208  28.89808  30.57853  1.000 27.14001  ? 36   ARG A CG    1 
ATOM   264  C  CD    . ARG A 1 36  ? -1.84641  30.23548  30.98604  1.000 27.80726  ? 36   ARG A CD    1 
ATOM   265  N  NE    . ARG A 1 36  ? -3.04271  30.06065  31.80006  1.000 28.73839  ? 36   ARG A NE    1 
ATOM   266  C  CZ    . ARG A 1 36  ? -4.26599  29.91962  31.30892  1.000 29.08190  ? 36   ARG A CZ    1 
ATOM   267  N  NH1   . ARG A 1 36  ? -4.49511  29.95023  30.00638  1.000 28.53942  ? 36   ARG A NH1   1 
ATOM   268  N  NH2   . ARG A 1 36  ? -5.28416  29.73804  32.14524  1.000 30.21423  ? 36   ARG A NH2   1 
ATOM   269  N  N     . VAL A 1 37  ? 2.98760   28.02427  28.56201  1.000 22.45728  ? 37   VAL A N     1 
ATOM   270  C  CA    . VAL A 1 37  ? 3.98823   27.95855  27.49968  1.000 21.81884  ? 37   VAL A CA    1 
ATOM   271  C  C     . VAL A 1 37  ? 3.86489   26.63800  26.75088  1.000 21.75874  ? 37   VAL A C     1 
ATOM   272  O  O     . VAL A 1 37  ? 3.78823   26.60415  25.51674  1.000 21.10060  ? 37   VAL A O     1 
ATOM   273  C  CB    . VAL A 1 37  ? 5.40231   28.14252  28.07945  1.000 22.41465  ? 37   VAL A CB    1 
ATOM   274  C  CG1   . VAL A 1 37  ? 6.45773   27.80940  27.03104  1.000 21.43682  ? 37   VAL A CG1   1 
ATOM   275  C  CG2   . VAL A 1 37  ? 5.58516   29.55268  28.59879  1.000 22.84034  ? 37   VAL A CG2   1 
ATOM   276  N  N     . GLU A 1 38  ? 3.83654   25.52833  27.49397  1.000 25.11450  ? 38   GLU A N     1 
ATOM   277  C  CA    . GLU A 1 38  ? 3.67971   24.21719  26.87527  1.000 24.67868  ? 38   GLU A CA    1 
ATOM   278  C  C     . GLU A 1 38  ? 2.29561   24.04627  26.26327  1.000 25.13612  ? 38   GLU A C     1 
ATOM   279  O  O     . GLU A 1 38  ? 2.14830   23.35317  25.25023  1.000 24.81564  ? 38   GLU A O     1 
ATOM   280  C  CB    . GLU A 1 38  ? 3.93792   23.11736  27.90640  1.000 24.83420  ? 38   GLU A CB    1 
ATOM   281  C  CG    . GLU A 1 38  ? 5.31449   23.17107  28.55340  1.000 24.98227  ? 38   GLU A CG    1 
ATOM   282  C  CD    . GLU A 1 38  ? 6.43388   23.23790  27.53497  1.000 25.30154  ? 38   GLU A CD    1 
ATOM   283  O  OE1   . GLU A 1 38  ? 6.44797   22.39726  26.61077  1.000 25.01131  ? 38   GLU A OE1   1 
ATOM   284  O  OE2   . GLU A 1 38  ? 7.29790   24.13258  27.65631  1.000 25.71035  ? 38   GLU A OE2   1 
ATOM   285  N  N     . ALA A 1 39  ? 1.27396   24.66548  26.85914  1.000 25.13322  ? 39   ALA A N     1 
ATOM   286  C  CA    . ALA A 1 39  ? -0.08293  24.53100  26.34481  1.000 25.12506  ? 39   ALA A CA    1 
ATOM   287  C  C     . ALA A 1 39  ? -0.29937  25.31971  25.06148  1.000 25.94370  ? 39   ALA A C     1 
ATOM   288  O  O     . ALA A 1 39  ? -1.24600  25.02671  24.32281  1.000 26.11030  ? 39   ALA A O     1 
ATOM   289  C  CB    . ALA A 1 39  ? -1.09367  24.97639  27.40216  1.000 26.51971  ? 39   ALA A CB    1 
ATOM   290  N  N     . THR A 1 40  ? 0.54880   26.31001  24.78054  1.000 19.23362  ? 40   THR A N     1 
ATOM   291  C  CA    . THR A 1 40  ? 0.40607   27.13876  23.59320  1.000 19.95394  ? 40   THR A CA    1 
ATOM   292  C  C     . THR A 1 40  ? 1.60840   27.08109  22.66078  1.000 20.00613  ? 40   THR A C     1 
ATOM   293  O  O     . THR A 1 40  ? 1.60643   27.78013  21.64005  1.000 20.71157  ? 40   THR A O     1 
ATOM   294  C  CB    . THR A 1 40  ? 0.14177   28.60067  23.98461  1.000 20.82494  ? 40   THR A CB    1 
ATOM   295  O  OG1   . THR A 1 40  ? 1.26482   29.11364  24.71059  1.000 20.89816  ? 40   THR A OG1   1 
ATOM   296  C  CG2   . THR A 1 40  ? -1.11270  28.70873  24.84352  1.000 20.91971  ? 40   THR A CG2   1 
ATOM   297  N  N     . ALA A 1 41  ? 2.63927   26.29222  22.98368  1.000 23.84529  ? 41   ALA A N     1 
ATOM   298  C  CA    . ALA A 1 41  ? 3.71596   26.05222  22.02569  1.000 23.88839  ? 41   ALA A CA    1 
ATOM   299  C  C     . ALA A 1 41  ? 3.13847   25.60371  20.69085  1.000 23.71677  ? 41   ALA A C     1 
ATOM   300  O  O     . ALA A 1 41  ? 3.49902   26.12366  19.62894  1.000 24.22533  ? 41   ALA A O     1 
ATOM   301  C  CB    . ALA A 1 41  ? 4.69095   25.01080  22.57722  1.000 23.04032  ? 41   ALA A CB    1 
ATOM   302  N  N     . TRP A 1 42  ? 2.23916   24.62955  20.73568  1.000 25.77326  ? 42   TRP A N     1 
ATOM   303  C  CA    . TRP A 1 42  ? 1.23657   24.42027  19.70724  1.000 26.17001  ? 42   TRP A CA    1 
ATOM   304  C  C     . TRP A 1 42  ? -0.12982  24.56184  20.35697  1.000 26.59402  ? 42   TRP A C     1 
ATOM   305  O  O     . TRP A 1 42  ? -0.28748  24.32992  21.55912  1.000 26.60630  ? 42   TRP A O     1 
ATOM   306  C  CB    . TRP A 1 42  ? 1.35522   23.04334  19.04875  1.000 26.02974  ? 42   TRP A CB    1 
ATOM   307  C  CG    . TRP A 1 42  ? 2.64558   22.82327  18.34066  1.000 25.68108  ? 42   TRP A CG    1 
ATOM   308  C  CD1   . TRP A 1 42  ? 2.91188   23.06777  17.02524  1.000 25.62053  ? 42   TRP A CD1   1 
ATOM   309  C  CD2   . TRP A 1 42  ? 3.85233   22.30424  18.90616  1.000 25.06992  ? 42   TRP A CD2   1 
ATOM   310  N  NE1   . TRP A 1 42  ? 4.21250   22.73451  16.73728  1.000 25.26373  ? 42   TRP A NE1   1 
ATOM   311  C  CE2   . TRP A 1 42  ? 4.81175   22.26401  17.87615  1.000 24.99693  ? 42   TRP A CE2   1 
ATOM   312  C  CE3   . TRP A 1 42  ? 4.21590   21.87233  20.18475  1.000 24.93631  ? 42   TRP A CE3   1 
ATOM   313  C  CZ2   . TRP A 1 42  ? 6.10983   21.80729  18.08470  1.000 25.31841  ? 42   TRP A CZ2   1 
ATOM   314  C  CZ3   . TRP A 1 42  ? 5.50446   21.42086  20.38998  1.000 24.12097  ? 42   TRP A CZ3   1 
ATOM   315  C  CH2   . TRP A 1 42  ? 6.43599   21.39144  19.34620  1.000 24.82647  ? 42   TRP A CH2   1 
ATOM   316  N  N     . LYS A 1 43  ? -1.12039  24.94876  19.55958  1.000 27.13373  ? 43   LYS A N     1 
ATOM   317  C  CA    . LYS A 1 43  ? -2.48070  25.09330  20.06809  1.000 28.23003  ? 43   LYS A CA    1 
ATOM   318  C  C     . LYS A 1 43  ? -3.11760  23.70754  20.08662  1.000 27.92246  ? 43   LYS A C     1 
ATOM   319  O  O     . LYS A 1 43  ? -3.95565  23.35562  19.25317  1.000 28.28664  ? 43   LYS A O     1 
ATOM   320  C  CB    . LYS A 1 43  ? -3.25964  26.08194  19.21915  1.000 29.36797  ? 43   LYS A CB    1 
ATOM   321  C  CG    . LYS A 1 43  ? -3.30493  27.44907  19.84006  1.000 30.18168  ? 43   LYS A CG    1 
ATOM   322  C  CD    . LYS A 1 43  ? -3.76827  28.47441  18.84835  1.000 31.50094  ? 43   LYS A CD    1 
ATOM   323  C  CE    . LYS A 1 43  ? -4.20158  29.70852  19.57787  1.000 33.09086  ? 43   LYS A CE    1 
ATOM   324  N  NZ    . LYS A 1 43  ? -5.60672  29.49577  19.94835  1.000 33.99441  ? 43   LYS A NZ    1 
ATOM   325  N  N     . HIS A 1 44  ? -2.69948  22.91420  21.07236  1.000 21.19949  ? 44   HIS A N     1 
ATOM   326  C  CA    . HIS A 1 44  ? -3.04220  21.49917  21.12277  1.000 21.66905  ? 44   HIS A CA    1 
ATOM   327  C  C     . HIS A 1 44  ? -4.55000  21.28828  21.08120  1.000 22.54031  ? 44   HIS A C     1 
ATOM   328  O  O     . HIS A 1 44  ? -5.33192  22.13077  21.53119  1.000 23.35023  ? 44   HIS A O     1 
ATOM   329  C  CB    . HIS A 1 44  ? -2.47895  20.85821  22.39232  1.000 21.04693  ? 44   HIS A CB    1 
ATOM   330  C  CG    . HIS A 1 44  ? -1.01529  21.09247  22.59376  1.000 20.38766  ? 44   HIS A CG    1 
ATOM   331  N  ND1   . HIS A 1 44  ? -0.04758  20.38559  21.91305  1.000 19.53878  ? 44   HIS A ND1   1 
ATOM   332  C  CD2   . HIS A 1 44  ? -0.35361  21.94797  23.40868  1.000 20.06048  ? 44   HIS A CD2   1 
ATOM   333  C  CE1   . HIS A 1 44  ? 1.14732   20.79979  22.29519  1.000 19.44096  ? 44   HIS A CE1   1 
ATOM   334  N  NE2   . HIS A 1 44  ? 0.98960   21.74780  23.20173  1.000 19.95559  ? 44   HIS A NE2   1 
ATOM   335  N  N     . HIS A 1 45  ? -4.94788  20.14987  20.51135  1.000 18.45135  ? 45   HIS A N     1 
ATOM   336  C  CA    . HIS A 1 45  ? -6.32631  19.68813  20.60094  1.000 18.73746  ? 45   HIS A CA    1 
ATOM   337  C  C     . HIS A 1 45  ? -6.82902  19.82084  22.03045  1.000 18.64469  ? 45   HIS A C     1 
ATOM   338  O  O     . HIS A 1 45  ? -6.11479  19.50538  22.98590  1.000 18.09093  ? 45   HIS A O     1 
ATOM   339  C  CB    . HIS A 1 45  ? -6.41787  18.22771  20.15021  1.000 18.40609  ? 45   HIS A CB    1 
ATOM   340  C  CG    . HIS A 1 45  ? -7.79620  17.79346  19.76297  1.000 18.93100  ? 45   HIS A CG    1 
ATOM   341  N  ND1   . HIS A 1 45  ? -8.85733  17.80652  20.64207  1.000 19.18208  ? 45   HIS A ND1   1 
ATOM   342  C  CD2   . HIS A 1 45  ? -8.28518  17.32580  18.59016  1.000 19.34699  ? 45   HIS A CD2   1 
ATOM   343  C  CE1   . HIS A 1 45  ? -9.94069  17.36665  20.02775  1.000 19.73492  ? 45   HIS A CE1   1 
ATOM   344  N  NE2   . HIS A 1 45  ? -9.62080  17.06873  18.78144  1.000 19.84217  ? 45   HIS A NE2   1 
ATOM   345  N  N     . LYS A 1 46  ? -8.06254  20.30973  22.17267  1.000 20.17211  ? 46   LYS A N     1 
ATOM   346  C  CA    . LYS A 1 46  ? -8.63742  20.46517  23.50338  1.000 21.05998  ? 46   LYS A CA    1 
ATOM   347  C  C     . LYS A 1 46  ? -8.62755  19.15140  24.27752  1.000 20.65353  ? 46   LYS A C     1 
ATOM   348  O  O     . LYS A 1 46  ? -8.41418  19.15048  25.49511  1.000 20.83416  ? 46   LYS A O     1 
ATOM   349  C  CB    . LYS A 1 46  ? -10.06003 21.00629  23.40098  1.000 22.66478  ? 46   LYS A CB    1 
ATOM   350  C  CG    . LYS A 1 46  ? -10.20375 22.36439  22.72818  1.000 23.45932  ? 46   LYS A CG    1 
ATOM   351  C  CD    . LYS A 1 46  ? -11.50017 23.04035  23.16606  1.000 24.17269  ? 46   LYS A CD    1 
ATOM   352  C  CE    . LYS A 1 46  ? -11.93438 24.14649  22.21951  1.000 24.81552  ? 46   LYS A CE    1 
ATOM   353  N  NZ    . LYS A 1 46  ? -12.69465 23.61079  21.05643  1.000 24.74044  ? 46   LYS A NZ    1 
ATOM   354  N  N     . GLN A 1 47  ? -8.83853  18.02478  23.59267  1.000 18.83138  ? 47   GLN A N     1 
ATOM   355  C  CA    . GLN A 1 47  ? -8.80181  16.73474  24.27458  1.000 18.45808  ? 47   GLN A CA    1 
ATOM   356  C  C     . GLN A 1 47  ? -7.40373  16.40333  24.78062  1.000 17.54396  ? 47   GLN A C     1 
ATOM   357  O  O     . GLN A 1 47  ? -7.26411  15.72144  25.80197  1.000 17.29924  ? 47   GLN A O     1 
ATOM   358  C  CB    . GLN A 1 47  ? -9.30521  15.62838  23.34678  1.000 18.58477  ? 47   GLN A CB    1 
ATOM   359  C  CG    . GLN A 1 47  ? -10.80748 15.64970  23.11724  1.000 19.95542  ? 47   GLN A CG    1 
ATOM   360  C  CD    . GLN A 1 47  ? -11.31776 14.38036  22.46223  1.000 20.82816  ? 47   GLN A CD    1 
ATOM   361  O  OE1   . GLN A 1 47  ? -10.74395 13.30423  22.63617  1.000 20.03693  ? 47   GLN A OE1   1 
ATOM   362  N  NE2   . GLN A 1 47  ? -12.40338 14.49937  21.70538  1.000 21.43216  ? 47   GLN A NE2   1 
ATOM   363  N  N     . LYS A 1 48  ? -6.35980  16.86807  24.08963  1.000 22.74436  ? 48   LYS A N     1 
ATOM   364  C  CA    . LYS A 1 48  ? -5.00640  16.63396  24.58290  1.000 21.39099  ? 48   LYS A CA    1 
ATOM   365  C  C     . LYS A 1 48  ? -4.73371  17.44428  25.84372  1.000 21.74635  ? 48   LYS A C     1 
ATOM   366  O  O     . LYS A 1 48  ? -4.02635  16.97947  26.74590  1.000 20.55261  ? 48   LYS A O     1 
ATOM   367  C  CB    . LYS A 1 48  ? -3.97660  16.96407  23.50472  1.000 20.39899  ? 48   LYS A CB    1 
ATOM   368  C  CG    . LYS A 1 48  ? -2.57226  16.50149  23.86293  1.000 19.40178  ? 48   LYS A CG    1 
ATOM   369  C  CD    . LYS A 1 48  ? -1.50923  17.27114  23.10385  1.000 19.53408  ? 48   LYS A CD    1 
ATOM   370  C  CE    . LYS A 1 48  ? -1.53744  16.93274  21.62305  1.000 19.14332  ? 48   LYS A CE    1 
ATOM   371  N  NZ    . LYS A 1 48  ? -0.45405  17.61769  20.86908  1.000 18.58445  ? 48   LYS A NZ    1 
ATOM   372  N  N     . LEU A 1 49  ? -5.27872  18.66152  25.92191  1.000 17.20993  ? 49   LEU A N     1 
ATOM   373  C  CA    . LEU A 1 49  ? -5.14828  19.44441  27.14581  1.000 17.71255  ? 49   LEU A CA    1 
ATOM   374  C  C     . LEU A 1 49  ? -5.87262  18.77034  28.30390  1.000 18.06728  ? 49   LEU A C     1 
ATOM   375  O  O     . LEU A 1 49  ? -5.35845  18.72775  29.42836  1.000 17.65288  ? 49   LEU A O     1 
ATOM   376  C  CB    . LEU A 1 49  ? -5.68590  20.85830  26.92781  1.000 18.58644  ? 49   LEU A CB    1 
ATOM   377  C  CG    . LEU A 1 49  ? -5.04063  21.69683  25.82311  1.000 18.52594  ? 49   LEU A CG    1 
ATOM   378  C  CD1   . LEU A 1 49  ? -5.79796  23.00365  25.64434  1.000 19.24368  ? 49   LEU A CD1   1 
ATOM   379  C  CD2   . LEU A 1 49  ? -3.57866  21.96729  26.13223  1.000 17.78801  ? 49   LEU A CD2   1 
ATOM   380  N  N     . VAL A 1 50  ? -7.07092  18.23901  28.04773  1.000 18.17400  ? 50   VAL A N     1 
ATOM   381  C  CA    . VAL A 1 50  ? -7.80853  17.52882  29.08900  1.000 18.78501  ? 50   VAL A CA    1 
ATOM   382  C  C     . VAL A 1 50  ? -7.04916  16.28110  29.51578  1.000 17.38641  ? 50   VAL A C     1 
ATOM   383  O  O     . VAL A 1 50  ? -6.93911  15.98068  30.71065  1.000 17.42723  ? 50   VAL A O     1 
ATOM   384  C  CB    . VAL A 1 50  ? -9.22969  17.18591  28.60251  1.000 19.66640  ? 50   VAL A CB    1 
ATOM   385  C  CG1   . VAL A 1 50  ? -9.94240  16.29653  29.61573  1.000 19.31833  ? 50   VAL A CG1   1 
ATOM   386  C  CG2   . VAL A 1 50  ? -10.02614 18.45311  28.34922  1.000 21.02102  ? 50   VAL A CG2   1 
ATOM   387  N  N     . LEU A 1 51  ? -6.50015  15.54495  28.54668  1.000 19.73570  ? 51   LEU A N     1 
ATOM   388  C  CA    . LEU A 1 51  ? -5.78963  14.30872  28.85634  1.000 18.21885  ? 51   LEU A CA    1 
ATOM   389  C  C     . LEU A 1 51  ? -4.58901  14.56938  29.75779  1.000 17.85997  ? 51   LEU A C     1 
ATOM   390  O  O     . LEU A 1 51  ? -4.46355  13.97071  30.83234  1.000 17.46487  ? 51   LEU A O     1 
ATOM   391  C  CB    . LEU A 1 51  ? -5.35029  13.62480  27.56213  1.000 17.78367  ? 51   LEU A CB    1 
ATOM   392  C  CG    . LEU A 1 51  ? -4.45944  12.39257  27.72299  1.000 17.00209  ? 51   LEU A CG    1 
ATOM   393  C  CD1   . LEU A 1 51  ? -5.08945  11.38454  28.66915  1.000 16.69266  ? 51   LEU A CD1   1 
ATOM   394  C  CD2   . LEU A 1 51  ? -4.18170  11.76113  26.37190  1.000 16.96958  ? 51   LEU A CD2   1 
ATOM   395  N  N     . VAL A 1 52  ? -3.69269  15.46271  29.33502  1.000 23.33183  ? 52   VAL A N     1 
ATOM   396  C  CA    . VAL A 1 52  ? -2.45858  15.68376  30.08443  1.000 22.66985  ? 52   VAL A CA    1 
ATOM   397  C  C     . VAL A 1 52  ? -2.76806  16.23123  31.47325  1.000 23.22488  ? 52   VAL A C     1 
ATOM   398  O  O     . VAL A 1 52  ? -2.31399  15.68960  32.48680  1.000 22.72823  ? 52   VAL A O     1 
ATOM   399  C  CB    . VAL A 1 52  ? -1.51339  16.61545  29.30418  1.000 22.15237  ? 52   VAL A CB    1 
ATOM   400  C  CG1   . VAL A 1 52  ? -0.27598  16.93378  30.13050  1.000 21.85601  ? 52   VAL A CG1   1 
ATOM   401  C  CG2   . VAL A 1 52  ? -1.12158  15.98171  27.98014  1.000 21.43903  ? 52   VAL A CG2   1 
ATOM   402  N  N     . TRP A 1 53  ? -3.57225  17.29363  31.54366  1.000 19.02970  ? 53   TRP A N     1 
ATOM   403  C  CA    . TRP A 1 53  ? -3.77289  17.97495  32.81979  1.000 19.71912  ? 53   TRP A CA    1 
ATOM   404  C  C     . TRP A 1 53  ? -4.53665  17.10828  33.81461  1.000 19.76830  ? 53   TRP A C     1 
ATOM   405  O  O     . TRP A 1 53  ? -4.21273  17.10092  35.00730  1.000 20.19478  ? 53   TRP A O     1 
ATOM   406  C  CB    . TRP A 1 53  ? -4.48308  19.30561  32.59444  1.000 20.87685  ? 53   TRP A CB    1 
ATOM   407  C  CG    . TRP A 1 53  ? -3.55485  20.34381  32.06445  1.000 21.74130  ? 53   TRP A CG    1 
ATOM   408  C  CD1   . TRP A 1 53  ? -2.20763  20.41756  32.27139  1.000 20.63452  ? 53   TRP A CD1   1 
ATOM   409  C  CD2   . TRP A 1 53  ? -3.89338  21.44839  31.22296  1.000 21.82277  ? 53   TRP A CD2   1 
ATOM   410  N  NE1   . TRP A 1 53  ? -1.68752  21.50522  31.61567  1.000 20.37141  ? 53   TRP A NE1   1 
ATOM   411  C  CE2   . TRP A 1 53  ? -2.70264  22.15500  30.96385  1.000 22.23393  ? 53   TRP A CE2   1 
ATOM   412  C  CE3   . TRP A 1 53  ? -5.08852  21.91158  30.66574  1.000 23.36369  ? 53   TRP A CE3   1 
ATOM   413  C  CZ2   . TRP A 1 53  ? -2.67305  23.30021  30.17380  1.000 22.13694  ? 53   TRP A CZ2   1 
ATOM   414  C  CZ3   . TRP A 1 53  ? -5.05730  23.04582  29.88099  1.000 23.59648  ? 53   TRP A CZ3   1 
ATOM   415  C  CH2   . TRP A 1 53  ? -3.85766  23.72760  29.64114  1.000 22.92548  ? 53   TRP A CH2   1 
ATOM   416  N  N     . SER A 1 54  ? -5.55176  16.37396  33.35435  1.000 23.06004  ? 54   SER A N     1 
ATOM   417  C  CA    . SER A 1 54  ? -6.23433  15.44333  34.24910  1.000 23.28778  ? 54   SER A CA    1 
ATOM   418  C  C     . SER A 1 54  ? -5.28194  14.36520  34.74801  1.000 21.92721  ? 54   SER A C     1 
ATOM   419  O  O     . SER A 1 54  ? -5.32561  13.98132  35.92242  1.000 22.37544  ? 54   SER A O     1 
ATOM   420  C  CB    . SER A 1 54  ? -7.43187  14.80641  33.54562  1.000 23.40842  ? 54   SER A CB    1 
ATOM   421  O  OG    . SER A 1 54  ? -7.94999  13.72849  34.30584  1.000 23.60198  ? 54   SER A OG    1 
ATOM   422  N  N     . ALA A 1 55  ? -4.40616  13.87164  33.87049  1.000 18.30190  ? 55   ALA A N     1 
ATOM   423  C  CA    . ALA A 1 55  ? -3.48650  12.80933  34.26183  1.000 16.91922  ? 55   ALA A CA    1 
ATOM   424  C  C     . ALA A 1 55  ? -2.42054  13.31577  35.22874  1.000 17.31060  ? 55   ALA A C     1 
ATOM   425  O  O     . ALA A 1 55  ? -2.05129  12.60540  36.17147  1.000 17.13803  ? 55   ALA A O     1 
ATOM   426  C  CB    . ALA A 1 55  ? -2.84549  12.18952  33.02153  1.000 16.39439  ? 55   ALA A CB    1 
ATOM   427  N  N     . MET A 1 56  ? -1.90454  14.53344  35.01447  1.000 19.35490  ? 56   MET A N     1 
ATOM   428  C  CA    . MET A 1 56  ? -0.93708  15.08515  35.96267  1.000 19.69071  ? 56   MET A CA    1 
ATOM   429  C  C     . MET A 1 56  ? -1.55031  15.26526  37.34475  1.000 20.23109  ? 56   MET A C     1 
ATOM   430  O  O     . MET A 1 56  ? -0.91307  14.95375  38.35795  1.000 20.47626  ? 56   MET A O     1 
ATOM   431  C  CB    . MET A 1 56  ? -0.36100  16.41592  35.46609  1.000 19.75250  ? 56   MET A CB    1 
ATOM   432  C  CG    . MET A 1 56  ? 0.18979   16.41417  34.05140  1.000 19.15597  ? 56   MET A CG    1 
ATOM   433  S  SD    . MET A 1 56  ? 0.62747   18.07183  33.47274  1.000 20.29124  ? 56   MET A SD    1 
ATOM   434  C  CE    . MET A 1 56  ? 1.55538   18.69486  34.87232  1.000 20.59807  ? 56   MET A CE    1 
ATOM   435  N  N     . ARG A 1 57  ? -2.78392  15.76848  37.40907  1.000 20.66204  ? 57   ARG A N     1 
ATOM   436  C  CA    . ARG A 1 57  ? -3.41828  15.99162  38.70385  1.000 21.51040  ? 57   ARG A CA    1 
ATOM   437  C  C     . ARG A 1 57  ? -3.60837  14.68179  39.45916  1.000 21.15103  ? 57   ARG A C     1 
ATOM   438  O  O     . ARG A 1 57  ? -3.39488  14.62164  40.67524  1.000 21.52110  ? 57   ARG A O     1 
ATOM   439  C  CB    . ARG A 1 57  ? -4.75163  16.71040  38.51045  1.000 21.95327  ? 57   ARG A CB    1 
ATOM   440  C  CG    . ARG A 1 57  ? -4.59357  18.14415  38.03621  1.000 23.43032  ? 57   ARG A CG    1 
ATOM   441  C  CD    . ARG A 1 57  ? -5.93055  18.81342  37.78313  1.000 24.36090  ? 57   ARG A CD    1 
ATOM   442  N  NE    . ARG A 1 57  ? -5.75578  20.18577  37.32215  1.000 25.58906  ? 57   ARG A NE    1 
ATOM   443  C  CZ    . ARG A 1 57  ? -6.73830  21.06713  37.19678  1.000 27.06888  ? 57   ARG A CZ    1 
ATOM   444  N  NH1   . ARG A 1 57  ? -7.98882  20.75620  37.49779  1.000 26.40743  ? 57   ARG A NH1   1 
ATOM   445  N  NH2   . ARG A 1 57  ? -6.45911  22.29132  36.75738  1.000 27.04033  ? 57   ARG A NH2   1 
ATOM   446  N  N     . GLN A 1 58  ? -3.99716  13.61766  38.75518  1.000 21.18348  ? 58   GLN A N     1 
ATOM   447  C  CA    . GLN A 1 58  ? -4.14684  12.32458  39.41369  1.000 21.59850  ? 58   GLN A CA    1 
ATOM   448  C  C     . GLN A 1 58  ? -2.79069  11.72715  39.76759  1.000 20.59284  ? 58   GLN A C     1 
ATOM   449  O  O     . GLN A 1 58  ? -2.63766  11.10911  40.82770  1.000 20.86664  ? 58   GLN A O     1 
ATOM   450  C  CB    . GLN A 1 58  ? -4.94479  11.37194  38.52508  1.000 20.57240  ? 58   GLN A CB    1 
ATOM   451  C  CG    . GLN A 1 58  ? -6.32860  11.88637  38.17560  1.000 21.50087  ? 58   GLN A CG    1 
ATOM   452  C  CD    . GLN A 1 58  ? -7.09005  10.94390  37.26849  1.000 21.78548  ? 58   GLN A CD    1 
ATOM   453  O  OE1   . GLN A 1 58  ? -7.43702  9.82968   37.66261  1.000 21.36095  ? 58   GLN A OE1   1 
ATOM   454  N  NE2   . GLN A 1 58  ? -7.35886  11.38771  36.04655  1.000 21.52657  ? 58   GLN A NE2   1 
ATOM   455  N  N     . PHE A 1 59  ? -1.79378  11.90680  38.89537  1.000 20.10783  ? 59   PHE A N     1 
ATOM   456  C  CA    . PHE A 1 59  ? -0.45072  11.41616  39.19105  1.000 19.72208  ? 59   PHE A CA    1 
ATOM   457  C  C     . PHE A 1 59  ? 0.12532   12.09760  40.42670  1.000 20.26681  ? 59   PHE A C     1 
ATOM   458  O  O     . PHE A 1 59  ? 0.83893   11.46756  41.21661  1.000 20.40557  ? 59   PHE A O     1 
ATOM   459  C  CB    . PHE A 1 59  ? 0.46497   11.62804  37.98365  1.000 18.92004  ? 59   PHE A CB    1 
ATOM   460  C  CG    . PHE A 1 59  ? 1.83555   11.03173  38.14941  1.000 19.08500  ? 59   PHE A CG    1 
ATOM   461  C  CD1   . PHE A 1 59  ? 2.00140   9.66157   38.26012  1.000 18.85813  ? 59   PHE A CD1   1 
ATOM   462  C  CD2   . PHE A 1 59  ? 2.95693   11.84218  38.20520  1.000 19.03137  ? 59   PHE A CD2   1 
ATOM   463  C  CE1   . PHE A 1 59  ? 3.26091   9.10872   38.41797  1.000 19.13856  ? 59   PHE A CE1   1 
ATOM   464  C  CE2   . PHE A 1 59  ? 4.21896   11.29539  38.36314  1.000 19.66098  ? 59   PHE A CE2   1 
ATOM   465  C  CZ    . PHE A 1 59  ? 4.37042   9.92754   38.47017  1.000 19.04179  ? 59   PHE A CZ    1 
ATOM   466  N  N     . ALA A 1 60  ? -0.17547  13.38612  40.61137  1.000 18.58638  ? 60   ALA A N     1 
ATOM   467  C  CA    . ALA A 1 60  ? 0.27388   14.08711  41.81005  1.000 19.12925  ? 60   ALA A CA    1 
ATOM   468  C  C     . ALA A 1 60  ? -0.38770  13.52301  43.06300  1.000 19.94599  ? 60   ALA A C     1 
ATOM   469  O  O     . ALA A 1 60  ? 0.27999   13.31531  44.08328  1.000 20.47872  ? 60   ALA A O     1 
ATOM   470  C  CB    . ALA A 1 60  ? -0.00438  15.58403  41.67740  1.000 19.11396  ? 60   ALA A CB    1 
ATOM   471  N  N     . GLU A 1 61  ? -1.69847  13.26735  43.00799  1.000 31.44359  ? 61   GLU A N     1 
ATOM   472  C  CA    . GLU A 1 61  ? -2.37289  12.65256  44.14693  1.000 31.47591  ? 61   GLU A CA    1 
ATOM   473  C  C     . GLU A 1 61  ? -1.82649  11.26038  44.42756  1.000 31.28879  ? 61   GLU A C     1 
ATOM   474  O  O     . GLU A 1 61  ? -1.77359  10.83567  45.58815  1.000 31.61078  ? 61   GLU A O     1 
ATOM   475  C  CB    . GLU A 1 61  ? -3.88134  12.59918  43.90401  1.000 32.05487  ? 61   GLU A CB    1 
ATOM   476  C  CG    . GLU A 1 61  ? -4.59788  13.93022  44.10565  0.747 34.24650  ? 61   GLU A CG    1 
ATOM   477  C  CD    . GLU A 1 61  ? -4.23662  14.60067  45.42222  1.000 35.57538  ? 61   GLU A CD    1 
ATOM   478  O  OE1   . GLU A 1 61  ? -4.89741  14.31283  46.44350  0.459 35.93083  ? 61   GLU A OE1   1 
ATOM   479  O  OE2   . GLU A 1 61  ? -3.30347  15.43196  45.43037  0.625 34.60066  ? 61   GLU A OE2   1 
ATOM   480  N  N     A ARG A 1 62  ? -1.41184  10.53262  43.38632  0.674 25.13766  ? 62   ARG A N     1 
ATOM   481  N  N     B ARG A 1 62  ? -1.41553  10.54365  43.37949  0.326 25.13846  ? 62   ARG A N     1 
ATOM   482  C  CA    A ARG A 1 62  ? -0.80636  9.22072   43.59987  0.674 24.82842  ? 62   ARG A CA    1 
ATOM   483  C  CA    B ARG A 1 62  ? -0.80237  9.23479   43.56712  0.326 24.81857  ? 62   ARG A CA    1 
ATOM   484  C  C     A ARG A 1 62  ? 0.53513   9.34280   44.31137  0.674 25.13592  ? 62   ARG A C     1 
ATOM   485  C  C     B ARG A 1 62  ? 0.52179   9.35220   44.30846  0.326 25.13468  ? 62   ARG A C     1 
ATOM   486  O  O     A ARG A 1 62  ? 0.86937   8.51315   45.16534  0.674 25.31907  ? 62   ARG A O     1 
ATOM   487  O  O     B ARG A 1 62  ? 0.83247   8.52841   45.17687  0.326 25.32773  ? 62   ARG A O     1 
ATOM   488  C  CB    A ARG A 1 62  ? -0.63756  8.49034   42.26637  0.674 24.38218  ? 62   ARG A CB    1 
ATOM   489  C  CB    B ARG A 1 62  ? -0.59419  8.55504   42.21352  0.326 24.37601  ? 62   ARG A CB    1 
ATOM   490  C  CG    A ARG A 1 62  ? -1.93363  7.97459   41.66379  0.674 24.40256  ? 62   ARG A CG    1 
ATOM   491  C  CG    B ARG A 1 62  ? -1.87535  8.11267   41.52745  0.326 24.37599  ? 62   ARG A CG    1 
ATOM   492  C  CD    A ARG A 1 62  ? -1.68058  6.84700   40.66989  0.674 24.18224  ? 62   ARG A CD    1 
ATOM   493  C  CD    B ARG A 1 62  ? -1.61722  7.61427   40.11711  0.326 24.04371  ? 62   ARG A CD    1 
ATOM   494  N  NE    A ARG A 1 62  ? -1.01401  7.30724   39.45566  0.674 23.50072  ? 62   ARG A NE    1 
ATOM   495  N  NE    B ARG A 1 62  ? -1.02383  6.28388   40.15178  0.326 23.69255  ? 62   ARG A NE    1 
ATOM   496  C  CZ    A ARG A 1 62  ? -1.58452  8.04599   38.51257  0.674 23.04805  ? 62   ARG A CZ    1 
ATOM   497  C  CZ    B ARG A 1 62  ? 0.26338   6.03300   39.95896  0.326 23.19140  ? 62   ARG A CZ    1 
ATOM   498  N  NH1   A ARG A 1 62  ? -2.84521  8.43686   38.60586  0.674 23.67533  ? 62   ARG A NH1   1 
ATOM   499  N  NH1   B ARG A 1 62  ? 1.10995   6.99230   39.62120  0.326 23.34113  ? 62   ARG A NH1   1 
ATOM   500  N  NH2   A ARG A 1 62  ? -0.87458  8.39339   37.44283  0.674 22.43913  ? 62   ARG A NH2   1 
ATOM   501  N  NH2   B ARG A 1 62  ? 0.71005   4.78710   40.10045  0.326 22.99549  ? 62   ARG A NH2   1 
ATOM   502  N  N     . LEU A 1 63  ? 1.31863   10.36906  43.97223  1.000 23.60048  ? 63   LEU A N     1 
ATOM   503  C  CA    . LEU A 1 63  ? 2.60035   10.56431  44.63933  1.000 23.97414  ? 63   LEU A CA    1 
ATOM   504  C  C     . LEU A 1 63  ? 2.40659   10.93496  46.10227  1.000 24.74697  ? 63   LEU A C     1 
ATOM   505  O  O     . LEU A 1 63  ? 3.13422   10.44563  46.97382  1.000 25.60952  ? 63   LEU A O     1 
ATOM   506  C  CB    . LEU A 1 63  ? 3.40399   11.64647  43.92158  1.000 24.29955  ? 63   LEU A CB    1 
ATOM   507  C  CG    . LEU A 1 63  ? 3.94882   11.31387  42.53308  1.000 24.32036  ? 63   LEU A CG    1 
ATOM   508  C  CD1   . LEU A 1 63  ? 4.59530   12.54552  41.92149  1.000 23.72932  ? 63   LEU A CD1   1 
ATOM   509  C  CD2   . LEU A 1 63  ? 4.93864   10.16026  42.59973  1.000 23.85178  ? 63   LEU A CD2   1 
ATOM   510  N  N     . ARG A 1 64  ? 1.43141   11.80126  46.38808  1.000 31.48338  ? 64   ARG A N     1 
ATOM   511  C  CA    . ARG A 1 64  ? 1.18446   12.21228  47.76589  1.000 32.01137  ? 64   ARG A CA    1 
ATOM   512  C  C     . ARG A 1 64  ? 0.78303   11.02644  48.63248  1.000 32.03074  ? 64   ARG A C     1 
ATOM   513  O  O     . ARG A 1 64  ? 1.19191   10.93276  49.79540  1.000 32.76687  ? 64   ARG A O     1 
ATOM   514  C  CB    . ARG A 1 64  ? 0.10725   13.29520  47.80521  1.000 32.39099  ? 64   ARG A CB    1 
ATOM   515  C  CG    . ARG A 1 64  ? 0.61991   14.68819  47.48688  1.000 33.18284  ? 64   ARG A CG    1 
ATOM   516  C  CD    . ARG A 1 64  ? -0.51977  15.62163  47.12336  1.000 33.80385  ? 64   ARG A CD    1 
ATOM   517  N  NE    . ARG A 1 64  ? -0.04232  16.94218  46.73303  1.000 34.26752  ? 64   ARG A NE    1 
ATOM   518  C  CZ    . ARG A 1 64  ? -0.64658  17.72352  45.84872  1.000 34.45618  ? 64   ARG A CZ    1 
ATOM   519  N  NH1   . ARG A 1 64  ? -1.75676  17.34415  45.23657  1.000 34.28842  ? 64   ARG A NH1   1 
ATOM   520  N  NH2   . ARG A 1 64  ? -0.12335  18.91453  45.57051  1.000 35.36547  ? 64   ARG A NH2   1 
ATOM   521  N  N     . ALA A 1 65  ? -0.01350  10.10599  48.08218  1.000 34.11176  ? 65   ALA A N     1 
ATOM   522  C  CA    . ALA A 1 65  ? -0.39079  8.91528   48.83619  1.000 33.96481  ? 65   ALA A CA    1 
ATOM   523  C  C     . ALA A 1 65  ? 0.82112   8.05141   49.15651  1.000 34.31779  ? 65   ALA A C     1 
ATOM   524  O  O     . ALA A 1 65  ? 0.82453   7.33507   50.16414  1.000 35.08154  ? 65   ALA A O     1 
ATOM   525  C  CB    . ALA A 1 65  ? -1.43185  8.10637   48.06195  1.000 32.89842  ? 65   ALA A CB    1 
ATOM   526  N  N     . ARG A 1 66  ? 1.85639   8.11105   48.32300  1.000 39.07565  ? 66   ARG A N     1 
ATOM   527  C  CA    . ARG A 1 66  ? 3.08632   7.36572   48.54609  1.000 38.65203  ? 66   ARG A CA    1 
ATOM   528  C  C     . ARG A 1 66  ? 4.06919   8.09626   49.45082  1.000 39.95211  ? 66   ARG A C     1 
ATOM   529  O  O     . ARG A 1 66  ? 5.17683   7.59452   49.66591  1.000 40.63743  ? 66   ARG A O     1 
ATOM   530  C  CB    . ARG A 1 66  ? 3.76256   7.05253   47.20839  1.000 38.50214  ? 66   ARG A CB    1 
ATOM   531  C  CG    . ARG A 1 66  ? 3.21091   5.82537   46.50864  1.000 38.65169  ? 66   ARG A CG    1 
ATOM   532  C  CD    . ARG A 1 66  ? 3.73712   5.72156   45.08836  1.000 38.18558  ? 66   ARG A CD    1 
ATOM   533  N  NE    . ARG A 1 66  ? 5.18053   5.51683   45.06001  1.000 39.16219  ? 66   ARG A NE    1 
ATOM   534  C  CZ    . ARG A 1 66  ? 5.97921   5.94408   44.09186  1.000 38.92664  ? 66   ARG A CZ    1 
ATOM   535  N  NH1   . ARG A 1 66  ? 5.50606   6.59905   43.04466  1.000 37.58599  ? 66   ARG A NH1   1 
ATOM   536  N  NH2   . ARG A 1 66  ? 7.28523   5.70626   44.17560  1.000 39.72798  ? 66   ARG A NH2   1 
ATOM   537  N  N     . GLY A 1 67  ? 3.70038   9.26341   49.97722  1.000 29.75695  ? 67   GLY A N     1 
ATOM   538  C  CA    . GLY A 1 67  ? 4.55435   10.00753  50.87838  1.000 30.13720  ? 67   GLY A CA    1 
ATOM   539  C  C     . GLY A 1 67  ? 5.35296   11.12429  50.24318  1.000 30.45802  ? 67   GLY A C     1 
ATOM   540  O  O     . GLY A 1 67  ? 6.14834   11.76522  50.94125  1.000 30.77129  ? 67   GLY A O     1 
ATOM   541  N  N     . PHE A 1 68  ? 5.17352   11.37711  48.94973  1.000 27.35924  ? 68   PHE A N     1 
ATOM   542  C  CA    . PHE A 1 68  ? 5.89890   12.45524  48.29360  1.000 27.11590  ? 68   PHE A CA    1 
ATOM   543  C  C     . PHE A 1 68  ? 5.32372   13.80747  48.69368  1.000 27.55189  ? 68   PHE A C     1 
ATOM   544  O  O     . PHE A 1 68  ? 4.11290   13.95642  48.88132  1.000 27.69529  ? 68   PHE A O     1 
ATOM   545  C  CB    . PHE A 1 68  ? 5.83069   12.30163  46.77366  1.000 26.34210  ? 68   PHE A CB    1 
ATOM   546  C  CG    . PHE A 1 68  ? 6.72840   11.22903  46.22322  1.000 26.40451  ? 68   PHE A CG    1 
ATOM   547  C  CD1   . PHE A 1 68  ? 6.34152   9.89868   46.25017  1.000 26.01298  ? 68   PHE A CD1   1 
ATOM   548  C  CD2   . PHE A 1 68  ? 7.95295   11.55392  45.66320  1.000 25.99847  ? 68   PHE A CD2   1 
ATOM   549  C  CE1   . PHE A 1 68  ? 7.16520   8.91127   45.73637  1.000 26.09276  ? 68   PHE A CE1   1 
ATOM   550  C  CE2   . PHE A 1 68  ? 8.77966   10.57285  45.14690  1.000 26.26609  ? 68   PHE A CE2   1 
ATOM   551  C  CZ    . PHE A 1 68  ? 8.38543   9.24958   45.18389  1.000 25.61628  ? 68   PHE A CZ    1 
ATOM   552  N  N     . ASN A 1 69  ? 6.20171   14.79669  48.82888  1.000 32.33078  ? 69   ASN A N     1 
ATOM   553  C  CA    . ASN A 1 69  ? 5.78635   16.18846  48.95718  1.000 32.85174  ? 69   ASN A CA    1 
ATOM   554  C  C     . ASN A 1 69  ? 5.74356   16.77898  47.55370  1.000 32.33572  ? 69   ASN A C     1 
ATOM   555  O  O     . ASN A 1 69  ? 6.78410   16.93139  46.90648  1.000 32.59405  ? 69   ASN A O     1 
ATOM   556  C  CB    . ASN A 1 69  ? 6.73861   16.96768  49.86004  1.000 33.60564  ? 69   ASN A CB    1 
ATOM   557  C  CG    . ASN A 1 69  ? 6.43368   18.45417  49.88136  1.000 34.96451  ? 69   ASN A CG    1 
ATOM   558  O  OD1   . ASN A 1 69  ? 7.33964   19.28650  49.86765  1.000 35.86283  ? 69   ASN A OD1   1 
ATOM   559  N  ND2   . ASN A 1 69  ? 5.15020   18.79435  49.91681  1.000 35.80840  ? 69   ASN A ND2   1 
ATOM   560  N  N     . VAL A 1 70  ? 4.54422   17.09713  47.07584  1.000 24.94456  ? 70   VAL A N     1 
ATOM   561  C  CA    . VAL A 1 70  ? 4.33577   17.52025  45.69587  1.000 24.40330  ? 70   VAL A CA    1 
ATOM   562  C  C     . VAL A 1 70  ? 3.93372   18.98783  45.68841  1.000 25.10101  ? 70   VAL A C     1 
ATOM   563  O  O     . VAL A 1 70  ? 2.93316   19.37215  46.30662  1.000 25.24589  ? 70   VAL A O     1 
ATOM   564  C  CB    . VAL A 1 70  ? 3.27797   16.65878  44.98984  1.000 23.87865  ? 70   VAL A CB    1 
ATOM   565  C  CG1   . VAL A 1 70  ? 3.23440   16.99187  43.50624  1.000 23.48178  ? 70   VAL A CG1   1 
ATOM   566  C  CG2   . VAL A 1 70  ? 3.56801   15.17914  45.20106  1.000 23.32859  ? 70   VAL A CG2   1 
ATOM   567  N  N     . ARG A 1 71  ? 4.71697   19.80391  44.98931  1.000 21.56671  ? 71   ARG A N     1 
ATOM   568  C  CA    . ARG A 1 71  ? 4.36010   21.19107  44.70622  1.000 21.65771  ? 71   ARG A CA    1 
ATOM   569  C  C     . ARG A 1 71  ? 3.70183   21.20861  43.33310  1.000 20.88873  ? 71   ARG A C     1 
ATOM   570  O  O     . ARG A 1 71  ? 4.37902   21.11995  42.30603  1.000 20.63805  ? 71   ARG A O     1 
ATOM   571  C  CB    . ARG A 1 71  ? 5.59247   22.08788  44.75692  1.000 21.95408  ? 71   ARG A CB    1 
ATOM   572  C  CG    . ARG A 1 71  ? 5.32498   23.55574  44.45351  1.000 22.17701  ? 71   ARG A CG    1 
ATOM   573  C  CD    . ARG A 1 71  ? 6.62028   24.35787  44.48814  1.000 22.77465  ? 71   ARG A CD    1 
ATOM   574  N  NE    . ARG A 1 71  ? 6.44096   25.72766  44.02054  1.000 22.88303  ? 71   ARG A NE    1 
ATOM   575  C  CZ    . ARG A 1 71  ? 6.23316   26.77129  44.81233  1.000 23.61543  ? 71   ARG A CZ    1 
ATOM   576  N  NH1   . ARG A 1 71  ? 6.16821   26.64006  46.12780  1.000 24.29707  ? 71   ARG A NH1   1 
ATOM   577  N  NH2   . ARG A 1 71  ? 6.08930   27.97798  44.27046  1.000 23.85400  ? 71   ARG A NH2   1 
ATOM   578  N  N     . TYR A 1 72  ? 2.37538   21.29767  43.31079  1.000 20.52392  ? 72   TYR A N     1 
ATOM   579  C  CA    . TYR A 1 72  ? 1.60798   21.27930  42.07193  1.000 19.93616  ? 72   TYR A CA    1 
ATOM   580  C  C     . TYR A 1 72  ? 1.12108   22.68924  41.77173  1.000 20.21167  ? 72   TYR A C     1 
ATOM   581  O  O     . TYR A 1 72  ? 0.33528   23.25520  42.53907  1.000 20.82983  ? 72   TYR A O     1 
ATOM   582  C  CB    . TYR A 1 72  ? 0.42917   20.30949  42.15978  1.000 19.87820  ? 72   TYR A CB    1 
ATOM   583  C  CG    . TYR A 1 72  ? -0.14806  19.96151  40.80672  1.000 19.23845  ? 72   TYR A CG    1 
ATOM   584  C  CD1   . TYR A 1 72  ? -1.08084  20.78849  40.19218  1.000 19.29651  ? 72   TYR A CD1   1 
ATOM   585  C  CD2   . TYR A 1 72  ? 0.25836   18.81869  40.13151  1.000 18.67066  ? 72   TYR A CD2   1 
ATOM   586  C  CE1   . TYR A 1 72  ? -1.60381  20.47818  38.94745  1.000 18.81622  ? 72   TYR A CE1   1 
ATOM   587  C  CE2   . TYR A 1 72  ? -0.25833  18.49916  38.88784  1.000 18.16738  ? 72   TYR A CE2   1 
ATOM   588  C  CZ    . TYR A 1 72  ? -1.18912  19.33251  38.30010  1.000 18.24606  ? 72   TYR A CZ    1 
ATOM   589  O  OH    . TYR A 1 72  ? -1.70443  19.01982  37.06215  1.000 17.84824  ? 72   TYR A OH    1 
ATOM   590  N  N     . VAL A 1 73  ? 1.58133   23.24531  40.65700  1.000 21.57535  ? 73   VAL A N     1 
ATOM   591  C  CA    . VAL A 1 73  ? 1.23722   24.60020  40.24444  1.000 21.32288  ? 73   VAL A CA    1 
ATOM   592  C  C     . VAL A 1 73  ? 0.19357   24.49680  39.13915  1.000 21.74548  ? 73   VAL A C     1 
ATOM   593  O  O     . VAL A 1 73  ? 0.50679   24.10825  38.00834  1.000 21.34124  ? 73   VAL A O     1 
ATOM   594  C  CB    . VAL A 1 73  ? 2.47535   25.37639  39.77856  1.000 21.72249  ? 73   VAL A CB    1 
ATOM   595  C  CG1   . VAL A 1 73  ? 2.12735   26.83470  39.53640  1.000 21.77382  ? 73   VAL A CG1   1 
ATOM   596  C  CG2   . VAL A 1 73  ? 3.59439   25.24835  40.80262  1.000 21.49588  ? 73   VAL A CG2   1 
ATOM   597  N  N     . THR A 1 74  ? -1.04993  24.83972  39.46458  1.000 28.34826  ? 74   THR A N     1 
ATOM   598  C  CA    . THR A 1 74  ? -2.14265  24.76861  38.50877  1.000 28.80434  ? 74   THR A CA    1 
ATOM   599  C  C     . THR A 1 74  ? -2.14743  26.00189  37.60692  1.000 29.22167  ? 74   THR A C     1 
ATOM   600  O  O     . THR A 1 74  ? -1.47277  27.00187  37.86695  1.000 29.15139  ? 74   THR A O     1 
ATOM   601  C  CB    . THR A 1 74  ? -3.48090  24.64405  39.23420  1.000 29.67728  ? 74   THR A CB    1 
ATOM   602  O  OG1   . THR A 1 74  ? -3.81275  25.90284  39.83268  1.000 30.63895  ? 74   THR A OG1   1 
ATOM   603  C  CG2   . THR A 1 74  ? -3.40950  23.57221  40.31875  1.000 28.96148  ? 74   THR A CG2   1 
ATOM   604  N  N     . LEU A 1 75  ? -2.92856  25.92630  36.52932  1.000 41.25086  ? 75   LEU A N     1 
ATOM   605  C  CA    . LEU A 1 75  ? -3.02287  27.05319  35.61045  1.000 41.87728  ? 75   LEU A CA    1 
ATOM   606  C  C     . LEU A 1 75  ? -3.89886  28.18118  36.13928  1.000 42.79775  ? 75   LEU A C     1 
ATOM   607  O  O     . LEU A 1 75  ? -3.90029  29.26732  35.55015  1.000 43.25395  ? 75   LEU A O     1 
ATOM   608  C  CB    . LEU A 1 75  ? -3.53671  26.58960  34.24331  1.000 41.92622  ? 75   LEU A CB    1 
ATOM   609  C  CG    . LEU A 1 75  ? -4.63089  25.52337  34.13970  1.000 42.21844  ? 75   LEU A CG    1 
ATOM   610  C  CD1   . LEU A 1 75  ? -5.94261  25.94394  34.79704  1.000 43.47113  ? 75   LEU A CD1   1 
ATOM   611  C  CD2   . LEU A 1 75  ? -4.85576  25.17710  32.68182  1.000 42.18227  ? 75   LEU A CD2   1 
ATOM   612  N  N     . GLU A 1 76  ? -4.64205  27.95490  37.22117  1.000 39.29864  ? 76   GLU A N     1 
ATOM   613  C  CA    . GLU A 1 76  ? -5.38331  29.02426  37.87251  1.000 39.77759  ? 76   GLU A CA    1 
ATOM   614  C  C     . GLU A 1 76  ? -4.56296  29.74412  38.93374  1.000 39.71864  ? 76   GLU A C     1 
ATOM   615  O  O     . GLU A 1 76  ? -5.00935  30.77745  39.44229  1.000 40.29285  ? 76   GLU A O     1 
ATOM   616  C  CB    . GLU A 1 76  ? -6.67018  28.47756  38.50382  1.000 42.92550  ? 76   GLU A CB    1 
ATOM   617  C  CG    . GLU A 1 76  ? -6.47529  27.80622  39.85531  0.919 43.12517  ? 76   GLU A CG    1 
ATOM   618  C  CD    . GLU A 1 76  ? -6.79041  26.32032  39.82813  0.000 42.91783  ? 76   GLU A CD    1 
ATOM   619  O  OE1   . GLU A 1 76  ? -6.59685  25.68180  38.77069  0.761 41.94924  ? 76   GLU A OE1   1 
ATOM   620  O  OE2   . GLU A 1 76  ? -7.23211  25.79029  40.86930  0.891 43.65358  ? 76   GLU A OE2   1 
ATOM   621  N  N     . ASP A 1 77  ? -3.38837  29.22782  39.27358  1.000 32.64571  ? 77   ASP A N     1 
ATOM   622  C  CA    . ASP A 1 77  ? -2.51594  29.85858  40.25308  1.000 31.72746  ? 77   ASP A CA    1 
ATOM   623  C  C     . ASP A 1 77  ? -2.11208  31.24991  39.77475  1.000 32.22999  ? 77   ASP A C     1 
ATOM   624  O  O     . ASP A 1 77  ? -1.43592  31.36813  38.74068  1.000 31.95842  ? 77   ASP A O     1 
ATOM   625  C  CB    . ASP A 1 77  ? -1.28123  28.98951  40.47887  1.000 32.29414  ? 77   ASP A CB    1 
ATOM   626  C  CG    . ASP A 1 77  ? -0.50090  29.38536  41.71395  1.000 32.84506  ? 77   ASP A CG    1 
ATOM   627  O  OD1   . ASP A 1 77  ? -0.61577  30.54707  42.15880  1.000 33.38568  ? 77   ASP A OD1   1 
ATOM   628  O  OD2   . ASP A 1 77  ? 0.23700   28.52708  42.23987  1.000 32.56953  ? 77   ASP A OD2   1 
ATOM   629  N  N     . PRO A 1 78  ? -2.49505  32.31861  40.48146  1.000 26.98640  ? 78   PRO A N     1 
ATOM   630  C  CA    . PRO A 1 78  ? -2.15671  33.67188  40.01283  1.000 27.54724  ? 78   PRO A CA    1 
ATOM   631  C  C     . PRO A 1 78  ? -0.66802  33.97269  40.01291  1.000 27.29260  ? 78   PRO A C     1 
ATOM   632  O  O     . PRO A 1 78  ? -0.26046  34.96270  39.39221  1.000 27.34344  ? 78   PRO A O     1 
ATOM   633  C  CB    . PRO A 1 78  ? -2.89853  34.58273  40.99792  1.000 27.74902  ? 78   PRO A CB    1 
ATOM   634  C  CG    . PRO A 1 78  ? -3.09652  33.75134  42.21821  1.000 27.16684  ? 78   PRO A CG    1 
ATOM   635  C  CD    . PRO A 1 78  ? -3.26388  32.34006  41.73795  1.000 27.38014  ? 78   PRO A CD    1 
ATOM   636  N  N     . ASP A 1 79  ? 0.15193   33.17072  40.68742  1.000 26.51468  ? 79   ASP A N     1 
ATOM   637  C  CA    . ASP A 1 79  ? 1.59149   33.38032  40.71276  1.000 26.32309  ? 79   ASP A CA    1 
ATOM   638  C  C     . ASP A 1 79  ? 2.34005   32.43544  39.78685  1.000 25.86272  ? 79   ASP A C     1 
ATOM   639  O  O     . ASP A 1 79  ? 3.57304   32.48516  39.73654  1.000 25.74244  ? 79   ASP A O     1 
ATOM   640  C  CB    . ASP A 1 79  ? 2.11945   33.23781  42.14138  1.000 26.68286  ? 79   ASP A CB    1 
ATOM   641  C  CG    . ASP A 1 79  ? 1.47485   34.21820  43.09368  1.000 28.54673  ? 79   ASP A CG    1 
ATOM   642  O  OD1   . ASP A 1 79  ? 1.83842   35.41261  43.04368  1.000 28.62364  ? 79   ASP A OD1   1 
ATOM   643  O  OD2   . ASP A 1 79  ? 0.60475   33.79973  43.88650  0.454 28.89607  ? 79   ASP A OD2   1 
ATOM   644  N  N     . ASN A 1 80  ? 1.62748   31.57649  39.06416  1.000 23.27346  ? 80   ASN A N     1 
ATOM   645  C  CA    . ASN A 1 80  ? 2.25515   30.71826  38.07036  1.000 22.42116  ? 80   ASN A CA    1 
ATOM   646  C  C     . ASN A 1 80  ? 2.91868   31.57291  36.99715  1.000 22.67635  ? 80   ASN A C     1 
ATOM   647  O  O     . ASN A 1 80  ? 2.25681   32.37981  36.33610  1.000 23.10063  ? 80   ASN A O     1 
ATOM   648  C  CB    . ASN A 1 80  ? 1.20669   29.79171  37.45437  1.000 21.77102  ? 80   ASN A CB    1 
ATOM   649  C  CG    . ASN A 1 80  ? 1.81798   28.66562  36.64446  1.000 20.88720  ? 80   ASN A CG    1 
ATOM   650  O  OD1   . ASN A 1 80  ? 2.96014   28.75121  36.19540  1.000 20.78291  ? 80   ASN A OD1   1 
ATOM   651  N  ND2   . ASN A 1 80  ? 1.05124   27.59854  36.45018  1.000 20.33155  ? 80   ASN A ND2   1 
ATOM   652  N  N     . THR A 1 81  ? 4.23296   31.40277  36.83237  1.000 23.29421  ? 81   THR A N     1 
ATOM   653  C  CA    . THR A 1 81  ? 4.95665   32.16613  35.82224  1.000 23.46381  ? 81   THR A CA    1 
ATOM   654  C  C     . THR A 1 81  ? 4.67978   31.66612  34.40977  1.000 22.95637  ? 81   THR A C     1 
ATOM   655  O  O     . THR A 1 81  ? 4.90901   32.40741  33.44812  1.000 22.70796  ? 81   THR A O     1 
ATOM   656  C  CB    . THR A 1 81  ? 6.45924   32.13029  36.10783  1.000 23.62395  ? 81   THR A CB    1 
ATOM   657  O  OG1   . THR A 1 81  ? 6.91123   30.77046  36.13751  1.000 23.67088  ? 81   THR A OG1   1 
ATOM   658  C  CG2   . THR A 1 81  ? 6.76270   32.79234  37.44687  1.000 23.86299  ? 81   THR A CG2   1 
ATOM   659  N  N     . GLY A 1 82  ? 4.19390   30.43395  34.26137  1.000 23.19209  ? 82   GLY A N     1 
ATOM   660  C  CA    . GLY A 1 82  ? 3.77555   29.90789  32.98318  1.000 23.05213  ? 82   GLY A CA    1 
ATOM   661  C  C     . GLY A 1 82  ? 4.77112   28.98599  32.30920  1.000 22.56802  ? 82   GLY A C     1 
ATOM   662  O  O     . GLY A 1 82  ? 4.38090   28.23127  31.40986  1.000 21.70934  ? 82   GLY A O     1 
ATOM   663  N  N     . SER A 1 83  ? 6.03683   29.02034  32.71655  1.000 22.23369  ? 83   SER A N     1 
ATOM   664  C  CA    . SER A 1 83  ? 7.07982   28.22344  32.09225  1.000 21.44442  ? 83   SER A CA    1 
ATOM   665  C  C     . SER A 1 83  ? 7.66191   27.23030  33.08917  1.000 21.85838  ? 83   SER A C     1 
ATOM   666  O  O     . SER A 1 83  ? 7.55961   27.40226  34.30730  1.000 22.18875  ? 83   SER A O     1 
ATOM   667  C  CB    . SER A 1 83  ? 8.20033   29.11205  31.54150  1.000 21.76270  ? 83   SER A CB    1 
ATOM   668  O  OG    . SER A 1 83  ? 8.84658   29.81423  32.58891  1.000 22.43098  ? 83   SER A OG    1 
ATOM   669  N  N     . ILE A 1 84  ? 8.28458   26.18218  32.54689  1.000 23.40908  ? 84   ILE A N     1 
ATOM   670  C  CA    . ILE A 1 84  ? 8.98156   25.21184  33.38522  1.000 23.67236  ? 84   ILE A CA    1 
ATOM   671  C  C     . ILE A 1 84  ? 10.16988  25.86887  34.07816  1.000 24.89387  ? 84   ILE A C     1 
ATOM   672  O  O     . ILE A 1 84  ? 10.37433  25.70653  35.28731  1.000 24.98026  ? 84   ILE A O     1 
ATOM   673  C  CB    . ILE A 1 84  ? 9.41938   23.99607  32.54706  1.000 23.37044  ? 84   ILE A CB    1 
ATOM   674  C  CG1   . ILE A 1 84  ? 8.21525   23.35004  31.85467  1.000 22.25478  ? 84   ILE A CG1   1 
ATOM   675  C  CG2   . ILE A 1 84  ? 10.14310  22.98335  33.41622  1.000 23.56816  ? 84   ILE A CG2   1 
ATOM   676  C  CD1   . ILE A 1 84  ? 7.13903   22.87903  32.81059  1.000 22.96559  ? 84   ILE A CD1   1 
ATOM   677  N  N     . GLY A 1 85  ? 10.96772  26.62523  33.32183  1.000 20.04868  ? 85   GLY A N     1 
ATOM   678  C  CA    . GLY A 1 85  ? 12.12924  27.27502  33.90691  1.000 20.80064  ? 85   GLY A CA    1 
ATOM   679  C  C     . GLY A 1 85  ? 11.76276  28.32062  34.94302  1.000 21.44763  ? 85   GLY A C     1 
ATOM   680  O  O     . GLY A 1 85  ? 12.40347  28.41622  35.99339  1.000 21.90645  ? 85   GLY A O     1 
ATOM   681  N  N     . GLY A 1 86  ? 10.73208  29.12043  34.66369  1.000 21.58510  ? 86   GLY A N     1 
ATOM   682  C  CA    . GLY A 1 86  ? 10.28888  30.10093  35.64191  1.000 22.25073  ? 86   GLY A CA    1 
ATOM   683  C  C     . GLY A 1 86  ? 9.77862   29.46090  36.91903  1.000 22.02693  ? 86   GLY A C     1 
ATOM   684  O  O     . GLY A 1 86  ? 10.03875  29.95244  38.01985  1.000 22.66373  ? 86   GLY A O     1 
ATOM   685  N  N     . GLU A 1 87  ? 9.05384   28.34904  36.79244  1.000 24.73511  ? 87   GLU A N     1 
ATOM   686  C  CA    . GLU A 1 87  ? 8.51975   27.68344  37.97307  1.000 24.75535  ? 87   GLU A CA    1 
ATOM   687  C  C     . GLU A 1 87  ? 9.59552   26.91650  38.72963  1.000 25.24381  ? 87   GLU A C     1 
ATOM   688  O  O     . GLU A 1 87  ? 9.47692   26.73021  39.94622  1.000 25.52666  ? 87   GLU A O     1 
ATOM   689  C  CB    . GLU A 1 87  ? 7.37563   26.75475  37.57353  1.000 23.81775  ? 87   GLU A CB    1 
ATOM   690  C  CG    . GLU A 1 87  ? 6.04860   27.47154  37.38909  1.000 24.22833  ? 87   GLU A CG    1 
ATOM   691  C  CD    . GLU A 1 87  ? 5.74051   28.42463  38.52756  1.000 24.92931  ? 87   GLU A CD    1 
ATOM   692  O  OE1   . GLU A 1 87  ? 5.50736   27.94259  39.65504  1.000 25.35850  ? 87   GLU A OE1   1 
ATOM   693  O  OE2   . GLU A 1 87  ? 5.73505   29.65294  38.29926  1.000 25.26667  ? 87   GLU A OE2   1 
ATOM   694  N  N     . LEU A 1 88  ? 10.64310  26.46595  38.03560  1.000 23.10439  ? 88   LEU A N     1 
ATOM   695  C  CA    . LEU A 1 88  ? 11.78864  25.88824  38.73000  1.000 23.82775  ? 88   LEU A CA    1 
ATOM   696  C  C     . LEU A 1 88  ? 12.46858  26.92790  39.61163  1.000 24.23700  ? 88   LEU A C     1 
ATOM   697  O  O     . LEU A 1 88  ? 12.85096  26.63405  40.75019  1.000 25.12834  ? 88   LEU A O     1 
ATOM   698  C  CB    . LEU A 1 88  ? 12.77912  25.30675  37.72036  1.000 23.24951  ? 88   LEU A CB    1 
ATOM   699  C  CG    . LEU A 1 88  ? 12.60619  23.82813  37.35915  1.000 23.81738  ? 88   LEU A CG    1 
ATOM   700  C  CD1   . LEU A 1 88  ? 13.35841  23.50072  36.07901  1.000 23.92253  ? 88   LEU A CD1   1 
ATOM   701  C  CD2   . LEU A 1 88  ? 13.06394  22.92520  38.49881  1.000 23.25636  ? 88   LEU A CD2   1 
ATOM   702  N  N     . ARG A 1 89  ? 12.61966  28.15397  39.10343  1.000 36.11619  ? 89   ARG A N     1 
ATOM   703  C  CA    . ARG A 1 89  ? 13.20428  29.22419  39.90501  1.000 37.09684  ? 89   ARG A CA    1 
ATOM   704  C  C     . ARG A 1 89  ? 12.32571  29.56071  41.10243  1.000 37.11137  ? 89   ARG A C     1 
ATOM   705  O  O     . ARG A 1 89  ? 12.82937  29.77237  42.21147  1.000 37.50668  ? 89   ARG A O     1 
ATOM   706  C  CB    . ARG A 1 89  ? 13.41961  30.46492  39.04094  1.000 37.04317  ? 89   ARG A CB    1 
ATOM   707  C  CG    . ARG A 1 89  ? 14.59947  30.36718  38.09631  1.000 38.55436  ? 89   ARG A CG    1 
ATOM   708  C  CD    . ARG A 1 89  ? 14.80464  31.67645  37.34297  1.000 38.24013  ? 89   ARG A CD    1 
ATOM   709  N  NE    . ARG A 1 89  ? 15.75423  31.55448  36.24157  1.000 38.83225  ? 89   ARG A NE    1 
ATOM   710  C  CZ    . ARG A 1 89  ? 17.03951  31.24968  36.37339  1.000 40.15397  ? 89   ARG A CZ    1 
ATOM   711  N  NH1   . ARG A 1 89  ? 17.59732  31.08481  37.56340  1.000 39.50374  ? 89   ARG A NH1   1 
ATOM   712  N  NH2   . ARG A 1 89  ? 17.78875  31.11827  35.28222  1.000 40.02289  ? 89   ARG A NH2   1 
ATOM   713  N  N     . ARG A 1 90  ? 11.00743  29.61658  40.89546  1.000 28.97003  ? 90   ARG A N     1 
ATOM   714  C  CA    . ARG A 1 90  ? 10.09640  29.96726  41.98081  1.000 29.39077  ? 90   ARG A CA    1 
ATOM   715  C  C     . ARG A 1 90  ? 10.11246  28.91161  43.07912  1.000 29.63951  ? 90   ARG A C     1 
ATOM   716  O  O     . ARG A 1 90  ? 10.03254  29.24011  44.26918  1.000 29.95566  ? 90   ARG A O     1 
ATOM   717  C  CB    . ARG A 1 90  ? 8.68157   30.15199  41.43195  1.000 28.42309  ? 90   ARG A CB    1 
ATOM   718  C  CG    . ARG A 1 90  ? 7.89207   31.26878  42.08728  1.000 28.75608  ? 90   ARG A CG    1 
ATOM   719  C  CD    . ARG A 1 90  ? 6.70368   31.67045  41.22913  1.000 28.47297  ? 90   ARG A CD    1 
ATOM   720  N  NE    . ARG A 1 90  ? 5.77706   30.56280  41.02442  1.000 28.38041  ? 90   ARG A NE    1 
ATOM   721  C  CZ    . ARG A 1 90  ? 4.75362   30.28589  41.82087  1.000 28.52070  ? 90   ARG A CZ    1 
ATOM   722  N  NH1   . ARG A 1 90  ? 4.49368   31.01773  42.89174  1.000 28.27417  ? 90   ARG A NH1   1 
ATOM   723  N  NH2   . ARG A 1 90  ? 3.97167   29.24842  41.53607  1.000 28.35275  ? 90   ARG A NH2   1 
ATOM   724  N  N     . ALA A 1 91  ? 10.21663  27.63608  42.69937  1.000 23.19645  ? 91   ALA A N     1 
ATOM   725  C  CA    . ALA A 1 91  ? 10.27414  26.57414  43.69600  1.000 23.21264  ? 91   ALA A CA    1 
ATOM   726  C  C     . ALA A 1 91  ? 11.59929  26.57914  44.44637  1.000 23.94968  ? 91   ALA A C     1 
ATOM   727  O  O     . ALA A 1 91  ? 11.64667  26.18894  45.61828  1.000 24.45233  ? 91   ALA A O     1 
ATOM   728  C  CB    . ALA A 1 91  ? 10.04428  25.21641  43.03312  1.000 22.27649  ? 91   ALA A CB    1 
ATOM   729  N  N     . LEU A 1 92  ? 12.68107  27.01442  43.79647  1.000 30.06716  ? 92   LEU A N     1 
ATOM   730  C  CA    . LEU A 1 92  ? 13.97496  27.04366  44.46832  1.000 30.44873  ? 92   LEU A CA    1 
ATOM   731  C  C     . LEU A 1 92  ? 14.06550  28.19321  45.46387  1.000 31.25860  ? 92   LEU A C     1 
ATOM   732  O  O     . LEU A 1 92  ? 14.81796  28.10416  46.44043  1.000 32.19664  ? 92   LEU A O     1 
ATOM   733  C  CB    . LEU A 1 92  ? 15.10136  27.13300  43.43885  1.000 30.82640  ? 92   LEU A CB    1 
ATOM   734  C  CG    . LEU A 1 92  ? 15.38695  25.85118  42.64872  1.000 31.31286  ? 92   LEU A CG    1 
ATOM   735  C  CD1   . LEU A 1 92  ? 16.48550  26.08374  41.62233  1.000 31.14956  ? 92   LEU A CD1   1 
ATOM   736  C  CD2   . LEU A 1 92  ? 15.75745  24.70560  43.58365  1.000 30.65845  ? 92   LEU A CD2   1 
ATOM   737  N  N     . GLU A 1 93  ? 13.31572  29.27534  45.23947  0.902 40.11962  ? 93   GLU A N     1 
ATOM   738  C  CA    . GLU A 1 93  ? 13.26343  30.35843  46.21368  0.902 40.43284  ? 93   GLU A CA    1 
ATOM   739  C  C     . GLU A 1 93  ? 12.38507  30.02465  47.41025  0.902 40.21649  ? 93   GLU A C     1 
ATOM   740  O  O     . GLU A 1 93  ? 12.57669  30.60673  48.48305  0.902 40.81047  ? 93   GLU A O     1 
ATOM   741  C  CB    . GLU A 1 93  ? 12.74489  31.64645  45.56795  0.902 40.34277  ? 93   GLU A CB    1 
ATOM   742  C  CG    . GLU A 1 93  ? 13.47079  32.08127  44.31021  0.902 41.59970  ? 93   GLU A CG    1 
ATOM   743  C  CD    . GLU A 1 93  ? 12.71279  33.16009  43.55710  0.902 42.49536  ? 93   GLU A CD    1 
ATOM   744  O  OE1   . GLU A 1 93  ? 12.06820  34.00217  44.21812  0.902 43.24702  ? 93   GLU A OE1   1 
ATOM   745  O  OE2   . GLU A 1 93  ? 12.75672  33.16596  42.30777  0.902 41.38566  ? 93   GLU A OE2   1 
ATOM   746  N  N     . ALA A 1 94  ? 11.43091  29.10405  47.24994  1.000 34.30646  ? 94   ALA A N     1 
ATOM   747  C  CA    . ALA A 1 94  ? 10.46557  28.83864  48.31079  1.000 34.08135  ? 94   ALA A CA    1 
ATOM   748  C  C     . ALA A 1 94  ? 11.10788  28.15925  49.51316  1.000 35.03216  ? 94   ALA A C     1 
ATOM   749  O  O     . ALA A 1 94  ? 10.71203  28.42473  50.65399  1.000 35.18293  ? 94   ALA A O     1 
ATOM   750  C  CB    . ALA A 1 94  ? 9.31561   27.98836  47.77176  1.000 34.00265  ? 94   ALA A CB    1 
ATOM   751  N  N     . ARG A 1 95  ? 12.08853  27.29013  49.28825  1.000 40.42129  ? 95   ARG A N     1 
ATOM   752  C  CA    . ARG A 1 95  ? 12.76204  26.59873  50.38013  1.000 40.66798  ? 95   ARG A CA    1 
ATOM   753  C  C     . ARG A 1 95  ? 14.14845  26.17870  49.90793  1.000 41.39031  ? 95   ARG A C     1 
ATOM   754  O  O     . ARG A 1 95  ? 14.51313  26.36018  48.74315  1.000 41.48126  ? 95   ARG A O     1 
ATOM   755  C  CB    . ARG A 1 95  ? 11.94220  25.40006  50.86502  1.000 40.37794  ? 95   ARG A CB    1 
ATOM   756  C  CG    . ARG A 1 95  ? 11.44059  24.50235  49.75126  1.000 40.45139  ? 95   ARG A CG    1 
ATOM   757  C  CD    . ARG A 1 95  ? 11.30927  23.06649  50.22394  1.000 40.49438  ? 95   ARG A CD    1 
ATOM   758  N  NE    . ARG A 1 95  ? 12.60405  22.40492  50.32989  1.000 40.51538  ? 95   ARG A NE    1 
ATOM   759  C  CZ    . ARG A 1 95  ? 12.76377  21.10322  50.52507  1.000 40.67022  ? 95   ARG A CZ    1 
ATOM   760  N  NH1   . ARG A 1 95  ? 11.72667  20.28893  50.63480  1.000 39.66665  ? 95   ARG A NH1   1 
ATOM   761  N  NH2   . ARG A 1 95  ? 13.99461  20.60581  50.61170  1.000 40.01595  ? 95   ARG A NH2   1 
ATOM   762  N  N     . ALA A 1 96  ? 14.92114  25.61071  50.82967  1.000 36.23135  ? 96   ALA A N     1 
ATOM   763  C  CA    . ALA A 1 96  ? 16.29038  25.21536  50.53731  1.000 36.05181  ? 96   ALA A CA    1 
ATOM   764  C  C     . ALA A 1 96  ? 16.32458  23.88596  49.79528  1.000 36.30048  ? 96   ALA A C     1 
ATOM   765  O  O     . ALA A 1 96  ? 15.61058  22.94138  50.14424  1.000 36.30279  ? 96   ALA A O     1 
ATOM   766  C  CB    . ALA A 1 96  ? 17.10301  25.11397  51.82792  1.000 37.07611  ? 96   ALA A CB    1 
ATOM   767  N  N     . PHE A 1 97  ? 17.16336  23.82146  48.76378  1.000 29.10396  ? 97   PHE A N     1 
ATOM   768  C  CA    . PHE A 1 97  ? 17.36313  22.60997  47.98400  1.000 28.83466  ? 97   PHE A CA    1 
ATOM   769  C  C     . PHE A 1 97  ? 18.84617  22.45015  47.69377  1.000 29.62042  ? 97   PHE A C     1 
ATOM   770  O  O     . PHE A 1 97  ? 19.56599  23.43512  47.51344  1.000 30.81329  ? 97   PHE A O     1 
ATOM   771  C  CB    . PHE A 1 97  ? 16.58461  22.64199  46.66340  1.000 27.99510  ? 97   PHE A CB    1 
ATOM   772  C  CG    . PHE A 1 97  ? 15.12804  22.31904  46.80793  1.000 27.36423  ? 97   PHE A CG    1 
ATOM   773  C  CD1   . PHE A 1 97  ? 14.71208  21.01653  47.02859  1.000 27.39419  ? 97   PHE A CD1   1 
ATOM   774  C  CD2   . PHE A 1 97  ? 14.17285  23.31685  46.71321  1.000 27.17587  ? 97   PHE A CD2   1 
ATOM   775  C  CE1   . PHE A 1 97  ? 13.37140  20.71629  47.15780  1.000 26.43324  ? 97   PHE A CE1   1 
ATOM   776  C  CE2   . PHE A 1 97  ? 12.83012  23.02310  46.84051  1.000 26.99926  ? 97   PHE A CE2   1 
ATOM   777  C  CZ    . PHE A 1 97  ? 12.42882  21.72159  47.06329  1.000 26.89405  ? 97   PHE A CZ    1 
ATOM   778  N  N     . ASP A 1 98  ? 19.29857  21.19882  47.64735  1.000 38.31243  ? 98   ASP A N     1 
ATOM   779  C  CA    . ASP A 1 98  ? 20.68941  20.92276  47.31372  1.000 38.30503  ? 98   ASP A CA    1 
ATOM   780  C  C     . ASP A 1 98  ? 20.92557  20.83911  45.81240  1.000 38.88848  ? 98   ASP A C     1 
ATOM   781  O  O     . ASP A 1 98  ? 22.01270  21.19859  45.34459  1.000 38.76911  ? 98   ASP A O     1 
ATOM   782  C  CB    . ASP A 1 98  ? 21.14708  19.62049  47.97813  1.000 39.14350  ? 98   ASP A CB    1 
ATOM   783  C  CG    . ASP A 1 98  ? 21.89864  19.85999  49.27544  1.000 40.62893  ? 98   ASP A CG    1 
ATOM   784  O  OD1   . ASP A 1 98  ? 21.93569  21.01936  49.73926  1.000 42.04612  ? 98   ASP A OD1   1 
ATOM   785  O  OD2   . ASP A 1 98  ? 22.45329  18.88905  49.83254  1.000 41.54554  ? 98   ASP A OD2   1 
ATOM   786  N  N     . ARG A 1 99  ? 19.93386  20.38898  45.04792  1.000 31.05651  ? 99   ARG A N     1 
ATOM   787  C  CA    . ARG A 1 99  ? 20.09188  20.20050  43.61114  1.000 31.49075  ? 99   ARG A CA    1 
ATOM   788  C  C     . ARG A 1 99  ? 18.71891  19.98348  42.98919  1.000 30.90894  ? 99   ARG A C     1 
ATOM   789  O  O     . ARG A 1 99  ? 17.72041  19.78558  43.68659  1.000 30.23763  ? 99   ARG A O     1 
ATOM   790  C  CB    . ARG A 1 99  ? 21.01800  19.02176  43.30084  1.000 34.68597  ? 99   ARG A CB    1 
ATOM   791  C  CG    . ARG A 1 99  ? 20.39070  17.66080  43.54804  1.000 34.12696  ? 99   ARG A CG    1 
ATOM   792  C  CD    . ARG A 1 99  ? 21.45663  16.59570  43.72895  1.000 34.55295  ? 99   ARG A CD    1 
ATOM   793  N  NE    . ARG A 1 99  ? 22.62731  16.86748  42.90401  0.397 35.09835  ? 99   ARG A NE    1 
ATOM   794  C  CZ    . ARG A 1 99  ? 22.96893  16.16455  41.83321  0.538 35.03096  ? 99   ARG A CZ    1 
ATOM   795  N  NH1   . ARG A 1 99  ? 22.24617  15.13570  41.42263  1.000 34.42492  ? 99   ARG A NH1   1 
ATOM   796  N  NH2   . ARG A 1 99  ? 24.06165  16.50438  41.15557  0.824 35.56049  ? 99   ARG A NH2   1 
ATOM   797  N  N     . VAL A 1 100 ? 18.68554  20.02385  41.66009  1.000 25.40908  ? 100  VAL A N     1 
ATOM   798  C  CA    . VAL A 1 100 ? 17.49239  19.71883  40.87970  1.000 25.20141  ? 100  VAL A CA    1 
ATOM   799  C  C     . VAL A 1 100 ? 17.76103  18.44203  40.09526  1.000 24.77526  ? 100  VAL A C     1 
ATOM   800  O  O     . VAL A 1 100 ? 18.83629  18.28465  39.50412  1.000 25.05646  ? 100  VAL A O     1 
ATOM   801  C  CB    . VAL A 1 100 ? 17.11689  20.87862  39.93903  1.000 24.73085  ? 100  VAL A CB    1 
ATOM   802  C  CG1   . VAL A 1 100 ? 15.96179  20.48086  39.03547  1.000 23.59527  ? 100  VAL A CG1   1 
ATOM   803  C  CG2   . VAL A 1 100 ? 16.76301  22.12196  40.73959  1.000 24.98125  ? 100  VAL A CG2   1 
ATOM   804  N  N     . ILE A 1 101 ? 16.79753  17.52479  40.10571  1.000 22.71781  ? 101  ILE A N     1 
ATOM   805  C  CA    . ILE A 1 101 ? 16.87760  16.28490  39.34394  1.000 22.65700  ? 101  ILE A CA    1 
ATOM   806  C  C     . ILE A 1 101 ? 15.69348  16.23143  38.39130  1.000 22.02360  ? 101  ILE A C     1 
ATOM   807  O  O     . ILE A 1 101 ? 14.56104  16.54303  38.77553  1.000 21.03857  ? 101  ILE A O     1 
ATOM   808  C  CB    . ILE A 1 101 ? 16.89795  15.04097  40.25786  1.000 22.21026  ? 101  ILE A CB    1 
ATOM   809  C  CG1   . ILE A 1 101 ? 18.01216  15.15454  41.29975  1.000 23.04347  ? 101  ILE A CG1   1 
ATOM   810  C  CG2   . ILE A 1 101 ? 17.06712  13.77229  39.43208  1.000 22.16575  ? 101  ILE A CG2   1 
ATOM   811  C  CD1   . ILE A 1 101 ? 17.99342  14.04522  42.33334  1.000 23.23154  ? 101  ILE A CD1   1 
ATOM   812  N  N     . ARG A 1 102 ? 15.95669  15.83978  37.14785  1.000 19.92958  ? 102  ARG A N     1 
ATOM   813  C  CA    . ARG A 1 102 ? 14.90810  15.75277  36.14545  1.000 19.20355  ? 102  ARG A CA    1 
ATOM   814  C  C     . ARG A 1 102 ? 15.26601  14.66779  35.14185  1.000 19.66961  ? 102  ARG A C     1 
ATOM   815  O  O     . ARG A 1 102 ? 16.37666  14.13004  35.13766  1.000 19.84340  ? 102  ARG A O     1 
ATOM   816  C  CB    . ARG A 1 102 ? 14.69477  17.09513  35.43876  1.000 19.73042  ? 102  ARG A CB    1 
ATOM   817  C  CG    . ARG A 1 102 ? 15.89330  17.55707  34.63199  1.000 20.77573  ? 102  ARG A CG    1 
ATOM   818  C  CD    . ARG A 1 102 ? 15.60659  18.84974  33.88683  1.000 20.66486  ? 102  ARG A CD    1 
ATOM   819  N  NE    . ARG A 1 102 ? 16.56175  19.05182  32.80482  1.000 21.48564  ? 102  ARG A NE    1 
ATOM   820  C  CZ    . ARG A 1 102 ? 16.38291  18.63494  31.55899  1.000 21.41468  ? 102  ARG A CZ    1 
ATOM   821  N  NH1   . ARG A 1 102 ? 15.26927  18.02452  31.18683  1.000 19.95507  ? 102  ARG A NH1   1 
ATOM   822  N  NH2   . ARG A 1 102 ? 17.34695  18.83322  30.66482  1.000 22.07981  ? 102  ARG A NH2   1 
ATOM   823  N  N     . THR A 1 103 ? 14.30078  14.35460  34.28576  1.000 18.74199  ? 103  THR A N     1 
ATOM   824  C  CA    . THR A 1 103 ? 14.45323  13.35895  33.23854  1.000 18.71222  ? 103  THR A CA    1 
ATOM   825  C  C     . THR A 1 103 ? 14.36896  14.04313  31.88048  1.000 19.20714  ? 103  THR A C     1 
ATOM   826  O  O     . THR A 1 103 ? 13.52390  14.92010  31.67249  1.000 18.58554  ? 103  THR A O     1 
ATOM   827  C  CB    . THR A 1 103 ? 13.37426  12.27761  33.36113  1.000 17.11403  ? 103  THR A CB    1 
ATOM   828  O  OG1   . THR A 1 103 ? 13.65358  11.44938  34.49776  1.000 17.44029  ? 103  THR A OG1   1 
ATOM   829  C  CG2   . THR A 1 103 ? 13.33126  11.41429  32.11724  1.000 16.85829  ? 103  THR A CG2   1 
ATOM   830  N  N     . ALA A 1 104 ? 15.25921  13.65194  30.96729  1.000 27.23514  ? 104  ALA A N     1 
ATOM   831  C  CA    . ALA A 1 104 ? 15.27923  14.23514  29.63070  1.000 27.73198  ? 104  ALA A CA    1 
ATOM   832  C  C     . ALA A 1 104 ? 13.91347  14.10587  28.96687  1.000 26.39952  ? 104  ALA A C     1 
ATOM   833  O  O     . ALA A 1 104 ? 13.33344  13.01730  28.91462  1.000 25.33547  ? 104  ALA A O     1 
ATOM   834  C  CB    . ALA A 1 104 ? 16.35151  13.55964  28.77638  1.000 29.04747  ? 104  ALA A CB    1 
ATOM   835  N  N     . CYS A 1 105 ? 13.40094  15.22571  28.46226  1.000 24.06164  ? 105  CYS A N     1 
ATOM   836  C  CA    . CYS A 1 105 ? 12.05013  15.28849  27.92692  1.000 22.30049  ? 105  CYS A CA    1 
ATOM   837  C  C     . CYS A 1 105 ? 12.04653  14.84435  26.46433  1.000 22.25053  ? 105  CYS A C     1 
ATOM   838  O  O     . CYS A 1 105 ? 13.05585  14.37791  25.93018  1.000 23.86539  ? 105  CYS A O     1 
ATOM   839  C  CB    . CYS A 1 105 ? 11.48299  16.69611  28.10337  1.000 21.82726  ? 105  CYS A CB    1 
ATOM   840  S  SG    . CYS A 1 105 ? 12.25997  17.96244  27.07585  1.000 22.46941  ? 105  CYS A SG    1 
ATOM   841  N  N     . GLY A 1 106 ? 10.90217  14.98802  25.79910  1.000 20.98744  ? 106  GLY A N     1 
ATOM   842  C  CA    . GLY A 1 106 ? 10.76318  14.53398  24.42907  1.000 21.37250  ? 106  GLY A CA    1 
ATOM   843  C  C     . GLY A 1 106 ? 10.59542  15.64628  23.41345  1.000 21.31547  ? 106  GLY A C     1 
ATOM   844  O  O     . GLY A 1 106 ? 10.02267  15.43261  22.33986  1.000 20.48677  ? 106  GLY A O     1 
ATOM   845  N  N     . LYS A 1 107 ? 11.08700  16.84000  23.73936  1.000 23.51266  ? 107  LYS A N     1 
ATOM   846  C  CA    . LYS A 1 107 ? 11.06683  17.97661  22.82592  1.000 23.45197  ? 107  LYS A CA    1 
ATOM   847  C  C     . LYS A 1 107 ? 12.43239  18.64416  22.86773  1.000 24.12349  ? 107  LYS A C     1 
ATOM   848  O  O     . LYS A 1 107 ? 12.86113  19.11420  23.92722  1.000 24.47790  ? 107  LYS A O     1 
ATOM   849  C  CB    . LYS A 1 107 ? 9.95901   18.96831  23.19496  1.000 22.84752  ? 107  LYS A CB    1 
ATOM   850  C  CG    . LYS A 1 107 ? 9.85657   20.15846  22.25719  1.000 22.51117  ? 107  LYS A CG    1 
ATOM   851  C  CD    . LYS A 1 107 ? 8.51582   20.86107  22.39528  1.000 21.86062  ? 107  LYS A CD    1 
ATOM   852  C  CE    . LYS A 1 107 ? 8.23045   21.23170  23.84211  1.000 22.22861  ? 107  LYS A CE    1 
ATOM   853  N  NZ    . LYS A 1 107 ? 7.22600   22.33032  23.94598  1.000 22.99638  ? 107  LYS A NZ    1 
ATOM   854  N  N     . TRP A 1 108 ? 13.11043  18.68365  21.71518  1.000 19.54515  ? 108  TRP A N     1 
ATOM   855  C  CA    . TRP A 1 108 ? 14.49222  19.15559  21.67678  1.000 20.69239  ? 108  TRP A CA    1 
ATOM   856  C  C     . TRP A 1 108 ? 14.60259  20.60319  22.13714  1.000 21.09456  ? 108  TRP A C     1 
ATOM   857  O  O     . TRP A 1 108 ? 15.55847  20.96764  22.83154  1.000 21.81920  ? 108  TRP A O     1 
ATOM   858  C  CB    . TRP A 1 108 ? 15.06502  18.99870  20.26663  1.000 20.65736  ? 108  TRP A CB    1 
ATOM   859  C  CG    . TRP A 1 108 ? 16.51987  19.36530  20.16674  1.000 21.92366  ? 108  TRP A CG    1 
ATOM   860  C  CD1   . TRP A 1 108 ? 17.58637  18.51558  20.23966  1.000 23.14913  ? 108  TRP A CD1   1 
ATOM   861  C  CD2   . TRP A 1 108 ? 17.06661  20.67801  19.97942  1.000 21.84481  ? 108  TRP A CD2   1 
ATOM   862  N  NE1   . TRP A 1 108 ? 18.76148  19.21718  20.11059  1.000 23.32540  ? 108  TRP A NE1   1 
ATOM   863  C  CE2   . TRP A 1 108 ? 18.46960  20.54592  19.94918  1.000 23.05540  ? 108  TRP A CE2   1 
ATOM   864  C  CE3   . TRP A 1 108 ? 16.50621  21.95091  19.83354  1.000 21.75629  ? 108  TRP A CE3   1 
ATOM   865  C  CZ2   . TRP A 1 108 ? 19.31914  21.63782  19.78157  1.000 24.05603  ? 108  TRP A CZ2   1 
ATOM   866  C  CZ3   . TRP A 1 108 ? 17.35310  23.03551  19.66810  1.000 22.91214  ? 108  TRP A CZ3   1 
ATOM   867  C  CH2   . TRP A 1 108 ? 18.74313  22.87124  19.64244  1.000 23.10977  ? 108  TRP A CH2   1 
ATOM   868  N  N     . GLY A 1 109 ? 13.63909  21.44412  21.75428  1.000 24.98949  ? 109  GLY A N     1 
ATOM   869  C  CA    . GLY A 1 109 ? 13.69210  22.84340  22.14896  1.000 24.79957  ? 109  GLY A CA    1 
ATOM   870  C  C     . GLY A 1 109 ? 13.60692  23.02840  23.65161  1.000 24.85135  ? 109  GLY A C     1 
ATOM   871  O  O     . GLY A 1 109 ? 14.37413  23.79325  24.24183  1.000 25.29980  ? 109  GLY A O     1 
ATOM   872  N  N     . LEU A 1 110 ? 12.66696  22.33068  24.29251  1.000 19.86488  ? 110  LEU A N     1 
ATOM   873  C  CA    . LEU A 1 110 ? 12.56779  22.40176  25.74640  1.000 20.30730  ? 110  LEU A CA    1 
ATOM   874  C  C     . LEU A 1 110 ? 13.80296  21.80699  26.40976  1.000 21.19835  ? 110  LEU A C     1 
ATOM   875  O  O     . LEU A 1 110 ? 14.34081  22.38238  27.36308  1.000 22.10414  ? 110  LEU A O     1 
ATOM   876  C  CB    . LEU A 1 110 ? 11.30385  21.68680  26.22387  1.000 19.34218  ? 110  LEU A CB    1 
ATOM   877  C  CG    . LEU A 1 110 ? 11.00722  21.76071  27.72461  1.000 19.92294  ? 110  LEU A CG    1 
ATOM   878  C  CD1   . LEU A 1 110 ? 10.88396  23.20746  28.19081  1.000 19.39501  ? 110  LEU A CD1   1 
ATOM   879  C  CD2   . LEU A 1 110 ? 9.75208   20.96923  28.06839  1.000 18.31309  ? 110  LEU A CD2   1 
ATOM   880  N  N     . GLU A 1 111 ? 14.27241  20.66137  25.91042  1.000 20.37208  ? 111  GLU A N     1 
ATOM   881  C  CA    . GLU A 1 111 ? 15.44725  20.02309  26.49456  1.000 22.15853  ? 111  GLU A CA    1 
ATOM   882  C  C     . GLU A 1 111 ? 16.67835  20.91002  26.36518  1.000 23.08474  ? 111  GLU A C     1 
ATOM   883  O  O     . GLU A 1 111 ? 17.45600  21.04855  27.31682  1.000 23.81041  ? 111  GLU A O     1 
ATOM   884  C  CB    . GLU A 1 111 ? 15.68751  18.66518  25.83228  1.000 22.17034  ? 111  GLU A CB    1 
ATOM   885  C  CG    . GLU A 1 111 ? 16.83107  17.86046  26.43040  1.000 23.79739  ? 111  GLU A CG    1 
ATOM   886  C  CD    . GLU A 1 111 ? 16.58339  17.46759  27.87576  1.000 25.03453  ? 111  GLU A CD    1 
ATOM   887  O  OE1   . GLU A 1 111 ? 15.40500  17.38150  28.28046  1.000 24.19312  ? 111  GLU A OE1   1 
ATOM   888  O  OE2   . GLU A 1 111 ? 17.56963  17.23746  28.60699  1.000 25.73833  ? 111  GLU A OE2   1 
ATOM   889  N  N     . SER A 1 112 ? 16.87159  21.52150  25.19490  1.000 25.79733  ? 112  SER A N     1 
ATOM   890  C  CA    . SER A 1 112 ? 18.00785  22.41797  25.01459  1.000 26.52560  ? 112  SER A CA    1 
ATOM   891  C  C     . SER A 1 112 ? 17.90954  23.62039  25.94484  1.000 26.77770  ? 112  SER A C     1 
ATOM   892  O  O     . SER A 1 112 ? 18.92019  24.07622  26.49233  1.000 27.68482  ? 112  SER A O     1 
ATOM   893  C  CB    . SER A 1 112 ? 18.09432  22.86792  23.55587  1.000 26.12427  ? 112  SER A CB    1 
ATOM   894  O  OG    . SER A 1 112 ? 19.20874  23.71848  23.34944  1.000 27.80073  ? 112  SER A OG    1 
ATOM   895  N  N     . HIS A 1 113 ? 16.69660  24.13984  26.14496  1.000 31.02164  ? 113  HIS A N     1 
ATOM   896  C  CA    . HIS A 1 113 ? 16.51377  25.28346  27.03297  1.000 30.72768  ? 113  HIS A CA    1 
ATOM   897  C  C     . HIS A 1 113 ? 16.81193  24.90961  28.48036  1.000 31.46442  ? 113  HIS A C     1 
ATOM   898  O  O     . HIS A 1 113 ? 17.50179  25.64812  29.19306  1.000 32.20785  ? 113  HIS A O     1 
ATOM   899  C  CB    . HIS A 1 113 ? 15.09121  25.82767  26.89633  1.000 29.42578  ? 113  HIS A CB    1 
ATOM   900  C  CG    . HIS A 1 113 ? 14.76864  26.92632  27.86027  1.000 29.78662  ? 113  HIS A CG    1 
ATOM   901  N  ND1   . HIS A 1 113 ? 15.38506  28.15846  27.81904  1.000 30.77403  ? 113  HIS A ND1   1 
ATOM   902  C  CD2   . HIS A 1 113 ? 13.89282  26.97863  28.89179  1.000 30.13573  ? 113  HIS A CD2   1 
ATOM   903  C  CE1   . HIS A 1 113 ? 14.90326  28.92219  28.78335  1.000 30.10920  ? 113  HIS A CE1   1 
ATOM   904  N  NE2   . HIS A 1 113 ? 13.99625  28.23027  29.44894  1.000 30.06543  ? 113  HIS A NE2   1 
ATOM   905  N  N     . LEU A 1 114 ? 16.29988  23.76200  28.93243  1.000 24.79818  ? 114  LEU A N     1 
ATOM   906  C  CA    . LEU A 1 114 ? 16.52944  23.34369  30.31188  1.000 25.90414  ? 114  LEU A CA    1 
ATOM   907  C  C     . LEU A 1 114 ? 18.00540  23.07240  30.57120  1.000 27.02126  ? 114  LEU A C     1 
ATOM   908  O  O     . LEU A 1 114 ? 18.52670  23.40963  31.64013  1.000 27.98972  ? 114  LEU A O     1 
ATOM   909  C  CB    . LEU A 1 114 ? 15.69421  22.10518  30.63247  1.000 25.47300  ? 114  LEU A CB    1 
ATOM   910  C  CG    . LEU A 1 114 ? 14.17989  22.30990  30.62636  1.000 24.84818  ? 114  LEU A CG    1 
ATOM   911  C  CD1   . LEU A 1 114 ? 13.46685  21.05678  31.11632  1.000 24.32825  ? 114  LEU A CD1   1 
ATOM   912  C  CD2   . LEU A 1 114 ? 13.80407  23.51647  31.47151  1.000 24.41108  ? 114  LEU A CD2   1 
ATOM   913  N  N     . LEU A 1 115 ? 18.69804  22.46871  29.60261  1.000 26.02206  ? 115  LEU A N     1 
ATOM   914  C  CA    . LEU A 1 115 ? 20.12137  22.19473  29.76635  1.000 27.30208  ? 115  LEU A CA    1 
ATOM   915  C  C     . LEU A 1 115 ? 20.94679  23.46754  29.89876  1.000 27.30252  ? 115  LEU A C     1 
ATOM   916  O  O     . LEU A 1 115 ? 22.05751  23.41935  30.43747  1.000 28.27073  ? 115  LEU A O     1 
ATOM   917  C  CB    . LEU A 1 115 ? 20.63665  21.36770  28.58855  1.000 27.27852  ? 115  LEU A CB    1 
ATOM   918  C  CG    . LEU A 1 115 ? 20.25739  19.88770  28.58280  1.000 27.86301  ? 115  LEU A CG    1 
ATOM   919  C  CD1   . LEU A 1 115 ? 20.63343  19.25152  27.25473  1.000 27.23655  ? 115  LEU A CD1   1 
ATOM   920  C  CD2   . LEU A 1 115 ? 20.91877  19.15829  29.74312  1.000 28.78541  ? 115  LEU A CD2   1 
ATOM   921  N  N     . SER A 1 116 ? 20.43550  24.59915  29.42255  1.000 35.86984  ? 116  SER A N     1 
ATOM   922  C  CA    . SER A 1 116 ? 21.15595  25.86286  29.46808  1.000 36.02905  ? 116  SER A CA    1 
ATOM   923  C  C     . SER A 1 116 ? 20.69954  26.76752  30.60396  1.000 36.11182  ? 116  SER A C     1 
ATOM   924  O  O     . SER A 1 116 ? 21.23580  27.86950  30.75175  1.000 36.47523  ? 116  SER A O     1 
ATOM   925  C  CB    . SER A 1 116 ? 21.00620  26.59816  28.13282  1.000 35.75683  ? 116  SER A CB    1 
ATOM   926  O  OG    . SER A 1 116 ? 19.75820  27.26695  28.06341  1.000 34.76206  ? 116  SER A OG    1 
ATOM   927  N  N     . LEU A 1 117 ? 19.73152  26.33144  31.40523  1.000 34.34622  ? 117  LEU A N     1 
ATOM   928  C  CA    . LEU A 1 117 ? 19.21768  27.15745  32.48871  1.000 34.56681  ? 117  LEU A CA    1 
ATOM   929  C  C     . LEU A 1 117 ? 20.29270  27.40672  33.54022  1.000 35.38441  ? 117  LEU A C     1 
ATOM   930  O  O     . LEU A 1 117 ? 21.04465  26.50183  33.91209  1.000 36.56447  ? 117  LEU A O     1 
ATOM   931  C  CB    . LEU A 1 117 ? 18.00498  26.48601  33.13091  1.000 33.87722  ? 117  LEU A CB    1 
ATOM   932  C  CG    . LEU A 1 117 ? 16.62332  27.07108  32.83442  1.000 33.56125  ? 117  LEU A CG    1 
ATOM   933  C  CD1   . LEU A 1 117 ? 15.74380  26.98287  34.07065  1.000 32.86716  ? 117  LEU A CD1   1 
ATOM   934  C  CD2   . LEU A 1 117 ? 16.72401  28.51013  32.34353  1.000 32.67583  ? 117  LEU A CD2   1 
ATOM   935  N  N     . ASP A 1 118 ? 20.36115  28.64601  34.02063  0.868 49.07952  ? 118  ASP A N     1 
ATOM   936  C  CA    . ASP A 1 118 ? 21.31131  29.04214  35.05812  0.868 50.15083  ? 118  ASP A CA    1 
ATOM   937  C  C     . ASP A 1 118 ? 20.56010  29.08588  36.38438  0.868 50.05538  ? 118  ASP A C     1 
ATOM   938  O  O     . ASP A 1 118 ? 19.92371  30.08790  36.71854  0.868 50.66218  ? 118  ASP A O     1 
ATOM   939  C  CB    . ASP A 1 118 ? 21.94935  30.38725  34.72673  0.868 51.00801  ? 118  ASP A CB    1 
ATOM   940  C  CG    . ASP A 1 118 ? 23.11990  30.71899  35.63439  0.868 52.89308  ? 118  ASP A CG    1 
ATOM   941  O  OD1   . ASP A 1 118 ? 23.47706  29.87708  36.48569  0.868 53.76690  ? 118  ASP A OD1   1 
ATOM   942  O  OD2   . ASP A 1 118 ? 23.68563  31.82362  35.49431  0.868 53.74929  ? 118  ASP A OD2   1 
ATOM   943  N  N     . LEU A 1 119 ? 20.63638  27.99882  37.13585  1.000 31.82223  ? 119  LEU A N     1 
ATOM   944  C  CA    . LEU A 1 119 ? 19.94735  27.85799  38.40688  1.000 31.84673  ? 119  LEU A CA    1 
ATOM   945  C  C     . LEU A 1 119 ? 20.91642  28.04311  39.56504  1.000 31.86464  ? 119  LEU A C     1 
ATOM   946  O  O     . LEU A 1 119 ? 22.12642  27.85035  39.41360  1.000 32.49754  ? 119  LEU A O     1 
ATOM   947  C  CB    . LEU A 1 119 ? 19.28301  26.47893  38.49403  1.000 31.20519  ? 119  LEU A CB    1 
ATOM   948  C  CG    . LEU A 1 119 ? 18.12222  26.25532  37.52214  1.000 30.30206  ? 119  LEU A CG    1 
ATOM   949  C  CD1   . LEU A 1 119 ? 17.58502  24.83806  37.63436  1.000 29.92929  ? 119  LEU A CD1   1 
ATOM   950  C  CD2   . LEU A 1 119 ? 17.01519  27.27408  37.76079  1.000 29.63824  ? 119  LEU A CD2   1 
ATOM   951  N  N     . PRO A 1 120 ? 20.42030  28.43021  40.74623  1.000 31.54365  ? 120  PRO A N     1 
ATOM   952  C  CA    . PRO A 1 120 ? 21.32484  28.59086  41.89725  1.000 32.22599  ? 120  PRO A CA    1 
ATOM   953  C  C     . PRO A 1 120 ? 21.92503  27.28397  42.38259  1.000 32.29169  ? 120  PRO A C     1 
ATOM   954  O  O     . PRO A 1 120 ? 22.93865  27.31422  43.09022  1.000 32.95656  ? 120  PRO A O     1 
ATOM   955  C  CB    . PRO A 1 120 ? 20.42899  29.22173  42.97512  1.000 31.51536  ? 120  PRO A CB    1 
ATOM   956  C  CG    . PRO A 1 120 ? 19.19438  29.67994  42.26390  1.000 31.02744  ? 120  PRO A CG    1 
ATOM   957  C  CD    . PRO A 1 120 ? 19.03287  28.79437  41.07691  1.000 30.97645  ? 120  PRO A CD    1 
ATOM   958  N  N     . VAL A 1 121 ? 21.33737  26.14898  42.03152  1.000 35.73718  ? 121  VAL A N     1 
ATOM   959  C  CA    . VAL A 1 121 ? 21.81625  24.84235  42.47462  1.000 35.39029  ? 121  VAL A CA    1 
ATOM   960  C  C     . VAL A 1 121 ? 22.10103  24.00932  41.23457  1.000 35.22585  ? 121  VAL A C     1 
ATOM   961  O  O     . VAL A 1 121 ? 21.59282  24.30534  40.13812  1.000 35.04401  ? 121  VAL A O     1 
ATOM   962  C  CB    . VAL A 1 121 ? 20.80215  24.15140  43.41684  1.000 34.46405  ? 121  VAL A CB    1 
ATOM   963  C  CG1   . VAL A 1 121 ? 20.36404  25.10508  44.51550  1.000 34.74632  ? 121  VAL A CG1   1 
ATOM   964  C  CG2   . VAL A 1 121 ? 19.59844  23.66339  42.63179  1.000 34.39582  ? 121  VAL A CG2   1 
ATOM   965  N  N     . PRO A 1 122 ? 22.92830  22.96820  41.35732  1.000 32.21977  ? 122  PRO A N     1 
ATOM   966  C  CA    . PRO A 1 122 ? 23.17725  22.09293  40.20566  1.000 32.15121  ? 122  PRO A CA    1 
ATOM   967  C  C     . PRO A 1 122 ? 21.90660  21.38558  39.75707  1.000 31.88454  ? 122  PRO A C     1 
ATOM   968  O  O     . PRO A 1 122 ? 20.98413  21.15467  40.54282  1.000 31.25356  ? 122  PRO A O     1 
ATOM   969  C  CB    . PRO A 1 122 ? 24.21669  21.09392  40.73055  1.000 31.99502  ? 122  PRO A CB    1 
ATOM   970  C  CG    . PRO A 1 122 ? 24.83612  21.75749  41.90829  1.000 32.35819  ? 122  PRO A CG    1 
ATOM   971  C  CD    . PRO A 1 122 ? 23.76711  22.60965  42.51509  1.000 32.53626  ? 122  PRO A CD    1 
ATOM   972  N  N     . MET A 1 123 ? 21.86764  21.04098  38.47040  1.000 38.26155  ? 123  MET A N     1 
ATOM   973  C  CA    . MET A 1 123 ? 20.72503  20.35757  37.87024  1.000 37.68039  ? 123  MET A CA    1 
ATOM   974  C  C     . MET A 1 123 ? 21.22032  19.09255  37.18186  1.000 37.89234  ? 123  MET A C     1 
ATOM   975  O  O     . MET A 1 123 ? 21.97985  19.16592  36.21038  1.000 38.11419  ? 123  MET A O     1 
ATOM   976  C  CB    . MET A 1 123 ? 19.99285  21.26833  36.88370  1.000 38.06862  ? 123  MET A CB    1 
ATOM   977  C  CG    . MET A 1 123 ? 18.93374  20.56586  36.04637  1.000 37.33205  ? 123  MET A CG    1 
ATOM   978  S  SD    . MET A 1 123 ? 17.39340  21.50490  35.95422  1.000 38.77405  ? 123  MET A SD    1 
ATOM   979  C  CE    . MET A 1 123 ? 17.72858  22.58431  34.56886  1.000 37.01978  ? 123  MET A CE    1 
ATOM   980  N  N     . GLU A 1 124 ? 20.79269  17.93776  37.68390  1.000 35.94523  ? 124  GLU A N     1 
ATOM   981  C  CA    . GLU A 1 124 ? 21.16163  16.64685  37.11928  1.000 35.29902  ? 124  GLU A CA    1 
ATOM   982  C  C     . GLU A 1 124 ? 20.06363  16.17889  36.17237  1.000 35.30974  ? 124  GLU A C     1 
ATOM   983  O  O     . GLU A 1 124 ? 18.88061  16.19471  36.52892  1.000 34.48441  ? 124  GLU A O     1 
ATOM   984  C  CB    . GLU A 1 124 ? 21.39610  15.61683  38.22787  1.000 35.33828  ? 124  GLU A CB    1 
ATOM   985  C  CG    . GLU A 1 124 ? 20.93018  14.20137  37.89794  1.000 36.48030  ? 124  GLU A CG    1 
ATOM   986  C  CD    . GLU A 1 124 ? 21.46708  13.16262  38.86946  1.000 36.21810  ? 124  GLU A CD    1 
ATOM   987  O  OE1   . GLU A 1 124 ? 21.41649  13.40656  40.09370  1.000 36.93049  ? 124  GLU A OE1   1 
ATOM   988  O  OE2   . GLU A 1 124 ? 21.93150  12.09726  38.40981  1.000 36.46583  ? 124  GLU A OE2   1 
ATOM   989  N  N     . THR A 1 125 ? 20.45616  15.77519  34.96712  1.000 25.91062  ? 125  THR A N     1 
ATOM   990  C  CA    . THR A 1 125 ? 19.52603  15.30685  33.94696  1.000 25.99139  ? 125  THR A CA    1 
ATOM   991  C  C     . THR A 1 125 ? 19.75664  13.82072  33.70880  1.000 25.50146  ? 125  THR A C     1 
ATOM   992  O  O     . THR A 1 125 ? 20.83099  13.42207  33.24639  1.000 26.47307  ? 125  THR A O     1 
ATOM   993  C  CB    . THR A 1 125 ? 19.69542  16.08893  32.64482  1.000 26.18494  ? 125  THR A CB    1 
ATOM   994  O  OG1   . THR A 1 125 ? 19.31996  17.45590  32.85491  1.000 26.47594  ? 125  THR A OG1   1 
ATOM   995  C  CG2   . THR A 1 125 ? 18.82132  15.49277  31.55327  1.000 25.88485  ? 125  THR A CG2   1 
ATOM   996  N  N     . ARG A 1 126 ? 18.75008  13.01024  34.01912  1.000 25.77360  ? 126  ARG A N     1 
ATOM   997  C  CA    . ARG A 1 126 ? 18.82332  11.56674  33.85940  1.000 24.92432  ? 126  ARG A CA    1 
ATOM   998  C  C     . ARG A 1 126 ? 18.09883  11.13520  32.59045  1.000 24.43679  ? 126  ARG A C     1 
ATOM   999  O  O     . ARG A 1 126 ? 17.10656  11.74318  32.18183  1.000 24.46271  ? 126  ARG A O     1 
ATOM   1000 C  CB    . ARG A 1 126 ? 18.21913  10.85452  35.07166  1.000 24.06304  ? 126  ARG A CB    1 
ATOM   1001 C  CG    . ARG A 1 126 ? 18.94493  11.13430  36.37826  1.000 24.55980  ? 126  ARG A CG    1 
ATOM   1002 C  CD    . ARG A 1 126 ? 18.21601  10.52146  37.56238  1.000 23.58834  ? 126  ARG A CD    1 
ATOM   1003 N  NE    . ARG A 1 126 ? 18.88192  10.82590  38.82288  1.000 23.87197  ? 126  ARG A NE    1 
ATOM   1004 C  CZ    . ARG A 1 126 ? 18.40950  10.50114  40.01846  1.000 24.13994  ? 126  ARG A CZ    1 
ATOM   1005 N  NH1   . ARG A 1 126 ? 17.26352  9.85435   40.15676  1.000 22.99915  ? 126  ARG A NH1   1 
ATOM   1006 N  NH2   . ARG A 1 126 ? 19.10291  10.83637  41.10311  1.000 24.72158  ? 126  ARG A NH2   1 
ATOM   1007 N  N     . GLU A 1 127 ? 18.60887  10.07590  31.96864  1.000 23.38130  ? 127  GLU A N     1 
ATOM   1008 C  CA    . GLU A 1 127 ? 17.99180  9.54710   30.76140  1.000 23.22413  ? 127  GLU A CA    1 
ATOM   1009 C  C     . GLU A 1 127 ? 16.63860  8.91822   31.07746  1.000 21.91900  ? 127  GLU A C     1 
ATOM   1010 O  O     . GLU A 1 127 ? 16.41134  8.38692   32.16753  1.000 21.29040  ? 127  GLU A O     1 
ATOM   1011 C  CB    . GLU A 1 127 ? 18.90500  8.51314   30.10134  1.000 23.05325  ? 127  GLU A CB    1 
ATOM   1012 C  CG    . GLU A 1 127 ? 20.08365  9.11106   29.34722  1.000 24.24858  ? 127  GLU A CG    1 
ATOM   1013 C  CD    . GLU A 1 127 ? 19.66467  10.18787  28.36375  1.000 25.28988  ? 127  GLU A CD    1 
ATOM   1014 O  OE1   . GLU A 1 127 ? 19.06196  9.84837   27.32293  1.000 24.77641  ? 127  GLU A OE1   1 
ATOM   1015 O  OE2   . GLU A 1 127 ? 19.93405  11.37639  28.63403  1.000 27.23597  ? 127  GLU A OE2   1 
ATOM   1016 N  N     . ASP A 1 128 ? 15.73346  8.98255   30.10276  1.000 24.30653  ? 128  ASP A N     1 
ATOM   1017 C  CA    . ASP A 1 128 ? 14.39082  8.42022   30.24435  1.000 22.93281  ? 128  ASP A CA    1 
ATOM   1018 C  C     . ASP A 1 128 ? 14.45664  6.94228   29.88353  1.000 22.69240  ? 128  ASP A C     1 
ATOM   1019 O  O     . ASP A 1 128 ? 14.22662  6.54925   28.73961  1.000 23.28364  ? 128  ASP A O     1 
ATOM   1020 C  CB    . ASP A 1 128 ? 13.39854  9.16961   29.36435  1.000 22.22414  ? 128  ASP A CB    1 
ATOM   1021 C  CG    . ASP A 1 128 ? 11.95965  8.79378   29.65566  1.000 21.05650  ? 128  ASP A CG    1 
ATOM   1022 O  OD1   . ASP A 1 128 ? 11.73215  7.89926   30.49834  1.000 20.58771  ? 128  ASP A OD1   1 
ATOM   1023 O  OD2   . ASP A 1 128 ? 11.05277  9.39569   29.04241  1.000 20.94336  ? 128  ASP A OD2   1 
ATOM   1024 N  N     . ASP A 1 129 ? 14.76360  6.10710   30.87353  1.000 37.81391  ? 129  ASP A N     1 
ATOM   1025 C  CA    . ASP A 1 129 ? 14.87769  4.67324   30.63962  1.000 37.86652  ? 129  ASP A CA    1 
ATOM   1026 C  C     . ASP A 1 129 ? 13.52585  3.96704   30.56179  1.000 36.67832  ? 129  ASP A C     1 
ATOM   1027 O  O     . ASP A 1 129 ? 13.48392  2.73308   30.62633  1.000 35.89712  ? 129  ASP A O     1 
ATOM   1028 C  CB    . ASP A 1 129 ? 15.75939  4.02845   31.71532  1.000 37.72709  ? 129  ASP A CB    1 
ATOM   1029 C  CG    . ASP A 1 129 ? 15.29623  4.33950   33.12364  1.000 38.71265  ? 129  ASP A CG    1 
ATOM   1030 O  OD1   . ASP A 1 129 ? 14.07147  4.37680   33.37090  1.000 38.27868  ? 129  ASP A OD1   1 
ATOM   1031 O  OD2   . ASP A 1 129 ? 16.16910  4.53145   33.99614  1.000 40.34057  ? 129  ASP A OD2   1 
ATOM   1032 N  N     . ARG A 1 130 ? 12.42470  4.71167   30.43181  1.000 24.76583  ? 130  ARG A N     1 
ATOM   1033 C  CA    . ARG A 1 130 ? 11.15207  4.08204   30.10267  1.000 24.59952  ? 130  ARG A CA    1 
ATOM   1034 C  C     . ARG A 1 130 ? 11.12852  3.58120   28.66552  1.000 24.26189  ? 130  ARG A C     1 
ATOM   1035 O  O     . ARG A 1 130 ? 10.32565  2.70056   28.34015  1.000 23.87383  ? 130  ARG A O     1 
ATOM   1036 C  CB    . ARG A 1 130 ? 9.99442   5.05435   30.33782  1.000 23.28868  ? 130  ARG A CB    1 
ATOM   1037 C  CG    . ARG A 1 130 ? 9.76274   5.40562   31.80032  1.000 22.79359  ? 130  ARG A CG    1 
ATOM   1038 C  CD    . ARG A 1 130 ? 8.66408   6.44780   31.94669  1.000 22.73690  ? 130  ARG A CD    1 
ATOM   1039 N  NE    . ARG A 1 130 ? 8.98285   7.68177   31.23707  1.000 22.71646  ? 130  ARG A NE    1 
ATOM   1040 C  CZ    . ARG A 1 130 ? 8.08882   8.59296   30.87707  1.000 22.70117  ? 130  ARG A CZ    1 
ATOM   1041 N  NH1   . ARG A 1 130 ? 6.80181   8.44376   31.14682  1.000 21.36044  ? 130  ARG A NH1   1 
ATOM   1042 N  NH2   . ARG A 1 130 ? 8.49650   9.68182   30.23082  1.000 22.69699  ? 130  ARG A NH2   1 
ATOM   1043 N  N     . PHE A 1 131 ? 11.98702  4.12059   27.80442  1.000 21.84133  ? 131  PHE A N     1 
ATOM   1044 C  CA    . PHE A 1 131 ? 12.13054  3.60608   26.45443  1.000 21.85038  ? 131  PHE A CA    1 
ATOM   1045 C  C     . PHE A 1 131 ? 13.06418  2.39912   26.45123  1.000 22.11099  ? 131  PHE A C     1 
ATOM   1046 O  O     . PHE A 1 131 ? 13.90305  2.22359   27.33970  1.000 22.59978  ? 131  PHE A O     1 
ATOM   1047 C  CB    . PHE A 1 131 ? 12.65554  4.69275   25.51396  1.000 22.75074  ? 131  PHE A CB    1 
ATOM   1048 C  CG    . PHE A 1 131 ? 11.67431  5.80622   25.26579  1.000 22.50527  ? 131  PHE A CG    1 
ATOM   1049 C  CD1   . PHE A 1 131 ? 10.72634  5.70285   24.25826  1.000 21.86400  ? 131  PHE A CD1   1 
ATOM   1050 C  CD2   . PHE A 1 131 ? 11.69698  6.95554   26.04175  1.000 22.79428  ? 131  PHE A CD2   1 
ATOM   1051 C  CE1   . PHE A 1 131 ? 9.81918   6.72532   24.02908  1.000 21.55950  ? 131  PHE A CE1   1 
ATOM   1052 C  CE2   . PHE A 1 131 ? 10.79371  7.98255   25.81632  1.000 22.02624  ? 131  PHE A CE2   1 
ATOM   1053 C  CZ    . PHE A 1 131 ? 9.85434   7.86643   24.80944  1.000 21.93344  ? 131  PHE A CZ    1 
ATOM   1054 N  N     . LEU A 1 132 ? 12.90254  1.55484   25.43451  1.000 24.17784  ? 132  LEU A N     1 
ATOM   1055 C  CA    . LEU A 1 132 ? 13.65627  0.31176   25.35045  1.000 23.56026  ? 132  LEU A CA    1 
ATOM   1056 C  C     . LEU A 1 132 ? 15.01695  0.47669   24.68923  1.000 24.44489  ? 132  LEU A C     1 
ATOM   1057 O  O     . LEU A 1 132 ? 15.88686  -0.38178  24.87293  1.000 24.51071  ? 132  LEU A O     1 
ATOM   1058 C  CB    . LEU A 1 132 ? 12.83995  -0.73834  24.59393  1.000 23.21871  ? 132  LEU A CB    1 
ATOM   1059 C  CG    . LEU A 1 132 ? 11.44235  -0.95751  25.17408  1.000 22.96381  ? 132  LEU A CG    1 
ATOM   1060 C  CD1   . LEU A 1 132 ? 10.62321  -1.88063  24.28789  1.000 22.96736  ? 132  LEU A CD1   1 
ATOM   1061 C  CD2   . LEU A 1 132 ? 11.53655  -1.50761  26.59222  1.000 22.62220  ? 132  LEU A CD2   1 
ATOM   1062 N  N     . CYS A 1 133 ? 15.22167  1.54950   23.93058  1.000 21.19867  ? 133  CYS A N     1 
ATOM   1063 C  CA    . CYS A 1 133 ? 16.50159  1.84300   23.29917  1.000 21.66124  ? 133  CYS A CA    1 
ATOM   1064 C  C     . CYS A 1 133 ? 16.95102  3.22648   23.74317  1.000 22.01851  ? 133  CYS A C     1 
ATOM   1065 O  O     . CYS A 1 133 ? 16.28589  4.22399   23.44303  1.000 22.03343  ? 133  CYS A O     1 
ATOM   1066 C  CB    . CYS A 1 133 ? 16.39484  1.77294   21.77404  1.000 21.60219  ? 133  CYS A CB    1 
ATOM   1067 S  SG    . CYS A 1 133 ? 17.97898  1.91650   20.91199  1.000 22.14076  ? 133  CYS A SG    1 
ATOM   1068 N  N     . SER A 1 134 ? 18.06920  3.28505   24.46014  1.000 22.08922  ? 134  SER A N     1 
ATOM   1069 C  CA    . SER A 1 134 ? 18.57917  4.56346   24.92677  1.000 22.47385  ? 134  SER A CA    1 
ATOM   1070 C  C     . SER A 1 134 ? 19.06858  5.40266   23.75020  1.000 22.73489  ? 134  SER A C     1 
ATOM   1071 O  O     . SER A 1 134 ? 19.33473  4.89605   22.65663  1.000 22.69649  ? 134  SER A O     1 
ATOM   1072 C  CB    . SER A 1 134 ? 19.71078  4.35649   25.93329  1.000 23.00561  ? 134  SER A CB    1 
ATOM   1073 O  OG    . SER A 1 134 ? 20.95740  4.21676   25.27517  1.000 23.49216  ? 134  SER A OG    1 
ATOM   1074 N  N     . ARG A 1 135 ? 19.17613  6.71189   23.98601  1.000 25.26635  ? 135  ARG A N     1 
ATOM   1075 C  CA    . ARG A 1 135 ? 19.68525  7.60202   22.94852  1.000 26.19870  ? 135  ARG A CA    1 
ATOM   1076 C  C     . ARG A 1 135 ? 21.10611  7.22308   22.55329  1.000 27.10938  ? 135  ARG A C     1 
ATOM   1077 O  O     . ARG A 1 135 ? 21.46527  7.27470   21.37124  1.000 28.09417  ? 135  ARG A O     1 
ATOM   1078 C  CB    . ARG A 1 135 ? 19.62679  9.05446   23.42374  1.000 25.57880  ? 135  ARG A CB    1 
ATOM   1079 C  CG    . ARG A 1 135 ? 18.21622  9.57788   23.64922  1.000 24.71047  ? 135  ARG A CG    1 
ATOM   1080 C  CD    . ARG A 1 135 ? 18.19406  11.09556  23.73834  1.000 24.25170  ? 135  ARG A CD    1 
ATOM   1081 N  NE    . ARG A 1 135 ? 18.65843  11.57261  25.03522  1.000 24.45026  ? 135  ARG A NE    1 
ATOM   1082 C  CZ    . ARG A 1 135 ? 18.83271  12.84975  25.34690  1.000 24.85304  ? 135  ARG A CZ    1 
ATOM   1083 N  NH1   . ARG A 1 135 ? 18.58787  13.81454  24.47441  1.000 25.13367  ? 135  ARG A NH1   1 
ATOM   1084 N  NH2   . ARG A 1 135 ? 19.26339  13.16730  26.56492  1.000 24.51622  ? 135  ARG A NH2   1 
ATOM   1085 N  N     . ALA A 1 136 ? 21.92638  6.82793   23.52904  1.000 23.30720  ? 136  ALA A N     1 
ATOM   1086 C  CA    . ALA A 1 136 ? 23.29582  6.42939   23.22429  1.000 24.16711  ? 136  ALA A CA    1 
ATOM   1087 C  C     . ALA A 1 136 ? 23.33127  5.10977   22.46464  1.000 25.08531  ? 136  ALA A C     1 
ATOM   1088 O  O     . ALA A 1 136 ? 24.16916  4.92269   21.57407  1.000 26.05463  ? 136  ALA A O     1 
ATOM   1089 C  CB    . ALA A 1 136 ? 24.11254  6.33080   24.51149  1.000 23.95911  ? 136  ALA A CB    1 
ATOM   1090 N  N     . GLN A 1 137 ? 22.42769  4.18448   22.79890  1.000 25.84870  ? 137  GLN A N     1 
ATOM   1091 C  CA    . GLN A 1 137 ? 22.40956  2.89127   22.12268  1.000 26.95568  ? 137  GLN A CA    1 
ATOM   1092 C  C     . GLN A 1 137 ? 22.01477  3.03497   20.65800  1.000 27.15019  ? 137  GLN A C     1 
ATOM   1093 O  O     . GLN A 1 137 ? 22.54045  2.32117   19.79631  1.000 27.93771  ? 137  GLN A O     1 
ATOM   1094 C  CB    . GLN A 1 137 ? 21.46245  1.93349   22.84508  1.000 26.72533  ? 137  GLN A CB    1 
ATOM   1095 C  CG    . GLN A 1 137 ? 22.03308  1.36766   24.13599  1.000 26.54522  ? 137  GLN A CG    1 
ATOM   1096 C  CD    . GLN A 1 137 ? 21.02541  0.54453   24.91261  1.000 26.37397  ? 137  GLN A CD    1 
ATOM   1097 O  OE1   . GLN A 1 137 ? 19.82387  0.81487   24.87805  1.000 25.21966  ? 137  GLN A OE1   1 
ATOM   1098 N  NE2   . GLN A 1 137 ? 21.51155  -0.46935  25.61934  1.000 26.83092  ? 137  GLN A NE2   1 
ATOM   1099 N  N     . PHE A 1 138 ? 21.09216  3.95070   20.35313  1.000 22.13937  ? 138  PHE A N     1 
ATOM   1100 C  CA    . PHE A 1 138 ? 20.71044  4.15720   18.96058  1.000 22.23369  ? 138  PHE A CA    1 
ATOM   1101 C  C     . PHE A 1 138 ? 21.84189  4.79634   18.16881  1.000 22.55456  ? 138  PHE A C     1 
ATOM   1102 O  O     . PHE A 1 138 ? 22.10507  4.40386   17.02627  1.000 22.62471  ? 138  PHE A O     1 
ATOM   1103 C  CB    . PHE A 1 138 ? 19.45171  5.01610   18.86918  1.000 21.88037  ? 138  PHE A CB    1 
ATOM   1104 C  CG    . PHE A 1 138 ? 18.85309  5.05487   17.49190  1.000 21.59640  ? 138  PHE A CG    1 
ATOM   1105 C  CD1   . PHE A 1 138 ? 17.95043  4.08573   17.08910  1.000 21.01490  ? 138  PHE A CD1   1 
ATOM   1106 C  CD2   . PHE A 1 138 ? 19.20476  6.05023   16.59494  1.000 20.80907  ? 138  PHE A CD2   1 
ATOM   1107 C  CE1   . PHE A 1 138 ? 17.40149  4.11233   15.82186  1.000 20.81268  ? 138  PHE A CE1   1 
ATOM   1108 C  CE2   . PHE A 1 138 ? 18.65952  6.08330   15.32483  1.000 20.20043  ? 138  PHE A CE2   1 
ATOM   1109 C  CZ    . PHE A 1 138 ? 17.75731  5.11349   14.93725  1.000 20.86327  ? 138  PHE A CZ    1 
ATOM   1110 N  N     . ALA A 1 139 ? 22.51463  5.78937   18.75434  1.000 26.10788  ? 139  ALA A N     1 
ATOM   1111 C  CA    . ALA A 1 139 ? 23.63730  6.41997   18.07026  1.000 26.29250  ? 139  ALA A CA    1 
ATOM   1112 C  C     . ALA A 1 139 ? 24.73549  5.40743   17.77574  1.000 27.10069  ? 139  ALA A C     1 
ATOM   1113 O  O     . ALA A 1 139 ? 25.34973  5.43982   16.70266  1.000 27.90545  ? 139  ALA A O     1 
ATOM   1114 C  CB    . ALA A 1 139 ? 24.17903  7.57896   18.90694  1.000 25.90377  ? 139  ALA A CB    1 
ATOM   1115 N  N     . ALA A 1 140 ? 24.98855  4.49139   18.71362  1.000 27.76417  ? 140  ALA A N     1 
ATOM   1116 C  CA    . ALA A 1 140 ? 25.99416  3.45974   18.48446  1.000 28.37979  ? 140  ALA A CA    1 
ATOM   1117 C  C     . ALA A 1 140 ? 25.58174  2.53140   17.34960  1.000 29.07189  ? 140  ALA A C     1 
ATOM   1118 O  O     . ALA A 1 140 ? 26.41441  2.14333   16.52191  1.000 30.18604  ? 140  ALA A O     1 
ATOM   1119 C  CB    . ALA A 1 140 ? 26.23525  2.66535   19.76817  1.000 28.45552  ? 140  ALA A CB    1 
ATOM   1120 N  N     . TRP A 1 141 ? 24.29847  2.16549   17.29262  1.000 25.78096  ? 141  TRP A N     1 
ATOM   1121 C  CA    . TRP A 1 141 ? 23.82862  1.28737   16.22598  1.000 26.52404  ? 141  TRP A CA    1 
ATOM   1122 C  C     . TRP A 1 141 ? 23.84963  1.99342   14.87668  1.000 26.65042  ? 141  TRP A C     1 
ATOM   1123 O  O     . TRP A 1 141 ? 24.14848  1.37278   13.84957  1.000 27.54178  ? 141  TRP A O     1 
ATOM   1124 C  CB    . TRP A 1 141 ? 22.41907  0.78118   16.53694  1.000 25.91110  ? 141  TRP A CB    1 
ATOM   1125 C  CG    . TRP A 1 141 ? 21.78227  0.05992   15.38151  1.000 27.09266  ? 141  TRP A CG    1 
ATOM   1126 C  CD1   . TRP A 1 141 ? 21.86055  -1.27435  15.10345  1.000 27.56208  ? 141  TRP A CD1   1 
ATOM   1127 C  CD2   . TRP A 1 141 ? 20.97815  0.63856   14.34345  1.000 26.02455  ? 141  TRP A CD2   1 
ATOM   1128 N  NE1   . TRP A 1 141 ? 21.15439  -1.56245  13.95954  1.000 27.44886  ? 141  TRP A NE1   1 
ATOM   1129 C  CE2   . TRP A 1 141 ? 20.60408  -0.40543  13.47364  1.000 26.47359  ? 141  TRP A CE2   1 
ATOM   1130 C  CE3   . TRP A 1 141 ? 20.54000  1.93727   14.06594  1.000 25.28144  ? 141  TRP A CE3   1 
ATOM   1131 C  CZ2   . TRP A 1 141 ? 19.81266  -0.19120  12.34604  1.000 25.96699  ? 141  TRP A CZ2   1 
ATOM   1132 C  CZ3   . TRP A 1 141 ? 19.75325  2.14812   12.94621  1.000 25.34254  ? 141  TRP A CZ3   1 
ATOM   1133 C  CH2   . TRP A 1 141 ? 19.39700  1.08868   12.10081  1.000 25.39945  ? 141  TRP A CH2   1 
ATOM   1134 N  N     . ALA A 1 142 ? 23.52843  3.28620   14.85744  1.000 28.33620  ? 142  ALA A N     1 
ATOM   1135 C  CA    . ALA A 1 142 ? 23.45107  4.03965   13.61374  1.000 28.22935  ? 142  ALA A CA    1 
ATOM   1136 C  C     . ALA A 1 142 ? 24.81391  4.44857   13.07316  1.000 28.37741  ? 142  ALA A C     1 
ATOM   1137 O  O     . ALA A 1 142 ? 24.90052  4.84262   11.90503  1.000 28.47561  ? 142  ALA A O     1 
ATOM   1138 C  CB    . ALA A 1 142 ? 22.58680  5.28762   13.81130  1.000 27.12920  ? 142  ALA A CB    1 
ATOM   1139 N  N     . GLU A 1 143 ? 25.86839  4.36177   13.88203  0.787 25.31426  ? 143  GLU A N     1 
ATOM   1140 C  CA    . GLU A 1 143 ? 27.18600  4.81921   13.45822  1.000 26.08646  ? 143  GLU A CA    1 
ATOM   1141 C  C     . GLU A 1 143 ? 27.68655  4.00935   12.26849  1.000 26.90110  ? 143  GLU A C     1 
ATOM   1142 O  O     . GLU A 1 143 ? 27.66209  2.77555   12.28404  0.797 27.10930  ? 143  GLU A O     1 
ATOM   1143 C  CB    . GLU A 1 143 ? 28.17533  4.71851   14.62087  1.000 26.52782  ? 143  GLU A CB    1 
ATOM   1144 C  CG    . GLU A 1 143 ? 29.42534  5.57044   14.45460  1.000 27.44165  ? 143  GLU A CG    1 
ATOM   1145 C  CD    . GLU A 1 143 ? 30.61053  5.02974   15.23285  0.551 28.29359  ? 143  GLU A CD    1 
ATOM   1146 O  OE1   . GLU A 1 143 ? 31.25035  5.81462   15.96438  0.284 28.61713  ? 143  GLU A OE1   1 
ATOM   1147 O  OE2   . GLU A 1 143 ? 30.90365  3.82199   15.11307  0.343 29.52300  ? 143  GLU A OE2   1 
ATOM   1148 N  N     . GLY A 1 144 ? 28.13937  4.71253   11.23093  1.000 27.64665  ? 144  GLY A N     1 
ATOM   1149 C  CA    . GLY A 1 144 ? 28.69736  4.07821   10.05689  1.000 28.69302  ? 144  GLY A CA    1 
ATOM   1150 C  C     . GLY A 1 144 ? 27.69318  3.56690   9.04763   1.000 28.40198  ? 144  GLY A C     1 
ATOM   1151 O  O     . GLY A 1 144 ? 28.10298  3.10585   7.97448   1.000 29.33845  ? 144  GLY A O     1 
ATOM   1152 N  N     . ARG A 1 145 ? 26.39760  3.62965   9.34363   1.000 31.32579  ? 145  ARG A N     1 
ATOM   1153 C  CA    . ARG A 1 145 ? 25.36969  3.13581   8.43591   1.000 31.01976  ? 145  ARG A CA    1 
ATOM   1154 C  C     . ARG A 1 145 ? 24.99059  4.23781   7.45510   1.000 30.38341  ? 145  ARG A C     1 
ATOM   1155 O  O     . ARG A 1 145 ? 24.48855  5.29185   7.86093   1.000 30.37205  ? 145  ARG A O     1 
ATOM   1156 C  CB    . ARG A 1 145 ? 24.14326  2.66105   9.21289   1.000 31.13887  ? 145  ARG A CB    1 
ATOM   1157 C  CG    . ARG A 1 145 ? 24.39649  1.43304   10.06684  1.000 31.56778  ? 145  ARG A CG    1 
ATOM   1158 C  CD    . ARG A 1 145 ? 23.11084  0.89562   10.66452  1.000 31.21938  ? 145  ARG A CD    1 
ATOM   1159 N  NE    . ARG A 1 145 ? 23.37972  -0.02915  11.75810  1.000 32.34529  ? 145  ARG A NE    1 
ATOM   1160 C  CZ    . ARG A 1 145 ? 23.65784  -1.31535  11.59893  1.000 32.95812  ? 145  ARG A CZ    1 
ATOM   1161 N  NH1   . ARG A 1 145 ? 23.69692  -1.87071  10.39856  1.000 33.42495  ? 145  ARG A NH1   1 
ATOM   1162 N  NH2   . ARG A 1 145 ? 23.90543  -2.06258  12.67072  1.000 34.00999  ? 145  ARG A NH2   1 
ATOM   1163 N  N     . ARG A 1 146 ? 25.22525  3.99039   6.16462   1.000 41.70799  ? 146  ARG A N     1 
ATOM   1164 C  CA    . ARG A 1 146 ? 24.93354  4.99841   5.15266   1.000 41.81799  ? 146  ARG A CA    1 
ATOM   1165 C  C     . ARG A 1 146 ? 23.43947  5.24909   5.00001   1.000 40.92385  ? 146  ARG A C     1 
ATOM   1166 O  O     . ARG A 1 146 ? 23.05006  6.28655   4.45362   1.000 40.79256  ? 146  ARG A O     1 
ATOM   1167 C  CB    . ARG A 1 146 ? 25.54899  4.59009   3.81375   1.000 41.73971  ? 146  ARG A CB    1 
ATOM   1168 C  CG    . ARG A 1 146 ? 27.06665  4.70217   3.79315   1.000 42.63522  ? 146  ARG A CG    1 
ATOM   1169 C  CD    . ARG A 1 146 ? 27.61468  4.70223   2.37877   1.000 43.01062  ? 146  ARG A CD    1 
ATOM   1170 N  NE    . ARG A 1 146 ? 29.04679  4.97732   2.34607   1.000 44.30270  ? 146  ARG A NE    1 
ATOM   1171 C  CZ    . ARG A 1 146 ? 29.58137  6.18863   2.42443   1.000 43.78507  ? 146  ARG A CZ    1 
ATOM   1172 N  NH1   . ARG A 1 146 ? 28.82932  7.26985   2.55364   1.000 42.49153  ? 146  ARG A NH1   1 
ATOM   1173 N  NH2   . ARG A 1 146 ? 30.90381  6.31861   2.36906   1.000 44.06496  ? 146  ARG A NH2   1 
ATOM   1174 N  N     . GLU A 1 147 ? 22.59934  4.32764   5.46346   1.000 36.79287  ? 147  GLU A N     1 
ATOM   1175 C  CA    . GLU A 1 147 ? 21.17069  4.57702   5.56630   1.000 36.23882  ? 147  GLU A CA    1 
ATOM   1176 C  C     . GLU A 1 147 ? 20.62169  3.74194   6.71311   1.000 36.35298  ? 147  GLU A C     1 
ATOM   1177 O  O     . GLU A 1 147 ? 21.09578  2.63321   6.97787   1.000 36.33569  ? 147  GLU A O     1 
ATOM   1178 C  CB    . GLU A 1 147 ? 20.43390  4.27536   4.25270   1.000 36.14616  ? 147  GLU A CB    1 
ATOM   1179 C  CG    . GLU A 1 147 ? 19.77613  2.91095   4.17973   1.000 37.49496  ? 147  GLU A CG    1 
ATOM   1180 C  CD    . GLU A 1 147 ? 19.54133  2.45534   2.75325   1.000 39.46712  ? 147  GLU A CD    1 
ATOM   1181 O  OE1   . GLU A 1 147 ? 19.19041  1.27269   2.55648   1.000 39.00768  ? 147  GLU A OE1   1 
ATOM   1182 O  OE2   . GLU A 1 147 ? 19.70022  3.28252   1.82909   1.000 38.94303  ? 147  GLU A OE2   1 
ATOM   1183 N  N     . LEU A 1 148 ? 19.63324  4.29977   7.40644   1.000 25.54018  ? 148  LEU A N     1 
ATOM   1184 C  CA    . LEU A 1 148 ? 19.05975  3.68824   8.59981   1.000 25.46574  ? 148  LEU A CA    1 
ATOM   1185 C  C     . LEU A 1 148 ? 17.72140  3.06269   8.23021   1.000 25.39048  ? 148  LEU A C     1 
ATOM   1186 O  O     . LEU A 1 148 ? 16.74707  3.77376   7.96478   1.000 24.39788  ? 148  LEU A O     1 
ATOM   1187 C  CB    . LEU A 1 148 ? 18.89513  4.72187   9.71063   1.000 24.50235  ? 148  LEU A CB    1 
ATOM   1188 C  CG    . LEU A 1 148 ? 20.10831  5.62107   9.95026   1.000 25.31324  ? 148  LEU A CG    1 
ATOM   1189 C  CD1   . LEU A 1 148 ? 19.80562  6.67110   11.00950  1.000 23.83126  ? 148  LEU A CD1   1 
ATOM   1190 C  CD2   . LEU A 1 148 ? 21.31820  4.78448   10.34018  1.000 25.70281  ? 148  LEU A CD2   1 
ATOM   1191 N  N     . ARG A 1 149 ? 17.67372  1.73653   8.21584   1.000 32.43081  ? 149  ARG A N     1 
ATOM   1192 C  CA    . ARG A 1 149 ? 16.47332  1.00104   7.85055   1.000 32.50391  ? 149  ARG A CA    1 
ATOM   1193 C  C     . ARG A 1 149 ? 15.86677  0.37793   9.09836   1.000 32.85576  ? 149  ARG A C     1 
ATOM   1194 O  O     . ARG A 1 149 ? 16.58186  -0.21455  9.91355   1.000 33.20281  ? 149  ARG A O     1 
ATOM   1195 C  CB    . ARG A 1 149 ? 16.78786  -0.07137  6.80936   1.000 36.46005  ? 149  ARG A CB    1 
ATOM   1196 C  CG    . ARG A 1 149 ? 17.39210  0.47932   5.53211   1.000 36.51279  ? 149  ARG A CG    1 
ATOM   1197 C  CD    . ARG A 1 149 ? 17.07291  -0.41056  4.34804   0.636 36.94121  ? 149  ARG A CD    1 
ATOM   1198 N  NE    . ARG A 1 149 ? 16.66086  0.36571   3.18561   0.227 36.68401  ? 149  ARG A NE    1 
ATOM   1199 C  CZ    . ARG A 1 149 ? 15.45845  0.29901   2.63177   0.695 36.52851  ? 149  ARG A CZ    1 
ATOM   1200 N  NH1   . ARG A 1 149 ? 14.52137  -0.50296  3.10970   0.517 36.57688  ? 149  ARG A NH1   1 
ATOM   1201 N  NH2   . ARG A 1 149 ? 15.18850  1.05752   1.57356   0.697 36.39701  ? 149  ARG A NH2   1 
ATOM   1202 N  N     . MET A 1 150 ? 14.54687  0.51395   9.23843   1.000 33.39473  ? 150  MET A N     1 
ATOM   1203 C  CA    . MET A 1 150 ? 13.87419  0.06570   10.45197  1.000 32.79249  ? 150  MET A CA    1 
ATOM   1204 C  C     . MET A 1 150 ? 13.99803  -1.43972  10.65390  1.000 33.93690  ? 150  MET A C     1 
ATOM   1205 O  O     . MET A 1 150 ? 14.01319  -1.90891  11.79710  1.000 34.04761  ? 150  MET A O     1 
ATOM   1206 C  CB    . MET A 1 150 ? 12.40268  0.47969   10.40895  1.000 31.96911  ? 150  MET A CB    1 
ATOM   1207 C  CG    . MET A 1 150 ? 11.76054  0.64010   11.77335  1.000 30.98756  ? 150  MET A CG    1 
ATOM   1208 S  SD    . MET A 1 150 ? 11.08899  -0.91392  12.39710  1.000 33.41049  ? 150  MET A SD    1 
ATOM   1209 C  CE    . MET A 1 150 ? 10.40168  -1.61992  10.90273  1.000 32.01114  ? 150  MET A CE    1 
ATOM   1210 N  N     . GLU A 1 151 ? 14.09852  -2.20951  9.56704   1.000 43.25233  ? 151  GLU A N     1 
ATOM   1211 C  CA    . GLU A 1 151 ? 14.10125  -3.66495  9.69035   1.000 43.58841  ? 151  GLU A CA    1 
ATOM   1212 C  C     . GLU A 1 151 ? 15.33240  -4.16467  10.43766  1.000 44.53201  ? 151  GLU A C     1 
ATOM   1213 O  O     . GLU A 1 151 ? 15.22028  -5.02752  11.31637  1.000 45.27382  ? 151  GLU A O     1 
ATOM   1214 C  CB    . GLU A 1 151 ? 14.01468  -4.31038  8.30834   1.000 47.19808  ? 151  GLU A CB    1 
ATOM   1215 C  CG    . GLU A 1 151 ? 14.67003  -3.49974  7.20642   0.627 47.02736  ? 151  GLU A CG    1 
ATOM   1216 C  CD    . GLU A 1 151 ? 13.67342  -2.66045  6.43285   0.000 46.31700  ? 151  GLU A CD    1 
ATOM   1217 O  OE1   . GLU A 1 151 ? 13.40718  -2.98641  5.25717   0.868 46.90280  ? 151  GLU A OE1   1 
ATOM   1218 O  OE2   . GLU A 1 151 ? 13.15382  -1.67661  7.00116   0.809 45.17224  ? 151  GLU A OE2   1 
ATOM   1219 N  N     . PHE A 1 152 ? 16.51542  -3.64196  10.10399  1.000 36.54519  ? 152  PHE A N     1 
ATOM   1220 C  CA    . PHE A 1 152 ? 17.72535  -4.06949  10.80102  1.000 36.50576  ? 152  PHE A CA    1 
ATOM   1221 C  C     . PHE A 1 152 ? 17.73898  -3.57334  12.24105  1.000 37.21356  ? 152  PHE A C     1 
ATOM   1222 O  O     . PHE A 1 152 ? 18.24658  -4.26089  13.13448  1.000 37.70925  ? 152  PHE A O     1 
ATOM   1223 C  CB    . PHE A 1 152 ? 18.96563  -3.58671  10.05255  1.000 37.14699  ? 152  PHE A CB    1 
ATOM   1224 C  CG    . PHE A 1 152 ? 18.91255  -3.83728  8.57716   1.000 38.39160  ? 152  PHE A CG    1 
ATOM   1225 C  CD1   . PHE A 1 152 ? 18.65782  -2.80253  7.69596   1.000 38.52350  ? 152  PHE A CD1   1 
ATOM   1226 C  CD2   . PHE A 1 152 ? 19.11230  -5.11080  8.07061   1.000 38.98258  ? 152  PHE A CD2   1 
ATOM   1227 C  CE1   . PHE A 1 152 ? 18.60467  -3.02998  6.33423   1.000 38.69678  ? 152  PHE A CE1   1 
ATOM   1228 C  CE2   . PHE A 1 152 ? 19.06154  -5.34596  6.71057   1.000 39.23085  ? 152  PHE A CE2   1 
ATOM   1229 C  CZ    . PHE A 1 152 ? 18.80647  -4.30313  5.84056   1.000 39.67722  ? 152  PHE A CZ    1 
ATOM   1230 N  N     . PHE A 1 153 ? 17.19468  -2.37947  12.48653  1.000 23.61539  ? 153  PHE A N     1 
ATOM   1231 C  CA    . PHE A 1 153 ? 17.04730  -1.91508  13.86132  1.000 23.42885  ? 153  PHE A CA    1 
ATOM   1232 C  C     . PHE A 1 153 ? 16.05300  -2.78010  14.62300  1.000 23.22484  ? 153  PHE A C     1 
ATOM   1233 O  O     . PHE A 1 153 ? 16.27977  -3.11601  15.79130  1.000 23.74178  ? 153  PHE A O     1 
ATOM   1234 C  CB    . PHE A 1 153 ? 16.60979  -0.45079  13.88043  1.000 22.25042  ? 153  PHE A CB    1 
ATOM   1235 C  CG    . PHE A 1 153 ? 16.29072  0.06816   15.25394  1.000 21.75762  ? 153  PHE A CG    1 
ATOM   1236 C  CD1   . PHE A 1 153 ? 17.30300  0.36495   16.15143  1.000 21.94317  ? 153  PHE A CD1   1 
ATOM   1237 C  CD2   . PHE A 1 153 ? 14.97564  0.25779   15.64782  1.000 20.88054  ? 153  PHE A CD2   1 
ATOM   1238 C  CE1   . PHE A 1 153 ? 17.00919  0.84034   17.41580  1.000 21.99412  ? 153  PHE A CE1   1 
ATOM   1239 C  CE2   . PHE A 1 153 ? 14.67513  0.73474   16.90959  1.000 19.93364  ? 153  PHE A CE2   1 
ATOM   1240 C  CZ    . PHE A 1 153 ? 15.69283  1.02774   17.79441  1.000 20.71890  ? 153  PHE A CZ    1 
ATOM   1241 N  N     . TYR A 1 154 ? 14.94875  -3.15314  13.97077  1.000 20.67430  ? 154  TYR A N     1 
ATOM   1242 C  CA    . TYR A 1 154 ? 13.93567  -3.98005  14.61806  1.000 20.49605  ? 154  TYR A CA    1 
ATOM   1243 C  C     . TYR A 1 154 ? 14.50552  -5.33220  15.02540  1.000 21.18629  ? 154  TYR A C     1 
ATOM   1244 O  O     . TYR A 1 154 ? 14.17459  -5.85752  16.09437  1.000 21.11008  ? 154  TYR A O     1 
ATOM   1245 C  CB    . TYR A 1 154 ? 12.74083  -4.15500  13.68077  1.000 20.47475  ? 154  TYR A CB    1 
ATOM   1246 C  CG    . TYR A 1 154 ? 11.70845  -5.15407  14.14916  1.000 20.52625  ? 154  TYR A CG    1 
ATOM   1247 C  CD1   . TYR A 1 154 ? 11.11332  -5.03812  15.39918  1.000 20.03575  ? 154  TYR A CD1   1 
ATOM   1248 C  CD2   . TYR A 1 154 ? 11.32518  -6.21175  13.33664  1.000 21.16776  ? 154  TYR A CD2   1 
ATOM   1249 C  CE1   . TYR A 1 154 ? 10.16652  -5.95108  15.82601  1.000 20.20541  ? 154  TYR A CE1   1 
ATOM   1250 C  CE2   . TYR A 1 154 ? 10.38079  -7.12936  13.75489  1.000 21.33384  ? 154  TYR A CE2   1 
ATOM   1251 C  CZ    . TYR A 1 154 ? 9.80349   -6.99364  14.99889  1.000 20.86076  ? 154  TYR A CZ    1 
ATOM   1252 O  OH    . TYR A 1 154 ? 8.86252   -7.90694  15.41375  1.000 21.14302  ? 154  TYR A OH    1 
ATOM   1253 N  N     . ARG A 1 155 ? 15.36972  -5.90777  14.18806  1.000 31.86201  ? 155  ARG A N     1 
ATOM   1254 C  CA    . ARG A 1 155 ? 15.98979  -7.18317  14.52822  1.000 32.34775  ? 155  ARG A CA    1 
ATOM   1255 C  C     . ARG A 1 155 ? 16.88280  -7.05262  15.75578  1.000 32.76092  ? 155  ARG A C     1 
ATOM   1256 O  O     . ARG A 1 155 ? 16.87774  -7.92817  16.62866  1.000 32.62516  ? 155  ARG A O     1 
ATOM   1257 C  CB    . ARG A 1 155 ? 16.78565  -7.70952  13.33610  1.000 33.05234  ? 155  ARG A CB    1 
ATOM   1258 C  CG    . ARG A 1 155 ? 15.93911  -8.43927  12.31194  1.000 33.71649  ? 155  ARG A CG    1 
ATOM   1259 C  CD    . ARG A 1 155 ? 16.44976  -8.20093  10.90396  1.000 34.07670  ? 155  ARG A CD    1 
ATOM   1260 N  NE    . ARG A 1 155 ? 16.46261  -9.43355  10.12759  1.000 35.16227  ? 155  ARG A NE    1 
ATOM   1261 C  CZ    . ARG A 1 155 ? 17.19952  -9.62995  9.04346   1.000 36.43671  ? 155  ARG A CZ    1 
ATOM   1262 N  NH1   . ARG A 1 155 ? 18.00595  -8.69061  8.57684   1.000 36.98908  ? 155  ARG A NH1   1 
ATOM   1263 N  NH2   . ARG A 1 155 ? 17.13088  -10.80080 8.41573   1.000 36.62282  ? 155  ARG A NH2   1 
ATOM   1264 N  N     . GLU A 1 156 ? 17.65319  -5.96455  15.84115  1.000 33.73451  ? 156  GLU A N     1 
ATOM   1265 C  CA    . GLU A 1 156 ? 18.48165  -5.73228  17.02052  1.000 33.43792  ? 156  GLU A CA    1 
ATOM   1266 C  C     . GLU A 1 156 ? 17.62895  -5.58620  18.27437  1.000 32.25035  ? 156  GLU A C     1 
ATOM   1267 O  O     . GLU A 1 156 ? 17.97349  -6.12113  19.33472  1.000 31.95196  ? 156  GLU A O     1 
ATOM   1268 C  CB    . GLU A 1 156 ? 19.34706  -4.48847  16.81779  1.000 33.49454  ? 156  GLU A CB    1 
ATOM   1269 C  CG    . GLU A 1 156 ? 20.55079  -4.40396  17.74455  1.000 34.15841  ? 156  GLU A CG    1 
ATOM   1270 C  CD    . GLU A 1 156 ? 21.70634  -5.26669  17.27867  1.000 35.55722  ? 156  GLU A CD    1 
ATOM   1271 O  OE1   . GLU A 1 156 ? 22.47380  -4.81136  16.40319  1.000 36.13653  ? 156  GLU A OE1   1 
ATOM   1272 O  OE2   . GLU A 1 156 ? 21.84725  -6.39955  17.78670  1.000 36.34943  ? 156  GLU A OE2   1 
ATOM   1273 N  N     . MET A 1 157 ? 16.50990  -4.86454  18.17240  1.000 26.64085  ? 157  MET A N     1 
ATOM   1274 C  CA    . MET A 1 157 ? 15.63509  -4.69020  19.32679  1.000 26.33495  ? 157  MET A CA    1 
ATOM   1275 C  C     . MET A 1 157 ? 14.99766  -6.00547  19.75468  1.000 25.85985  ? 157  MET A C     1 
ATOM   1276 O  O     . MET A 1 157 ? 14.73123  -6.20333  20.94534  1.000 25.13184  ? 157  MET A O     1 
ATOM   1277 C  CB    . MET A 1 157 ? 14.55368  -3.65578  19.01652  1.000 25.30711  ? 157  MET A CB    1 
ATOM   1278 C  CG    . MET A 1 157 ? 15.07358  -2.23381  18.88555  1.000 25.62563  ? 157  MET A CG    1 
ATOM   1279 S  SD    . MET A 1 157 ? 15.88884  -1.61627  20.36982  1.000 24.26109  ? 157  MET A SD    1 
ATOM   1280 C  CE    . MET A 1 157 ? 14.68711  -2.05212  21.62463  1.000 22.30477  ? 157  MET A CE    1 
ATOM   1281 N  N     . ARG A 1 158 ? 14.74043  -6.90954  18.80631  1.000 21.48604  ? 158  ARG A N     1 
ATOM   1282 C  CA    . ARG A 1 158 ? 14.20103  -8.21600  19.16732  1.000 22.04639  ? 158  ARG A CA    1 
ATOM   1283 C  C     . ARG A 1 158 ? 15.22036  -9.03146  19.95467  1.000 22.87005  ? 158  ARG A C     1 
ATOM   1284 O  O     . ARG A 1 158 ? 14.85441  -9.76967  20.87635  1.000 23.22472  ? 158  ARG A O     1 
ATOM   1285 C  CB    . ARG A 1 158 ? 13.75731  -8.96975  17.91172  1.000 22.47549  ? 158  ARG A CB    1 
ATOM   1286 C  CG    . ARG A 1 158 ? 12.48932  -8.42559  17.25884  1.000 21.85663  ? 158  ARG A CG    1 
ATOM   1287 C  CD    . ARG A 1 158 ? 11.22890  -8.97883  17.91634  1.000 21.82497  ? 158  ARG A CD    1 
ATOM   1288 N  NE    . ARG A 1 158 ? 11.11550  -10.42385 17.75951  1.000 22.76548  ? 158  ARG A NE    1 
ATOM   1289 C  CZ    . ARG A 1 158 ? 10.70008  -11.03069 16.65524  1.000 23.22239  ? 158  ARG A CZ    1 
ATOM   1290 N  NH1   . ARG A 1 158 ? 10.31789  -10.34444 15.59055  1.000 22.84436  ? 158  ARG A NH1   1 
ATOM   1291 N  NH2   . ARG A 1 158 ? 10.66890  -12.36032 16.61786  1.000 24.17708  ? 158  ARG A NH2   1 
ATOM   1292 N  N     . ARG A 1 159 ? 16.50512  -8.90731  19.61064  1.000 35.13135  ? 159  ARG A N     1 
ATOM   1293 C  CA    . ARG A 1 159 ? 17.54157  -9.61622  20.35482  1.000 34.34498  ? 159  ARG A CA    1 
ATOM   1294 C  C     . ARG A 1 159 ? 17.77820  -8.98060  21.71902  1.000 33.56896  ? 159  ARG A C     1 
ATOM   1295 O  O     . ARG A 1 159 ? 17.95877  -9.68990  22.71549  1.000 33.94359  ? 159  ARG A O     1 
ATOM   1296 C  CB    . ARG A 1 159 ? 18.84055  -9.64848  19.55065  1.000 35.79480  ? 159  ARG A CB    1 
ATOM   1297 C  CG    . ARG A 1 159 ? 18.67163  -10.09430 18.11053  1.000 36.52776  ? 159  ARG A CG    1 
ATOM   1298 C  CD    . ARG A 1 159 ? 19.78336  -11.03949 17.69567  1.000 38.03602  ? 159  ARG A CD    1 
ATOM   1299 N  NE    . ARG A 1 159 ? 20.14507  -10.87786 16.29261  1.000 38.98744  ? 159  ARG A NE    1 
ATOM   1300 C  CZ    . ARG A 1 159 ? 20.24145  -11.87700 15.42608  1.000 39.74691  ? 159  ARG A CZ    1 
ATOM   1301 N  NH1   . ARG A 1 159 ? 20.00370  -13.12849 15.78519  1.000 38.52328  ? 159  ARG A NH1   1 
ATOM   1302 N  NH2   . ARG A 1 159 ? 20.58626  -11.61436 14.16819  1.000 39.19505  ? 159  ARG A NH2   1 
ATOM   1303 N  N     . LYS A 1 160 ? 17.78788  -7.64630  21.78404  1.000 39.49222  ? 160  LYS A N     1 
ATOM   1304 C  CA    . LYS A 1 160 ? 18.00170  -6.96974  23.05981  1.000 38.54189  ? 160  LYS A CA    1 
ATOM   1305 C  C     . LYS A 1 160 ? 16.86723  -7.26479  24.03172  1.000 37.52965  ? 160  LYS A C     1 
ATOM   1306 O  O     . LYS A 1 160 ? 17.10291  -7.64772  25.18312  1.000 37.06262  ? 160  LYS A O     1 
ATOM   1307 C  CB    . LYS A 1 160 ? 18.14304  -5.46208  22.84493  1.000 38.24621  ? 160  LYS A CB    1 
ATOM   1308 C  CG    . LYS A 1 160 ? 18.61633  -4.71196  24.08403  1.000 37.37527  ? 160  LYS A CG    1 
ATOM   1309 C  CD    . LYS A 1 160 ? 17.95238  -3.34722  24.21640  0.751 36.47762  ? 160  LYS A CD    1 
ATOM   1310 C  CE    . LYS A 1 160 ? 18.15469  -2.49659  22.97041  0.690 36.90836  ? 160  LYS A CE    1 
ATOM   1311 N  NZ    . LYS A 1 160 ? 19.59422  -2.27633  22.66121  0.886 37.68438  ? 160  LYS A NZ    1 
ATOM   1312 N  N     . THR A 1 161 ? 15.62361  -7.09336  23.58294  1.000 25.58023  ? 161  THR A N     1 
ATOM   1313 C  CA    . THR A 1 161 ? 14.47676  -7.32152  24.45129  1.000 24.73215  ? 161  THR A CA    1 
ATOM   1314 C  C     . THR A 1 161 ? 14.16692  -8.79889  24.64618  1.000 25.09424  ? 161  THR A C     1 
ATOM   1315 O  O     . THR A 1 161 ? 13.47179  -9.14858  25.60614  1.000 24.03673  ? 161  THR A O     1 
ATOM   1316 C  CB    . THR A 1 161 ? 13.23772  -6.61729  23.89224  1.000 23.67411  ? 161  THR A CB    1 
ATOM   1317 O  OG1   . THR A 1 161 ? 12.91695  -7.15937  22.60525  1.000 25.00464  ? 161  THR A OG1   1 
ATOM   1318 C  CG2   . THR A 1 161 ? 13.48648  -5.12020  23.75989  1.000 23.74220  ? 161  THR A CG2   1 
ATOM   1319 N  N     . GLY A 1 162 ? 14.66067  -9.66930  23.76739  1.000 27.34717  ? 162  GLY A N     1 
ATOM   1320 C  CA    . GLY A 1 162 ? 14.28142  -11.06706 23.82016  1.000 26.77214  ? 162  GLY A CA    1 
ATOM   1321 C  C     . GLY A 1 162 ? 12.83174  -11.34374 23.49451  1.000 27.23779  ? 162  GLY A C     1 
ATOM   1322 O  O     . GLY A 1 162 ? 12.37133  -12.47185 23.69312  1.000 27.16128  ? 162  GLY A O     1 
ATOM   1323 N  N     . LEU A 1 163 ? 12.09749  -10.34965 22.99882  1.000 26.55817  ? 163  LEU A N     1 
ATOM   1324 C  CA    . LEU A 1 163 ? 10.68394  -10.52831 22.69611  1.000 26.70792  ? 163  LEU A CA    1 
ATOM   1325 C  C     . LEU A 1 163 ? 10.50795  -11.40297 21.46072  1.000 27.40193  ? 163  LEU A C     1 
ATOM   1326 O  O     . LEU A 1 163 ? 11.17764  -11.19996 20.44299  1.000 28.68431  ? 163  LEU A O     1 
ATOM   1327 C  CB    . LEU A 1 163 ? 10.01930  -9.17030  22.47981  1.000 26.52658  ? 163  LEU A CB    1 
ATOM   1328 C  CG    . LEU A 1 163 ? 9.72436   -8.35293  23.73810  1.000 26.19485  ? 163  LEU A CG    1 
ATOM   1329 C  CD1   . LEU A 1 163 ? 9.52184   -6.88900  23.38310  1.000 24.82804  ? 163  LEU A CD1   1 
ATOM   1330 C  CD2   . LEU A 1 163 ? 8.50942   -8.90490  24.47071  1.000 24.10348  ? 163  LEU A CD2   1 
ATOM   1331 N  N     . LEU A 1 164 ? 9.59671   -12.37261 21.55312  1.000 23.36644  ? 164  LEU A N     1 
ATOM   1332 C  CA    . LEU A 1 164 ? 9.29298   -13.28345 20.44704  1.000 23.82500  ? 164  LEU A CA    1 
ATOM   1333 C  C     . LEU A 1 164 ? 10.55201  -13.98673 19.94700  1.000 24.34418  ? 164  LEU A C     1 
ATOM   1334 O  O     . LEU A 1 164 ? 10.75425  -14.17040 18.74473  1.000 24.51872  ? 164  LEU A O     1 
ATOM   1335 C  CB    . LEU A 1 164 ? 8.58668   -12.54925 19.30633  1.000 23.37270  ? 164  LEU A CB    1 
ATOM   1336 C  CG    . LEU A 1 164 ? 7.17526   -12.05836 19.62796  1.000 23.04172  ? 164  LEU A CG    1 
ATOM   1337 C  CD1   . LEU A 1 164 ? 6.53811   -11.40619 18.41122  1.000 22.75391  ? 164  LEU A CD1   1 
ATOM   1338 C  CD2   . LEU A 1 164 ? 6.32077   -13.20813 20.14040  1.000 23.73347  ? 164  LEU A CD2   1 
ATOM   1339 N  N     . MET A 1 165 ? 11.40949  -14.37868 20.88598  1.000 26.33158  ? 165  MET A N     1 
ATOM   1340 C  CA    . MET A 1 165 ? 12.64278  -15.09417 20.59301  1.000 26.44993  ? 165  MET A CA    1 
ATOM   1341 C  C     . MET A 1 165 ? 12.60177  -16.45965 21.25999  1.000 26.22727  ? 165  MET A C     1 
ATOM   1342 O  O     . MET A 1 165 ? 12.28724  -16.56589 22.45024  1.000 26.38313  ? 165  MET A O     1 
ATOM   1343 C  CB    . MET A 1 165 ? 13.86984  -14.31499 21.07806  1.000 26.00031  ? 165  MET A CB    1 
ATOM   1344 C  CG    . MET A 1 165 ? 13.98343  -12.90705 20.52582  1.000 26.62722  ? 165  MET A CG    1 
ATOM   1345 S  SD    . MET A 1 165 ? 14.29522  -12.88762 18.75086  1.000 28.39285  ? 165  MET A SD    1 
ATOM   1346 C  CE    . MET A 1 165 ? 15.81130  -13.83459 18.65522  1.000 28.15219  ? 165  MET A CE    1 
ATOM   1347 N  N     . ASP A 1 166 ? 12.90951  -17.49587 20.49252  1.000 34.77187  ? 166  ASP A N     1 
ATOM   1348 C  CA    . ASP A 1 166 ? 13.13867  -18.83571 21.02305  1.000 35.24829  ? 166  ASP A CA    1 
ATOM   1349 C  C     . ASP A 1 166 ? 14.64336  -19.06628 20.96325  1.000 35.36647  ? 166  ASP A C     1 
ATOM   1350 O  O     . ASP A 1 166 ? 15.19235  -19.35930 19.89710  1.000 36.16524  ? 166  ASP A O     1 
ATOM   1351 C  CB    . ASP A 1 166 ? 12.36909  -19.88816 20.23256  1.000 35.34000  ? 166  ASP A CB    1 
ATOM   1352 C  CG    . ASP A 1 166 ? 10.87068  -19.79605 20.44552  1.000 35.69795  ? 166  ASP A CG    1 
ATOM   1353 O  OD1   . ASP A 1 166 ? 10.44806  -19.29255 21.50822  1.000 34.62393  ? 166  ASP A OD1   1 
ATOM   1354 O  OD2   . ASP A 1 166 ? 10.11436  -20.23336 19.55326  1.000 36.37425  ? 166  ASP A OD2   1 
ATOM   1355 N  N     . GLY A 1 167 ? 15.30673  -18.92407 22.10562  1.000 39.51700  ? 167  GLY A N     1 
ATOM   1356 C  CA    . GLY A 1 167 ? 16.76009  -18.96094 22.10538  1.000 39.34538  ? 167  GLY A CA    1 
ATOM   1357 C  C     . GLY A 1 167 ? 17.30590  -17.75432 21.36742  1.000 39.95510  ? 167  GLY A C     1 
ATOM   1358 O  O     . GLY A 1 167 ? 16.88146  -16.61548 21.59440  1.000 39.70349  ? 167  GLY A O     1 
ATOM   1359 N  N     . ASP A 1 168 ? 18.25373  -17.99684 20.46661  1.000 43.59092  ? 168  ASP A N     1 
ATOM   1360 C  CA    . ASP A 1 168 ? 18.81052  -16.94831 19.62438  1.000 44.30889  ? 168  ASP A CA    1 
ATOM   1361 C  C     . ASP A 1 168 ? 18.11916  -16.85612 18.26920  1.000 44.81449  ? 168  ASP A C     1 
ATOM   1362 O  O     . ASP A 1 168 ? 18.64776  -16.21283 17.35700  1.000 46.29807  ? 168  ASP A O     1 
ATOM   1363 C  CB    . ASP A 1 168 ? 20.31662  -17.16490 19.43908  1.000 44.77445  ? 168  ASP A CB    1 
ATOM   1364 C  CG    . ASP A 1 168 ? 20.63435  -18.28460 18.46455  1.000 46.68580  ? 168  ASP A CG    1 
ATOM   1365 O  OD1   . ASP A 1 168 ? 19.83102  -19.23550 18.35728  1.000 48.01610  ? 168  ASP A OD1   1 
ATOM   1366 O  OD2   . ASP A 1 168 ? 21.68957  -18.21185 17.79989  1.000 47.23643  ? 168  ASP A OD2   1 
ATOM   1367 N  N     . GLN A 1 169 ? 16.95274  -17.48024 18.12009  1.000 40.52822  ? 169  GLN A N     1 
ATOM   1368 C  CA    . GLN A 1 169 ? 16.22278  -17.48294 16.86868  1.000 40.58054  ? 169  GLN A CA    1 
ATOM   1369 C  C     . GLN A 1 169 ? 14.85483  -16.83839 17.05409  1.000 40.72640  ? 169  GLN A C     1 
ATOM   1370 O  O     . GLN A 1 169 ? 14.23043  -17.00323 18.10774  1.000 40.02401  ? 169  GLN A O     1 
ATOM   1371 C  CB    . GLN A 1 169 ? 16.04688  -18.91437 16.33897  1.000 40.85944  ? 169  GLN A CB    1 
ATOM   1372 C  CG    . GLN A 1 169 ? 17.31399  -19.52527 15.75747  1.000 42.28710  ? 169  GLN A CG    1 
ATOM   1373 C  CD    . GLN A 1 169 ? 17.81760  -18.78403 14.53237  1.000 43.48965  ? 169  GLN A CD    1 
ATOM   1374 O  OE1   . GLN A 1 169 ? 18.91234  -18.21946 14.54121  1.000 43.70459  ? 169  GLN A OE1   1 
ATOM   1375 N  NE2   . GLN A 1 169 ? 17.02065  -18.78580 13.46800  1.000 44.12401  ? 169  GLN A NE2   1 
ATOM   1376 N  N     . PRO A 1 170 ? 14.36618  -16.10113 16.06077  1.000 26.58078  ? 170  PRO A N     1 
ATOM   1377 C  CA    . PRO A 1 170 ? 13.04609  -15.47852 16.19201  1.000 25.93998  ? 170  PRO A CA    1 
ATOM   1378 C  C     . PRO A 1 170 ? 11.93910  -16.51800 16.12663  1.000 26.50188  ? 170  PRO A C     1 
ATOM   1379 O  O     . PRO A 1 170 ? 12.07116  -17.56424 15.48623  1.000 27.38846  ? 170  PRO A O     1 
ATOM   1380 C  CB    . PRO A 1 170 ? 12.98578  -14.52139 14.99722  1.000 25.60959  ? 170  PRO A CB    1 
ATOM   1381 C  CG    . PRO A 1 170 ? 13.88252  -15.14573 13.98168  1.000 26.41451  ? 170  PRO A CG    1 
ATOM   1382 C  CD    . PRO A 1 170 ? 14.98134  -15.83649 14.74790  1.000 26.82989  ? 170  PRO A CD    1 
ATOM   1383 N  N     . ALA A 1 171 ? 10.83773  -16.21906 16.81135  1.000 29.70617  ? 171  ALA A N     1 
ATOM   1384 C  CA    . ALA A 1 171 ? 9.71118   -17.14158 16.85113  1.000 29.60175  ? 171  ALA A CA    1 
ATOM   1385 C  C     . ALA A 1 171 ? 9.11932   -17.32136 15.45945  1.000 29.80677  ? 171  ALA A C     1 
ATOM   1386 O  O     . ALA A 1 171 ? 8.86424   -16.34639 14.74683  1.000 30.51573  ? 171  ALA A O     1 
ATOM   1387 C  CB    . ALA A 1 171 ? 8.64412   -16.63221 17.81868  1.000 28.48035  ? 171  ALA A CB    1 
ATOM   1388 N  N     . GLY A 1 172 ? 8.90398   -18.57596 15.07360  1.000 32.48914  ? 172  GLY A N     1 
ATOM   1389 C  CA    . GLY A 1 172 ? 8.34960   -18.89100 13.77632  1.000 33.42230  ? 172  GLY A CA    1 
ATOM   1390 C  C     . GLY A 1 172 ? 9.36324   -19.05964 12.66743  1.000 34.24776  ? 172  GLY A C     1 
ATOM   1391 O  O     . GLY A 1 172 ? 8.97549   -19.41523 11.54715  1.000 34.21296  ? 172  GLY A O     1 
ATOM   1392 N  N     . GLY A 1 173 ? 10.64370  -18.81443 12.93507  1.000 28.99516  ? 173  GLY A N     1 
ATOM   1393 C  CA    . GLY A 1 173 ? 11.67946  -19.00955 11.94519  1.000 29.56592  ? 173  GLY A CA    1 
ATOM   1394 C  C     . GLY A 1 173 ? 11.99253  -17.80571 11.08578  1.000 29.04331  ? 173  GLY A C     1 
ATOM   1395 O  O     . GLY A 1 173 ? 12.87118  -17.89846 10.21881  1.000 29.59891  ? 173  GLY A O     1 
ATOM   1396 N  N     . ARG A 1 174 ? 11.30633  -16.68363 11.28841  1.000 32.27264  ? 174  ARG A N     1 
ATOM   1397 C  CA    . ARG A 1 174 ? 11.59096  -15.47393 10.53372  1.000 32.30553  ? 174  ARG A CA    1 
ATOM   1398 C  C     . ARG A 1 174 ? 11.18660  -14.26460 11.36360  1.000 32.27152  ? 174  ARG A C     1 
ATOM   1399 O  O     . ARG A 1 174 ? 10.30175  -14.34617 12.22015  1.000 31.65134  ? 174  ARG A O     1 
ATOM   1400 C  CB    . ARG A 1 174 ? 10.87586  -15.47527 9.17639   1.000 33.71720  ? 174  ARG A CB    1 
ATOM   1401 C  CG    . ARG A 1 174 ? 9.44820   -14.96725 9.20993   1.000 33.54542  ? 174  ARG A CG    1 
ATOM   1402 C  CD    . ARG A 1 174 ? 8.62869   -15.57035 8.07878   1.000 33.69734  ? 174  ARG A CD    1 
ATOM   1403 N  NE    . ARG A 1 174 ? 9.36933   -15.59908 6.82432   1.000 35.61493  ? 174  ARG A NE    1 
ATOM   1404 C  CZ    . ARG A 1 174 ? 9.51523   -14.55861 6.01511   1.000 35.64996  ? 174  ARG A CZ    1 
ATOM   1405 N  NH1   . ARG A 1 174 ? 8.96498   -13.38645 6.28812   1.000 34.60374  ? 174  ARG A NH1   1 
ATOM   1406 N  NH2   . ARG A 1 174 ? 10.23353  -14.69707 4.90538   1.000 34.92945  ? 174  ARG A NH2   1 
ATOM   1407 N  N     . TRP A 1 175 ? 11.85477  -13.13941 11.10115  1.000 30.67272  ? 175  TRP A N     1 
ATOM   1408 C  CA    . TRP A 1 175 ? 11.65197  -11.94656 11.91647  1.000 31.07669  ? 175  TRP A CA    1 
ATOM   1409 C  C     . TRP A 1 175 ? 10.29312  -11.31344 11.65625  1.000 30.92839  ? 175  TRP A C     1 
ATOM   1410 O  O     . TRP A 1 175 ? 9.59256   -10.92119 12.59687  1.000 30.31912  ? 175  TRP A O     1 
ATOM   1411 C  CB    . TRP A 1 175 ? 12.76218  -10.93212 11.64345  1.000 31.02768  ? 175  TRP A CB    1 
ATOM   1412 C  CG    . TRP A 1 175 ? 14.12857  -11.43596 11.95605  1.000 31.50250  ? 175  TRP A CG    1 
ATOM   1413 C  CD1   . TRP A 1 175 ? 15.03146  -11.95247 11.07523  1.000 31.76799  ? 175  TRP A CD1   1 
ATOM   1414 C  CD2   . TRP A 1 175 ? 14.75612  -11.46885 13.24226  1.000 30.86746  ? 175  TRP A CD2   1 
ATOM   1415 N  NE1   . TRP A 1 175 ? 16.18420  -12.30596 11.73281  1.000 31.65226  ? 175  TRP A NE1   1 
ATOM   1416 C  CE2   . TRP A 1 175 ? 16.04064  -12.01928 13.06505  1.000 31.19828  ? 175  TRP A CE2   1 
ATOM   1417 C  CE3   . TRP A 1 175 ? 14.35748  -11.08438 14.52587  1.000 30.33021  ? 175  TRP A CE3   1 
ATOM   1418 C  CZ2   . TRP A 1 175 ? 16.92840  -12.19810 14.12330  1.000 31.15832  ? 175  TRP A CZ2   1 
ATOM   1419 C  CZ3   . TRP A 1 175 ? 15.23951  -11.26258 15.57508  1.000 30.27426  ? 175  TRP A CZ3   1 
ATOM   1420 C  CH2   . TRP A 1 175 ? 16.51064  -11.81366 15.36774  1.000 30.67919  ? 175  TRP A CH2   1 
ATOM   1421 N  N     . ASN A 1 176 ? 9.90509   -11.20598 10.39130  1.000 38.44789  ? 176  ASN A N     1 
ATOM   1422 C  CA    . ASN A 1 176 ? 8.77502   -10.38770 9.98292   1.000 38.46861  ? 176  ASN A CA    1 
ATOM   1423 C  C     . ASN A 1 176 ? 7.76364   -11.24556 9.23935   1.000 39.26670  ? 176  ASN A C     1 
ATOM   1424 O  O     . ASN A 1 176 ? 8.11172   -11.91725 8.26251   1.000 38.89624  ? 176  ASN A O     1 
ATOM   1425 C  CB    . ASN A 1 176 ? 9.24960   -9.22926  9.10003   1.000 39.00108  ? 176  ASN A CB    1 
ATOM   1426 C  CG    . ASN A 1 176 ? 8.21882   -8.13355  8.97323   1.000 39.66467  ? 176  ASN A CG    1 
ATOM   1427 O  OD1   . ASN A 1 176 ? 7.02229   -8.37455  9.11412   1.000 39.87695  ? 176  ASN A OD1   1 
ATOM   1428 N  ND2   . ASN A 1 176 ? 8.67882   -6.91560  8.71049   1.000 40.28855  ? 176  ASN A ND2   1 
ATOM   1429 N  N     . PHE A 1 177 ? 6.51484   -11.21981 9.70385   1.000 38.26386  ? 177  PHE A N     1 
ATOM   1430 C  CA    . PHE A 1 177 ? 5.41226   -11.90435 9.04152   1.000 39.42824  ? 177  PHE A CA    1 
ATOM   1431 C  C     . PHE A 1 177 ? 4.47429   -10.92216 8.34761   1.000 39.12599  ? 177  PHE A C     1 
ATOM   1432 O  O     . PHE A 1 177 ? 3.27991   -11.19398 8.20105   1.000 40.59985  ? 177  PHE A O     1 
ATOM   1433 C  CB    . PHE A 1 177 ? 4.63136   -12.76573 10.03315  1.000 39.02222  ? 177  PHE A CB    1 
ATOM   1434 C  CG    . PHE A 1 177 ? 5.46562   -13.80261 10.73064  1.000 37.78793  ? 177  PHE A CG    1 
ATOM   1435 C  CD1   . PHE A 1 177 ? 5.74498   -15.01096 10.11749  1.000 37.40516  ? 177  PHE A CD1   1 
ATOM   1436 C  CD2   . PHE A 1 177 ? 5.96093   -13.57258 12.00356  1.000 37.83920  ? 177  PHE A CD2   1 
ATOM   1437 C  CE1   . PHE A 1 177 ? 6.50297   -15.97131 10.75899  1.000 37.65659  ? 177  PHE A CE1   1 
ATOM   1438 C  CE2   . PHE A 1 177 ? 6.72432   -14.52733 12.64822  1.000 37.32292  ? 177  PHE A CE2   1 
ATOM   1439 C  CZ    . PHE A 1 177 ? 6.99634   -15.72827 12.02377  1.000 37.33895  ? 177  PHE A CZ    1 
ATOM   1440 N  N     . ASP A 1 178 ? 4.99948   -9.77165  7.92822   0.936 60.15163  ? 178  ASP A N     1 
ATOM   1441 C  CA    . ASP A 1 178 ? 4.19382   -8.79200  7.21256   0.936 60.18414  ? 178  ASP A CA    1 
ATOM   1442 C  C     . ASP A 1 178 ? 3.64806   -9.40581  5.93194   0.936 61.04318  ? 178  ASP A C     1 
ATOM   1443 O  O     . ASP A 1 178 ? 4.39267   -9.61738  4.96986   0.936 60.61153  ? 178  ASP A O     1 
ATOM   1444 C  CB    . ASP A 1 178 ? 5.01196   -7.53942  6.89979   0.936 59.60974  ? 178  ASP A CB    1 
ATOM   1445 C  CG    . ASP A 1 178 ? 4.24755   -6.26454  7.17689   0.936 60.48148  ? 178  ASP A CG    1 
ATOM   1446 O  OD1   . ASP A 1 178 ? 3.42652   -6.25630  8.11829   0.936 60.95143  ? 178  ASP A OD1   1 
ATOM   1447 O  OD2   . ASP A 1 178 ? 4.46709   -5.27157  6.45249   0.936 60.70615  ? 178  ASP A OD2   1 
ATOM   1448 N  N     . ALA A 1 179 ? 2.35629   -9.71653  5.92133   0.952 89.96331  ? 179  ALA A N     1 
ATOM   1449 C  CA    . ALA A 1 179 ? 1.71347   -10.31704 4.76180   0.952 90.98295  ? 179  ALA A CA    1 
ATOM   1450 C  C     . ALA A 1 179 ? 1.28457   -9.21468  3.80256   0.952 91.71371  ? 179  ALA A C     1 
ATOM   1451 O  O     . ALA A 1 179 ? 0.46917   -8.35706  4.15928   0.952 91.75925  ? 179  ALA A O     1 
ATOM   1452 C  CB    . ALA A 1 179 ? 0.51419   -11.16368 5.18531   0.952 90.98981  ? 179  ALA A CB    1 
ATOM   1453 N  N     . GLU A 1 180 ? 1.83171   -9.23707  2.59226   0.911 88.60377  ? 180  GLU A N     1 
ATOM   1454 C  CA    . GLU A 1 180 ? 1.44615   -8.27985  1.56445   0.911 88.15907  ? 180  GLU A CA    1 
ATOM   1455 C  C     . GLU A 1 180 ? 0.02004   -8.58524  1.10473   0.911 88.50930  ? 180  GLU A C     1 
ATOM   1456 O  O     . GLU A 1 180 ? -0.69181  -9.40974  1.68632   0.911 88.76574  ? 180  GLU A O     1 
ATOM   1457 C  CB    . GLU A 1 180 ? 2.44154   -8.30936  0.40786   0.911 89.04936  ? 180  GLU A CB    1 
ATOM   1458 C  CG    . GLU A 1 180 ? 3.90515   -8.22628  0.82406   0.911 88.87756  ? 180  GLU A CG    1 
ATOM   1459 C  CD    . GLU A 1 180 ? 4.15328   -7.19220  1.90661   0.911 88.19786  ? 180  GLU A CD    1 
ATOM   1460 O  OE1   . GLU A 1 180 ? 4.22399   -5.98970  1.57689   0.911 88.00280  ? 180  GLU A OE1   1 
ATOM   1461 O  OE2   . GLU A 1 180 ? 4.28338   -7.58065  3.08615   0.911 87.86618  ? 180  GLU A OE2   1 
ATOM   1462 N  N     . ASN A 1 181 ? -0.41098  -7.90545  0.04129   0.891 77.20574  ? 181  ASN A N     1 
ATOM   1463 C  CA    . ASN A 1 181 ? -1.75100  -8.07587  -0.52065  0.891 78.07700  ? 181  ASN A CA    1 
ATOM   1464 C  C     . ASN A 1 181 ? -2.83941  -7.75825  0.50196   0.891 77.09480  ? 181  ASN A C     1 
ATOM   1465 O  O     . ASN A 1 181 ? -3.91137  -8.36851  0.49286   0.891 76.66047  ? 181  ASN A O     1 
ATOM   1466 C  CB    . ASN A 1 181 ? -1.94369  -9.48737  -1.08513  0.891 78.94486  ? 181  ASN A CB    1 
ATOM   1467 C  CG    . ASN A 1 181 ? -0.75705  -9.95354  -1.90645  0.891 79.49458  ? 181  ASN A CG    1 
ATOM   1468 O  OD1   . ASN A 1 181 ? -0.45694  -9.39132  -2.95957  0.891 79.87759  ? 181  ASN A OD1   1 
ATOM   1469 N  ND2   . ASN A 1 181 ? -0.07219  -10.98528 -1.42480  0.891 79.54963  ? 181  ASN A ND2   1 
ATOM   1470 N  N     . ARG A 1 182 ? -2.56829  -6.80977  1.39632   1.000 105.25126 ? 182  ARG A N     1 
ATOM   1471 C  CA    . ARG A 1 182 ? -3.58517  -6.35791  2.33547   1.000 105.22042 ? 182  ARG A CA    1 
ATOM   1472 C  C     . ARG A 1 182 ? -4.72588  -5.68244  1.58358   1.000 104.79852 ? 182  ARG A C     1 
ATOM   1473 O  O     . ARG A 1 182 ? -4.51243  -5.00796  0.57263   1.000 104.51212 ? 182  ARG A O     1 
ATOM   1474 C  CB    . ARG A 1 182 ? -2.97083  -5.39997  3.35766   1.000 104.98404 ? 182  ARG A CB    1 
ATOM   1475 C  CG    . ARG A 1 182 ? -2.24742  -6.09974  4.50099   1.000 104.84565 ? 182  ARG A CG    1 
ATOM   1476 C  CD    . ARG A 1 182 ? -0.92553  -5.42246  4.83265   1.000 104.64632 ? 182  ARG A CD    1 
ATOM   1477 N  NE    . ARG A 1 182 ? 0.00623   -6.34397  5.47257   1.000 104.77062 ? 182  ARG A NE    1 
ATOM   1478 C  CZ    . ARG A 1 182 ? 0.12562   -6.49845  6.78430   1.000 104.46196 ? 182  ARG A CZ    1 
ATOM   1479 N  NH1   . ARG A 1 182 ? -0.59850  -5.78721  7.63293   1.000 104.05897 ? 182  ARG A NH1   1 
ATOM   1480 N  NH2   . ARG A 1 182 ? 0.99483   -7.38742  7.25666   1.000 104.55503 ? 182  ARG A NH2   1 
ATOM   1481 N  N     . ARG A 1 183 ? -5.94668  -5.87052  2.07660   1.000 70.46966  ? 183  ARG A N     1 
ATOM   1482 C  CA    . ARG A 1 183 ? -7.13723  -5.43351  1.36338   1.000 71.25649  ? 183  ARG A CA    1 
ATOM   1483 C  C     . ARG A 1 183 ? -8.08678  -4.71213  2.31158   1.000 69.98806  ? 183  ARG A C     1 
ATOM   1484 O  O     . ARG A 1 183 ? -7.91945  -4.72957  3.53380   1.000 68.74324  ? 183  ARG A O     1 
ATOM   1485 C  CB    . ARG A 1 183 ? -7.84054  -6.62119  0.68496   1.000 72.96084  ? 183  ARG A CB    1 
ATOM   1486 C  CG    . ARG A 1 183 ? -8.86443  -7.36639  1.54582   1.000 72.69083  ? 183  ARG A CG    1 
ATOM   1487 C  CD    . ARG A 1 183 ? -8.23745  -8.02675  2.77925   1.000 72.22345  ? 183  ARG A CD    1 
ATOM   1488 N  NE    . ARG A 1 183 ? -6.97343  -8.70893  2.51622   1.000 72.63512  ? 183  ARG A NE    1 
ATOM   1489 C  CZ    . ARG A 1 183 ? -6.81360  -9.72317  1.67475   1.000 73.92919  ? 183  ARG A CZ    1 
ATOM   1490 N  NH1   . ARG A 1 183 ? -7.83136  -10.23292 0.99829   1.000 75.01414  ? 183  ARG A NH1   1 
ATOM   1491 N  NH2   . ARG A 1 183 ? -5.60300  -10.25175 1.52016   1.000 74.17125  ? 183  ARG A NH2   1 
ATOM   1492 N  N     . LYS A 1 184 ? -9.09282  -4.06894  1.72234   1.000 42.80802  ? 184  LYS A N     1 
ATOM   1493 C  CA    . LYS A 1 184 ? -10.11330 -3.36579  2.48218   1.000 41.67717  ? 184  LYS A CA    1 
ATOM   1494 C  C     . LYS A 1 184 ? -11.03723 -4.36068  3.18629   1.000 41.65315  ? 184  LYS A C     1 
ATOM   1495 O  O     . LYS A 1 184 ? -11.01788 -5.56643  2.92436   1.000 41.49895  ? 184  LYS A O     1 
ATOM   1496 C  CB    . LYS A 1 184 ? -10.92353 -2.45487  1.56163   1.000 40.77392  ? 184  LYS A CB    1 
ATOM   1497 C  CG    . LYS A 1 184 ? -11.77872 -3.21924  0.56162   1.000 41.76729  ? 184  LYS A CG    1 
ATOM   1498 C  CD    . LYS A 1 184 ? -12.62750 -2.29185  -0.29279  1.000 42.25087  ? 184  LYS A CD    1 
ATOM   1499 C  CE    . LYS A 1 184 ? -11.86203 -1.80686  -1.51208  1.000 42.29572  ? 184  LYS A CE    1 
ATOM   1500 N  NZ    . LYS A 1 184 ? -12.63252 -0.79292  -2.28496  1.000 42.14601  ? 184  LYS A NZ    1 
ATOM   1501 N  N     . LEU A 1 185 ? -11.86190 -3.83803  4.08853   1.000 36.67393  ? 185  LEU A N     1 
ATOM   1502 C  CA    . LEU A 1 185 ? -12.79856 -4.69083  4.80558   1.000 36.32816  ? 185  LEU A CA    1 
ATOM   1503 C  C     . LEU A 1 185 ? -13.80666 -5.29431  3.83221   1.000 37.25306  ? 185  LEU A C     1 
ATOM   1504 O  O     . LEU A 1 185 ? -14.22980 -4.62665  2.87931   1.000 37.35267  ? 185  LEU A O     1 
ATOM   1505 C  CB    . LEU A 1 185 ? -13.53718 -3.90201  5.88948   1.000 35.07742  ? 185  LEU A CB    1 
ATOM   1506 C  CG    . LEU A 1 185 ? -12.72315 -3.13136  6.93106   1.000 34.86613  ? 185  LEU A CG    1 
ATOM   1507 C  CD1   . LEU A 1 185 ? -13.62484 -2.64813  8.05630   1.000 34.53863  ? 185  LEU A CD1   1 
ATOM   1508 C  CD2   . LEU A 1 185 ? -11.60010 -3.98524  7.48239   1.000 34.75829  ? 185  LEU A CD2   1 
ATOM   1509 N  N     . PRO A 1 186 ? -14.20633 -6.55082  4.02673   1.000 33.53444  ? 186  PRO A N     1 
ATOM   1510 C  CA    . PRO A 1 186 ? -15.28403 -7.10251  3.21551   1.000 35.25855  ? 186  PRO A CA    1 
ATOM   1511 C  C     . PRO A 1 186 ? -16.58077 -6.36932  3.49611   1.000 35.45979  ? 186  PRO A C     1 
ATOM   1512 O  O     . PRO A 1 186 ? -16.77802 -5.81935  4.59579   1.000 34.32747  ? 186  PRO A O     1 
ATOM   1513 C  CB    . PRO A 1 186 ? -15.35212 -8.56957  3.66203   1.000 35.80064  ? 186  PRO A CB    1 
ATOM   1514 C  CG    . PRO A 1 186 ? -14.69132 -8.61194  4.99198   1.000 34.25487  ? 186  PRO A CG    1 
ATOM   1515 C  CD    . PRO A 1 186 ? -13.66978 -7.52109  4.99636   1.000 32.93492  ? 186  PRO A CD    1 
ATOM   1516 N  N     . PRO A 1 187 ? -17.49748 -6.32983  2.52514   1.000 45.47781  ? 187  PRO A N     1 
ATOM   1517 C  CA    . PRO A 1 187 ? -18.70207 -5.49519  2.68420   1.000 45.46008  ? 187  PRO A CA    1 
ATOM   1518 C  C     . PRO A 1 187 ? -19.55909 -5.85327  3.88812   1.000 46.19057  ? 187  PRO A C     1 
ATOM   1519 O  O     . PRO A 1 187 ? -20.29054 -4.98657  4.38309   1.000 46.41088  ? 187  PRO A O     1 
ATOM   1520 C  CB    . PRO A 1 187 ? -19.46620 -5.72069  1.37033   1.000 46.93982  ? 187  PRO A CB    1 
ATOM   1521 C  CG    . PRO A 1 187 ? -18.86045 -6.95031  0.76010   1.000 48.18795  ? 187  PRO A CG    1 
ATOM   1522 C  CD    . PRO A 1 187 ? -17.43674 -6.97238  1.20239   1.000 47.08211  ? 187  PRO A CD    1 
ATOM   1523 N  N     . GLY A 1 188 ? -19.48933 -7.08494  4.38453   1.000 60.16315  ? 188  GLY A N     1 
ATOM   1524 C  CA    . GLY A 1 188 ? -20.34082 -7.48873  5.48662   1.000 60.63736  ? 188  GLY A CA    1 
ATOM   1525 C  C     . GLY A 1 188 ? -19.73435 -7.30778  6.86388   1.000 59.21049  ? 188  GLY A C     1 
ATOM   1526 O  O     . GLY A 1 188 ? -20.45175 -7.32947  7.86859   1.000 59.09848  ? 188  GLY A O     1 
ATOM   1527 N  N     . LEU A 1 189 ? -18.41842 -7.12462  6.92886   1.000 38.84270  ? 189  LEU A N     1 
ATOM   1528 C  CA    . LEU A 1 189 ? -17.72059 -7.05754  8.20690   1.000 38.00942  ? 189  LEU A CA    1 
ATOM   1529 C  C     . LEU A 1 189 ? -17.92875 -5.68864  8.84343   1.000 37.78927  ? 189  LEU A C     1 
ATOM   1530 O  O     . LEU A 1 189 ? -17.52315 -4.66582  8.28018   1.000 37.91223  ? 189  LEU A O     1 
ATOM   1531 C  CB    . LEU A 1 189 ? -16.23268 -7.34098  8.01605   1.000 38.58521  ? 189  LEU A CB    1 
ATOM   1532 C  CG    . LEU A 1 189 ? -15.38513 -7.36682  9.28984   1.000 37.80864  ? 189  LEU A CG    1 
ATOM   1533 C  CD1   . LEU A 1 189 ? -15.88842 -8.43628  10.24907  1.000 36.85920  ? 189  LEU A CD1   1 
ATOM   1534 C  CD2   . LEU A 1 189 ? -13.91783 -7.58366  8.95873   1.000 37.04734  ? 189  LEU A CD2   1 
ATOM   1535 N  N     . ARG A 1 190 ? -18.55682 -5.67057  10.01947  1.000 42.95314  ? 190  ARG A N     1 
ATOM   1536 C  CA    . ARG A 1 190 ? -18.74759 -4.43758  10.76567  1.000 42.24551  ? 190  ARG A CA    1 
ATOM   1537 C  C     . ARG A 1 190 ? -17.71620 -4.35538  11.87720  1.000 41.80980  ? 190  ARG A C     1 
ATOM   1538 O  O     . ARG A 1 190 ? -17.65062 -5.27107  12.71279  1.000 42.19452  ? 190  ARG A O     1 
ATOM   1539 C  CB    . ARG A 1 190 ? -20.15376 -4.36970  11.34770  1.000 42.68644  ? 190  ARG A CB    1 
ATOM   1540 C  CG    . ARG A 1 190 ? -20.57108 -2.96783  11.75322  1.000 42.25853  ? 190  ARG A CG    1 
ATOM   1541 C  CD    . ARG A 1 190 ? -21.83995 -2.97419  12.59108  1.000 42.32596  ? 190  ARG A CD    1 
ATOM   1542 N  NE    . ARG A 1 190 ? -21.91576 -1.81355  13.47147  1.000 43.36084  ? 190  ARG A NE    1 
ATOM   1543 C  CZ    . ARG A 1 190 ? -22.13072 -0.56944  13.06300  1.000 42.60779  ? 190  ARG A CZ    1 
ATOM   1544 N  NH1   . ARG A 1 190 ? -22.31814 -0.28224  11.78472  1.000 43.03597  ? 190  ARG A NH1   1 
ATOM   1545 N  NH2   . ARG A 1 190 ? -22.16130 0.41179   13.96056  1.000 41.23749  ? 190  ARG A NH2   1 
ATOM   1546 N  N     . PRO A 1 191 ? -16.89986 -3.30598  11.92880  1.000 33.71484  ? 191  PRO A N     1 
ATOM   1547 C  CA    . PRO A 1 191 ? -15.89223 -3.18668  12.99295  1.000 33.81731  ? 191  PRO A CA    1 
ATOM   1548 C  C     . PRO A 1 191 ? -16.54318 -3.16249  14.36346  1.000 33.48320  ? 191  PRO A C     1 
ATOM   1549 O  O     . PRO A 1 191 ? -17.62165 -2.57563  14.53977  1.000 33.63371  ? 191  PRO A O     1 
ATOM   1550 C  CB    . PRO A 1 191 ? -15.20290 -1.85063  12.67802  1.000 33.23620  ? 191  PRO A CB    1 
ATOM   1551 C  CG    . PRO A 1 191 ? -15.43339 -1.64860  11.21389  1.000 34.74000  ? 191  PRO A CG    1 
ATOM   1552 C  CD    . PRO A 1 191 ? -16.79394 -2.22007  10.93990  1.000 33.89850  ? 191  PRO A CD    1 
ATOM   1553 N  N     . PRO A 1 192 ? -15.91692 -3.78368  15.35960  1.000 30.55307  ? 192  PRO A N     1 
ATOM   1554 C  CA    . PRO A 1 192 ? -16.56563 -3.93035  16.66594  1.000 30.12662  ? 192  PRO A CA    1 
ATOM   1555 C  C     . PRO A 1 192 ? -16.60510 -2.62290  17.44226  1.000 30.55286  ? 192  PRO A C     1 
ATOM   1556 O  O     . PRO A 1 192 ? -15.89326 -1.65977  17.14722  1.000 30.05039  ? 192  PRO A O     1 
ATOM   1557 C  CB    . PRO A 1 192 ? -15.68931 -4.96515  17.37814  1.000 29.16507  ? 192  PRO A CB    1 
ATOM   1558 C  CG    . PRO A 1 192 ? -14.34400 -4.78375  16.76347  1.000 30.35569  ? 192  PRO A CG    1 
ATOM   1559 C  CD    . PRO A 1 192 ? -14.59113 -4.42455  15.32385  1.000 30.58849  ? 192  PRO A CD    1 
ATOM   1560 N  N     . GLU A 1 193 ? -17.46585 -2.60709  18.45718  1.000 30.93351  ? 193  GLU A N     1 
ATOM   1561 C  CA    . GLU A 1 193 ? -17.52019 -1.48018  19.37622  1.000 30.86820  ? 193  GLU A CA    1 
ATOM   1562 C  C     . GLU A 1 193 ? -16.26694 -1.45577  20.24131  1.000 30.60733  ? 193  GLU A C     1 
ATOM   1563 O  O     . GLU A 1 193 ? -15.73999 -2.50192  20.62976  1.000 29.72425  ? 193  GLU A O     1 
ATOM   1564 C  CB    . GLU A 1 193 ? -18.76732 -1.56875  20.25419  1.000 34.41277  ? 193  GLU A CB    1 
ATOM   1565 C  CG    . GLU A 1 193 ? -19.46056 -0.23697  20.49043  0.795 34.54202  ? 193  GLU A CG    1 
ATOM   1566 C  CD    . GLU A 1 193 ? -20.62410 -0.35165  21.45632  0.280 34.56632  ? 193  GLU A CD    1 
ATOM   1567 O  OE1   . GLU A 1 193 ? -21.71065 -0.79926  21.03188  0.730 34.84545  ? 193  GLU A OE1   1 
ATOM   1568 O  OE2   . GLU A 1 193 ? -20.45249 0.00766   22.64016  0.694 34.34094  ? 193  GLU A OE2   1 
ATOM   1569 N  N     . ARG A 1 194 ? -15.78689 -0.25412  20.54067  1.000 28.11591  ? 194  ARG A N     1 
ATOM   1570 C  CA    . ARG A 1 194 ? -14.55458 -0.07610  21.29030  1.000 28.00930  ? 194  ARG A CA    1 
ATOM   1571 C  C     . ARG A 1 194 ? -14.84447 0.51910   22.66115  1.000 28.28534  ? 194  ARG A C     1 
ATOM   1572 O  O     . ARG A 1 194 ? -15.79452 1.28694   22.83929  1.000 29.11296  ? 194  ARG A O     1 
ATOM   1573 C  CB    . ARG A 1 194 ? -13.57350 0.81708   20.52653  1.000 27.92794  ? 194  ARG A CB    1 
ATOM   1574 C  CG    . ARG A 1 194 ? -13.38512 0.41156   19.07373  1.000 27.82919  ? 194  ARG A CG    1 
ATOM   1575 C  CD    . ARG A 1 194 ? -12.72750 -0.96010  18.96046  1.000 28.55088  ? 194  ARG A CD    1 
ATOM   1576 N  NE    . ARG A 1 194 ? -11.64429 -1.12862  19.92193  1.000 27.82333  ? 194  ARG A NE    1 
ATOM   1577 C  CZ    . ARG A 1 194 ? -10.36135 -0.94389  19.64381  1.000 28.06625  ? 194  ARG A CZ    1 
ATOM   1578 N  NH1   . ARG A 1 194 ? -9.96008  -0.59723  18.43164  1.000 28.05033  ? 194  ARG A NH1   1 
ATOM   1579 N  NH2   . ARG A 1 194 ? -9.45832  -1.10857  20.60646  1.000 27.79790  ? 194  ARG A NH2   1 
ATOM   1580 N  N     . LEU A 1 195 ? -14.01243 0.15171   23.63042  1.000 28.62846  ? 195  LEU A N     1 
ATOM   1581 C  CA    . LEU A 1 195 ? -14.16554 0.64099   24.99229  1.000 28.05105  ? 195  LEU A CA    1 
ATOM   1582 C  C     . LEU A 1 195 ? -13.69125 2.08479   25.09117  1.000 28.95215  ? 195  LEU A C     1 
ATOM   1583 O  O     . LEU A 1 195 ? -12.57220 2.40989   24.68298  1.000 29.16378  ? 195  LEU A O     1 
ATOM   1584 C  CB    . LEU A 1 195 ? -13.37914 -0.23928  25.96229  1.000 27.97072  ? 195  LEU A CB    1 
ATOM   1585 C  CG    . LEU A 1 195 ? -13.39242 0.16661   27.43650  1.000 28.16525  ? 195  LEU A CG    1 
ATOM   1586 C  CD1   . LEU A 1 195 ? -14.78782 0.02215   28.02645  1.000 27.65457  ? 195  LEU A CD1   1 
ATOM   1587 C  CD2   . LEU A 1 195 ? -12.38708 -0.66099  28.22047  1.000 27.39788  ? 195  LEU A CD2   1 
ATOM   1588 N  N     . ARG A 1 196 ? -14.54833 2.94973   25.62309  1.000 32.61617  ? 196  ARG A N     1 
ATOM   1589 C  CA    . ARG A 1 196 ? -14.18238 4.31354   25.96926  1.000 33.40519  ? 196  ARG A CA    1 
ATOM   1590 C  C     . ARG A 1 196 ? -14.26663 4.48931   27.47996  1.000 33.19234  ? 196  ARG A C     1 
ATOM   1591 O  O     . ARG A 1 196 ? -14.96394 3.74619   28.17529  1.000 32.67340  ? 196  ARG A O     1 
ATOM   1592 C  CB    . ARG A 1 196 ? -15.08615 5.33269   25.26435  1.000 33.19079  ? 196  ARG A CB    1 
ATOM   1593 C  CG    . ARG A 1 196 ? -15.13503 5.19185   23.74904  1.000 33.90126  ? 196  ARG A CG    1 
ATOM   1594 C  CD    . ARG A 1 196 ? -13.74409 5.03279   23.14232  1.000 34.37512  ? 196  ARG A CD    1 
ATOM   1595 N  NE    . ARG A 1 196 ? -13.05328 6.30771   22.98481  1.000 36.13953  ? 196  ARG A NE    1 
ATOM   1596 C  CZ    . ARG A 1 196 ? -11.74961 6.48126   23.15768  1.000 35.68443  ? 196  ARG A CZ    1 
ATOM   1597 N  NH1   . ARG A 1 196 ? -10.95685 5.47681   23.49419  1.000 34.00607  ? 196  ARG A NH1   1 
ATOM   1598 N  NH2   . ARG A 1 196 ? -11.22811 7.69306   22.98732  1.000 35.33312  ? 196  ARG A NH2   1 
ATOM   1599 N  N     . ILE A 1 197 ? -13.54478 5.48283   27.98558  1.000 26.85632  ? 197  ILE A N     1 
ATOM   1600 C  CA    . ILE A 1 197 ? -13.45453 5.73197   29.41875  1.000 26.57943  ? 197  ILE A CA    1 
ATOM   1601 C  C     . ILE A 1 197 ? -14.29129 6.96913   29.73862  1.000 27.70605  ? 197  ILE A C     1 
ATOM   1602 O  O     . ILE A 1 197 ? -13.90638 8.08859   29.36771  1.000 28.24499  ? 197  ILE A O     1 
ATOM   1603 C  CB    . ILE A 1 197 ? -12.00132 5.91507   29.87354  1.000 27.03375  ? 197  ILE A CB    1 
ATOM   1604 C  CG1   . ILE A 1 197 ? -11.14282 4.73858   29.40509  1.000 25.50155  ? 197  ILE A CG1   1 
ATOM   1605 C  CG2   . ILE A 1 197 ? -11.94146 6.06703   31.38341  1.000 26.55375  ? 197  ILE A CG2   1 
ATOM   1606 C  CD1   . ILE A 1 197 ? -11.53966 3.41531   30.01892  1.000 25.12158  ? 197  ILE A CD1   1 
ATOM   1607 N  N     . PRO A 1 198 ? -15.42520 6.82639   30.41847  1.000 27.79407  ? 198  PRO A N     1 
ATOM   1608 C  CA    . PRO A 1 198 ? -16.18006 8.00378   30.86127  1.000 28.38852  ? 198  PRO A CA    1 
ATOM   1609 C  C     . PRO A 1 198 ? -15.36447 8.81923   31.84696  1.000 28.83363  ? 198  PRO A C     1 
ATOM   1610 O  O     . PRO A 1 198 ? -14.69084 8.25527   32.72294  1.000 28.51111  ? 198  PRO A O     1 
ATOM   1611 C  CB    . PRO A 1 198 ? -17.42775 7.40248   31.52782  1.000 28.29395  ? 198  PRO A CB    1 
ATOM   1612 C  CG    . PRO A 1 198 ? -17.06377 5.98878   31.83737  1.000 27.54905  ? 198  PRO A CG    1 
ATOM   1613 C  CD    . PRO A 1 198 ? -16.08887 5.56461   30.78495  1.000 26.76667  ? 198  PRO A CD    1 
ATOM   1614 N  N     . PRO A 1 199 ? -15.38930 10.14540  31.72850  1.000 28.49805  ? 199  PRO A N     1 
ATOM   1615 C  CA    . PRO A 1 199 ? -14.52517 10.98343  32.57175  1.000 28.43706  ? 199  PRO A CA    1 
ATOM   1616 C  C     . PRO A 1 199 ? -14.81318 10.79620  34.05511  1.000 28.42649  ? 199  PRO A C     1 
ATOM   1617 O  O     . PRO A 1 199 ? -15.96445 10.83756  34.49415  1.000 28.82230  ? 199  PRO A O     1 
ATOM   1618 C  CB    . PRO A 1 199 ? -14.85866 12.40638  32.10904  1.000 29.56155  ? 199  PRO A CB    1 
ATOM   1619 C  CG    . PRO A 1 199 ? -15.35699 12.24101  30.71163  1.000 29.23412  ? 199  PRO A CG    1 
ATOM   1620 C  CD    . PRO A 1 199 ? -16.09400 10.93113  30.70113  1.000 28.67878  ? 199  PRO A CD    1 
ATOM   1621 N  N     . ASN A 1 200 ? -13.74945 10.58407  34.82308  1.000 25.90773  ? 200  ASN A N     1 
ATOM   1622 C  CA    . ASN A 1 200 ? -13.82754 10.53947  36.27555  1.000 26.94099  ? 200  ASN A CA    1 
ATOM   1623 C  C     . ASN A 1 200 ? -13.97994 11.95951  36.81653  1.000 27.52750  ? 200  ASN A C     1 
ATOM   1624 O  O     . ASN A 1 200 ? -13.87750 12.92900  36.06337  1.000 27.07447  ? 200  ASN A O     1 
ATOM   1625 C  CB    . ASN A 1 200 ? -12.59318 9.82072   36.82774  1.000 26.87519  ? 200  ASN A CB    1 
ATOM   1626 C  CG    . ASN A 1 200 ? -11.28638 10.51267  36.47053  1.000 26.24197  ? 200  ASN A CG    1 
ATOM   1627 O  OD1   . ASN A 1 200 ? -11.14686 11.72760  36.60504  1.000 26.44469  ? 200  ASN A OD1   1 
ATOM   1628 N  ND2   . ASN A 1 200 ? -10.31398 9.72869   36.01922  1.000 25.57399  ? 200  ASN A ND2   1 
ATOM   1629 N  N     . PRO A 1 201 ? -14.25285 12.12156  38.12193  1.000 21.54791  ? 201  PRO A N     1 
ATOM   1630 C  CA    . PRO A 1 201 ? -14.43798 13.48467  38.65950  1.000 22.44099  ? 201  PRO A CA    1 
ATOM   1631 C  C     . PRO A 1 201 ? -13.29508 14.44233  38.35526  1.000 21.92670  ? 201  PRO A C     1 
ATOM   1632 O  O     . PRO A 1 201 ? -13.54675 15.61676  38.05862  1.000 22.35852  ? 201  PRO A O     1 
ATOM   1633 C  CB    . PRO A 1 201 ? -14.58665 13.23652  40.16501  1.000 23.58996  ? 201  PRO A CB    1 
ATOM   1634 C  CG    . PRO A 1 201 ? -15.21919 11.89818  40.24200  1.000 23.61417  ? 201  PRO A CG    1 
ATOM   1635 C  CD    . PRO A 1 201 ? -14.59544 11.09703  39.12845  1.000 22.20139  ? 201  PRO A CD    1 
ATOM   1636 N  N     . THR A 1 202 ? -12.04533 13.97746  38.41643  1.000 26.60628  ? 202  THR A N     1 
ATOM   1637 C  CA    . THR A 1 202 ? -10.92393 14.84172  38.06128  1.000 26.82075  ? 202  THR A CA    1 
ATOM   1638 C  C     . THR A 1 202 ? -10.97781 15.22943  36.58922  1.000 27.44119  ? 202  THR A C     1 
ATOM   1639 O  O     . THR A 1 202 ? -10.76858 16.39633  36.23579  1.000 27.91335  ? 202  THR A O     1 
ATOM   1640 C  CB    . THR A 1 202 ? -9.60124  14.14656  38.38654  1.000 26.11710  ? 202  THR A CB    1 
ATOM   1641 O  OG1   . THR A 1 202 ? -9.41555  14.11276  39.80678  1.000 26.79822  ? 202  THR A OG1   1 
ATOM   1642 C  CG2   . THR A 1 202 ? -8.43295  14.87984  37.74448  1.000 25.77105  ? 202  THR A CG2   1 
ATOM   1643 N  N     . THR A 1 203 ? -11.27281 14.26421  35.71709  1.000 22.77704  ? 203  THR A N     1 
ATOM   1644 C  CA    . THR A 1 203 ? -11.35328 14.55425  34.29065  1.000 22.79190  ? 203  THR A CA    1 
ATOM   1645 C  C     . THR A 1 203 ? -12.51269 15.49356  33.97961  1.000 23.56842  ? 203  THR A C     1 
ATOM   1646 O  O     . THR A 1 203 ? -12.39953 16.35099  33.09602  1.000 23.56864  ? 203  THR A O     1 
ATOM   1647 C  CB    . THR A 1 203 ? -11.48396 13.25219  33.50346  1.000 21.59418  ? 203  THR A CB    1 
ATOM   1648 O  OG1   . THR A 1 203 ? -10.42302 12.36555  33.87867  1.000 21.07100  ? 203  THR A OG1   1 
ATOM   1649 C  CG2   . THR A 1 203 ? -11.40517 13.51845  32.00876  1.000 21.47037  ? 203  THR A CG2   1 
ATOM   1650 N  N     . GLN A 1 204 ? -13.63296 15.35207  34.69639  1.000 22.68622  ? 204  GLN A N     1 
ATOM   1651 C  CA    A GLN A 1 204 ? -14.77348 16.23652  34.47281  0.455 23.45720  ? 204  GLN A CA    1 
ATOM   1652 C  CA    B GLN A 1 204 ? -14.76915 16.23805  34.46246  0.545 23.45676  ? 204  GLN A CA    1 
ATOM   1653 C  C     . GLN A 1 204 ? -14.42434 17.67951  34.81285  1.000 24.57871  ? 204  GLN A C     1 
ATOM   1654 O  O     . GLN A 1 204 ? -14.83119 18.61087  34.10731  1.000 24.73175  ? 204  GLN A O     1 
ATOM   1655 C  CB    A GLN A 1 204 ? -15.97302 15.77174  35.30142  0.455 23.96208  ? 204  GLN A CB    1 
ATOM   1656 C  CB    B GLN A 1 204 ? -15.98297 15.76986  35.26583  0.545 23.94783  ? 204  GLN A CB    1 
ATOM   1657 C  CG    A GLN A 1 204 ? -16.50015 14.38986  34.93960  0.455 23.33372  ? 204  GLN A CG    1 
ATOM   1658 C  CG    B GLN A 1 204 ? -17.01655 14.99682  34.45482  0.545 23.64701  ? 204  GLN A CG    1 
ATOM   1659 C  CD    A GLN A 1 204 ? -17.34331 13.77696  36.04512  0.455 23.76706  ? 204  GLN A CD    1 
ATOM   1660 C  CD    B GLN A 1 204 ? -17.47076 15.73364  33.20465  0.545 23.69080  ? 204  GLN A CD    1 
ATOM   1661 O  OE1   A GLN A 1 204 ? -17.81692 14.47498  36.94248  0.455 24.66538  ? 204  GLN A OE1   1 
ATOM   1662 O  OE1   B GLN A 1 204 ? -17.57179 15.14389  32.12851  0.545 23.06073  ? 204  GLN A OE1   1 
ATOM   1663 N  NE2   A GLN A 1 204 ? -17.53321 12.46418  35.98451  0.455 23.18075  ? 204  GLN A NE2   1 
ATOM   1664 N  NE2   B GLN A 1 204 ? -17.75940 17.02276  33.34404  0.545 24.42797  ? 204  GLN A NE2   1 
ATOM   1665 N  N     . THR A 1 205 ? -13.67515 17.88274  35.89828  1.000 24.63213  ? 205  THR A N     1 
ATOM   1666 C  CA    . THR A 1 205 ? -13.28396 19.23082  36.29340  1.000 25.34068  ? 205  THR A CA    1 
ATOM   1667 C  C     . THR A 1 205 ? -12.36478 19.85854  35.25308  1.000 25.22125  ? 205  THR A C     1 
ATOM   1668 O  O     . THR A 1 205 ? -12.56812 21.00708  34.84243  1.000 25.93385  ? 205  THR A O     1 
ATOM   1669 C  CB    . THR A 1 205 ? -12.60556 19.19718  37.66386  1.000 25.64601  ? 205  THR A CB    1 
ATOM   1670 O  OG1   . THR A 1 205 ? -13.52512 18.69389  38.64104  1.000 26.17834  ? 205  THR A OG1   1 
ATOM   1671 C  CG2   . THR A 1 205 ? -12.15843 20.59369  38.07301  1.000 26.40881  ? 205  THR A CG2   1 
ATOM   1672 N  N     . VAL A 1 206 ? -11.34811 19.11484  34.80980  1.000 27.83751  ? 206  VAL A N     1 
ATOM   1673 C  CA    . VAL A 1 206 ? -10.43829 19.63455  33.79252  1.000 27.76885  ? 206  VAL A CA    1 
ATOM   1674 C  C     . VAL A 1 206 ? -11.18589 19.86642  32.48618  1.000 27.84311  ? 206  VAL A C     1 
ATOM   1675 O  O     . VAL A 1 206 ? -10.91594 20.83033  31.75778  1.000 27.88614  ? 206  VAL A O     1 
ATOM   1676 C  CB    . VAL A 1 206 ? -9.24357  18.67866  33.61015  1.000 27.02353  ? 206  VAL A CB    1 
ATOM   1677 C  CG1   . VAL A 1 206 ? -8.37286  19.11618  32.44334  1.000 26.34188  ? 206  VAL A CG1   1 
ATOM   1678 C  CG2   . VAL A 1 206 ? -8.42292  18.61322  34.88852  1.000 27.15212  ? 206  VAL A CG2   1 
ATOM   1679 N  N     . LEU A 1 207 ? -12.15353 18.99882  32.18333  1.000 31.42233  ? 207  LEU A N     1 
ATOM   1680 C  CA    . LEU A 1 207 ? -12.94565 19.14914  30.96788  1.000 31.16010  ? 207  LEU A CA    1 
ATOM   1681 C  C     . LEU A 1 207 ? -13.71364 20.46722  30.97491  1.000 31.37300  ? 207  LEU A C     1 
ATOM   1682 O  O     . LEU A 1 207 ? -13.71706 21.20079  29.97985  1.000 31.11403  ? 207  LEU A O     1 
ATOM   1683 C  CB    . LEU A 1 207 ? -13.88818 17.95083  30.82432  1.000 30.60397  ? 207  LEU A CB    1 
ATOM   1684 C  CG    . LEU A 1 207 ? -14.57053 17.63654  29.49254  1.000 30.86189  ? 207  LEU A CG    1 
ATOM   1685 C  CD1   . LEU A 1 207 ? -15.13055 16.22839  29.53309  1.000 30.97842  ? 207  LEU A CD1   1 
ATOM   1686 C  CD2   . LEU A 1 207 ? -15.69208 18.62253  29.20860  1.000 30.45776  ? 207  LEU A CD2   1 
ATOM   1687 N  N     . GLU A 1 208 ? -14.36804 20.78768  32.09439  1.000 39.37627  ? 208  GLU A N     1 
ATOM   1688 C  CA    . GLU A 1 208 ? -15.09562 22.04997  32.18715  1.000 40.20385  ? 208  GLU A CA    1 
ATOM   1689 C  C     . GLU A 1 208 ? -14.14485 23.23825  32.10203  1.000 40.39567  ? 208  GLU A C     1 
ATOM   1690 O  O     . GLU A 1 208 ? -14.46438 24.25558  31.47616  1.000 39.93674  ? 208  GLU A O     1 
ATOM   1691 C  CB    . GLU A 1 208 ? -15.90474 22.09225  33.48553  1.000 40.35918  ? 208  GLU A CB    1 
ATOM   1692 C  CG    . GLU A 1 208 ? -16.97058 23.18242  33.54041  0.208 43.12195  ? 208  GLU A CG    1 
ATOM   1693 C  CD    . GLU A 1 208 ? -16.41301 24.54418  33.92092  1.000 44.41374  ? 208  GLU A CD    1 
ATOM   1694 O  OE1   . GLU A 1 208 ? -15.39210 24.59311  34.64036  1.000 43.05165  ? 208  GLU A OE1   1 
ATOM   1695 O  OE2   . GLU A 1 208 ? -16.99713 25.56684  33.50058  1.000 44.27627  ? 208  GLU A OE2   1 
ATOM   1696 N  N     . GLN A 1 209 ? -12.96770 23.12441  32.72202  1.000 39.82383  ? 209  GLN A N     1 
ATOM   1697 C  CA    . GLN A 1 209 ? -11.99530 24.21141  32.67736  1.000 39.44618  ? 209  GLN A CA    1 
ATOM   1698 C  C     . GLN A 1 209 ? -11.46439 24.42377  31.26480  1.000 38.57661  ? 209  GLN A C     1 
ATOM   1699 O  O     . GLN A 1 209 ? -11.27613 25.56647  30.83224  1.000 38.25990  ? 209  GLN A O     1 
ATOM   1700 C  CB    . GLN A 1 209 ? -10.84801 23.92543  33.64660  1.000 39.73356  ? 209  GLN A CB    1 
ATOM   1701 C  CG    . GLN A 1 209 ? -11.21704 24.08167  35.11480  1.000 41.94938  ? 209  GLN A CG    1 
ATOM   1702 C  CD    . GLN A 1 209 ? -10.08057 23.70409  36.04917  1.000 42.79315  ? 209  GLN A CD    1 
ATOM   1703 O  OE1   . GLN A 1 209 ? -8.94480  23.50472  35.61686  1.000 41.77411  ? 209  GLN A OE1   1 
ATOM   1704 N  NE2   . GLN A 1 209 ? -10.38276 23.60815  37.33948  1.000 43.11095  ? 209  GLN A NE2   1 
ATOM   1705 N  N     . VAL A 1 210 ? -11.21899 23.33754  30.52973  1.000 25.67474  ? 210  VAL A N     1 
ATOM   1706 C  CA    . VAL A 1 210 ? -10.71533 23.46778  29.16576  1.000 23.99898  ? 210  VAL A CA    1 
ATOM   1707 C  C     . VAL A 1 210 ? -11.80645 23.99634  28.24066  1.000 23.52433  ? 210  VAL A C     1 
ATOM   1708 O  O     . VAL A 1 210 ? -11.54191 24.82103  27.35742  1.000 23.35674  ? 210  VAL A O     1 
ATOM   1709 C  CB    . VAL A 1 210 ? -10.14518 22.12106  28.68112  1.000 23.59508  ? 210  VAL A CB    1 
ATOM   1710 C  CG1   . VAL A 1 210 ? -9.92070  22.13194  27.17320  1.000 21.80833  ? 210  VAL A CG1   1 
ATOM   1711 C  CG2   . VAL A 1 210 ? -8.84585  21.80679  29.41203  1.000 23.04103  ? 210  VAL A CG2   1 
ATOM   1712 N  N     . SER A 1 211 ? -13.05040 23.54666  28.43797  1.000 33.26997  ? 211  SER A N     1 
ATOM   1713 C  CA    . SER A 1 211 ? -14.16445 24.05249  27.63846  1.000 33.18137  ? 211  SER A CA    1 
ATOM   1714 C  C     . SER A 1 211 ? -14.28651 25.56358  27.75477  1.000 33.32252  ? 211  SER A C     1 
ATOM   1715 O  O     . SER A 1 211 ? -14.64676 26.24591  26.78840  1.000 33.27791  ? 211  SER A O     1 
ATOM   1716 C  CB    . SER A 1 211 ? -15.47296 23.40028  28.08264  1.000 33.63329  ? 211  SER A CB    1 
ATOM   1717 O  OG    . SER A 1 211 ? -15.54830 22.05455  27.66965  1.000 34.01275  ? 211  SER A OG    1 
ATOM   1718 N  N     . ARG A 1 212 ? -13.98663 26.10054  28.93179  1.000 42.63890  ? 212  ARG A N     1 
ATOM   1719 C  CA    . ARG A 1 212 ? -14.22801 27.50190  29.23202  1.000 42.94963  ? 212  ARG A CA    1 
ATOM   1720 C  C     . ARG A 1 212 ? -13.01673 28.38513  28.96993  1.000 42.77919  ? 212  ARG A C     1 
ATOM   1721 O  O     . ARG A 1 212 ? -13.18184 29.54580  28.57652  1.000 42.63170  ? 212  ARG A O     1 
ATOM   1722 C  CB    . ARG A 1 212 ? -14.66001 27.63625  30.69344  1.000 44.20351  ? 212  ARG A CB    1 
ATOM   1723 C  CG    . ARG A 1 212 ? -15.24026 28.97713  31.05656  1.000 46.49951  ? 212  ARG A CG    1 
ATOM   1724 C  CD    . ARG A 1 212 ? -16.34797 28.83502  32.09459  1.000 47.34251  ? 212  ARG A CD    1 
ATOM   1725 N  NE    . ARG A 1 212 ? -15.99013 27.94781  33.19803  1.000 47.94932  ? 212  ARG A NE    1 
ATOM   1726 C  CZ    . ARG A 1 212 ? -14.99215 28.15162  34.04989  1.000 48.68120  ? 212  ARG A CZ    1 
ATOM   1727 N  NH1   . ARG A 1 212 ? -14.22462 29.22866  33.97850  1.000 48.58224  ? 212  ARG A NH1   1 
ATOM   1728 N  NH2   . ARG A 1 212 ? -14.76398 27.25575  35.00590  1.000 49.18201  ? 212  ARG A NH2   1 
ATOM   1729 N  N     . GLY A 1 213 ? -11.80702 27.86386  29.16394  1.000 29.14883  ? 213  GLY A N     1 
ATOM   1730 C  CA    . GLY A 1 213 ? -10.61553 28.68749  29.09746  1.000 29.04699  ? 213  GLY A CA    1 
ATOM   1731 C  C     . GLY A 1 213 ? -9.78944  28.54361  27.83593  1.000 27.57121  ? 213  GLY A C     1 
ATOM   1732 O  O     . GLY A 1 213 ? -8.90811  29.36759  27.57446  1.000 27.57749  ? 213  GLY A O     1 
ATOM   1733 N  N     . PHE A 1 214 ? -10.05381 27.50678  27.04631  1.000 26.34867  ? 214  PHE A N     1 
ATOM   1734 C  CA    . PHE A 1 214 ? -9.30515  27.24779  25.82155  1.000 24.75694  ? 214  PHE A CA    1 
ATOM   1735 C  C     . PHE A 1 214 ? -10.24977 26.99130  24.65736  1.000 24.58864  ? 214  PHE A C     1 
ATOM   1736 O  O     . PHE A 1 214 ? -10.02255 26.09772  23.83678  1.000 23.91158  ? 214  PHE A O     1 
ATOM   1737 C  CB    . PHE A 1 214 ? -8.34557  26.07263  26.00281  1.000 24.09330  ? 214  PHE A CB    1 
ATOM   1738 C  CG    . PHE A 1 214 ? -7.29276  26.30527  27.04721  1.000 24.46885  ? 214  PHE A CG    1 
ATOM   1739 C  CD1   . PHE A 1 214 ? -7.57029  26.09827  28.38822  1.000 25.76220  ? 214  PHE A CD1   1 
ATOM   1740 C  CD2   . PHE A 1 214 ? -6.02620  26.73137  26.68866  1.000 23.79107  ? 214  PHE A CD2   1 
ATOM   1741 C  CE1   . PHE A 1 214 ? -6.60738  26.31591  29.35117  1.000 26.52541  ? 214  PHE A CE1   1 
ATOM   1742 C  CE2   . PHE A 1 214 ? -5.05617  26.94868  27.64932  1.000 24.39417  ? 214  PHE A CE2   1 
ATOM   1743 C  CZ    . PHE A 1 214 ? -5.34831  26.74145  28.98170  1.000 25.90441  ? 214  PHE A CZ    1 
ATOM   1744 N  N     . ASP A 1 215 ? -11.32370 27.78111  24.56306  1.000 44.96572  ? 215  ASP A N     1 
ATOM   1745 C  CA    . ASP A 1 215 ? -12.32596 27.56346  23.52432  1.000 45.01537  ? 215  ASP A CA    1 
ATOM   1746 C  C     . ASP A 1 215 ? -11.77142 27.75353  22.11935  1.000 42.79711  ? 215  ASP A C     1 
ATOM   1747 O  O     . ASP A 1 215 ? -12.32108 27.19017  21.16632  1.000 42.41551  ? 215  ASP A O     1 
ATOM   1748 C  CB    . ASP A 1 215 ? -13.51730 28.49926  23.73281  1.000 45.15564  ? 215  ASP A CB    1 
ATOM   1749 C  CG    . ASP A 1 215 ? -14.75185 28.03846  22.98661  1.000 45.53773  ? 215  ASP A CG    1 
ATOM   1750 O  OD1   . ASP A 1 215 ? -15.10701 26.84601  23.09730  1.000 46.43845  ? 215  ASP A OD1   1 
ATOM   1751 O  OD2   . ASP A 1 215 ? -15.35643 28.86500  22.27249  1.000 46.05385  ? 215  ASP A OD2   1 
ATOM   1752 N  N     . ASP A 1 216 ? -10.69991 28.52291  21.96939  1.000 46.25431  ? 216  ASP A N     1 
ATOM   1753 C  CA    . ASP A 1 216 ? -10.13591 28.83873  20.66680  1.000 45.19593  ? 216  ASP A CA    1 
ATOM   1754 C  C     . ASP A 1 216 ? -9.10582  27.80864  20.20316  1.000 44.30294  ? 216  ASP A C     1 
ATOM   1755 O  O     . ASP A 1 216 ? -8.41469  28.04011  19.20553  1.000 43.63104  ? 216  ASP A O     1 
ATOM   1756 C  CB    . ASP A 1 216 ? -9.54773  30.25301  20.70779  1.000 44.73144  ? 216  ASP A CB    1 
ATOM   1757 C  CG    . ASP A 1 216 ? -8.14409  30.28791  21.25486  1.000 47.48392  ? 216  ASP A CG    1 
ATOM   1758 O  OD1   . ASP A 1 216 ? -7.96124  29.98563  22.45355  1.000 48.31740  ? 216  ASP A OD1   1 
ATOM   1759 O  OD2   . ASP A 1 216 ? -7.22949  30.67370  20.50030  1.000 47.30896  ? 216  ASP A OD2   1 
ATOM   1760 N  N     . HIS A 1 217 ? -9.00675  26.67359  20.89024  1.000 27.64611  ? 217  HIS A N     1 
ATOM   1761 C  CA    . HIS A 1 217 ? -8.18654  25.55503  20.45313  1.000 26.54315  ? 217  HIS A CA    1 
ATOM   1762 C  C     . HIS A 1 217 ? -9.00632  24.61752  19.57145  1.000 26.87622  ? 217  HIS A C     1 
ATOM   1763 O  O     . HIS A 1 217 ? -10.23647 24.57409  19.64200  1.000 26.95687  ? 217  HIS A O     1 
ATOM   1764 C  CB    . HIS A 1 217 ? -7.62603  24.78619  21.65212  1.000 27.38829  ? 217  HIS A CB    1 
ATOM   1765 C  CG    . HIS A 1 217 ? -6.42472  25.42577  22.27876  1.000 27.99746  ? 217  HIS A CG    1 
ATOM   1766 N  ND1   . HIS A 1 217 ? -5.29195  24.71340  22.61015  1.000 26.81930  ? 217  HIS A ND1   1 
ATOM   1767 C  CD2   . HIS A 1 217 ? -6.18124  26.70820  22.64093  1.000 27.97195  ? 217  HIS A CD2   1 
ATOM   1768 C  CE1   . HIS A 1 217 ? -4.40174  25.52910  23.14632  1.000 27.13352  ? 217  HIS A CE1   1 
ATOM   1769 N  NE2   . HIS A 1 217 ? -4.91607  26.74551  23.17590  1.000 27.70161  ? 217  HIS A NE2   1 
ATOM   1770 N  N     . PHE A 1 218 ? -8.30213  23.85966  18.73653  1.000 21.67253  ? 218  PHE A N     1 
ATOM   1771 C  CA    . PHE A 1 218 ? -8.95212  22.94604  17.80854  1.000 21.30466  ? 218  PHE A CA    1 
ATOM   1772 C  C     . PHE A 1 218 ? -9.59070  21.77426  18.54895  1.000 21.61432  ? 218  PHE A C     1 
ATOM   1773 O  O     . PHE A 1 218 ? -9.09034  21.30872  19.57692  1.000 21.71977  ? 218  PHE A O     1 
ATOM   1774 C  CB    . PHE A 1 218 ? -7.93523  22.43276  16.78390  1.000 20.37332  ? 218  PHE A CB    1 
ATOM   1775 C  CG    . PHE A 1 218 ? -8.46085  21.34641  15.88050  1.000 20.05792  ? 218  PHE A CG    1 
ATOM   1776 C  CD1   . PHE A 1 218 ? -9.12548  21.66568  14.70715  1.000 20.06500  ? 218  PHE A CD1   1 
ATOM   1777 C  CD2   . PHE A 1 218 ? -8.26259  20.00768  16.18905  1.000 19.82937  ? 218  PHE A CD2   1 
ATOM   1778 C  CE1   . PHE A 1 218 ? -9.60058  20.67266  13.86957  1.000 19.88490  ? 218  PHE A CE1   1 
ATOM   1779 C  CE2   . PHE A 1 218 ? -8.73589  19.01068  15.35599  1.000 19.67560  ? 218  PHE A CE2   1 
ATOM   1780 C  CZ    . PHE A 1 218 ? -9.40508  19.34387  14.19413  1.000 19.71462  ? 218  PHE A CZ    1 
ATOM   1781 N  N     . GLY A 1 219 ? -10.71514 21.30693  18.01872  1.000 24.42290  ? 219  GLY A N     1 
ATOM   1782 C  CA    . GLY A 1 219 ? -11.28587 20.04163  18.42460  1.000 25.42860  ? 219  GLY A CA    1 
ATOM   1783 C  C     . GLY A 1 219 ? -12.42154 20.19317  19.42428  1.000 26.88833  ? 219  GLY A C     1 
ATOM   1784 O  O     . GLY A 1 219 ? -12.57882 21.21739  20.09376  1.000 27.73914  ? 219  GLY A O     1 
ATOM   1785 N  N     . GLU A 1 220 ? -13.22608 19.13604  19.51745  1.000 22.21177  ? 220  GLU A N     1 
ATOM   1786 C  CA    . GLU A 1 220 ? -14.31020 19.04815  20.48484  0.677 23.71037  ? 220  GLU A CA    1 
ATOM   1787 C  C     . GLU A 1 220 ? -13.82140 18.35049  21.74740  1.000 24.26385  ? 220  GLU A C     1 
ATOM   1788 O  O     . GLU A 1 220 ? -13.00405 17.42820  21.68206  1.000 23.59593  ? 220  GLU A O     1 
ATOM   1789 C  CB    . GLU A 1 220 ? -15.49756 18.28343  19.89300  1.000 23.67995  ? 220  GLU A CB    1 
ATOM   1790 C  CG    . GLU A 1 220 ? -16.84452 18.62257  20.51695  0.639 25.03661  ? 220  GLU A CG    1 
ATOM   1791 C  CD    . GLU A 1 220 ? -17.60764 19.67262  19.73155  0.483 26.54473  ? 220  GLU A CD    1 
ATOM   1792 O  OE1   . GLU A 1 220 ? -16.99817 20.32403  18.85746  0.346 25.25679  ? 220  GLU A OE1   1 
ATOM   1793 O  OE2   . GLU A 1 220 ? -18.81846 19.84469  19.98786  0.545 26.94197  ? 220  GLU A OE2   1 
ATOM   1794 N  N     . VAL A 1 221 ? -14.32838 18.79568  22.89741  1.000 39.07414  ? 221  VAL A N     1 
ATOM   1795 C  CA    . VAL A 1 221 ? -13.97993 18.18908  24.17813  1.000 40.38247  ? 221  VAL A CA    1 
ATOM   1796 C  C     . VAL A 1 221 ? -15.05881 17.18947  24.56625  1.000 40.96163  ? 221  VAL A C     1 
ATOM   1797 O  O     . VAL A 1 221 ? -14.79180 16.21717  25.28074  1.000 41.72821  ? 221  VAL A O     1 
ATOM   1798 C  CB    . VAL A 1 221 ? -13.80351 19.24875  25.28114  1.000 41.59604  ? 221  VAL A CB    1 
ATOM   1799 C  CG1   . VAL A 1 221 ? -13.03351 20.41296  24.76162  1.000 41.45154  ? 221  VAL A CG1   1 
ATOM   1800 C  CG2   . VAL A 1 221 ? -15.14506 19.71739  25.79478  1.000 42.63200  ? 221  VAL A CG2   1 
ATOM   1801 N  N     . GLU A 1 222 ? -16.28343 17.42281  24.10352  1.000 72.53317  ? 222  GLU A N     1 
ATOM   1802 C  CA    . GLU A 1 222 ? -17.39561 16.57550  24.49988  1.000 72.93924  ? 222  GLU A CA    1 
ATOM   1803 C  C     . GLU A 1 222 ? -17.23756 15.19401  23.88052  1.000 72.66878  ? 222  GLU A C     1 
ATOM   1804 O  O     . GLU A 1 222 ? -16.79034 15.05394  22.73827  1.000 72.08867  ? 222  GLU A O     1 
ATOM   1805 C  CB    . GLU A 1 222 ? -18.72072 17.21503  24.08679  1.000 73.77506  ? 222  GLU A CB    1 
ATOM   1806 C  CG    . GLU A 1 222 ? -19.87923 16.24878  23.94485  1.000 74.49551  ? 222  GLU A CG    1 
ATOM   1807 C  CD    . GLU A 1 222 ? -20.08843 15.81930  22.51061  1.000 74.04767  ? 222  GLU A CD    1 
ATOM   1808 O  OE1   . GLU A 1 222 ? -20.30633 16.70468  21.65736  1.000 73.69521  ? 222  GLU A OE1   1 
ATOM   1809 O  OE2   . GLU A 1 222 ? -20.03430 14.60198  22.23655  1.000 73.80132  ? 222  GLU A OE2   1 
ATOM   1810 N  N     . GLY A 1 223 ? -17.59555 14.17001  24.64924  1.000 35.87478  ? 223  GLY A N     1 
ATOM   1811 C  CA    . GLY A 1 223 ? -17.34281 12.80143  24.25936  1.000 35.65720  ? 223  GLY A CA    1 
ATOM   1812 C  C     . GLY A 1 223 ? -15.95047 12.30669  24.57041  1.000 35.02001  ? 223  GLY A C     1 
ATOM   1813 O  O     . GLY A 1 223 ? -15.58240 11.21932  24.10980  1.000 35.15307  ? 223  GLY A O     1 
ATOM   1814 N  N     . PHE A 1 224 ? -15.16271 13.07943  25.31850  1.000 24.31089  ? 224  PHE A N     1 
ATOM   1815 C  CA    . PHE A 1 224 ? -13.82949 12.67027  25.74454  1.000 24.05177  ? 224  PHE A CA    1 
ATOM   1816 C  C     . PHE A 1 224 ? -13.87546 11.29946  26.40097  1.000 24.04449  ? 224  PHE A C     1 
ATOM   1817 O  O     . PHE A 1 224 ? -14.59726 11.09296  27.38048  1.000 24.09316  ? 224  PHE A O     1 
ATOM   1818 C  CB    . PHE A 1 224 ? -13.26529 13.71188  26.71583  1.000 24.96908  ? 224  PHE A CB    1 
ATOM   1819 C  CG    . PHE A 1 224 ? -11.87003 13.41568  27.19463  1.000 24.60109  ? 224  PHE A CG    1 
ATOM   1820 C  CD1   . PHE A 1 224 ? -11.65418 12.68689  28.35592  1.000 25.09322  ? 224  PHE A CD1   1 
ATOM   1821 C  CD2   . PHE A 1 224 ? -10.77264 13.88028  26.48977  1.000 23.82640  ? 224  PHE A CD2   1 
ATOM   1822 C  CE1   . PHE A 1 224 ? -10.36973 12.42087  28.79572  1.000 24.40485  ? 224  PHE A CE1   1 
ATOM   1823 C  CE2   . PHE A 1 224 ? -9.48769  13.61812  26.92589  1.000 23.84734  ? 224  PHE A CE2   1 
ATOM   1824 C  CZ    . PHE A 1 224 ? -9.28640  12.88809  28.08021  1.000 24.60706  ? 224  PHE A CZ    1 
ATOM   1825 N  N     . GLY A 1 225 ? -13.10841 10.36019  25.85609  1.000 20.44214  ? 225  GLY A N     1 
ATOM   1826 C  CA    . GLY A 1 225 ? -13.13297 9.00333   26.36215  1.000 19.50125  ? 225  GLY A CA    1 
ATOM   1827 C  C     . GLY A 1 225 ? -11.76141 8.38196   26.51094  1.000 18.97085  ? 225  GLY A C     1 
ATOM   1828 O  O     . GLY A 1 225 ? -11.63223 7.15462   26.53733  1.000 18.29147  ? 225  GLY A O     1 
ATOM   1829 N  N     . TRP A 1 226 ? -10.72804 9.21848   26.60964  1.000 19.80698  ? 226  TRP A N     1 
ATOM   1830 C  CA    . TRP A 1 226 ? -9.37571  8.71170   26.76885  1.000 19.11535  ? 226  TRP A CA    1 
ATOM   1831 C  C     . TRP A 1 226 ? -9.09532  8.37041   28.23192  1.000 18.75102  ? 226  TRP A C     1 
ATOM   1832 O  O     . TRP A 1 226 ? -9.62489  9.01457   29.14124  1.000 19.58311  ? 226  TRP A O     1 
ATOM   1833 C  CB    . TRP A 1 226 ? -8.35829  9.73629   26.27581  1.000 19.45081  ? 226  TRP A CB    1 
ATOM   1834 C  CG    . TRP A 1 226 ? -8.44108  10.00150  24.80473  1.000 20.02999  ? 226  TRP A CG    1 
ATOM   1835 C  CD1   . TRP A 1 226 ? -8.92129  11.12624  24.20056  1.000 20.86880  ? 226  TRP A CD1   1 
ATOM   1836 C  CD2   . TRP A 1 226 ? -8.03362  9.12197   23.74941  1.000 19.54992  ? 226  TRP A CD2   1 
ATOM   1837 N  NE1   . TRP A 1 226 ? -8.83809  11.00233  22.83462  1.000 19.68121  ? 226  TRP A NE1   1 
ATOM   1838 C  CE2   . TRP A 1 226 ? -8.29708  9.78072   22.53195  1.000 19.66065  ? 226  TRP A CE2   1 
ATOM   1839 C  CE3   . TRP A 1 226 ? -7.47091  7.84233   23.71602  1.000 18.13894  ? 226  TRP A CE3   1 
ATOM   1840 C  CZ2   . TRP A 1 226 ? -8.01691  9.20382   21.29488  1.000 18.74520  ? 226  TRP A CZ2   1 
ATOM   1841 C  CZ3   . TRP A 1 226 ? -7.19547  7.26999   22.48702  1.000 17.62735  ? 226  TRP A CZ3   1 
ATOM   1842 C  CH2   . TRP A 1 226 ? -7.46803  7.95070   21.29369  1.000 18.44191  ? 226  TRP A CH2   1 
ATOM   1843 N  N     . PRO A 1 227 ? -8.27238  7.35339   28.48155  1.000 19.07135  ? 227  PRO A N     1 
ATOM   1844 C  CA    . PRO A 1 227 ? -7.91446  7.02124   29.86604  1.000 18.68100  ? 227  PRO A CA    1 
ATOM   1845 C  C     . PRO A 1 227 ? -6.91416  8.01899   30.43014  1.000 18.61325  ? 227  PRO A C     1 
ATOM   1846 O  O     . PRO A 1 227 ? -6.03141  8.50724   29.72143  1.000 18.45839  ? 227  PRO A O     1 
ATOM   1847 C  CB    . PRO A 1 227 ? -7.30423  5.62083   29.74623  1.000 17.49076  ? 227  PRO A CB    1 
ATOM   1848 C  CG    . PRO A 1 227 ? -6.77200  5.56458   28.34643  1.000 16.80897  ? 227  PRO A CG    1 
ATOM   1849 C  CD    . PRO A 1 227 ? -7.70285  6.40152   27.51017  1.000 18.56657  ? 227  PRO A CD    1 
ATOM   1850 N  N     . THR A 1 228 ? -7.05390  8.31401   31.72494  1.000 18.85832  ? 228  THR A N     1 
ATOM   1851 C  CA    . THR A 1 228 ? -6.24925  9.34193   32.37395  1.000 18.98149  ? 228  THR A CA    1 
ATOM   1852 C  C     . THR A 1 228 ? -5.45619  8.85143   33.57922  1.000 18.08887  ? 228  THR A C     1 
ATOM   1853 O  O     . THR A 1 228 ? -4.79225  9.66739   34.22946  1.000 18.57583  ? 228  THR A O     1 
ATOM   1854 C  CB    . THR A 1 228 ? -7.13682  10.51394  32.81445  1.000 20.33351  ? 228  THR A CB    1 
ATOM   1855 O  OG1   . THR A 1 228 ? -8.05114  10.06589  33.82160  1.000 20.34264  ? 228  THR A OG1   1 
ATOM   1856 C  CG2   . THR A 1 228 ? -7.91774  11.07429  31.63401  1.000 21.08099  ? 228  THR A CG2   1 
ATOM   1857 N  N     . ASN A 1 229 ? -5.50308  7.56416   33.90209  1.000 19.98268  ? 229  ASN A N     1 
ATOM   1858 C  CA    . ASN A 1 229 ? -4.74447  7.02043   35.02047  1.000 19.22407  ? 229  ASN A CA    1 
ATOM   1859 C  C     . ASN A 1 229 ? -4.37429  5.58512   34.68216  1.000 18.32961  ? 229  ASN A C     1 
ATOM   1860 O  O     . ASN A 1 229 ? -4.87601  5.02212   33.70085  1.000 18.41718  ? 229  ASN A O     1 
ATOM   1861 C  CB    . ASN A 1 229 ? -5.53815  7.11234   36.33593  1.000 19.77429  ? 229  ASN A CB    1 
ATOM   1862 C  CG    . ASN A 1 229 ? -6.85163  6.35079   36.29953  1.000 20.61722  ? 229  ASN A CG    1 
ATOM   1863 O  OD1   . ASN A 1 229 ? -6.89084  5.16009   35.99277  1.000 19.44052  ? 229  ASN A OD1   1 
ATOM   1864 N  ND2   . ASN A 1 229 ? -7.93797  7.03884   36.63377  1.000 21.09067  ? 229  ASN A ND2   1 
ATOM   1865 N  N     . PRO A 1 230 ? -3.46977  4.96708   35.45854  1.000 25.62288  ? 230  PRO A N     1 
ATOM   1866 C  CA    . PRO A 1 230 ? -3.05679  3.59075   35.12094  1.000 25.91977  ? 230  PRO A CA    1 
ATOM   1867 C  C     . PRO A 1 230 ? -4.20069  2.59161   35.07315  1.000 25.49748  ? 230  PRO A C     1 
ATOM   1868 O  O     . PRO A 1 230 ? -4.18102  1.68260   34.23404  1.000 25.48630  ? 230  PRO A O     1 
ATOM   1869 C  CB    . PRO A 1 230 ? -2.05398  3.24756   36.23106  1.000 26.39825  ? 230  PRO A CB    1 
ATOM   1870 C  CG    . PRO A 1 230 ? -1.50867  4.55383   36.65331  1.000 26.30204  ? 230  PRO A CG    1 
ATOM   1871 C  CD    . PRO A 1 230 ? -2.64415  5.52498   36.54612  1.000 25.24531  ? 230  PRO A CD    1 
ATOM   1872 N  N     . ASP A 1 231 ? -5.19874  2.72674   35.94894  1.000 31.68946  ? 231  ASP A N     1 
ATOM   1873 C  CA    . ASP A 1 231 ? -6.29877  1.76688   35.95409  1.000 31.68785  ? 231  ASP A CA    1 
ATOM   1874 C  C     . ASP A 1 231 ? -7.15965  1.89802   34.70299  1.000 31.67295  ? 231  ASP A C     1 
ATOM   1875 O  O     . ASP A 1 231 ? -7.54643  0.88854   34.10210  1.000 31.19656  ? 231  ASP A O     1 
ATOM   1876 C  CB    . ASP A 1 231 ? -7.14444  1.94266   37.21365  1.000 32.18687  ? 231  ASP A CB    1 
ATOM   1877 C  CG    . ASP A 1 231 ? -6.50530  1.31230   38.43514  1.000 32.99921  ? 231  ASP A CG    1 
ATOM   1878 O  OD1   . ASP A 1 231 ? -5.28171  1.05834   38.40684  1.000 34.03888  ? 231  ASP A OD1   1 
ATOM   1879 O  OD2   . ASP A 1 231 ? -7.22661  1.06989   39.42407  1.000 34.07513  ? 231  ASP A OD2   1 
ATOM   1880 N  N     . GLU A 1 232 ? -7.47165  3.13093   34.29507  1.000 19.03570  ? 232  GLU A N     1 
ATOM   1881 C  CA    . GLU A 1 232 ? -8.24259  3.32695   33.07079  1.000 18.91299  ? 232  GLU A CA    1 
ATOM   1882 C  C     . GLU A 1 232 ? -7.43932  2.91313   31.84239  1.000 19.00071  ? 232  GLU A C     1 
ATOM   1883 O  O     . GLU A 1 232 ? -7.99687  2.36508   30.88480  1.000 19.19793  ? 232  GLU A O     1 
ATOM   1884 C  CB    . GLU A 1 232 ? -8.69245  4.78664   32.95458  1.000 18.78527  ? 232  GLU A CB    1 
ATOM   1885 C  CG    . GLU A 1 232 ? -9.55086  5.28824   34.11393  1.000 19.09373  ? 232  GLU A CG    1 
ATOM   1886 C  CD    . GLU A 1 232 ? -9.88583  6.77186   34.00719  1.000 19.18744  ? 232  GLU A CD    1 
ATOM   1887 O  OE1   . GLU A 1 232 ? -9.22005  7.48879   33.22854  1.000 19.20965  ? 232  GLU A OE1   1 
ATOM   1888 O  OE2   . GLU A 1 232 ? -10.82307 7.22192   34.69876  1.000 19.24708  ? 232  GLU A OE2   1 
ATOM   1889 N  N     . ALA A 1 233 ? -6.12830  3.16686   31.85005  1.000 19.79252  ? 233  ALA A N     1 
ATOM   1890 C  CA    . ALA A 1 233 ? -5.29513  2.77421   30.71743  1.000 20.04095  ? 233  ALA A CA    1 
ATOM   1891 C  C     . ALA A 1 233 ? -5.15019  1.25995   30.63739  1.000 20.76113  ? 233  ALA A C     1 
ATOM   1892 O  O     . ALA A 1 233 ? -5.12549  0.69017   29.54021  1.000 20.59938  ? 233  ALA A O     1 
ATOM   1893 C  CB    . ALA A 1 233 ? -3.92418  3.44180   30.81521  1.000 19.76758  ? 233  ALA A CB    1 
ATOM   1894 N  N     . THR A 1 234 ? -5.04407  0.59243   31.78839  1.000 19.82428  ? 234  THR A N     1 
ATOM   1895 C  CA    . THR A 1 234 ? -4.99785  -0.86562  31.79163  1.000 20.49910  ? 234  THR A CA    1 
ATOM   1896 C  C     . THR A 1 234 ? -6.29887  -1.45043  31.25608  1.000 20.81397  ? 234  THR A C     1 
ATOM   1897 O  O     . THR A 1 234 ? -6.28963  -2.46629  30.54963  1.000 20.90799  ? 234  THR A O     1 
ATOM   1898 C  CB    . THR A 1 234 ? -4.71188  -1.37805  33.20514  1.000 20.79902  ? 234  THR A CB    1 
ATOM   1899 O  OG1   . THR A 1 234 ? -3.38591  -0.99487  33.59185  1.000 20.41811  ? 234  THR A OG1   1 
ATOM   1900 C  CG2   . THR A 1 234 ? -4.82753  -2.89640  33.26578  1.000 20.95929  ? 234  THR A CG2   1 
ATOM   1901 N  N     . ALA A 1 235 ? -7.42875  -0.80906  31.56796  1.000 21.18060  ? 235  ALA A N     1 
ATOM   1902 C  CA    . ALA A 1 235 ? -8.71025  -1.26606  31.04034  1.000 21.49804  ? 235  ALA A CA    1 
ATOM   1903 C  C     . ALA A 1 235 ? -8.74484  -1.16918  29.52060  1.000 21.42650  ? 235  ALA A C     1 
ATOM   1904 O  O     . ALA A 1 235 ? -9.31094  -2.03878  28.84749  1.000 21.54228  ? 235  ALA A O     1 
ATOM   1905 C  CB    . ALA A 1 235 ? -9.85107  -0.45774  31.65873  1.000 20.78010  ? 235  ALA A CB    1 
ATOM   1906 N  N     . ILE A 1 236 ? -8.14276  -0.11691  28.96257  1.000 25.23995  ? 236  ILE A N     1 
ATOM   1907 C  CA    . ILE A 1 236 ? -8.05668  0.00792   27.51170  1.000 24.94859  ? 236  ILE A CA    1 
ATOM   1908 C  C     . ILE A 1 236 ? -7.13872  -1.06494  26.94086  1.000 25.52054  ? 236  ILE A C     1 
ATOM   1909 O  O     . ILE A 1 236 ? -7.44196  -1.67885  25.91001  1.000 25.77643  ? 236  ILE A O     1 
ATOM   1910 C  CB    . ILE A 1 236 ? -7.58593  1.42354   27.12898  1.000 25.20461  ? 236  ILE A CB    1 
ATOM   1911 C  CG1   . ILE A 1 236 ? -8.70965  2.43569   27.35436  1.000 24.49572  ? 236  ILE A CG1   1 
ATOM   1912 C  CG2   . ILE A 1 236 ? -7.11827  1.46686   25.68240  1.000 24.43932  ? 236  ILE A CG2   1 
ATOM   1913 C  CD1   . ILE A 1 236 ? -9.94297  2.15664   26.53670  1.000 24.90083  ? 236  ILE A CD1   1 
ATOM   1914 N  N     . LEU A 1 237 ? -6.00777  -1.31587  27.60535  1.000 16.36223  ? 237  LEU A N     1 
ATOM   1915 C  CA    . LEU A 1 237 ? -5.07960  -2.33278  27.12413  1.000 16.82866  ? 237  LEU A CA    1 
ATOM   1916 C  C     . LEU A 1 237 ? -5.67116  -3.73070  27.26442  1.000 17.63999  ? 237  LEU A C     1 
ATOM   1917 O  O     . LEU A 1 237 ? -5.52882  -4.56177  26.35965  1.000 17.74190  ? 237  LEU A O     1 
ATOM   1918 C  CB    . LEU A 1 237 ? -3.75051  -2.22772  27.87242  1.000 17.06917  ? 237  LEU A CB    1 
ATOM   1919 C  CG    . LEU A 1 237 ? -2.65117  -3.20749  27.45268  1.000 17.72483  ? 237  LEU A CG    1 
ATOM   1920 C  CD1   . LEU A 1 237 ? -2.23001  -2.96067  26.01207  1.000 17.91251  ? 237  LEU A CD1   1 
ATOM   1921 C  CD2   . LEU A 1 237 ? -1.45609  -3.10864  28.38651  1.000 17.86662  ? 237  LEU A CD2   1 
ATOM   1922 N  N     . ASP A 1 238 ? -6.33632  -4.00936  28.38989  1.000 25.87440  ? 238  ASP A N     1 
ATOM   1923 C  CA    . ASP A 1 238 ? -7.02474  -5.28769  28.54323  1.000 26.74800  ? 238  ASP A CA    1 
ATOM   1924 C  C     . ASP A 1 238 ? -8.01578  -5.51157  27.41004  1.000 26.98668  ? 238  ASP A C     1 
ATOM   1925 O  O     . ASP A 1 238 ? -8.08383  -6.60576  26.83754  1.000 27.31993  ? 238  ASP A O     1 
ATOM   1926 C  CB    . ASP A 1 238 ? -7.74550  -5.34225  29.89033  1.000 26.59868  ? 238  ASP A CB    1 
ATOM   1927 C  CG    . ASP A 1 238 ? -6.79370  -5.48564  31.05753  1.000 26.70463  ? 238  ASP A CG    1 
ATOM   1928 O  OD1   . ASP A 1 238 ? -5.60338  -5.77770  30.82322  1.000 27.82091  ? 238  ASP A OD1   1 
ATOM   1929 O  OD2   . ASP A 1 238 ? -7.23807  -5.30724  32.21119  1.000 27.41751  ? 238  ASP A OD2   1 
ATOM   1930 N  N     . HIS A 1 239 ? -8.78276  -4.47499  27.06596  1.000 24.56832  ? 239  HIS A N     1 
ATOM   1931 C  CA    . HIS A 1 239 ? -9.77441  -4.59326  26.00350  1.000 24.24790  ? 239  HIS A CA    1 
ATOM   1932 C  C     . HIS A 1 239 ? -9.12045  -4.91385  24.66414  1.000 24.77892  ? 239  HIS A C     1 
ATOM   1933 O  O     . HIS A 1 239 ? -9.62702  -5.74729  23.90331  1.000 25.11860  ? 239  HIS A O     1 
ATOM   1934 C  CB    . HIS A 1 239 ? -10.59038 -3.30240  25.91918  1.000 23.57337  ? 239  HIS A CB    1 
ATOM   1935 C  CG    . HIS A 1 239 ? -11.37683 -3.15965  24.65370  1.000 24.06914  ? 239  HIS A CG    1 
ATOM   1936 N  ND1   . HIS A 1 239 ? -12.42317 -3.99506  24.32698  1.000 24.63554  ? 239  HIS A ND1   1 
ATOM   1937 C  CD2   . HIS A 1 239 ? -11.27101 -2.27334  23.63531  1.000 23.62001  ? 239  HIS A CD2   1 
ATOM   1938 C  CE1   . HIS A 1 239 ? -12.92711 -3.63074  23.16128  1.000 24.12782  ? 239  HIS A CE1   1 
ATOM   1939 N  NE2   . HIS A 1 239 ? -12.24558 -2.58869  22.72002  1.000 23.91785  ? 239  HIS A NE2   1 
ATOM   1940 N  N     . PHE A 1 240 ? -7.98911  -4.27179  24.36037  1.000 17.75770  ? 240  PHE A N     1 
ATOM   1941 C  CA    . PHE A 1 240 ? -7.31581  -4.53294  23.09110  1.000 18.39247  ? 240  PHE A CA    1 
ATOM   1942 C  C     . PHE A 1 240 ? -6.74851  -5.94670  23.04134  1.000 19.36248  ? 240  PHE A C     1 
ATOM   1943 O  O     . PHE A 1 240 ? -6.96995  -6.67885  22.06945  1.000 19.64054  ? 240  PHE A O     1 
ATOM   1944 C  CB    . PHE A 1 240 ? -6.19998  -3.51694  22.85143  1.000 17.91203  ? 240  PHE A CB    1 
ATOM   1945 C  CG    . PHE A 1 240 ? -5.26049  -3.91787  21.74923  1.000 18.31749  ? 240  PHE A CG    1 
ATOM   1946 C  CD1   . PHE A 1 240 ? -5.67807  -3.90182  20.42664  1.000 18.31263  ? 240  PHE A CD1   1 
ATOM   1947 C  CD2   . PHE A 1 240 ? -3.97404  -4.34225  22.03462  1.000 18.74866  ? 240  PHE A CD2   1 
ATOM   1948 C  CE1   . PHE A 1 240 ? -4.82255  -4.28147  19.40856  1.000 19.04558  ? 240  PHE A CE1   1 
ATOM   1949 C  CE2   . PHE A 1 240 ? -3.11478  -4.72653  21.02105  1.000 19.19318  ? 240  PHE A CE2   1 
ATOM   1950 C  CZ    . PHE A 1 240 ? -3.53907  -4.69512  19.70630  1.000 19.00257  ? 240  PHE A CZ    1 
ATOM   1951 N  N     . ILE A 1 241 ? -5.99862  -6.33920  24.07547  1.000 23.16068  ? 241  ILE A N     1 
ATOM   1952 C  CA    . ILE A 1 241 ? -5.31429  -7.63109  24.06608  1.000 24.09880  ? 241  ILE A CA    1 
ATOM   1953 C  C     . ILE A 1 241 ? -6.31488  -8.76639  23.89136  1.000 24.71431  ? 241  ILE A C     1 
ATOM   1954 O  O     . ILE A 1 241 ? -6.10799  -9.68298  23.08768  1.000 25.28754  ? 241  ILE A O     1 
ATOM   1955 C  CB    . ILE A 1 241 ? -4.48481  -7.81082  25.35156  1.000 24.68823  ? 241  ILE A CB    1 
ATOM   1956 C  CG1   . ILE A 1 241 ? -3.38817  -6.74706  25.44752  1.000 23.53520  ? 241  ILE A CG1   1 
ATOM   1957 C  CG2   . ILE A 1 241 ? -3.88232  -9.20662  25.40694  1.000 24.61573  ? 241  ILE A CG2   1 
ATOM   1958 C  CD1   . ILE A 1 241 ? -2.32963  -6.85918  24.37549  1.000 24.52666  ? 241  ILE A CD1   1 
ATOM   1959 N  N     . ALA A 1 242 ? -7.42238  -8.71464  24.63126  1.000 27.32371  ? 242  ALA A N     1 
ATOM   1960 C  CA    . ALA A 1 242 ? -8.35985  -9.83121  24.63426  1.000 27.92992  ? 242  ALA A CA    1 
ATOM   1961 C  C     . ALA A 1 242 ? -9.26033  -9.83100  23.40414  1.000 28.16152  ? 242  ALA A C     1 
ATOM   1962 O  O     . ALA A 1 242 ? -9.56741  -10.89825 22.86107  1.000 28.73074  ? 242  ALA A O     1 
ATOM   1963 C  CB    . ALA A 1 242 ? -9.20567  -9.80113  25.90806  1.000 27.01976  ? 242  ALA A CB    1 
ATOM   1964 N  N     . ASP A 1 243 ? -9.68847  -8.65318  22.94366  1.000 35.58966  ? 243  ASP A N     1 
ATOM   1965 C  CA    . ASP A 1 243 ? -10.75111 -8.57001  21.95171  1.000 35.85282  ? 243  ASP A CA    1 
ATOM   1966 C  C     . ASP A 1 243 ? -10.30370 -8.11779  20.56839  1.000 35.74780  ? 243  ASP A C     1 
ATOM   1967 O  O     . ASP A 1 243 ? -11.01699 -8.38634  19.59725  1.000 35.55291  ? 243  ASP A O     1 
ATOM   1968 C  CB    . ASP A 1 243 ? -11.85709 -7.62217  22.44016  1.000 35.16161  ? 243  ASP A CB    1 
ATOM   1969 C  CG    . ASP A 1 243 ? -12.52031 -8.10856  23.71544  1.000 35.72238  ? 243  ASP A CG    1 
ATOM   1970 O  OD1   . ASP A 1 243 ? -12.34508 -9.29489  24.06405  1.000 36.84376  ? 243  ASP A OD1   1 
ATOM   1971 O  OD2   . ASP A 1 243 ? -13.21354 -7.30313  24.37221  1.000 36.37335  ? 243  ASP A OD2   1 
ATOM   1972 N  N     . MET A 1 244 ? -9.16302  -7.44276  20.44324  1.000 25.94017  ? 244  MET A N     1 
ATOM   1973 C  CA    . MET A 1 244 ? -8.74972  -6.90505  19.15293  1.000 25.58445  ? 244  MET A CA    1 
ATOM   1974 C  C     . MET A 1 244 ? -7.41337  -7.42642  18.65080  1.000 26.52517  ? 244  MET A C     1 
ATOM   1975 O  O     . MET A 1 244 ? -7.23585  -7.53491  17.43517  1.000 27.01920  ? 244  MET A O     1 
ATOM   1976 C  CB    . MET A 1 244 ? -8.69376  -5.37129  19.20587  1.000 25.02449  ? 244  MET A CB    1 
ATOM   1977 C  CG    . MET A 1 244 ? -9.85039  -4.76178  19.96446  1.000 24.78388  ? 244  MET A CG    1 
ATOM   1978 S  SD    . MET A 1 244 ? -11.23570 -4.44088  18.86086  1.000 25.38137  ? 244  MET A SD    1 
ATOM   1979 C  CE    . MET A 1 244 ? -12.61257 -4.89525  19.91283  1.000 23.96582  ? 244  MET A CE    1 
ATOM   1980 N  N     . LEU A 1 245 ? -6.47725  -7.74872  19.53979  1.000 20.58608  ? 245  LEU A N     1 
ATOM   1981 C  CA    . LEU A 1 245 ? -5.17946  -8.26423  19.10990  1.000 21.32925  ? 245  LEU A CA    1 
ATOM   1982 C  C     . LEU A 1 245 ? -5.25985  -9.45329  18.15332  1.000 22.10899  ? 245  LEU A C     1 
ATOM   1983 O  O     . LEU A 1 245 ? -4.45780  -9.49202  17.20452  1.000 22.21111  ? 245  LEU A O     1 
ATOM   1984 C  CB    . LEU A 1 245 ? -4.33792  -8.62633  20.34257  1.000 21.31527  ? 245  LEU A CB    1 
ATOM   1985 C  CG    . LEU A 1 245 ? -2.93596  -9.16976  20.05630  1.000 22.54772  ? 245  LEU A CG    1 
ATOM   1986 C  CD1   . LEU A 1 245 ? -2.13907  -8.18498  19.20963  1.000 21.18102  ? 245  LEU A CD1   1 
ATOM   1987 C  CD2   . LEU A 1 245 ? -2.20810  -9.48890  21.35194  1.000 21.71481  ? 245  LEU A CD2   1 
ATOM   1988 N  N     . PRO A 1 246 ? -6.15693  -10.43438 18.32259  1.000 23.86195  ? 246  PRO A N     1 
ATOM   1989 C  CA    . PRO A 1 246 ? -6.20310  -11.54467 17.35326  1.000 24.65245  ? 246  PRO A CA    1 
ATOM   1990 C  C     . PRO A 1 246 ? -6.48387  -11.11247 15.92268  1.000 24.39494  ? 246  PRO A C     1 
ATOM   1991 O  O     . PRO A 1 246 ? -6.15125  -11.85940 14.99386  1.000 24.76422  ? 246  PRO A O     1 
ATOM   1992 C  CB    . PRO A 1 246 ? -7.32710  -12.43668 17.89652  1.000 24.03498  ? 246  PRO A CB    1 
ATOM   1993 C  CG    . PRO A 1 246 ? -7.32781  -12.17143 19.35353  1.000 23.80549  ? 246  PRO A CG    1 
ATOM   1994 C  CD    . PRO A 1 246 ? -7.02522  -10.70716 19.48462  1.000 23.40929  ? 246  PRO A CD    1 
ATOM   1995 N  N     . SER A 1 247 ? -7.07346  -9.93628  15.71000  1.000 27.50962  ? 247  SER A N     1 
ATOM   1996 C  CA    . SER A 1 247 ? -7.39512  -9.45407  14.37323  1.000 27.88486  ? 247  SER A CA    1 
ATOM   1997 C  C     . SER A 1 247 ? -6.45736  -8.34984  13.90233  1.000 27.79840  ? 247  SER A C     1 
ATOM   1998 O  O     . SER A 1 247 ? -6.69717  -7.76160  12.84284  1.000 28.02687  ? 247  SER A O     1 
ATOM   1999 C  CB    . SER A 1 247 ? -8.84156  -8.95655  14.32580  1.000 27.51669  ? 247  SER A CB    1 
ATOM   2000 O  OG    . SER A 1 247 ? -9.75970  -10.03036 14.40568  1.000 28.04414  ? 247  SER A OG    1 
ATOM   2001 N  N     . PHE A 1 248 ? -5.39305  -8.06128  14.65774  1.000 28.33780  ? 248  PHE A N     1 
ATOM   2002 C  CA    . PHE A 1 248 ? -4.54548  -6.91072  14.35211  1.000 27.77070  ? 248  PHE A CA    1 
ATOM   2003 C  C     . PHE A 1 248 ? -3.89863  -7.03080  12.97738  1.000 28.39603  ? 248  PHE A C     1 
ATOM   2004 O  O     . PHE A 1 248 ? -3.84950  -6.05456  12.21984  1.000 28.33052  ? 248  PHE A O     1 
ATOM   2005 C  CB    . PHE A 1 248 ? -3.47113  -6.75147  15.42738  1.000 27.92886  ? 248  PHE A CB    1 
ATOM   2006 C  CG    . PHE A 1 248 ? -2.76496  -5.42524  15.38773  1.000 27.53878  ? 248  PHE A CG    1 
ATOM   2007 C  CD1   . PHE A 1 248 ? -3.40591  -4.26923  15.80312  1.000 26.77273  ? 248  PHE A CD1   1 
ATOM   2008 C  CD2   . PHE A 1 248 ? -1.46061  -5.33435  14.92984  1.000 27.92067  ? 248  PHE A CD2   1 
ATOM   2009 C  CE1   . PHE A 1 248 ? -2.75629  -3.04759  15.76690  1.000 26.08241  ? 248  PHE A CE1   1 
ATOM   2010 C  CE2   . PHE A 1 248 ? -0.80680  -4.11560  14.88973  1.000 27.76433  ? 248  PHE A CE2   1 
ATOM   2011 C  CZ    . PHE A 1 248 ? -1.45579  -2.97162  15.30942  1.000 26.65272  ? 248  PHE A CZ    1 
ATOM   2012 N  N     . GLY A 1 249 ? -3.39202  -8.21467  12.63803  1.000 41.59275  ? 249  GLY A N     1 
ATOM   2013 C  CA    . GLY A 1 249 ? -2.67696  -8.37984  11.38535  1.000 42.04905  ? 249  GLY A CA    1 
ATOM   2014 C  C     . GLY A 1 249 ? -3.55000  -8.38318  10.14765  1.000 42.07080  ? 249  GLY A C     1 
ATOM   2015 O  O     . GLY A 1 249 ? -3.01042  -8.36189  9.03630   1.000 42.59996  ? 249  GLY A O     1 
ATOM   2016 N  N     . ASP A 1 250 ? -4.87280  -8.40179  10.30670  1.000 33.44080  ? 250  ASP A N     1 
ATOM   2017 C  CA    . ASP A 1 250 ? -5.77073  -8.50824  9.16320   1.000 33.09790  ? 250  ASP A CA    1 
ATOM   2018 C  C     . ASP A 1 250 ? -6.10581  -7.15653  8.54337   1.000 33.54535  ? 250  ASP A C     1 
ATOM   2019 O  O     . ASP A 1 250 ? -6.12313  -7.03054  7.31422   1.000 33.45106  ? 250  ASP A O     1 
ATOM   2020 C  CB    . ASP A 1 250 ? -7.06453  -9.21932  9.57246   1.000 33.56550  ? 250  ASP A CB    1 
ATOM   2021 C  CG    . ASP A 1 250 ? -6.84419  -10.67971 9.92442   1.000 34.58829  ? 250  ASP A CG    1 
ATOM   2022 O  OD1   . ASP A 1 250 ? -5.88953  -11.28561 9.39299   1.000 35.59535  ? 250  ASP A OD1   1 
ATOM   2023 O  OD2   . ASP A 1 250 ? -7.63058  -11.22354 10.72903  1.000 34.49140  ? 250  ASP A OD2   1 
ATOM   2024 N  N     . TRP A 1 251 ? -6.36719  -6.14043  9.36177   1.000 32.04777  ? 251  TRP A N     1 
ATOM   2025 C  CA    . TRP A 1 251 ? -6.90195  -4.87040  8.88262   1.000 32.60007  ? 251  TRP A CA    1 
ATOM   2026 C  C     . TRP A 1 251 ? -6.04585  -3.70294  9.35146   1.000 32.23711  ? 251  TRP A C     1 
ATOM   2027 O  O     . TRP A 1 251 ? -6.55693  -2.63467  9.69964   1.000 32.11611  ? 251  TRP A O     1 
ATOM   2028 C  CB    . TRP A 1 251 ? -8.34840  -4.69308  9.33770   1.000 31.45511  ? 251  TRP A CB    1 
ATOM   2029 C  CG    . TRP A 1 251 ? -9.14991  -5.95957  9.27534   1.000 31.55537  ? 251  TRP A CG    1 
ATOM   2030 C  CD1   . TRP A 1 251 ? -9.67360  -6.65190  10.32979  1.000 31.43251  ? 251  TRP A CD1   1 
ATOM   2031 C  CD2   . TRP A 1 251 ? -9.51701  -6.68728  8.09722   1.000 32.15677  ? 251  TRP A CD2   1 
ATOM   2032 N  NE1   . TRP A 1 251 ? -10.34467 -7.76333  9.88080   1.000 31.64946  ? 251  TRP A NE1   1 
ATOM   2033 C  CE2   . TRP A 1 251 ? -10.26372 -7.80780  8.51401   1.000 32.12300  ? 251  TRP A CE2   1 
ATOM   2034 C  CE3   . TRP A 1 251 ? -9.28819  -6.49991  6.73059   1.000 32.44611  ? 251  TRP A CE3   1 
ATOM   2035 C  CZ2   . TRP A 1 251 ? -10.78152 -8.73557  7.61433   1.000 31.90833  ? 251  TRP A CZ2   1 
ATOM   2036 C  CZ3   . TRP A 1 251 ? -9.80525  -7.42146  5.83957   1.000 32.66644  ? 251  TRP A CZ3   1 
ATOM   2037 C  CH2   . TRP A 1 251 ? -10.54130 -8.52573  6.28486   1.000 32.77557  ? 251  TRP A CH2   1 
ATOM   2038 N  N     . GLN A 1 252 ? -4.72362  -3.88372  9.35704   1.000 47.56965  ? 252  GLN A N     1 
ATOM   2039 C  CA    . GLN A 1 252 ? -3.83889  -2.83097  9.84583   1.000 47.85375  ? 252  GLN A CA    1 
ATOM   2040 C  C     . GLN A 1 252 ? -3.79043  -1.63827  8.89764   1.000 46.96671  ? 252  GLN A C     1 
ATOM   2041 O  O     . GLN A 1 252 ? -3.49908  -0.51769  9.33143   1.000 45.84373  ? 252  GLN A O     1 
ATOM   2042 C  CB    . GLN A 1 252 ? -2.43400  -3.39014  10.06611  1.000 48.04985  ? 252  GLN A CB    1 
ATOM   2043 C  CG    . GLN A 1 252 ? -1.75073  -2.86872  11.31672  1.000 47.74925  ? 252  GLN A CG    1 
ATOM   2044 C  CD    . GLN A 1 252 ? -0.27658  -3.21573  11.35949  1.000 49.44800  ? 252  GLN A CD    1 
ATOM   2045 O  OE1   . GLN A 1 252 ? 0.53508   -2.46182  11.89648  1.000 48.88828  ? 252  GLN A OE1   1 
ATOM   2046 N  NE2   . GLN A 1 252 ? 0.07750   -4.36539  10.79492  1.000 49.55748  ? 252  GLN A NE2   1 
ATOM   2047 N  N     . ASP A 1 253 ? -4.07265  -1.85207  7.61217   1.000 30.32246  ? 253  ASP A N     1 
ATOM   2048 C  CA    . ASP A 1 253 ? -3.99164  -0.80218  6.60403   1.000 30.38510  ? 253  ASP A CA    1 
ATOM   2049 C  C     . ASP A 1 253 ? -5.34487  -0.45910  5.99433   1.000 29.92885  ? 253  ASP A C     1 
ATOM   2050 O  O     . ASP A 1 253 ? -5.40184  0.32558   5.04167   1.000 29.74796  ? 253  ASP A O     1 
ATOM   2051 C  CB    . ASP A 1 253 ? -3.01631  -1.20647  5.49591   1.000 31.08984  ? 253  ASP A CB    1 
ATOM   2052 C  CG    . ASP A 1 253 ? -1.57539  -1.21008  5.95942   1.000 31.43762  ? 253  ASP A CG    1 
ATOM   2053 O  OD1   . ASP A 1 253 ? -1.33762  -1.02001  7.17029   1.000 31.24220  ? 253  ASP A OD1   1 
ATOM   2054 O  OD2   . ASP A 1 253 ? -0.68022  -1.40242  5.10981   1.000 31.79116  ? 253  ASP A OD2   1 
ATOM   2055 N  N     . ALA A 1 254 ? -6.43057  -1.02446  6.51123   1.000 23.89614  ? 254  ALA A N     1 
ATOM   2056 C  CA    . ALA A 1 254 ? -7.74618  -0.75500  5.95661   1.000 24.70702  ? 254  ALA A CA    1 
ATOM   2057 C  C     . ALA A 1 254 ? -8.30451  0.55879   6.49890   1.000 23.47156  ? 254  ALA A C     1 
ATOM   2058 O  O     . ALA A 1 254 ? -7.85679  1.08278   7.52240   1.000 22.99707  ? 254  ALA A O     1 
ATOM   2059 C  CB    . ALA A 1 254 ? -8.70604  -1.90329  6.26869   1.000 24.41392  ? 254  ALA A CB    1 
ATOM   2060 N  N     . MET A 1 255 ? -9.29042  1.09804   5.78293   1.000 22.88416  ? 255  MET A N     1 
ATOM   2061 C  CA    . MET A 1 255 ? -10.00940 2.29257   6.20957   1.000 22.08132  ? 255  MET A CA    1 
ATOM   2062 C  C     . MET A 1 255 ? -11.49305 2.08839   5.95432   1.000 22.46518  ? 255  MET A C     1 
ATOM   2063 O  O     . MET A 1 255 ? -11.88226 1.65333   4.86710   1.000 22.96039  ? 255  MET A O     1 
ATOM   2064 C  CB    . MET A 1 255 ? -9.52256  3.54843   5.47346   1.000 22.44752  ? 255  MET A CB    1 
ATOM   2065 C  CG    . MET A 1 255 ? -8.01659  3.71869   5.44025   1.000 22.25781  ? 255  MET A CG    1 
ATOM   2066 S  SD    . MET A 1 255 ? -7.47880  5.12512   4.44926   1.000 22.63928  ? 255  MET A SD    1 
ATOM   2067 C  CE    . MET A 1 255 ? -6.57860  4.28219   3.14915   1.000 22.61130  ? 255  MET A CE    1 
ATOM   2068 N  N     . SER A 1 256 ? -12.31629 2.40233   6.95098   1.000 26.48709  ? 256  SER A N     1 
ATOM   2069 C  CA    . SER A 1 256 ? -13.76230 2.28234   6.83128   1.000 26.74055  ? 256  SER A CA    1 
ATOM   2070 C  C     . SER A 1 256 ? -14.40125 3.61930   7.16984   1.000 26.44601  ? 256  SER A C     1 
ATOM   2071 O  O     . SER A 1 256 ? -14.03181 4.25436   8.16323   1.000 25.88098  ? 256  SER A O     1 
ATOM   2072 C  CB    . SER A 1 256 ? -14.31208 1.18153   7.74394   1.000 26.60092  ? 256  SER A CB    1 
ATOM   2073 O  OG    . SER A 1 256 ? -15.72362 1.10568   7.64134   1.000 27.21373  ? 256  SER A OG    1 
ATOM   2074 N  N     . TRP A 1 257 ? -15.35989 4.03245   6.34350   1.000 23.72904  ? 257  TRP A N     1 
ATOM   2075 C  CA    . TRP A 1 257 ? -16.00763 5.33039   6.48765   1.000 23.05161  ? 257  TRP A CA    1 
ATOM   2076 C  C     . TRP A 1 257 ? -16.66125 5.46740   7.85797   1.000 23.43455  ? 257  TRP A C     1 
ATOM   2077 O  O     . TRP A 1 257 ? -17.54816 4.68559   8.21640   1.000 23.19964  ? 257  TRP A O     1 
ATOM   2078 C  CB    . TRP A 1 257 ? -17.04064 5.50210   5.37482   1.000 23.32404  ? 257  TRP A CB    1 
ATOM   2079 C  CG    . TRP A 1 257 ? -17.81159 6.78463   5.41222   1.000 24.17766  ? 257  TRP A CG    1 
ATOM   2080 C  CD1   . TRP A 1 257 ? -17.37586 8.01760   5.01906   1.000 23.82773  ? 257  TRP A CD1   1 
ATOM   2081 C  CD2   . TRP A 1 257 ? -19.16982 6.95518   5.83477   1.000 24.02317  ? 257  TRP A CD2   1 
ATOM   2082 N  NE1   . TRP A 1 257 ? -18.37411 8.94773   5.18654   1.000 23.80013  ? 257  TRP A NE1   1 
ATOM   2083 C  CE2   . TRP A 1 257 ? -19.48647 8.32039   5.68321   1.000 23.73439  ? 257  TRP A CE2   1 
ATOM   2084 C  CE3   . TRP A 1 257 ? -20.14624 6.08734   6.33385   1.000 24.04370  ? 257  TRP A CE3   1 
ATOM   2085 C  CZ2   . TRP A 1 257 ? -20.73742 8.83755   6.01386   1.000 24.12170  ? 257  TRP A CZ2   1 
ATOM   2086 C  CZ3   . TRP A 1 257 ? -21.38838 6.60302   6.66158   1.000 24.42339  ? 257  TRP A CZ3   1 
ATOM   2087 C  CH2   . TRP A 1 257 ? -21.67242 7.96542   6.50020   1.000 24.75338  ? 257  TRP A CH2   1 
ATOM   2088 N  N     . ARG A 1 258 ? -16.20534 6.45858   8.62468   1.000 27.42732  ? 258  ARG A N     1 
ATOM   2089 C  CA    . ARG A 1 258 ? -16.75275 6.80467   9.93626   1.000 27.35921  ? 258  ARG A CA    1 
ATOM   2090 C  C     . ARG A 1 258 ? -16.63645 5.66812   10.94885  1.000 27.45679  ? 258  ARG A C     1 
ATOM   2091 O  O     . ARG A 1 258 ? -17.40190 5.61429   11.91621  1.000 27.51581  ? 258  ARG A O     1 
ATOM   2092 C  CB    . ARG A 1 258 ? -18.20683 7.27507   9.82157   1.000 27.63636  ? 258  ARG A CB    1 
ATOM   2093 C  CG    . ARG A 1 258 ? -18.37681 8.42928   8.85241   1.000 27.89699  ? 258  ARG A CG    1 
ATOM   2094 C  CD    . ARG A 1 258 ? -19.26652 9.52533   9.41123   1.000 27.97831  ? 258  ARG A CD    1 
ATOM   2095 N  NE    . ARG A 1 258 ? -19.27069 10.69776  8.54346   1.000 28.88667  ? 258  ARG A NE    1 
ATOM   2096 C  CZ    . ARG A 1 258 ? -20.36423 11.31836  8.12264   1.000 29.34733  ? 258  ARG A CZ    1 
ATOM   2097 N  NH1   . ARG A 1 258 ? -21.57110 10.90651  8.47328   1.000 30.23171  ? 258  ARG A NH1   1 
ATOM   2098 N  NH2   . ARG A 1 258 ? -20.24390 12.37481  7.32383   1.000 29.85746  ? 258  ARG A NH2   1 
ATOM   2099 N  N     . ARG A 1 259 ? -15.68469 4.75422   10.74896  1.000 34.30070  ? 259  ARG A N     1 
ATOM   2100 C  CA    . ARG A 1 259 ? -15.28104 3.77729   11.75833  1.000 33.71124  ? 259  ARG A CA    1 
ATOM   2101 C  C     . ARG A 1 259 ? -13.82279 4.07850   12.08232  1.000 33.85514  ? 259  ARG A C     1 
ATOM   2102 O  O     . ARG A 1 259 ? -12.90787 3.42145   11.56295  1.000 33.96928  ? 259  ARG A O     1 
ATOM   2103 C  CB    . ARG A 1 259 ? -15.47458 2.33900   11.27962  1.000 34.67485  ? 259  ARG A CB    1 
ATOM   2104 C  CG    . ARG A 1 259 ? -16.89108 2.00901   10.81178  1.000 34.96060  ? 259  ARG A CG    1 
ATOM   2105 C  CD    . ARG A 1 259 ? -17.95352 2.28964   11.87968  1.000 35.33646  ? 259  ARG A CD    1 
ATOM   2106 N  NE    . ARG A 1 259 ? -17.50836 1.98859   13.23730  1.000 35.16868  ? 259  ARG A NE    1 
ATOM   2107 C  CZ    . ARG A 1 259 ? -17.95933 0.97960   13.97111  1.000 35.13820  ? 259  ARG A CZ    1 
ATOM   2108 N  NH1   . ARG A 1 259 ? -18.86931 0.13873   13.50680  1.000 35.66258  ? 259  ARG A NH1   1 
ATOM   2109 N  NH2   . ARG A 1 259 ? -17.48573 0.81016   15.20260  1.000 35.05457  ? 259  ARG A NH2   1 
ATOM   2110 N  N     . PRO A 1 260 ? -13.56786 5.07195   12.93834  1.000 25.85694  ? 260  PRO A N     1 
ATOM   2111 C  CA    . PRO A 1 260 ? -12.20949 5.62519   13.04541  1.000 26.25196  ? 260  PRO A CA    1 
ATOM   2112 C  C     . PRO A 1 260 ? -11.22900 4.75213   13.80988  1.000 26.18031  ? 260  PRO A C     1 
ATOM   2113 O  O     . PRO A 1 260 ? -10.02418 5.03178   13.76064  1.000 25.82343  ? 260  PRO A O     1 
ATOM   2114 C  CB    . PRO A 1 260 ? -12.43804 6.95673   13.76999  1.000 25.67189  ? 260  PRO A CB    1 
ATOM   2115 C  CG    . PRO A 1 260 ? -13.64533 6.70280   14.60876  1.000 26.07986  ? 260  PRO A CG    1 
ATOM   2116 C  CD    . PRO A 1 260 ? -14.52887 5.79578   13.78986  1.000 25.95756  ? 260  PRO A CD    1 
ATOM   2117 N  N     . PHE A 1 261 ? -11.68543 3.71275   14.50255  1.000 24.68326  ? 261  PHE A N     1 
ATOM   2118 C  CA    . PHE A 1 261 ? -10.81622 2.93563   15.37896  1.000 24.62258  ? 261  PHE A CA    1 
ATOM   2119 C  C     . PHE A 1 261 ? -10.46234 1.56051   14.83629  1.000 24.97825  ? 261  PHE A C     1 
ATOM   2120 O  O     . PHE A 1 261 ? -9.32675  1.11408   15.01481  1.000 25.19493  ? 261  PHE A O     1 
ATOM   2121 C  CB    . PHE A 1 261 ? -11.46528 2.78993   16.75929  1.000 24.58813  ? 261  PHE A CB    1 
ATOM   2122 C  CG    . PHE A 1 261 ? -11.76068 4.10481   17.42696  1.000 24.18150  ? 261  PHE A CG    1 
ATOM   2123 C  CD1   . PHE A 1 261 ? -10.89158 5.17674   17.28961  1.000 24.51905  ? 261  PHE A CD1   1 
ATOM   2124 C  CD2   . PHE A 1 261 ? -12.90797 4.27257   18.18444  1.000 24.50025  ? 261  PHE A CD2   1 
ATOM   2125 C  CE1   . PHE A 1 261 ? -11.15949 6.39019   17.89886  1.000 24.32225  ? 261  PHE A CE1   1 
ATOM   2126 C  CE2   . PHE A 1 261 ? -13.18180 5.48510   18.79628  1.000 24.67862  ? 261  PHE A CE2   1 
ATOM   2127 C  CZ    . PHE A 1 261 ? -12.30590 6.54351   18.65337  1.000 24.38209  ? 261  PHE A CZ    1 
ATOM   2128 N  N     . LEU A 1 262 ? -11.39965 0.88163   14.17256  1.000 18.01303  ? 262  LEU A N     1 
ATOM   2129 C  CA    . LEU A 1 262 ? -11.18726 -0.45488  13.59090  1.000 18.33592  ? 262  LEU A CA    1 
ATOM   2130 C  C     . LEU A 1 262 ? -10.66349 -1.37266  14.69734  1.000 18.35372  ? 262  LEU A C     1 
ATOM   2131 O  O     . LEU A 1 262 ? -11.30313 -1.46923  15.75390  1.000 18.49559  ? 262  LEU A O     1 
ATOM   2132 C  CB    . LEU A 1 262 ? -10.30095 -0.33537  12.35713  1.000 18.50151  ? 262  LEU A CB    1 
ATOM   2133 C  CG    . LEU A 1 262 ? -10.84399 0.53868   11.22238  1.000 18.53349  ? 262  LEU A CG    1 
ATOM   2134 C  CD1   . LEU A 1 262 ? -9.91996  0.50420   10.01424  1.000 18.34255  ? 262  LEU A CD1   1 
ATOM   2135 C  CD2   . LEU A 1 262 ? -12.24644 0.10503   10.83645  1.000 18.02883  ? 262  LEU A CD2   1 
ATOM   2136 N  N     . TRP A 1 263 ? -9.52410  -2.04349  14.51298  1.000 21.00318  ? 263  TRP A N     1 
ATOM   2137 C  CA    . TRP A 1 263 ? -8.98751  -2.97206  15.50151  1.000 21.25818  ? 263  TRP A CA    1 
ATOM   2138 C  C     . TRP A 1 263 ? -7.70816  -2.45690  16.15328  1.000 21.34331  ? 263  TRP A C     1 
ATOM   2139 O  O     . TRP A 1 263 ? -6.96151  -3.23947  16.74994  1.000 21.76437  ? 263  TRP A O     1 
ATOM   2140 C  CB    . TRP A 1 263 ? -8.73597  -4.33842  14.86287  1.000 22.24175  ? 263  TRP A CB    1 
ATOM   2141 C  CG    . TRP A 1 263 ? -9.98217  -5.13766  14.62341  1.000 22.03211  ? 263  TRP A CG    1 
ATOM   2142 C  CD1   . TRP A 1 263 ? -10.49748 -6.11209  15.42730  1.000 22.30529  ? 263  TRP A CD1   1 
ATOM   2143 C  CD2   . TRP A 1 263 ? -10.86550 -5.03638  13.49975  1.000 21.91985  ? 263  TRP A CD2   1 
ATOM   2144 N  NE1   . TRP A 1 263 ? -11.64686 -6.62216  14.87596  1.000 22.23767  ? 263  TRP A NE1   1 
ATOM   2145 C  CE2   . TRP A 1 263 ? -11.89508 -5.97880  13.69230  1.000 22.45912  ? 263  TRP A CE2   1 
ATOM   2146 C  CE3   . TRP A 1 263 ? -10.88652 -4.23921  12.35039  1.000 22.14395  ? 263  TRP A CE3   1 
ATOM   2147 C  CZ2   . TRP A 1 263 ? -12.93475 -6.14663  12.77905  1.000 22.46612  ? 263  TRP A CZ2   1 
ATOM   2148 C  CZ3   . TRP A 1 263 ? -11.91967 -4.40700  11.44467  1.000 21.92937  ? 263  TRP A CZ3   1 
ATOM   2149 C  CH2   . TRP A 1 263 ? -12.92999 -5.35260  11.66484  1.000 22.71103  ? 263  TRP A CH2   1 
ATOM   2150 N  N     . HIS A 1 264 ? -7.43862  -1.15989  16.05277  1.000 19.52574  ? 264  HIS A N     1 
ATOM   2151 C  CA    . HIS A 1 264 ? -6.22949  -0.60058  16.63229  1.000 19.21252  ? 264  HIS A CA    1 
ATOM   2152 C  C     . HIS A 1 264 ? -6.35146  -0.51254  18.15280  1.000 18.40108  ? 264  HIS A C     1 
ATOM   2153 O  O     . HIS A 1 264 ? -7.44584  -0.55535  18.72114  1.000 18.57048  ? 264  HIS A O     1 
ATOM   2154 C  CB    . HIS A 1 264 ? -5.93869  0.76998   16.02140  1.000 18.64850  ? 264  HIS A CB    1 
ATOM   2155 C  CG    . HIS A 1 264 ? -5.74539  0.73114   14.53681  1.000 19.23624  ? 264  HIS A CG    1 
ATOM   2156 N  ND1   . HIS A 1 264 ? -4.52119  0.48606   13.95198  1.000 19.50103  ? 264  HIS A ND1   1 
ATOM   2157 C  CD2   . HIS A 1 264 ? -6.62505  0.88209   13.51802  1.000 19.12548  ? 264  HIS A CD2   1 
ATOM   2158 C  CE1   . HIS A 1 264 ? -4.65261  0.49846   12.63722  1.000 19.63990  ? 264  HIS A CE1   1 
ATOM   2159 N  NE2   . HIS A 1 264 ? -5.91938  0.73696   12.34773  1.000 19.72291  ? 264  HIS A NE2   1 
ATOM   2160 N  N     . SER A 1 265 ? -5.19736  -0.39599  18.81369  1.000 19.56741  ? 265  SER A N     1 
ATOM   2161 C  CA    . SER A 1 265 ? -5.16332  -0.46682  20.27142  1.000 19.64791  ? 265  SER A CA    1 
ATOM   2162 C  C     . SER A 1 265 ? -5.63261  0.82234   20.93177  1.000 18.77471  ? 265  SER A C     1 
ATOM   2163 O  O     . SER A 1 265 ? -6.18615  0.77637   22.03609  1.000 18.61198  ? 265  SER A O     1 
ATOM   2164 C  CB    . SER A 1 265 ? -3.75102  -0.81078  20.74706  1.000 19.76668  ? 265  SER A CB    1 
ATOM   2165 O  OG    . SER A 1 265 ? -2.82611  0.18956   20.35884  1.000 19.24107  ? 265  SER A OG    1 
ATOM   2166 N  N     . LEU A 1 266 ? -5.42239  1.96747   20.27995  1.000 20.21847  ? 266  LEU A N     1 
ATOM   2167 C  CA    . LEU A 1 266 ? -5.78023  3.27720   20.82756  1.000 20.16231  ? 266  LEU A CA    1 
ATOM   2168 C  C     . LEU A 1 266 ? -5.03782  3.56663   22.12965  1.000 19.80473  ? 266  LEU A C     1 
ATOM   2169 O  O     . LEU A 1 266 ? -5.56179  4.24199   23.01776  1.000 20.14533  ? 266  LEU A O     1 
ATOM   2170 C  CB    . LEU A 1 266 ? -7.29411  3.40814   21.04045  1.000 20.30216  ? 266  LEU A CB    1 
ATOM   2171 C  CG    . LEU A 1 266 ? -8.24387  2.85668   19.97169  1.000 20.60921  ? 266  LEU A CG    1 
ATOM   2172 C  CD1   . LEU A 1 266 ? -9.67997  3.24814   20.28858  1.000 20.59456  ? 266  LEU A CD1   1 
ATOM   2173 C  CD2   . LEU A 1 266 ? -7.85510  3.33137   18.57959  1.000 20.31807  ? 266  LEU A CD2   1 
ATOM   2174 N  N     . ILE A 1 267 ? -3.80607  3.06662   22.25497  1.000 17.98136  ? 267  ILE A N     1 
ATOM   2175 C  CA    . ILE A 1 267 ? -3.03571  3.23781   23.48415  1.000 18.25532  ? 267  ILE A CA    1 
ATOM   2176 C  C     . ILE A 1 267 ? -1.98610  4.33442   23.38398  1.000 17.99864  ? 267  ILE A C     1 
ATOM   2177 O  O     . ILE A 1 267 ? -1.36867  4.67405   24.40677  1.000 18.64084  ? 267  ILE A O     1 
ATOM   2178 C  CB    . ILE A 1 267 ? -2.35064  1.92020   23.90672  1.000 18.61085  ? 267  ILE A CB    1 
ATOM   2179 C  CG1   . ILE A 1 267 ? -1.29248  1.51617   22.87894  1.000 18.95829  ? 267  ILE A CG1   1 
ATOM   2180 C  CG2   . ILE A 1 267 ? -3.37859  0.81367   24.08592  1.000 18.82351  ? 267  ILE A CG2   1 
ATOM   2181 C  CD1   . ILE A 1 267 ? -0.50109  0.29042   23.27067  1.000 19.10339  ? 267  ILE A CD1   1 
ATOM   2182 N  N     . SER A 1 268 ? -1.76148  4.89913   22.19850  1.000 14.93396  ? 268  SER A N     1 
ATOM   2183 C  CA    . SER A 1 268 ? -0.67511  5.86374   22.04408  1.000 14.90313  ? 268  SER A CA    1 
ATOM   2184 C  C     . SER A 1 268 ? -0.80941  7.09495   22.93625  1.000 15.22441  ? 268  SER A C     1 
ATOM   2185 O  O     . SER A 1 268 ? 0.21850   7.52940   23.48439  1.000 15.52486  ? 268  SER A O     1 
ATOM   2186 C  CB    . SER A 1 268 ? -0.53789  6.26978   20.56991  1.000 15.00573  ? 268  SER A CB    1 
ATOM   2187 O  OG    . SER A 1 268 ? -1.75676  6.75254   20.03796  1.000 14.98969  ? 268  SER A OG    1 
ATOM   2188 N  N     . PRO A 1 269 ? -1.98867  7.69909   23.13367  1.000 18.84087  ? 269  PRO A N     1 
ATOM   2189 C  CA    . PRO A 1 269 ? -2.04466  8.85961   24.03815  1.000 19.26748  ? 269  PRO A CA    1 
ATOM   2190 C  C     . PRO A 1 269 ? -1.70646  8.51718   25.47965  1.000 18.70014  ? 269  PRO A C     1 
ATOM   2191 O  O     . PRO A 1 269 ? -1.11207  9.34594   26.18108  1.000 18.82621  ? 269  PRO A O     1 
ATOM   2192 C  CB    . PRO A 1 269 ? -3.49460  9.34443   23.89183  1.000 18.93506  ? 269  PRO A CB    1 
ATOM   2193 C  CG    . PRO A 1 269 ? -3.94134  8.80804   22.57458  1.000 18.78819  ? 269  PRO A CG    1 
ATOM   2194 C  CD    . PRO A 1 269 ? -3.30280  7.46191   22.50987  1.000 18.51124  ? 269  PRO A CD    1 
ATOM   2195 N  N     . ALA A 1 270 ? -2.06205  7.31781   25.94290  1.000 17.82938  ? 270  ALA A N     1 
ATOM   2196 C  CA    . ALA A 1 270 ? -1.72088  6.91133   27.30214  1.000 17.85040  ? 270  ALA A CA    1 
ATOM   2197 C  C     . ALA A 1 270 ? -0.28171  6.42225   27.39358  1.000 17.94392  ? 270  ALA A C     1 
ATOM   2198 O  O     . ALA A 1 270 ? 0.39034   6.64571   28.40627  1.000 17.68185  ? 270  ALA A O     1 
ATOM   2199 C  CB    . ALA A 1 270 ? -2.68065  5.82388   27.78482  1.000 17.23162  ? 270  ALA A CB    1 
ATOM   2200 N  N     . LEU A 1 271 ? 0.20449   5.74665   26.35133  1.000 16.81111  ? 271  LEU A N     1 
ATOM   2201 C  CA    . LEU A 1 271 ? 1.58720   5.28397   26.35836  1.000 16.97948  ? 271  LEU A CA    1 
ATOM   2202 C  C     . LEU A 1 271 ? 2.56140   6.45588   26.33103  1.000 16.90816  ? 271  LEU A C     1 
ATOM   2203 O  O     . LEU A 1 271 ? 3.58957   6.43518   27.01912  1.000 16.65480  ? 271  LEU A O     1 
ATOM   2204 C  CB    . LEU A 1 271 ? 1.83027   4.35329   25.17087  1.000 17.13490  ? 271  LEU A CB    1 
ATOM   2205 C  CG    . LEU A 1 271 ? 3.24117   3.78319   25.02607  1.000 17.20264  ? 271  LEU A CG    1 
ATOM   2206 C  CD1   . LEU A 1 271 ? 3.68735   3.11245   26.31854  1.000 17.13802  ? 271  LEU A CD1   1 
ATOM   2207 C  CD2   . LEU A 1 271 ? 3.30322   2.81099   23.85529  1.000 17.67812  ? 271  LEU A CD2   1 
ATOM   2208 N  N     . ASN A 1 272 ? 2.24453   7.49586   25.56060  1.000 17.88133  ? 272  ASN A N     1 
ATOM   2209 C  CA    . ASN A 1 272 ? 3.18250   8.59163   25.36298  1.000 18.31979  ? 272  ASN A CA    1 
ATOM   2210 C  C     . ASN A 1 272 ? 3.31782   9.49704   26.58162  1.000 17.91410  ? 272  ASN A C     1 
ATOM   2211 O  O     . ASN A 1 272 ? 4.25719   10.29830  26.62623  1.000 18.92132  ? 272  ASN A O     1 
ATOM   2212 C  CB    . ASN A 1 272 ? 2.76868   9.40621   24.13572  1.000 17.93367  ? 272  ASN A CB    1 
ATOM   2213 C  CG    . ASN A 1 272 ? 3.08401   8.68959   22.83703  1.000 18.59704  ? 272  ASN A CG    1 
ATOM   2214 O  OD1   . ASN A 1 272 ? 3.76692   7.66309   22.83461  1.000 18.51583  ? 272  ASN A OD1   1 
ATOM   2215 N  ND2   . ASN A 1 272 ? 2.58947   9.22333   21.72652  1.000 18.03577  ? 272  ASN A ND2   1 
ATOM   2216 N  N     . ILE A 1 273 ? 2.42847   9.39229   27.56828  1.000 20.07905  ? 273  ILE A N     1 
ATOM   2217 C  CA    . ILE A 1 273 ? 2.56645   10.14876  28.80736  1.000 20.01708  ? 273  ILE A CA    1 
ATOM   2218 C  C     . ILE A 1 273 ? 2.91748   9.24988   29.98564  1.000 20.47800  ? 273  ILE A C     1 
ATOM   2219 O  O     . ILE A 1 273 ? 2.93572   9.71490   31.13051  1.000 20.65105  ? 273  ILE A O     1 
ATOM   2220 C  CB    . ILE A 1 273 ? 1.31219   10.98552  29.10969  1.000 19.92525  ? 273  ILE A CB    1 
ATOM   2221 C  CG1   . ILE A 1 273 ? 0.12403   10.09272  29.46682  1.000 20.64599  ? 273  ILE A CG1   1 
ATOM   2222 C  CG2   . ILE A 1 273 ? 0.97163   11.86718  27.93160  1.000 20.58202  ? 273  ILE A CG2   1 
ATOM   2223 C  CD1   . ILE A 1 273 ? -1.12027  10.87646  29.83221  1.000 20.29418  ? 273  ILE A CD1   1 
ATOM   2224 N  N     . GLY A 1 274 ? 3.19919   7.97373   29.73689  1.000 22.53235  ? 274  GLY A N     1 
ATOM   2225 C  CA    . GLY A 1 274 ? 3.70597   7.08901   30.76531  1.000 22.89152  ? 274  GLY A CA    1 
ATOM   2226 C  C     . GLY A 1 274 ? 2.67205   6.29701   31.53181  1.000 22.65645  ? 274  GLY A C     1 
ATOM   2227 O  O     . GLY A 1 274 ? 3.03284   5.63064   32.50982  1.000 23.13485  ? 274  GLY A O     1 
ATOM   2228 N  N     . LEU A 1 275 ? 1.40136   6.33943   31.12377  1.000 18.23710  ? 275  LEU A N     1 
ATOM   2229 C  CA    . LEU A 1 275 ? 0.36800   5.59503   31.83546  1.000 18.00756  ? 275  LEU A CA    1 
ATOM   2230 C  C     . LEU A 1 275 ? 0.46233   4.09516   31.58516  1.000 18.55711  ? 275  LEU A C     1 
ATOM   2231 O  O     . LEU A 1 275 ? -0.11877  3.31356   32.34553  1.000 18.48437  ? 275  LEU A O     1 
ATOM   2232 C  CB    . LEU A 1 275 ? -1.01488  6.11552   31.44022  1.000 17.93782  ? 275  LEU A CB    1 
ATOM   2233 C  CG    . LEU A 1 275 ? -1.34892  7.51558   31.96438  1.000 18.28830  ? 275  LEU A CG    1 
ATOM   2234 C  CD1   . LEU A 1 275 ? -2.76946  7.91180   31.59642  1.000 17.80011  ? 275  LEU A CD1   1 
ATOM   2235 C  CD2   . LEU A 1 275 ? -1.13964  7.59420   33.47283  1.000 17.85129  ? 275  LEU A CD2   1 
ATOM   2236 N  N     . LEU A 1 276 ? 1.17170   3.68373   30.53691  1.000 21.55733  ? 276  LEU A N     1 
ATOM   2237 C  CA    . LEU A 1 276 ? 1.47733   2.28797   30.27010  1.000 22.16609  ? 276  LEU A CA    1 
ATOM   2238 C  C     . LEU A 1 276 ? 2.96848   2.16740   29.99147  1.000 22.89484  ? 276  LEU A C     1 
ATOM   2239 O  O     . LEU A 1 276 ? 3.64522   3.15718   29.70054  1.000 22.08868  ? 276  LEU A O     1 
ATOM   2240 C  CB    . LEU A 1 276 ? 0.67338   1.74226   29.07997  1.000 22.28476  ? 276  LEU A CB    1 
ATOM   2241 C  CG    . LEU A 1 276 ? -0.85129  1.71768   29.20518  1.000 22.29499  ? 276  LEU A CG    1 
ATOM   2242 C  CD1   . LEU A 1 276 ? -1.49384  1.44530   27.85596  1.000 22.11493  ? 276  LEU A CD1   1 
ATOM   2243 C  CD2   . LEU A 1 276 ? -1.29758  0.68760   30.23157  1.000 22.00532  ? 276  LEU A CD2   1 
ATOM   2244 N  N     . ASP A 1 277 ? 3.47902   0.94006   30.07854  1.000 23.85204  ? 277  ASP A N     1 
ATOM   2245 C  CA    . ASP A 1 277 ? 4.90063   0.70065   29.87922  1.000 24.12543  ? 277  ASP A CA    1 
ATOM   2246 C  C     . ASP A 1 277 ? 5.13069   -0.07763  28.59355  1.000 24.62856  ? 277  ASP A C     1 
ATOM   2247 O  O     . ASP A 1 277 ? 4.42681   -1.06457  28.33856  1.000 24.85398  ? 277  ASP A O     1 
ATOM   2248 C  CB    . ASP A 1 277 ? 5.49213   -0.06562  31.06757  1.000 24.72965  ? 277  ASP A CB    1 
ATOM   2249 C  CG    . ASP A 1 277 ? 6.95250   -0.41599  30.86554  1.000 25.03804  ? 277  ASP A CG    1 
ATOM   2250 O  OD1   . ASP A 1 277 ? 7.81449   0.44156   31.15496  1.000 25.50725  ? 277  ASP A OD1   1 
ATOM   2251 O  OD2   . ASP A 1 277 ? 7.23973   -1.54719  30.42070  1.000 25.59066  ? 277  ASP A OD2   1 
ATOM   2252 N  N     . PRO A 1 278 ? 6.09870   0.33259   27.76674  1.000 20.18831  ? 278  PRO A N     1 
ATOM   2253 C  CA    . PRO A 1 278 ? 6.30130   -0.35322  26.47625  1.000 20.41302  ? 278  PRO A CA    1 
ATOM   2254 C  C     . PRO A 1 278 ? 6.64862   -1.82453  26.61124  1.000 20.82603  ? 278  PRO A C     1 
ATOM   2255 O  O     . PRO A 1 278 ? 6.11188   -2.65258  25.86444  1.000 21.54399  ? 278  PRO A O     1 
ATOM   2256 C  CB    . PRO A 1 278 ? 7.45158   0.43894   25.83526  1.000 20.10836  ? 278  PRO A CB    1 
ATOM   2257 C  CG    . PRO A 1 278 ? 7.45597   1.75944   26.52991  1.000 19.93962  ? 278  PRO A CG    1 
ATOM   2258 C  CD    . PRO A 1 278 ? 6.96744   1.51125   27.92136  1.000 19.92761  ? 278  PRO A CD    1 
ATOM   2259 N  N     . LEU A 1 279 ? 7.54221   -2.17620  27.53813  1.000 18.37975  ? 279  LEU A N     1 
ATOM   2260 C  CA    . LEU A 1 279 ? 7.93141   -3.57449  27.68372  1.000 18.77634  ? 279  LEU A CA    1 
ATOM   2261 C  C     . LEU A 1 279 ? 6.77018   -4.42145  28.18973  1.000 18.95456  ? 279  LEU A C     1 
ATOM   2262 O  O     . LEU A 1 279 ? 6.55834   -5.54140  27.70983  1.000 19.17172  ? 279  LEU A O     1 
ATOM   2263 C  CB    . LEU A 1 279 ? 9.13558   -3.69450  28.61893  1.000 19.02255  ? 279  LEU A CB    1 
ATOM   2264 C  CG    . LEU A 1 279 ? 9.78542   -5.08225  28.68253  1.000 20.15278  ? 279  LEU A CG    1 
ATOM   2265 C  CD1   . LEU A 1 279 ? 10.21832  -5.54591  27.29456  1.000 19.36498  ? 279  LEU A CD1   1 
ATOM   2266 C  CD2   . LEU A 1 279 ? 10.96398  -5.09614  29.64819  1.000 18.93438  ? 279  LEU A CD2   1 
ATOM   2267 N  N     . ASP A 1 280 ? 6.00436   -3.90273  29.15427  1.000 25.42401  ? 280  ASP A N     1 
ATOM   2268 C  CA    . ASP A 1 280 ? 4.86392   -4.65010  29.67625  1.000 25.56777  ? 280  ASP A CA    1 
ATOM   2269 C  C     . ASP A 1 280 ? 3.79195   -4.84072  28.61174  1.000 25.42006  ? 280  ASP A C     1 
ATOM   2270 O  O     . ASP A 1 280 ? 3.14628   -5.89371  28.55622  1.000 25.45401  ? 280  ASP A O     1 
ATOM   2271 C  CB    . ASP A 1 280 ? 4.28115   -3.94197  30.89954  1.000 24.25912  ? 280  ASP A CB    1 
ATOM   2272 C  CG    . ASP A 1 280 ? 2.97651   -4.56403  31.36622  1.000 25.35660  ? 280  ASP A CG    1 
ATOM   2273 O  OD1   . ASP A 1 280 ? 3.02332   -5.54584  32.13738  1.000 25.72160  ? 280  ASP A OD1   1 
ATOM   2274 O  OD2   . ASP A 1 280 ? 1.90193   -4.07027  30.96238  1.000 26.01884  ? 280  ASP A OD2   1 
ATOM   2275 N  N     . ILE A 1 281 ? 3.58277   -3.83059  27.76477  1.000 17.45082  ? 281  ILE A N     1 
ATOM   2276 C  CA    . ILE A 1 281 ? 2.60654   -3.95252  26.68516  1.000 17.28536  ? 281  ILE A CA    1 
ATOM   2277 C  C     . ILE A 1 281 ? 3.00532   -5.07975  25.74219  1.000 18.06883  ? 281  ILE A C     1 
ATOM   2278 O  O     . ILE A 1 281 ? 2.18651   -5.93195  25.37701  1.000 18.22234  ? 281  ILE A O     1 
ATOM   2279 C  CB    . ILE A 1 281 ? 2.46913   -2.61700  25.93271  1.000 16.76824  ? 281  ILE A CB    1 
ATOM   2280 C  CG1   . ILE A 1 281 ? 1.66851   -1.60768  26.75591  1.000 16.36724  ? 281  ILE A CG1   1 
ATOM   2281 C  CG2   . ILE A 1 281 ? 1.81263   -2.83482  24.58106  1.000 16.67699  ? 281  ILE A CG2   1 
ATOM   2282 C  CD1   . ILE A 1 281 ? 1.83136   -0.17892  26.27148  1.000 15.95977  ? 281  ILE A CD1   1 
ATOM   2283 N  N     . CYS A 1 282 ? 4.27826   -5.10558  25.34470  1.000 16.73344  ? 282  CYS A N     1 
ATOM   2284 C  CA    . CYS A 1 282 ? 4.73531   -6.10378  24.38505  1.000 17.71113  ? 282  CYS A CA    1 
ATOM   2285 C  C     . CYS A 1 282 ? 4.72929   -7.50193  24.98877  1.000 18.07265  ? 282  CYS A C     1 
ATOM   2286 O  O     . CYS A 1 282 ? 4.41614   -8.47899  24.29874  1.000 18.61271  ? 282  CYS A O     1 
ATOM   2287 C  CB    . CYS A 1 282 ? 6.12975   -5.73732  23.88284  1.000 17.61613  ? 282  CYS A CB    1 
ATOM   2288 S  SG    . CYS A 1 282 ? 6.13209   -4.32965  22.75379  1.000 17.82215  ? 282  CYS A SG    1 
ATOM   2289 N  N     . ARG A 1 283 ? 5.07162   -7.62018  26.27353  1.000 29.01865  ? 283  ARG A N     1 
ATOM   2290 C  CA    . ARG A 1 283 ? 5.08589   -8.93507  26.90505  1.000 29.51187  ? 283  ARG A CA    1 
ATOM   2291 C  C     . ARG A 1 283 ? 3.68018   -9.50942  26.99653  1.000 29.17152  ? 283  ARG A C     1 
ATOM   2292 O  O     . ARG A 1 283 ? 3.48309   -10.71819 26.82501  1.000 30.03004  ? 283  ARG A O     1 
ATOM   2293 C  CB    . ARG A 1 283 ? 5.72350   -8.84996  28.29108  1.000 28.66598  ? 283  ARG A CB    1 
ATOM   2294 C  CG    . ARG A 1 283 ? 7.22556   -9.05855  28.28339  1.000 29.60872  ? 283  ARG A CG    1 
ATOM   2295 C  CD    . ARG A 1 283 ? 7.87062   -8.55651  29.56144  1.000 29.66536  ? 283  ARG A CD    1 
ATOM   2296 N  NE    . ARG A 1 283 ? 9.25838   -8.99243  29.65896  1.000 30.62840  ? 283  ARG A NE    1 
ATOM   2297 C  CZ    . ARG A 1 283 ? 10.12602  -8.54372  30.55535  1.000 31.59634  ? 283  ARG A CZ    1 
ATOM   2298 N  NH1   . ARG A 1 283 ? 9.77120   -7.67025  31.48406  1.000 30.36122  ? 283  ARG A NH1   1 
ATOM   2299 N  NH2   . ARG A 1 283 ? 11.37777  -8.99374  30.52831  1.000 31.77000  ? 283  ARG A NH2   1 
ATOM   2300 N  N     . ARG A 1 284 ? 2.69073   -8.65377  27.25893  1.000 28.51774  ? 284  ARG A N     1 
ATOM   2301 C  CA    . ARG A 1 284 ? 1.30789   -9.11247  27.29674  1.000 28.61588  ? 284  ARG A CA    1 
ATOM   2302 C  C     . ARG A 1 284 ? 0.86010   -9.60794  25.92919  1.000 29.52959  ? 284  ARG A C     1 
ATOM   2303 O  O     . ARG A 1 284 ? 0.13812   -10.60676 25.82877  1.000 29.69586  ? 284  ARG A O     1 
ATOM   2304 C  CB    . ARG A 1 284 ? 0.39568   -7.98790  27.78466  1.000 28.13986  ? 284  ARG A CB    1 
ATOM   2305 C  CG    . ARG A 1 284 ? 0.53542   -7.66687  29.26333  1.000 28.56661  ? 284  ARG A CG    1 
ATOM   2306 C  CD    . ARG A 1 284 ? -0.65337  -6.86756  29.75680  1.000 28.12308  ? 284  ARG A CD    1 
ATOM   2307 N  NE    . ARG A 1 284 ? -1.89269  -7.61898  29.60753  1.000 29.26333  ? 284  ARG A NE    1 
ATOM   2308 C  CZ    . ARG A 1 284 ? -3.09046  -7.15989  29.93995  1.000 28.12039  ? 284  ARG A CZ    1 
ATOM   2309 N  NH1   . ARG A 1 284 ? -3.25066  -5.94407  30.43673  1.000 27.22797  ? 284  ARG A NH1   1 
ATOM   2310 N  NH2   . ARG A 1 284 ? -4.15500  -7.93744  29.76311  1.000 27.84973  ? 284  ARG A NH2   1 
ATOM   2311 N  N     . ALA A 1 285 ? 1.27883   -8.92117  24.86276  1.000 17.29414  ? 285  ALA A N     1 
ATOM   2312 C  CA    . ALA A 1 285 ? 0.94345   -9.37085  23.51573  1.000 17.87601  ? 285  ALA A CA    1 
ATOM   2313 C  C     . ALA A 1 285 ? 1.61792   -10.69960 23.20160  1.000 18.30839  ? 285  ALA A C     1 
ATOM   2314 O  O     . ALA A 1 285 ? 0.98480   -11.61609 22.66418  1.000 18.61791  ? 285  ALA A O     1 
ATOM   2315 C  CB    . ALA A 1 285 ? 1.33766   -8.30821  22.48955  1.000 17.50412  ? 285  ALA A CB    1 
ATOM   2316 N  N     . GLU A 1 286 ? 2.90612   -10.82326 23.53500  1.000 23.27142  ? 286  GLU A N     1 
ATOM   2317 C  CA    . GLU A 1 286 ? 3.60813   -12.08392 23.31556  1.000 24.29039  ? 286  GLU A CA    1 
ATOM   2318 C  C     . GLU A 1 286 ? 2.95668   -13.21819 24.09702  1.000 24.63001  ? 286  GLU A C     1 
ATOM   2319 O  O     . GLU A 1 286 ? 2.79463   -14.32794 23.57601  1.000 24.90440  ? 286  GLU A O     1 
ATOM   2320 C  CB    . GLU A 1 286 ? 5.08173   -11.94105 23.69969  1.000 23.77431  ? 286  GLU A CB    1 
ATOM   2321 C  CG    . GLU A 1 286 ? 5.75094   -13.25154 24.09314  1.000 25.21594  ? 286  GLU A CG    1 
ATOM   2322 C  CD    . GLU A 1 286 ? 7.26300   -13.18622 24.01591  1.000 25.44056  ? 286  GLU A CD    1 
ATOM   2323 O  OE1   . GLU A 1 286 ? 7.82522   -12.09017 24.21342  1.000 25.68758  ? 286  GLU A OE1   1 
ATOM   2324 O  OE2   . GLU A 1 286 ? 7.89133   -14.23293 23.75989  1.000 26.80858  ? 286  GLU A OE2   1 
ATOM   2325 N  N     . ALA A 1 287 ? 2.56308   -12.95404 25.34609  1.000 23.00108  ? 287  ALA A N     1 
ATOM   2326 C  CA    . ALA A 1 287 ? 1.89779   -13.97958 26.14237  1.000 23.60065  ? 287  ALA A CA    1 
ATOM   2327 C  C     . ALA A 1 287 ? 0.59517   -14.43211 25.49720  1.000 23.72321  ? 287  ALA A C     1 
ATOM   2328 O  O     . ALA A 1 287 ? 0.20822   -15.59790 25.63534  1.000 23.72116  ? 287  ALA A O     1 
ATOM   2329 C  CB    . ALA A 1 287 ? 1.64051   -13.46277 27.55806  1.000 22.39805  ? 287  ALA A CB    1 
ATOM   2330 N  N     . ALA A 1 288 ? -0.09070  -13.53073 24.78812  1.000 18.84845  ? 288  ALA A N     1 
ATOM   2331 C  CA    . ALA A 1 288 ? -1.30875  -13.91773 24.08404  1.000 18.52566  ? 288  ALA A CA    1 
ATOM   2332 C  C     . ALA A 1 288 ? -1.01439  -14.94805 23.00066  1.000 19.10378  ? 288  ALA A C     1 
ATOM   2333 O  O     . ALA A 1 288 ? -1.78330  -15.89786 22.81186  1.000 19.61526  ? 288  ALA A O     1 
ATOM   2334 C  CB    . ALA A 1 288 ? -1.98656  -12.68512 23.48682  1.000 18.01603  ? 288  ALA A CB    1 
ATOM   2335 N  N     . TRP A 1 289 ? 0.09729   -14.78138 22.27955  1.000 22.62794  ? 289  TRP A N     1 
ATOM   2336 C  CA    . TRP A 1 289 ? 0.48283   -15.78394 21.29119  1.000 23.49925  ? 289  TRP A CA    1 
ATOM   2337 C  C     . TRP A 1 289 ? 1.02770   -17.03961 21.95943  1.000 24.02729  ? 289  TRP A C     1 
ATOM   2338 O  O     . TRP A 1 289 ? 0.69344   -18.15857 21.55287  1.000 24.62999  ? 289  TRP A O     1 
ATOM   2339 C  CB    . TRP A 1 289 ? 1.52147   -15.21742 20.32497  1.000 23.66843  ? 289  TRP A CB    1 
ATOM   2340 C  CG    . TRP A 1 289 ? 2.22686   -16.29717 19.56444  1.000 24.69903  ? 289  TRP A CG    1 
ATOM   2341 C  CD1   . TRP A 1 289 ? 1.70728   -17.06565 18.56358  1.000 25.07610  ? 289  TRP A CD1   1 
ATOM   2342 C  CD2   . TRP A 1 289 ? 3.57011   -16.75571 19.76570  1.000 24.52398  ? 289  TRP A CD2   1 
ATOM   2343 N  NE1   . TRP A 1 289 ? 2.64729   -17.96327 18.11876  1.000 25.69341  ? 289  TRP A NE1   1 
ATOM   2344 C  CE2   . TRP A 1 289 ? 3.79938   -17.79397 18.84079  1.000 25.49520  ? 289  TRP A CE2   1 
ATOM   2345 C  CE3   . TRP A 1 289 ? 4.60244   -16.38408 20.63194  1.000 24.23978  ? 289  TRP A CE3   1 
ATOM   2346 C  CZ2   . TRP A 1 289 ? 5.01761   -18.46474 18.75817  1.000 25.87065  ? 289  TRP A CZ2   1 
ATOM   2347 C  CZ3   . TRP A 1 289 ? 5.81129   -17.05004 20.54728  1.000 25.23067  ? 289  TRP A CZ3   1 
ATOM   2348 C  CH2   . TRP A 1 289 ? 6.00804   -18.07919 19.61846  1.000 26.13005  ? 289  TRP A CH2   1 
ATOM   2349 N  N     . ARG A 1 290 ? 1.87327   -16.87325 22.98134  1.000 29.84957  ? 290  ARG A N     1 
ATOM   2350 C  CA    . ARG A 1 290 ? 2.48424   -18.02400 23.64016  1.000 30.78585  ? 290  ARG A CA    1 
ATOM   2351 C  C     . ARG A 1 290 ? 1.43843   -18.96031 24.23060  1.000 31.06418  ? 290  ARG A C     1 
ATOM   2352 O  O     . ARG A 1 290 ? 1.63968   -20.17970 24.25124  1.000 31.83734  ? 290  ARG A O     1 
ATOM   2353 C  CB    . ARG A 1 290 ? 3.44500   -17.55618 24.73466  1.000 30.74031  ? 290  ARG A CB    1 
ATOM   2354 C  CG    . ARG A 1 290 ? 4.69482   -16.85578 24.22537  1.000 31.14018  ? 290  ARG A CG    1 
ATOM   2355 C  CD    . ARG A 1 290 ? 5.84274   -17.83028 24.05097  1.000 32.23748  ? 290  ARG A CD    1 
ATOM   2356 N  NE    . ARG A 1 290 ? 7.07675   -17.15355 23.67016  1.000 32.17716  ? 290  ARG A NE    1 
ATOM   2357 C  CZ    . ARG A 1 290 ? 8.08720   -17.73825 23.04162  1.000 32.92678  ? 290  ARG A CZ    1 
ATOM   2358 N  NH1   . ARG A 1 290 ? 8.04019   -19.01472 22.69611  1.000 33.01341  ? 290  ARG A NH1   1 
ATOM   2359 N  NH2   . ARG A 1 290 ? 9.17132   -17.02387 22.75103  1.000 32.85619  ? 290  ARG A NH2   1 
ATOM   2360 N  N     . GLU A 1 291 ? 0.31936   -18.41757 24.70948  1.000 35.51722  ? 291  GLU A N     1 
ATOM   2361 C  CA    . GLU A 1 291 ? -0.72982  -19.21476 25.32839  1.000 36.02806  ? 291  GLU A CA    1 
ATOM   2362 C  C     . GLU A 1 291 ? -1.89734  -19.48247 24.38247  1.000 35.73275  ? 291  GLU A C     1 
ATOM   2363 O  O     . GLU A 1 291 ? -2.97934  -19.87244 24.83525  1.000 35.93107  ? 291  GLU A O     1 
ATOM   2364 C  CB    . GLU A 1 291 ? -1.21213  -18.53668 26.61070  1.000 35.14704  ? 291  GLU A CB    1 
ATOM   2365 C  CG    . GLU A 1 291 ? -0.26677  -18.73867 27.78676  1.000 35.68472  ? 291  GLU A CG    1 
ATOM   2366 C  CD    . GLU A 1 291 ? -0.42272  -17.67913 28.85888  1.000 35.63872  ? 291  GLU A CD    1 
ATOM   2367 O  OE1   . GLU A 1 291 ? -1.44505  -16.96182 28.84665  1.000 35.17600  ? 291  GLU A OE1   1 
ATOM   2368 O  OE2   . GLU A 1 291 ? 0.48122   -17.56249 29.71349  1.000 36.17774  ? 291  GLU A OE2   1 
ATOM   2369 N  N     . GLY A 1 292 ? -1.69932  -19.27818 23.08149  1.000 26.19067  ? 292  GLY A N     1 
ATOM   2370 C  CA    . GLY A 1 292 ? -2.67572  -19.68856 22.09150  1.000 26.60898  ? 292  GLY A CA    1 
ATOM   2371 C  C     . GLY A 1 292 ? -3.89104  -18.80336 21.94823  1.000 26.02768  ? 292  GLY A C     1 
ATOM   2372 O  O     . GLY A 1 292 ? -4.91942  -19.26556 21.44482  1.000 26.59116  ? 292  GLY A O     1 
ATOM   2373 N  N     . ARG A 1 293 ? -3.81143  -17.54047 22.36156  1.000 29.70421  ? 293  ARG A N     1 
ATOM   2374 C  CA    . ARG A 1 293 ? -4.95581  -16.64382 22.28621  1.000 29.64684  ? 293  ARG A CA    1 
ATOM   2375 C  C     . ARG A 1 293 ? -4.89142  -15.67869 21.10917  1.000 29.47630  ? 293  ARG A C     1 
ATOM   2376 O  O     . ARG A 1 293 ? -5.88751  -15.00346 20.82946  1.000 29.03191  ? 293  ARG A O     1 
ATOM   2377 C  CB    . ARG A 1 293 ? -5.09228  -15.85104 23.59244  1.000 29.10458  ? 293  ARG A CB    1 
ATOM   2378 C  CG    . ARG A 1 293 ? -5.52080  -16.69773 24.78419  1.000 29.54947  ? 293  ARG A CG    1 
ATOM   2379 C  CD    . ARG A 1 293 ? -5.74839  -15.84033 26.01801  1.000 29.80221  ? 293  ARG A CD    1 
ATOM   2380 N  NE    . ARG A 1 293 ? -4.55754  -15.08325 26.38675  1.000 29.51570  ? 293  ARG A NE    1 
ATOM   2381 C  CZ    . ARG A 1 293 ? -3.61556  -15.52398 27.20949  1.000 29.79465  ? 293  ARG A CZ    1 
ATOM   2382 N  NH1   . ARG A 1 293 ? -3.69127  -16.72082 27.76923  1.000 30.46455  ? 293  ARG A NH1   1 
ATOM   2383 N  NH2   . ARG A 1 293 ? -2.57242  -14.74407 27.47926  1.000 29.02813  ? 293  ARG A NH2   1 
ATOM   2384 N  N     . ALA A 1 294 ? -3.76000  -15.59904 20.41433  1.000 20.14004  ? 294  ALA A N     1 
ATOM   2385 C  CA    . ALA A 1 294 ? -3.61602  -14.71654 19.26709  1.000 19.91121  ? 294  ALA A CA    1 
ATOM   2386 C  C     . ALA A 1 294 ? -2.61587  -15.33528 18.30525  1.000 20.96052  ? 294  ALA A C     1 
ATOM   2387 O  O     . ALA A 1 294 ? -1.67287  -16.00423 18.74424  1.000 20.87004  ? 294  ALA A O     1 
ATOM   2388 C  CB    . ALA A 1 294 ? -3.15400  -13.31371 19.68887  1.000 19.47540  ? 294  ALA A CB    1 
ATOM   2389 N  N     . PRO A 1 295 ? -2.79200  -15.14292 16.99989  1.000 26.11044  ? 295  PRO A N     1 
ATOM   2390 C  CA    . PRO A 1 295 ? -1.82568  -15.68725 16.04207  1.000 26.53439  ? 295  PRO A CA    1 
ATOM   2391 C  C     . PRO A 1 295 ? -0.52681  -14.89473 16.05362  1.000 26.56170  ? 295  PRO A C     1 
ATOM   2392 O  O     . PRO A 1 295 ? -0.46396  -13.74621 16.49848  1.000 26.18295  ? 295  PRO A O     1 
ATOM   2393 C  CB    . PRO A 1 295 ? -2.54686  -15.56238 14.69689  1.000 26.69919  ? 295  PRO A CB    1 
ATOM   2394 C  CG    . PRO A 1 295 ? -3.47583  -14.41410 14.88156  1.000 25.80931  ? 295  PRO A CG    1 
ATOM   2395 C  CD    . PRO A 1 295 ? -3.88882  -14.41858 16.33288  1.000 25.27574  ? 295  PRO A CD    1 
ATOM   2396 N  N     . LEU A 1 296 ? 0.52715   -15.53933 15.54703  1.000 23.15678  ? 296  LEU A N     1 
ATOM   2397 C  CA    . LEU A 1 296 ? 1.86347   -14.95808 15.62929  1.000 22.99216  ? 296  LEU A CA    1 
ATOM   2398 C  C     . LEU A 1 296 ? 2.00253   -13.73658 14.72639  1.000 23.02712  ? 296  LEU A C     1 
ATOM   2399 O  O     . LEU A 1 296 ? 2.63015   -12.74411 15.11436  1.000 22.34303  ? 296  LEU A O     1 
ATOM   2400 C  CB    . LEU A 1 296 ? 2.91387   -16.01569 15.28337  1.000 23.45819  ? 296  LEU A CB    1 
ATOM   2401 C  CG    . LEU A 1 296 ? 4.37665   -15.56344 15.27855  1.000 23.83801  ? 296  LEU A CG    1 
ATOM   2402 C  CD1   . LEU A 1 296 ? 4.73445   -14.85521 16.57886  1.000 23.56731  ? 296  LEU A CD1   1 
ATOM   2403 C  CD2   . LEU A 1 296 ? 5.30452   -16.74291 15.03419  1.000 23.75665  ? 296  LEU A CD2   1 
ATOM   2404 N  N     . ASN A 1 297 ? 1.42191   -13.78131 13.52312  1.000 31.45738  ? 297  ASN A N     1 
ATOM   2405 C  CA    . ASN A 1 297 ? 1.53538   -12.63994 12.61801  1.000 30.99636  ? 297  ASN A CA    1 
ATOM   2406 C  C     . ASN A 1 297 ? 0.86606   -11.39763 13.19160  1.000 30.17304  ? 297  ASN A C     1 
ATOM   2407 O  O     . ASN A 1 297 ? 1.30879   -10.27547 12.92318  1.000 29.76887  ? 297  ASN A O     1 
ATOM   2408 C  CB    . ASN A 1 297 ? 0.94342   -12.98073 11.24744  1.000 30.96055  ? 297  ASN A CB    1 
ATOM   2409 C  CG    . ASN A 1 297 ? -0.43717  -13.60797 11.33864  1.000 32.26310  ? 297  ASN A CG    1 
ATOM   2410 O  OD1   . ASN A 1 297 ? -1.19057  -13.35817 12.27988  1.000 31.94865  ? 297  ASN A OD1   1 
ATOM   2411 N  ND2   . ASN A 1 297 ? -0.77029  -14.44074 10.35748  1.000 33.20622  ? 297  ASN A ND2   1 
ATOM   2412 N  N     . ALA A 1 298 ? -0.19309  -11.57483 13.98453  1.000 17.89957  ? 298  ALA A N     1 
ATOM   2413 C  CA    . ALA A 1 298 ? -0.84800  -10.42911 14.60648  1.000 17.36395  ? 298  ALA A CA    1 
ATOM   2414 C  C     . ALA A 1 298 ? -0.01529  -9.87155  15.75381  1.000 17.31043  ? 298  ALA A C     1 
ATOM   2415 O  O     . ALA A 1 298 ? 0.13803   -8.65078  15.88076  1.000 16.59817  ? 298  ALA A O     1 
ATOM   2416 C  CB    . ALA A 1 298 ? -2.24087  -10.82227 15.09671  1.000 16.81909  ? 298  ALA A CB    1 
ATOM   2417 N  N     . VAL A 1 299 ? 0.53203   -10.75057 16.59654  1.000 19.05534  ? 299  VAL A N     1 
ATOM   2418 C  CA    . VAL A 1 299 ? 1.30948   -10.29897 17.74628  1.000 19.05971  ? 299  VAL A CA    1 
ATOM   2419 C  C     . VAL A 1 299 ? 2.63276   -9.69285  17.29486  1.000 19.18652  ? 299  VAL A C     1 
ATOM   2420 O  O     . VAL A 1 299 ? 3.06697   -8.65820  17.81699  1.000 18.25831  ? 299  VAL A O     1 
ATOM   2421 C  CB    . VAL A 1 299 ? 1.52233   -11.46264 18.73178  1.000 19.43556  ? 299  VAL A CB    1 
ATOM   2422 C  CG1   . VAL A 1 299 ? 2.60246   -11.11601 19.74773  1.000 18.91006  ? 299  VAL A CG1   1 
ATOM   2423 C  CG2   . VAL A 1 299 ? 0.21555   -11.80764 19.43049  1.000 19.25126  ? 299  VAL A CG2   1 
ATOM   2424 N  N     . GLU A 1 300 ? 3.29583   -10.32386 16.32103  1.000 20.57289  ? 300  GLU A N     1 
ATOM   2425 C  CA    . GLU A 1 300 ? 4.54301   -9.77035  15.80169  1.000 20.38218  ? 300  GLU A CA    1 
ATOM   2426 C  C     . GLU A 1 300 ? 4.30799   -8.42213  15.13430  1.000 19.64848  ? 300  GLU A C     1 
ATOM   2427 O  O     . GLU A 1 300 ? 5.10553   -7.49118  15.30117  1.000 19.29047  ? 300  GLU A O     1 
ATOM   2428 C  CB    . GLU A 1 300 ? 5.18977   -10.74774 14.82007  1.000 20.10071  ? 300  GLU A CB    1 
ATOM   2429 C  CG    . GLU A 1 300 ? 6.61317   -10.37863 14.42252  1.000 20.17037  ? 300  GLU A CG    1 
ATOM   2430 C  CD    . GLU A 1 300 ? 6.66217   -9.37977  13.27671  1.000 20.29039  ? 300  GLU A CD    1 
ATOM   2431 O  OE1   . GLU A 1 300 ? 5.97305   -9.60387  12.25923  1.000 20.28133  ? 300  GLU A OE1   1 
ATOM   2432 O  OE2   . GLU A 1 300 ? 7.38350   -8.36685  13.39767  1.000 19.74868  ? 300  GLU A OE2   1 
ATOM   2433 N  N     . GLY A 1 301 ? 3.22187   -8.30173  14.36627  1.000 25.66486  ? 301  GLY A N     1 
ATOM   2434 C  CA    . GLY A 1 301 ? 2.89653   -7.02468  13.75672  1.000 25.34364  ? 301  GLY A CA    1 
ATOM   2435 C  C     . GLY A 1 301 ? 2.64886   -5.93184  14.77626  1.000 25.22040  ? 301  GLY A C     1 
ATOM   2436 O  O     . GLY A 1 301 ? 2.99964   -4.77187  14.54674  1.000 24.47701  ? 301  GLY A O     1 
ATOM   2437 N  N     . PHE A 1 302 ? 2.05260   -6.28493  15.91652  1.000 21.78421  ? 302  PHE A N     1 
ATOM   2438 C  CA    . PHE A 1 302 ? 1.82016   -5.30647  16.97372  1.000 21.29721  ? 302  PHE A CA    1 
ATOM   2439 C  C     . PHE A 1 302 ? 3.12466   -4.92147  17.66143  1.000 21.51215  ? 302  PHE A C     1 
ATOM   2440 O  O     . PHE A 1 302 ? 3.41405   -3.73363  17.84745  1.000 20.52124  ? 302  PHE A O     1 
ATOM   2441 C  CB    . PHE A 1 302 ? 0.81836   -5.86692  17.98453  1.000 21.29726  ? 302  PHE A CB    1 
ATOM   2442 C  CG    . PHE A 1 302 ? 0.53967   -4.95059  19.14064  1.000 20.31349  ? 302  PHE A CG    1 
ATOM   2443 C  CD1   . PHE A 1 302 ? -0.11110  -3.74407  18.94588  1.000 19.30938  ? 302  PHE A CD1   1 
ATOM   2444 C  CD2   . PHE A 1 302 ? 0.92261   -5.30155  20.42504  1.000 20.30530  ? 302  PHE A CD2   1 
ATOM   2445 C  CE1   . PHE A 1 302 ? -0.37010  -2.90144  20.01136  1.000 18.84978  ? 302  PHE A CE1   1 
ATOM   2446 C  CE2   . PHE A 1 302 ? 0.66659   -4.46447  21.49371  1.000 19.62436  ? 302  PHE A CE2   1 
ATOM   2447 C  CZ    . PHE A 1 302 ? 0.01979   -3.26269  21.28706  1.000 19.12234  ? 302  PHE A CZ    1 
ATOM   2448 N  N     . ILE A 1 303 ? 3.92926   -5.91748  18.04208  1.000 23.42441  ? 303  ILE A N     1 
ATOM   2449 C  CA    . ILE A 1 303 ? 5.18024   -5.64311  18.74372  1.000 22.95123  ? 303  ILE A CA    1 
ATOM   2450 C  C     . ILE A 1 303 ? 6.14753   -4.87540  17.85112  1.000 22.64925  ? 303  ILE A C     1 
ATOM   2451 O  O     . ILE A 1 303 ? 6.92611   -4.04328  18.33585  1.000 22.15645  ? 303  ILE A O     1 
ATOM   2452 C  CB    . ILE A 1 303 ? 5.78931   -6.96335  19.26149  1.000 23.52448  ? 303  ILE A CB    1 
ATOM   2453 C  CG1   . ILE A 1 303 ? 5.06721   -7.41094  20.53451  1.000 23.60701  ? 303  ILE A CG1   1 
ATOM   2454 C  CG2   . ILE A 1 303 ? 7.28009   -6.81991  19.52857  1.000 23.03916  ? 303  ILE A CG2   1 
ATOM   2455 C  CD1   . ILE A 1 303 ? 5.32604   -8.85035  20.91164  1.000 23.57603  ? 303  ILE A CD1   1 
ATOM   2456 N  N     . ARG A 1 304 ? 6.10050   -5.11562  16.53763  1.000 26.44945  ? 304  ARG A N     1 
ATOM   2457 C  CA    . ARG A 1 304 ? 6.98354   -4.39703  15.62421  1.000 26.13343  ? 304  ARG A CA    1 
ATOM   2458 C  C     . ARG A 1 304 ? 6.70255   -2.90038  15.62073  1.000 25.20455  ? 304  ARG A C     1 
ATOM   2459 O  O     . ARG A 1 304 ? 7.61202   -2.10051  15.37735  1.000 24.72308  ? 304  ARG A O     1 
ATOM   2460 C  CB    . ARG A 1 304 ? 6.85069   -4.95455  14.20824  1.000 26.60600  ? 304  ARG A CB    1 
ATOM   2461 C  CG    . ARG A 1 304 ? 8.00793   -4.58075  13.29833  1.000 27.21018  ? 304  ARG A CG    1 
ATOM   2462 C  CD    . ARG A 1 304 ? 7.61572   -4.66630  11.83746  1.000 27.71139  ? 304  ARG A CD    1 
ATOM   2463 N  NE    . ARG A 1 304 ? 7.02340   -5.95726  11.51169  1.000 28.48216  ? 304  ARG A NE    1 
ATOM   2464 C  CZ    . ARG A 1 304 ? 5.95998   -6.11492  10.73545  1.000 29.28912  ? 304  ARG A CZ    1 
ATOM   2465 N  NH1   . ARG A 1 304 ? 5.35439   -5.08072  10.17448  1.000 28.70501  ? 304  ARG A NH1   1 
ATOM   2466 N  NH2   . ARG A 1 304 ? 5.49444   -7.34115  10.51304  1.000 28.79725  ? 304  ARG A NH2   1 
ATOM   2467 N  N     . GLN A 1 305 ? 5.45701   -2.50001  15.87743  1.000 27.87370  ? 305  GLN A N     1 
ATOM   2468 C  CA    . GLN A 1 305 ? 5.14297   -1.07613  15.89937  1.000 27.37375  ? 305  GLN A CA    1 
ATOM   2469 C  C     . GLN A 1 305 ? 5.76264   -0.37844  17.10589  1.000 27.14250  ? 305  GLN A C     1 
ATOM   2470 O  O     . GLN A 1 305 ? 6.09289   0.81068   17.02802  1.000 26.19199  ? 305  GLN A O     1 
ATOM   2471 C  CB    . GLN A 1 305 ? 3.62718   -0.86772  15.89180  1.000 26.82506  ? 305  GLN A CB    1 
ATOM   2472 C  CG    . GLN A 1 305 ? 2.86771   -1.61687  14.79992  1.000 27.48594  ? 305  GLN A CG    1 
ATOM   2473 C  CD    . GLN A 1 305 ? 3.55929   -1.57007  13.44974  1.000 28.23614  ? 305  GLN A CD    1 
ATOM   2474 O  OE1   . GLN A 1 305 ? 3.83287   -0.49486  12.91735  1.000 27.73520  ? 305  GLN A OE1   1 
ATOM   2475 N  NE2   . GLN A 1 305 ? 3.83263   -2.74141  12.88149  1.000 28.82106  ? 305  GLN A NE2   1 
ATOM   2476 N  N     . ILE A 1 306 ? 5.94661   -1.09805  18.21404  1.000 21.97982  ? 306  ILE A N     1 
ATOM   2477 C  CA    . ILE A 1 306 ? 6.33721   -0.49042  19.48309  1.000 22.08435  ? 306  ILE A CA    1 
ATOM   2478 C  C     . ILE A 1 306 ? 7.84750   -0.55507  19.68078  1.000 22.01294  ? 306  ILE A C     1 
ATOM   2479 O  O     . ILE A 1 306 ? 8.50023   0.47535   19.87921  1.000 21.83294  ? 306  ILE A O     1 
ATOM   2480 C  CB    . ILE A 1 306 ? 5.59462   -1.16058  20.65378  1.000 23.12917  ? 306  ILE A CB    1 
ATOM   2481 C  CG1   . ILE A 1 306 ? 4.10186   -0.83144  20.57908  1.000 22.02509  ? 306  ILE A CG1   1 
ATOM   2482 C  CG2   . ILE A 1 306 ? 6.17888   -0.71800  21.98708  1.000 21.99045  ? 306  ILE A CG2   1 
ATOM   2483 C  CD1   . ILE A 1 306 ? 3.23372   -1.70172  21.45485  1.000 22.26833  ? 306  ILE A CD1   1 
ATOM   2484 N  N     . ILE A 1 307 ? 8.41747   -1.76269  19.64500  1.000 15.35229  ? 307  ILE A N     1 
ATOM   2485 C  CA    . ILE A 1 307 ? 9.86802   -1.89610  19.77398  1.000 15.49445  ? 307  ILE A CA    1 
ATOM   2486 C  C     . ILE A 1 307 ? 10.59683  -1.58662  18.47852  1.000 15.39875  ? 307  ILE A C     1 
ATOM   2487 O  O     . ILE A 1 307 ? 11.82091  -1.40595  18.49423  1.000 15.07462  ? 307  ILE A O     1 
ATOM   2488 C  CB    . ILE A 1 307 ? 10.26463  -3.30469  20.25509  1.000 15.86480  ? 307  ILE A CB    1 
ATOM   2489 C  CG1   . ILE A 1 307 ? 10.26369  -4.29816  19.09117  1.000 16.87409  ? 307  ILE A CG1   1 
ATOM   2490 C  CG2   . ILE A 1 307 ? 9.33432   -3.76876  21.35822  1.000 16.07273  ? 307  ILE A CG2   1 
ATOM   2491 C  CD1   . ILE A 1 307 ? 10.82835  -5.65508  19.45294  1.000 17.31855  ? 307  ILE A CD1   1 
ATOM   2492 N  N     . GLY A 1 308 ? 9.88238   -1.51638  17.35990  1.000 25.47494  ? 308  GLY A N     1 
ATOM   2493 C  CA    . GLY A 1 308 ? 10.49313  -1.16093  16.09717  1.000 24.81858  ? 308  GLY A CA    1 
ATOM   2494 C  C     . GLY A 1 308 ? 10.29625  0.29962   15.75084  1.000 24.37105  ? 308  GLY A C     1 
ATOM   2495 O  O     . GLY A 1 308 ? 11.19775  1.11509   15.95939  1.000 24.12301  ? 308  GLY A O     1 
ATOM   2496 N  N     . TRP A 1 309 ? 9.10813   0.64630   15.24937  1.000 23.12075  ? 309  TRP A N     1 
ATOM   2497 C  CA    . TRP A 1 309 ? 8.88764   1.98916   14.71791  1.000 23.03329  ? 309  TRP A CA    1 
ATOM   2498 C  C     . TRP A 1 309 ? 8.97987   3.05537   15.80422  1.000 22.33281  ? 309  TRP A C     1 
ATOM   2499 O  O     . TRP A 1 309 ? 9.59312   4.10707   15.59090  1.000 22.03901  ? 309  TRP A O     1 
ATOM   2500 C  CB    . TRP A 1 309 ? 7.53350   2.05854   14.01356  1.000 22.74140  ? 309  TRP A CB    1 
ATOM   2501 C  CG    . TRP A 1 309 ? 7.58599   1.59724   12.58978  1.000 23.70965  ? 309  TRP A CG    1 
ATOM   2502 C  CD1   . TRP A 1 309 ? 6.93481   0.52539   12.04995  1.000 23.60158  ? 309  TRP A CD1   1 
ATOM   2503 C  CD2   . TRP A 1 309 ? 8.33567   2.19067   11.52198  1.000 23.46312  ? 309  TRP A CD2   1 
ATOM   2504 N  NE1   . TRP A 1 309 ? 7.23134   0.41625   10.71271  1.000 23.98062  ? 309  TRP A NE1   1 
ATOM   2505 C  CE2   . TRP A 1 309 ? 8.08886   1.42645   10.36384  1.000 24.00905  ? 309  TRP A CE2   1 
ATOM   2506 C  CE3   . TRP A 1 309 ? 9.18960   3.29470   11.43254  1.000 22.95333  ? 309  TRP A CE3   1 
ATOM   2507 C  CZ2   . TRP A 1 309 ? 8.66571   1.72995   9.13221   1.000 23.87925  ? 309  TRP A CZ2   1 
ATOM   2508 C  CZ3   . TRP A 1 309 ? 9.76248   3.59344   10.20902  1.000 23.24779  ? 309  TRP A CZ3   1 
ATOM   2509 C  CH2   . TRP A 1 309 ? 9.49750   2.81451   9.07551   1.000 23.60562  ? 309  TRP A CH2   1 
ATOM   2510 N  N     . ARG A 1 310 ? 8.38156   2.80806   16.97249  1.000 16.71436  ? 310  ARG A N     1 
ATOM   2511 C  CA    . ARG A 1 310 ? 8.36656   3.82427   18.02211  1.000 16.51792  ? 310  ARG A CA    1 
ATOM   2512 C  C     . ARG A 1 310 ? 9.77653   4.13266   18.51202  1.000 16.55684  ? 310  ARG A C     1 
ATOM   2513 O  O     . ARG A 1 310 ? 10.14750  5.30062   18.67810  1.000 16.39751  ? 310  ARG A O     1 
ATOM   2514 C  CB    . ARG A 1 310 ? 7.47596   3.37364   19.17988  1.000 16.82962  ? 310  ARG A CB    1 
ATOM   2515 C  CG    . ARG A 1 310 ? 7.12819   4.48022   20.16238  1.000 15.90071  ? 310  ARG A CG    1 
ATOM   2516 C  CD    . ARG A 1 310 ? 6.05742   4.02828   21.13998  1.000 16.13266  ? 310  ARG A CD    1 
ATOM   2517 N  NE    . ARG A 1 310 ? 5.76576   5.05303   22.13414  1.000 15.88203  ? 310  ARG A NE    1 
ATOM   2518 C  CZ    . ARG A 1 310 ? 6.35964   5.14156   23.31638  1.000 16.16960  ? 310  ARG A CZ    1 
ATOM   2519 N  NH1   . ARG A 1 310 ? 7.28603   4.27463   23.69137  1.000 16.48495  ? 310  ARG A NH1   1 
ATOM   2520 N  NH2   . ARG A 1 310 ? 6.01550   6.12507   24.14289  1.000 15.52126  ? 310  ARG A NH2   1 
ATOM   2521 N  N     . GLU A 1 311 ? 10.58007  3.09431   18.74952  1.000 17.30526  ? 311  GLU A N     1 
ATOM   2522 C  CA    . GLU A 1 311 ? 11.96661  3.31903   19.14121  1.000 17.17507  ? 311  GLU A CA    1 
ATOM   2523 C  C     . GLU A 1 311 ? 12.78858  3.87394   17.98455  1.000 17.26953  ? 311  GLU A C     1 
ATOM   2524 O  O     . GLU A 1 311 ? 13.72118  4.65536   18.20564  1.000 16.86426  ? 311  GLU A O     1 
ATOM   2525 C  CB    . GLU A 1 311 ? 12.58469  2.01870   19.65864  1.000 17.69692  ? 311  GLU A CB    1 
ATOM   2526 C  CG    . GLU A 1 311 ? 11.83471  1.38415   20.82417  1.000 18.01933  ? 311  GLU A CG    1 
ATOM   2527 C  CD    . GLU A 1 311 ? 11.96984  2.17553   22.11289  1.000 18.10412  ? 311  GLU A CD    1 
ATOM   2528 O  OE1   . GLU A 1 311 ? 12.97875  2.89661   22.27027  1.000 17.57246  ? 311  GLU A OE1   1 
ATOM   2529 O  OE2   . GLU A 1 311 ? 11.06957  2.07072   22.97254  1.000 17.80466  ? 311  GLU A OE2   1 
ATOM   2530 N  N     . PHE A 1 312 ? 12.45124  3.49003   16.75107  1.000 17.65490  ? 312  PHE A N     1 
ATOM   2531 C  CA    . PHE A 1 312 ? 13.19817  3.95260   15.58553  1.000 17.73045  ? 312  PHE A CA    1 
ATOM   2532 C  C     . PHE A 1 312 ? 13.02251  5.45103   15.37293  1.000 17.63881  ? 312  PHE A C     1 
ATOM   2533 O  O     . PHE A 1 312 ? 13.99650  6.16975   15.11967  1.000 17.12109  ? 312  PHE A O     1 
ATOM   2534 C  CB    . PHE A 1 312 ? 12.74991  3.17865   14.34685  1.000 17.77311  ? 312  PHE A CB    1 
ATOM   2535 C  CG    . PHE A 1 312 ? 13.57536  3.44574   13.12460  1.000 18.36765  ? 312  PHE A CG    1 
ATOM   2536 C  CD1   . PHE A 1 312 ? 14.89344  3.02391   13.05676  1.000 18.46884  ? 312  PHE A CD1   1 
ATOM   2537 C  CD2   . PHE A 1 312 ? 13.02532  4.09524   12.03151  1.000 17.72220  ? 312  PHE A CD2   1 
ATOM   2538 C  CE1   . PHE A 1 312 ? 15.65330  3.25723   11.92726  1.000 19.03256  ? 312  PHE A CE1   1 
ATOM   2539 C  CE2   . PHE A 1 312 ? 13.77862  4.32871   10.89738  1.000 18.43169  ? 312  PHE A CE2   1 
ATOM   2540 C  CZ    . PHE A 1 312 ? 15.09564  3.91083   10.84590  1.000 18.72670  ? 312  PHE A CZ    1 
ATOM   2541 N  N     . VAL A 1 313 ? 11.78477  5.94275   15.46702  1.000 17.49195  ? 313  VAL A N     1 
ATOM   2542 C  CA    . VAL A 1 313 ? 11.54463  7.35845   15.20771  1.000 17.43672  ? 313  VAL A CA    1 
ATOM   2543 C  C     . VAL A 1 313 ? 12.13724  8.21640   16.31994  1.000 17.17373  ? 313  VAL A C     1 
ATOM   2544 O  O     . VAL A 1 313 ? 12.67313  9.30033   16.06115  1.000 17.41961  ? 313  VAL A O     1 
ATOM   2545 C  CB    . VAL A 1 313 ? 10.04085  7.62796   15.00296  1.000 16.99317  ? 313  VAL A CB    1 
ATOM   2546 C  CG1   . VAL A 1 313 ? 9.52952   6.85494   13.79692  1.000 17.15407  ? 313  VAL A CG1   1 
ATOM   2547 C  CG2   . VAL A 1 313 ? 9.23726   7.27997   16.24668  1.000 17.35377  ? 313  VAL A CG2   1 
ATOM   2548 N  N     . ARG A 1 314 ? 12.07442  7.74395   17.56929  1.000 22.09275  ? 314  ARG A N     1 
ATOM   2549 C  CA    . ARG A 1 314 ? 12.72280  8.47428   18.65444  1.000 21.89752  ? 314  ARG A CA    1 
ATOM   2550 C  C     . ARG A 1 314 ? 14.23234  8.49721   18.46950  1.000 22.62592  ? 314  ARG A C     1 
ATOM   2551 O  O     . ARG A 1 314 ? 14.88369  9.51183   18.74597  1.000 22.30210  ? 314  ARG A O     1 
ATOM   2552 C  CB    . ARG A 1 314 ? 12.37034  7.85778   20.00706  1.000 21.80525  ? 314  ARG A CB    1 
ATOM   2553 C  CG    . ARG A 1 314 ? 13.22091  8.39212   21.15411  1.000 22.11341  ? 314  ARG A CG    1 
ATOM   2554 C  CD    . ARG A 1 314 ? 12.59406  8.09623   22.50122  1.000 22.71487  ? 314  ARG A CD    1 
ATOM   2555 N  NE    . ARG A 1 314 ? 13.44384  8.50870   23.61232  1.000 22.98315  ? 314  ARG A NE    1 
ATOM   2556 C  CZ    . ARG A 1 314 ? 14.46487  7.80213   24.07744  1.000 22.83722  ? 314  ARG A CZ    1 
ATOM   2557 N  NH1   . ARG A 1 314 ? 14.80721  6.64377   23.53686  1.000 22.99302  ? 314  ARG A NH1   1 
ATOM   2558 N  NH2   . ARG A 1 314 ? 15.15869  8.26847   25.11193  1.000 22.28091  ? 314  ARG A NH2   1 
ATOM   2559 N  N     . GLY A 1 315 ? 14.80479  7.38495   18.00686  1.000 18.95165  ? 315  GLY A N     1 
ATOM   2560 C  CA    . GLY A 1 315 ? 16.23659  7.34890   17.77477  1.000 18.51780  ? 315  GLY A CA    1 
ATOM   2561 C  C     . GLY A 1 315 ? 16.68017  8.35159   16.72856  1.000 18.62721  ? 315  GLY A C     1 
ATOM   2562 O  O     . GLY A 1 315 ? 17.68839  9.03839   16.90276  1.000 18.82058  ? 315  GLY A O     1 
ATOM   2563 N  N     . ILE A 1 316 ? 15.92720  8.45750   15.63268  1.000 21.68820  ? 316  ILE A N     1 
ATOM   2564 C  CA    . ILE A 1 316 ? 16.29874  9.37940   14.56406  1.000 21.89530  ? 316  ILE A CA    1 
ATOM   2565 C  C     . ILE A 1 316 ? 16.12232  10.82420  15.01324  1.000 21.70118  ? 316  ILE A C     1 
ATOM   2566 O  O     . ILE A 1 316 ? 16.95794  11.68603  14.71281  1.000 21.88715  ? 316  ILE A O     1 
ATOM   2567 C  CB    . ILE A 1 316 ? 15.48628  9.07315   13.29388  1.000 21.74451  ? 316  ILE A CB    1 
ATOM   2568 C  CG1   . ILE A 1 316 ? 16.02962  7.81078   12.62505  1.000 22.50786  ? 316  ILE A CG1   1 
ATOM   2569 C  CG2   . ILE A 1 316 ? 15.52240  10.25224  12.33016  1.000 22.00835  ? 316  ILE A CG2   1 
ATOM   2570 C  CD1   . ILE A 1 316 ? 15.25937  7.39203   11.40906  1.000 22.61242  ? 316  ILE A CD1   1 
ATOM   2571 N  N     . TYR A 1 317 ? 15.03633  11.11067  15.73649  1.000 18.92959  ? 317  TYR A N     1 
ATOM   2572 C  CA    . TYR A 1 317 ? 14.79516  12.45549  16.25030  1.000 18.82768  ? 317  TYR A CA    1 
ATOM   2573 C  C     . TYR A 1 317 ? 16.00673  12.97691  17.01390  1.000 19.28623  ? 317  TYR A C     1 
ATOM   2574 O  O     . TYR A 1 317 ? 16.61587  13.98129  16.63309  1.000 19.15436  ? 317  TYR A O     1 
ATOM   2575 C  CB    . TYR A 1 317 ? 13.55155  12.45174  17.14353  1.000 19.00863  ? 317  TYR A CB    1 
ATOM   2576 C  CG    . TYR A 1 317 ? 13.17101  13.80650  17.70431  1.000 19.00076  ? 317  TYR A CG    1 
ATOM   2577 C  CD1   . TYR A 1 317 ? 12.55891  14.76380  16.90516  1.000 19.01486  ? 317  TYR A CD1   1 
ATOM   2578 C  CD2   . TYR A 1 317 ? 13.41199  14.12276  19.03702  1.000 19.19919  ? 317  TYR A CD2   1 
ATOM   2579 C  CE1   . TYR A 1 317 ? 12.20251  16.00149  17.41324  1.000 19.20336  ? 317  TYR A CE1   1 
ATOM   2580 C  CE2   . TYR A 1 317 ? 13.05833  15.35950  19.55594  1.000 18.97041  ? 317  TYR A CE2   1 
ATOM   2581 C  CZ    . TYR A 1 317 ? 12.45398  16.29527  18.73769  1.000 19.54992  ? 317  TYR A CZ    1 
ATOM   2582 O  OH    . TYR A 1 317 ? 12.10081  17.52890  19.24149  1.000 19.49967  ? 317  TYR A OH    1 
ATOM   2583 N  N     . TRP A 1 318 ? 16.39058  12.28075  18.08431  1.000 21.80168  ? 318  TRP A N     1 
ATOM   2584 C  CA    . TRP A 1 318 ? 17.49823  12.74852  18.90655  1.000 21.94360  ? 318  TRP A CA    1 
ATOM   2585 C  C     . TRP A 1 318 ? 18.84506  12.60606  18.20963  1.000 22.10385  ? 318  TRP A C     1 
ATOM   2586 O  O     . TRP A 1 318 ? 19.80800  13.26665  18.61229  1.000 22.16819  ? 318  TRP A O     1 
ATOM   2587 C  CB    . TRP A 1 318 ? 17.49858  12.00438  20.24125  1.000 21.42242  ? 318  TRP A CB    1 
ATOM   2588 C  CG    . TRP A 1 318 ? 16.33791  12.39221  21.10289  1.000 21.73377  ? 318  TRP A CG    1 
ATOM   2589 C  CD1   . TRP A 1 318 ? 15.27782  11.60998  21.45298  1.000 21.94372  ? 318  TRP A CD1   1 
ATOM   2590 C  CD2   . TRP A 1 318 ? 16.11027  13.67094  21.70875  1.000 21.90028  ? 318  TRP A CD2   1 
ATOM   2591 N  NE1   . TRP A 1 318 ? 14.40750  12.31797  22.24575  1.000 21.42824  ? 318  TRP A NE1   1 
ATOM   2592 C  CE2   . TRP A 1 318 ? 14.89606  13.58631  22.41790  1.000 21.57468  ? 318  TRP A CE2   1 
ATOM   2593 C  CE3   . TRP A 1 318 ? 16.81812  14.87688  21.72458  1.000 21.59953  ? 318  TRP A CE3   1 
ATOM   2594 C  CZ2   . TRP A 1 318 ? 14.37365  14.66113  23.13396  1.000 21.63744  ? 318  TRP A CZ2   1 
ATOM   2595 C  CZ3   . TRP A 1 318 ? 16.29763  15.94318  22.43681  1.000 21.77103  ? 318  TRP A CZ3   1 
ATOM   2596 C  CH2   . TRP A 1 318 ? 15.08786  15.82813  23.13136  1.000 21.38738  ? 318  TRP A CH2   1 
ATOM   2597 N  N     . LEU A 1 319 ? 18.93421  11.77736  17.16848  1.000 21.93313  ? 319  LEU A N     1 
ATOM   2598 C  CA    . LEU A 1 319 ? 20.19074  11.64697  16.43993  1.000 22.01283  ? 319  LEU A CA    1 
ATOM   2599 C  C     . LEU A 1 319 ? 20.41163  12.81220  15.48209  1.000 22.07544  ? 319  LEU A C     1 
ATOM   2600 O  O     . LEU A 1 319 ? 21.54828  13.26160  15.30335  1.000 22.64301  ? 319  LEU A O     1 
ATOM   2601 C  CB    . LEU A 1 319 ? 20.22075  10.32434  15.67423  1.000 22.11588  ? 319  LEU A CB    1 
ATOM   2602 C  CG    . LEU A 1 319 ? 21.47571  10.02604  14.85260  1.000 22.79554  ? 319  LEU A CG    1 
ATOM   2603 C  CD1   . LEU A 1 319 ? 22.69773  9.91150   15.75217  1.000 22.43099  ? 319  LEU A CD1   1 
ATOM   2604 C  CD2   . LEU A 1 319 ? 21.28246  8.76147   14.03269  1.000 22.77255  ? 319  LEU A CD2   1 
ATOM   2605 N  N     . LYS A 1 320 ? 19.34165  13.32022  14.86518  1.000 21.91945  ? 320  LYS A N     1 
ATOM   2606 C  CA    . LYS A 1 320 ? 19.46501  14.30249  13.79691  1.000 22.28249  ? 320  LYS A CA    1 
ATOM   2607 C  C     . LYS A 1 320 ? 19.04175  15.71313  14.18266  1.000 22.32156  ? 320  LYS A C     1 
ATOM   2608 O  O     . LYS A 1 320 ? 19.36568  16.65139  13.44842  1.000 22.54240  ? 320  LYS A O     1 
ATOM   2609 C  CB    . LYS A 1 320 ? 18.64463  13.86367  12.57457  1.000 22.13565  ? 320  LYS A CB    1 
ATOM   2610 C  CG    . LYS A 1 320 ? 19.04594  12.51179  12.01123  1.000 22.48316  ? 320  LYS A CG    1 
ATOM   2611 C  CD    . LYS A 1 320 ? 20.48980  12.51383  11.53922  1.000 22.68792  ? 320  LYS A CD    1 
ATOM   2612 C  CE    . LYS A 1 320 ? 20.72655  11.43163  10.49907  1.000 22.53003  ? 320  LYS A CE    1 
ATOM   2613 N  NZ    . LYS A 1 320 ? 22.17420  11.12146  10.34572  1.000 23.24683  ? 320  LYS A NZ    1 
ATOM   2614 N  N     . MET A 1 321 ? 18.32524  15.88996  15.29217  1.000 20.88736  ? 321  MET A N     1 
ATOM   2615 C  CA    . MET A 1 321 ? 17.94887  17.22825  15.72280  1.000 20.84567  ? 321  MET A CA    1 
ATOM   2616 C  C     . MET A 1 321 ? 19.19180  18.01219  16.14533  1.000 20.85778  ? 321  MET A C     1 
ATOM   2617 O  O     . MET A 1 321 ? 20.18185  17.42527  16.58840  1.000 21.12936  ? 321  MET A O     1 
ATOM   2618 C  CB    . MET A 1 321 ? 16.95690  17.16595  16.88328  1.000 20.64238  ? 321  MET A CB    1 
ATOM   2619 C  CG    . MET A 1 321 ? 15.52022  16.87231  16.47759  1.000 20.51620  ? 321  MET A CG    1 
ATOM   2620 S  SD    . MET A 1 321 ? 14.79012  18.16794  15.46115  1.000 21.26258  ? 321  MET A SD    1 
ATOM   2621 C  CE    . MET A 1 321 ? 14.33632  19.37480  16.70706  1.000 20.99166  ? 321  MET A CE    1 
ATOM   2622 N  N     . PRO A 1 322 ? 19.16290  19.35134  16.03421  1.000 20.46546  ? 322  PRO A N     1 
ATOM   2623 C  CA    . PRO A 1 322 ? 18.04829  20.21158  15.60984  1.000 20.30187  ? 322  PRO A CA    1 
ATOM   2624 C  C     . PRO A 1 322 ? 17.93968  20.37543  14.09774  1.000 20.47118  ? 322  PRO A C     1 
ATOM   2625 O  O     . PRO A 1 322 ? 16.92394  20.85896  13.60559  1.000 20.56647  ? 322  PRO A O     1 
ATOM   2626 C  CB    . PRO A 1 322 ? 18.38088  21.54159  16.29223  1.000 20.75765  ? 322  PRO A CB    1 
ATOM   2627 C  CG    . PRO A 1 322 ? 19.88311  21.58686  16.26411  1.000 21.56432  ? 322  PRO A CG    1 
ATOM   2628 C  CD    . PRO A 1 322 ? 20.34524  20.14849  16.41124  1.000 21.35322  ? 322  PRO A CD    1 
ATOM   2629 N  N     . GLU A 1 323 ? 18.96699  19.98005  13.34012  1.000 30.38073  ? 323  GLU A N     1 
ATOM   2630 C  CA    . GLU A 1 323 ? 18.95139  20.19096  11.89534  1.000 31.03842  ? 323  GLU A CA    1 
ATOM   2631 C  C     . GLU A 1 323 ? 17.80918  19.44141  11.22580  1.000 31.07210  ? 323  GLU A C     1 
ATOM   2632 O  O     . GLU A 1 323 ? 17.34802  19.84562  10.15203  1.000 31.45626  ? 323  GLU A O     1 
ATOM   2633 C  CB    . GLU A 1 323 ? 20.28572  19.76059  11.28779  1.000 30.99035  ? 323  GLU A CB    1 
ATOM   2634 C  CG    . GLU A 1 323 ? 21.45174  20.66064  11.64942  1.000 31.28602  ? 323  GLU A CG    1 
ATOM   2635 C  CD    . GLU A 1 323 ? 22.11792  20.24845  12.94738  1.000 32.00564  ? 323  GLU A CD    1 
ATOM   2636 O  OE1   . GLU A 1 323 ? 21.78659  19.16102  13.46616  1.000 30.72445  ? 323  GLU A OE1   1 
ATOM   2637 O  OE2   . GLU A 1 323 ? 22.97699  21.00779  13.44441  1.000 33.61590  ? 323  GLU A OE2   1 
ATOM   2638 N  N     . TYR A 1 324 ? 17.34258  18.35159  11.83945  1.000 21.37306  ? 324  TYR A N     1 
ATOM   2639 C  CA    . TYR A 1 324 ? 16.25299  17.58009  11.25133  1.000 21.17272  ? 324  TYR A CA    1 
ATOM   2640 C  C     . TYR A 1 324 ? 14.98716  18.41883  11.12603  1.000 21.87341  ? 324  TYR A C     1 
ATOM   2641 O  O     . TYR A 1 324 ? 14.26434  18.31893  10.12730  1.000 21.37045  ? 324  TYR A O     1 
ATOM   2642 C  CB    . TYR A 1 324 ? 15.98959  16.32876  12.08868  1.000 20.71946  ? 324  TYR A CB    1 
ATOM   2643 C  CG    . TYR A 1 324 ? 15.06542  15.33084  11.43011  1.000 20.50195  ? 324  TYR A CG    1 
ATOM   2644 C  CD1   . TYR A 1 324 ? 15.56179  14.35107  10.58124  1.000 20.57925  ? 324  TYR A CD1   1 
ATOM   2645 C  CD2   . TYR A 1 324 ? 13.69655  15.36708  11.65969  1.000 20.75442  ? 324  TYR A CD2   1 
ATOM   2646 C  CE1   . TYR A 1 324 ? 14.72052  13.43473  9.97902   1.000 20.43824  ? 324  TYR A CE1   1 
ATOM   2647 C  CE2   . TYR A 1 324 ? 12.84799  14.45699  11.06286  1.000 19.86754  ? 324  TYR A CE2   1 
ATOM   2648 C  CZ    . TYR A 1 324 ? 13.36490  13.49368  10.22297  1.000 20.49700  ? 324  TYR A CZ    1 
ATOM   2649 O  OH    . TYR A 1 324 ? 12.51944  12.58802  9.62624   1.000 20.44983  ? 324  TYR A OH    1 
ATOM   2650 N  N     . ALA A 1 325 ? 14.71090  19.26353  12.12376  1.000 20.86318  ? 325  ALA A N     1 
ATOM   2651 C  CA    . ALA A 1 325 ? 13.50973  20.09159  12.12432  1.000 21.36917  ? 325  ALA A CA    1 
ATOM   2652 C  C     . ALA A 1 325 ? 13.51447  21.14882  11.03167  1.000 21.44066  ? 325  ALA A C     1 
ATOM   2653 O  O     . ALA A 1 325 ? 12.47832  21.78239  10.80276  1.000 21.45396  ? 325  ALA A O     1 
ATOM   2654 C  CB    . ALA A 1 325 ? 13.34060  20.77550  13.48216  1.000 21.27081  ? 325  ALA A CB    1 
ATOM   2655 N  N     . GLN A 1 326 ? 14.64393  21.36014  10.36326  1.000 23.00747  ? 326  GLN A N     1 
ATOM   2656 C  CA    . GLN A 1 326 ? 14.76677  22.39238  9.34773   1.000 23.57898  ? 326  GLN A CA    1 
ATOM   2657 C  C     . GLN A 1 326 ? 14.90810  21.82420  7.94369   1.000 23.93282  ? 326  GLN A C     1 
ATOM   2658 O  O     . GLN A 1 326 ? 15.00232  22.59679  6.98397   0.939 23.93029  ? 326  GLN A O     1 
ATOM   2659 C  CB    . GLN A 1 326 ? 15.96462  23.29647  9.66788   1.000 24.21156  ? 326  GLN A CB    1 
ATOM   2660 C  CG    . GLN A 1 326 ? 15.85609  24.06476  10.98844  1.000 24.29328  ? 326  GLN A CG    1 
ATOM   2661 C  CD    . GLN A 1 326 ? 14.50484  24.73438  11.20095  0.338 25.83077  ? 326  GLN A CD    1 
ATOM   2662 O  OE1   . GLN A 1 326 ? 13.86277  25.19413  10.25441  0.644 25.73042  ? 326  GLN A OE1   1 
ATOM   2663 N  NE2   . GLN A 1 326 ? 14.06724  24.78806  12.45380  0.461 25.74498  ? 326  GLN A NE2   1 
ATOM   2664 N  N     . ARG A 1 327 ? 14.92142  20.50200  7.79514   1.000 32.50804  ? 327  ARG A N     1 
ATOM   2665 C  CA    . ARG A 1 327 ? 15.10976  19.90101  6.48240   1.000 32.54612  ? 327  ARG A CA    1 
ATOM   2666 C  C     . ARG A 1 327 ? 13.85694  20.06122  5.63042   1.000 32.25738  ? 327  ARG A C     1 
ATOM   2667 O  O     . ARG A 1 327 ? 12.73120  19.91558  6.11466   1.000 32.17436  ? 327  ARG A O     1 
ATOM   2668 C  CB    . ARG A 1 327 ? 15.46764  18.42089  6.61916   1.000 32.04404  ? 327  ARG A CB    1 
ATOM   2669 C  CG    . ARG A 1 327 ? 16.75596  18.16380  7.38566   1.000 32.07185  ? 327  ARG A CG    1 
ATOM   2670 C  CD    . ARG A 1 327 ? 17.90486  17.83081  6.44712   1.000 33.31043  ? 327  ARG A CD    1 
ATOM   2671 N  NE    . ARG A 1 327 ? 19.14055  17.55809  7.17180   1.000 32.66595  ? 327  ARG A NE    1 
ATOM   2672 C  CZ    . ARG A 1 327 ? 20.25938  18.25739  7.03649   1.000 33.97856  ? 327  ARG A CZ    1 
ATOM   2673 N  NH1   . ARG A 1 327 ? 20.33710  19.28436  6.20566   1.000 32.83109  ? 327  ARG A NH1   1 
ATOM   2674 N  NH2   . ARG A 1 327 ? 21.32771  17.91734  7.75244   1.000 33.36493  ? 327  ARG A NH2   1 
ATOM   2675 N  N     . ASN A 1 328 ? 14.06297  20.36950  4.34552   1.000 23.86880  ? 328  ASN A N     1 
ATOM   2676 C  CA    . ASN A 1 328 ? 12.99294  20.54070  3.36494   1.000 23.81238  ? 328  ASN A CA    1 
ATOM   2677 C  C     . ASN A 1 328 ? 13.52805  20.03641  2.02182   1.000 24.52670  ? 328  ASN A C     1 
ATOM   2678 O  O     . ASN A 1 328 ? 13.84251  20.79827  1.10822   1.000 24.30035  ? 328  ASN A O     1 
ATOM   2679 C  CB    . ASN A 1 328 ? 12.52498  21.99550  3.28412   1.000 24.23939  ? 328  ASN A CB    1 
ATOM   2680 C  CG    . ASN A 1 328 ? 11.27587  22.16336  2.43714   1.000 25.19456  ? 328  ASN A CG    1 
ATOM   2681 O  OD1   . ASN A 1 328 ? 10.67055  21.18526  1.99553   1.000 24.16055  ? 328  ASN A OD1   1 
ATOM   2682 N  ND2   . ASN A 1 328 ? 10.88539  23.41102  2.20499   1.000 24.45546  ? 328  ASN A ND2   1 
ATOM   2683 N  N     . ALA A 1 329 ? 13.62002  18.70830  1.90304   1.000 27.84536  ? 329  ALA A N     1 
ATOM   2684 C  CA    . ALA A 1 329 ? 14.31590  18.09667  0.77445   1.000 27.67637  ? 329  ALA A CA    1 
ATOM   2685 C  C     . ALA A 1 329 ? 13.63442  18.38263  -0.55792  1.000 27.51369  ? 329  ALA A C     1 
ATOM   2686 O  O     . ALA A 1 329 ? 14.31058  18.45941  -1.58924  1.000 28.68149  ? 329  ALA A O     1 
ATOM   2687 C  CB    . ALA A 1 329 ? 14.43172  16.58867  0.98927   1.000 26.67116  ? 329  ALA A CB    1 
ATOM   2688 N  N     . LEU A 1 330 ? 12.31285  18.53644  -0.56808  1.000 21.62474  ? 330  LEU A N     1 
ATOM   2689 C  CA    . LEU A 1 330 ? 11.57540  18.74948  -1.80608  1.000 22.82204  ? 330  LEU A CA    1 
ATOM   2690 C  C     . LEU A 1 330 ? 11.23587  20.21519  -2.05038  1.000 22.66619  ? 330  LEU A C     1 
ATOM   2691 O  O     . LEU A 1 330 ? 10.54095  20.52219  -3.02464  1.000 23.29921  ? 330  LEU A O     1 
ATOM   2692 C  CB    . LEU A 1 330 ? 10.29977  17.90515  -1.81104  1.000 21.87665  ? 330  LEU A CB    1 
ATOM   2693 C  CG    . LEU A 1 330 ? 10.51966  16.40364  -1.60884  1.000 21.85401  ? 330  LEU A CG    1 
ATOM   2694 C  CD1   . LEU A 1 330 ? 9.21003   15.64037  -1.72006  1.000 21.68644  ? 330  LEU A CD1   1 
ATOM   2695 C  CD2   . LEU A 1 330 ? 11.54138  15.87138  -2.60422  1.000 22.09620  ? 330  LEU A CD2   1 
ATOM   2696 N  N     . ASP A 1 331 ? 11.71776  21.12190  -1.19705  1.000 33.85175  ? 331  ASP A N     1 
ATOM   2697 C  CA    . ASP A 1 331 ? 11.46556  22.55832  -1.33268  1.000 34.48798  ? 331  ASP A CA    1 
ATOM   2698 C  C     . ASP A 1 331 ? 9.96681   22.85748  -1.38664  1.000 34.23064  ? 331  ASP A C     1 
ATOM   2699 O  O     . ASP A 1 331 ? 9.49099   23.62549  -2.22527  1.000 34.48531  ? 331  ASP A O     1 
ATOM   2700 C  CB    . ASP A 1 331 ? 12.18456  23.13406  -2.55721  1.000 34.89395  ? 331  ASP A CB    1 
ATOM   2701 C  CG    . ASP A 1 331 ? 13.68586  23.23230  -2.36077  1.000 35.61443  ? 331  ASP A CG    1 
ATOM   2702 O  OD1   . ASP A 1 331 ? 14.43316  23.00068  -3.33550  1.000 37.57072  ? 331  ASP A OD1   1 
ATOM   2703 O  OD2   . ASP A 1 331 ? 14.11954  23.53948  -1.22976  1.000 35.57767  ? 331  ASP A OD2   1 
ATOM   2704 N  N     . ALA A 1 332 ? 9.21868   22.23473  -0.47841  1.000 21.74995  ? 332  ALA A N     1 
ATOM   2705 C  CA    . ALA A 1 332 ? 7.78609   22.47825  -0.37548  1.000 21.65370  ? 332  ALA A CA    1 
ATOM   2706 C  C     . ALA A 1 332 ? 7.53889   23.81638  0.30912   1.000 21.66442  ? 332  ALA A C     1 
ATOM   2707 O  O     . ALA A 1 332 ? 8.02741   24.05559  1.41792   1.000 21.13880  ? 332  ALA A O     1 
ATOM   2708 C  CB    . ALA A 1 332 ? 7.10458   21.35067  0.39756   1.000 20.63068  ? 332  ALA A CB    1 
ATOM   2709 N  N     . GLN A 1 333 ? 6.77758   24.68954  -0.35430  1.000 27.74326  ? 333  GLN A N     1 
ATOM   2710 C  CA    . GLN A 1 333 ? 6.56262   26.04697  0.12979   1.000 28.14655  ? 333  GLN A CA    1 
ATOM   2711 C  C     . GLN A 1 333 ? 5.08857   26.43350  0.18781   1.000 28.86954  ? 333  GLN A C     1 
ATOM   2712 O  O     . GLN A 1 333 ? 4.77959   27.60316  0.44216   1.000 28.96549  ? 333  GLN A O     1 
ATOM   2713 C  CB    . GLN A 1 333 ? 7.32178   27.05011  -0.74917  1.000 28.78520  ? 333  GLN A CB    1 
ATOM   2714 C  CG    . GLN A 1 333 ? 8.82665   26.82913  -0.79998  1.000 28.70489  ? 333  GLN A CG    1 
ATOM   2715 C  CD    . GLN A 1 333 ? 9.51054   27.17944  0.50697   1.000 28.80688  ? 333  GLN A CD    1 
ATOM   2716 O  OE1   . GLN A 1 333 ? 9.07833   28.08231  1.22348   1.000 29.71891  ? 333  GLN A OE1   1 
ATOM   2717 N  NE2   . GLN A 1 333 ? 10.58528  26.46607  0.82383   1.000 28.73555  ? 333  GLN A NE2   1 
ATOM   2718 N  N     . GLY A 1 334 ? 4.17178   25.49224  -0.03769  1.000 20.02076  ? 334  GLY A N     1 
ATOM   2719 C  CA    . GLY A 1 334 ? 2.76598   25.82682  -0.09683  1.000 19.87104  ? 334  GLY A CA    1 
ATOM   2720 C  C     . GLY A 1 334 ? 2.12787   25.97997  1.27085   1.000 19.52987  ? 334  GLY A C     1 
ATOM   2721 O  O     . GLY A 1 334 ? 2.68485   25.60574  2.30237   1.000 19.50072  ? 334  GLY A O     1 
ATOM   2722 N  N     . LYS A 1 335 ? 0.92656   26.54887  1.26467   1.000 25.38570  ? 335  LYS A N     1 
ATOM   2723 C  CA    . LYS A 1 335 ? 0.13314   26.70596  2.47339   1.000 25.86146  ? 335  LYS A CA    1 
ATOM   2724 C  C     . LYS A 1 335 ? -0.73755  25.47615  2.69890   1.000 25.33951  ? 335  LYS A C     1 
ATOM   2725 O  O     . LYS A 1 335 ? -1.07246  24.74554  1.76233   1.000 25.10071  ? 335  LYS A O     1 
ATOM   2726 C  CB    . LYS A 1 335 ? -0.74948  27.95255  2.38491   1.000 29.72773  ? 335  LYS A CB    1 
ATOM   2727 C  CG    . LYS A 1 335 ? -0.02290  29.25498  2.66162   1.000 30.10754  ? 335  LYS A CG    1 
ATOM   2728 C  CD    . LYS A 1 335 ? -0.36755  30.30196  1.61852   1.000 30.63186  ? 335  LYS A CD    1 
ATOM   2729 C  CE    . LYS A 1 335 ? -1.69285  30.97914  1.92327   0.562 30.80346  ? 335  LYS A CE    1 
ATOM   2730 N  NZ    . LYS A 1 335 ? -2.07196  31.94647  0.85496   0.830 31.28715  ? 335  LYS A NZ    1 
ATOM   2731 N  N     . LEU A 1 336 ? -1.10136  25.25313  3.95259   1.000 20.09147  ? 336  LEU A N     1 
ATOM   2732 C  CA    . LEU A 1 336 ? -1.99218  24.14537  4.27169   1.000 19.74490  ? 336  LEU A CA    1 
ATOM   2733 C  C     . LEU A 1 336 ? -3.42938  24.53349  3.93970   1.000 19.71212  ? 336  LEU A C     1 
ATOM   2734 O  O     . LEU A 1 336 ? -3.87611  25.61660  4.33022   1.000 20.44224  ? 336  LEU A O     1 
ATOM   2735 C  CB    . LEU A 1 336 ? -1.87298  23.76559  5.74503   1.000 19.39572  ? 336  LEU A CB    1 
ATOM   2736 C  CG    . LEU A 1 336 ? -2.56350  22.46903  6.17015   1.000 19.14180  ? 336  LEU A CG    1 
ATOM   2737 C  CD1   . LEU A 1 336 ? -1.86423  21.26614  5.56106   1.000 18.56061  ? 336  LEU A CD1   1 
ATOM   2738 C  CD2   . LEU A 1 336 ? -2.60596  22.35650  7.68656   1.000 18.99028  ? 336  LEU A CD2   1 
ATOM   2739 N  N     . PRO A 1 337 ? -4.17282  23.69178  3.21970   1.000 23.58691  ? 337  PRO A N     1 
ATOM   2740 C  CA    . PRO A 1 337 ? -5.54902  24.05122  2.85748   1.000 23.42813  ? 337  PRO A CA    1 
ATOM   2741 C  C     . PRO A 1 337 ? -6.44241  24.16942  4.08426   1.000 23.91793  ? 337  PRO A C     1 
ATOM   2742 O  O     . PRO A 1 337 ? -6.23141  23.51009  5.10478   1.000 23.83694  ? 337  PRO A O     1 
ATOM   2743 C  CB    . PRO A 1 337 ? -5.99468  22.89628  1.95095   1.000 23.20669  ? 337  PRO A CB    1 
ATOM   2744 C  CG    . PRO A 1 337 ? -4.73107  22.21901  1.51936   1.000 23.19334  ? 337  PRO A CG    1 
ATOM   2745 C  CD    . PRO A 1 337 ? -3.76893  22.39698  2.64895   1.000 22.90046  ? 337  PRO A CD    1 
ATOM   2746 N  N     . GLY A 1 338 ? -7.46340  25.01983  3.96414   1.000 21.63807  ? 338  GLY A N     1 
ATOM   2747 C  CA    . GLY A 1 338 ? -8.32746  25.29698  5.09798   1.000 21.78632  ? 338  GLY A CA    1 
ATOM   2748 C  C     . GLY A 1 338 ? -9.13218  24.10006  5.56480   1.000 21.55304  ? 338  GLY A C     1 
ATOM   2749 O  O     . GLY A 1 338 ? -9.51651  24.02762  6.73581   1.000 21.66996  ? 338  GLY A O     1 
ATOM   2750 N  N     . PHE A 1 339 ? -9.40068  23.14530  4.66964   1.000 20.12340  ? 339  PHE A N     1 
ATOM   2751 C  CA    . PHE A 1 339 ? -10.19334 21.99096  5.07697   1.000 20.17036  ? 339  PHE A CA    1 
ATOM   2752 C  C     . PHE A 1 339 ? -9.43676  21.04853  6.00586   1.000 19.83761  ? 339  PHE A C     1 
ATOM   2753 O  O     . PHE A 1 339 ? -10.04980 20.12452  6.54901   1.000 19.66810  ? 339  PHE A O     1 
ATOM   2754 C  CB    . PHE A 1 339 ? -10.71840 21.22670  3.85256   1.000 20.44824  ? 339  PHE A CB    1 
ATOM   2755 C  CG    . PHE A 1 339 ? -9.65429  20.79723  2.87182   1.000 19.97514  ? 339  PHE A CG    1 
ATOM   2756 C  CD1   . PHE A 1 339 ? -8.75752  19.78601  3.18529   1.000 19.31703  ? 339  PHE A CD1   1 
ATOM   2757 C  CD2   . PHE A 1 339 ? -9.58652  21.37631  1.61289   1.000 20.20997  ? 339  PHE A CD2   1 
ATOM   2758 C  CE1   . PHE A 1 339 ? -7.79463  19.38429  2.27632   1.000 19.51180  ? 339  PHE A CE1   1 
ATOM   2759 C  CE2   . PHE A 1 339 ? -8.62717  20.97650  0.69769   1.000 19.94337  ? 339  PHE A CE2   1 
ATOM   2760 C  CZ    . PHE A 1 339 ? -7.73001  19.97901  1.03097   1.000 19.35730  ? 339  PHE A CZ    1 
ATOM   2761 N  N     . TYR A 1 340 ? -8.13172  21.25057  6.20350   1.000 18.68868  ? 340  TYR A N     1 
ATOM   2762 C  CA    . TYR A 1 340 ? -7.42699  20.48073  7.22340   1.000 18.47669  ? 340  TYR A CA    1 
ATOM   2763 C  C     . TYR A 1 340 ? -7.92457  20.83012  8.61939   1.000 19.05623  ? 340  TYR A C     1 
ATOM   2764 O  O     . TYR A 1 340 ? -7.92345  19.97319  9.51147   1.000 18.78929  ? 340  TYR A O     1 
ATOM   2765 C  CB    . TYR A 1 340 ? -5.91888  20.71498  7.12236   1.000 18.09188  ? 340  TYR A CB    1 
ATOM   2766 C  CG    . TYR A 1 340 ? -5.20948  19.74384  6.20539   1.000 17.94045  ? 340  TYR A CG    1 
ATOM   2767 C  CD1   . TYR A 1 340 ? -5.28020  19.88550  4.82595   1.000 18.39652  ? 340  TYR A CD1   1 
ATOM   2768 C  CD2   . TYR A 1 340 ? -4.47374  18.68110  6.71819   1.000 17.54124  ? 340  TYR A CD2   1 
ATOM   2769 C  CE1   . TYR A 1 340 ? -4.63668  18.99978  3.98168   1.000 17.78982  ? 340  TYR A CE1   1 
ATOM   2770 C  CE2   . TYR A 1 340 ? -3.82532  17.78797  5.87931   1.000 17.16465  ? 340  TYR A CE2   1 
ATOM   2771 C  CZ    . TYR A 1 340 ? -3.91103  17.95435  4.51233   1.000 17.32721  ? 340  TYR A CZ    1 
ATOM   2772 O  OH    . TYR A 1 340 ? -3.27232  17.07510  3.66843   1.000 17.49822  ? 340  TYR A OH    1 
ATOM   2773 N  N     . TRP A 1 341 ? -8.35833  22.07393  8.82265   1.000 22.88597  ? 341  TRP A N     1 
ATOM   2774 C  CA    . TRP A 1 341 ? -8.90513  22.50540  10.10226  1.000 23.16866  ? 341  TRP A CA    1 
ATOM   2775 C  C     . TRP A 1 341 ? -10.42309 22.41138  10.15743  1.000 23.40032  ? 341  TRP A C     1 
ATOM   2776 O  O     . TRP A 1 341 ? -10.97917 22.11722  11.22190  1.000 23.81981  ? 341  TRP A O     1 
ATOM   2777 C  CB    . TRP A 1 341 ? -8.48271  23.94753  10.39755  1.000 23.99574  ? 341  TRP A CB    1 
ATOM   2778 C  CG    . TRP A 1 341 ? -7.00263  24.16008  10.38571  1.000 23.61681  ? 341  TRP A CG    1 
ATOM   2779 C  CD1   . TRP A 1 341 ? -6.27801  24.82423  9.43990   1.000 23.34720  ? 341  TRP A CD1   1 
ATOM   2780 C  CD2   . TRP A 1 341 ? -6.06338  23.71103  11.36938  1.000 23.05424  ? 341  TRP A CD2   1 
ATOM   2781 N  NE1   . TRP A 1 341 ? -4.94519  24.81503  9.77234   1.000 22.93822  ? 341  TRP A NE1   1 
ATOM   2782 C  CE2   . TRP A 1 341 ? -4.78681  24.13784  10.95286  1.000 22.61991  ? 341  TRP A CE2   1 
ATOM   2783 C  CE3   . TRP A 1 341 ? -6.17763  22.98782  12.56071  1.000 23.35106  ? 341  TRP A CE3   1 
ATOM   2784 C  CZ2   . TRP A 1 341 ? -3.63236  23.86495  11.68452  1.000 22.50402  ? 341  TRP A CZ2   1 
ATOM   2785 C  CZ3   . TRP A 1 341 ? -5.02981  22.71882  13.28650  1.000 22.68894  ? 341  TRP A CZ3   1 
ATOM   2786 C  CH2   . TRP A 1 341 ? -3.77480  23.15641  12.84573  1.000 22.55270  ? 341  TRP A CH2   1 
ATOM   2787 N  N     . THR A 1 342 ? -11.10685 22.65562  9.03865   1.000 27.64408  ? 342  THR A N     1 
ATOM   2788 C  CA    . THR A 1 342 ? -12.56337 22.68331  9.01797   1.000 28.50078  ? 342  THR A CA    1 
ATOM   2789 C  C     . THR A 1 342 ? -13.19286 21.39621  8.50505   1.000 28.28102  ? 342  THR A C     1 
ATOM   2790 O  O     . THR A 1 342 ? -14.37689 21.16076  8.76853   1.000 27.77271  ? 342  THR A O     1 
ATOM   2791 C  CB    . THR A 1 342 ? -13.06495 23.84648  8.15244   1.000 28.22773  ? 342  THR A CB    1 
ATOM   2792 O  OG1   . THR A 1 342 ? -12.86691 23.53121  6.76838   1.000 28.25297  ? 342  THR A OG1   1 
ATOM   2793 C  CG2   . THR A 1 342 ? -12.31728 25.12736  8.48854   1.000 28.42556  ? 342  THR A CG2   1 
ATOM   2794 N  N     . GLY A 1 343 ? -12.44508 20.56650  7.78160   1.000 26.33987  ? 343  GLY A N     1 
ATOM   2795 C  CA    . GLY A 1 343 ? -13.03368 19.38632  7.18311   1.000 26.00484  ? 343  GLY A CA    1 
ATOM   2796 C  C     . GLY A 1 343 ? -14.00488 19.66022  6.05896   1.000 27.05078  ? 343  GLY A C     1 
ATOM   2797 O  O     . GLY A 1 343 ? -14.70349 18.73844  5.62665   1.000 27.06439  ? 343  GLY A O     1 
ATOM   2798 N  N     . GLN A 1 344 ? -14.06907 20.89823  5.56666   1.000 32.46394  ? 344  GLN A N     1 
ATOM   2799 C  CA    . GLN A 1 344 ? -15.01620 21.27314  4.51578   1.000 33.36463  ? 344  GLN A CA    1 
ATOM   2800 C  C     . GLN A 1 344 ? -14.38509 21.03095  3.14406   1.000 32.90540  ? 344  GLN A C     1 
ATOM   2801 O  O     . GLN A 1 344 ? -13.97469 21.94719  2.42940   1.000 33.36583  ? 344  GLN A O     1 
ATOM   2802 C  CB    . GLN A 1 344 ? -15.45361 22.72246  4.68584   1.000 33.70149  ? 344  GLN A CB    1 
ATOM   2803 C  CG    . GLN A 1 344 ? -16.32037 22.96112  5.90799   1.000 33.81283  ? 344  GLN A CG    1 
ATOM   2804 C  CD    . GLN A 1 344 ? -17.48540 21.99688  5.98624   1.000 35.20942  ? 344  GLN A CD    1 
ATOM   2805 O  OE1   . GLN A 1 344 ? -18.33366 21.95372  5.09305   1.000 35.76534  ? 344  GLN A OE1   1 
ATOM   2806 N  NE2   . GLN A 1 344 ? -17.52815 21.20769  7.05453   1.000 34.49636  ? 344  GLN A NE2   1 
ATOM   2807 N  N     . THR A 1 345 ? -14.31769 19.75144  2.78479   1.000 23.85633  ? 345  THR A N     1 
ATOM   2808 C  CA    . THR A 1 345 ? -13.78920 19.32819  1.49771   1.000 23.85915  ? 345  THR A CA    1 
ATOM   2809 C  C     . THR A 1 345 ? -14.66101 18.21507  0.93785   1.000 24.15779  ? 345  THR A C     1 
ATOM   2810 O  O     . THR A 1 345 ? -15.21227 17.40084  1.68405   1.000 24.23463  ? 345  THR A O     1 
ATOM   2811 C  CB    . THR A 1 345 ? -12.33726 18.84028  1.60306   1.000 24.08291  ? 345  THR A CB    1 
ATOM   2812 O  OG1   . THR A 1 345 ? -11.96975 18.17209  0.39036   1.000 24.05821  ? 345  THR A OG1   1 
ATOM   2813 C  CG2   . THR A 1 345 ? -12.17844 17.87871  2.77364   1.000 23.15520  ? 345  THR A CG2   1 
ATOM   2814 N  N     . ASP A 1 346 ? -14.77890 18.18780  -0.38808  1.000 38.00600  ? 346  ASP A N     1 
ATOM   2815 C  CA    . ASP A 1 346 ? -15.53535 17.14460  -1.06705  1.000 37.96580  ? 346  ASP A CA    1 
ATOM   2816 C  C     . ASP A 1 346 ? -14.76550 15.83504  -1.18070  1.000 37.59187  ? 346  ASP A C     1 
ATOM   2817 O  O     . ASP A 1 346 ? -15.30417 14.86406  -1.72318  1.000 38.35615  ? 346  ASP A O     1 
ATOM   2818 C  CB    . ASP A 1 346 ? -15.96158 17.62398  -2.45801  1.000 38.41673  ? 346  ASP A CB    1 
ATOM   2819 C  CG    . ASP A 1 346 ? -17.23373 18.45079  -2.42332  1.000 40.00343  ? 346  ASP A CG    1 
ATOM   2820 O  OD1   . ASP A 1 346 ? -17.92747 18.43502  -1.38397  1.000 40.27197  ? 346  ASP A OD1   1 
ATOM   2821 O  OD2   . ASP A 1 346 ? -17.54311 19.11276  -3.43665  1.000 41.51328  ? 346  ASP A OD2   1 
ATOM   2822 N  N     . MET A 1 347 ? -13.52929 15.78293  -0.68961  1.000 27.89193  ? 347  MET A N     1 
ATOM   2823 C  CA    . MET A 1 347 ? -12.76994 14.53870  -0.64537  1.000 28.27760  ? 347  MET A CA    1 
ATOM   2824 C  C     . MET A 1 347 ? -13.23748 13.74675  0.56651   1.000 27.97239  ? 347  MET A C     1 
ATOM   2825 O  O     . MET A 1 347 ? -12.94791 14.12503  1.70506   1.000 27.63326  ? 347  MET A O     1 
ATOM   2826 C  CB    . MET A 1 347 ? -11.27376 14.81459  -0.55082  1.000 28.34889  ? 347  MET A CB    1 
ATOM   2827 C  CG    . MET A 1 347 ? -10.74487 15.88687  -1.47469  1.000 28.20444  ? 347  MET A CG    1 
ATOM   2828 S  SD    . MET A 1 347 ? -9.03839  15.52766  -1.91375  1.000 29.10998  ? 347  MET A SD    1 
ATOM   2829 C  CE    . MET A 1 347 ? -8.26457  17.07894  -1.50178  1.000 28.00067  ? 347  MET A CE    1 
ATOM   2830 N  N     . ALA A 1 348 ? -13.95968 12.64989  0.32709   1.000 24.38744  ? 348  ALA A N     1 
ATOM   2831 C  CA    . ALA A 1 348 ? -14.52139 11.87797  1.43138   1.000 24.54527  ? 348  ALA A CA    1 
ATOM   2832 C  C     . ALA A 1 348 ? -13.42997 11.33151  2.34540   1.000 23.95998  ? 348  ALA A C     1 
ATOM   2833 O  O     . ALA A 1 348 ? -13.57319 11.35020  3.57340   1.000 23.99501  ? 348  ALA A O     1 
ATOM   2834 C  CB    . ALA A 1 348 ? -15.38774 10.74324  0.88648   1.000 24.39755  ? 348  ALA A CB    1 
ATOM   2835 N  N     . CYS A 1 349 ? -12.32743 10.85106  1.76639   1.000 21.98278  ? 349  CYS A N     1 
ATOM   2836 C  CA    . CYS A 1 349 ? -11.25321 10.27844  2.57282   1.000 21.61474  ? 349  CYS A CA    1 
ATOM   2837 C  C     . CYS A 1 349 ? -10.63396 11.32681  3.48963   1.000 21.71821  ? 349  CYS A C     1 
ATOM   2838 O  O     . CYS A 1 349 ? -10.41328 11.07632  4.68068   1.000 21.22848  ? 349  CYS A O     1 
ATOM   2839 C  CB    . CYS A 1 349 ? -10.18867 9.66483   1.66387   1.000 21.43181  ? 349  CYS A CB    1 
ATOM   2840 S  SG    . CYS A 1 349 ? -9.58477  10.78858  0.37988   1.000 22.55012  ? 349  CYS A SG    1 
ATOM   2841 N  N     . VAL A 1 350 ? -10.34216 12.51101  2.94723   1.000 19.73404  ? 350  VAL A N     1 
ATOM   2842 C  CA    . VAL A 1 350 ? -9.75010  13.57144  3.75593   1.000 18.86599  ? 350  VAL A CA    1 
ATOM   2843 C  C     . VAL A 1 350 ? -10.75338 14.08418  4.77984   1.000 19.45543  ? 350  VAL A C     1 
ATOM   2844 O  O     . VAL A 1 350 ? -10.40506 14.32989  5.94128   1.000 19.11909  ? 350  VAL A O     1 
ATOM   2845 C  CB    . VAL A 1 350 ? -9.23399  14.70622  2.85253   1.000 19.18899  ? 350  VAL A CB    1 
ATOM   2846 C  CG1   . VAL A 1 350 ? -8.66144  15.83880  3.69136   1.000 18.94753  ? 350  VAL A CG1   1 
ATOM   2847 C  CG2   . VAL A 1 350 ? -8.19487  14.17810  1.87685   1.000 19.15518  ? 350  VAL A CG2   1 
ATOM   2848 N  N     . ALA A 1 351 ? -12.01385 14.24916  4.37009   1.000 18.68166  ? 351  ALA A N     1 
ATOM   2849 C  CA    . ALA A 1 351 ? -13.02752 14.76128  5.28572   1.000 19.05657  ? 351  ALA A CA    1 
ATOM   2850 C  C     . ALA A 1 351 ? -13.23212 13.82216  6.46757   1.000 18.58904  ? 351  ALA A C     1 
ATOM   2851 O  O     . ALA A 1 351 ? -13.43300 14.27436  7.60076   1.000 18.87392  ? 351  ALA A O     1 
ATOM   2852 C  CB    . ALA A 1 351 ? -14.34385 14.98412  4.54185   1.000 19.51885  ? 351  ALA A CB    1 
ATOM   2853 N  N     . ASP A 1 352 ? -13.17489 12.51015  6.22648   1.000 21.00724  ? 352  ASP A N     1 
ATOM   2854 C  CA    . ASP A 1 352 ? -13.35576 11.55505  7.31494   1.000 21.09871  ? 352  ASP A CA    1 
ATOM   2855 C  C     . ASP A 1 352 ? -12.17121 11.55781  8.27177   1.000 20.62621  ? 352  ASP A C     1 
ATOM   2856 O  O     . ASP A 1 352 ? -12.34992 11.34501  9.47591   1.000 20.62624  ? 352  ASP A O     1 
ATOM   2857 C  CB    . ASP A 1 352 ? -13.57922 10.15131  6.75283   1.000 21.09656  ? 352  ASP A CB    1 
ATOM   2858 C  CG    . ASP A 1 352 ? -14.23138 9.21955   7.75502   1.000 21.03895  ? 352  ASP A CG    1 
ATOM   2859 O  OD1   . ASP A 1 352 ? -15.15463 9.66173   8.46881   1.000 21.18864  ? 352  ASP A OD1   1 
ATOM   2860 O  OD2   . ASP A 1 352 ? -13.82058 8.04301   7.82906   1.000 21.61459  ? 352  ASP A OD2   1 
ATOM   2861 N  N     . THR A 1 353 ? -10.96131 11.79203  7.76176   1.000 20.11645  ? 353  THR A N     1 
ATOM   2862 C  CA    . THR A 1 353 ? -9.78942  11.83503  8.62984   1.000 19.59805  ? 353  THR A CA    1 
ATOM   2863 C  C     . THR A 1 353 ? -9.82134  13.06554  9.52723   1.000 19.97107  ? 353  THR A C     1 
ATOM   2864 O  O     . THR A 1 353 ? -9.57717  12.97224  10.73601  1.000 19.75492  ? 353  THR A O     1 
ATOM   2865 C  CB    . THR A 1 353 ? -8.51381  11.81128  7.78816   1.000 20.03066  ? 353  THR A CB    1 
ATOM   2866 O  OG1   . THR A 1 353 ? -8.44872  10.57996  7.05808   1.000 20.88013  ? 353  THR A OG1   1 
ATOM   2867 C  CG2   . THR A 1 353 ? -7.28434  11.93068  8.67633   1.000 19.37965  ? 353  THR A CG2   1 
ATOM   2868 N  N     . VAL A 1 354 ? -10.12723 14.23051  8.95030   1.000 17.03013  ? 354  VAL A N     1 
ATOM   2869 C  CA    . VAL A 1 354 ? -10.24081 15.44966  9.74555   1.000 17.04245  ? 354  VAL A CA    1 
ATOM   2870 C  C     . VAL A 1 354 ? -11.38741 15.32772  10.74035  1.000 17.27156  ? 354  VAL A C     1 
ATOM   2871 O  O     . VAL A 1 354 ? -11.30270 15.81900  11.87352  1.000 17.81115  ? 354  VAL A O     1 
ATOM   2872 C  CB    . VAL A 1 354 ? -10.41276 16.67158  8.82324   1.000 17.64019  ? 354  VAL A CB    1 
ATOM   2873 C  CG1   . VAL A 1 354 ? -10.63991 17.93928  9.63932   1.000 18.04216  ? 354  VAL A CG1   1 
ATOM   2874 C  CG2   . VAL A 1 354 ? -9.20103  16.82131  7.91183   1.000 17.37851  ? 354  VAL A CG2   1 
ATOM   2875 N  N     . ARG A 1 355 ? -12.47360 14.66335  10.33691  1.000 25.43722  ? 355  ARG A N     1 
ATOM   2876 C  CA    . ARG A 1 355 ? -13.60058 14.46533  11.24258  1.000 25.63575  ? 355  ARG A CA    1 
ATOM   2877 C  C     . ARG A 1 355 ? -13.18768 13.66054  12.46803  1.000 25.43805  ? 355  ARG A C     1 
ATOM   2878 O  O     . ARG A 1 355 ? -13.57745 13.98709  13.59509  1.000 25.66151  ? 355  ARG A O     1 
ATOM   2879 C  CB    . ARG A 1 355 ? -14.74647 13.77484  10.50438  1.000 26.11300  ? 355  ARG A CB    1 
ATOM   2880 C  CG    . ARG A 1 355 ? -15.93252 13.40645  11.37716  1.000 25.71642  ? 355  ARG A CG    1 
ATOM   2881 C  CD    . ARG A 1 355 ? -16.79430 12.36771  10.68176  1.000 27.12564  ? 355  ARG A CD    1 
ATOM   2882 N  NE    . ARG A 1 355 ? -18.02561 12.08181  11.40904  1.000 28.35606  ? 355  ARG A NE    1 
ATOM   2883 C  CZ    . ARG A 1 355 ? -19.12422 12.82200  11.34747  1.000 28.19548  ? 355  ARG A CZ    1 
ATOM   2884 N  NH1   . ARG A 1 355 ? -19.17990 13.91728  10.60673  1.000 28.17342  ? 355  ARG A NH1   1 
ATOM   2885 N  NH2   . ARG A 1 355 ? -20.19544 12.45139  12.04401  1.000 28.67656  ? 355  ARG A NH2   1 
ATOM   2886 N  N     . ALA A 1 356 ? -12.39203 12.60770  12.26874  1.000 14.96730  ? 356  ALA A N     1 
ATOM   2887 C  CA    . ALA A 1 356 ? -11.91454 11.82062  13.40082  1.000 14.95071  ? 356  ALA A CA    1 
ATOM   2888 C  C     . ALA A 1 356 ? -10.93579 12.61828  14.25295  1.000 15.08274  ? 356  ALA A C     1 
ATOM   2889 O  O     . ALA A 1 356 ? -10.94499 12.50982  15.48499  1.000 15.11257  ? 356  ALA A O     1 
ATOM   2890 C  CB    . ALA A 1 356 ? -11.26881 10.52698  12.90645  1.000 14.48791  ? 356  ALA A CB    1 
ATOM   2891 N  N     . ALA A 1 357 ? -10.08284 13.42408  13.61550  1.000 17.57333  ? 357  ALA A N     1 
ATOM   2892 C  CA    . ALA A 1 357 ? -9.16986  14.27559  14.37063  1.000 18.10719  ? 357  ALA A CA    1 
ATOM   2893 C  C     . ALA A 1 357 ? -9.93429  15.28605  15.21593  1.000 18.48194  ? 357  ALA A C     1 
ATOM   2894 O  O     . ALA A 1 357 ? -9.56988  15.54647  16.36805  1.000 18.60536  ? 357  ALA A O     1 
ATOM   2895 C  CB    . ALA A 1 357 ? -8.20793  14.98877  13.41971  1.000 18.17259  ? 357  ALA A CB    1 
ATOM   2896 N  N     . HIS A 1 358 ? -11.00733 15.85535  14.66495  1.000 21.20670  ? 358  HIS A N     1 
ATOM   2897 C  CA    . HIS A 1 358 ? -11.78058 16.85021  15.40068  1.000 21.75135  ? 358  HIS A CA    1 
ATOM   2898 C  C     . HIS A 1 358 ? -12.56405 16.21075  16.54160  1.000 21.86952  ? 358  HIS A C     1 
ATOM   2899 O  O     . HIS A 1 358 ? -12.57211 16.72372  17.66671  1.000 21.79197  ? 358  HIS A O     1 
ATOM   2900 C  CB    . HIS A 1 358 ? -12.72262 17.58631  14.44691  1.000 21.80302  ? 358  HIS A CB    1 
ATOM   2901 C  CG    . HIS A 1 358 ? -13.56776 18.62641  15.11421  1.000 23.08621  ? 358  HIS A CG    1 
ATOM   2902 N  ND1   . HIS A 1 358 ? -14.73586 18.32251  15.78093  1.000 23.44033  ? 358  HIS A ND1   1 
ATOM   2903 C  CD2   . HIS A 1 358 ? -13.41459 19.96778  15.21693  1.000 22.91006  ? 358  HIS A CD2   1 
ATOM   2904 C  CE1   . HIS A 1 358 ? -15.26493 19.43149  16.26642  1.000 22.88345  ? 358  HIS A CE1   1 
ATOM   2905 N  NE2   . HIS A 1 358 ? -14.48270 20.44391  15.93816  1.000 23.61881  ? 358  HIS A NE2   1 
ATOM   2906 N  N     . ASP A 1 359 ? -13.22484 15.08326  16.27141  1.000 26.05003  ? 359  ASP A N     1 
ATOM   2907 C  CA    . ASP A 1 359 ? -14.14046 14.50065  17.24611  1.000 25.91892  ? 359  ASP A CA    1 
ATOM   2908 C  C     . ASP A 1 359 ? -13.42493 13.66892  18.30363  1.000 25.34216  ? 359  ASP A C     1 
ATOM   2909 O  O     . ASP A 1 359 ? -13.87080 13.62981  19.45610  1.000 25.38739  ? 359  ASP A O     1 
ATOM   2910 C  CB    . ASP A 1 359 ? -15.18709 13.64233  16.53174  1.000 25.28695  ? 359  ASP A CB    1 
ATOM   2911 C  CG    . ASP A 1 359 ? -16.20071 14.47408  15.76532  1.000 25.83713  ? 359  ASP A CG    1 
ATOM   2912 O  OD1   . ASP A 1 359 ? -16.14423 15.71871  15.85451  1.000 27.00172  ? 359  ASP A OD1   1 
ATOM   2913 O  OD2   . ASP A 1 359 ? -17.05382 13.88378  15.07057  1.000 26.40567  ? 359  ASP A OD2   1 
ATOM   2914 N  N     . HIS A 1 360 ? -12.32655 13.00282  17.94479  1.000 21.99502  ? 360  HIS A N     1 
ATOM   2915 C  CA    . HIS A 1 360 ? -11.66907 12.07638  18.85495  1.000 21.84347  ? 360  HIS A CA    1 
ATOM   2916 C  C     . HIS A 1 360 ? -10.19190 12.36494  19.07589  1.000 21.95702  ? 360  HIS A C     1 
ATOM   2917 O  O     . HIS A 1 360 ? -9.56184  11.66464  19.87712  1.000 21.47905  ? 360  HIS A O     1 
ATOM   2918 C  CB    . HIS A 1 360 ? -11.81566 10.63402  18.34636  1.000 20.94089  ? 360  HIS A CB    1 
ATOM   2919 C  CG    . HIS A 1 360 ? -13.21099 10.27381  17.94579  1.000 21.04489  ? 360  HIS A CG    1 
ATOM   2920 N  ND1   . HIS A 1 360 ? -14.23088 10.11670  18.85926  1.000 21.20458  ? 360  HIS A ND1   1 
ATOM   2921 C  CD2   . HIS A 1 360 ? -13.75643 10.04064  16.72885  1.000 20.92117  ? 360  HIS A CD2   1 
ATOM   2922 C  CE1   . HIS A 1 360 ? -15.34440 9.80096   18.22245  1.000 21.88508  ? 360  HIS A CE1   1 
ATOM   2923 N  NE2   . HIS A 1 360 ? -15.08370 9.74836   16.92861  1.000 21.14134  ? 360  HIS A NE2   1 
ATOM   2924 N  N     . ALA A 1 361 ? -9.62393  13.36339  18.39586  1.000 14.30293  ? 361  ALA A N     1 
ATOM   2925 C  CA    . ALA A 1 361 ? -8.18986  13.64700  18.46604  1.000 15.09170  ? 361  ALA A CA    1 
ATOM   2926 C  C     . ALA A 1 361 ? -7.37562  12.40867  18.10171  1.000 14.70765  ? 361  ALA A C     1 
ATOM   2927 O  O     . ALA A 1 361 ? -6.33100  12.12495  18.69244  1.000 14.13128  ? 361  ALA A O     1 
ATOM   2928 C  CB    . ALA A 1 361 ? -7.79518  14.17902  19.84554  1.000 15.13114  ? 361  ALA A CB    1 
ATOM   2929 N  N     . TYR A 1 362 ? -7.86339  11.66159  17.11341  1.000 14.86223  ? 362  TYR A N     1 
ATOM   2930 C  CA    . TYR A 1 362 ? -7.23356  10.40894  16.73314  1.000 14.15897  ? 362  TYR A CA    1 
ATOM   2931 C  C     . TYR A 1 362 ? -7.52717  10.09432  15.27373  1.000 13.80872  ? 362  TYR A C     1 
ATOM   2932 O  O     . TYR A 1 362 ? -8.60484  10.39856  14.75601  1.000 14.44466  ? 362  TYR A O     1 
ATOM   2933 C  CB    . TYR A 1 362 ? -7.71177  9.25124   17.61825  1.000 13.75512  ? 362  TYR A CB    1 
ATOM   2934 C  CG    . TYR A 1 362 ? -7.19738  7.90035   17.17987  1.000 13.42917  ? 362  TYR A CG    1 
ATOM   2935 C  CD1   . TYR A 1 362 ? -5.98220  7.41769   17.64178  1.000 13.52755  ? 362  TYR A CD1   1 
ATOM   2936 C  CD2   . TYR A 1 362 ? -7.92655  7.10804   16.30089  1.000 13.51605  ? 362  TYR A CD2   1 
ATOM   2937 C  CE1   . TYR A 1 362 ? -5.50851  6.18339   17.24317  1.000 13.13721  ? 362  TYR A CE1   1 
ATOM   2938 C  CE2   . TYR A 1 362 ? -7.45881  5.87825   15.89320  1.000 13.53294  ? 362  TYR A CE2   1 
ATOM   2939 C  CZ    . TYR A 1 362 ? -6.25033  5.41988   16.36696  1.000 13.60960  ? 362  TYR A CZ    1 
ATOM   2940 O  OH    . TYR A 1 362 ? -5.78669  4.18871   15.96475  1.000 13.71541  ? 362  TYR A OH    1 
ATOM   2941 N  N     . ALA A 1 363 ? -6.54634  9.47379   14.62433  1.000 17.32417  ? 363  ALA A N     1 
ATOM   2942 C  CA    . ALA A 1 363 ? -6.71256  8.83073   13.33001  1.000 17.57473  ? 363  ALA A CA    1 
ATOM   2943 C  C     . ALA A 1 363 ? -5.64699  7.75068   13.23952  1.000 17.19766  ? 363  ALA A C     1 
ATOM   2944 O  O     . ALA A 1 363 ? -4.50621  7.97417   13.65274  1.000 17.40569  ? 363  ALA A O     1 
ATOM   2945 C  CB    . ALA A 1 363 ? -6.58408  9.82541   12.16970  1.000 17.40979  ? 363  ALA A CB    1 
ATOM   2946 N  N     . HIS A 1 364 ? -6.01489  6.57904   12.72553  1.000 18.49715  ? 364  HIS A N     1 
ATOM   2947 C  CA    . HIS A 1 364 ? -5.03569  5.50539   12.74721  1.000 19.05640  ? 364  HIS A CA    1 
ATOM   2948 C  C     . HIS A 1 364 ? -3.99027  5.70824   11.64950  1.000 19.46968  ? 364  HIS A C     1 
ATOM   2949 O  O     . HIS A 1 364 ? -4.08241  6.61663   10.81818  1.000 19.11754  ? 364  HIS A O     1 
ATOM   2950 C  CB    . HIS A 1 364 ? -5.70936  4.13225   12.65120  1.000 19.41124  ? 364  HIS A CB    1 
ATOM   2951 C  CG    . HIS A 1 364 ? -6.63563  3.96820   11.48659  1.000 19.76187  ? 364  HIS A CG    1 
ATOM   2952 N  ND1   . HIS A 1 364 ? -6.18825  3.76949   10.19835  1.000 20.12091  ? 364  HIS A ND1   1 
ATOM   2953 C  CD2   . HIS A 1 364 ? -7.98765  3.92926   11.42517  1.000 19.49663  ? 364  HIS A CD2   1 
ATOM   2954 C  CE1   . HIS A 1 364 ? -7.22489  3.63556   9.39047   1.000 20.44457  ? 364  HIS A CE1   1 
ATOM   2955 N  NE2   . HIS A 1 364 ? -8.32869  3.72951   10.10973  1.000 20.10371  ? 364  HIS A NE2   1 
ATOM   2956 N  N     . HIS A 1 365 ? -2.98058  4.83426   11.66623  1.000 18.24896  ? 365  HIS A N     1 
ATOM   2957 C  CA    . HIS A 1 365 ? -1.71294  5.11861   10.99761  1.000 18.05936  ? 365  HIS A CA    1 
ATOM   2958 C  C     . HIS A 1 365 ? -1.88961  5.34614   9.50001   1.000 18.87896  ? 365  HIS A C     1 
ATOM   2959 O  O     . HIS A 1 365 ? -1.37397  6.32436   8.94700   1.000 18.78435  ? 365  HIS A O     1 
ATOM   2960 C  CB    . HIS A 1 365 ? -0.72823  3.97784   11.25192  1.000 18.25206  ? 365  HIS A CB    1 
ATOM   2961 C  CG    . HIS A 1 365 ? 0.62046   4.20013   10.64310  1.000 18.71300  ? 365  HIS A CG    1 
ATOM   2962 N  ND1   . HIS A 1 365 ? 1.49435   5.16202   11.10169  1.000 18.27915  ? 365  HIS A ND1   1 
ATOM   2963 C  CD2   . HIS A 1 365 ? 1.24114   3.59192   9.60473   1.000 19.15834  ? 365  HIS A CD2   1 
ATOM   2964 C  CE1   . HIS A 1 365 ? 2.59831   5.13212   10.37676  1.000 18.35485  ? 365  HIS A CE1   1 
ATOM   2965 N  NE2   . HIS A 1 365 ? 2.46986   4.18898   9.46094   1.000 18.92583  ? 365  HIS A NE2   1 
ATOM   2966 N  N     . ILE A 1 366 ? -2.60737  4.44937   8.82102   1.000 20.61598  ? 366  ILE A N     1 
ATOM   2967 C  CA    . ILE A 1 366 ? -2.65551  4.52521   7.36341   1.000 21.54739  ? 366  ILE A CA    1 
ATOM   2968 C  C     . ILE A 1 366 ? -3.38363  5.78437   6.89542   1.000 21.00060  ? 366  ILE A C     1 
ATOM   2969 O  O     . ILE A 1 366 ? -3.10963  6.28910   5.80000   1.000 21.13860  ? 366  ILE A O     1 
ATOM   2970 C  CB    . ILE A 1 366 ? -3.27668  3.24072   6.77643   1.000 22.01648  ? 366  ILE A CB    1 
ATOM   2971 C  CG1   . ILE A 1 366 ? -2.74005  2.98376   5.36509   1.000 22.68279  ? 366  ILE A CG1   1 
ATOM   2972 C  CG2   . ILE A 1 366 ? -4.79067  3.31221   6.77424   1.000 21.61389  ? 366  ILE A CG2   1 
ATOM   2973 C  CD1   . ILE A 1 366 ? -1.28532  2.55928   5.33059   1.000 23.47360  ? 366  ILE A CD1   1 
ATOM   2974 N  N     . GLN A 1 367 ? -4.29883  6.32736   7.70723   1.000 24.81500  ? 367  GLN A N     1 
ATOM   2975 C  CA    . GLN A 1 367 ? -4.92618  7.59886   7.35036   1.000 24.54788  ? 367  GLN A CA    1 
ATOM   2976 C  C     . GLN A 1 367 ? -3.95451  8.75833   7.52450   1.000 24.44311  ? 367  GLN A C     1 
ATOM   2977 O  O     . GLN A 1 367 ? -3.88004  9.64811   6.66869   1.000 24.76792  ? 367  GLN A O     1 
ATOM   2978 C  CB    . GLN A 1 367 ? -6.18287  7.84022   8.18795   1.000 24.35320  ? 367  GLN A CB    1 
ATOM   2979 C  CG    . GLN A 1 367 ? -7.24836  6.77249   8.05944   1.000 25.03657  ? 367  GLN A CG    1 
ATOM   2980 C  CD    . GLN A 1 367 ? -8.41313  6.99219   9.00827   1.000 25.35063  ? 367  GLN A CD    1 
ATOM   2981 O  OE1   . GLN A 1 367 ? -9.52492  7.30183   8.57993   1.000 25.85507  ? 367  GLN A OE1   1 
ATOM   2982 N  NE2   . GLN A 1 367 ? -8.16278  6.83649   10.30412  1.000 24.94082  ? 367  GLN A NE2   1 
ATOM   2983 N  N     . ARG A 1 368 ? -3.21335  8.77415   8.63548   1.000 18.35508  ? 368  ARG A N     1 
ATOM   2984 C  CA    . ARG A 1 368 ? -2.19469  9.80019   8.82733   1.000 18.14707  ? 368  ARG A CA    1 
ATOM   2985 C  C     . ARG A 1 368 ? -1.13994  9.74405   7.73230   1.000 18.85999  ? 368  ARG A C     1 
ATOM   2986 O  O     . ARG A 1 368 ? -0.61799  10.78437  7.31592   1.000 18.91867  ? 368  ARG A O     1 
ATOM   2987 C  CB    . ARG A 1 368 ? -1.53271  9.64048   10.19557  1.000 17.49981  ? 368  ARG A CB    1 
ATOM   2988 C  CG    . ARG A 1 368 ? -2.45979  9.82394   11.38142  1.000 17.37938  ? 368  ARG A CG    1 
ATOM   2989 C  CD    . ARG A 1 368 ? -1.66042  10.06744  12.65267  1.000 17.16390  ? 368  ARG A CD    1 
ATOM   2990 N  NE    . ARG A 1 368 ? -2.31076  9.48773   13.82162  1.000 17.78888  ? 368  ARG A NE    1 
ATOM   2991 C  CZ    . ARG A 1 368 ? -1.99631  9.77465   15.07816  1.000 17.69467  ? 368  ARG A CZ    1 
ATOM   2992 N  NH1   . ARG A 1 368 ? -1.02976  10.63021  15.37249  1.000 17.09285  ? 368  ARG A NH1   1 
ATOM   2993 N  NH2   . ARG A 1 368 ? -2.66970  9.18828   16.06452  1.000 17.66762  ? 368  ARG A NH2   1 
ATOM   2994 N  N     . LEU A 1 369 ? -0.82235  8.54458   7.24906   1.000 19.12208  ? 369  LEU A N     1 
ATOM   2995 C  CA    . LEU A 1 369 ? 0.22577   8.36671   6.25116   1.000 19.74771  ? 369  LEU A CA    1 
ATOM   2996 C  C     . LEU A 1 369 ? -0.29582  8.57650   4.83265   1.000 20.19263  ? 369  LEU A C     1 
ATOM   2997 O  O     . LEU A 1 369 ? 0.20978   9.42959   4.09623   1.000 20.33488  ? 369  LEU A O     1 
ATOM   2998 C  CB    . LEU A 1 369 ? 0.84349   6.96983   6.38815   1.000 19.73365  ? 369  LEU A CB    1 
ATOM   2999 C  CG    . LEU A 1 369 ? 2.01047   6.65177   5.45124   1.000 20.21719  ? 369  LEU A CG    1 
ATOM   3000 C  CD1   . LEU A 1 369 ? 3.22460   7.51232   5.77639   1.000 19.93759  ? 369  LEU A CD1   1 
ATOM   3001 C  CD2   . LEU A 1 369 ? 2.36327   5.17176   5.50830   1.000 20.43326  ? 369  LEU A CD2   1 
ATOM   3002 N  N     . MET A 1 370 ? -1.31420  7.81278   4.44663   1.000 22.15717  ? 370  MET A N     1 
ATOM   3003 C  CA    . MET A 1 370 ? -1.71327  7.69164   3.05263   1.000 22.69549  ? 370  MET A CA    1 
ATOM   3004 C  C     . MET A 1 370 ? -2.80200  8.67705   2.64077   1.000 22.84369  ? 370  MET A C     1 
ATOM   3005 O  O     . MET A 1 370 ? -3.01673  8.86599   1.43900   1.000 22.66909  ? 370  MET A O     1 
ATOM   3006 C  CB    . MET A 1 370 ? -2.18634  6.25905   2.78136   1.000 22.56723  ? 370  MET A CB    1 
ATOM   3007 C  CG    . MET A 1 370 ? -1.06444  5.22482   2.71851   1.000 22.91233  ? 370  MET A CG    1 
ATOM   3008 S  SD    . MET A 1 370 ? 0.53608   5.85643   2.18539   1.000 24.19971  ? 370  MET A SD    1 
ATOM   3009 C  CE    . MET A 1 370 ? 0.34359   5.76331   0.41161   1.000 24.83482  ? 370  MET A CE    1 
ATOM   3010 N  N     . VAL A 1 371 ? -3.49238  9.30905   3.59003   1.000 19.09535  ? 371  VAL A N     1 
ATOM   3011 C  CA    . VAL A 1 371 ? -4.55725  10.24529  3.24048   1.000 19.16503  ? 371  VAL A CA    1 
ATOM   3012 C  C     . VAL A 1 371 ? -4.06506  11.67710  3.41503   1.000 19.11348  ? 371  VAL A C     1 
ATOM   3013 O  O     . VAL A 1 371 ? -3.72858  12.34938  2.43480   1.000 19.45601  ? 371  VAL A O     1 
ATOM   3014 C  CB    . VAL A 1 371 ? -5.83124  9.99207   4.06927   1.000 19.46311  ? 371  VAL A CB    1 
ATOM   3015 C  CG1   . VAL A 1 371 ? -6.94294  10.94441  3.64320   1.000 18.48669  ? 371  VAL A CG1   1 
ATOM   3016 C  CG2   . VAL A 1 371 ? -6.28464  8.54446   3.92270   1.000 18.57121  ? 371  VAL A CG2   1 
ATOM   3017 N  N     . THR A 1 372 ? -4.01540  12.15437  4.66080   1.000 22.85842  ? 372  THR A N     1 
ATOM   3018 C  CA    . THR A 1 372 ? -3.64625  13.54598  4.90425   1.000 22.19171  ? 372  THR A CA    1 
ATOM   3019 C  C     . THR A 1 372 ? -2.14786  13.77676  4.73492   1.000 22.57722  ? 372  THR A C     1 
ATOM   3020 O  O     . THR A 1 372 ? -1.73309  14.84247  4.26581   1.000 22.69940  ? 372  THR A O     1 
ATOM   3021 C  CB    . THR A 1 372 ? -4.09678  13.97555  6.30145   1.000 21.70517  ? 372  THR A CB    1 
ATOM   3022 O  OG1   . THR A 1 372 ? -3.75348  12.96153  7.25340   1.000 21.45078  ? 372  THR A OG1   1 
ATOM   3023 C  CG2   . THR A 1 372 ? -5.60153  14.20071  6.32419   1.000 21.88273  ? 372  THR A CG2   1 
ATOM   3024 N  N     . GLY A 1 373 ? -1.32173  12.79956  5.11205   1.000 20.70534  ? 373  GLY A N     1 
ATOM   3025 C  CA    . GLY A 1 373 ? 0.11406   12.95668  4.93620   1.000 20.46472  ? 373  GLY A CA    1 
ATOM   3026 C  C     . GLY A 1 373 ? 0.51873   12.92140  3.47515   1.000 21.50510  ? 373  GLY A C     1 
ATOM   3027 O  O     . GLY A 1 373 ? 1.26846   13.78059  3.00171   1.000 21.19996  ? 373  GLY A O     1 
ATOM   3028 N  N     . ASN A 1 374 ? 0.01795   11.92699  2.74026   1.000 20.13138  ? 374  ASN A N     1 
ATOM   3029 C  CA    . ASN A 1 374 ? 0.29135   11.83861  1.31048   1.000 20.55555  ? 374  ASN A CA    1 
ATOM   3030 C  C     . ASN A 1 374 ? -0.19013  13.08614  0.57697   1.000 20.12122  ? 374  ASN A C     1 
ATOM   3031 O  O     . ASN A 1 374 ? 0.50737   13.60562  -0.30144  1.000 20.38479  ? 374  ASN A O     1 
ATOM   3032 C  CB    . ASN A 1 374 ? -0.36846  10.57948  0.74613   1.000 20.06841  ? 374  ASN A CB    1 
ATOM   3033 C  CG    . ASN A 1 374 ? -0.27891  10.49239  -0.76129  1.000 20.75159  ? 374  ASN A CG    1 
ATOM   3034 O  OD1   . ASN A 1 374 ? 0.78691   10.68328  -1.34711  1.000 21.10497  ? 374  ASN A OD1   1 
ATOM   3035 N  ND2   . ASN A 1 374 ? -1.40404  10.19504  -1.40023  1.000 20.84277  ? 374  ASN A ND2   1 
ATOM   3036 N  N     . LEU A 1 375 ? -1.36880  13.59676  0.94306   1.000 20.67821  ? 375  LEU A N     1 
ATOM   3037 C  CA    . LEU A 1 375 ? -1.92102  14.76294  0.25860   1.000 21.57296  ? 375  LEU A CA    1 
ATOM   3038 C  C     . LEU A 1 375 ? -1.05548  15.99962  0.47891   1.000 21.45793  ? 375  LEU A C     1 
ATOM   3039 O  O     . LEU A 1 375 ? -0.77673  16.74833  -0.46480  1.000 21.29063  ? 375  LEU A O     1 
ATOM   3040 C  CB    . LEU A 1 375 ? -3.35473  15.01809  0.72748   1.000 20.95450  ? 375  LEU A CB    1 
ATOM   3041 C  CG    . LEU A 1 375 ? -4.04556  16.24786  0.13266   1.000 21.34852  ? 375  LEU A CG    1 
ATOM   3042 C  CD1   . LEU A 1 375 ? -4.33462  16.04765  -1.34857  1.000 20.90839  ? 375  LEU A CD1   1 
ATOM   3043 C  CD2   . LEU A 1 375 ? -5.32126  16.58347  0.89094   1.000 20.74164  ? 375  LEU A CD2   1 
ATOM   3044 N  N     . ALA A 1 376 ? -0.62390  16.23373  1.72163   1.000 23.27178  ? 376  ALA A N     1 
ATOM   3045 C  CA    . ALA A 1 376 ? 0.22655   17.38750  2.00086   1.000 23.41237  ? 376  ALA A CA    1 
ATOM   3046 C  C     . ALA A 1 376 ? 1.54042   17.30197  1.23442   1.000 23.65451  ? 376  ALA A C     1 
ATOM   3047 O  O     . ALA A 1 376 ? 2.07880   18.32382  0.79131   1.000 24.46457  ? 376  ALA A O     1 
ATOM   3048 C  CB    . ALA A 1 376 ? 0.48594   17.49999  3.50249   1.000 22.57386  ? 376  ALA A CB    1 
ATOM   3049 N  N     . MET A 1 377 ? 2.07239   16.08920  1.07216   1.000 23.82027  ? 377  MET A N     1 
ATOM   3050 C  CA    . MET A 1 377 ? 3.26166   15.89528  0.24919   1.000 23.69434  ? 377  MET A CA    1 
ATOM   3051 C  C     . MET A 1 377 ? 2.98089   16.22757  -1.21147  1.000 24.76841  ? 377  MET A C     1 
ATOM   3052 O  O     . MET A 1 377 ? 3.71817   16.99753  -1.83973  1.000 24.82633  ? 377  MET A O     1 
ATOM   3053 C  CB    . MET A 1 377 ? 3.75291   14.45433  0.38341   1.000 23.75110  ? 377  MET A CB    1 
ATOM   3054 C  CG    . MET A 1 377 ? 4.82748   14.07070  -0.61755  1.000 24.62534  ? 377  MET A CG    1 
ATOM   3055 S  SD    . MET A 1 377 ? 5.90190   12.74145  -0.04918  1.000 24.68094  ? 377  MET A SD    1 
ATOM   3056 C  CE    . MET A 1 377 ? 4.94425   11.32738  -0.56351  1.000 24.39661  ? 377  MET A CE    1 
ATOM   3057 N  N     . LEU A 1 378 ? 1.91729   15.64306  -1.77189  1.000 22.37734  ? 378  LEU A N     1 
ATOM   3058 C  CA    . LEU A 1 378 ? 1.59844   15.86515  -3.17927  1.000 22.58521  ? 378  LEU A CA    1 
ATOM   3059 C  C     . LEU A 1 378 ? 1.29250   17.33266  -3.45215  1.000 22.85053  ? 378  LEU A C     1 
ATOM   3060 O  O     . LEU A 1 378 ? 1.63598   17.85873  -4.51718  1.000 23.08373  ? 378  LEU A O     1 
ATOM   3061 C  CB    . LEU A 1 378 ? 0.41524   14.98917  -3.59545  1.000 22.36731  ? 378  LEU A CB    1 
ATOM   3062 C  CG    . LEU A 1 378 ? 0.55470   13.46927  -3.45973  1.000 23.02531  ? 378  LEU A CG    1 
ATOM   3063 C  CD1   . LEU A 1 378 ? -0.71797  12.77093  -3.91905  1.000 22.78327  ? 378  LEU A CD1   1 
ATOM   3064 C  CD2   . LEU A 1 378 ? 1.75954   12.94194  -4.22170  1.000 23.38574  ? 378  LEU A CD2   1 
ATOM   3065 N  N     . LEU A 1 379 ? 0.64558   18.01030  -2.50123  1.000 22.24492  ? 379  LEU A N     1 
ATOM   3066 C  CA    . LEU A 1 379 ? 0.32538   19.42141  -2.67820  1.000 22.55579  ? 379  LEU A CA    1 
ATOM   3067 C  C     . LEU A 1 379 ? 1.54938   20.31677  -2.54910  1.000 22.70683  ? 379  LEU A C     1 
ATOM   3068 O  O     . LEU A 1 379 ? 1.53057   21.44530  -3.05285  1.000 23.60535  ? 379  LEU A O     1 
ATOM   3069 C  CB    . LEU A 1 379 ? -0.73508  19.85499  -1.66439  1.000 21.87730  ? 379  LEU A CB    1 
ATOM   3070 C  CG    . LEU A 1 379 ? -2.15696  19.33498  -1.88036  1.000 22.12316  ? 379  LEU A CG    1 
ATOM   3071 C  CD1   . LEU A 1 379 ? -3.00344  19.59415  -0.64763  1.000 21.57855  ? 379  LEU A CD1   1 
ATOM   3072 C  CD2   . LEU A 1 379 ? -2.78549  19.97606  -3.10939  1.000 22.39694  ? 379  LEU A CD2   1 
ATOM   3073 N  N     . GLY A 1 380 ? 2.60657   19.84566  -1.89342  1.000 22.11433  ? 380  GLY A N     1 
ATOM   3074 C  CA    . GLY A 1 380 ? 3.77332   20.67663  -1.67735  1.000 21.88915  ? 380  GLY A CA    1 
ATOM   3075 C  C     . GLY A 1 380 ? 3.64166   21.64887  -0.52878  1.000 22.52868  ? 380  GLY A C     1 
ATOM   3076 O  O     . GLY A 1 380 ? 4.23580   22.73223  -0.57125  1.000 22.56550  ? 380  GLY A O     1 
ATOM   3077 N  N     . VAL A 1 381 ? 2.86674   21.29780  0.49892   1.000 19.88629  ? 381  VAL A N     1 
ATOM   3078 C  CA    . VAL A 1 381 ? 2.72546   22.15930  1.66494   1.000 19.87797  ? 381  VAL A CA    1 
ATOM   3079 C  C     . VAL A 1 381 ? 4.04993   22.22206  2.41220   1.000 20.08932  ? 381  VAL A C     1 
ATOM   3080 O  O     . VAL A 1 381 ? 4.73673   21.20476  2.58102   1.000 19.65037  ? 381  VAL A O     1 
ATOM   3081 C  CB    . VAL A 1 381 ? 1.59525   21.64603  2.57412   1.000 19.75161  ? 381  VAL A CB    1 
ATOM   3082 C  CG1   . VAL A 1 381 ? 1.46152   22.52148  3.81508   1.000 19.76579  ? 381  VAL A CG1   1 
ATOM   3083 C  CG2   . VAL A 1 381 ? 0.28019   21.58445  1.80606   1.000 19.22437  ? 381  VAL A CG2   1 
ATOM   3084 N  N     . HIS A 1 382 ? 4.41877   23.42301  2.85388   1.000 23.18539  ? 382  HIS A N     1 
ATOM   3085 C  CA    . HIS A 1 382 ? 5.65916   23.60559  3.59630   1.000 22.67385  ? 382  HIS A CA    1 
ATOM   3086 C  C     . HIS A 1 382 ? 5.67704   22.68000  4.80980   1.000 22.09279  ? 382  HIS A C     1 
ATOM   3087 O  O     . HIS A 1 382 ? 4.67231   22.59190  5.52916   1.000 22.21827  ? 382  HIS A O     1 
ATOM   3088 C  CB    . HIS A 1 382 ? 5.80706   25.06375  4.03502   1.000 22.57305  ? 382  HIS A CB    1 
ATOM   3089 C  CG    . HIS A 1 382 ? 7.17022   25.40853  4.55121   1.000 22.85033  ? 382  HIS A CG    1 
ATOM   3090 N  ND1   . HIS A 1 382 ? 7.67117   24.90316  5.73140   1.000 23.29599  ? 382  HIS A ND1   1 
ATOM   3091 C  CD2   . HIS A 1 382 ? 8.13605   26.21324  4.04842   1.000 23.28520  ? 382  HIS A CD2   1 
ATOM   3092 C  CE1   . HIS A 1 382 ? 8.88728   25.37829  5.93195   1.000 22.85076  ? 382  HIS A CE1   1 
ATOM   3093 N  NE2   . HIS A 1 382 ? 9.19298   26.17657  4.92546   1.000 23.35829  ? 382  HIS A NE2   1 
ATOM   3094 N  N     . PRO A 1 383 ? 6.77980   21.96968  5.06339   1.000 17.90243  ? 383  PRO A N     1 
ATOM   3095 C  CA    . PRO A 1 383 ? 6.78976   20.99536  6.16992   1.000 17.62496  ? 383  PRO A CA    1 
ATOM   3096 C  C     . PRO A 1 383 ? 6.54045   21.60987  7.53522   1.000 17.69607  ? 383  PRO A C     1 
ATOM   3097 O  O     . PRO A 1 383 ? 6.09645   20.89550  8.44339   1.000 17.48078  ? 383  PRO A O     1 
ATOM   3098 C  CB    . PRO A 1 383 ? 8.19072   20.37076  6.08579   1.000 17.42950  ? 383  PRO A CB    1 
ATOM   3099 C  CG    . PRO A 1 383 ? 8.99700   21.30116  5.24101   1.000 18.20278  ? 383  PRO A CG    1 
ATOM   3100 C  CD    . PRO A 1 383 ? 8.04248   21.97486  4.30741   1.000 18.01645  ? 383  PRO A CD    1 
ATOM   3101 N  N     . ASP A 1 384 ? 6.81518   22.90273  7.71643   1.000 22.39973  ? 384  ASP A N     1 
ATOM   3102 C  CA    . ASP A 1 384 ? 6.46940   23.55462  8.97432   1.000 22.65901  ? 384  ASP A CA    1 
ATOM   3103 C  C     . ASP A 1 384 ? 4.96343   23.53644  9.20127   1.000 23.01525  ? 384  ASP A C     1 
ATOM   3104 O  O     . ASP A 1 384 ? 4.49791   23.29012  10.32024  1.000 22.78603  ? 384  ASP A O     1 
ATOM   3105 C  CB    . ASP A 1 384 ? 6.99204   24.99154  8.98460   1.000 23.42963  ? 384  ASP A CB    1 
ATOM   3106 C  CG    . ASP A 1 384 ? 8.49513   25.07039  9.18014   1.000 23.98013  ? 384  ASP A CG    1 
ATOM   3107 O  OD1   . ASP A 1 384 ? 9.16180   24.01376  9.20643   1.000 24.13589  ? 384  ASP A OD1   1 
ATOM   3108 O  OD2   . ASP A 1 384 ? 9.01370   26.20026  9.29172   1.000 24.46753  ? 384  ASP A OD2   1 
ATOM   3109 N  N     . ALA A 1 385 ? 4.18423   23.79114  8.14669   1.000 21.00392  ? 385  ALA A N     1 
ATOM   3110 C  CA    . ALA A 1 385 ? 2.73329   23.81721  8.29032   1.000 20.82279  ? 385  ALA A CA    1 
ATOM   3111 C  C     . ALA A 1 385 ? 2.16200   22.42014  8.48779   1.000 20.59968  ? 385  ALA A C     1 
ATOM   3112 O  O     . ALA A 1 385 ? 1.14482   22.26117  9.17225   1.000 20.68366  ? 385  ALA A O     1 
ATOM   3113 C  CB    . ALA A 1 385 ? 2.09558   24.48717  7.07357   1.000 20.58922  ? 385  ALA A CB    1 
ATOM   3114 N  N     . VAL A 1 386 ? 2.79561   21.40161  7.90127   1.000 17.44112  ? 386  VAL A N     1 
ATOM   3115 C  CA    . VAL A 1 386 ? 2.33622   20.03027  8.09924   1.000 17.22374  ? 386  VAL A CA    1 
ATOM   3116 C  C     . VAL A 1 386 ? 2.64484   19.56508  9.51663   1.000 16.90708  ? 386  VAL A C     1 
ATOM   3117 O  O     . VAL A 1 386 ? 1.84148   18.86444  10.14329  1.000 16.80696  ? 386  VAL A O     1 
ATOM   3118 C  CB    . VAL A 1 386 ? 2.96320   19.09509  7.04793   1.000 17.46588  ? 386  VAL A CB    1 
ATOM   3119 C  CG1   . VAL A 1 386 ? 2.35063   17.70499  7.14055   1.000 16.33853  ? 386  VAL A CG1   1 
ATOM   3120 C  CG2   . VAL A 1 386 ? 2.78314   19.66261  5.64891   1.000 17.06419  ? 386  VAL A CG2   1 
ATOM   3121 N  N     . ASP A 1 387 ? 3.81207   19.94154  10.04324  1.000 24.61469  ? 387  ASP A N     1 
ATOM   3122 C  CA    . ASP A 1 387 ? 4.15603   19.57484  11.41268  1.000 24.85109  ? 387  ASP A CA    1 
ATOM   3123 C  C     . ASP A 1 387 ? 3.19147   20.20468  12.40754  1.000 25.17396  ? 387  ASP A C     1 
ATOM   3124 O  O     . ASP A 1 387 ? 2.82656   19.58111  13.41146  1.000 24.64520  ? 387  ASP A O     1 
ATOM   3125 C  CB    . ASP A 1 387 ? 5.59034   19.99862  11.72528  1.000 25.18517  ? 387  ASP A CB    1 
ATOM   3126 C  CG    . ASP A 1 387 ? 6.60798   18.97006  11.28784  1.000 25.56674  ? 387  ASP A CG    1 
ATOM   3127 O  OD1   . ASP A 1 387 ? 7.81697   19.28348  11.30525  1.000 25.70465  ? 387  ASP A OD1   1 
ATOM   3128 O  OD2   . ASP A 1 387 ? 6.19750   17.84959  10.91838  1.000 25.19816  ? 387  ASP A OD2   1 
ATOM   3129 N  N     . ASP A 1 388 ? 2.76636   21.44262  12.14282  1.000 29.02176  ? 388  ASP A N     1 
ATOM   3130 C  CA    . ASP A 1 388 ? 1.86542   22.13044  13.06125  1.000 29.53962  ? 388  ASP A CA    1 
ATOM   3131 C  C     . ASP A 1 388 ? 0.50897   21.44067  13.13126  1.000 28.89114  ? 388  ASP A C     1 
ATOM   3132 O  O     . ASP A 1 388 ? -0.09616  21.35939  14.20613  1.000 29.30969  ? 388  ASP A O     1 
ATOM   3133 C  CB    . ASP A 1 388 ? 1.70131   23.59012  12.64099  1.000 29.50951  ? 388  ASP A CB    1 
ATOM   3134 C  CG    . ASP A 1 388 ? 0.65831   24.31682  13.46382  1.000 30.86349  ? 388  ASP A CG    1 
ATOM   3135 O  OD1   . ASP A 1 388 ? 0.93238   24.62638  14.64390  1.000 31.27254  ? 388  ASP A OD1   1 
ATOM   3136 O  OD2   . ASP A 1 388 ? -0.44346  24.56720  12.93246  1.000 31.94276  ? 388  ASP A OD2   1 
ATOM   3137 N  N     . TRP A 1 389 ? 0.01320   20.93840  11.99922  1.000 19.03461  ? 389  TRP A N     1 
ATOM   3138 C  CA    . TRP A 1 389 ? -1.27775  20.25915  12.00621  1.000 19.18769  ? 389  TRP A CA    1 
ATOM   3139 C  C     . TRP A 1 389 ? -1.21208  18.96675  12.81059  1.000 18.52771  ? 389  TRP A C     1 
ATOM   3140 O  O     . TRP A 1 389 ? -2.06530  18.71394  13.66866  1.000 18.84425  ? 389  TRP A O     1 
ATOM   3141 C  CB    . TRP A 1 389 ? -1.73943  19.98090  10.57568  1.000 18.85659  ? 389  TRP A CB    1 
ATOM   3142 C  CG    . TRP A 1 389 ? -3.15575  19.49307  10.50180  1.000 18.88813  ? 389  TRP A CG    1 
ATOM   3143 C  CD1   . TRP A 1 389 ? -4.28791  20.24154  10.63921  1.000 19.18834  ? 389  TRP A CD1   1 
ATOM   3144 C  CD2   . TRP A 1 389 ? -3.59014  18.14330  10.28789  1.000 18.50442  ? 389  TRP A CD2   1 
ATOM   3145 N  NE1   . TRP A 1 389 ? -5.40033  19.44349  10.51718  1.000 19.62807  ? 389  TRP A NE1   1 
ATOM   3146 C  CE2   . TRP A 1 389 ? -4.99876  18.15101  10.30163  1.000 18.79539  ? 389  TRP A CE2   1 
ATOM   3147 C  CE3   . TRP A 1 389 ? -2.92430  16.93096  10.08261  1.000 18.27438  ? 389  TRP A CE3   1 
ATOM   3148 C  CZ2   . TRP A 1 389 ? -5.75403  16.99366  10.11825  1.000 18.77018  ? 389  TRP A CZ2   1 
ATOM   3149 C  CZ3   . TRP A 1 389 ? -3.67603  15.78215  9.90004   1.000 18.19112  ? 389  TRP A CZ3   1 
ATOM   3150 C  CH2   . TRP A 1 389 ? -5.07609  15.82222  9.91884   1.000 18.08113  ? 389  TRP A CH2   1 
ATOM   3151 N  N     . TYR A 1 390 ? -0.19613  18.13945  12.55633  1.000 15.62966  ? 390  TYR A N     1 
ATOM   3152 C  CA    . TYR A 1 390 ? -0.11088  16.85552  13.24389  1.000 15.88492  ? 390  TYR A CA    1 
ATOM   3153 C  C     . TYR A 1 390 ? 0.18748   17.02793  14.72666  1.000 16.09908  ? 390  TYR A C     1 
ATOM   3154 O  O     . TYR A 1 390 ? -0.21588  16.18766  15.53810  1.000 15.66033  ? 390  TYR A O     1 
ATOM   3155 C  CB    . TYR A 1 390 ? 0.94045   15.97312  12.57488  1.000 15.19700  ? 390  TYR A CB    1 
ATOM   3156 C  CG    . TYR A 1 390 ? 0.42055   15.30004  11.32807  1.000 15.48683  ? 390  TYR A CG    1 
ATOM   3157 C  CD1   . TYR A 1 390 ? 0.49190   15.93012  10.09175  1.000 15.23824  ? 390  TYR A CD1   1 
ATOM   3158 C  CD2   . TYR A 1 390 ? -0.16354  14.04381  11.39012  1.000 14.95831  ? 390  TYR A CD2   1 
ATOM   3159 C  CE1   . TYR A 1 390 ? 0.00696   15.31865  8.95097   1.000 15.14795  ? 390  TYR A CE1   1 
ATOM   3160 C  CE2   . TYR A 1 390 ? -0.65491  13.42777  10.25755  1.000 15.30941  ? 390  TYR A CE2   1 
ATOM   3161 C  CZ    . TYR A 1 390 ? -0.56468  14.06690  9.04084   1.000 15.24969  ? 390  TYR A CZ    1 
ATOM   3162 O  OH    . TYR A 1 390 ? -1.05178  13.44730  7.91403   1.000 15.04653  ? 390  TYR A OH    1 
ATOM   3163 N  N     . MET A 1 391 ? 0.88035   18.10617  15.09897  1.000 19.68392  ? 391  MET A N     1 
ATOM   3164 C  CA    . MET A 1 391 ? 1.09665   18.39024  16.51224  1.000 19.81120  ? 391  MET A CA    1 
ATOM   3165 C  C     . MET A 1 391 ? -0.19830  18.79724  17.20309  1.000 20.05411  ? 391  MET A C     1 
ATOM   3166 O  O     . MET A 1 391 ? -0.39505  18.48586  18.38275  1.000 20.25342  ? 391  MET A O     1 
ATOM   3167 C  CB    . MET A 1 391 ? 2.14277   19.49554  16.67444  1.000 20.16283  ? 391  MET A CB    1 
ATOM   3168 C  CG    . MET A 1 391 ? 3.59086   19.02322  16.72029  1.000 20.04950  ? 391  MET A CG    1 
ATOM   3169 S  SD    . MET A 1 391 ? 3.87057   17.59647  17.78727  1.000 20.19740  ? 391  MET A SD    1 
ATOM   3170 C  CE    . MET A 1 391 ? 3.84214   18.37749  19.39802  1.000 19.77673  ? 391  MET A CE    1 
ATOM   3171 N  N     . VAL A 1 392 ? -1.09344  19.47775  16.48735  1.000 13.67504  ? 392  VAL A N     1 
ATOM   3172 C  CA    . VAL A 1 392 ? -2.26890  20.06381  17.12326  1.000 14.39857  ? 392  VAL A CA    1 
ATOM   3173 C  C     . VAL A 1 392 ? -3.39079  19.04025  17.26488  1.000 14.31366  ? 392  VAL A C     1 
ATOM   3174 O  O     . VAL A 1 392 ? -4.01228  18.92802  18.32695  1.000 14.44406  ? 392  VAL A O     1 
ATOM   3175 C  CB    . VAL A 1 392 ? -2.73604  21.30457  16.33643  1.000 15.26696  ? 392  VAL A CB    1 
ATOM   3176 C  CG1   . VAL A 1 392 ? -4.20738  21.59761  16.61373  1.000 14.88771  ? 392  VAL A CG1   1 
ATOM   3177 C  CG2   . VAL A 1 392 ? -1.87270  22.51354  16.68119  1.000 15.12901  ? 392  VAL A CG2   1 
ATOM   3178 N  N     . VAL A 1 393 ? -3.66136  18.26572  16.20856  1.000 16.29096  ? 393  VAL A N     1 
ATOM   3179 C  CA    . VAL A 1 393 ? -4.95492  17.59278  16.09477  1.000 16.77349  ? 393  VAL A CA    1 
ATOM   3180 C  C     . VAL A 1 393 ? -5.01168  16.20295  16.71947  1.000 16.61417  ? 393  VAL A C     1 
ATOM   3181 O  O     . VAL A 1 393 ? -6.11244  15.64454  16.84345  1.000 16.79686  ? 393  VAL A O     1 
ATOM   3182 C  CB    . VAL A 1 393 ? -5.38406  17.49324  14.61674  1.000 16.28814  ? 393  VAL A CB    1 
ATOM   3183 C  CG1   . VAL A 1 393 ? -5.38119  18.87172  13.97370  1.000 16.67458  ? 393  VAL A CG1   1 
ATOM   3184 C  CG2   . VAL A 1 393 ? -4.47658  16.54278  13.85559  1.000 15.63054  ? 393  VAL A CG2   1 
ATOM   3185 N  N     . PHE A 1 394 ? -3.88382  15.62587  17.12708  1.000 18.63377  ? 394  PHE A N     1 
ATOM   3186 C  CA    . PHE A 1 394 ? -3.86037  14.25502  17.62688  1.000 18.82241  ? 394  PHE A CA    1 
ATOM   3187 C  C     . PHE A 1 394 ? -3.41265  14.22635  19.08099  1.000 18.49500  ? 394  PHE A C     1 
ATOM   3188 O  O     . PHE A 1 394 ? -2.43035  14.87829  19.44711  1.000 18.25171  ? 394  PHE A O     1 
ATOM   3189 C  CB    . PHE A 1 394 ? -2.95440  13.37681  16.76231  1.000 17.42411  ? 394  PHE A CB    1 
ATOM   3190 C  CG    . PHE A 1 394 ? -3.43976  13.23458  15.35164  1.000 17.23181  ? 394  PHE A CG    1 
ATOM   3191 C  CD1   . PHE A 1 394 ? -4.73413  12.81405  15.09624  1.000 17.03421  ? 394  PHE A CD1   1 
ATOM   3192 C  CD2   . PHE A 1 394 ? -2.61622  13.54266  14.28225  1.000 17.10319  ? 394  PHE A CD2   1 
ATOM   3193 C  CE1   . PHE A 1 394 ? -5.19541  12.69156  13.80157  1.000 17.31270  ? 394  PHE A CE1   1 
ATOM   3194 C  CE2   . PHE A 1 394 ? -3.07358  13.42133  12.98378  1.000 16.82513  ? 394  PHE A CE2   1 
ATOM   3195 C  CZ    . PHE A 1 394 ? -4.36397  12.99591  12.74369  1.000 17.24005  ? 394  PHE A CZ    1 
ATOM   3196 N  N     . ALA A 1 395 ? -4.13213  13.45575  19.90112  1.000 18.52685  ? 395  ALA A N     1 
ATOM   3197 C  CA    . ALA A 1 395 ? -3.89960  13.41829  21.34030  1.000 18.47853  ? 395  ALA A CA    1 
ATOM   3198 C  C     . ALA A 1 395 ? -2.60984  12.70581  21.72598  1.000 18.29695  ? 395  ALA A C     1 
ATOM   3199 O  O     . ALA A 1 395 ? -2.19652  12.80340  22.88673  1.000 17.69471  ? 395  ALA A O     1 
ATOM   3200 C  CB    . ALA A 1 395 ? -5.08302  12.74890  22.04159  1.000 19.16971  ? 395  ALA A CB    1 
ATOM   3201 N  N     . ASP A 1 396 ? -1.97308  11.99076  20.80108  1.000 21.14294  ? 396  ASP A N     1 
ATOM   3202 C  CA    . ASP A 1 396 ? -0.69647  11.34119  21.06153  1.000 20.76924  ? 396  ASP A CA    1 
ATOM   3203 C  C     . ASP A 1 396 ? 0.48169   12.13320  20.51117  1.000 20.84099  ? 396  ASP A C     1 
ATOM   3204 O  O     . ASP A 1 396 ? 1.59496   11.60239  20.44020  1.000 20.18571  ? 396  ASP A O     1 
ATOM   3205 C  CB    . ASP A 1 396 ? -0.69376  9.92563   20.47783  1.000 20.40587  ? 396  ASP A CB    1 
ATOM   3206 C  CG    . ASP A 1 396 ? -1.02943  9.89784   18.99225  1.000 20.63483  ? 396  ASP A CG    1 
ATOM   3207 O  OD1   . ASP A 1 396 ? -1.11355  10.97566  18.36395  1.000 20.70470  ? 396  ASP A OD1   1 
ATOM   3208 O  OD2   . ASP A 1 396 ? -1.20840  8.78766   18.44822  1.000 21.08260  ? 396  ASP A OD2   1 
ATOM   3209 N  N     . ALA A 1 397 ? 0.26394   13.38938  20.13133  1.000 14.13019  ? 397  ALA A N     1 
ATOM   3210 C  CA    . ALA A 1 397 ? 1.25694   14.14366  19.37896  1.000 14.20614  ? 397  ALA A CA    1 
ATOM   3211 C  C     . ALA A 1 397 ? 2.29661   14.74698  20.31326  1.000 14.49211  ? 397  ALA A C     1 
ATOM   3212 O  O     . ALA A 1 397 ? 1.97229   15.58403  21.16288  1.000 14.51170  ? 397  ALA A O     1 
ATOM   3213 C  CB    . ALA A 1 397 ? 0.58337   15.23373  18.54899  1.000 14.42413  ? 397  ALA A CB    1 
ATOM   3214 N  N     . TYR A 1 398 ? 3.54246   14.30582  20.15797  1.000 19.43747  ? 398  TYR A N     1 
ATOM   3215 C  CA    . TYR A 1 398 ? 4.70261   14.93304  20.77117  1.000 19.51341  ? 398  TYR A CA    1 
ATOM   3216 C  C     . TYR A 1 398 ? 5.80870   14.94719  19.72777  1.000 19.55105  ? 398  TYR A C     1 
ATOM   3217 O  O     . TYR A 1 398 ? 5.86209   14.07598  18.85651  1.000 19.46686  ? 398  TYR A O     1 
ATOM   3218 C  CB    . TYR A 1 398 ? 5.12306   14.20723  22.06285  1.000 19.35595  ? 398  TYR A CB    1 
ATOM   3219 C  CG    . TYR A 1 398 ? 3.99067   14.15059  23.06478  1.000 19.71033  ? 398  TYR A CG    1 
ATOM   3220 C  CD1   . TYR A 1 398 ? 3.05243   13.12634  23.02724  1.000 19.16679  ? 398  TYR A CD1   1 
ATOM   3221 C  CD2   . TYR A 1 398 ? 3.83102   15.14938  24.01671  1.000 20.02911  ? 398  TYR A CD2   1 
ATOM   3222 C  CE1   . TYR A 1 398 ? 2.00177   13.08759  23.92013  1.000 19.39729  ? 398  TYR A CE1   1 
ATOM   3223 C  CE2   . TYR A 1 398 ? 2.78342   15.11657  24.91721  1.000 19.82025  ? 398  TYR A CE2   1 
ATOM   3224 C  CZ    . TYR A 1 398 ? 1.87207   14.08428  24.86291  1.000 19.87331  ? 398  TYR A CZ    1 
ATOM   3225 O  OH    . TYR A 1 398 ? 0.82384   14.04850  25.75151  1.000 20.02403  ? 398  TYR A OH    1 
ATOM   3226 N  N     . GLU A 1 399 ? 6.67261   15.96285  19.79899  1.000 18.76990  ? 399  GLU A N     1 
ATOM   3227 C  CA    . GLU A 1 399 ? 7.55577   16.24512  18.67037  1.000 19.02491  ? 399  GLU A CA    1 
ATOM   3228 C  C     . GLU A 1 399 ? 8.51422   15.09543  18.38298  1.000 18.93886  ? 399  GLU A C     1 
ATOM   3229 O  O     . GLU A 1 399 ? 8.83949   14.84091  17.21750  1.000 18.95826  ? 399  GLU A O     1 
ATOM   3230 C  CB    . GLU A 1 399 ? 8.33449   17.53819  18.91276  1.000 19.69956  ? 399  GLU A CB    1 
ATOM   3231 C  CG    . GLU A 1 399 ? 9.19810   17.93901  17.72760  1.000 20.21699  ? 399  GLU A CG    1 
ATOM   3232 C  CD    . GLU A 1 399 ? 9.79702   19.31914  17.86917  1.000 20.51704  ? 399  GLU A CD    1 
ATOM   3233 O  OE1   . GLU A 1 399 ? 10.89628  19.43847  18.45040  1.000 20.30803  ? 399  GLU A OE1   1 
ATOM   3234 O  OE2   . GLU A 1 399 ? 9.16870   20.28420  17.38577  1.000 21.62741  ? 399  GLU A OE2   1 
ATOM   3235 N  N     . TRP A 1 400 ? 8.96505   14.38142  19.41724  1.000 14.90724  ? 400  TRP A N     1 
ATOM   3236 C  CA    . TRP A 1 400 ? 9.91636   13.29584  19.19359  1.000 14.68715  ? 400  TRP A CA    1 
ATOM   3237 C  C     . TRP A 1 400 ? 9.33274   12.20139  18.30920  1.000 14.46716  ? 400  TRP A C     1 
ATOM   3238 O  O     . TRP A 1 400 ? 10.07291  11.54120  17.57259  1.000 14.54008  ? 400  TRP A O     1 
ATOM   3239 C  CB    . TRP A 1 400 ? 10.37566  12.70913  20.52859  1.000 14.56169  ? 400  TRP A CB    1 
ATOM   3240 C  CG    . TRP A 1 400 ? 9.29607   12.00727  21.28091  1.000 14.31136  ? 400  TRP A CG    1 
ATOM   3241 C  CD1   . TRP A 1 400 ? 8.46950   12.54786  22.22124  1.000 14.25687  ? 400  TRP A CD1   1 
ATOM   3242 C  CD2   . TRP A 1 400 ? 8.92323   10.62998  21.16097  1.000 14.33920  ? 400  TRP A CD2   1 
ATOM   3243 N  NE1   . TRP A 1 400 ? 7.60298   11.59227  22.69439  1.000 14.71189  ? 400  TRP A NE1   1 
ATOM   3244 C  CE2   . TRP A 1 400 ? 7.86132   10.40556  22.05972  1.000 14.46033  ? 400  TRP A CE2   1 
ATOM   3245 C  CE3   . TRP A 1 400 ? 9.38347   9.56477   20.38024  1.000 14.36264  ? 400  TRP A CE3   1 
ATOM   3246 C  CZ2   . TRP A 1 400 ? 7.25196   9.15925   22.20024  1.000 14.40720  ? 400  TRP A CZ2   1 
ATOM   3247 C  CZ3   . TRP A 1 400 ? 8.77789   8.32781   20.52069  1.000 14.42027  ? 400  TRP A CZ3   1 
ATOM   3248 C  CH2   . TRP A 1 400 ? 7.72182   8.13623   21.42265  1.000 14.31724  ? 400  TRP A CH2   1 
ATOM   3249 N  N     . VAL A 1 401 ? 8.01853   11.99436  18.36127  1.000 19.72985  ? 401  VAL A N     1 
ATOM   3250 C  CA    . VAL A 1 401 ? 7.37538   10.96734  17.56137  1.000 19.90235  ? 401  VAL A CA    1 
ATOM   3251 C  C     . VAL A 1 401 ? 6.60811   11.55114  16.37825  1.000 19.80523  ? 401  VAL A C     1 
ATOM   3252 O  O     . VAL A 1 401 ? 6.55122   10.91670  15.31764  1.000 19.61576  ? 401  VAL A O     1 
ATOM   3253 C  CB    . VAL A 1 401 ? 6.45067   10.09504  18.44023  1.000 19.37903  ? 401  VAL A CB    1 
ATOM   3254 C  CG1   . VAL A 1 401 ? 5.42729   10.95713  19.16421  1.000 19.46962  ? 401  VAL A CG1   1 
ATOM   3255 C  CG2   . VAL A 1 401 ? 5.77500   9.00288   17.61595  1.000 19.00455  ? 401  VAL A CG2   1 
ATOM   3256 N  N     . GLU A 1 402 ? 6.04287   12.75009  16.51757  1.000 19.02444  ? 402  GLU A N     1 
ATOM   3257 C  CA    . GLU A 1 402 ? 5.29349   13.35160  15.42042  1.000 19.28479  ? 402  GLU A CA    1 
ATOM   3258 C  C     . GLU A 1 402 ? 6.20777   13.69585  14.25062  1.000 19.88080  ? 402  GLU A C     1 
ATOM   3259 O  O     . GLU A 1 402 ? 5.87669   13.42438  13.09126  1.000 19.57722  ? 402  GLU A O     1 
ATOM   3260 C  CB    . GLU A 1 402 ? 4.55431   14.59866  15.91794  1.000 19.72804  ? 402  GLU A CB    1 
ATOM   3261 C  CG    . GLU A 1 402 ? 3.93108   15.48122  14.82747  1.000 19.80917  ? 402  GLU A CG    1 
ATOM   3262 C  CD    . GLU A 1 402 ? 4.91753   16.45452  14.19564  1.000 20.82904  ? 402  GLU A CD    1 
ATOM   3263 O  OE1   . GLU A 1 402 ? 5.72230   17.07148  14.92958  1.000 21.06422  ? 402  GLU A OE1   1 
ATOM   3264 O  OE2   . GLU A 1 402 ? 4.88336   16.59704  12.95641  1.000 20.65299  ? 402  GLU A OE2   1 
ATOM   3265 N  N     . MET A 1 403 ? 7.36574   14.30024  14.53384  1.000 18.52693  ? 403  MET A N     1 
ATOM   3266 C  CA    . MET A 1 403 ? 8.16996   14.86241  13.44905  1.000 19.12822  ? 403  MET A CA    1 
ATOM   3267 C  C     . MET A 1 403 ? 8.81026   13.79794  12.56414  1.000 19.03137  ? 403  MET A C     1 
ATOM   3268 O  O     . MET A 1 403 ? 8.73956   13.93479  11.32980  1.000 18.74410  ? 403  MET A O     1 
ATOM   3269 C  CB    . MET A 1 403 ? 9.20929   15.82780  14.01984  1.000 18.78404  ? 403  MET A CB    1 
ATOM   3270 C  CG    . MET A 1 403 ? 9.96022   16.59750  12.95609  1.000 19.51856  ? 403  MET A CG    1 
ATOM   3271 S  SD    . MET A 1 403 ? 11.19352  17.67315  13.69229  1.000 20.23988  ? 403  MET A SD    1 
ATOM   3272 C  CE    . MET A 1 403 ? 10.18230  19.11042  14.03181  1.000 19.99111  ? 403  MET A CE    1 
ATOM   3273 N  N     . PRO A 1 404 ? 9.44863   12.74308  13.08906  1.000 18.90240  ? 404  PRO A N     1 
ATOM   3274 C  CA    . PRO A 1 404 ? 10.00108  11.72798  12.17431  1.000 18.75251  ? 404  PRO A CA    1 
ATOM   3275 C  C     . PRO A 1 404 ? 8.93376   11.01840  11.36187  1.000 18.79792  ? 404  PRO A C     1 
ATOM   3276 O  O     . PRO A 1 404 ? 9.20710   10.58655  10.23480  1.000 19.13541  ? 404  PRO A O     1 
ATOM   3277 C  CB    . PRO A 1 404 ? 10.74163  10.76249  13.11246  1.000 18.40691  ? 404  PRO A CB    1 
ATOM   3278 C  CG    . PRO A 1 404 ? 10.93132  11.51339  14.37998  1.000 18.63662  ? 404  PRO A CG    1 
ATOM   3279 C  CD    . PRO A 1 404 ? 9.76467   12.43239  14.49430  1.000 18.55293  ? 404  PRO A CD    1 
ATOM   3280 N  N     . ASN A 1 405 ? 7.71705   10.90149  11.89569  1.000 15.10816  ? 405  ASN A N     1 
ATOM   3281 C  CA    . ASN A 1 405 ? 6.62142   10.29440  11.15217  1.000 15.12015  ? 405  ASN A CA    1 
ATOM   3282 C  C     . ASN A 1 405 ? 6.02049   11.24946  10.12924  1.000 15.50829  ? 405  ASN A C     1 
ATOM   3283 O  O     . ASN A 1 405 ? 5.50715   10.80131  9.09764   1.000 15.57709  ? 405  ASN A O     1 
ATOM   3284 C  CB    . ASN A 1 405 ? 5.53558   9.82465   12.11859  1.000 14.94193  ? 405  ASN A CB    1 
ATOM   3285 C  CG    . ASN A 1 405 ? 5.84940   8.47986   12.73558  1.000 15.05956  ? 405  ASN A CG    1 
ATOM   3286 O  OD1   . ASN A 1 405 ? 6.02743   7.48639   12.02917  1.000 15.15406  ? 405  ASN A OD1   1 
ATOM   3287 N  ND2   . ASN A 1 405 ? 5.92512   8.44045   14.06096  1.000 14.45031  ? 405  ASN A ND2   1 
ATOM   3288 N  N     . THR A 1 406 ? 6.06900   12.55591  10.39327  1.000 20.68035  ? 406  THR A N     1 
ATOM   3289 C  CA    . THR A 1 406 ? 5.44597   13.55317  9.52839   1.000 21.07643  ? 406  THR A CA    1 
ATOM   3290 C  C     . THR A 1 406 ? 6.44991   14.17717  8.56497   1.000 21.06803  ? 406  THR A C     1 
ATOM   3291 O  O     . THR A 1 406 ? 6.29441   14.06865  7.34482   1.000 21.32147  ? 406  THR A O     1 
ATOM   3292 C  CB    . THR A 1 406 ? 4.77619   14.64184  10.37679  1.000 21.00839  ? 406  THR A CB    1 
ATOM   3293 O  OG1   . THR A 1 406 ? 3.79669   14.04569  11.23608  1.000 20.19798  ? 406  THR A OG1   1 
ATOM   3294 C  CG2   . THR A 1 406 ? 4.10373   15.66970  9.48665   1.000 20.44944  ? 406  THR A CG2   1 
ATOM   3295 N  N     . ARG A 1 407 ? 7.48096   14.83925  9.09611   1.000 24.13449  ? 407  ARG A N     1 
ATOM   3296 C  CA    . ARG A 1 407 ? 8.52163   15.39931  8.24189   1.000 24.20375  ? 407  ARG A CA    1 
ATOM   3297 C  C     . ARG A 1 407 ? 9.29223   14.31784  7.49809   1.000 23.83357  ? 407  ARG A C     1 
ATOM   3298 O  O     . ARG A 1 407 ? 9.85596   14.59103  6.43252   1.000 24.47348  ? 407  ARG A O     1 
ATOM   3299 C  CB    . ARG A 1 407 ? 9.48539   16.25164  9.07285   1.000 23.87758  ? 407  ARG A CB    1 
ATOM   3300 C  CG    . ARG A 1 407 ? 10.42306  17.11561  8.24096   1.000 25.03539  ? 407  ARG A CG    1 
ATOM   3301 C  CD    . ARG A 1 407 ? 11.13426  18.15636  9.08699   1.000 24.85275  ? 407  ARG A CD    1 
ATOM   3302 N  NE    . ARG A 1 407 ? 10.23747  19.22679  9.50401   1.000 25.24953  ? 407  ARG A NE    1 
ATOM   3303 C  CZ    . ARG A 1 407 ? 10.26443  20.45997  9.01655   1.000 25.22087  ? 407  ARG A CZ    1 
ATOM   3304 N  NH1   . ARG A 1 407 ? 11.13482  20.81696  8.08592   1.000 25.45610  ? 407  ARG A NH1   1 
ATOM   3305 N  NH2   . ARG A 1 407 ? 9.39701   21.35760  9.47518   1.000 24.65227  ? 407  ARG A NH2   1 
ATOM   3306 N  N     . GLY A 1 408 ? 9.31935   13.09806  8.02519   1.000 18.36090  ? 408  GLY A N     1 
ATOM   3307 C  CA    . GLY A 1 408 ? 10.05617  12.02515  7.39162   1.000 19.33397  ? 408  GLY A CA    1 
ATOM   3308 C  C     . GLY A 1 408 ? 9.20211   11.07587  6.57701   1.000 18.73115  ? 408  GLY A C     1 
ATOM   3309 O  O     . GLY A 1 408 ? 9.16605   11.16419  5.34676   1.000 18.93395  ? 408  GLY A O     1 
ATOM   3310 N  N     . MET A 1 409 ? 8.49896   10.16928  7.25860   1.000 23.52415  ? 409  MET A N     1 
ATOM   3311 C  CA    . MET A 1 409 ? 7.82487   9.07438   6.56758   1.000 23.42291  ? 409  MET A CA    1 
ATOM   3312 C  C     . MET A 1 409 ? 6.68536   9.57678   5.68741   1.000 24.07475  ? 409  MET A C     1 
ATOM   3313 O  O     . MET A 1 409 ? 6.50199   9.09054   4.56564   1.000 24.12234  ? 409  MET A O     1 
ATOM   3314 C  CB    . MET A 1 409 ? 7.31442   8.05729   7.59106   1.000 23.35528  ? 409  MET A CB    1 
ATOM   3315 C  CG    . MET A 1 409 ? 6.84606   6.73005   7.00689   1.000 24.86031  ? 409  MET A CG    1 
ATOM   3316 S  SD    . MET A 1 409 ? 5.67131   5.87112   8.08235   1.000 25.01729  ? 409  MET A SD    1 
ATOM   3317 C  CE    . MET A 1 409 ? 6.74905   5.33610   9.40705   1.000 23.82577  ? 409  MET A CE    1 
ATOM   3318 N  N     . ALA A 1 410 ? 5.92048   10.56001  6.16415   1.000 17.51122  ? 410  ALA A N     1 
ATOM   3319 C  CA    . ALA A 1 410 ? 4.69552   10.93041  5.46375   1.000 17.11085  ? 410  ALA A CA    1 
ATOM   3320 C  C     . ALA A 1 410 ? 4.95791   11.85188  4.27806   1.000 18.07401  ? 410  ALA A C     1 
ATOM   3321 O  O     . ALA A 1 410 ? 4.26346   11.76107  3.25945   1.000 18.31000  ? 410  ALA A O     1 
ATOM   3322 C  CB    . ALA A 1 410 ? 3.71259   11.58760  6.43174   1.000 17.18640  ? 410  ALA A CB    1 
ATOM   3323 N  N     . THR A 1 411 ? 5.93736   12.74980  4.38365   1.000 17.85614  ? 411  THR A N     1 
ATOM   3324 C  CA    . THR A 1 411 ? 6.10503   13.79866  3.38747   1.000 18.14911  ? 411  THR A CA    1 
ATOM   3325 C  C     . THR A 1 411 ? 7.48466   13.84933  2.74457   1.000 19.22002  ? 411  THR A C     1 
ATOM   3326 O  O     . THR A 1 411 ? 7.71057   14.71070  1.88523   1.000 19.09767  ? 411  THR A O     1 
ATOM   3327 C  CB    . THR A 1 411 ? 5.79710   15.16889  4.00311   1.000 17.87830  ? 411  THR A CB    1 
ATOM   3328 O  OG1   . THR A 1 411 ? 6.79089   15.48234  4.98482   1.000 18.16502  ? 411  THR A OG1   1 
ATOM   3329 C  CG2   . THR A 1 411 ? 4.42305   15.16796  4.65423   1.000 17.67997  ? 411  THR A CG2   1 
ATOM   3330 N  N     . PHE A 1 412 ? 8.41296   12.97453  3.13317   1.000 24.27481  ? 412  PHE A N     1 
ATOM   3331 C  CA    . PHE A 1 412 ? 9.73574   12.89167  2.51403   1.000 24.67721  ? 412  PHE A CA    1 
ATOM   3332 C  C     . PHE A 1 412 ? 10.52043  14.19903  2.62492   1.000 25.09625  ? 412  PHE A C     1 
ATOM   3333 O  O     . PHE A 1 412 ? 11.46310  14.42612  1.86121   1.000 24.75702  ? 412  PHE A O     1 
ATOM   3334 C  CB    . PHE A 1 412 ? 9.62643   12.46380  1.04269   1.000 25.76095  ? 412  PHE A CB    1 
ATOM   3335 C  CG    . PHE A 1 412 ? 10.84538  11.75584  0.51608   1.000 25.87285  ? 412  PHE A CG    1 
ATOM   3336 C  CD1   . PHE A 1 412 ? 11.15331  10.47210  0.93171   1.000 25.36536  ? 412  PHE A CD1   1 
ATOM   3337 C  CD2   . PHE A 1 412 ? 11.67600  12.37167  -0.40850  1.000 26.40335  ? 412  PHE A CD2   1 
ATOM   3338 C  CE1   . PHE A 1 412 ? 12.27113  9.81936   0.44209   1.000 25.76433  ? 412  PHE A CE1   1 
ATOM   3339 C  CE2   . PHE A 1 412 ? 12.79732  11.72332  -0.89852  1.000 26.25867  ? 412  PHE A CE2   1 
ATOM   3340 C  CZ    . PHE A 1 412 ? 13.09340  10.44518  -0.47243  1.000 25.79447  ? 412  PHE A CZ    1 
ATOM   3341 N  N     . ALA A 1 413 ? 10.15589  15.07297  3.56678   1.000 20.85970  ? 413  ALA A N     1 
ATOM   3342 C  CA    . ALA A 1 413 ? 10.87879  16.32925  3.72628   1.000 20.90497  ? 413  ALA A CA    1 
ATOM   3343 C  C     . ALA A 1 413 ? 12.28849  16.12371  4.26666   1.000 21.16663  ? 413  ALA A C     1 
ATOM   3344 O  O     . ALA A 1 413 ? 13.12403  17.02580  4.13677   1.000 21.09427  ? 413  ALA A O     1 
ATOM   3345 C  CB    . ALA A 1 413 ? 10.10162  17.27722  4.64093   1.000 20.48379  ? 413  ALA A CB    1 
ATOM   3346 N  N     . ASP A 1 414 ? 12.57213  14.96542  4.86308   1.000 23.19053  ? 414  ASP A N     1 
ATOM   3347 C  CA    . ASP A 1 414 ? 13.90852  14.63445  5.34021   1.000 22.69653  ? 414  ASP A CA    1 
ATOM   3348 C  C     . ASP A 1 414 ? 14.74754  13.90822  4.29439   1.000 23.24565  ? 414  ASP A C     1 
ATOM   3349 O  O     . ASP A 1 414 ? 15.83176  13.41397  4.62090   1.000 23.12535  ? 414  ASP A O     1 
ATOM   3350 C  CB    . ASP A 1 414 ? 13.82395  13.79493  6.62175   1.000 22.41730  ? 414  ASP A CB    1 
ATOM   3351 C  CG    . ASP A 1 414 ? 13.29440  12.38528  6.37983   1.000 22.87786  ? 414  ASP A CG    1 
ATOM   3352 O  OD1   . ASP A 1 414 ? 12.73473  12.11460  5.29506   1.000 22.71000  ? 414  ASP A OD1   1 
ATOM   3353 O  OD2   . ASP A 1 414 ? 13.43349  11.54084  7.29128   1.000 22.38333  ? 414  ASP A OD2   1 
ATOM   3354 N  N     . GLY A 1 415 ? 14.26959  13.82368  3.05436   1.000 32.44055  ? 415  GLY A N     1 
ATOM   3355 C  CA    . GLY A 1 415 ? 15.03093  13.18607  1.99924   1.000 33.00290  ? 415  GLY A CA    1 
ATOM   3356 C  C     . GLY A 1 415 ? 15.10361  11.67864  2.06649   1.000 32.72911  ? 415  GLY A C     1 
ATOM   3357 O  O     . GLY A 1 415 ? 15.82736  11.07454  1.26947   1.000 33.67084  ? 415  GLY A O     1 
ATOM   3358 N  N     . GLY A 1 416 ? 14.38543  11.05114  2.98557   1.000 28.29128  ? 416  GLY A N     1 
ATOM   3359 C  CA    . GLY A 1 416 ? 14.37238  9.61376   3.11069   1.000 28.79001  ? 416  GLY A CA    1 
ATOM   3360 C  C     . GLY A 1 416 ? 15.13912  9.03590   4.28449   1.000 29.00152  ? 416  GLY A C     1 
ATOM   3361 O  O     . GLY A 1 416 ? 15.46936  7.84335   4.25171   1.000 28.85974  ? 416  GLY A O     1 
ATOM   3362 N  N     . ILE A 1 417 ? 15.43371  9.83355   5.31162   1.000 25.94859  ? 417  ILE A N     1 
ATOM   3363 C  CA    . ILE A 1 417 ? 16.14443  9.31009   6.47443   1.000 25.64749  ? 417  ILE A CA    1 
ATOM   3364 C  C     . ILE A 1 417 ? 15.29039  8.27056   7.18994   1.000 25.54863  ? 417  ILE A C     1 
ATOM   3365 O  O     . ILE A 1 417 ? 15.76894  7.19060   7.55634   1.000 25.71660  ? 417  ILE A O     1 
ATOM   3366 C  CB    . ILE A 1 417 ? 16.55033  10.45953  7.41436   1.000 25.90170  ? 417  ILE A CB    1 
ATOM   3367 C  CG1   . ILE A 1 417 ? 17.68564  11.27482  6.79058   1.000 25.37638  ? 417  ILE A CG1   1 
ATOM   3368 C  CG2   . ILE A 1 417 ? 16.95871  9.92227   8.77725   1.000 25.28473  ? 417  ILE A CG2   1 
ATOM   3369 C  CD1   . ILE A 1 417 ? 18.01029  12.54715  7.53750   1.000 24.87953  ? 417  ILE A CD1   1 
ATOM   3370 N  N     . VAL A 1 418 ? 14.00895  8.57090   7.37656   1.000 22.16536  ? 418  VAL A N     1 
ATOM   3371 C  CA    . VAL A 1 418 ? 13.11247  7.68116   8.10866   1.000 22.23971  ? 418  VAL A CA    1 
ATOM   3372 C  C     . VAL A 1 418 ? 12.50808  6.62116   7.19693   1.000 22.45430  ? 418  VAL A C     1 
ATOM   3373 O  O     . VAL A 1 418 ? 12.55142  5.42651   7.50299   1.000 22.91504  ? 418  VAL A O     1 
ATOM   3374 C  CB    . VAL A 1 418 ? 12.01501  8.50684   8.81329   1.000 21.65233  ? 418  VAL A CB    1 
ATOM   3375 C  CG1   . VAL A 1 418 ? 10.94331  7.59161   9.38917   1.000 21.45139  ? 418  VAL A CG1   1 
ATOM   3376 C  CG2   . VAL A 1 418 ? 12.62219  9.37316   9.90178   1.000 21.26551  ? 418  VAL A CG2   1 
ATOM   3377 N  N     . GLY A 1 419 ? 11.94314  7.03579   6.06508   1.000 28.87944  ? 419  GLY A N     1 
ATOM   3378 C  CA    . GLY A 1 419 ? 11.17121  6.13392   5.23198   1.000 29.91557  ? 419  GLY A CA    1 
ATOM   3379 C  C     . GLY A 1 419 ? 11.89060  5.54981   4.03239   1.000 30.92363  ? 419  GLY A C     1 
ATOM   3380 O  O     . GLY A 1 419 ? 11.35908  4.64677   3.37898   1.000 32.34064  ? 419  GLY A O     1 
ATOM   3381 N  N     . SER A 1 420 ? 13.07730  6.07535   3.71414   1.000 41.25111  ? 420  SER A N     1 
ATOM   3382 C  CA    . SER A 1 420 ? 13.92896  5.57910   2.63252   1.000 42.50878  ? 420  SER A CA    1 
ATOM   3383 C  C     . SER A 1 420 ? 13.34283  5.81752   1.24218   1.000 43.16591  ? 420  SER A C     1 
ATOM   3384 O  O     . SER A 1 420 ? 14.05785  5.70144   0.24131   1.000 43.56961  ? 420  SER A O     1 
ATOM   3385 C  CB    . SER A 1 420 ? 14.22948  4.08776   2.82244   1.000 42.80143  ? 420  SER A CB    1 
ATOM   3386 O  OG    . SER A 1 420 ? 13.17306  3.28566   2.32284   1.000 43.85431  ? 420  SER A OG    1 
ATOM   3387 N  N     . LYS A 1 421 ? 12.05590  6.15124   1.16102   1.000 37.56848  ? 421  LYS A N     1 
ATOM   3388 C  CA    . LYS A 1 421 ? 11.41040  6.44649   -0.11116  1.000 37.32698  ? 421  LYS A CA    1 
ATOM   3389 C  C     . LYS A 1 421 ? 10.10632  7.17237   0.17349   1.000 36.90591  ? 421  LYS A C     1 
ATOM   3390 O  O     . LYS A 1 421 ? 9.50308   6.95698   1.23087   1.000 36.58745  ? 421  LYS A O     1 
ATOM   3391 C  CB    . LYS A 1 421 ? 11.15055  5.16495   -0.91891  1.000 38.08424  ? 421  LYS A CB    1 
ATOM   3392 C  CG    . LYS A 1 421 ? 10.09157  4.24895   -0.32835  1.000 37.72692  ? 421  LYS A CG    1 
ATOM   3393 C  CD    . LYS A 1 421 ? 9.25613   3.60122   -1.42123  1.000 39.13021  ? 421  LYS A CD    1 
ATOM   3394 C  CE    . LYS A 1 421 ? 8.16985   2.71295   -0.83555  1.000 39.82884  ? 421  LYS A CE    1 
ATOM   3395 N  NZ    . LYS A 1 421 ? 8.65875   1.32881   -0.58285  1.000 40.48888  ? 421  LYS A NZ    1 
ATOM   3396 N  N     . PRO A 1 422 ? 9.65012   8.03813   -0.73000  1.000 27.05207  ? 422  PRO A N     1 
ATOM   3397 C  CA    . PRO A 1 422 ? 8.39081   8.74728   -0.48263  1.000 26.82162  ? 422  PRO A CA    1 
ATOM   3398 C  C     . PRO A 1 422 ? 7.20376   7.81687   -0.65429  1.000 27.27669  ? 422  PRO A C     1 
ATOM   3399 O  O     . PRO A 1 422 ? 7.18637   6.95737   -1.53786  1.000 27.63940  ? 422  PRO A O     1 
ATOM   3400 C  CB    . PRO A 1 422 ? 8.39247   9.85789   -1.53712  1.000 26.98619  ? 422  PRO A CB    1 
ATOM   3401 C  CG    . PRO A 1 422 ? 9.21579   9.31631   -2.64139  1.000 27.54255  ? 422  PRO A CG    1 
ATOM   3402 C  CD    . PRO A 1 422 ? 10.24201  8.39709   -2.03096  1.000 28.04557  ? 422  PRO A CD    1 
ATOM   3403 N  N     . TYR A 1 423 ? 6.20978   7.99170   0.20618   1.000 39.95656  ? 423  TYR A N     1 
ATOM   3404 C  CA    . TYR A 1 423 ? 5.01697   7.14587   0.19271   1.000 39.85179  ? 423  TYR A CA    1 
ATOM   3405 C  C     . TYR A 1 423 ? 3.89076   7.80204   -0.59289  1.000 39.66249  ? 423  TYR A C     1 
ATOM   3406 O  O     . TYR A 1 423 ? 2.74389   7.86612   -0.15356  1.000 39.79317  ? 423  TYR A O     1 
ATOM   3407 C  CB    . TYR A 1 423 ? 4.58788   6.82583   1.61851   1.000 39.63978  ? 423  TYR A CB    1 
ATOM   3408 C  CG    . TYR A 1 423 ? 5.40876   5.72278   2.24496   1.000 39.86194  ? 423  TYR A CG    1 
ATOM   3409 C  CD1   . TYR A 1 423 ? 6.68890   5.97171   2.72235   1.000 39.34351  ? 423  TYR A CD1   1 
ATOM   3410 C  CD2   . TYR A 1 423 ? 4.91161   4.43045   2.34533   1.000 40.46234  ? 423  TYR A CD2   1 
ATOM   3411 C  CE1   . TYR A 1 423 ? 7.44814   4.96722   3.29002   1.000 40.31879  ? 423  TYR A CE1   1 
ATOM   3412 C  CE2   . TYR A 1 423 ? 5.66370   3.41824   2.91331   1.000 41.36598  ? 423  TYR A CE2   1 
ATOM   3413 C  CZ    . TYR A 1 423 ? 6.93133   3.69333   3.38323   1.000 41.08501  ? 423  TYR A CZ    1 
ATOM   3414 O  OH    . TYR A 1 423 ? 7.68649   2.69292   3.94829   1.000 41.13665  ? 423  TYR A OH    1 
ATOM   3415 N  N     . ALA A 1 424 ? 4.22427   8.30445   -1.77762  1.000 22.98418  ? 424  ALA A N     1 
ATOM   3416 C  CA    . ALA A 1 424 ? 3.22793   8.91906   -2.63834  1.000 23.10260  ? 424  ALA A CA    1 
ATOM   3417 C  C     . ALA A 1 424 ? 2.33028   7.85509   -3.25665  1.000 23.51132  ? 424  ALA A C     1 
ATOM   3418 O  O     . ALA A 1 424 ? 2.76548   6.74159   -3.56224  1.000 23.66997  ? 424  ALA A O     1 
ATOM   3419 C  CB    . ALA A 1 424 ? 3.90338   9.74115   -3.73632  1.000 23.27523  ? 424  ALA A CB    1 
ATOM   3420 N  N     . ALA A 1 425 ? 1.06007   8.20874   -3.43243  1.000 28.50919  ? 425  ALA A N     1 
ATOM   3421 C  CA    . ALA A 1 425 ? 0.09568   7.30817   -4.04395  1.000 28.60940  ? 425  ALA A CA    1 
ATOM   3422 C  C     . ALA A 1 425 ? -1.05951  8.12688   -4.59618  1.000 28.17790  ? 425  ALA A C     1 
ATOM   3423 O  O     . ALA A 1 425 ? -1.38058  9.20099   -4.08091  1.000 28.39390  ? 425  ALA A O     1 
ATOM   3424 C  CB    . ALA A 1 425 ? -0.41865  6.26438   -3.04691  1.000 28.83785  ? 425  ALA A CB    1 
ATOM   3425 N  N     . SER A 1 426 ? -1.67420  7.60621   -5.65173  1.000 25.66026  ? 426  SER A N     1 
ATOM   3426 C  CA    . SER A 1 426 ? -2.82717  8.24714   -6.26598  1.000 25.60129  ? 426  SER A CA    1 
ATOM   3427 C  C     . SER A 1 426 ? -4.09133  7.82554   -5.52035  1.000 25.45842  ? 426  SER A C     1 
ATOM   3428 O  O     . SER A 1 426 ? -4.03806  7.19488   -4.46101  1.000 25.55559  ? 426  SER A O     1 
ATOM   3429 C  CB    . SER A 1 426 ? -2.89509  7.89384   -7.74754  1.000 26.01944  ? 426  SER A CB    1 
ATOM   3430 O  OG    . SER A 1 426 ? -3.18350  6.51630   -7.91798  1.000 26.21624  ? 426  SER A OG    1 
ATOM   3431 N  N     . GLY A 1 427 ? -5.25567  8.16937   -6.07320  1.000 32.18201  ? 427  GLY A N     1 
ATOM   3432 C  CA    . GLY A 1 427 ? -6.50249  7.69987   -5.49914  1.000 31.99632  ? 427  GLY A CA    1 
ATOM   3433 C  C     . GLY A 1 427 ? -6.71001  6.20728   -5.63774  1.000 32.96662  ? 427  GLY A C     1 
ATOM   3434 O  O     . GLY A 1 427 ? -7.56944  5.64432   -4.95053  1.000 31.67674  ? 427  GLY A O     1 
ATOM   3435 N  N     . ALA A 1 428 ? -5.93984  5.55521   -6.51312  1.000 28.16378  ? 428  ALA A N     1 
ATOM   3436 C  CA    . ALA A 1 428 ? -6.06613  4.11261   -6.68645  1.000 28.16566  ? 428  ALA A CA    1 
ATOM   3437 C  C     . ALA A 1 428 ? -5.77094  3.37224   -5.38921  1.000 27.35945  ? 428  ALA A C     1 
ATOM   3438 O  O     . ALA A 1 428 ? -6.44516  2.38843   -5.06167  1.000 27.50450  ? 428  ALA A O     1 
ATOM   3439 C  CB    . ALA A 1 428 ? -5.13694  3.63536   -7.80249  1.000 28.63460  ? 428  ALA A CB    1 
ATOM   3440 N  N     . TYR A 1 429 ? -4.77097  3.83230   -4.63305  1.000 29.99717  ? 429  TYR A N     1 
ATOM   3441 C  CA    . TYR A 1 429 ? -4.44900  3.18395   -3.36550  1.000 29.74933  ? 429  TYR A CA    1 
ATOM   3442 C  C     . TYR A 1 429 ? -5.60262  3.31178   -2.37891  1.000 28.77502  ? 429  TYR A C     1 
ATOM   3443 O  O     . TYR A 1 429 ? -6.04177  2.31845   -1.78737  1.000 27.72846  ? 429  TYR A O     1 
ATOM   3444 C  CB    . TYR A 1 429 ? -3.16905  3.77573   -2.77099  1.000 29.93475  ? 429  TYR A CB    1 
ATOM   3445 C  CG    . TYR A 1 429 ? -2.80556  3.17583   -1.42870  1.000 29.85240  ? 429  TYR A CG    1 
ATOM   3446 C  CD1   . TYR A 1 429 ? -1.99859  2.04800   -1.34550  1.000 30.09643  ? 429  TYR A CD1   1 
ATOM   3447 C  CD2   . TYR A 1 429 ? -3.28452  3.72605   -0.24493  1.000 28.85101  ? 429  TYR A CD2   1 
ATOM   3448 C  CE1   . TYR A 1 429 ? -1.67301  1.49132   -0.12234  1.000 29.02327  ? 429  TYR A CE1   1 
ATOM   3449 C  CE2   . TYR A 1 429 ? -2.97186  3.17203   0.97644   1.000 28.10454  ? 429  TYR A CE2   1 
ATOM   3450 C  CZ    . TYR A 1 429 ? -2.16049  2.06019   1.03550   1.000 28.76367  ? 429  TYR A CZ    1 
ATOM   3451 O  OH    . TYR A 1 429 ? -1.84209  1.51193   2.25767   1.000 27.44337  ? 429  TYR A OH    1 
ATOM   3452 N  N     . ILE A 1 430 ? -6.09804  4.53689   -2.17843  1.000 30.31268  ? 430  ILE A N     1 
ATOM   3453 C  CA    . ILE A 1 430 ? -7.20901  4.74985   -1.25460  1.000 29.03246  ? 430  ILE A CA    1 
ATOM   3454 C  C     . ILE A 1 430 ? -8.43259  3.96264   -1.69837  1.000 28.66695  ? 430  ILE A C     1 
ATOM   3455 O  O     . ILE A 1 430 ? -9.20363  3.47108   -0.86418  1.000 28.42859  ? 430  ILE A O     1 
ATOM   3456 C  CB    . ILE A 1 430 ? -7.51595  6.25608   -1.12886  1.000 28.59792  ? 430  ILE A CB    1 
ATOM   3457 C  CG1   . ILE A 1 430 ? -6.32307  6.99274   -0.51810  1.000 28.38931  ? 430  ILE A CG1   1 
ATOM   3458 C  CG2   . ILE A 1 430 ? -8.76349  6.49010   -0.28939  1.000 27.24532  ? 430  ILE A CG2   1 
ATOM   3459 C  CD1   . ILE A 1 430 ? -6.15031  8.40019   -1.03406  1.000 28.52146  ? 430  ILE A CD1   1 
ATOM   3460 N  N     . ASP A 1 431 ? -8.62299  3.81294   -3.01029  1.000 37.55828  ? 431  ASP A N     1 
ATOM   3461 C  CA    . ASP A 1 431 ? -9.75605  3.04360   -3.51126  1.000 37.54256  ? 431  ASP A CA    1 
ATOM   3462 C  C     . ASP A 1 431 ? -9.62147  1.57007   -3.15250  1.000 37.42557  ? 431  ASP A C     1 
ATOM   3463 O  O     . ASP A 1 431 ? -10.57902 0.94579   -2.68245  1.000 36.50443  ? 431  ASP A O     1 
ATOM   3464 C  CB    . ASP A 1 431 ? -9.88596  3.21930   -5.02292  1.000 37.93937  ? 431  ASP A CB    1 
ATOM   3465 C  CG    . ASP A 1 431 ? -11.19064 2.67194   -5.55803  1.000 37.67276  ? 431  ASP A CG    1 
ATOM   3466 O  OD1   . ASP A 1 431 ? -12.19313 2.68740   -4.81259  1.000 37.35472  ? 431  ASP A OD1   1 
ATOM   3467 O  OD2   . ASP A 1 431 ? -11.21469 2.22729   -6.72382  1.000 38.65712  ? 431  ASP A OD2   1 
ATOM   3468 N  N     . ARG A 1 432 ? -8.43533  0.99651   -3.36184  1.000 47.97076  ? 432  ARG A N     1 
ATOM   3469 C  CA    . ARG A 1 432 ? -8.23238  -0.40842  -3.02590  1.000 47.59873  ? 432  ARG A CA    1 
ATOM   3470 C  C     . ARG A 1 432 ? -8.31152  -0.64943  -1.52100  1.000 46.19622  ? 432  ARG A C     1 
ATOM   3471 O  O     . ARG A 1 432 ? -8.67154  -1.74847  -1.08826  1.000 45.52046  ? 432  ARG A O     1 
ATOM   3472 C  CB    . ARG A 1 432 ? -6.88567  -0.88792  -3.57894  1.000 48.54369  ? 432  ARG A CB    1 
ATOM   3473 C  CG    . ARG A 1 432 ? -6.39427  -2.21975  -3.00958  1.000 47.72952  ? 432  ARG A CG    1 
ATOM   3474 C  CD    . ARG A 1 432 ? -5.19706  -2.77175  -3.77685  1.000 50.01539  ? 432  ARG A CD    1 
ATOM   3475 N  NE    . ARG A 1 432 ? -3.94162  -2.53493  -3.07273  1.000 50.72600  ? 432  ARG A NE    1 
ATOM   3476 C  CZ    . ARG A 1 432 ? -3.09258  -1.55501  -3.35295  1.000 52.00098  ? 432  ARG A CZ    1 
ATOM   3477 N  NH1   . ARG A 1 432 ? -3.31777  -0.70510  -4.34244  1.000 51.73182  ? 432  ARG A NH1   1 
ATOM   3478 N  NH2   . ARG A 1 432 ? -1.98910  -1.42436  -2.62152  1.000 51.76847  ? 432  ARG A NH2   1 
ATOM   3479 N  N     . MET A 1 433 ? -8.02185  0.36194   -0.70970  1.000 35.86167  ? 433  MET A N     1 
ATOM   3480 C  CA    . MET A 1 433 ? -7.82986  0.17164   0.72032   1.000 35.26053  ? 433  MET A CA    1 
ATOM   3481 C  C     . MET A 1 433 ? -8.98588  0.67126   1.57794   1.000 33.66459  ? 433  MET A C     1 
ATOM   3482 O  O     . MET A 1 433 ? -8.90065  0.59196   2.80885   1.000 32.97479  ? 433  MET A O     1 
ATOM   3483 C  CB    . MET A 1 433 ? -6.53552  0.87145   1.14103   1.000 35.47068  ? 433  MET A CB    1 
ATOM   3484 C  CG    . MET A 1 433 ? -5.24769  0.22412   0.61721   1.000 36.64544  ? 433  MET A CG    1 
ATOM   3485 S  SD    . MET A 1 433 ? -4.97078  -1.57480  0.60048   1.000 35.98831  ? 433  MET A SD    1 
ATOM   3486 C  CE    . MET A 1 433 ? -5.82139  -2.16192  2.06473   1.000 34.97196  ? 433  MET A CE    1 
ATOM   3487 N  N     . SER A 1 434 ? -10.05870 1.18187   0.97848   1.000 26.02738  ? 434  SER A N     1 
ATOM   3488 C  CA    . SER A 1 434 ? -11.12018 1.79261   1.76491   1.000 25.66537  ? 434  SER A CA    1 
ATOM   3489 C  C     . SER A 1 434 ? -12.45828 1.65556   1.05149   1.000 25.90592  ? 434  SER A C     1 
ATOM   3490 O  O     . SER A 1 434 ? -12.54297 1.17802   -0.08290  1.000 26.10234  ? 434  SER A O     1 
ATOM   3491 C  CB    . SER A 1 434 ? -10.82127 3.26856   2.04125   1.000 25.96437  ? 434  SER A CB    1 
ATOM   3492 O  OG    . SER A 1 434 ? -11.12986 4.06262   0.90922   1.000 26.70759  ? 434  SER A OG    1 
ATOM   3493 N  N     . ASP A 1 435 ? -13.51440 2.08314   1.74707   1.000 28.34228  ? 435  ASP A N     1 
ATOM   3494 C  CA    . ASP A 1 435 ? -14.85236 2.20128   1.18012   1.000 28.86913  ? 435  ASP A CA    1 
ATOM   3495 C  C     . ASP A 1 435 ? -15.25572 3.66318   0.99797   1.000 29.35747  ? 435  ASP A C     1 
ATOM   3496 O  O     . ASP A 1 435 ? -16.42914 4.01787   1.13522   1.000 29.63813  ? 435  ASP A O     1 
ATOM   3497 C  CB    . ASP A 1 435 ? -15.87357 1.45680   2.04251   1.000 27.41512  ? 435  ASP A CB    1 
ATOM   3498 C  CG    . ASP A 1 435 ? -15.93672 1.97628   3.47223   1.000 27.14224  ? 435  ASP A CG    1 
ATOM   3499 O  OD1   . ASP A 1 435 ? -15.12714 2.85404   3.83687   1.000 27.37927  ? 435  ASP A OD1   1 
ATOM   3500 O  OD2   . ASP A 1 435 ? -16.79890 1.49248   4.23796   1.000 26.48146  ? 435  ASP A OD2   1 
ATOM   3501 N  N     . TYR A 1 436 ? -14.28579 4.51815   0.67811   1.000 26.39427  ? 436  TYR A N     1 
ATOM   3502 C  CA    . TYR A 1 436 ? -14.51755 5.95217   0.56275   1.000 27.38084  ? 436  TYR A CA    1 
ATOM   3503 C  C     . TYR A 1 436 ? -14.98604 6.36462   -0.82549  1.000 28.44080  ? 436  TYR A C     1 
ATOM   3504 O  O     . TYR A 1 436 ? -15.87118 7.21792   -0.95227  1.000 28.64733  ? 436  TYR A O     1 
ATOM   3505 C  CB    . TYR A 1 436 ? -13.23644 6.72488   0.89253   1.000 26.92354  ? 436  TYR A CB    1 
ATOM   3506 C  CG    . TYR A 1 436 ? -12.89021 6.83282   2.36043   1.000 26.35056  ? 436  TYR A CG    1 
ATOM   3507 C  CD1   . TYR A 1 436 ? -13.84277 7.20850   3.29712   1.000 25.97507  ? 436  TYR A CD1   1 
ATOM   3508 C  CD2   . TYR A 1 436 ? -11.59731 6.58600   2.80457   1.000 25.83637  ? 436  TYR A CD2   1 
ATOM   3509 C  CE1   . TYR A 1 436 ? -13.51981 7.31794   4.63905   1.000 25.09049  ? 436  TYR A CE1   1 
ATOM   3510 C  CE2   . TYR A 1 436 ? -11.26568 6.69204   4.14211   1.000 25.13089  ? 436  TYR A CE2   1 
ATOM   3511 C  CZ    . TYR A 1 436 ? -12.22943 7.05850   5.05504   1.000 24.58613  ? 436  TYR A CZ    1 
ATOM   3512 O  OH    . TYR A 1 436 ? -11.89914 7.16540   6.38795   1.000 24.17510  ? 436  TYR A OH    1 
ATOM   3513 N  N     . CYS A 1 437 ? -14.40802 5.76922   -1.87070  1.000 31.57406  ? 437  CYS A N     1 
ATOM   3514 C  CA    . CYS A 1 437 ? -14.46192 6.38438   -3.19278  1.000 33.18485  ? 437  CYS A CA    1 
ATOM   3515 C  C     . CYS A 1 437 ? -15.83728 6.26900   -3.83955  1.000 32.53718  ? 437  CYS A C     1 
ATOM   3516 O  O     . CYS A 1 437 ? -16.23936 7.16929   -4.58471  1.000 33.07368  ? 437  CYS A O     1 
ATOM   3517 C  CB    . CYS A 1 437 ? -13.39381 5.76893   -4.09476  1.000 33.01544  ? 437  CYS A CB    1 
ATOM   3518 S  SG    . CYS A 1 437 ? -11.70377 6.07940   -3.53467  1.000 32.96649  ? 437  CYS A SG    1 
ATOM   3519 N  N     . LYS A 1 438 ? -16.57137 5.18318   -3.58860  0.848 37.76654  ? 438  LYS A N     1 
ATOM   3520 C  CA    . LYS A 1 438 ? -17.89598 5.07304   -4.19339  0.848 38.75072  ? 438  LYS A CA    1 
ATOM   3521 C  C     . LYS A 1 438 ? -18.86598 6.08415   -3.60019  0.848 39.16515  ? 438  LYS A C     1 
ATOM   3522 O  O     . LYS A 1 438 ? -19.77275 6.55457   -4.29662  0.848 39.89112  ? 438  LYS A O     1 
ATOM   3523 C  CB    . LYS A 1 438 ? -18.45674 3.65536   -4.05307  0.848 41.95665  ? 438  LYS A CB    1 
ATOM   3524 C  CG    . LYS A 1 438 ? -17.70593 2.57016   -4.83447  0.848 42.12996  ? 438  LYS A CG    1 
ATOM   3525 C  CD    . LYS A 1 438 ? -16.33848 2.21381   -4.26494  0.848 41.38191  ? 438  LYS A CD    1 
ATOM   3526 C  CE    . LYS A 1 438 ? -15.46491 1.52376   -5.30796  0.848 42.05860  ? 438  LYS A CE    1 
ATOM   3527 N  NZ    . LYS A 1 438 ? -15.16124 2.40442   -6.47586  0.848 42.91934  ? 438  LYS A NZ    1 
ATOM   3528 N  N     . GLY A 1 439 ? -18.69288 6.43247   -2.32859  1.000 41.98392  ? 439  GLY A N     1 
ATOM   3529 C  CA    . GLY A 1 439 ? -19.48424 7.49297   -1.74166  1.000 42.87711  ? 439  GLY A CA    1 
ATOM   3530 C  C     . GLY A 1 439 ? -18.95788 8.88971   -1.98561  1.000 42.96279  ? 439  GLY A C     1 
ATOM   3531 O  O     . GLY A 1 439 ? -19.61406 9.85895   -1.59476  1.000 43.67034  ? 439  GLY A O     1 
ATOM   3532 N  N     . CYS A 1 440 ? -17.79718 9.01562   -2.62411  1.000 29.05961  ? 440  CYS A N     1 
ATOM   3533 C  CA    . CYS A 1 440 ? -17.18648 10.31423  -2.86644  1.000 28.93619  ? 440  CYS A CA    1 
ATOM   3534 C  C     . CYS A 1 440 ? -17.80075 10.98571  -4.09042  1.000 29.90481  ? 440  CYS A C     1 
ATOM   3535 O  O     . CYS A 1 440 ? -18.22051 10.32495  -5.04440  1.000 29.55609  ? 440  CYS A O     1 
ATOM   3536 C  CB    . CYS A 1 440 ? -15.67576 10.16199  -3.05760  1.000 29.01764  ? 440  CYS A CB    1 
ATOM   3537 S  SG    . CYS A 1 440 ? -14.76065 11.71705  -3.17266  1.000 28.42020  ? 440  CYS A SG    1 
ATOM   3538 N  N     . ARG A 1 441 ? -17.85054 12.32085  -4.05395  1.000 41.69058  ? 441  ARG A N     1 
ATOM   3539 C  CA    . ARG A 1 441 ? -18.35835 13.07527  -5.19738  1.000 41.79475  ? 441  ARG A CA    1 
ATOM   3540 C  C     . ARG A 1 441 ? -17.40045 13.00818  -6.38111  1.000 41.38519  ? 441  ARG A C     1 
ATOM   3541 O  O     . ARG A 1 441 ? -17.82946 13.11518  -7.53666  1.000 42.20540  ? 441  ARG A O     1 
ATOM   3542 C  CB    . ARG A 1 441 ? -18.64099 14.52261  -4.77057  1.000 42.23262  ? 441  ARG A CB    1 
ATOM   3543 C  CG    . ARG A 1 441 ? -18.49457 15.60784  -5.83428  1.000 42.51972  ? 441  ARG A CG    1 
ATOM   3544 C  CD    . ARG A 1 441 ? -17.12430 16.28759  -5.77604  1.000 42.10927  ? 441  ARG A CD    1 
ATOM   3545 N  NE    . ARG A 1 441 ? -17.05822 17.49256  -6.59800  1.000 42.46515  ? 441  ARG A NE    1 
ATOM   3546 C  CZ    . ARG A 1 441 ? -17.26414 17.53725  -7.90949  1.000 43.11578  ? 441  ARG A CZ    1 
ATOM   3547 N  NH1   . ARG A 1 441 ? -17.53088 16.44612  -8.61250  1.000 43.48672  ? 441  ARG A NH1   1 
ATOM   3548 N  NH2   . ARG A 1 441 ? -17.19864 18.70856  -8.53492  1.000 43.85354  ? 441  ARG A NH2   1 
ATOM   3549 N  N     . TYR A 1 442 ? -16.11579 12.80402  -6.11896  1.000 28.85747  ? 442  TYR A N     1 
ATOM   3550 C  CA    . TYR A 1 442 ? -15.14140 12.69533  -7.18761  1.000 28.84172  ? 442  TYR A CA    1 
ATOM   3551 C  C     . TYR A 1 442 ? -15.14599 11.28828  -7.77996  1.000 28.99675  ? 442  TYR A C     1 
ATOM   3552 O  O     . TYR A 1 442 ? -15.68746 10.33992  -7.20429  1.000 29.70247  ? 442  TYR A O     1 
ATOM   3553 C  CB    . TYR A 1 442 ? -13.74863 13.05214  -6.67308  1.000 28.53463  ? 442  TYR A CB    1 
ATOM   3554 C  CG    . TYR A 1 442 ? -13.60646 14.49878  -6.25372  1.000 28.90628  ? 442  TYR A CG    1 
ATOM   3555 C  CD1   . TYR A 1 442 ? -13.60479 15.51810  -7.19768  1.000 28.45449  ? 442  TYR A CD1   1 
ATOM   3556 C  CD2   . TYR A 1 442 ? -13.47546 14.84616  -4.91394  1.000 28.21447  ? 442  TYR A CD2   1 
ATOM   3557 C  CE1   . TYR A 1 442 ? -13.47322 16.84289  -6.82050  1.000 28.62082  ? 442  TYR A CE1   1 
ATOM   3558 C  CE2   . TYR A 1 442 ? -13.34336 16.16878  -4.52727  1.000 28.00210  ? 442  TYR A CE2   1 
ATOM   3559 C  CZ    . TYR A 1 442 ? -13.34314 17.16246  -5.48462  1.000 28.68455  ? 442  TYR A CZ    1 
ATOM   3560 O  OH    . TYR A 1 442 ? -13.21202 18.48025  -5.10562  1.000 28.28180  ? 442  TYR A OH    1 
ATOM   3561 N  N     . ASP A 1 443 ? -14.53714 11.16745  -8.95629  1.000 38.29616  ? 443  ASP A N     1 
ATOM   3562 C  CA    . ASP A 1 443 ? -14.41849 9.90157   -9.67143  1.000 38.39778  ? 443  ASP A CA    1 
ATOM   3563 C  C     . ASP A 1 443 ? -12.96000 9.46715   -9.60950  1.000 38.62480  ? 443  ASP A C     1 
ATOM   3564 O  O     . ASP A 1 443 ? -12.09562 10.08656  -10.23926 1.000 38.95597  ? 443  ASP A O     1 
ATOM   3565 C  CB    . ASP A 1 443 ? -14.89259 10.04509  -11.11639 1.000 39.49823  ? 443  ASP A CB    1 
ATOM   3566 C  CG    . ASP A 1 443 ? -15.02396 8.70874   -11.82852 1.000 40.74177  ? 443  ASP A CG    1 
ATOM   3567 O  OD1   . ASP A 1 443 ? -14.44738 7.70750   -11.35258 1.000 40.29779  ? 443  ASP A OD1   1 
ATOM   3568 O  OD2   . ASP A 1 443 ? -15.71055 8.65926   -12.87091 1.000 41.40934  ? 443  ASP A OD2   1 
ATOM   3569 N  N     . VAL A 1 444 ? -12.69176 8.39534   -8.85888  1.000 33.76805  ? 444  VAL A N     1 
ATOM   3570 C  CA    . VAL A 1 444 ? -11.32508 7.91824   -8.67725  1.000 34.52101  ? 444  VAL A CA    1 
ATOM   3571 C  C     . VAL A 1 444 ? -10.73549 7.31071   -9.94111  1.000 34.91089  ? 444  VAL A C     1 
ATOM   3572 O  O     . VAL A 1 444 ? -9.52218  7.08137   -9.99902  1.000 35.19258  ? 444  VAL A O     1 
ATOM   3573 C  CB    . VAL A 1 444 ? -11.26965 6.90020   -7.51833  1.000 34.72594  ? 444  VAL A CB    1 
ATOM   3574 C  CG1   . VAL A 1 444 ? -11.58606 5.49533   -8.01452  1.000 34.22523  ? 444  VAL A CG1   1 
ATOM   3575 C  CG2   . VAL A 1 444 ? -9.91260  6.94554   -6.83089  1.000 34.45312  ? 444  VAL A CG2   1 
ATOM   3576 N  N     . LYS A 1 445 ? -11.55324 7.05017   -10.95719 1.000 35.51043  ? 445  LYS A N     1 
ATOM   3577 C  CA    . LYS A 1 445 ? -11.06507 6.51344   -12.21963 1.000 36.56196  ? 445  LYS A CA    1 
ATOM   3578 C  C     . LYS A 1 445 ? -10.70941 7.59894   -13.22645 1.000 37.33657  ? 445  LYS A C     1 
ATOM   3579 O  O     . LYS A 1 445 ? -10.35243 7.27395   -14.36354 1.000 37.95375  ? 445  LYS A O     1 
ATOM   3580 C  CB    . LYS A 1 445 ? -12.10317 5.56500   -12.82880 1.000 40.42599  ? 445  LYS A CB    1 
ATOM   3581 C  CG    . LYS A 1 445 ? -12.31829 4.28477   -12.03187 1.000 40.14314  ? 445  LYS A CG    1 
ATOM   3582 C  CD    . LYS A 1 445 ? -13.62388 3.59775   -12.41553 1.000 41.16905  ? 445  LYS A CD    1 
ATOM   3583 C  CE    . LYS A 1 445 ? -14.75472 4.59970   -12.59950 0.307 41.38717  ? 445  LYS A CE    1 
ATOM   3584 N  NZ    . LYS A 1 445 ? -15.36969 4.99488   -11.30094 0.727 40.48791  ? 445  LYS A NZ    1 
ATOM   3585 N  N     . LYS A 1 446 ? -10.79240 8.87052   -12.83964 1.000 40.17233  ? 446  LYS A N     1 
ATOM   3586 C  CA    . LYS A 1 446 ? -10.46968 9.98606   -13.71552 1.000 40.68514  ? 446  LYS A CA    1 
ATOM   3587 C  C     . LYS A 1 446 ? -9.33728  10.81212  -13.12054 1.000 40.48427  ? 446  LYS A C     1 
ATOM   3588 O  O     . LYS A 1 446 ? -9.17191  10.88609  -11.89935 1.000 39.78057  ? 446  LYS A O     1 
ATOM   3589 C  CB    . LYS A 1 446 ? -11.68950 10.88574  -13.95409 1.000 39.62927  ? 446  LYS A CB    1 
ATOM   3590 C  CG    . LYS A 1 446 ? -12.84981 10.19983  -14.65096 1.000 41.41145  ? 446  LYS A CG    1 
ATOM   3591 C  CD    . LYS A 1 446 ? -14.03812 11.13934  -14.77465 1.000 41.65362  ? 446  LYS A CD    1 
ATOM   3592 C  CE    . LYS A 1 446 ? -14.97013 10.71332  -15.89437 1.000 43.59239  ? 446  LYS A CE    1 
ATOM   3593 N  NZ    . LYS A 1 446 ? -16.04385 11.71870  -16.11859 1.000 44.27455  ? 446  LYS A NZ    1 
ATOM   3594 N  N     . ARG A 1 447 ? -8.56298  11.43957  -14.00117 1.000 38.73133  ? 447  ARG A N     1 
ATOM   3595 C  CA    . ARG A 1 447 ? -7.43767  12.27555  -13.61001 1.000 37.82466  ? 447  ARG A CA    1 
ATOM   3596 C  C     . ARG A 1 447 ? -7.61348  13.73945  -13.97819 1.000 38.36713  ? 447  ARG A C     1 
ATOM   3597 O  O     . ARG A 1 447 ? -7.09535  14.60628  -13.26958 1.000 38.07876  ? 447  ARG A O     1 
ATOM   3598 C  CB    . ARG A 1 447 ? -6.14237  11.74908  -14.24867 1.000 38.71912  ? 447  ARG A CB    1 
ATOM   3599 C  CG    . ARG A 1 447 ? -4.87572  12.44524  -13.78751 1.000 38.90799  ? 447  ARG A CG    1 
ATOM   3600 C  CD    . ARG A 1 447 ? -3.69009  12.01212  -14.62847 1.000 40.36878  ? 447  ARG A CD    1 
ATOM   3601 N  NE    . ARG A 1 447 ? -3.56621  10.56035  -14.67421 1.000 40.88330  ? 447  ARG A NE    1 
ATOM   3602 C  CZ    . ARG A 1 447 ? -2.89929  9.89522   -15.60716 1.000 41.60696  ? 447  ARG A CZ    1 
ATOM   3603 N  NH1   . ARG A 1 447 ? -2.28273  10.52239  -16.59550 1.000 42.15560  ? 447  ARG A NH1   1 
ATOM   3604 N  NH2   . ARG A 1 447 ? -2.84908  8.56761   -15.54658 1.000 42.00270  ? 447  ARG A NH2   1 
ATOM   3605 N  N     . LEU A 1 448 ? -8.34347  14.03859  -15.04841 1.000 35.17798  ? 448  LEU A N     1 
ATOM   3606 C  CA    . LEU A 1 448 ? -8.58648  15.40283  -15.48577 1.000 34.64991  ? 448  LEU A CA    1 
ATOM   3607 C  C     . LEU A 1 448 ? -10.07154 15.72342  -15.37983 1.000 34.76851  ? 448  LEU A C     1 
ATOM   3608 O  O     . LEU A 1 448 ? -10.92275 14.82982  -15.36015 1.000 35.21478  ? 448  LEU A O     1 
ATOM   3609 C  CB    . LEU A 1 448 ? -8.10531  15.61601  -16.92599 1.000 35.85044  ? 448  LEU A CB    1 
ATOM   3610 C  CG    . LEU A 1 448 ? -6.74542  15.00522  -17.26622 1.000 36.14267  ? 448  LEU A CG    1 
ATOM   3611 C  CD1   . LEU A 1 448 ? -6.43375  15.18446  -18.74245 1.000 37.55049  ? 448  LEU A CD1   1 
ATOM   3612 C  CD2   . LEU A 1 448 ? -5.65094  15.61663  -16.40412 1.000 36.09901  ? 448  LEU A CD2   1 
ATOM   3613 N  N     . GLY A 1 449 ? -10.37417 17.01497  -15.31338 1.000 41.49865  ? 449  GLY A N     1 
ATOM   3614 C  CA    . GLY A 1 449 ? -11.73850 17.48580  -15.20249 1.000 40.69535  ? 449  GLY A CA    1 
ATOM   3615 C  C     . GLY A 1 449 ? -12.14332 17.75077  -13.76137 1.000 40.38829  ? 449  GLY A C     1 
ATOM   3616 O  O     . GLY A 1 449 ? -11.44986 17.40196  -12.80239 1.000 38.98726  ? 449  GLY A O     1 
ATOM   3617 N  N     . ASP A 1 450 ? -13.31250 18.37994  -13.61915 1.000 49.16543  ? 450  ASP A N     1 
ATOM   3618 C  CA    . ASP A 1 450 ? -13.78873 18.76717  -12.29462 1.000 48.47861  ? 450  ASP A CA    1 
ATOM   3619 C  C     . ASP A 1 450 ? -14.20306 17.56103  -11.45959 1.000 47.79053  ? 450  ASP A C     1 
ATOM   3620 O  O     . ASP A 1 450 ? -14.14101 17.61486  -10.22610 1.000 47.10307  ? 450  ASP A O     1 
ATOM   3621 C  CB    . ASP A 1 450 ? -14.95345 19.74922  -12.42505 1.000 48.95577  ? 450  ASP A CB    1 
ATOM   3622 C  CG    . ASP A 1 450 ? -14.52342 21.09577  -12.98306 1.000 50.97499  ? 450  ASP A CG    1 
ATOM   3623 O  OD1   . ASP A 1 450 ? -13.31428 21.41012  -12.92842 1.000 50.12425  ? 450  ASP A OD1   1 
ATOM   3624 O  OD2   . ASP A 1 450 ? -15.39573 21.83727  -13.48433 1.000 51.55874  ? 450  ASP A OD2   1 
ATOM   3625 N  N     . ASP A 1 451 ? -14.63010 16.47405  -12.10266 1.000 42.61399  ? 451  ASP A N     1 
ATOM   3626 C  CA    . ASP A 1 451 ? -15.03567 15.27539  -11.38059 1.000 41.74434  ? 451  ASP A CA    1 
ATOM   3627 C  C     . ASP A 1 451 ? -13.85993 14.39324  -10.98043 1.000 40.58864  ? 451  ASP A C     1 
ATOM   3628 O  O     . ASP A 1 451 ? -14.05581 13.44347  -10.21877 1.000 40.88203  ? 451  ASP A O     1 
ATOM   3629 C  CB    . ASP A 1 451 ? -16.01397 14.45310  -12.22651 1.000 42.68784  ? 451  ASP A CB    1 
ATOM   3630 C  CG    . ASP A 1 451 ? -17.23259 15.24438  -12.64339 1.000 43.16050  ? 451  ASP A CG    1 
ATOM   3631 O  OD1   . ASP A 1 451 ? -17.97248 15.70937  -11.75188 1.000 42.70453  ? 451  ASP A OD1   1 
ATOM   3632 O  OD2   . ASP A 1 451 ? -17.44945 15.40061  -13.86403 1.000 45.55256  ? 451  ASP A OD2   1 
ATOM   3633 N  N     . ALA A 1 452 ? -12.65692 14.67677  -11.46794 1.000 30.91276  ? 452  ALA A N     1 
ATOM   3634 C  CA    . ALA A 1 452 ? -11.51890 13.80223  -11.22985 1.000 31.12968  ? 452  ALA A CA    1 
ATOM   3635 C  C     . ALA A 1 452 ? -11.11008 13.83131  -9.76412  1.000 31.06735  ? 452  ALA A C     1 
ATOM   3636 O  O     . ALA A 1 452 ? -11.13860 14.88291  -9.11609  1.000 30.41400  ? 452  ALA A O     1 
ATOM   3637 C  CB    . ALA A 1 452 ? -10.35035 14.22594  -12.11600 1.000 31.48119  ? 452  ALA A CB    1 
ATOM   3638 N  N     . CYS A 1 453 ? -10.73617 12.66642  -9.24402  1.000 27.94567  ? 453  CYS A N     1 
ATOM   3639 C  CA    . CYS A 1 453 ? -10.20230 12.58483  -7.89209  1.000 27.73411  ? 453  CYS A CA    1 
ATOM   3640 C  C     . CYS A 1 453 ? -8.90885  13.38813  -7.80878  1.000 27.82192  ? 453  CYS A C     1 
ATOM   3641 O  O     . CYS A 1 453 ? -7.98729  13.12589  -8.58971  1.000 28.58996  ? 453  CYS A O     1 
ATOM   3642 C  CB    . CYS A 1 453 ? -9.94758  11.13671  -7.51224  1.000 27.59329  ? 453  CYS A CB    1 
ATOM   3643 S  SG    . CYS A 1 453 ? -8.84079  10.90069  -6.11630  1.000 27.75096  ? 453  CYS A SG    1 
ATOM   3644 N  N     . PRO A 1 454 ? -8.79204  14.37753  -6.91092  1.000 26.34587  ? 454  PRO A N     1 
ATOM   3645 C  CA    . PRO A 1 454 ? -7.58811  15.23682  -6.93368  1.000 26.40237  ? 454  PRO A CA    1 
ATOM   3646 C  C     . PRO A 1 454 ? -6.29141  14.48525  -6.69791  1.000 27.67178  ? 454  PRO A C     1 
ATOM   3647 O  O     . PRO A 1 454 ? -5.25536  14.91231  -7.21425  1.000 27.52366  ? 454  PRO A O     1 
ATOM   3648 C  CB    . PRO A 1 454 ? -7.84538  16.26879  -5.82431  1.000 26.30070  ? 454  PRO A CB    1 
ATOM   3649 C  CG    . PRO A 1 454 ? -9.24038  16.09702  -5.40859  1.000 26.20937  ? 454  PRO A CG    1 
ATOM   3650 C  CD    . PRO A 1 454 ? -9.82028  14.85270  -5.96360  1.000 26.03294  ? 454  PRO A CD    1 
ATOM   3651 N  N     . PHE A 1 455 ? -6.31999  13.36476  -5.96795  1.000 22.14570  ? 455  PHE A N     1 
ATOM   3652 C  CA    . PHE A 1 455 ? -5.09884  12.60395  -5.70919  1.000 22.37321  ? 455  PHE A CA    1 
ATOM   3653 C  C     . PHE A 1 455 ? -4.45166  12.10862  -6.99789  1.000 23.63084  ? 455  PHE A C     1 
ATOM   3654 O  O     . PHE A 1 455 ? -3.23586  11.88781  -7.03625  1.000 24.20138  ? 455  PHE A O     1 
ATOM   3655 C  CB    . PHE A 1 455 ? -5.40268  11.41305  -4.79380  1.000 22.11618  ? 455  PHE A CB    1 
ATOM   3656 C  CG    . PHE A 1 455 ? -5.45414  11.75900  -3.32802  1.000 21.27770  ? 455  PHE A CG    1 
ATOM   3657 C  CD1   . PHE A 1 455 ? -6.64587  12.13997  -2.72988  1.000 21.59140  ? 455  PHE A CD1   1 
ATOM   3658 C  CD2   . PHE A 1 455 ? -4.31407  11.68593  -2.54664  1.000 20.58975  ? 455  PHE A CD2   1 
ATOM   3659 C  CE1   . PHE A 1 455 ? -6.69483  12.45480  -1.37911  1.000 20.28747  ? 455  PHE A CE1   1 
ATOM   3660 C  CE2   . PHE A 1 455 ? -4.35631  11.99665  -1.19769  1.000 19.80487  ? 455  PHE A CE2   1 
ATOM   3661 C  CZ    . PHE A 1 455 ? -5.54750  12.38161  -0.61359  1.000 19.58296  ? 455  PHE A CZ    1 
ATOM   3662 N  N     . ASN A 1 456 ? -5.24020  11.93202  -8.05892  1.000 28.97879  ? 456  ASN A N     1 
ATOM   3663 C  CA    . ASN A 1 456 ? -4.72502  11.32109  -9.27988  1.000 30.16434  ? 456  ASN A CA    1 
ATOM   3664 C  C     . ASN A 1 456 ? -3.75939  12.25286  -10.00433 1.000 30.88032  ? 456  ASN A C     1 
ATOM   3665 O  O     . ASN A 1 456 ? -2.60495  11.89221  -10.26105 1.000 31.98178  ? 456  ASN A O     1 
ATOM   3666 C  CB    . ASN A 1 456 ? -5.88831  10.92017  -10.18757 1.000 30.30720  ? 456  ASN A CB    1 
ATOM   3667 C  CG    . ASN A 1 456 ? -6.60125  9.67585   -9.69732  1.000 30.00202  ? 456  ASN A CG    1 
ATOM   3668 O  OD1   . ASN A 1 456 ? -6.04318  8.89035   -8.93128  1.000 29.78281  ? 456  ASN A OD1   1 
ATOM   3669 N  ND2   . ASN A 1 456 ? -7.83926  9.48786   -10.13934 1.000 29.54726  ? 456  ASN A ND2   1 
ATOM   3670 N  N     . ALA A 1 457 ? -4.21470  13.45967  -10.34875 1.000 24.05217  ? 457  ALA A N     1 
ATOM   3671 C  CA    . ALA A 1 457 ? -3.33523  14.39720  -11.03982 1.000 24.64328  ? 457  ALA A CA    1 
ATOM   3672 C  C     . ALA A 1 457 ? -2.22298  14.89963  -10.13011 1.000 23.75337  ? 457  ALA A C     1 
ATOM   3673 O  O     . ALA A 1 457 ? -1.10274  15.13816  -10.59624 1.000 24.71225  ? 457  ALA A O     1 
ATOM   3674 C  CB    . ALA A 1 457 ? -4.13977  15.57315  -11.58936 1.000 25.28375  ? 457  ALA A CB    1 
ATOM   3675 N  N     . LEU A 1 458 ? -2.50874  15.06564  -8.83708  1.000 23.38932  ? 458  LEU A N     1 
ATOM   3676 C  CA    . LEU A 1 458 ? -1.47863  15.51046  -7.90629  1.000 23.58037  ? 458  LEU A CA    1 
ATOM   3677 C  C     . LEU A 1 458 ? -0.38177  14.46640  -7.73952  1.000 24.39302  ? 458  LEU A C     1 
ATOM   3678 O  O     . LEU A 1 458 ? 0.78518   14.82394  -7.54423  1.000 25.60284  ? 458  LEU A O     1 
ATOM   3679 C  CB    . LEU A 1 458 ? -2.10581  15.84897  -6.55382  1.000 22.27914  ? 458  LEU A CB    1 
ATOM   3680 C  CG    . LEU A 1 458 ? -2.99199  17.09578  -6.52230  1.000 21.78584  ? 458  LEU A CG    1 
ATOM   3681 C  CD1   . LEU A 1 458 ? -3.80552  17.14640  -5.23739  1.000 20.57659  ? 458  LEU A CD1   1 
ATOM   3682 C  CD2   . LEU A 1 458 ? -2.15307  18.35504  -6.68147  1.000 22.66965  ? 458  LEU A CD2   1 
ATOM   3683 N  N     . TYR A 1 459 ? -0.72981  13.17998  -7.81462  1.000 29.08151  ? 459  TYR A N     1 
ATOM   3684 C  CA    . TYR A 1 459 ? 0.28178   12.13394  -7.70085  1.000 30.28260  ? 459  TYR A CA    1 
ATOM   3685 C  C     . TYR A 1 459 ? 1.23563   12.16477  -8.88673  1.000 32.08018  ? 459  TYR A C     1 
ATOM   3686 O  O     . TYR A 1 459 ? 2.45949   12.14343  -8.71399  1.000 33.46164  ? 459  TYR A O     1 
ATOM   3687 C  CB    . TYR A 1 459 ? -0.38476  10.76250  -7.59001  1.000 29.82615  ? 459  TYR A CB    1 
ATOM   3688 C  CG    . TYR A 1 459 ? 0.56391   9.60405   -7.80026  1.000 31.22496  ? 459  TYR A CG    1 
ATOM   3689 C  CD1   . TYR A 1 459 ? 1.47828   9.24442   -6.81901  1.000 31.35875  ? 459  TYR A CD1   1 
ATOM   3690 C  CD2   . TYR A 1 459 ? 0.54945   8.87335   -8.98224  1.000 32.60896  ? 459  TYR A CD2   1 
ATOM   3691 C  CE1   . TYR A 1 459 ? 2.34905   8.18841   -7.00545  1.000 32.89101  ? 459  TYR A CE1   1 
ATOM   3692 C  CE2   . TYR A 1 459 ? 1.41793   7.81459   -9.17820  1.000 33.66198  ? 459  TYR A CE2   1 
ATOM   3693 C  CZ    . TYR A 1 459 ? 2.31515   7.47759   -8.18546  1.000 33.58095  ? 459  TYR A CZ    1 
ATOM   3694 O  OH    . TYR A 1 459 ? 3.18313   6.42742   -8.36918  1.000 34.65194  ? 459  TYR A OH    1 
ATOM   3695 N  N     . TRP A 1 460 ? 0.69071   12.21802  -10.10312 1.000 32.23720  ? 460  TRP A N     1 
ATOM   3696 C  CA    . TRP A 1 460 ? 1.53683   12.17328  -11.28911 1.000 33.49692  ? 460  TRP A CA    1 
ATOM   3697 C  C     . TRP A 1 460 ? 2.33280   13.45756  -11.46460 1.000 33.64623  ? 460  TRP A C     1 
ATOM   3698 O  O     . TRP A 1 460 ? 3.44817   13.42430  -11.99594 1.000 35.08181  ? 460  TRP A O     1 
ATOM   3699 C  CB    . TRP A 1 460 ? 0.68621   11.88798  -12.52404 1.000 32.90611  ? 460  TRP A CB    1 
ATOM   3700 C  CG    . TRP A 1 460 ? 0.30014   10.45057  -12.61670 1.000 33.48214  ? 460  TRP A CG    1 
ATOM   3701 C  CD1   . TRP A 1 460 ? -0.96243  9.93540   -12.59388 1.000 32.35029  ? 460  TRP A CD1   1 
ATOM   3702 C  CD2   . TRP A 1 460 ? 1.18910   9.33285   -12.72080 1.000 33.86936  ? 460  TRP A CD2   1 
ATOM   3703 N  NE1   . TRP A 1 460 ? -0.91545  8.56522   -12.68863 1.000 32.57970  ? 460  TRP A NE1   1 
ATOM   3704 C  CE2   . TRP A 1 460 ? 0.39454   8.17083   -12.76778 1.000 33.85499  ? 460  TRP A CE2   1 
ATOM   3705 C  CE3   . TRP A 1 460 ? 2.58002   9.20262   -12.78664 1.000 35.02175  ? 460  TRP A CE3   1 
ATOM   3706 C  CZ2   . TRP A 1 460 ? 0.94432   6.89566   -12.87670 1.000 33.90841  ? 460  TRP A CZ2   1 
ATOM   3707 C  CZ3   . TRP A 1 460 ? 3.12347   7.93698   -12.89373 1.000 36.16977  ? 460  TRP A CZ3   1 
ATOM   3708 C  CH2   . TRP A 1 460 ? 2.30752   6.80029   -12.93681 1.000 35.30254  ? 460  TRP A CH2   1 
ATOM   3709 N  N     . ASP A 1 461 ? 1.78476   14.59228  -11.02978 1.000 31.29457  ? 461  ASP A N     1 
ATOM   3710 C  CA    . ASP A 1 461 ? 2.56542   15.82335  -11.03169 1.000 31.76513  ? 461  ASP A CA    1 
ATOM   3711 C  C     . ASP A 1 461 ? 3.72183   15.73538  -10.04510 1.000 32.28211  ? 461  ASP A C     1 
ATOM   3712 O  O     . ASP A 1 461 ? 4.80379   16.27708  -10.29773 1.000 33.24160  ? 461  ASP A O     1 
ATOM   3713 C  CB    . ASP A 1 461 ? 1.66780   17.01401  -10.70528 1.000 31.09732  ? 461  ASP A CB    1 
ATOM   3714 C  CG    . ASP A 1 461 ? 2.36789   18.34176  -10.90224 1.000 31.85932  ? 461  ASP A CG    1 
ATOM   3715 O  OD1   . ASP A 1 461 ? 2.69103   18.68039  -12.06000 1.000 32.34870  ? 461  ASP A OD1   1 
ATOM   3716 O  OD2   . ASP A 1 461 ? 2.59880   19.04557  -9.89786  1.000 31.40233  ? 461  ASP A OD2   1 
ATOM   3717 N  N     . PHE A 1 462 ? 3.51168   15.05044  -8.91872  1.000 25.35571  ? 462  PHE A N     1 
ATOM   3718 C  CA    . PHE A 1 462 ? 4.58197   14.86753  -7.94352  1.000 25.96393  ? 462  PHE A CA    1 
ATOM   3719 C  C     . PHE A 1 462 ? 5.71840   14.03838  -8.52914  1.000 27.03418  ? 462  PHE A C     1 
ATOM   3720 O  O     . PHE A 1 462 ? 6.89248   14.41523  -8.43352  1.000 27.52332  ? 462  PHE A O     1 
ATOM   3721 C  CB    . PHE A 1 462 ? 4.02305   14.21130  -6.67979  1.000 25.08266  ? 462  PHE A CB    1 
ATOM   3722 C  CG    . PHE A 1 462 ? 5.05786   13.93205  -5.62582  1.000 25.87146  ? 462  PHE A CG    1 
ATOM   3723 C  CD1   . PHE A 1 462 ? 5.42956   14.91526  -4.72401  1.000 25.40767  ? 462  PHE A CD1   1 
ATOM   3724 C  CD2   . PHE A 1 462 ? 5.64482   12.68134  -5.52522  1.000 26.39452  ? 462  PHE A CD2   1 
ATOM   3725 C  CE1   . PHE A 1 462 ? 6.37496   14.66112  -3.75082  1.000 24.34877  ? 462  PHE A CE1   1 
ATOM   3726 C  CE2   . PHE A 1 462 ? 6.59182   12.42013  -4.55283  1.000 26.26274  ? 462  PHE A CE2   1 
ATOM   3727 C  CZ    . PHE A 1 462 ? 6.95639   13.41100  -3.66392  1.000 24.64179  ? 462  PHE A CZ    1 
ATOM   3728 N  N     . ILE A 1 463 ? 5.38522   12.90032  -9.14192  1.000 32.91508  ? 463  ILE A N     1 
ATOM   3729 C  CA    . ILE A 1 463 ? 6.40740   12.05920  -9.75851  1.000 32.72298  ? 463  ILE A CA    1 
ATOM   3730 C  C     . ILE A 1 463 ? 7.09705   12.80391  -10.89363 1.000 33.70624  ? 463  ILE A C     1 
ATOM   3731 O  O     . ILE A 1 463 ? 8.30601   12.65608  -11.10929 1.000 34.05225  ? 463  ILE A O     1 
ATOM   3732 C  CB    . ILE A 1 463 ? 5.78793   10.73521  -10.24300 1.000 32.81163  ? 463  ILE A CB    1 
ATOM   3733 C  CG1   . ILE A 1 463 ? 4.94507   10.10545  -9.12980  1.000 32.06533  ? 463  ILE A CG1   1 
ATOM   3734 C  CG2   . ILE A 1 463 ? 6.87190   9.78476   -10.74135 1.000 34.22445  ? 463  ILE A CG2   1 
ATOM   3735 C  CD1   . ILE A 1 463 ? 5.69911   9.12203   -8.26133  1.000 32.39694  ? 463  ILE A CD1   1 
ATOM   3736 N  N     . ASP A 1 464 ? 6.34269   13.62120  -11.63238 1.000 37.22868  ? 464  ASP A N     1 
ATOM   3737 C  CA    . ASP A 1 464 ? 6.92884   14.37662  -12.73478 1.000 37.51779  ? 464  ASP A CA    1 
ATOM   3738 C  C     . ASP A 1 464 ? 7.83081   15.49465  -12.22569 1.000 37.88069  ? 464  ASP A C     1 
ATOM   3739 O  O     . ASP A 1 464 ? 8.88773   15.76056  -12.80975 1.000 38.34550  ? 464  ASP A O     1 
ATOM   3740 C  CB    . ASP A 1 464 ? 5.82330   14.94433  -13.62504 1.000 38.03265  ? 464  ASP A CB    1 
ATOM   3741 C  CG    . ASP A 1 464 ? 6.36755   15.70900  -14.81642 1.000 38.48438  ? 464  ASP A CG    1 
ATOM   3742 O  OD1   . ASP A 1 464 ? 6.59614   15.08351  -15.87313 1.000 39.56788  ? 464  ASP A OD1   1 
ATOM   3743 O  OD2   . ASP A 1 464 ? 6.56776   16.93616  -14.69613 1.000 38.52499  ? 464  ASP A OD2   1 
ATOM   3744 N  N     . ARG A 1 465 ? 7.42869   16.16150  -11.14149 1.000 46.40437  ? 465  ARG A N     1 
ATOM   3745 C  CA    . ARG A 1 465 ? 8.21795   17.26793  -10.60852 1.000 46.16903  ? 465  ARG A CA    1 
ATOM   3746 C  C     . ARG A 1 465 ? 9.57636   16.78869  -10.11296 1.000 46.11124  ? 465  ARG A C     1 
ATOM   3747 O  O     . ARG A 1 465 ? 10.60981  17.40402  -10.39986 1.000 46.38888  ? 465  ARG A O     1 
ATOM   3748 C  CB    . ARG A 1 465 ? 7.45037   17.95805  -9.47983  1.000 45.37271  ? 465  ARG A CB    1 
ATOM   3749 C  CG    . ARG A 1 465 ? 8.20623   19.09606  -8.81578  1.000 45.38905  ? 465  ARG A CG    1 
ATOM   3750 C  CD    . ARG A 1 465 ? 7.27775   19.95910  -7.97523  1.000 45.13714  ? 465  ARG A CD    1 
ATOM   3751 N  NE    . ARG A 1 465 ? 5.94317   20.05238  -8.55448  1.000 45.77167  ? 465  ARG A NE    1 
ATOM   3752 C  CZ    . ARG A 1 465 ? 5.57696   20.97113  -9.43760  1.000 45.65034  ? 465  ARG A CZ    1 
ATOM   3753 N  NH1   . ARG A 1 465 ? 6.42304   21.89455  -9.86432  1.000 45.14786  ? 465  ARG A NH1   1 
ATOM   3754 N  NH2   . ARG A 1 465 ? 4.33117   20.96379  -9.90379  1.000 44.63368  ? 465  ARG A NH2   1 
ATOM   3755 N  N     . HIS A 1 466 ? 9.59271   15.68628  -9.36589  1.000 30.91977  ? 466  HIS A N     1 
ATOM   3756 C  CA    . HIS A 1 466 ? 10.79635  15.18806  -8.71364  1.000 30.74753  ? 466  HIS A CA    1 
ATOM   3757 C  C     . HIS A 1 466 ? 11.36974  13.96837  -9.42971  1.000 31.38338  ? 466  HIS A C     1 
ATOM   3758 O  O     . HIS A 1 466 ? 11.99898  13.11408  -8.80224  1.000 31.08765  ? 466  HIS A O     1 
ATOM   3759 C  CB    . HIS A 1 466 ? 10.50157  14.85817  -7.25063  1.000 29.83746  ? 466  HIS A CB    1 
ATOM   3760 C  CG    . HIS A 1 466 ? 9.85823   15.98014  -6.49439  1.000 29.15507  ? 466  HIS A CG    1 
ATOM   3761 N  ND1   . HIS A 1 466 ? 10.50470  17.16892  -6.23147  1.000 28.67935  ? 466  HIS A ND1   1 
ATOM   3762 C  CD2   . HIS A 1 466 ? 8.62625   16.09249  -5.94262  1.000 28.75268  ? 466  HIS A CD2   1 
ATOM   3763 C  CE1   . HIS A 1 466 ? 9.69914   17.96496  -5.55110  1.000 28.03373  ? 466  HIS A CE1   1 
ATOM   3764 N  NE2   . HIS A 1 466 ? 8.55294   17.33576  -5.36268  1.000 28.05621  ? 466  HIS A NE2   1 
ATOM   3765 N  N     . ALA A 1 467 ? 11.16917  13.88503  -10.74733 1.000 42.90725  ? 467  ALA A N     1 
ATOM   3766 C  CA    . ALA A 1 467 ? 11.55555  12.68853  -11.49036 1.000 43.43838  ? 467  ALA A CA    1 
ATOM   3767 C  C     . ALA A 1 467 ? 13.05782  12.44089  -11.41256 1.000 43.81990  ? 467  ALA A C     1 
ATOM   3768 O  O     . ALA A 1 467 ? 13.49920  11.31055  -11.17509 1.000 44.75333  ? 467  ALA A O     1 
ATOM   3769 C  CB    . ALA A 1 467 ? 11.10324  12.80941  -12.94552 1.000 43.93515  ? 467  ALA A CB    1 
ATOM   3770 N  N     . GLN A 1 468 ? 13.86173  13.48917  -11.60724 0.954 50.86920  ? 468  GLN A N     1 
ATOM   3771 C  CA    . GLN A 1 468 ? 15.31112  13.31429  -11.60575 0.954 50.80107  ? 468  GLN A CA    1 
ATOM   3772 C  C     . GLN A 1 468 ? 15.81850  12.87965  -10.23605 0.954 50.34528  ? 468  GLN A C     1 
ATOM   3773 O  O     . GLN A 1 468 ? 16.67376  11.99158  -10.13655 0.954 50.67843  ? 468  GLN A O     1 
ATOM   3774 C  CB    . GLN A 1 468 ? 15.99759  14.60626  -12.04662 0.954 50.92288  ? 468  GLN A CB    1 
ATOM   3775 C  CG    . GLN A 1 468 ? 17.32888  14.38739  -12.74769 0.954 52.52482  ? 468  GLN A CG    1 
ATOM   3776 C  CD    . GLN A 1 468 ? 18.09017  15.67894  -12.97157 0.954 52.39801  ? 468  GLN A CD    1 
ATOM   3777 O  OE1   . GLN A 1 468 ? 17.55052  16.64668  -13.50913 0.954 52.75116  ? 468  GLN A OE1   1 
ATOM   3778 N  NE2   . GLN A 1 468 ? 19.35253  15.70043  -12.55930 0.954 52.56622  ? 468  GLN A NE2   1 
ATOM   3779 N  N     . ARG A 1 469 ? 15.30656  13.49559  -9.16753  1.000 54.48663  ? 469  ARG A N     1 
ATOM   3780 C  CA    . ARG A 1 469 ? 15.72943  13.11031  -7.82497  1.000 53.29573  ? 469  ARG A CA    1 
ATOM   3781 C  C     . ARG A 1 469 ? 15.28747  11.69170  -7.49280  1.000 53.63090  ? 469  ARG A C     1 
ATOM   3782 O  O     . ARG A 1 469 ? 16.04699  10.92272  -6.89095  1.000 53.08735  ? 469  ARG A O     1 
ATOM   3783 C  CB    . ARG A 1 469 ? 15.17933  14.09493  -6.79396  1.000 52.37752  ? 469  ARG A CB    1 
ATOM   3784 C  CG    . ARG A 1 469 ? 15.65670  13.82482  -5.37517  1.000 51.18584  ? 469  ARG A CG    1 
ATOM   3785 C  CD    . ARG A 1 469 ? 14.84360  14.61214  -4.35629  1.000 49.97213  ? 469  ARG A CD    1 
ATOM   3786 N  NE    . ARG A 1 469 ? 15.65544  15.17902  -3.28322  1.000 48.90675  ? 469  ARG A NE    1 
ATOM   3787 C  CZ    . ARG A 1 469 ? 16.37685  14.47824  -2.41609  1.000 47.95088  ? 469  ARG A CZ    1 
ATOM   3788 N  NH1   . ARG A 1 469 ? 16.37879  13.15373  -2.42073  1.000 48.17041  ? 469  ARG A NH1   1 
ATOM   3789 N  NH2   . ARG A 1 469 ? 17.10459  15.12380  -1.50883  1.000 47.07432  ? 469  ARG A NH2   1 
ATOM   3790 N  N     . LEU A 1 470 ? 14.06618  11.32414  -7.88563  1.000 45.51066  ? 470  LEU A N     1 
ATOM   3791 C  CA    . LEU A 1 470 ? 13.55573  9.99669   -7.57381  1.000 45.82767  ? 470  LEU A CA    1 
ATOM   3792 C  C     . LEU A 1 470 ? 14.27271  8.90687   -8.35820  1.000 46.41201  ? 470  LEU A C     1 
ATOM   3793 O  O     . LEU A 1 470 ? 14.29561  7.75454   -7.91294  1.000 46.86254  ? 470  LEU A O     1 
ATOM   3794 C  CB    . LEU A 1 470 ? 12.05350  9.93327   -7.84534  1.000 45.54757  ? 470  LEU A CB    1 
ATOM   3795 C  CG    . LEU A 1 470 ? 11.20782  10.70576  -6.83088  1.000 45.10502  ? 470  LEU A CG    1 
ATOM   3796 C  CD1   . LEU A 1 470 ? 9.86977   11.14303  -7.42848  1.000 45.53559  ? 470  LEU A CD1   1 
ATOM   3797 C  CD2   . LEU A 1 470 ? 11.02169  9.92304   -5.54874  1.000 44.60025  ? 470  LEU A CD2   1 
ATOM   3798 N  N     . ALA A 1 471 ? 14.85269  9.24305   -9.51343  1.000 46.89200  ? 471  ALA A N     1 
ATOM   3799 C  CA    . ALA A 1 471 ? 15.65390  8.27015   -10.24907 1.000 47.72917  ? 471  ALA A CA    1 
ATOM   3800 C  C     . ALA A 1 471 ? 16.90881  7.89455   -9.47343  1.000 47.01331  ? 471  ALA A C     1 
ATOM   3801 O  O     . ALA A 1 471 ? 17.31885  6.72805   -9.47178  1.000 46.51925  ? 471  ALA A O     1 
ATOM   3802 C  CB    . ALA A 1 471 ? 16.01946  8.81995   -11.62749 1.000 47.37363  ? 471  ALA A CB    1 
ATOM   3803 N  N     . GLY A 1 472 ? 17.53489  8.86993   -8.81171  1.000 78.21350  ? 472  GLY A N     1 
ATOM   3804 C  CA    . GLY A 1 472 ? 18.67761  8.56366   -7.97094  1.000 77.59098  ? 472  GLY A CA    1 
ATOM   3805 C  C     . GLY A 1 472 ? 18.30095  7.79763   -6.72000  1.000 76.67306  ? 472  GLY A C     1 
ATOM   3806 O  O     . GLY A 1 472 ? 19.10502  7.01601   -6.20269  1.000 76.03055  ? 472  GLY A O     1 
ATOM   3807 N  N     . ASN A 1 473 ? 17.08094  8.00712   -6.21860  1.000 74.24023  ? 473  ASN A N     1 
ATOM   3808 C  CA    . ASN A 1 473 ? 16.61374  7.28040   -5.04196  1.000 73.60108  ? 473  ASN A CA    1 
ATOM   3809 C  C     . ASN A 1 473 ? 16.64526  5.77565   -5.28525  1.000 73.30902  ? 473  ASN A C     1 
ATOM   3810 O  O     . ASN A 1 473 ? 17.27306  5.02231   -4.53236  1.000 72.57014  ? 473  ASN A O     1 
ATOM   3811 C  CB    . ASN A 1 473 ? 15.20384  7.74651   -4.66938  1.000 73.60419  ? 473  ASN A CB    1 
ATOM   3812 C  CG    . ASN A 1 473 ? 14.65007  7.02449   -3.45466  1.000 72.15949  ? 473  ASN A CG    1 
ATOM   3813 O  OD1   . ASN A 1 473 ? 14.01351  5.97747   -3.57606  1.000 72.26050  ? 473  ASN A OD1   1 
ATOM   3814 N  ND2   . ASN A 1 473 ? 14.88900  7.58424   -2.27395  1.000 69.21935  ? 473  ASN A ND2   1 
ATOM   3815 N  N     . GLY A 1 474 ? 15.97445  5.32089   -6.34130  1.000 64.94494  ? 474  GLY A N     1 
ATOM   3816 C  CA    . GLY A 1 474 ? 16.05148  3.92959   -6.74055  1.000 65.71824  ? 474  GLY A CA    1 
ATOM   3817 C  C     . GLY A 1 474 ? 14.77852  3.13627   -6.53108  1.000 65.38792  ? 474  GLY A C     1 
ATOM   3818 O  O     . GLY A 1 474 ? 14.38956  2.34153   -7.39222  1.000 65.87899  ? 474  GLY A O     1 
ATOM   3819 N  N     . ARG A 1 475 ? 14.11806  3.34238   -5.39374  0.889 56.18566  ? 475  ARG A N     1 
ATOM   3820 C  CA    . ARG A 1 475 ? 12.94133  2.56378   -5.02389  0.889 55.65419  ? 475  ARG A CA    1 
ATOM   3821 C  C     . ARG A 1 475 ? 11.66842  3.03866   -5.71904  0.889 57.06105  ? 475  ARG A C     1 
ATOM   3822 O  O     . ARG A 1 475 ? 10.57623  2.59767   -5.34459  0.889 56.34134  ? 475  ARG A O     1 
ATOM   3823 C  CB    . ARG A 1 475 ? 12.73763  2.59432   -3.50257  0.889 54.75921  ? 475  ARG A CB    1 
ATOM   3824 C  CG    . ARG A 1 475 ? 13.62236  1.63969   -2.68767  0.889 52.76510  ? 475  ARG A CG    1 
ATOM   3825 C  CD    . ARG A 1 475 ? 15.11140  1.91613   -2.85819  0.889 53.19605  ? 475  ARG A CD    1 
ATOM   3826 N  NE    . ARG A 1 475 ? 15.52838  3.12253   -2.15248  0.889 52.79758  ? 475  ARG A NE    1 
ATOM   3827 C  CZ    . ARG A 1 475 ? 16.34033  3.13876   -1.10367  0.889 51.30648  ? 475  ARG A CZ    1 
ATOM   3828 N  NH1   . ARG A 1 475 ? 16.86974  2.02621   -0.62133  0.889 49.52240  ? 475  ARG A NH1   1 
ATOM   3829 N  NH2   . ARG A 1 475 ? 16.63549  4.30206   -0.52948  0.889 50.14563  ? 475  ARG A NH2   1 
ATOM   3830 N  N     . MET A 1 476 ? 11.78236  3.91714   -6.71215  1.000 42.66863  ? 476  MET A N     1 
ATOM   3831 C  CA    . MET A 1 476 ? 10.64578  4.48492   -7.42743  1.000 43.06763  ? 476  MET A CA    1 
ATOM   3832 C  C     . MET A 1 476 ? 10.68097  4.08392   -8.89697  1.000 44.07696  ? 476  MET A C     1 
ATOM   3833 O  O     . MET A 1 476 ? 10.34595  4.87100   -9.78542  1.000 44.30494  ? 476  MET A O     1 
ATOM   3834 C  CB    . MET A 1 476 ? 10.62733  6.00528   -7.28793  1.000 42.63427  ? 476  MET A CB    1 
ATOM   3835 C  CG    . MET A 1 476 ? 10.29584  6.51007   -5.89282  1.000 40.96156  ? 476  MET A CG    1 
ATOM   3836 S  SD    . MET A 1 476 ? 8.75525   5.86075   -5.22579  1.000 41.27693  ? 476  MET A SD    1 
ATOM   3837 C  CE    . MET A 1 476 ? 7.69765   7.29717   -5.38836  1.000 41.35476  ? 476  MET A CE    1 
ATOM   3838 N  N     . MET A 1 477 ? 11.08517  2.84091   -9.16552  1.000 52.28338  ? 477  MET A N     1 
ATOM   3839 C  CA    . MET A 1 477 ? 11.35685  2.42721   -10.53834 1.000 52.20318  ? 477  MET A CA    1 
ATOM   3840 C  C     . MET A 1 477 ? 10.07530  2.33430   -11.35869 1.000 51.92276  ? 477  MET A C     1 
ATOM   3841 O  O     . MET A 1 477 ? 10.00198  2.86650   -12.47235 1.000 52.76041  ? 477  MET A O     1 
ATOM   3842 C  CB    . MET A 1 477 ? 12.10264  1.09317   -10.54078 1.000 54.95992  ? 477  MET A CB    1 
ATOM   3843 C  CG    . MET A 1 477 ? 12.23075  0.45796   -11.91201 1.000 55.88010  ? 477  MET A CG    1 
ATOM   3844 S  SD    . MET A 1 477 ? 13.72340  -0.54037  -12.05634 0.307 56.00301  ? 477  MET A SD    1 
ATOM   3845 C  CE    . MET A 1 477 ? 14.84468  0.38576   -11.00802 1.000 55.54967  ? 477  MET A CE    1 
ATOM   3846 N  N     . MET A 1 478 ? 9.05206   1.66734   -10.82489 1.000 51.16228  ? 478  MET A N     1 
ATOM   3847 C  CA    . MET A 1 478 ? 7.81957   1.48052   -11.58954 1.000 52.48121  ? 478  MET A CA    1 
ATOM   3848 C  C     . MET A 1 478 ? 7.09804   2.78954   -11.89109 0.725 52.69380  ? 478  MET A C     1 
ATOM   3849 O  O     . MET A 1 478 ? 6.69498   2.98754   -13.05083 1.000 52.05544  ? 478  MET A O     1 
ATOM   3850 C  CB    . MET A 1 478 ? 6.89990   0.49148   -10.86407 1.000 53.92319  ? 478  MET A CB    1 
ATOM   3851 C  CG    . MET A 1 478 ? 5.58482   0.23379   -11.59053 1.000 53.47581  ? 478  MET A CG    1 
ATOM   3852 S  SD    . MET A 1 478 ? 4.74626   -1.27117  -11.05367 0.463 52.52534  ? 478  MET A SD    1 
ATOM   3853 C  CE    . MET A 1 478 ? 3.18761   -0.60075  -10.47621 1.000 51.66448  ? 478  MET A CE    1 
ATOM   3854 N  N     . PRO A 1 479 ? 6.88778   3.70778   -10.93563 1.000 44.96763  ? 479  PRO A N     1 
ATOM   3855 C  CA    . PRO A 1 479 ? 6.20775   4.96521   -11.29874 1.000 44.61791  ? 479  PRO A CA    1 
ATOM   3856 C  C     . PRO A 1 479 ? 6.97249   5.78987   -12.31903 1.000 45.04889  ? 479  PRO A C     1 
ATOM   3857 O  O     . PRO A 1 479 ? 6.35938   6.39700   -13.20659 1.000 44.85844  ? 479  PRO A O     1 
ATOM   3858 C  CB    . PRO A 1 479 ? 6.08146   5.69746   -9.95375  1.000 44.12410  ? 479  PRO A CB    1 
ATOM   3859 C  CG    . PRO A 1 479 ? 6.17566   4.62857   -8.92375  1.000 43.18574  ? 479  PRO A CG    1 
ATOM   3860 C  CD    . PRO A 1 479 ? 7.13733   3.63100   -9.48422  1.000 43.36738  ? 479  PRO A CD    1 
ATOM   3861 N  N     . LEU A 1 480 ? 8.30245   5.82651   -12.21877 1.000 40.31002  ? 480  LEU A N     1 
ATOM   3862 C  CA    . LEU A 1 480 ? 9.09415   6.59076   -13.17644 1.000 41.04056  ? 480  LEU A CA    1 
ATOM   3863 C  C     . LEU A 1 480 ? 9.03239   5.96623   -14.56429 1.000 42.00989  ? 480  LEU A C     1 
ATOM   3864 O  O     . LEU A 1 480 ? 8.99564   6.68088   -15.57356 1.000 42.37403  ? 480  LEU A O     1 
ATOM   3865 C  CB    . LEU A 1 480 ? 10.53892  6.68860   -12.69148 1.000 41.42844  ? 480  LEU A CB    1 
ATOM   3866 C  CG    . LEU A 1 480 ? 10.83000  7.84342   -11.73383 1.000 40.77881  ? 480  LEU A CG    1 
ATOM   3867 C  CD1   . LEU A 1 480 ? 12.27499  7.80311   -11.28490 1.000 40.56779  ? 480  LEU A CD1   1 
ATOM   3868 C  CD2   . LEU A 1 480 ? 10.50680  9.17645   -12.39143 1.000 40.89777  ? 480  LEU A CD2   1 
ATOM   3869 N  N     . ARG A 1 481 ? 9.02077   4.63310   -14.63281 1.000 66.23222  ? 481  ARG A N     1 
ATOM   3870 C  CA    . ARG A 1 481 ? 8.91759   3.95775   -15.92128 1.000 65.81966  ? 481  ARG A CA    1 
ATOM   3871 C  C     . ARG A 1 481 ? 7.57988   4.25006   -16.58668 1.000 65.58289  ? 481  ARG A C     1 
ATOM   3872 O  O     . ARG A 1 481 ? 7.51648   4.47450   -17.80087 1.000 66.21451  ? 481  ARG A O     1 
ATOM   3873 C  CB    . ARG A 1 481 ? 9.11220   2.45296   -15.73783 1.000 69.34399  ? 481  ARG A CB    1 
ATOM   3874 C  CG    . ARG A 1 481 ? 10.47491  1.94862   -16.17614 1.000 70.04870  ? 481  ARG A CG    1 
ATOM   3875 C  CD    . ARG A 1 481 ? 10.56146  0.43862   -16.07933 1.000 69.67602  ? 481  ARG A CD    1 
ATOM   3876 N  NE    . ARG A 1 481 ? 11.78889  -0.07248  -16.67623 1.000 70.21527  ? 481  ARG A NE    1 
ATOM   3877 C  CZ    . ARG A 1 481 ? 11.89475  -1.25753  -17.26042 1.000 70.13832  ? 481  ARG A CZ    1 
ATOM   3878 N  NH1   . ARG A 1 481 ? 10.86844  -2.08803  -17.32509 1.000 69.53634  ? 481  ARG A NH1   1 
ATOM   3879 N  NH2   . ARG A 1 481 ? 13.05705  -1.61520  -17.79895 1.000 70.65150  ? 481  ARG A NH2   1 
ATOM   3880 N  N     . THR A 1 482 ? 6.49891   4.25655   -15.80458 1.000 49.36637  ? 482  THR A N     1 
ATOM   3881 C  CA    . THR A 1 482 ? 5.19017   4.59049   -16.35451 1.000 49.43048  ? 482  THR A CA    1 
ATOM   3882 C  C     . THR A 1 482 ? 5.14537   6.04458   -16.80649 1.000 49.35154  ? 482  THR A C     1 
ATOM   3883 O  O     . THR A 1 482 ? 4.58807   6.35686   -17.86572 1.000 50.21345  ? 482  THR A O     1 
ATOM   3884 C  CB    . THR A 1 482 ? 4.10319   4.31268   -15.31509 1.000 48.45792  ? 482  THR A CB    1 
ATOM   3885 O  OG1   . THR A 1 482 ? 4.00290   2.90090   -15.09629 1.000 48.50261  ? 482  THR A OG1   1 
ATOM   3886 C  CG2   . THR A 1 482 ? 2.75710   4.82943   -15.79468 1.000 48.08260  ? 482  THR A CG2   1 
ATOM   3887 N  N     . LEU A 1 483 ? 5.74108   6.94451   -16.02018 1.000 44.93176  ? 483  LEU A N     1 
ATOM   3888 C  CA    . LEU A 1 483 ? 5.78723   8.35213   -16.40091 1.000 45.50367  ? 483  LEU A CA    1 
ATOM   3889 C  C     . LEU A 1 483 ? 6.58410   8.55285   -17.68491 1.000 45.74358  ? 483  LEU A C     1 
ATOM   3890 O  O     . LEU A 1 483 ? 6.22410   9.38826   -18.52270 1.000 45.11578  ? 483  LEU A O     1 
ATOM   3891 C  CB    . LEU A 1 483 ? 6.38308   9.18145   -15.26245 1.000 44.98166  ? 483  LEU A CB    1 
ATOM   3892 C  CG    . LEU A 1 483 ? 6.70398   10.64465  -15.57679 1.000 44.09884  ? 483  LEU A CG    1 
ATOM   3893 C  CD1   . LEU A 1 483 ? 5.44665   11.50558  -15.54813 1.000 43.40333  ? 483  LEU A CD1   1 
ATOM   3894 C  CD2   . LEU A 1 483 ? 7.76535   11.18957  -14.63008 1.000 44.36232  ? 483  LEU A CD2   1 
ATOM   3895 N  N     . GLU A 1 484 ? 7.66560   7.78871   -17.86386 0.802 55.97437  ? 484  GLU A N     1 
ATOM   3896 C  CA    . GLU A 1 484 ? 8.49518   7.94607   -19.05320 0.802 56.84061  ? 484  GLU A CA    1 
ATOM   3897 C  C     . GLU A 1 484 ? 7.80495   7.44016   -20.31486 0.802 57.24729  ? 484  GLU A C     1 
ATOM   3898 O  O     . GLU A 1 484 ? 8.13114   7.90699   -21.41116 0.802 57.02002  ? 484  GLU A O     1 
ATOM   3899 C  CB    . GLU A 1 484 ? 9.83589   7.23034   -18.86262 0.802 60.59135  ? 484  GLU A CB    1 
ATOM   3900 C  CG    . GLU A 1 484 ? 9.91726   5.85356   -19.50545 0.802 60.83839  ? 484  GLU A CG    1 
ATOM   3901 C  CD    . GLU A 1 484 ? 11.07306  5.02932   -18.97941 0.802 61.12588  ? 484  GLU A CD    1 
ATOM   3902 O  OE1   . GLU A 1 484 ? 10.85778  3.84383   -18.65233 0.802 61.29943  ? 484  GLU A OE1   1 
ATOM   3903 O  OE2   . GLU A 1 484 ? 12.19505  5.56925   -18.88872 0.802 61.09037  ? 484  GLU A OE2   1 
ATOM   3904 N  N     . LYS A 1 485 ? 6.85990   6.50998   -20.18872 1.000 62.02001  ? 485  LYS A N     1 
ATOM   3905 C  CA    . LYS A 1 485 ? 6.10309   6.00495   -21.32739 1.000 60.92928  ? 485  LYS A CA    1 
ATOM   3906 C  C     . LYS A 1 485 ? 4.88180   6.86248   -21.64839 1.000 61.71337  ? 485  LYS A C     1 
ATOM   3907 O  O     . LYS A 1 485 ? 4.14824   6.55267   -22.59392 1.000 61.95349  ? 485  LYS A O     1 
ATOM   3908 C  CB    . LYS A 1 485 ? 5.70568   4.53950   -21.07295 1.000 64.36589  ? 485  LYS A CB    1 
ATOM   3909 C  CG    . LYS A 1 485 ? 4.26152   4.28191   -20.66264 0.676 63.13495  ? 485  LYS A CG    1 
ATOM   3910 C  CD    . LYS A 1 485 ? 3.94566   2.79454   -20.72835 0.648 63.59776  ? 485  LYS A CD    1 
ATOM   3911 C  CE    . LYS A 1 485 ? 3.58461   2.36599   -22.14140 0.725 64.73616  ? 485  LYS A CE    1 
ATOM   3912 N  NZ    . LYS A 1 485 ? 2.97613   1.00713   -22.18346 1.000 64.76296  ? 485  LYS A NZ    1 
ATOM   3913 N  N     . MET A 1 486 ? 4.67851   7.95780   -20.91643 1.000 50.34796  ? 486  MET A N     1 
ATOM   3914 C  CA    . MET A 1 486 ? 3.55801   8.87932   -21.07414 1.000 49.63050  ? 486  MET A CA    1 
ATOM   3915 C  C     . MET A 1 486 ? 3.90045   9.94854   -22.10772 1.000 50.24987  ? 486  MET A C     1 
ATOM   3916 O  O     . MET A 1 486 ? 4.95109   10.59277  -21.99617 1.000 51.57205  ? 486  MET A O     1 
ATOM   3917 C  CB    . MET A 1 486 ? 3.22560   9.53744   -19.74192 1.000 49.40353  ? 486  MET A CB    1 
ATOM   3918 C  CG    . MET A 1 486 ? 1.93523   9.05338   -19.10409 1.000 48.32477  ? 486  MET A CG    1 
ATOM   3919 S  SD    . MET A 1 486 ? 1.36606   10.13068  -17.77347 1.000 48.73697  ? 486  MET A SD    1 
ATOM   3920 C  CE    . MET A 1 486 ? 1.27653   8.97008   -16.41534 1.000 46.45103  ? 486  MET A CE    1 
ATOM   3921 N  N     . PRO A 1 487 ? 3.05661   10.16280  -23.11535 1.000 40.35739  ? 487  PRO A N     1 
ATOM   3922 C  CA    . PRO A 1 487 ? 3.34066   11.20297  -24.11062 1.000 41.63478  ? 487  PRO A CA    1 
ATOM   3923 C  C     . PRO A 1 487 ? 3.27303   12.59526  -23.50022 1.000 40.55357  ? 487  PRO A C     1 
ATOM   3924 O  O     . PRO A 1 487 ? 2.69490   12.81304  -22.43288 1.000 38.94069  ? 487  PRO A O     1 
ATOM   3925 C  CB    . PRO A 1 487 ? 2.24424   11.00091  -25.16174 1.000 42.98454  ? 487  PRO A CB    1 
ATOM   3926 C  CG    . PRO A 1 487 ? 1.13789   10.32430  -24.42293 1.000 41.87547  ? 487  PRO A CG    1 
ATOM   3927 C  CD    . PRO A 1 487 ? 1.80209   9.44716   -23.40206 1.000 40.69268  ? 487  PRO A CD    1 
ATOM   3928 N  N     . ASP A 1 488 ? 3.88122   13.55016  -24.21027 0.811 48.58110  ? 488  ASP A N     1 
ATOM   3929 C  CA    . ASP A 1 488 ? 4.04691   14.89374  -23.66191 0.811 49.16154  ? 488  ASP A CA    1 
ATOM   3930 C  C     . ASP A 1 488 ? 2.70312   15.56434  -23.40013 0.811 48.23486  ? 488  ASP A C     1 
ATOM   3931 O  O     . ASP A 1 488 ? 2.55037   16.29600  -22.41493 0.811 47.77084  ? 488  ASP A O     1 
ATOM   3932 C  CB    . ASP A 1 488 ? 4.90026   15.74323  -24.60559 0.811 50.04022  ? 488  ASP A CB    1 
ATOM   3933 C  CG    . ASP A 1 488 ? 6.38531   15.44902  -24.47469 0.811 51.38840  ? 488  ASP A CG    1 
ATOM   3934 O  OD1   . ASP A 1 488 ? 6.78661   14.84460  -23.45839 0.811 51.63434  ? 488  ASP A OD1   1 
ATOM   3935 O  OD2   . ASP A 1 488 ? 7.15133   15.81944  -25.38851 0.811 51.81906  ? 488  ASP A OD2   1 
ATOM   3936 N  N     . ALA A 1 489 ? 1.71440   15.32250  -24.26591 1.000 51.33098  ? 489  ALA A N     1 
ATOM   3937 C  CA    . ALA A 1 489 ? 0.40630   15.94606  -24.08778 1.000 50.47640  ? 489  ALA A CA    1 
ATOM   3938 C  C     . ALA A 1 489 ? -0.29404  15.44501  -22.83091 1.000 48.74855  ? 489  ALA A C     1 
ATOM   3939 O  O     . ALA A 1 489 ? -1.05200  16.19500  -22.20509 1.000 47.56622  ? 489  ALA A O     1 
ATOM   3940 C  CB    . ALA A 1 489 ? -0.46666  15.69887  -25.31730 1.000 50.53303  ? 489  ALA A CB    1 
ATOM   3941 N  N     . GLU A 1 490 ? -0.06036  14.18820  -22.44788 1.000 47.20685  ? 490  GLU A N     1 
ATOM   3942 C  CA    . GLU A 1 490 ? -0.62999  13.68505  -21.20345 1.000 46.72059  ? 490  GLU A CA    1 
ATOM   3943 C  C     . GLU A 1 490 ? 0.10589   14.24001  -19.99068 1.000 47.30332  ? 490  GLU A C     1 
ATOM   3944 O  O     . GLU A 1 490 ? -0.51598  14.48714  -18.95086 1.000 45.69434  ? 490  GLU A O     1 
ATOM   3945 C  CB    . GLU A 1 490 ? -0.60565  12.15709  -21.19545 1.000 46.34645  ? 490  GLU A CB    1 
ATOM   3946 C  CG    . GLU A 1 490 ? -1.49205  11.52292  -20.13690 1.000 46.10841  ? 490  GLU A CG    1 
ATOM   3947 C  CD    . GLU A 1 490 ? -1.26521  10.02970  -20.01489 1.000 47.03190  ? 490  GLU A CD    1 
ATOM   3948 O  OE1   . GLU A 1 490 ? -0.74136  9.43197   -20.97775 1.000 47.65196  ? 490  GLU A OE1   1 
ATOM   3949 O  OE2   . GLU A 1 490 ? -1.60517  9.45370   -18.95935 1.000 46.61927  ? 490  GLU A OE2   1 
ATOM   3950 N  N     . ARG A 1 491 ? 1.42113   14.44472  -20.10482 1.000 55.35911  ? 491  ARG A N     1 
ATOM   3951 C  CA    . ARG A 1 491 ? 2.17714   15.05871  -19.01739 1.000 54.61007  ? 491  ARG A CA    1 
ATOM   3952 C  C     . ARG A 1 491 ? 1.68678   16.47473  -18.74510 1.000 54.58813  ? 491  ARG A C     1 
ATOM   3953 O  O     . ARG A 1 491 ? 1.36722   16.82651  -17.60395 1.000 53.45841  ? 491  ARG A O     1 
ATOM   3954 C  CB    . ARG A 1 491 ? 3.66858   15.07185  -19.35175 1.000 56.13934  ? 491  ARG A CB    1 
ATOM   3955 C  CG    . ARG A 1 491 ? 4.34986   13.71379  -19.37085 1.000 57.30893  ? 491  ARG A CG    1 
ATOM   3956 C  CD    . ARG A 1 491 ? 5.85113   13.89334  -19.20611 1.000 58.25748  ? 491  ARG A CD    1 
ATOM   3957 N  NE    . ARG A 1 491 ? 6.56696   12.63255  -19.05942 1.000 59.04335  ? 491  ARG A NE    1 
ATOM   3958 C  CZ    . ARG A 1 491 ? 7.68594   12.48633  -18.36292 1.000 60.26620  ? 491  ARG A CZ    1 
ATOM   3959 N  NH1   . ARG A 1 491 ? 8.22125   13.49571  -17.69495 1.000 59.01426  ? 491  ARG A NH1   1 
ATOM   3960 N  NH2   . ARG A 1 491 ? 8.28670   11.29960  -18.34119 1.000 60.67414  ? 491  ARG A NH2   1 
ATOM   3961 N  N     . GLU A 1 492 ? 1.62076   17.30439  -19.79034 1.000 44.03777  ? 492  GLU A N     1 
ATOM   3962 C  CA    . GLU A 1 492 ? 1.17468   18.68265  -19.61724 1.000 43.27937  ? 492  GLU A CA    1 
ATOM   3963 C  C     . GLU A 1 492 ? -0.26641  18.74904  -19.13085 0.874 42.14204  ? 492  GLU A C     1 
ATOM   3964 O  O     . GLU A 1 492 ? -0.65883  19.72902  -18.48715 1.000 41.41974  ? 492  GLU A O     1 
ATOM   3965 C  CB    . GLU A 1 492 ? 1.32632   19.45170  -20.93068 1.000 43.27885  ? 492  GLU A CB    1 
ATOM   3966 C  CG    . GLU A 1 492 ? 2.76409   19.79208  -21.29203 1.000 45.42918  ? 492  GLU A CG    1 
ATOM   3967 C  CD    . GLU A 1 492 ? 3.16301   19.26455  -22.65785 0.000 48.39221  ? 492  GLU A CD    1 
ATOM   3968 O  OE1   . GLU A 1 492 ? 4.28600   18.73295  -22.78707 0.599 48.02016  ? 492  GLU A OE1   1 
ATOM   3969 O  OE2   . GLU A 1 492 ? 2.35384   19.37989  -23.60269 0.657 49.07247  ? 492  GLU A OE2   1 
ATOM   3970 N  N     . ALA A 1 493 ? -1.06310  17.71673  -19.41876 1.000 39.53948  ? 493  ALA A N     1 
ATOM   3971 C  CA    . ALA A 1 493 ? -2.46817  17.72471  -19.02450 1.000 38.53107  ? 493  ALA A CA    1 
ATOM   3972 C  C     . ALA A 1 493 ? -2.62255  17.63827  -17.50965 1.000 37.94000  ? 493  ALA A C     1 
ATOM   3973 O  O     . ALA A 1 493 ? -3.30229  18.47234  -16.89967 1.000 37.01203  ? 493  ALA A O     1 
ATOM   3974 C  CB    . ALA A 1 493 ? -3.21168  16.58069  -19.71234 1.000 37.97093  ? 493  ALA A CB    1 
ATOM   3975 N  N     . PHE A 1 494 ? -2.00617  16.63254  -16.87868 1.000 31.68674  ? 494  PHE A N     1 
ATOM   3976 C  CA    . PHE A 1 494 ? -2.11708  16.53557  -15.42724 1.000 30.05755  ? 494  PHE A CA    1 
ATOM   3977 C  C     . PHE A 1 494 ? -1.32000  17.62408  -14.72280 1.000 29.38830  ? 494  PHE A C     1 
ATOM   3978 O  O     . PHE A 1 494 ? -1.62311  17.94623  -13.56926 1.000 28.21694  ? 494  PHE A O     1 
ATOM   3979 C  CB    . PHE A 1 494 ? -1.71446  15.13193  -14.93240 1.000 29.45759  ? 494  PHE A CB    1 
ATOM   3980 C  CG    . PHE A 1 494 ? -0.24552  14.78796  -15.08982 1.000 29.80682  ? 494  PHE A CG    1 
ATOM   3981 C  CD1   . PHE A 1 494 ? 0.73716   15.42718  -14.34463 1.000 29.72347  ? 494  PHE A CD1   1 
ATOM   3982 C  CD2   . PHE A 1 494 ? 0.14056   13.77558  -15.95126 1.000 30.67024  ? 494  PHE A CD2   1 
ATOM   3983 C  CE1   . PHE A 1 494 ? 2.07057   15.09332  -14.48952 1.000 30.49540  ? 494  PHE A CE1   1 
ATOM   3984 C  CE2   . PHE A 1 494 ? 1.47206   13.43184  -16.09198 1.000 31.41804  ? 494  PHE A CE2   1 
ATOM   3985 C  CZ    . PHE A 1 494 ? 2.43762   14.09345  -15.36291 1.000 31.33363  ? 494  PHE A CZ    1 
ATOM   3986 N  N     . ARG A 1 495 ? -0.31258  18.19465  -15.38697 1.000 34.42691  ? 495  ARG A N     1 
ATOM   3987 C  CA    . ARG A 1 495 ? 0.37358   19.35367  -14.82807 1.000 35.14681  ? 495  ARG A CA    1 
ATOM   3988 C  C     . ARG A 1 495 ? -0.59266  20.51844  -14.65848 1.000 33.94150  ? 495  ARG A C     1 
ATOM   3989 O  O     . ARG A 1 495 ? -0.73131  21.06899  -13.56094 1.000 33.80216  ? 495  ARG A O     1 
ATOM   3990 C  CB    . ARG A 1 495 ? 1.55065   19.75251  -15.72015 1.000 35.86209  ? 495  ARG A CB    1 
ATOM   3991 C  CG    . ARG A 1 495 ? 2.77630   18.86438  -15.57674 1.000 36.79451  ? 495  ARG A CG    1 
ATOM   3992 C  CD    . ARG A 1 495 ? 3.93200   19.38529  -16.41687 1.000 37.68478  ? 495  ARG A CD    1 
ATOM   3993 N  NE    . ARG A 1 495 ? 4.95492   18.36888  -16.63195 1.000 38.86582  ? 495  ARG A NE    1 
ATOM   3994 C  CZ    . ARG A 1 495 ? 5.46827   18.06352  -17.81591 1.000 40.43502  ? 495  ARG A CZ    1 
ATOM   3995 N  NH1   . ARG A 1 495 ? 5.08072   18.68451  -18.91798 1.000 39.65579  ? 495  ARG A NH1   1 
ATOM   3996 N  NH2   . ARG A 1 495 ? 6.39295   17.11057  -17.89629 1.000 39.93435  ? 495  ARG A NH2   1 
ATOM   3997 N  N     . LYS A 1 496 ? -1.28479  20.89385  -15.73933 1.000 36.30337  ? 496  LYS A N     1 
ATOM   3998 C  CA    . LYS A 1 496 ? -2.26844  21.97144  -15.66634 1.000 35.89210  ? 496  LYS A CA    1 
ATOM   3999 C  C     . LYS A 1 496 ? -3.32509  21.68717  -14.60682 1.000 34.83558  ? 496  LYS A C     1 
ATOM   4000 O  O     . LYS A 1 496 ? -3.72684  22.58879  -13.86169 1.000 34.47474  ? 496  LYS A O     1 
ATOM   4001 C  CB    . LYS A 1 496 ? -2.92937  22.17160  -17.03031 1.000 39.12249  ? 496  LYS A CB    1 
ATOM   4002 C  CG    . LYS A 1 496 ? -2.08942  22.94491  -18.03011 0.879 39.89702  ? 496  LYS A CG    1 
ATOM   4003 C  CD    . LYS A 1 496 ? -2.83954  23.14340  -19.33909 0.740 40.06341  ? 496  LYS A CD    1 
ATOM   4004 C  CE    . LYS A 1 496 ? -1.92191  23.67376  -20.42920 0.930 41.02345  ? 496  LYS A CE    1 
ATOM   4005 N  NZ    . LYS A 1 496 ? -2.08115  22.91632  -21.70195 1.000 42.59833  ? 496  LYS A NZ    1 
ATOM   4006 N  N     . GLN A 1 497 ? -3.78668  20.43731  -14.52605 1.000 40.35522  ? 497  GLN A N     1 
ATOM   4007 C  CA    . GLN A 1 497 ? -4.77898  20.07575  -13.51929 1.000 39.59254  ? 497  GLN A CA    1 
ATOM   4008 C  C     . GLN A 1 497 ? -4.23124  20.26217  -12.10974 1.000 39.32529  ? 497  GLN A C     1 
ATOM   4009 O  O     . GLN A 1 497 ? -4.93186  20.76818  -11.22522 1.000 38.54304  ? 497  GLN A O     1 
ATOM   4010 C  CB    . GLN A 1 497 ? -5.23259  18.63108  -13.72987 1.000 39.06326  ? 497  GLN A CB    1 
ATOM   4011 C  CG    . GLN A 1 497 ? -6.27878  18.15532  -12.73681 1.000 38.41058  ? 497  GLN A CG    1 
ATOM   4012 C  CD    . GLN A 1 497 ? -7.68954  18.53936  -13.13506 1.000 38.46864  ? 497  GLN A CD    1 
ATOM   4013 O  OE1   . GLN A 1 497 ? -7.93084  19.00867  -14.24792 1.000 39.38575  ? 497  GLN A OE1   1 
ATOM   4014 N  NE2   . GLN A 1 497 ? -8.63288  18.33907  -12.22331 1.000 38.37971  ? 497  GLN A NE2   1 
ATOM   4015 N  N     . ALA A 1 498 ? -2.97695  19.86496  -11.88275 1.000 29.99521  ? 498  ALA A N     1 
ATOM   4016 C  CA    . ALA A 1 498 ? -2.40614  19.95372  -10.54287 1.000 30.07224  ? 498  ALA A CA    1 
ATOM   4017 C  C     . ALA A 1 498 ? -2.20260  21.40207  -10.11460 1.000 30.06624  ? 498  ALA A C     1 
ATOM   4018 O  O     . ALA A 1 498 ? -2.43027  21.74317  -8.94774  1.000 30.06541  ? 498  ALA A O     1 
ATOM   4019 C  CB    . ALA A 1 498 ? -1.08878  19.18464  -10.47944 1.000 30.70374  ? 498  ALA A CB    1 
ATOM   4020 N  N     . ARG A 1 499 ? -1.76166  22.26673  -11.03439 1.000 34.70494  ? 499  ARG A N     1 
ATOM   4021 C  CA    . ARG A 1 499 ? -1.64192  23.68401  -10.70318 1.000 34.51557  ? 499  ARG A CA    1 
ATOM   4022 C  C     . ARG A 1 499 ? -2.99630  24.27350  -10.33330 1.000 33.69519  ? 499  ARG A C     1 
ATOM   4023 O  O     . ARG A 1 499 ? -3.09339  25.10220  -9.42044  1.000 33.68250  ? 499  ARG A O     1 
ATOM   4024 C  CB    . ARG A 1 499 ? -1.02582  24.46179  -11.86915 1.000 35.10114  ? 499  ARG A CB    1 
ATOM   4025 C  CG    . ARG A 1 499 ? 0.16726   23.79064  -12.52554 1.000 36.68058  ? 499  ARG A CG    1 
ATOM   4026 C  CD    . ARG A 1 499 ? 1.08295   24.79940  -13.20149 1.000 38.29089  ? 499  ARG A CD    1 
ATOM   4027 N  NE    . ARG A 1 499 ? 0.55783   25.23783  -14.48989 1.000 39.15980  ? 499  ARG A NE    1 
ATOM   4028 C  CZ    . ARG A 1 499 ? 0.64351   24.53999  -15.61505 1.000 39.49677  ? 499  ARG A CZ    1 
ATOM   4029 N  NH1   . ARG A 1 499 ? 1.23095   23.35469  -15.65143 1.000 39.26386  ? 499  ARG A NH1   1 
ATOM   4030 N  NH2   . ARG A 1 499 ? 0.12772   25.04501  -16.73264 1.000 39.34620  ? 499  ARG A NH2   1 
ATOM   4031 N  N     . ALA A 1 500 ? -4.05579  23.85290  -11.02946 1.000 29.22496  ? 500  ALA A N     1 
ATOM   4032 C  CA    . ALA A 1 500 ? -5.38903  24.36472  -10.72994 1.000 28.50089  ? 500  ALA A CA    1 
ATOM   4033 C  C     . ALA A 1 500 ? -5.87036  23.88972  -9.36464  1.000 27.84534  ? 500  ALA A C     1 
ATOM   4034 O  O     . ALA A 1 500 ? -6.48909  24.65762  -8.61816  1.000 27.24389  ? 500  ALA A O     1 
ATOM   4035 C  CB    . ALA A 1 500 ? -6.37057  23.94517  -11.82362 1.000 28.11511  ? 500  ALA A CB    1 
ATOM   4036 N  N     . LEU A 1 501 ? -5.59707  22.62681  -9.02205  1.000 24.36526  ? 501  LEU A N     1 
ATOM   4037 C  CA    . LEU A 1 501 ? -5.98321  22.11319  -7.71159  1.000 23.20984  ? 501  LEU A CA    1 
ATOM   4038 C  C     . LEU A 1 501 ? -5.24435  22.82976  -6.58977  1.000 22.54809  ? 501  LEU A C     1 
ATOM   4039 O  O     . LEU A 1 501 ? -5.81123  23.04567  -5.51179  1.000 22.15005  ? 501  LEU A O     1 
ATOM   4040 C  CB    . LEU A 1 501 ? -5.72461  20.60765  -7.63857  1.000 22.69781  ? 501  LEU A CB    1 
ATOM   4041 C  CG    . LEU A 1 501 ? -6.61587  19.70579  -8.49579  1.000 23.35113  ? 501  LEU A CG    1 
ATOM   4042 C  CD1   . LEU A 1 501 ? -6.06141  18.28936  -8.53169  1.000 23.00928  ? 501  LEU A CD1   1 
ATOM   4043 C  CD2   . LEU A 1 501 ? -8.04830  19.70943  -7.98002  1.000 23.25055  ? 501  LEU A CD2   1 
ATOM   4044 N  N     . ARG A 1 502 ? -3.98425  23.20532  -6.82200  1.000 33.07465  ? 502  ARG A N     1 
ATOM   4045 C  CA    . ARG A 1 502 ? -3.23333  23.94288  -5.81258  1.000 33.55614  ? 502  ARG A CA    1 
ATOM   4046 C  C     . ARG A 1 502 ? -3.80515  25.33768  -5.59755  1.000 33.61723  ? 502  ARG A C     1 
ATOM   4047 O  O     . ARG A 1 502 ? -3.79712  25.84094  -4.46853  1.000 33.80790  ? 502  ARG A O     1 
ATOM   4048 C  CB    . ARG A 1 502 ? -1.76156  24.01977  -6.21360  1.000 34.49512  ? 502  ARG A CB    1 
ATOM   4049 C  CG    . ARG A 1 502 ? -1.02826  22.69823  -6.06270  1.000 35.43791  ? 502  ARG A CG    1 
ATOM   4050 C  CD    . ARG A 1 502 ? 0.47229   22.89639  -5.92383  1.000 36.11938  ? 502  ARG A CD    1 
ATOM   4051 N  NE    . ARG A 1 502 ? 1.22990   21.77180  -6.46271  1.000 38.22299  ? 502  ARG A NE    1 
ATOM   4052 C  CZ    . ARG A 1 502 ? 1.25113   21.40953  -7.73934  1.000 38.01818  ? 502  ARG A CZ    1 
ATOM   4053 N  NH1   . ARG A 1 502 ? 0.61796   22.10521  -8.67005  1.000 37.56383  ? 502  ARG A NH1   1 
ATOM   4054 N  NH2   . ARG A 1 502 ? 1.93500   20.32578  -8.09316  1.000 39.92714  ? 502  ARG A NH2   1 
ATOM   4055 N  N     . VAL A 1 503 ? -4.30387  25.97517  -6.65918  1.000 28.37591  ? 503  VAL A N     1 
ATOM   4056 C  CA    . VAL A 1 503 ? -4.97247  27.26206  -6.49746  1.000 28.31125  ? 503  VAL A CA    1 
ATOM   4057 C  C     . VAL A 1 503 ? -6.32952  27.07508  -5.83123  1.000 28.32912  ? 503  VAL A C     1 
ATOM   4058 O  O     . VAL A 1 503 ? -6.69581  27.82186  -4.91515  1.000 27.99707  ? 503  VAL A O     1 
ATOM   4059 C  CB    . VAL A 1 503 ? -5.10739  27.97554  -7.85562  1.000 28.98847  ? 503  VAL A CB    1 
ATOM   4060 C  CG1   . VAL A 1 503 ? -5.80898  29.31250  -7.68020  1.000 28.86634  ? 503  VAL A CG1   1 
ATOM   4061 C  CG2   . VAL A 1 503 ? -3.74428  28.16976  -8.49754  1.000 29.68318  ? 503  VAL A CG2   1 
ATOM   4062 N  N     . LYS A 1 504 ? -7.09237  26.07208  -6.27731  1.000 30.25103  ? 504  LYS A N     1 
ATOM   4063 C  CA    . LYS A 1 504 ? -8.42814  25.83617  -5.73708  1.000 29.86245  ? 504  LYS A CA    1 
ATOM   4064 C  C     . LYS A 1 504 ? -8.39883  25.57250  -4.23716  0.910 29.56879  ? 504  LYS A C     1 
ATOM   4065 O  O     . LYS A 1 504 ? -9.32098  25.97358  -3.51830  1.000 29.57050  ? 504  LYS A O     1 
ATOM   4066 C  CB    . LYS A 1 504 ? -9.07933  24.66019  -6.46737  1.000 32.87011  ? 504  LYS A CB    1 
ATOM   4067 C  CG    . LYS A 1 504 ? -10.54223 24.43283  -6.12599  1.000 32.65550  ? 504  LYS A CG    1 
ATOM   4068 C  CD    . LYS A 1 504 ? -11.22718 23.58701  -7.18751  0.128 32.59789  ? 504  LYS A CD    1 
ATOM   4069 C  CE    . LYS A 1 504 ? -12.73915 23.70919  -7.11175  0.680 32.65308  ? 504  LYS A CE    1 
ATOM   4070 N  NZ    . LYS A 1 504 ? -13.26653 24.58721  -8.19206  0.925 33.20211  ? 504  LYS A NZ    1 
ATOM   4071 N  N     . MET A 1 505 ? -7.35123  24.91931  -3.74597  1.000 27.50559  ? 505  MET A N     1 
ATOM   4072 C  CA    . MET A 1 505 ? -7.26494  24.52773  -2.34735  1.000 27.50456  ? 505  MET A CA    1 
ATOM   4073 C  C     . MET A 1 505 ? -6.50309  25.53872  -1.50052  1.000 27.11443  ? 505  MET A C     1 
ATOM   4074 O  O     . MET A 1 505 ? -6.31626  25.30890  -0.30178  1.000 26.52525  ? 505  MET A O     1 
ATOM   4075 C  CB    . MET A 1 505 ? -6.60768  23.15031  -2.25270  1.000 26.36317  ? 505  MET A CB    1 
ATOM   4076 C  CG    . MET A 1 505 ? -7.52744  22.05198  -2.74982  1.000 26.29051  ? 505  MET A CG    1 
ATOM   4077 S  SD    . MET A 1 505 ? -6.82593  20.39473  -2.78675  1.000 26.02205  ? 505  MET A SD    1 
ATOM   4078 C  CE    . MET A 1 505 ? -7.98296  19.62587  -3.91847  1.000 25.83759  ? 505  MET A CE    1 
ATOM   4079 N  N     . GLY A 1 506 ? -6.06221  26.64399  -2.09165  1.000 29.91308  ? 506  GLY A N     1 
ATOM   4080 C  CA    . GLY A 1 506 ? -5.35412  27.67053  -1.34607  1.000 29.60290  ? 506  GLY A CA    1 
ATOM   4081 C  C     . GLY A 1 506 ? -3.96232  27.27247  -0.90654  1.000 29.88460  ? 506  GLY A C     1 
ATOM   4082 O  O     . GLY A 1 506 ? -3.52818  27.65827  0.18616   1.000 29.77755  ? 506  GLY A O     1 
ATOM   4083 N  N     . VAL A 1 507 ? -3.24712  26.51295  -1.73411  1.000 21.71843  ? 507  VAL A N     1 
ATOM   4084 C  CA    . VAL A 1 507 ? -1.91744  26.02992  -1.38245  1.000 21.76325  ? 507  VAL A CA    1 
ATOM   4085 C  C     . VAL A 1 507 ? -0.86885  26.98356  -1.93842  1.000 22.22437  ? 507  VAL A C     1 
ATOM   4086 O  O     . VAL A 1 507 ? -0.10734  27.59671  -1.18191  1.000 21.98921  ? 507  VAL A O     1 
ATOM   4087 C  CB    . VAL A 1 507 ? -1.69285  24.59743  -1.89921  1.000 25.54506  ? 507  VAL A CB    1 
ATOM   4088 C  CG1   . VAL A 1 507 ? -0.23931  24.18718  -1.71639  1.000 26.04324  ? 507  VAL A CG1   1 
ATOM   4089 C  CG2   . VAL A 1 507 ? -2.62645  23.62691  -1.19013  1.000 24.89324  ? 507  VAL A CG2   1 
ATOM   4090 N  N     . SER A 1 508 ? -0.82083  27.11291  -3.25981  1.000 36.47194  ? 508  SER A N     1 
ATOM   4091 C  CA    . SER A 1 508 ? 0.16601   27.96907  -3.90694  1.000 37.03879  ? 508  SER A CA    1 
ATOM   4092 C  C     . SER A 1 508 ? -0.24242  28.27826  -5.34160  1.000 37.67878  ? 508  SER A C     1 
ATOM   4093 O  O     . SER A 1 508 ? -1.24088  27.75607  -5.83571  1.000 37.92679  ? 508  SER A O     1 
ATOM   4094 C  CB    . SER A 1 508 ? 1.54946   27.31273  -3.88043  1.000 37.63317  ? 508  SER A CB    1 
ATOM   4095 O  OG    . SER A 1 508 ? 1.55206   26.09222  -4.59955  1.000 38.81143  ? 508  SER A OG    1 
HETATM 4096 P  PA    . FAD B 2 .   ? -1.69716  0.95530   16.77817  1.000 21.46000  ? 601  FAD A PA    1 
HETATM 4097 O  O1A   . FAD B 2 .   ? -2.04205  0.73491   15.35452  1.000 22.92000  ? 601  FAD A O1A   1 
HETATM 4098 O  O2A   . FAD B 2 .   ? -2.60784  0.22434   17.77567  1.000 17.94000  ? 601  FAD A O2A   1 
HETATM 4099 O  O5B   . FAD B 2 .   ? -0.18036  0.59756   17.04638  1.000 22.35000  ? 601  FAD A O5B   1 
HETATM 4100 C  C5B   . FAD B 2 .   ? 0.26388   0.13748   18.34027  1.000 22.15000  ? 601  FAD A C5B   1 
HETATM 4101 C  C4B   . FAD B 2 .   ? 1.27541   1.10458   18.90714  1.000 24.05000  ? 601  FAD A C4B   1 
HETATM 4102 O  O4B   . FAD B 2 .   ? 2.44505   1.12639   18.06744  1.000 24.23000  ? 601  FAD A O4B   1 
HETATM 4103 C  C3B   . FAD B 2 .   ? 0.83337   2.55896   18.97861  1.000 19.82000  ? 601  FAD A C3B   1 
HETATM 4104 O  O3B   . FAD B 2 .   ? 0.09096   2.80150   20.16769  1.000 24.77000  ? 601  FAD A O3B   1 
HETATM 4105 C  C2B   . FAD B 2 .   ? 2.16846   3.30875   18.98573  1.000 19.31000  ? 601  FAD A C2B   1 
HETATM 4106 O  O2B   . FAD B 2 .   ? 2.71298   3.40783   20.29624  1.000 23.39000  ? 601  FAD A O2B   1 
HETATM 4107 C  C1B   . FAD B 2 .   ? 3.06442   2.39945   18.13727  1.000 20.31000  ? 601  FAD A C1B   1 
HETATM 4108 N  N9A   . FAD B 2 .   ? 3.30817   2.86943   16.77657  1.000 19.26000  ? 601  FAD A N9A   1 
HETATM 4109 C  C8A   . FAD B 2 .   ? 2.72046   2.41374   15.62657  1.000 16.04000  ? 601  FAD A C8A   1 
HETATM 4110 N  N7A   . FAD B 2 .   ? 3.14645   3.00586   14.53655  1.000 20.92000  ? 601  FAD A N7A   1 
HETATM 4111 C  C5A   . FAD B 2 .   ? 4.08609   3.91293   15.00265  1.000 19.72000  ? 601  FAD A C5A   1 
HETATM 4112 C  C6A   . FAD B 2 .   ? 4.90988   4.84889   14.34719  1.000 18.75000  ? 601  FAD A C6A   1 
HETATM 4113 N  N6A   . FAD B 2 .   ? 4.91133   5.04224   13.02536  1.000 17.23000  ? 601  FAD A N6A   1 
HETATM 4114 N  N1A   . FAD B 2 .   ? 5.73209   5.60233   15.10964  1.000 18.31000  ? 601  FAD A N1A   1 
HETATM 4115 C  C2A   . FAD B 2 .   ? 5.73047   5.41994   16.43221  1.000 16.25000  ? 601  FAD A C2A   1 
HETATM 4116 N  N3A   . FAD B 2 .   ? 5.00643   4.56639   17.15941  1.000 17.55000  ? 601  FAD A N3A   1 
HETATM 4117 C  C4A   . FAD B 2 .   ? 4.19820   3.83769   16.38098  1.000 16.35000  ? 601  FAD A C4A   1 
HETATM 4118 N  N1    . FAD B 2 .   ? 2.37446   8.31120   16.81920  1.000 21.22000  ? 601  FAD A N1    1 
HETATM 4119 C  C2    . FAD B 2 .   ? 2.36471   8.96608   18.01716  1.000 18.25000  ? 601  FAD A C2    1 
HETATM 4120 O  O2    . FAD B 2 .   ? 2.40881   8.35570   19.09154  1.000 19.92000  ? 601  FAD A O2    1 
HETATM 4121 N  N3    . FAD B 2 .   ? 2.31627   10.34873  18.03839  1.000 17.96000  ? 601  FAD A N3    1 
HETATM 4122 C  C4    . FAD B 2 .   ? 2.26546   11.17504  16.93579  1.000 21.60000  ? 601  FAD A C4    1 
HETATM 4123 O  O4    . FAD B 2 .   ? 2.22595   12.39508  17.07431  1.000 18.58000  ? 601  FAD A O4    1 
HETATM 4124 C  C4X   . FAD B 2 .   ? 2.26834   10.46977  15.67093  1.000 18.43000  ? 601  FAD A C4X   1 
HETATM 4125 N  N5    . FAD B 2 .   ? 2.22150   11.17496  14.57958  1.000 20.08000  ? 601  FAD A N5    1 
HETATM 4126 C  C5X   . FAD B 2 .   ? 2.22282   10.50350  13.36962  1.000 19.35000  ? 601  FAD A C5X   1 
HETATM 4127 C  C6    . FAD B 2 .   ? 2.17358   11.24879  12.19320  1.000 15.12000  ? 601  FAD A C6    1 
HETATM 4128 C  C7    . FAD B 2 .   ? 2.17224   10.62491  10.95036  1.000 23.11000  ? 601  FAD A C7    1 
HETATM 4129 C  C7M   . FAD B 2 .   ? 2.11899   11.46385  9.70082   1.000 18.88000  ? 601  FAD A C7M   1 
HETATM 4130 C  C8    . FAD B 2 .   ? 2.22282   9.22311   10.87820  1.000 18.02000  ? 601  FAD A C8    1 
HETATM 4131 C  C8M   . FAD B 2 .   ? 2.22401   8.51649   9.54838   1.000 18.34000  ? 601  FAD A C8M   1 
HETATM 4132 C  C9    . FAD B 2 .   ? 2.27493   8.47635   12.05144  1.000 17.24000  ? 601  FAD A C9    1 
HETATM 4133 C  C9A   . FAD B 2 .   ? 2.27346   9.10323   13.29242  1.000 17.41000  ? 601  FAD A C9A   1 
HETATM 4134 N  N10   . FAD B 2 .   ? 2.30794   8.37617   14.50178  1.000 20.60000  ? 601  FAD A N10   1 
HETATM 4135 C  C10   . FAD B 2 .   ? 2.32161   9.03257   15.71294  1.000 16.41000  ? 601  FAD A C10   1 
HETATM 4136 C  "C1'" . FAD B 2 .   ? 2.38124   6.90403   14.49612  1.000 19.02000  ? 601  FAD A "C1'" 1 
HETATM 4137 C  "C2'" . FAD B 2 .   ? 1.02125   6.21529   14.39318  1.000 19.40000  ? 601  FAD A "C2'" 1 
HETATM 4138 O  "O2'" . FAD B 2 .   ? 0.17678   6.86845   13.44511  1.000 26.66000  ? 601  FAD A "O2'" 1 
HETATM 4139 C  "C3'" . FAD B 2 .   ? 0.34856   6.20843   15.76659  1.000 19.00000  ? 601  FAD A "C3'" 1 
HETATM 4140 O  "O3'" . FAD B 2 .   ? 1.27617   5.72210   16.73067  1.000 19.24000  ? 601  FAD A "O3'" 1 
HETATM 4141 C  "C4'" . FAD B 2 .   ? -0.93544  5.38109   15.84200  1.000 20.69000  ? 601  FAD A "C4'" 1 
HETATM 4142 O  "O4'" . FAD B 2 .   ? -1.79473  5.74426   14.76062  1.000 19.47000  ? 601  FAD A "O4'" 1 
HETATM 4143 C  "C5'" . FAD B 2 .   ? -1.64665  5.54301   17.16913  1.000 18.84000  ? 601  FAD A "C5'" 1 
HETATM 4144 O  "O5'" . FAD B 2 .   ? -2.81878  4.70093   17.18574  1.000 21.32000  ? 601  FAD A "O5'" 1 
HETATM 4145 P  P     . FAD B 2 .   ? -2.81817  3.30638   17.92298  1.000 16.80000  ? 601  FAD A P     1 
HETATM 4146 O  O1P   . FAD B 2 .   ? -2.31452  3.45334   19.36210  1.000 16.08000  ? 601  FAD A O1P   1 
HETATM 4147 O  O2P   . FAD B 2 .   ? -4.13771  2.66135   17.78126  1.000 14.57000  ? 601  FAD A O2P   1 
HETATM 4148 O  O3P   . FAD B 2 .   ? -1.72720  2.50536   17.10488  1.000 23.41000  ? 601  FAD A O3P   1 
HETATM 4149 C  C7    . DLZ C 3 .   ? 1.79060   18.65580  26.08447  1.000 27.21000  ? 602  DLZ A C7    1 
HETATM 4150 C  C7A   . DLZ C 3 .   ? 1.81653   19.31546  27.42091  1.000 31.33000  ? 602  DLZ A C7A   1 
HETATM 4151 C  C5A   . DLZ C 3 .   ? 0.74468   20.10088  27.85418  1.000 32.88000  ? 602  DLZ A C5A   1 
HETATM 4152 C  C6    . DLZ C 3 .   ? -0.47261  20.31938  27.01001  1.000 28.85000  ? 602  DLZ A C6    1 
HETATM 4153 N  N5    . DLZ C 3 .   ? 0.77488   20.68358  29.04282  1.000 34.31000  ? 602  DLZ A N5    1 
HETATM 4154 C  C4A   . DLZ C 3 .   ? 1.81421   20.52440  29.81844  1.000 34.71000  ? 602  DLZ A C4A   1 
HETATM 4155 C  C4    . DLZ C 3 .   ? 1.81835   21.18456  31.13132  1.000 26.66000  ? 602  DLZ A C4    1 
HETATM 4156 O  O4    . DLZ C 3 .   ? 0.90778   21.87171  31.53690  1.000 30.40000  ? 602  DLZ A O4    1 
HETATM 4157 N  N3    . DLZ C 3 .   ? 2.95467   20.94364  31.84894  1.000 31.41000  ? 602  DLZ A N3    1 
HETATM 4158 C  C2    . DLZ C 3 .   ? 4.04509   20.16658  31.45453  1.000 30.05000  ? 602  DLZ A C2    1 
HETATM 4159 O  O2    . DLZ C 3 .   ? 4.98841   20.04891  32.21486  1.000 30.71000  ? 602  DLZ A O2    1 
HETATM 4160 N  N1    . DLZ C 3 .   ? 4.00034   19.57355  30.23522  1.000 26.11000  ? 602  DLZ A N1    1 
HETATM 4161 C  C8    . DLZ C 3 .   ? 2.94316   19.75239  29.47281  1.000 35.38000  ? 602  DLZ A C8    1 
HETATM 4162 N  N8    . DLZ C 3 .   ? 2.89021   19.15626  28.23290  1.000 32.10000  ? 602  DLZ A N8    1 
HETATM 4163 C  "C1'" . DLZ C 3 .   ? 4.04342   18.33847  27.81646  1.000 27.94000  ? 602  DLZ A "C1'" 1 
HETATM 4164 C  "C2'" . DLZ C 3 .   ? 5.19056   19.19927  27.25107  1.000 37.02000  ? 602  DLZ A "C2'" 1 
HETATM 4165 O  "O2'" . DLZ C 3 .   ? 4.70921   20.32177  26.55675  1.000 29.56000  ? 602  DLZ A "O2'" 1 
HETATM 4166 C  "C3'" . DLZ C 3 .   ? 6.10309   18.35085  26.33830  1.000 35.20000  ? 602  DLZ A "C3'" 1 
HETATM 4167 O  "O3'" . DLZ C 3 .   ? 5.48500   18.01572  25.11423  1.000 45.69000  ? 602  DLZ A "O3'" 1 
HETATM 4168 C  "C4'" . DLZ C 3 .   ? 6.65559   17.07378  27.00428  1.000 35.73000  ? 602  DLZ A "C4'" 1 
HETATM 4169 O  "O4'" . DLZ C 3 .   ? 6.95881   17.20527  28.36995  1.000 37.35000  ? 602  DLZ A "O4'" 1 
HETATM 4170 C  "C5'" . DLZ C 3 .   ? 7.85068   16.57475  26.20678  1.000 32.75000  ? 602  DLZ A "C5'" 1 
HETATM 4171 O  "O5'" . DLZ C 3 .   ? 8.55124   15.62748  26.97800  1.000 36.10000  ? 602  DLZ A "O5'" 1 
HETATM 4172 FE FE1   . SF4 D 4 .   ? -11.44286 8.32037   -3.24291  1.000 41.04729  ? 603  SF4 A FE1   1 
HETATM 4173 FE FE2   . SF4 D 4 .   ? -10.25511 10.50219  -4.38708  1.000 27.91771  ? 603  SF4 A FE2   1 
HETATM 4174 FE FE3   . SF4 D 4 .   ? -10.46668 10.32751  -1.66293  1.000 26.51134  ? 603  SF4 A FE3   1 
HETATM 4175 FE FE4   . SF4 D 4 .   ? -12.70616 10.74785  -3.18766  1.000 28.48474  ? 603  SF4 A FE4   1 
HETATM 4176 S  S1    . SF4 D 4 .   ? -10.92259 12.15181  -2.96058  1.000 24.70882  ? 603  SF4 A S1    1 
HETATM 4177 S  S2    . SF4 D 4 .   ? -12.48287 9.28070   -1.45604  1.000 27.92145  ? 603  SF4 A S2    1 
HETATM 4178 S  S3    . SF4 D 4 .   ? -12.20313 9.51012   -5.03505  1.000 30.38236  ? 603  SF4 A S3    1 
HETATM 4179 S  S4    . SF4 D 4 .   ? -9.26248  8.96276   -3.02788  1.000 31.69456  ? 603  SF4 A S4    1 
HETATM 4180 O  O     . HOH E 5 .   ? -0.58212  2.95989   40.05083  1.000 30.00000  ? 701  HOH A O     1 
HETATM 4181 O  O     . HOH E 5 .   ? 2.31817   -6.87655  9.97934   1.000 30.00000  ? 702  HOH A O     1 
HETATM 4182 O  O     . HOH E 5 .   ? 10.18518  17.12384  51.40463  1.000 35.29000  ? 703  HOH A O     1 
HETATM 4183 O  O     . HOH E 5 .   ? -2.88268  -6.20975  8.03586   1.000 44.37000  ? 704  HOH A O     1 
HETATM 4184 O  O     . HOH E 5 .   ? -3.15798  11.66253  47.33767  1.000 35.23000  ? 705  HOH A O     1 
HETATM 4185 O  O     . HOH E 5 .   ? -2.04773  30.69640  35.00003  1.000 34.37000  ? 706  HOH A O     1 
HETATM 4186 O  O     . HOH E 5 .   ? -16.54378 14.04922  20.56212  1.000 38.73000  ? 707  HOH A O     1 
HETATM 4187 O  O     . HOH E 5 .   ? -14.69862 3.37687   -1.92980  1.000 30.00000  ? 708  HOH A O     1 
HETATM 4188 O  O     . HOH E 5 .   ? -8.28347  -15.08792 21.12430  1.000 34.28000  ? 709  HOH A O     1 
HETATM 4189 O  O     . HOH E 5 .   ? 17.79486  9.90954   43.23443  1.000 35.42000  ? 710  HOH A O     1 
HETATM 4190 O  O     . HOH E 5 .   ? -9.63498  7.39547   12.18311  1.000 26.53000  ? 711  HOH A O     1 
HETATM 4191 O  O     . HOH E 5 .   ? -4.28558  -12.66894 25.90076  1.000 35.55000  ? 712  HOH A O     1 
HETATM 4192 O  O     . HOH E 5 .   ? 7.05826   26.97503  41.34418  1.000 19.19000  ? 713  HOH A O     1 
HETATM 4193 O  O     . HOH E 5 .   ? 17.72866  12.31959  -0.49696  1.000 43.63000  ? 714  HOH A O     1 
HETATM 4194 O  O     . HOH E 5 .   ? -7.03800  14.65343  -10.31849 1.000 25.19000  ? 715  HOH A O     1 
HETATM 4195 O  O     . HOH E 5 .   ? 10.56105  -9.86579  27.70903  1.000 40.39000  ? 716  HOH A O     1 
HETATM 4196 O  O     . HOH E 5 .   ? -17.11215 -3.35743  6.17606   1.000 32.75000  ? 717  HOH A O     1 
HETATM 4197 O  O     . HOH E 5 .   ? 31.89664  8.25251   1.10592   1.000 29.87000  ? 718  HOH A O     1 
HETATM 4198 O  O     . HOH E 5 .   ? -2.54166  1.34407   -5.58802  1.000 43.95000  ? 719  HOH A O     1 
HETATM 4199 O  O     . HOH E 5 .   ? 5.78706   4.48463   29.95145  1.000 19.68000  ? 720  HOH A O     1 
HETATM 4200 O  O     . HOH E 5 .   ? 6.15723   17.82684  5.72136   1.000 30.59000  ? 721  HOH A O     1 
HETATM 4201 O  O     . HOH E 5 .   ? 11.94601  21.56746  19.39843  1.000 19.85000  ? 722  HOH A O     1 
HETATM 4202 O  O     . HOH E 5 .   ? -4.54265  -4.07444  6.42834   1.000 32.23000  ? 723  HOH A O     1 
HETATM 4203 O  O     . HOH E 5 .   ? 10.68674  -14.41278 23.88706  1.000 30.53000  ? 724  HOH A O     1 
HETATM 4204 O  O     . HOH E 5 .   ? -14.45030 8.46712   22.77229  1.000 32.69000  ? 725  HOH A O     1 
HETATM 4205 O  O     . HOH E 5 .   ? -12.65146 2.79745   -2.27108  1.000 30.20000  ? 726  HOH A O     1 
HETATM 4206 O  O     . HOH E 5 .   ? 2.17171   21.21547  -12.14406 1.000 39.14000  ? 727  HOH A O     1 
HETATM 4207 O  O     . HOH E 5 .   ? -17.07303 11.41521  7.37493   1.000 26.31000  ? 728  HOH A O     1 
HETATM 4208 O  O     . HOH E 5 .   ? 9.34037   -13.54448 14.73468  1.000 21.60000  ? 729  HOH A O     1 
HETATM 4209 O  O     . HOH E 5 .   ? 12.76816  17.30735  32.34341  1.000 17.70000  ? 730  HOH A O     1 
HETATM 4210 O  O     . HOH E 5 .   ? 20.41913  -8.73302  14.83031  1.000 45.33000  ? 731  HOH A O     1 
HETATM 4211 O  O     . HOH E 5 .   ? 20.23932  0.47315   8.17549   1.000 30.79000  ? 732  HOH A O     1 
HETATM 4212 O  O     . HOH E 5 .   ? 18.13166  7.55507   26.47782  1.000 22.95000  ? 733  HOH A O     1 
HETATM 4213 O  O     . HOH E 5 .   ? 3.49025   -9.80540  11.45896  1.000 33.16000  ? 734  HOH A O     1 
HETATM 4214 O  O     . HOH E 5 .   ? 8.50258   2.06105   22.45781  1.000 18.04000  ? 735  HOH A O     1 
HETATM 4215 O  O     . HOH E 5 .   ? 21.40934  18.93782  33.66420  1.000 35.60000  ? 736  HOH A O     1 
HETATM 4216 O  O     . HOH E 5 .   ? -4.93796  5.61591   25.15970  1.000 28.46000  ? 737  HOH A O     1 
HETATM 4217 O  O     . HOH E 5 .   ? 11.78238  11.46025  27.48368  1.000 27.74000  ? 738  HOH A O     1 
HETATM 4218 O  O     . HOH E 5 .   ? -12.41352 25.49606  5.08902   1.000 30.56000  ? 739  HOH A O     1 
HETATM 4219 O  O     . HOH E 5 .   ? -17.08071 11.93061  27.62344  1.000 39.62000  ? 740  HOH A O     1 
HETATM 4220 O  O     . HOH E 5 .   ? -13.76610 -0.56060  15.55326  1.000 20.79000  ? 741  HOH A O     1 
HETATM 4221 O  O     . HOH E 5 .   ? -11.83540 9.72702   30.40464  1.000 22.50000  ? 742  HOH A O     1 
HETATM 4222 O  O     . HOH E 5 .   ? 9.55164   8.56757   3.32942   1.000 26.56000  ? 743  HOH A O     1 
HETATM 4223 O  O     . HOH E 5 .   ? 26.45646  6.24980   21.46658  1.000 31.28000  ? 744  HOH A O     1 
HETATM 4224 O  O     . HOH E 5 .   ? 2.35210   28.68735  43.82480  1.000 39.02000  ? 745  HOH A O     1 
HETATM 4225 O  O     . HOH E 5 .   ? -11.39138 3.58852   9.13152   1.000 20.86000  ? 746  HOH A O     1 
HETATM 4226 O  O     . HOH E 5 .   ? 14.31053  4.99532   21.34972  1.000 23.25000  ? 747  HOH A O     1 
HETATM 4227 O  O     . HOH E 5 .   ? -12.61141 -0.86971  4.49125   1.000 28.95000  ? 748  HOH A O     1 
HETATM 4228 O  O     . HOH E 5 .   ? -1.84308  -11.76617 27.16023  1.000 24.15000  ? 749  HOH A O     1 
HETATM 4229 O  O     . HOH E 5 .   ? -15.58480 20.30102  39.12485  1.000 40.23000  ? 750  HOH A O     1 
HETATM 4230 O  O     . HOH E 5 .   ? 6.39960   10.04287  2.08286   1.000 22.45000  ? 751  HOH A O     1 
HETATM 4231 O  O     . HOH E 5 .   ? -2.70359  9.83132   36.14952  1.000 19.15000  ? 752  HOH A O     1 
HETATM 4232 O  O     . HOH E 5 .   ? -9.27271  2.08137   -8.54114  1.000 33.22000  ? 753  HOH A O     1 
HETATM 4233 O  O     . HOH E 5 .   ? 6.15851   6.32633   27.71621  1.000 24.04000  ? 754  HOH A O     1 
HETATM 4234 O  O     . HOH E 5 .   ? 1.01795   6.55408   36.16778  1.000 31.34000  ? 755  HOH A O     1 
HETATM 4235 O  O     . HOH E 5 .   ? -2.80594  3.36635   14.06276  1.000 22.81000  ? 756  HOH A O     1 
HETATM 4236 O  O     . HOH E 5 .   ? -12.18835 11.05952  22.96788  1.000 19.89000  ? 757  HOH A O     1 
HETATM 4237 O  O     . HOH E 5 .   ? -19.37529 23.81379  3.45266   1.000 44.18000  ? 758  HOH A O     1 
HETATM 4238 O  O     . HOH E 5 .   ? -11.21305 -3.75383  29.68168  1.000 28.82000  ? 759  HOH A O     1 
HETATM 4239 O  O     . HOH E 5 .   ? 3.92661   6.14915   19.39151  1.000 17.08000  ? 760  HOH A O     1 
HETATM 4240 O  O     . HOH E 5 .   ? 6.54553   18.18529  8.26303   1.000 18.89000  ? 761  HOH A O     1 
HETATM 4241 O  O     . HOH E 5 .   ? 12.44905  29.39004  31.33355  1.000 34.07000  ? 762  HOH A O     1 
HETATM 4242 O  O     . HOH E 5 .   ? 5.27028   18.58508  -12.85321 1.000 39.37000  ? 763  HOH A O     1 
HETATM 4243 O  O     . HOH E 5 .   ? -0.77126  11.98722  25.03546  1.000 20.96000  ? 764  HOH A O     1 
HETATM 4244 O  O     . HOH E 5 .   ? -19.87714 -7.81705  10.99709  1.000 37.71000  ? 765  HOH A O     1 
HETATM 4245 O  O     . HOH E 5 .   ? 9.53035   24.78628  46.77339  1.000 27.90000  ? 766  HOH A O     1 
HETATM 4246 O  O     . HOH E 5 .   ? 9.57849   -0.07374  29.16892  1.000 30.28000  ? 767  HOH A O     1 
HETATM 4247 O  O     . HOH E 5 .   ? -1.20361  0.96092   9.01669   1.000 36.39000  ? 768  HOH A O     1 
HETATM 4248 O  O     . HOH E 5 .   ? 16.212    21.824    3.550     1.000 30.35000  ? 769  HOH A O     1 
HETATM 4249 O  O     . HOH E 5 .   ? -8.06887  -13.15124 23.10709  1.000 28.43000  ? 770  HOH A O     1 
HETATM 4250 O  O     . HOH E 5 .   ? -10.67282 20.86500  -13.27504 1.000 44.16000  ? 771  HOH A O     1 
HETATM 4251 O  O     . HOH E 5 .   ? -11.22121 9.89897   33.05448  1.000 21.30000  ? 772  HOH A O     1 
HETATM 4252 O  O     . HOH E 5 .   ? -16.17232 11.42010  4.38969   1.000 26.43000  ? 773  HOH A O     1 
HETATM 4253 O  O     . HOH E 5 .   ? 0.63351   13.65564  14.98025  1.000 20.50000  ? 774  HOH A O     1 
HETATM 4254 O  O     . HOH E 5 .   ? 5.32019   -12.51693 27.73798  1.000 27.43000  ? 775  HOH A O     1 
HETATM 4255 O  O     . HOH E 5 .   ? 5.50125   19.80562  35.01248  1.000 26.33000  ? 776  HOH A O     1 
HETATM 4256 O  O     . HOH E 5 .   ? 13.70252  23.69886  -5.87317  1.000 26.04000  ? 777  HOH A O     1 
HETATM 4257 O  O     . HOH E 5 .   ? 7.60053   17.37206  1.27379   1.000 21.73000  ? 778  HOH A O     1 
HETATM 4258 O  O     . HOH E 5 .   ? -0.43973  32.82089  36.44955  1.000 22.04000  ? 779  HOH A O     1 
HETATM 4259 O  O     . HOH E 5 .   ? 11.85471  15.69193  34.46715  1.000 17.85000  ? 780  HOH A O     1 
HETATM 4260 O  O     . HOH E 5 .   ? 9.16178   31.49952  45.55587  1.000 39.57000  ? 781  HOH A O     1 
HETATM 4261 O  O     . HOH E 5 .   ? 5.36095   24.55156  47.71511  1.000 26.32000  ? 782  HOH A O     1 
HETATM 4262 O  O     . HOH E 5 .   ? 6.17280   11.89029  25.02895  1.000 22.74000  ? 783  HOH A O     1 
HETATM 4263 O  O     . HOH E 5 .   ? 8.81688   14.19122  49.41623  1.000 27.24000  ? 784  HOH A O     1 
HETATM 4264 O  O     . HOH E 5 .   ? 23.79333  -0.10455  20.13506  1.000 29.28000  ? 785  HOH A O     1 
HETATM 4265 O  O     . HOH E 5 .   ? 15.28278  12.78198  25.67819  1.000 28.65000  ? 786  HOH A O     1 
HETATM 4266 O  O     . HOH E 5 .   ? -6.49257  0.14021   9.71932   1.000 25.94000  ? 787  HOH A O     1 
HETATM 4267 O  O     . HOH E 5 .   ? 11.60687  9.58166   5.07037   1.000 21.52000  ? 788  HOH A O     1 
HETATM 4268 O  O     . HOH E 5 .   ? 16.58506  2.84937   27.40888  1.000 30.38000  ? 789  HOH A O     1 
HETATM 4269 O  O     . HOH E 5 .   ? 19.49009  16.41993  24.38349  1.000 26.25000  ? 790  HOH A O     1 
HETATM 4270 O  O     . HOH E 5 .   ? 2.89119   9.57955   2.26916   1.000 35.86000  ? 791  HOH A O     1 
HETATM 4271 O  O     . HOH E 5 .   ? 18.39186  6.62722   6.58755   1.000 27.79000  ? 792  HOH A O     1 
HETATM 4272 O  O     . HOH E 5 .   ? 3.13876   1.95119   11.83135  1.000 19.80000  ? 793  HOH A O     1 
HETATM 4273 O  O     . HOH E 5 .   ? -1.05528  -18.76710 19.49559  1.000 18.93000  ? 794  HOH A O     1 
HETATM 4274 O  O     . HOH E 5 .   ? -4.61012  27.77292  2.73575   1.000 33.86000  ? 795  HOH A O     1 
HETATM 4275 O  O     . HOH E 5 .   ? -12.49013 6.13477   9.49724   1.000 25.46000  ? 796  HOH A O     1 
HETATM 4276 O  O     . HOH E 5 .   ? -5.02278  7.75451   40.18379  1.000 30.62000  ? 797  HOH A O     1 
HETATM 4277 O  O     . HOH E 5 .   ? -8.31955  -0.50179  23.26943  1.000 18.76000  ? 798  HOH A O     1 
HETATM 4278 O  O     . HOH E 5 .   ? 7.00462   19.47277  15.47535  0.702 23.14000  ? 799  HOH A O     1 
HETATM 4279 O  O     . HOH E 5 .   ? 21.63148  23.79652  25.94609  1.000 27.01000  ? 800  HOH A O     1 
HETATM 4280 O  O     . HOH E 5 .   ? -13.55149 6.71581   34.86484  1.000 36.93000  ? 801  HOH A O     1 
HETATM 4281 O  O     . HOH E 5 .   ? -5.46956  -12.38502 23.25057  1.000 27.61000  ? 802  HOH A O     1 
HETATM 4282 O  O     . HOH E 5 .   ? 19.76223  15.73300  27.77707  1.000 27.98000  ? 803  HOH A O     1 
HETATM 4283 O  O     . HOH E 5 .   ? 5.90626   23.72383  12.68646  1.000 39.44000  ? 804  HOH A O     1 
HETATM 4284 O  O     . HOH E 5 .   ? -3.90258  2.17310   10.10597  1.000 22.53000  ? 805  HOH A O     1 
HETATM 4285 O  O     . HOH E 5 .   ? 1.51808   17.51308  -7.42353  1.000 39.26000  ? 806  HOH A O     1 
HETATM 4286 O  O     . HOH E 5 .   ? 20.95477  8.92276   32.95116  1.000 31.01000  ? 807  HOH A O     1 
HETATM 4287 O  O     . HOH E 5 .   ? -8.04991  26.45717  1.56676   1.000 19.99000  ? 808  HOH A O     1 
HETATM 4288 O  O     . HOH E 5 .   ? -17.68663 8.00265   13.34240  1.000 41.81000  ? 809  HOH A O     1 
HETATM 4289 O  O     . HOH E 5 .   ? 30.645    2.416     7.026     1.000 34.00000  ? 810  HOH A O     1 
HETATM 4290 O  O     . HOH E 5 .   ? -22.28172 -1.28908  9.17097   1.000 44.41000  ? 811  HOH A O     1 
HETATM 4291 O  O     . HOH E 5 .   ? -5.84947  24.78466  17.74643  1.000 20.87000  ? 812  HOH A O     1 
HETATM 4292 O  O     . HOH E 5 .   ? -14.05920 2.23294   14.72617  1.000 20.40000  ? 813  HOH A O     1 
HETATM 4293 O  O     . HOH E 5 .   ? -14.54409 11.26806  21.50188  1.000 34.46000  ? 814  HOH A O     1 
HETATM 4294 O  O     . HOH E 5 .   ? -0.95000  -1.71962  32.39843  1.000 31.00000  ? 815  HOH A O     1 
HETATM 4295 O  O     . HOH E 5 .   ? -5.25135  -19.87678 26.48950  1.000 31.64000  ? 816  HOH A O     1 
HETATM 4296 O  O     . HOH E 5 .   ? 0.87553   28.24650  33.16601  1.000 20.08000  ? 817  HOH A O     1 
HETATM 4297 O  O     . HOH E 5 .   ? -14.60105 9.06898   11.16094  1.000 33.47000  ? 818  HOH A O     1 
HETATM 4298 O  O     . HOH E 5 .   ? -0.82089  26.41315  -8.40779  1.000 31.11000  ? 819  HOH A O     1 
HETATM 4299 O  O     . HOH E 5 .   ? 7.96702   26.06012  29.59576  1.000 26.47000  ? 820  HOH A O     1 
HETATM 4300 O  O     . HOH E 5 .   ? -7.62828  -2.38398  12.29502  1.000 16.27000  ? 821  HOH A O     1 
HETATM 4301 O  O     . HOH E 5 .   ? -12.11678 26.09727  -3.86104  1.000 25.90000  ? 822  HOH A O     1 
HETATM 4302 O  O     . HOH E 5 .   ? -15.81204 -1.06472  4.90002   1.000 30.00000  ? 823  HOH A O     1 
HETATM 4303 O  O     . HOH E 5 .   ? -7.86448  -1.81886  34.82678  1.000 37.58000  ? 824  HOH A O     1 
HETATM 4304 O  O     . HOH E 5 .   ? 8.19279   32.53693  32.22927  1.000 35.10000  ? 825  HOH A O     1 
HETATM 4305 O  O     . HOH E 5 .   ? 13.41160  2.72976   7.44510   1.000 32.04000  ? 826  HOH A O     1 
HETATM 4306 O  O     . HOH E 5 .   ? -1.02233  25.98534  42.18471  1.000 27.00000  ? 827  HOH A O     1 
HETATM 4307 O  O     . HOH E 5 .   ? 19.57980  16.01252  19.30844  1.000 30.11000  ? 828  HOH A O     1 
HETATM 4308 O  O     . HOH E 5 .   ? -3.57058  -14.21732 10.98419  1.000 42.01000  ? 829  HOH A O     1 
HETATM 4309 O  O     . HOH E 5 .   ? -2.07202  18.70634  -23.07223 1.000 41.93000  ? 830  HOH A O     1 
HETATM 4310 O  O     . HOH E 5 .   ? -4.75934  8.79454   -12.78428 1.000 28.95000  ? 831  HOH A O     1 
HETATM 4311 O  O     . HOH E 5 .   ? -4.70123  -10.74289 12.72895  1.000 28.42000  ? 832  HOH A O     1 
HETATM 4312 O  O     . HOH E 5 .   ? -14.83918 16.68567  8.18589   1.000 27.24000  ? 833  HOH A O     1 
HETATM 4313 O  O     . HOH E 5 .   ? 2.32011   17.47123  48.82338  1.000 29.46000  ? 834  HOH A O     1 
HETATM 4314 O  O     . HOH E 5 .   ? -1.03634  -1.21041  1.97457   1.000 43.41000  ? 835  HOH A O     1 
HETATM 4315 O  O     . HOH E 5 .   ? 11.18208  27.35185  30.57090  1.000 32.18000  ? 836  HOH A O     1 
HETATM 4316 O  O     . HOH E 5 .   ? 2.37105   17.96918  22.67802  1.000 33.07000  ? 837  HOH A O     1 
HETATM 4317 O  O     . HOH E 5 .   ? 15.53094  26.07664  22.97873  1.000 34.44000  ? 838  HOH A O     1 
HETATM 4318 O  O     . HOH E 5 .   ? 22.64417  3.17792   27.33172  1.000 39.26000  ? 839  HOH A O     1 
HETATM 4319 O  O     . HOH E 5 .   ? 10.07088  18.46082  1.36532   1.000 20.35000  ? 840  HOH A O     1 
HETATM 4320 O  O     . HOH E 5 .   ? 21.52341  7.60699   26.25398  1.000 33.72000  ? 841  HOH A O     1 
HETATM 4321 O  O     . HOH E 5 .   ? 6.85688   3.09134   31.68572  1.000 35.25000  ? 842  HOH A O     1 
HETATM 4322 O  O     A HOH E 5 .   ? 17.19358  26.53675  46.79439  0.552 20.21000  ? 843  HOH A O     1 
HETATM 4323 O  O     B HOH E 5 .   ? 18.87451  27.94581  46.80357  0.448 21.78000  ? 843  HOH A O     1 
HETATM 4324 O  O     . HOH E 5 .   ? 1.67922   -1.22563  30.66138  1.000 25.18000  ? 844  HOH A O     1 
HETATM 4325 O  O     . HOH E 5 .   ? 10.54160  32.70767  38.66163  1.000 26.38000  ? 845  HOH A O     1 
HETATM 4326 O  O     . HOH E 5 .   ? -11.65457 30.28229  25.94209  1.000 39.96000  ? 846  HOH A O     1 
HETATM 4327 O  O     . HOH E 5 .   ? 11.89704  11.18533  23.07397  1.000 21.41000  ? 847  HOH A O     1 
HETATM 4328 O  O     . HOH E 5 .   ? 6.36979   17.98877  -1.31594  1.000 24.61000  ? 848  HOH A O     1 
HETATM 4329 O  O     . HOH E 5 .   ? 8.89818   24.82376  25.36295  1.000 34.13000  ? 849  HOH A O     1 
HETATM 4330 O  O     . HOH E 5 .   ? 16.83735  5.65288   27.90636  1.000 33.48000  ? 850  HOH A O     1 
HETATM 4331 O  O     . HOH E 5 .   ? 10.17857  22.92335  16.80724  1.000 38.95000  ? 851  HOH A O     1 
HETATM 4332 O  O     . HOH E 5 .   ? 6.08883   18.69977  3.05113   1.000 29.95000  ? 852  HOH A O     1 
HETATM 4333 O  O     . HOH E 5 .   ? -14.29233 23.07304  17.11257  1.000 35.56000  ? 853  HOH A O     1 
HETATM 4334 O  O     . HOH E 5 .   ? 19.32149  15.57220  9.26015   1.000 20.87000  ? 854  HOH A O     1 
HETATM 4335 O  O     . HOH E 5 .   ? 15.83276  4.96007   5.49217   1.000 37.33000  ? 855  HOH A O     1 
HETATM 4336 O  O     . HOH E 5 .   ? 6.70524   18.63900  -3.55936  1.000 21.40000  ? 856  HOH A O     1 
HETATM 4337 O  O     . HOH E 5 .   ? 24.16593  7.09704   10.24754  1.000 35.45000  ? 857  HOH A O     1 
HETATM 4338 O  O     . HOH E 5 .   ? -7.15689  -8.67695  28.63656  1.000 30.54000  ? 858  HOH A O     1 
HETATM 4339 O  O     . HOH E 5 .   ? -7.74170  29.71705  30.60816  1.000 31.39000  ? 859  HOH A O     1 
HETATM 4340 O  O     . HOH E 5 .   ? -2.64217  30.38743  -1.52154  1.000 42.26000  ? 860  HOH A O     1 
HETATM 4341 O  O     . HOH E 5 .   ? -3.31450  19.28139  43.74278  1.000 38.05000  ? 861  HOH A O     1 
HETATM 4342 O  O     . HOH E 5 .   ? -10.82655 11.61036  40.22827  1.000 21.78000  ? 862  HOH A O     1 
HETATM 4343 O  O     . HOH E 5 .   ? 12.66546  7.27969   33.22403  1.000 21.28000  ? 863  HOH A O     1 
HETATM 4344 O  O     . HOH E 5 .   ? -16.87661 15.01131  1.80735   1.000 30.00000  ? 864  HOH A O     1 
HETATM 4345 O  O     . HOH E 5 .   ? 16.18495  10.30078  27.46879  1.000 24.78000  ? 865  HOH A O     1 
HETATM 4346 O  O     . HOH E 5 .   ? 6.25217   18.01859  22.29881  1.000 8.04000   ? 866  HOH A O     1 
HETATM 4347 O  O     . HOH E 5 .   ? 17.97805  14.03283  48.06429  1.000 36.40000  ? 867  HOH A O     1 
HETATM 4348 O  O     . HOH E 5 .   ? 23.56407  22.40008  36.51976  1.000 43.12000  ? 868  HOH A O     1 
HETATM 4349 O  O     . HOH E 5 .   ? -8.14937  4.50914   24.34691  1.000 28.15000  ? 869  HOH A O     1 
HETATM 4350 O  O     . HOH E 5 .   ? 19.77804  8.87717   18.94043  1.000 27.03000  ? 870  HOH A O     1 
HETATM 4351 O  O     . HOH E 5 .   ? 26.27838  1.37293   5.35825   1.000 40.44000  ? 871  HOH A O     1 
HETATM 4352 O  O     . HOH E 5 .   ? 3.18164   23.81137  -3.69248  1.000 30.40000  ? 872  HOH A O     1 
HETATM 4353 O  O     . HOH E 5 .   ? 8.29602   4.89496   26.39372  1.000 29.73000  ? 873  HOH A O     1 
HETATM 4354 O  O     . HOH E 5 .   ? -18.21667 9.64545   -8.56265  1.000 30.00000  ? 874  HOH A O     1 
HETATM 4355 O  O     . HOH E 5 .   ? -13.77093 15.01595  -14.52566 1.000 42.54000  ? 875  HOH A O     1 
HETATM 4356 O  O     . HOH E 5 .   ? 20.46034  13.21766  22.25824  1.000 35.73000  ? 876  HOH A O     1 
HETATM 4357 O  O     . HOH E 5 .   ? -18.19308 20.03538  2.83724   1.000 39.57000  ? 877  HOH A O     1 
HETATM 4358 O  O     . HOH E 5 .   ? -4.90845  -6.33525  33.73409  1.000 28.51000  ? 878  HOH A O     1 
HETATM 4359 O  O     . HOH E 5 .   ? -17.99029 15.12271  27.43780  1.000 44.62000  ? 879  HOH A O     1 
HETATM 4360 O  O     . HOH E 5 .   ? -0.72191  25.98272  16.79567  1.000 29.31000  ? 880  HOH A O     1 
HETATM 4361 O  O     . HOH E 5 .   ? 3.02543   4.50018   37.05539  1.000 35.58000  ? 881  HOH A O     1 
HETATM 4362 O  O     . HOH E 5 .   ? -3.62515  6.11516   -10.83751 1.000 38.26000  ? 882  HOH A O     1 
HETATM 4363 O  O     . HOH E 5 .   ? 9.45923   12.96300  28.61481  1.000 28.23000  ? 883  HOH A O     1 
HETATM 4364 O  O     . HOH E 5 .   ? -5.22747  8.48646   26.84802  1.000 29.28000  ? 884  HOH A O     1 
HETATM 4365 O  O     . HOH E 5 .   ? -2.65990  -10.49843 29.35536  1.000 32.37000  ? 885  HOH A O     1 
HETATM 4366 O  O     . HOH E 5 .   ? 4.84937   2.57813   10.29136  1.000 26.94000  ? 886  HOH A O     1 
HETATM 4367 O  O     . HOH E 5 .   ? 13.85979  10.84181  25.91821  1.000 32.32000  ? 887  HOH A O     1 
HETATM 4368 O  O     . HOH E 5 .   ? 12.34978  23.99264  6.86301   1.000 26.68000  ? 888  HOH A O     1 
HETATM 4369 O  O     . HOH E 5 .   ? -10.12398 24.52834  2.10584   1.000 30.00000  ? 889  HOH A O     1 
HETATM 4370 O  O     . HOH E 5 .   ? -11.00651 17.80199  -9.81092  1.000 38.27000  ? 890  HOH A O     1 
HETATM 4371 O  O     . HOH E 5 .   ? -3.40332  6.72824   -13.23348 1.000 32.10000  ? 891  HOH A O     1 
HETATM 4372 O  O     . HOH E 5 .   ? 19.60427  20.45198  32.78959  1.000 37.76000  ? 892  HOH A O     1 
HETATM 4373 O  O     . HOH E 5 .   ? -0.58940  24.65263  9.92495   1.000 30.82000  ? 893  HOH A O     1 
HETATM 4374 O  O     . HOH E 5 .   ? 4.36621   3.07120   33.39091  1.000 34.27000  ? 894  HOH A O     1 
HETATM 4375 O  O     . HOH E 5 .   ? -1.05512  -4.10737  31.56795  1.000 37.63000  ? 895  HOH A O     1 
HETATM 4376 O  O     . HOH E 5 .   ? -0.93923  4.79288   -6.49829  1.000 26.22000  ? 896  HOH A O     1 
HETATM 4377 O  O     . HOH E 5 .   ? 12.33304  8.03040   51.78334  1.000 33.71000  ? 897  HOH A O     1 
HETATM 4378 O  O     . HOH E 5 .   ? 5.97701   23.92981  -3.19297  1.000 37.45000  ? 898  HOH A O     1 
HETATM 4379 O  O     . HOH E 5 .   ? -5.00114  -3.38006  13.11896  1.000 32.60000  ? 899  HOH A O     1 
HETATM 4380 O  O     . HOH E 5 .   ? -16.64028 2.33132   19.16568  1.000 28.87000  ? 900  HOH A O     1 
HETATM 4381 O  O     . HOH E 5 .   ? -5.08643  4.26290   38.58690  1.000 32.29000  ? 901  HOH A O     1 
HETATM 4382 O  O     . HOH E 5 .   ? -3.09354  13.45161  -17.67998 1.000 39.17000  ? 902  HOH A O     1 
HETATM 4383 O  O     . HOH E 5 .   ? 11.95655  6.45826   47.33006  1.000 37.98000  ? 903  HOH A O     1 
HETATM 4384 O  O     . HOH E 5 .   ? -12.90454 -9.90347  27.00844  1.000 44.15000  ? 904  HOH A O     1 
HETATM 4385 O  O     . HOH E 5 .   ? 16.84855  5.83962   20.90672  1.000 26.65000  ? 905  HOH A O     1 
HETATM 4386 O  O     . HOH E 5 .   ? -17.52821 2.37056   26.00838  1.000 33.50000  ? 906  HOH A O     1 
HETATM 4387 O  O     . HOH E 5 .   ? 4.63818   28.84599  23.61496  1.000 31.31000  ? 907  HOH A O     1 
HETATM 4388 O  O     . HOH E 5 .   ? -18.07129 13.68625  -1.09322  1.000 31.70000  ? 908  HOH A O     1 
HETATM 4389 O  O     . HOH E 5 .   ? 24.23898  12.08024  12.41123  1.000 43.92000  ? 909  HOH A O     1 
HETATM 4390 O  O     . HOH E 5 .   ? -12.00615 23.36279  16.11941  1.000 31.06000  ? 910  HOH A O     1 
HETATM 4391 O  O     . HOH E 5 .   ? 26.00766  7.90620   14.97445  1.000 34.84000  ? 911  HOH A O     1 
HETATM 4392 O  O     . HOH E 5 .   ? 21.66981  16.30080  11.42807  1.000 32.42000  ? 912  HOH A O     1 
HETATM 4393 O  O     . HOH E 5 .   ? 11.52639  -11.75284 7.82377   1.000 28.28000  ? 913  HOH A O     1 
HETATM 4394 O  O     . HOH E 5 .   ? -6.621    -16.348   18.151    1.000 34.64000  ? 914  HOH A O     1 
HETATM 4395 O  O     . HOH E 5 .   ? 15.16117  29.16537  49.85606  1.000 35.91000  ? 915  HOH A O     1 
HETATM 4396 O  O     . HOH E 5 .   ? 0.41532   21.94056  45.85449  1.000 29.30000  ? 916  HOH A O     1 
HETATM 4397 O  O     . HOH E 5 .   ? 4.34391   18.97212  -5.51467  1.000 32.99000  ? 917  HOH A O     1 
HETATM 4398 O  O     . HOH E 5 .   ? 11.68084  27.90845  3.33571   1.000 32.51000  ? 918  HOH A O     1 
HETATM 4399 O  O     . HOH E 5 .   ? 4.50173   29.01179  3.19281   1.000 39.70000  ? 919  HOH A O     1 
HETATM 4400 O  O     . HOH E 5 .   ? 6.78805   8.51539   26.86914  1.000 32.92000  ? 920  HOH A O     1 
HETATM 4401 O  O     . HOH E 5 .   ? 7.99753   24.79137  48.79887  1.000 32.02000  ? 921  HOH A O     1 
HETATM 4402 O  O     . HOH E 5 .   ? 19.03694  12.96931  50.79383  1.000 30.00000  ? 922  HOH A O     1 
HETATM 4403 O  O     . HOH E 5 .   ? 3.68819   22.72377  -13.80575 1.000 30.00000  ? 923  HOH A O     1 
HETATM 4404 O  O     . HOH E 5 .   ? 4.63732   20.64674  23.38675  1.000 35.91000  ? 924  HOH A O     1 
HETATM 4405 O  O     . HOH E 5 .   ? -4.58009  29.49943  24.64476  1.000 38.42000  ? 925  HOH A O     1 
HETATM 4406 O  O     . HOH E 5 .   ? -0.21245  27.29045  6.18469   1.000 24.35000  ? 926  HOH A O     1 
HETATM 4407 O  O     . HOH E 5 .   ? 11.38404  -19.01707 24.51350  1.000 32.63000  ? 927  HOH A O     1 
HETATM 4408 O  O     . HOH E 5 .   ? -17.37239 23.37797  19.57773  1.000 30.00000  ? 928  HOH A O     1 
HETATM 4409 O  O     . HOH E 5 .   ? -2.32570  -0.02372  38.10585  1.000 43.68000  ? 929  HOH A O     1 
HETATM 4410 O  O     . HOH E 5 .   ? 21.95273  -20.20838 15.35911  1.000 42.85000  ? 930  HOH A O     1 
HETATM 4411 O  O     . HOH E 5 .   ? 18.91736  27.59991  25.02906  1.000 39.30000  ? 931  HOH A O     1 
HETATM 4412 O  O     . HOH E 5 .   ? -12.00639 8.38720   10.55320  1.000 38.23000  ? 932  HOH A O     1 
HETATM 4413 O  O     . HOH E 5 .   ? -17.49771 13.93040  7.65561   1.000 37.14000  ? 933  HOH A O     1 
HETATM 4414 O  O     . HOH E 5 .   ? -10.33328 -4.60520  32.27188  1.000 30.00000  ? 934  HOH A O     1 
HETATM 4415 O  O     . HOH E 5 .   ? -9.25054  11.79007  -17.09770 1.000 30.87000  ? 935  HOH A O     1 
HETATM 4416 O  O     . HOH E 5 .   ? -7.95277  -19.00193 22.34799  1.000 34.70000  ? 936  HOH A O     1 
HETATM 4417 O  O     . HOH E 5 .   ? 23.02178  16.72456  15.09636  1.000 34.59000  ? 937  HOH A O     1 
HETATM 4418 O  O     . HOH E 5 .   ? 8.40466   2.34992   39.96972  1.000 41.11000  ? 938  HOH A O     1 
HETATM 4419 O  O     . HOH E 5 .   ? 17.42899  8.69904   20.47500  1.000 35.73000  ? 939  HOH A O     1 
HETATM 4420 O  O     . HOH E 5 .   ? -6.81884  21.35893  -16.08949 1.000 39.78000  ? 940  HOH A O     1 
HETATM 4421 O  O     . HOH E 5 .   ? 7.27455   -2.41166  9.22327   1.000 37.05000  ? 941  HOH A O     1 
HETATM 4422 O  O     . HOH E 5 .   ? 5.28837   35.15595  40.28368  1.000 31.36000  ? 942  HOH A O     1 
HETATM 4423 O  O     . HOH E 5 .   ? 10.58096  27.40081  53.71014  1.000 30.00000  ? 943  HOH A O     1 
HETATM 4424 O  O     . HOH E 5 .   ? 1.61336   14.83466  50.75229  1.000 41.71000  ? 944  HOH A O     1 
HETATM 4425 O  O     . HOH E 5 .   ? -15.76734 21.65623  22.37680  1.000 37.15000  ? 945  HOH A O     1 
HETATM 4426 O  O     . HOH E 5 .   ? 23.47251  0.96416   5.52821   1.000 23.69000  ? 946  HOH A O     1 
HETATM 4427 O  O     . HOH E 5 .   ? 22.09798  16.57832  4.88865   1.000 42.07000  ? 947  HOH A O     1 
HETATM 4428 O  O     A HOH E 5 .   ? -3.70546  25.80785  -14.37806 0.488 24.80000  ? 948  HOH A O     1 
HETATM 4429 O  O     B HOH E 5 .   ? -4.09514  27.29652  -12.61341 0.512 20.55000  ? 948  HOH A O     1 
HETATM 4430 O  O     . HOH E 5 .   ? 27.03739  7.71499   10.59456  1.000 40.99000  ? 949  HOH A O     1 
HETATM 4431 O  O     . HOH E 5 .   ? 4.34549   22.23631  -5.56382  1.000 37.89000  ? 950  HOH A O     1 
HETATM 4432 O  O     . HOH E 5 .   ? 8.06073   10.47814  26.64373  1.000 31.51000  ? 951  HOH A O     1 
HETATM 4433 O  O     . HOH E 5 .   ? 4.88723   21.60246  51.59582  1.000 46.42000  ? 952  HOH A O     1 
HETATM 4434 O  O     . HOH E 5 .   ? 16.86275  8.09370   0.29919   1.000 45.04000  ? 953  HOH A O     1 
HETATM 4435 O  O     . HOH E 5 .   ? 23.05659  13.45606  19.06378  1.000 43.55000  ? 954  HOH A O     1 
HETATM 4436 O  O     . HOH E 5 .   ? 13.72730  30.97826  33.71953  1.000 41.94000  ? 955  HOH A O     1 
HETATM 4437 O  O     . HOH E 5 .   ? 19.77315  -9.62909  11.67536  1.000 40.21000  ? 956  HOH A O     1 
HETATM 4438 O  O     . HOH E 5 .   ? 6.35436   14.59877  52.61078  1.000 39.21000  ? 957  HOH A O     1 
HETATM 4439 O  O     . HOH E 5 .   ? 4.49869   2.45362   7.52439   1.000 29.91000  ? 958  HOH A O     1 
HETATM 4440 O  O     . HOH E 5 .   ? -18.63922 0.11449   8.85589   1.000 38.71000  ? 959  HOH A O     1 
HETATM 4441 O  O     . HOH E 5 .   ? 9.98498   22.89385  19.27384  1.000 43.26000  ? 960  HOH A O     1 
HETATM 4442 O  O     . HOH E 5 .   ? 23.56900  9.63845   22.43700  1.000 33.75000  ? 961  HOH A O     1 
HETATM 4443 O  O     . HOH E 5 .   ? 13.82042  17.56936  -6.28450  1.000 42.47000  ? 962  HOH A O     1 
HETATM 4444 O  O     . HOH E 5 .   ? -1.02205  6.37597   -17.71216 1.000 43.65000  ? 963  HOH A O     1 
HETATM 4445 O  O     . HOH E 5 .   ? 23.79053  15.63582  34.46823  1.000 33.85000  ? 964  HOH A O     1 
HETATM 4446 O  O     . HOH E 5 .   ? 10.83451  -16.80456 25.70665  1.000 40.32000  ? 965  HOH A O     1 
HETATM 4447 O  O     . HOH E 5 .   ? 20.86822  31.63928  39.67199  1.000 38.43000  ? 966  HOH A O     1 
HETATM 4448 O  O     . HOH E 5 .   ? 0.23253   30.50894  34.31886  1.000 27.96000  ? 967  HOH A O     1 
HETATM 4449 O  O     . HOH E 5 .   ? -15.98602 9.89264   13.63590  1.000 30.00000  ? 968  HOH A O     1 
HETATM 4450 O  O     . HOH E 5 .   ? 13.73787  27.74419  1.41503   1.000 31.50000  ? 969  HOH A O     1 
HETATM 4451 O  O     . HOH E 5 .   ? -11.62496 21.08864  -1.46614  1.000 38.92000  ? 970  HOH A O     1 
HETATM 4452 O  O     . HOH E 5 .   ? -9.36666  27.23815  8.11087   1.000 36.68000  ? 971  HOH A O     1 
HETATM 4453 O  O     . HOH E 5 .   ? 6.84952   25.26079  18.97005  1.000 30.68000  ? 972  HOH A O     1 
HETATM 4454 O  O     . HOH E 5 .   ? 18.91920  18.80705  23.60856  1.000 33.33000  ? 973  HOH A O     1 
HETATM 4455 O  O     . HOH E 5 .   ? 8.33217   22.42439  12.85466  1.000 30.00000  ? 974  HOH A O     1 
HETATM 4456 O  O     . HOH E 5 .   ? 21.81002  10.75504  20.46046  1.000 37.41000  ? 975  HOH A O     1 
HETATM 4457 O  O     . HOH E 5 .   ? -17.12424 8.72988   26.25704  1.000 39.20000  ? 976  HOH A O     1 
HETATM 4458 O  O     . HOH E 5 .   ? 10.46119  11.33424  24.94199  1.000 32.23000  ? 977  HOH A O     1 
HETATM 4459 O  O     A HOH E 5 .   ? 21.06701  9.43989   7.29604   0.492 27.37000  ? 978  HOH A O     1 
HETATM 4460 O  O     B HOH E 5 .   ? 22.48557  8.61150   9.01840   0.508 21.12000  ? 978  HOH A O     1 
HETATM 4461 O  O     . HOH E 5 .   ? 21.74576  13.85141  7.95129   1.000 35.24000  ? 979  HOH A O     1 
HETATM 4462 O  O     . HOH E 5 .   ? 4.81302   -14.98167 27.41174  1.000 30.22000  ? 980  HOH A O     1 
HETATM 4463 O  O     . HOH E 5 .   ? 2.73844   27.88121  5.17860   1.000 31.43000  ? 981  HOH A O     1 
HETATM 4464 O  O     . HOH E 5 .   ? -1.67307  30.66981  -3.59096  1.000 37.81000  ? 982  HOH A O     1 
HETATM 4465 O  O     . HOH E 5 .   ? 4.65213   16.12863  52.40444  1.000 34.64000  ? 983  HOH A O     1 
HETATM 4466 O  O     . HOH E 5 .   ? -19.66752 -6.18354  15.67581  1.000 30.00000  ? 984  HOH A O     1 
HETATM 4467 O  O     . HOH E 5 .   ? 12.16077  -7.38307  9.91877   1.000 34.02000  ? 985  HOH A O     1 
HETATM 4468 O  O     . HOH E 5 .   ? -11.50281 -6.93581  28.26831  1.000 39.11000  ? 986  HOH A O     1 
HETATM 4469 O  O     . HOH E 5 .   ? -14.63121 18.33364  11.19504  1.000 31.53000  ? 987  HOH A O     1 
HETATM 4470 O  O     . HOH E 5 .   ? 4.23400   27.38567  7.10733   1.000 34.34000  ? 988  HOH A O     1 
HETATM 4471 O  O     . HOH E 5 .   ? -20.17305 15.92947  14.64927  1.000 38.88000  ? 989  HOH A O     1 
HETATM 4472 O  O     . HOH E 5 .   ? 25.58487  2.27481   23.83426  1.000 35.23000  ? 990  HOH A O     1 
HETATM 4473 O  O     . HOH E 5 .   ? 18.19371  -3.05312  2.77560   1.000 44.58000  ? 991  HOH A O     1 
HETATM 4474 O  O     . HOH E 5 .   ? -3.21602  30.68218  22.63172  1.000 42.09000  ? 992  HOH A O     1 
HETATM 4475 O  O     . HOH E 5 .   ? 28.21599  6.80005   18.78308  1.000 39.36000  ? 993  HOH A O     1 
HETATM 4476 O  O     . HOH E 5 .   ? 1.89848   1.50807   3.01632   1.000 38.36000  ? 994  HOH A O     1 
HETATM 4477 O  O     . HOH E 5 .   ? 13.49836  -13.47961 7.66324   1.000 53.02000  ? 995  HOH A O     1 
HETATM 4478 O  O     . HOH E 5 .   ? 25.06118  8.62497   12.47617  1.000 30.00000  ? 996  HOH A O     1 
HETATM 4479 O  O     . HOH E 5 .   ? 3.75426   22.83063  47.75767  1.000 35.48000  ? 997  HOH A O     1 
HETATM 4480 O  O     . HOH E 5 .   ? 8.69644   24.97398  12.92321  1.000 45.48000  ? 998  HOH A O     1 
HETATM 4481 O  O     . HOH E 5 .   ? -16.36852 7.03051   21.10534  1.000 34.03000  ? 999  HOH A O     1 
HETATM 4482 O  O     . HOH E 5 .   ? -6.31900  -11.21052 27.51051  1.000 29.13000  ? 1000 HOH A O     1 
HETATM 4483 O  O     . HOH E 5 .   ? -11.50074 1.83018   34.05715  1.000 37.09000  ? 1001 HOH A O     1 
HETATM 4484 O  O     . HOH E 5 .   ? -16.53659 17.56607  12.17759  1.000 43.81000  ? 1002 HOH A O     1 
HETATM 4485 O  O     . HOH E 5 .   ? 19.60472  7.41679   36.50366  1.000 34.31000  ? 1003 HOH A O     1 
HETATM 4486 O  O     . HOH E 5 .   ? 7.80529   24.83825  16.28610  1.000 40.35000  ? 1004 HOH A O     1 
HETATM 4487 O  O     . HOH E 5 .   ? 11.24985  26.18798  25.72334  1.000 47.73000  ? 1005 HOH A O     1 
HETATM 4488 O  O     . HOH E 5 .   ? -6.59082  11.07793  42.32524  1.000 29.62000  ? 1006 HOH A O     1 
HETATM 4489 O  O     . HOH E 5 .   ? 22.98454  10.28650  25.74236  1.000 37.03000  ? 1007 HOH A O     1 
HETATM 4490 O  O     . HOH E 5 .   ? 9.92424   27.66698  28.40203  1.000 41.64000  ? 1008 HOH A O     1 
HETATM 4491 O  O     . HOH E 5 .   ? 2.00205   26.06626  45.55944  1.000 34.80000  ? 1009 HOH A O     1 
HETATM 4492 O  O     . HOH E 5 .   ? -9.71615  -14.86996 18.97732  1.000 30.85000  ? 1010 HOH A O     1 
HETATM 4493 O  O     . HOH E 5 .   ? 17.30302  31.05267  44.63374  1.000 35.14000  ? 1011 HOH A O     1 
HETATM 4494 O  O     . HOH E 5 .   ? 21.96640  15.19295  29.21613  1.000 38.52000  ? 1012 HOH A O     1 
HETATM 4495 O  O     . HOH E 5 .   ? 1.79689   2.60435   -2.32718  1.000 46.46000  ? 1013 HOH A O     1 
HETATM 4496 O  O     . HOH E 5 .   ? -11.55823 11.76978  43.12203  1.000 39.11000  ? 1014 HOH A O     1 
HETATM 4497 O  O     . HOH E 5 .   ? -6.66634  28.28057  7.13120   1.000 37.28000  ? 1015 HOH A O     1 
HETATM 4498 O  O     . HOH E 5 .   ? -7.61022  -19.61727 25.73561  1.000 41.21000  ? 1016 HOH A O     1 
HETATM 4499 O  O     . HOH E 5 .   ? -17.73830 13.60109  3.50405   1.000 41.86000  ? 1017 HOH A O     1 
HETATM 4500 O  O     . HOH E 5 .   ? -4.74455  19.81502  41.93091  1.000 27.27000  ? 1018 HOH A O     1 
HETATM 4501 O  O     . HOH E 5 .   ? 1.34362   31.52487  -4.16630  1.000 41.07000  ? 1019 HOH A O     1 
HETATM 4502 O  O     . HOH E 5 .   ? -5.64164  26.06508  15.29526  1.000 36.87000  ? 1020 HOH A O     1 
HETATM 4503 O  O     . HOH E 5 .   ? -7.836    -16.107   12.039    1.000 30.00000  ? 1021 HOH A O     1 
HETATM 4504 O  O     . HOH E 5 .   ? -13.27477 0.37344   32.29618  1.000 35.59000  ? 1022 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . MET A 1   ? 1.22141 1.29785 1.08066 0.02922  -0.15922 -0.07846 1   MET A N   
2    C  CA  . MET A 1   ? 1.22471 1.28433 1.06351 0.03312  -0.15169 -0.06342 1   MET A CA  
3    C  C   . MET A 1   ? 1.22623 1.27234 1.05607 0.02661  -0.13877 -0.06218 1   MET A C   
4    O  O   . MET A 1   ? 1.23531 1.26984 1.04060 0.02932  -0.13446 -0.05464 1   MET A O   
5    C  CB  . MET A 1   ? 1.26227 1.31967 1.07265 0.04340  -0.16124 -0.05769 1   MET A CB  
6    C  CG  . MET A 1   ? 1.27681 1.33532 1.06472 0.04411  -0.16601 -0.06530 1   MET A CG  
7    S  SD  . MET A 1   ? 1.27597 1.35643 1.08060 0.04217  -0.17930 -0.08513 1   MET A SD  
8    C  CE  . MET A 1   ? 1.29432 1.37082 1.06634 0.04304  -0.18139 -0.09147 1   MET A CE  
9    N  N   . ALA A 2   ? 0.59757 0.64507 0.44806 0.01799  -0.13233 -0.06955 2   ALA A N   
10   C  CA  . ALA A 2   ? 0.60172 0.63758 0.44653 0.01247  -0.12108 -0.07005 2   ALA A CA  
11   C  C   . ALA A 2   ? 0.58962 0.61227 0.43079 0.01236  -0.10975 -0.05683 2   ALA A C   
12   O  O   . ALA A 2   ? 0.59703 0.60988 0.42693 0.01038  -0.10124 -0.05510 2   ALA A O   
13   C  CB  . ALA A 2   ? 0.57942 0.61872 0.44733 0.00385  -0.11807 -0.08123 2   ALA A CB  
14   N  N   . GLY A 3   ? 0.41539 0.43842 0.26656 0.01445  -0.10948 -0.04846 3   GLY A N   
15   C  CA  . GLY A 3   ? 0.41216 0.42367 0.26083 0.01436  -0.09965 -0.03667 3   GLY A CA  
16   C  C   . GLY A 3   ? 0.40568 0.41725 0.27860 0.00871  -0.09294 -0.03627 3   GLY A C   
17   O  O   . GLY A 3   ? 0.39481 0.41358 0.28606 0.00383  -0.09431 -0.04477 3   GLY A O   
18   N  N   . ALA A 4   ? 0.37171 0.37457 0.24368 0.00911  -0.08531 -0.02609 4   ALA A N   
19   C  CA  . ALA A 4   ? 0.35956 0.36142 0.25096 0.00477  -0.07875 -0.02379 4   ALA A CA  
20   C  C   . ALA A 4   ? 0.35200 0.34285 0.23997 0.00129  -0.06811 -0.02029 4   ALA A C   
21   O  O   . ALA A 4   ? 0.35738 0.34088 0.22847 0.00347  -0.06455 -0.01536 4   ALA A O   
22   C  CB  . ALA A 4   ? 0.35048 0.35356 0.24680 0.00879  -0.07990 -0.01579 4   ALA A CB  
23   N  N   . LEU A 5   ? 0.37973 0.36968 0.28385 -0.00409 -0.06307 -0.02289 5   LEU A N   
24   C  CA  . LEU A 5   ? 0.37325 0.35373 0.27746 -0.00662 -0.05376 -0.01935 5   LEU A CA  
25   C  C   . LEU A 5   ? 0.37326 0.35171 0.28463 -0.00621 -0.04958 -0.01077 5   LEU A C   
26   O  O   . LEU A 5   ? 0.36846 0.35186 0.29455 -0.00812 -0.05050 -0.01112 5   LEU A O   
27   C  CB  . LEU A 5   ? 0.37520 0.35373 0.29095 -0.01202 -0.05112 -0.02667 5   LEU A CB  
28   C  CG  . LEU A 5   ? 0.37833 0.34729 0.29617 -0.01383 -0.04256 -0.02352 5   LEU A CG  
29   C  CD1 . LEU A 5   ? 0.37373 0.33785 0.27605 -0.01119 -0.03922 -0.02328 5   LEU A CD1 
30   C  CD2 . LEU A 5   ? 0.37198 0.33760 0.30278 -0.01888 -0.04091 -0.02976 5   LEU A CD2 
31   N  N   . ARG A 6   ? 0.30963 0.28141 0.21088 -0.00412 -0.04467 -0.00372 6   ARG A N   
32   C  CA  . ARG A 6   ? 0.29889 0.26864 0.20441 -0.00309 -0.04139 0.00407  6   ARG A CA  
33   C  C   . ARG A 6   ? 0.28915 0.25294 0.19903 -0.00583 -0.03347 0.00627  6   ARG A C   
34   O  O   . ARG A 6   ? 0.28961 0.24852 0.19055 -0.00557 -0.02929 0.00707  6   ARG A O   
35   C  CB  . ARG A 6   ? 0.30233 0.26886 0.19344 0.00140  -0.04264 0.01046  6   ARG A CB  
36   C  CG  . ARG A 6   ? 0.31183 0.28396 0.19895 0.00556  -0.05165 0.00929  6   ARG A CG  
37   C  CD  . ARG A 6   ? 0.32381 0.28978 0.19364 0.01032  -0.05306 0.01631  6   ARG A CD  
38   N  NE  . ARG A 6   ? 0.33611 0.30705 0.20002 0.01531  -0.06286 0.01472  6   ARG A NE  
39   C  CZ  . ARG A 6   ? 0.33485 0.31035 0.20635 0.01949  -0.06875 0.01625  6   ARG A CZ  
40   N  NH1 . ARG A 6   ? 0.32214 0.29753 0.20663 0.01899  -0.06530 0.01939  6   ARG A NH1 
41   N  NH2 . ARG A 6   ? 0.34751 0.32847 0.21347 0.02474  -0.07861 0.01402  6   ARG A NH2 
42   N  N   . LEU A 7   ? 0.31605 0.28090 0.23949 -0.00824 -0.03147 0.00709  7   LEU A N   
43   C  CA  . LEU A 7   ? 0.30923 0.26871 0.23711 -0.01020 -0.02515 0.00928  7   LEU A CA  
44   C  C   . LEU A 7   ? 0.29632 0.25365 0.22143 -0.00829 -0.02171 0.01624  7   LEU A C   
45   O  O   . LEU A 7   ? 0.29310 0.25330 0.22042 -0.00683 -0.02350 0.01941  7   LEU A O   
46   C  CB  . LEU A 7   ? 0.31138 0.27189 0.25292 -0.01391 -0.02436 0.00757  7   LEU A CB  
47   C  CG  . LEU A 7   ? 0.31647 0.27063 0.26206 -0.01546 -0.01880 0.01030  7   LEU A CG  
48   C  CD1 . LEU A 7   ? 0.31162 0.25957 0.25309 -0.01531 -0.01699 0.00680  7   LEU A CD1 
49   C  CD2 . LEU A 7   ? 0.30825 0.26310 0.26534 -0.01942 -0.01782 0.01009  7   LEU A CD2 
50   N  N   . VAL A 8   ? 0.29575 0.24855 0.21706 -0.00821 -0.01690 0.01778  8   VAL A N   
51   C  CA  . VAL A 8   ? 0.28133 0.23236 0.20143 -0.00726 -0.01322 0.02317  8   VAL A CA  
52   C  C   . VAL A 8   ? 0.27491 0.22375 0.20134 -0.00831 -0.00925 0.02329  8   VAL A C   
53   O  O   . VAL A 8   ? 0.28208 0.22877 0.20729 -0.00831 -0.00747 0.02019  8   VAL A O   
54   C  CB  . VAL A 8   ? 0.28022 0.22899 0.18849 -0.00599 -0.01131 0.02497  8   VAL A CB  
55   C  CG1 . VAL A 8   ? 0.26202 0.20906 0.17127 -0.00615 -0.00681 0.02919  8   VAL A CG1 
56   C  CG2 . VAL A 8   ? 0.28326 0.23238 0.18318 -0.00404 -0.01579 0.02647  8   VAL A CG2 
57   N  N   . LEU A 9   ? 0.27807 0.22751 0.21074 -0.00863 -0.00813 0.02659  9   LEU A N   
58   C  CA  . LEU A 9   ? 0.26705 0.21422 0.20447 -0.00895 -0.00531 0.02742  9   LEU A CA  
59   C  C   . LEU A 9   ? 0.25484 0.20218 0.18989 -0.00754 -0.00231 0.02956  9   LEU A C   
60   O  O   . LEU A 9   ? 0.25684 0.20512 0.18699 -0.00718 -0.00163 0.03086  9   LEU A O   
61   C  CB  . LEU A 9   ? 0.26215 0.21022 0.20641 -0.01039 -0.00543 0.02952  9   LEU A CB  
62   C  CG  . LEU A 9   ? 0.28249 0.23106 0.23165 -0.01301 -0.00747 0.02673  9   LEU A CG  
63   C  CD1 . LEU A 9   ? 0.27367 0.22359 0.22943 -0.01521 -0.00602 0.02901  9   LEU A CD1 
64   C  CD2 . LEU A 9   ? 0.28515 0.22836 0.23417 -0.01384 -0.00735 0.02310  9   LEU A CD2 
65   N  N   . GLY A 10  ? 0.26414 0.21022 0.20282 -0.00679 -0.00065 0.02989  10  GLY A N   
66   C  CA  . GLY A 10  ? 0.26196 0.20989 0.20039 -0.00545 0.00177  0.03030  10  GLY A CA  
67   C  C   . GLY A 10  ? 0.25732 0.20772 0.19580 -0.00590 0.00256  0.03325  10  GLY A C   
68   O  O   . GLY A 10  ? 0.25290 0.20541 0.19080 -0.00589 0.00475  0.03290  10  GLY A O   
69   N  N   . ASP A 11  ? 0.32523 0.27577 0.26524 -0.00652 0.00115  0.03546  11  ASP A N   
70   C  CA  . ASP A 11  ? 0.31702 0.26922 0.25737 -0.00660 0.00173  0.03746  11  ASP A CA  
71   C  C   . ASP A 11  ? 0.32403 0.27535 0.26136 -0.00670 0.00029  0.03839  11  ASP A C   
72   O  O   . ASP A 11  ? 0.32294 0.27478 0.26167 -0.00626 -0.00002 0.03977  11  ASP A O   
73   C  CB  . ASP A 11  ? 0.32386 0.27749 0.26810 -0.00646 0.00158  0.03884  11  ASP A CB  
74   C  CG  . ASP A 11  ? 0.33826 0.29206 0.28487 -0.00747 0.00027  0.03916  11  ASP A CG  
75   O  OD1 . ASP A 11  ? 0.33877 0.29135 0.28502 -0.00816 -0.00111 0.03767  11  ASP A OD1 
76   O  OD2 . ASP A 11  ? 0.33872 0.29467 0.28793 -0.00786 0.00086  0.04028  11  ASP A OD2 
77   N  N   . GLN A 12  ? 0.25120 0.20105 0.18394 -0.00670 -0.00095 0.03740  12  GLN A N   
78   C  CA  . GLN A 12  ? 0.25463 0.20331 0.18312 -0.00578 -0.00356 0.03848  12  GLN A CA  
79   C  C   . GLN A 12  ? 0.26167 0.20667 0.18079 -0.00591 -0.00221 0.03937  12  GLN A C   
80   O  O   . GLN A 12  ? 0.27289 0.21630 0.18535 -0.00488 -0.00484 0.03963  12  GLN A O   
81   C  CB  . GLN A 12  ? 0.26196 0.21297 0.19253 -0.00561 -0.00724 0.03629  12  GLN A CB  
82   C  CG  . GLN A 12  ? 0.26510 0.21944 0.20470 -0.00665 -0.00738 0.03559  12  GLN A CG  
83   C  CD  . GLN A 12  ? 0.27954 0.23722 0.22306 -0.00742 -0.01075 0.03283  12  GLN A CD  
84   O  OE1 . GLN A 12  ? 0.28388 0.24094 0.22389 -0.00761 -0.01283 0.03025  12  GLN A OE1 
85   N  NE2 . GLN A 12  ? 0.28003 0.24219 0.23133 -0.00811 -0.01111 0.03263  12  GLN A NE2 
86   N  N   . LEU A 13  ? 0.25669 0.20078 0.17498 -0.00734 0.00198  0.03973  13  LEU A N   
87   C  CA  . LEU A 13  ? 0.26744 0.20877 0.17725 -0.00869 0.00506  0.04015  13  LEU A CA  
88   C  C   . LEU A 13  ? 0.27285 0.20815 0.17666 -0.00903 0.00580  0.04429  13  LEU A C   
89   O  O   . LEU A 13  ? 0.27014 0.20342 0.17379 -0.01143 0.01005  0.04525  13  LEU A O   
90   C  CB  . LEU A 13  ? 0.25942 0.20425 0.17321 -0.01040 0.00956  0.03750  13  LEU A CB  
91   C  CG  . LEU A 13  ? 0.26329 0.21216 0.18430 -0.00903 0.00821  0.03414  13  LEU A CG  
92   C  CD1 . LEU A 13  ? 0.25324 0.20635 0.17943 -0.00937 0.01164  0.03135  13  LEU A CD1 
93   C  CD2 . LEU A 13  ? 0.26652 0.21466 0.18364 -0.00819 0.00605  0.03174  13  LEU A CD2 
94   N  N   . SER A 14  ? 0.32523 0.25740 0.22451 -0.00647 0.00133  0.04647  14  SER A N   
95   C  CA  . SER A 14  ? 0.33260 0.25693 0.22522 -0.00544 0.00076  0.05090  14  SER A CA  
96   C  C   . SER A 14  ? 0.34261 0.26305 0.22324 -0.00293 -0.00311 0.05300  14  SER A C   
97   O  O   . SER A 14  ? 0.34419 0.26976 0.22606 -0.00087 -0.00771 0.05036  14  SER A O   
98   C  CB  . SER A 14  ? 0.32493 0.24955 0.22581 -0.00304 -0.00211 0.05138  14  SER A CB  
99   O  OG  . SER A 14  ? 0.32514 0.25600 0.23686 -0.00452 -0.00021 0.04841  14  SER A OG  
100  N  N   . ASP A 15  ? 0.53874 0.44973 0.40729 -0.00328 -0.00131 0.05772  15  ASP A N   
101  C  CA  . ASP A 15  ? 0.55102 0.45713 0.40544 -0.00016 -0.00557 0.06060  15  ASP A CA  
102  C  C   . ASP A 15  ? 0.56352 0.47035 0.42127 0.00568  -0.01377 0.06115  15  ASP A C   
103  O  O   . ASP A 15  ? 0.57218 0.48129 0.42385 0.00908  -0.01967 0.06043  15  ASP A O   
104  C  CB  . ASP A 15  ? 0.57336 0.46703 0.41272 -0.00195 -0.00133 0.06677  15  ASP A CB  
105  C  CG  . ASP A 15  ? 0.57341 0.46789 0.41193 -0.00839 0.00779  0.06559  15  ASP A CG  
106  O  OD1 . ASP A 15  ? 0.58725 0.47250 0.41976 -0.01178 0.01322  0.06985  15  ASP A OD1 
107  O  OD2 . ASP A 15  ? 0.56064 0.46492 0.40518 -0.01008 0.00960  0.06012  15  ASP A OD2 
108  N  N   . ASN A 16  ? 0.53318 0.43928 0.40116 0.00706  -0.01437 0.06158  16  ASN A N   
109  C  CA  . ASN A 16  ? 0.53839 0.44633 0.41168 0.01290  -0.02148 0.06138  16  ASN A CA  
110  C  C   . ASN A 16  ? 0.52845 0.44994 0.41669 0.01314  -0.02410 0.05535  16  ASN A C   
111  O  O   . ASN A 16  ? 0.53590 0.46153 0.43328 0.01682  -0.02807 0.05390  16  ASN A O   
112  C  CB  . ASN A 16  ? 0.53814 0.43793 0.41464 0.01459  -0.02044 0.06428  16  ASN A CB  
113  C  CG  . ASN A 16  ? 0.53443 0.43767 0.42246 0.01012  -0.01450 0.06146  16  ASN A CG  
114  O  OD1 . ASN A 16  ? 0.53258 0.44393 0.42604 0.00627  -0.01141 0.05801  16  ASN A OD1 
115  N  ND2 . ASN A 16  ? 0.54964 0.44628 0.44109 0.01110  -0.01332 0.06269  16  ASN A ND2 
116  N  N   . LEU A 17  ? 0.29355 0.22157 0.18466 0.00922  -0.02157 0.05170  17  LEU A N   
117  C  CA  . LEU A 17  ? 0.28792 0.22675 0.19182 0.00862  -0.02352 0.04658  17  LEU A CA  
118  C  C   . LEU A 17  ? 0.29436 0.23864 0.19931 0.01266  -0.03119 0.04443  17  LEU A C   
119  O  O   . LEU A 17  ? 0.30386 0.24574 0.19756 0.01466  -0.03494 0.04518  17  LEU A O   
120  C  CB  . LEU A 17  ? 0.28157 0.22354 0.18620 0.00430  -0.01994 0.04347  17  LEU A CB  
121  C  CG  . LEU A 17  ? 0.28021 0.23036 0.19764 0.00240  -0.02018 0.03908  17  LEU A CG  
122  C  CD1 . LEU A 17  ? 0.26685 0.21792 0.19297 0.00100  -0.01620 0.03987  17  LEU A CD1 
123  C  CD2 . LEU A 17  ? 0.27570 0.22683 0.19151 -0.00047 -0.01856 0.03580  17  LEU A CD2 
124  N  N   . SER A 18  ? 0.34926 0.30188 0.26787 0.01383  -0.03348 0.04130  18  SER A N   
125  C  CA  . SER A 18  ? 0.36350 0.32359 0.28633 0.01796  -0.04109 0.03833  18  SER A CA  
126  C  C   . SER A 18  ? 0.37194 0.33707 0.29201 0.01620  -0.04430 0.03420  18  SER A C   
127  O  O   . SER A 18  ? 0.38001 0.34884 0.29696 0.02021  -0.05164 0.03250  18  SER A O   
128  C  CB  . SER A 18  ? 0.35926 0.32943 0.29937 0.01811  -0.04119 0.03463  18  SER A CB  
129  O  OG  . SER A 18  ? 0.36253 0.33671 0.31055 0.01206  -0.03558 0.03220  18  SER A OG  
130  N  N   . ALA A 19  ? 0.31010 0.27532 0.23121 0.01072  -0.03941 0.03211  19  ALA A N   
131  C  CA  . ALA A 19  ? 0.31288 0.28174 0.23157 0.00878  -0.04199 0.02730  19  ALA A CA  
132  C  C   . ALA A 19  ? 0.32077 0.28347 0.22145 0.01106  -0.04425 0.02922  19  ALA A C   
133  O  O   . ALA A 19  ? 0.32593 0.29253 0.22275 0.01113  -0.04858 0.02468  19  ALA A O   
134  C  CB  . ALA A 19  ? 0.31110 0.27950 0.23512 0.00308  -0.03600 0.02485  19  ALA A CB  
135  N  N   . LEU A 20  ? 0.39300 0.34613 0.28224 0.01248  -0.04112 0.03553  20  LEU A N   
136  C  CA  . LEU A 20  ? 0.39118 0.33723 0.26142 0.01394  -0.04170 0.03842  20  LEU A CA  
137  C  C   . LEU A 20  ? 0.41062 0.35246 0.27079 0.02028  -0.04839 0.04288  20  LEU A C   
138  O  O   . LEU A 20  ? 0.41888 0.35411 0.26088 0.02200  -0.04960 0.04605  20  LEU A O   
139  C  CB  . LEU A 20  ? 0.38178 0.31932 0.24499 0.01045  -0.03296 0.04256  20  LEU A CB  
140  C  CG  . LEU A 20  ? 0.38032 0.32121 0.25191 0.00540  -0.02678 0.03849  20  LEU A CG  
141  C  CD1 . LEU A 20  ? 0.36892 0.30371 0.23743 0.00258  -0.01883 0.04217  20  LEU A CD1 
142  C  CD2 . LEU A 20  ? 0.38401 0.32826 0.25040 0.00417  -0.02789 0.03289  20  LEU A CD2 
143  N  N   . VAL A 21  ? 0.51760 0.46286 0.38854 0.02415  -0.05268 0.04320  21  VAL A N   
144  C  CA  . VAL A 21  ? 0.53797 0.47870 0.40056 0.03152  -0.05989 0.04737  21  VAL A CA  
145  C  C   . VAL A 21  ? 0.55121 0.49916 0.40798 0.03539  -0.06923 0.04336  21  VAL A C   
146  O  O   . VAL A 21  ? 0.54863 0.50933 0.41768 0.03339  -0.07204 0.03557  21  VAL A O   
147  C  CB  . VAL A 21  ? 0.52548 0.46964 0.40364 0.03507  -0.06184 0.04723  21  VAL A CB  
148  C  CG1 . VAL A 21  ? 0.52947 0.47384 0.40405 0.04416  -0.07203 0.04861  21  VAL A CG1 
149  C  CG2 . VAL A 21  ? 0.51228 0.44581 0.39031 0.03293  -0.05412 0.05242  21  VAL A CG2 
150  N  N   . ASP A 22  ? 0.69417 0.63342 0.53139 0.04070  -0.07407 0.04867  22  ASP A N   
151  C  CA  . ASP A 22  ? 0.70125 0.64670 0.53002 0.04589  -0.08447 0.04548  22  ASP A CA  
152  C  C   . ASP A 22  ? 0.70788 0.65988 0.53274 0.04064  -0.08316 0.03882  22  ASP A C   
153  O  O   . ASP A 22  ? 0.71612 0.67973 0.54504 0.04237  -0.09107 0.03151  22  ASP A O   
154  C  CB  . ASP A 22  ? 0.70746 0.66659 0.55438 0.05133  -0.09382 0.03991  22  ASP A CB  
155  C  CG  . ASP A 22  ? 0.72976 0.68200 0.57192 0.06082  -0.10052 0.04608  22  ASP A CG  
156  O  OD1 . ASP A 22  ? 0.73663 0.67187 0.56458 0.06193  -0.09621 0.05518  22  ASP A OD1 
157  O  OD2 . ASP A 22  ? 0.73808 0.70192 0.59158 0.06721  -0.11013 0.04145  22  ASP A OD2 
158  N  N   . ALA A 23  ? 0.47119 0.41633 0.28905 0.03433  -0.07331 0.04048  23  ALA A N   
159  C  CA  . ALA A 23  ? 0.47521 0.42528 0.28932 0.02971  -0.07122 0.03382  23  ALA A CA  
160  C  C   . ALA A 23  ? 0.49129 0.43812 0.28130 0.03330  -0.07638 0.03475  23  ALA A C   
161  O  O   . ALA A 23  ? 0.49676 0.43208 0.26784 0.03680  -0.07636 0.04338  23  ALA A O   
162  C  CB  . ALA A 23  ? 0.45776 0.40231 0.27276 0.02285  -0.05925 0.03494  23  ALA A CB  
163  N  N   . ASP A 24  ? 0.52125 0.47758 0.31125 0.03224  -0.08072 0.02575  24  ASP A N   
164  C  CA  . ASP A 24  ? 0.52982 0.48474 0.29632 0.03492  -0.08521 0.02473  24  ASP A CA  
165  C  C   . ASP A 24  ? 0.53859 0.48968 0.29656 0.02861  -0.07489 0.02254  24  ASP A C   
166  O  O   . ASP A 24  ? 0.52291 0.48152 0.29204 0.02429  -0.07310 0.01319  24  ASP A O   
167  C  CB  . ASP A 24  ? 0.54020 0.50899 0.31248 0.03783  -0.09693 0.01479  24  ASP A CB  
168  C  CG  . ASP A 24  ? 0.56751 0.53560 0.31391 0.04160  -0.10310 0.01341  24  ASP A CG  
169  O  OD1 . ASP A 24  ? 0.57776 0.53399 0.30072 0.04168  -0.09749 0.02075  24  ASP A OD1 
170  O  OD2 . ASP A 24  ? 0.57230 0.55215 0.32157 0.04430  -0.11356 0.00472  24  ASP A OD2 
171  N  N   . LEU A 25  ? 0.53649 0.47561 0.27506 0.02804  -0.06786 0.03096  25  LEU A N   
172  C  CA  . LEU A 25  ? 0.53865 0.47493 0.27178 0.02195  -0.05653 0.02922  25  LEU A CA  
173  C  C   . LEU A 25  ? 0.54862 0.49129 0.27115 0.02126  -0.05848 0.01990  25  LEU A C   
174  O  O   . LEU A 25  ? 0.54752 0.49225 0.27382 0.01644  -0.05065 0.01408  25  LEU A O   
175  C  CB  . LEU A 25  ? 0.54735 0.47025 0.26154 0.02104  -0.04856 0.04003  25  LEU A CB  
176  C  CG  . LEU A 25  ? 0.53819 0.45534 0.26530 0.01680  -0.03900 0.04541  25  LEU A CG  
177  C  CD1 . LEU A 25  ? 0.52663 0.44641 0.27503 0.01913  -0.04417 0.04629  25  LEU A CD1 
178  C  CD2 . LEU A 25  ? 0.54509 0.44820 0.25213 0.01603  -0.03270 0.05625  25  LEU A CD2 
179  N  N   . SER A 26  ? 0.56652 0.51275 0.27607 0.02645  -0.06920 0.01771  26  SER A N   
180  C  CA  . SER A 26  ? 0.58228 0.53459 0.27954 0.02613  -0.07175 0.00827  26  SER A CA  
181  C  C   . SER A 26  ? 0.57437 0.53905 0.29334 0.02409  -0.07679 -0.00500 26  SER A C   
182  O  O   . SER A 26  ? 0.58147 0.55112 0.29392 0.02274  -0.07767 -0.01473 26  SER A O   
183  C  CB  . SER A 26  ? 0.60830 0.55896 0.27957 0.03285  -0.08160 0.01152  26  SER A CB  
184  O  OG  . SER A 26  ? 0.60067 0.55683 0.28195 0.03868  -0.09417 0.01175  26  SER A OG  
185  N  N   . ARG A 27  ? 0.53146 0.50078 0.27562 0.02344  -0.07960 -0.00593 27  ARG A N   
186  C  CA  . ARG A 27  ? 0.51829 0.49828 0.28331 0.02062  -0.08393 -0.01792 27  ARG A CA  
187  C  C   . ARG A 27  ? 0.50314 0.48228 0.29274 0.01526  -0.07621 -0.01833 27  ARG A C   
188  O  O   . ARG A 27  ? 0.51019 0.49362 0.31396 0.01103  -0.07514 -0.02766 27  ARG A O   
189  C  CB  . ARG A 27  ? 0.53506 0.52489 0.30748 0.02514  -0.09719 -0.02098 27  ARG A CB  
190  C  CG  . ARG A 27  ? 0.54221 0.53360 0.29037 0.03183  -0.10708 -0.02044 27  ARG A CG  
191  C  CD  . ARG A 27  ? 0.54863 0.55189 0.30799 0.03681  -0.12081 -0.02445 27  ARG A CD  
192  N  NE  . ARG A 27  ? 0.55655 0.56786 0.30120 0.04065  -0.13178 -0.03252 27  ARG A NE  
193  C  CZ  . ARG A 27  ? 0.57495 0.58451 0.29677 0.04883  -0.14068 -0.02710 27  ARG A CZ  
194  N  NH1 . ARG A 27  ? 0.58329 0.58192 0.29422 0.05395  -0.13968 -0.01331 27  ARG A NH1 
195  N  NH2 . ARG A 27  ? 0.58385 0.60213 0.29292 0.05212  -0.15114 -0.03579 27  ARG A NH2 
196  N  N   . ASP A 28  ? 0.48171 0.45457 0.27581 0.01547  -0.07099 -0.00835 28  ASP A N   
197  C  CA  . ASP A 28  ? 0.47180 0.44455 0.28837 0.01129  -0.06515 -0.00809 28  ASP A CA  
198  C  C   . ASP A 28  ? 0.46185 0.42887 0.27826 0.00704  -0.05434 -0.00877 28  ASP A C   
199  O  O   . ASP A 28  ? 0.47191 0.43462 0.27115 0.00721  -0.04975 -0.00766 28  ASP A O   
200  C  CB  . ASP A 28  ? 0.45553 0.42491 0.27783 0.01351  -0.06454 0.00167  28  ASP A CB  
201  C  CG  . ASP A 28  ? 0.46708 0.44386 0.29580 0.01801  -0.07503 0.00114  28  ASP A CG  
202  O  OD1 . ASP A 28  ? 0.47048 0.45624 0.30129 0.01879  -0.08293 -0.00719 28  ASP A OD1 
203  O  OD2 . ASP A 28  ? 0.46519 0.43942 0.29782 0.02090  -0.07551 0.00832  28  ASP A OD2 
204  N  N   . GLN A 29  ? 0.36949 0.33689 0.20541 0.00340  -0.05024 -0.01067 29  GLN A N   
205  C  CA  . GLN A 29  ? 0.36832 0.33087 0.20777 0.00033  -0.04086 -0.01098 29  GLN A CA  
206  C  C   . GLN A 29  ? 0.35640 0.31681 0.21146 -0.00117 -0.03687 -0.00526 29  GLN A C   
207  O  O   . GLN A 29  ? 0.35174 0.31570 0.22014 -0.00164 -0.04079 -0.00531 29  GLN A O   
208  C  CB  . GLN A 29  ? 0.37037 0.33458 0.21628 -0.00230 -0.04047 -0.02173 29  GLN A CB  
209  C  CG  . GLN A 29  ? 0.36993 0.32949 0.21606 -0.00378 -0.03157 -0.02322 29  GLN A CG  
210  C  CD  . GLN A 29  ? 0.37809 0.33766 0.23030 -0.00556 -0.03163 -0.03426 29  GLN A CD  
211  O  OE1 . GLN A 29  ? 0.38188 0.34131 0.22354 -0.00491 -0.02913 -0.04006 29  GLN A OE1 
212  N  NE2 . GLN A 29  ? 0.36690 0.32604 0.23603 -0.00803 -0.03401 -0.03738 29  GLN A NE2 
213  N  N   . VAL A 30  ? 0.35768 0.31329 0.21108 -0.00202 -0.02898 -0.00086 30  VAL A N   
214  C  CA  . VAL A 30  ? 0.34533 0.29900 0.21198 -0.00333 -0.02487 0.00387  30  VAL A CA  
215  C  C   . VAL A 30  ? 0.34563 0.29813 0.22257 -0.00555 -0.02064 -0.00116 30  VAL A C   
216  O  O   . VAL A 30  ? 0.34753 0.29886 0.21869 -0.00561 -0.01668 -0.00502 30  VAL A O   
217  C  CB  . VAL A 30  ? 0.34149 0.29103 0.20066 -0.00274 -0.01961 0.01177  30  VAL A CB  
218  C  CG1 . VAL A 30  ? 0.32963 0.27801 0.20208 -0.00423 -0.01500 0.01479  30  VAL A CG1 
219  C  CG2 . VAL A 30  ? 0.34281 0.29097 0.19346 -0.00002 -0.02423 0.01778  30  VAL A CG2 
220  N  N   . LEU A 31  ? 0.29904 0.25156 0.19078 -0.00710 -0.02133 -0.00115 31  LEU A N   
221  C  CA  . LEU A 31  ? 0.29455 0.24377 0.19595 -0.00863 -0.01788 -0.00447 31  LEU A CA  
222  C  C   . LEU A 31  ? 0.28387 0.23090 0.19138 -0.00841 -0.01335 0.00179  31  LEU A C   
223  O  O   . LEU A 31  ? 0.27653 0.22475 0.18889 -0.00873 -0.01438 0.00686  31  LEU A O   
224  C  CB  . LEU A 31  ? 0.29381 0.24311 0.20628 -0.01121 -0.02157 -0.00907 31  LEU A CB  
225  C  CG  . LEU A 31  ? 0.29291 0.23593 0.21506 -0.01275 -0.01837 -0.01128 31  LEU A CG  
226  C  CD1 . LEU A 31  ? 0.30025 0.23991 0.21757 -0.01132 -0.01612 -0.01765 31  LEU A CD1 
227  C  CD2 . LEU A 31  ? 0.29340 0.23559 0.22650 -0.01659 -0.02123 -0.01439 31  LEU A CD2 
228  N  N   . MET A 32  ? 0.31595 0.26075 0.22354 -0.00753 -0.00860 0.00068  32  MET A N   
229  C  CA  . MET A 32  ? 0.30568 0.24919 0.21987 -0.00695 -0.00501 0.00509  32  MET A CA  
230  C  C   . MET A 32  ? 0.31358 0.25324 0.23430 -0.00593 -0.00328 0.00092  32  MET A C   
231  O  O   . MET A 32  ? 0.31793 0.25732 0.23541 -0.00479 -0.00193 -0.00499 32  MET A O   
232  C  CB  . MET A 32  ? 0.29382 0.23974 0.20178 -0.00618 -0.00094 0.00851  32  MET A CB  
233  C  CG  . MET A 32  ? 0.28435 0.23125 0.18637 -0.00669 -0.00241 0.01408  32  MET A CG  
234  S  SD  . MET A 32  ? 0.28310 0.23054 0.17582 -0.00713 0.00317  0.01743  32  MET A SD  
235  C  CE  . MET A 32  ? 0.26826 0.21673 0.17242 -0.00735 0.00616  0.02060  32  MET A CE  
236  N  N   . VAL A 33  ? 0.27055 0.20678 0.19972 -0.00597 -0.00334 0.00396  33  VAL A N   
237  C  CA  . VAL A 33  ? 0.27420 0.20415 0.20937 -0.00455 -0.00277 0.00108  33  VAL A CA  
238  C  C   . VAL A 33  ? 0.26874 0.19839 0.20790 -0.00186 -0.00065 0.00527  33  VAL A C   
239  O  O   . VAL A 33  ? 0.26189 0.19282 0.20266 -0.00269 -0.00083 0.01111  33  VAL A O   
240  C  CB  . VAL A 33  ? 0.27709 0.20099 0.21775 -0.00746 -0.00533 0.00074  33  VAL A CB  
241  C  CG1 . VAL A 33  ? 0.28427 0.19866 0.22976 -0.00580 -0.00469 -0.00175 33  VAL A CG1 
242  C  CG2 . VAL A 33  ? 0.28216 0.20859 0.22022 -0.01026 -0.00834 -0.00423 33  VAL A CG2 
243  N  N   . GLU A 34  ? 0.33405 0.26287 0.27510 0.00175  0.00107  0.00158  34  GLU A N   
244  C  CA  . GLU A 34  ? 0.33607 0.26407 0.28226 0.00535  0.00169  0.00429  34  GLU A CA  
245  C  C   . GLU A 34  ? 0.33860 0.25552 0.28867 0.00629  -0.00047 0.00522  34  GLU A C   
246  O  O   . GLU A 34  ? 0.34436 0.25506 0.29647 0.00874  -0.00082 0.00021  34  GLU A O   
247  C  CB  . GLU A 34  ? 0.34139 0.27498 0.28923 0.00925  0.00429  -0.00068 34  GLU A CB  
248  C  CG  . GLU A 34  ? 0.33992 0.28329 0.28318 0.00713  0.00761  -0.00098 34  GLU A CG  
249  C  CD  . GLU A 34  ? 0.35350 0.30455 0.30045 0.01014  0.01123  -0.00559 34  GLU A CD  
250  O  OE1 . GLU A 34  ? 0.36108 0.31043 0.31399 0.01478  0.01071  -0.01009 34  GLU A OE1 
251  O  OE2 . GLU A 34  ? 0.34155 0.30028 0.28599 0.00782  0.01479  -0.00490 34  GLU A OE2 
252  N  N   . SER A 35  ? 0.29270 0.20643 0.24336 0.00414  -0.00150 0.01159  35  SER A N   
253  C  CA  . SER A 35  ? 0.28976 0.19200 0.24237 0.00278  -0.00267 0.01366  35  SER A CA  
254  C  C   . SER A 35  ? 0.29455 0.19068 0.24819 0.00725  -0.00328 0.01826  35  SER A C   
255  O  O   . SER A 35  ? 0.28674 0.18825 0.23929 0.00840  -0.00324 0.02299  35  SER A O   
256  C  CB  . SER A 35  ? 0.28318 0.18641 0.23549 -0.00306 -0.00275 0.01746  35  SER A CB  
257  O  OG  . SER A 35  ? 0.28636 0.17912 0.24031 -0.00501 -0.00258 0.02119  35  SER A OG  
258  N  N   . ARG A 36  ? 0.37981 0.26403 0.33506 0.01006  -0.00423 0.01670  36  ARG A N   
259  C  CA  . ARG A 36  ? 0.37587 0.25194 0.33062 0.01513  -0.00570 0.02172  36  ARG A CA  
260  C  C   . ARG A 36  ? 0.37974 0.24719 0.33103 0.01111  -0.00524 0.02966  36  ARG A C   
261  O  O   . ARG A 36  ? 0.37947 0.24282 0.32751 0.01476  -0.00640 0.03565  36  ARG A O   
262  C  CB  . ARG A 36  ? 0.39946 0.26425 0.35683 0.02054  -0.00710 0.01736  36  ARG A CB  
263  C  CG  . ARG A 36  ? 0.39845 0.27296 0.35979 0.02647  -0.00725 0.01000  36  ARG A CG  
264  C  CD  . ARG A 36  ? 0.40943 0.27281 0.37430 0.03225  -0.00858 0.00446  36  ARG A CD  
265  N  NE  . ARG A 36  ? 0.41585 0.29057 0.38550 0.03764  -0.00787 -0.00362 36  ARG A NE  
266  C  CZ  . ARG A 36  ? 0.41658 0.29798 0.39042 0.04507  -0.00940 -0.00398 36  ARG A CZ  
267  N  NH1 . ARG A 36  ? 0.41152 0.28874 0.38410 0.04880  -0.01259 0.00342  36  ARG A NH1 
268  N  NH2 . ARG A 36  ? 0.42505 0.31853 0.40442 0.04877  -0.00765 -0.01233 36  ARG A NH2 
269  N  N   . VAL A 37  ? 0.34536 0.21073 0.29718 0.00372  -0.00353 0.02950  37  VAL A N   
270  C  CA  . VAL A 37  ? 0.33944 0.20085 0.28873 -0.00130 -0.00178 0.03652  37  VAL A CA  
271  C  C   . VAL A 37  ? 0.33549 0.20911 0.28213 -0.00062 -0.00148 0.04064  37  VAL A C   
272  O  O   . VAL A 37  ? 0.32981 0.20007 0.27185 0.00056  -0.00117 0.04717  37  VAL A O   
273  C  CB  . VAL A 37  ? 0.34579 0.20704 0.29883 -0.00958 -0.00001 0.03373  37  VAL A CB  
274  C  CG1 . VAL A 37  ? 0.33352 0.19559 0.28539 -0.01521 0.00274  0.04000  37  VAL A CG1 
275  C  CG2 . VAL A 37  ? 0.35514 0.20190 0.31079 -0.01112 -0.00009 0.02994  37  VAL A CG2 
276  N  N   . GLU A 38  ? 0.37281 0.25997 0.32145 -0.00129 -0.00157 0.03681  38  GLU A N   
277  C  CA  . GLU A 38  ? 0.36427 0.26228 0.31113 -0.00070 -0.00128 0.03969  38  GLU A CA  
278  C  C   . GLU A 38  ? 0.36996 0.26994 0.31516 0.00590  -0.00301 0.04093  38  GLU A C   
279  O  O   . GLU A 38  ? 0.36535 0.26971 0.30782 0.00679  -0.00315 0.04480  38  GLU A O   
280  C  CB  . GLU A 38  ? 0.36181 0.27119 0.31058 -0.00275 -0.00105 0.03554  38  GLU A CB  
281  C  CG  . GLU A 38  ? 0.36269 0.27276 0.31377 -0.00839 -0.00057 0.03352  38  GLU A CG  
282  C  CD  . GLU A 38  ? 0.36709 0.27531 0.31895 -0.01268 0.00117  0.03796  38  GLU A CD  
283  O  OE1 . GLU A 38  ? 0.36240 0.27556 0.31236 -0.01217 0.00210  0.04180  38  GLU A OE1 
284  O  OE2 . GLU A 38  ? 0.37335 0.27550 0.32803 -0.01695 0.00199  0.03707  38  GLU A OE2 
285  N  N   . ALA A 39  ? 0.36989 0.26772 0.31734 0.01073  -0.00451 0.03686  39  ALA A N   
286  C  CA  . ALA A 39  ? 0.36823 0.27010 0.31631 0.01745  -0.00666 0.03673  39  ALA A CA  
287  C  C   . ALA A 39  ? 0.38345 0.27516 0.32714 0.02152  -0.00895 0.04268  39  ALA A C   
288  O  O   . ALA A 39  ? 0.38411 0.28075 0.32721 0.02689  -0.01154 0.04378  39  ALA A O   
289  C  CB  . ALA A 39  ? 0.38351 0.28755 0.33657 0.02169  -0.00719 0.02969  39  ALA A CB  
290  N  N   . THR A 40  ? 0.30434 0.18184 0.24461 0.01896  -0.00813 0.04652  40  THR A N   
291  C  CA  . THR A 40  ? 0.31989 0.18466 0.25362 0.02254  -0.00989 0.05338  40  THR A CA  
292  C  C   . THR A 40  ? 0.32460 0.18388 0.25166 0.01626  -0.00688 0.06047  40  THR A C   
293  O  O   . THR A 40  ? 0.34019 0.18731 0.25944 0.01828  -0.00753 0.06733  40  THR A O   
294  C  CB  . THR A 40  ? 0.33598 0.18462 0.27066 0.02605  -0.01127 0.05231  40  THR A CB  
295  O  OG1 . THR A 40  ? 0.33861 0.17996 0.27546 0.01861  -0.00799 0.05042  40  THR A OG1 
296  C  CG2 . THR A 40  ? 0.33268 0.18771 0.27447 0.03311  -0.01391 0.04460  40  THR A CG2 
297  N  N   . ALA A 41  ? 0.36958 0.23725 0.29919 0.00895  -0.00351 0.05905  41  ALA A N   
298  C  CA  . ALA A 41  ? 0.37223 0.23863 0.29679 0.00332  -0.00014 0.06480  41  ALA A CA  
299  C  C   . ALA A 41  ? 0.37202 0.24076 0.28835 0.00769  -0.00170 0.07011  41  ALA A C   
300  O  O   . ALA A 41  ? 0.38462 0.24367 0.29216 0.00682  -0.00025 0.07711  41  ALA A O   
301  C  CB  . ALA A 41  ? 0.35537 0.23454 0.28552 -0.00291 0.00250  0.06113  41  ALA A CB  
302  N  N   . TRP A 42  ? 0.39300 0.27463 0.31164 0.01206  -0.00449 0.06665  42  TRP A N   
303  C  CA  . TRP A 42  ? 0.39920 0.28320 0.31194 0.01874  -0.00825 0.06928  42  TRP A CA  
304  C  C   . TRP A 42  ? 0.40110 0.28919 0.32016 0.02582  -0.01263 0.06396  42  TRP A C   
305  O  O   . TRP A 42  ? 0.39651 0.29037 0.32403 0.02451  -0.01175 0.05769  42  TRP A O   
306  C  CB  . TRP A 42  ? 0.39339 0.29101 0.30461 0.01712  -0.00753 0.06873  42  TRP A CB  
307  C  CG  . TRP A 42  ? 0.39135 0.28733 0.29708 0.01082  -0.00291 0.07300  42  TRP A CG  
308  C  CD1 . TRP A 42  ? 0.39617 0.28675 0.29055 0.01103  -0.00197 0.07950  42  TRP A CD1 
309  C  CD2 . TRP A 42  ? 0.38012 0.28090 0.29152 0.00358  0.00156  0.07070  42  TRP A CD2 
310  N  NE1 . TRP A 42  ? 0.39136 0.28375 0.28480 0.00381  0.00368  0.08098  42  TRP A NE1 
311  C  CE2 . TRP A 42  ? 0.38200 0.28106 0.28671 -0.00054 0.00554  0.07540  42  TRP A CE2 
312  C  CE3 . TRP A 42  ? 0.37325 0.27996 0.29425 0.00056  0.00237  0.06506  42  TRP A CE3 
313  C  CZ2 . TRP A 42  ? 0.38268 0.28705 0.29225 -0.00734 0.01021  0.07386  42  TRP A CZ2 
314  C  CZ3 . TRP A 42  ? 0.36028 0.27130 0.28490 -0.00563 0.00607  0.06410  42  TRP A CZ3 
315  C  CH2 . TRP A 42  ? 0.37094 0.28139 0.29097 -0.00943 0.00991  0.06810  42  TRP A CH2 
316  N  N   . LYS A 43  ? 0.41019 0.29588 0.32489 0.03359  -0.01738 0.06626  43  LYS A N   
317  C  CA  . LYS A 43  ? 0.41959 0.31122 0.34180 0.04106  -0.02172 0.06054  43  LYS A CA  
318  C  C   . LYS A 43  ? 0.40737 0.31815 0.33540 0.04086  -0.02235 0.05516  43  LYS A C   
319  O  O   . LYS A 43  ? 0.41000 0.32807 0.33670 0.04605  -0.02659 0.05495  43  LYS A O   
320  C  CB  . LYS A 43  ? 0.43935 0.32104 0.35546 0.05021  -0.02734 0.06481  43  LYS A CB  
321  C  CG  . LYS A 43  ? 0.45442 0.32023 0.37212 0.05318  -0.02786 0.06499  43  LYS A CG  
322  C  CD  . LYS A 43  ? 0.47918 0.33023 0.38748 0.06156  -0.03302 0.07182  43  LYS A CD  
323  C  CE  . LYS A 43  ? 0.50198 0.34007 0.41526 0.06703  -0.03487 0.06934  43  LYS A CE  
324  N  NZ  . LYS A 43  ? 0.50512 0.35744 0.42907 0.07596  -0.03987 0.06138  43  LYS A NZ  
325  N  N   . HIS A 44  ? 0.31754 0.23601 0.25193 0.03463  -0.01821 0.05064  44  HIS A N   
326  C  CA  . HIS A 44  ? 0.31687 0.25068 0.25578 0.03230  -0.01738 0.04646  44  HIS A CA  
327  C  C   . HIS A 44  ? 0.32189 0.26672 0.26781 0.03845  -0.02120 0.04109  44  HIS A C   
328  O  O   . HIS A 44  ? 0.33114 0.27427 0.28180 0.04391  -0.02339 0.03832  44  HIS A O   
329  C  CB  . HIS A 44  ? 0.30598 0.24367 0.25004 0.02588  -0.01280 0.04270  44  HIS A CB  
330  C  CG  . HIS A 44  ? 0.30185 0.23104 0.24175 0.02012  -0.00959 0.04635  44  HIS A CG  
331  N  ND1 . HIS A 44  ? 0.29206 0.22256 0.22777 0.01582  -0.00766 0.04963  44  HIS A ND1 
332  C  CD2 . HIS A 44  ? 0.30041 0.22090 0.24090 0.01785  -0.00800 0.04623  44  HIS A CD2 
333  C  CE1 . HIS A 44  ? 0.29335 0.21723 0.22808 0.01117  -0.00499 0.05146  44  HIS A CE1 
334  N  NE2 . HIS A 44  ? 0.30106 0.21863 0.23854 0.01207  -0.00533 0.04942  44  HIS A NE2 
335  N  N   . HIS A 45  ? 0.26563 0.22235 0.21309 0.03754  -0.02200 0.03892  45  HIS A N   
336  C  CA  . HIS A 45  ? 0.26144 0.23210 0.21841 0.04119  -0.02456 0.03212  45  HIS A CA  
337  C  C   . HIS A 45  ? 0.25578 0.23027 0.22237 0.04021  -0.02141 0.02626  45  HIS A C   
338  O  O   . HIS A 45  ? 0.24979 0.22148 0.21610 0.03413  -0.01642 0.02610  45  HIS A O   
339  C  CB  . HIS A 45  ? 0.25281 0.23495 0.21159 0.03686  -0.02357 0.02943  45  HIS A CB  
340  C  CG  . HIS A 45  ? 0.25174 0.24846 0.21909 0.04080  -0.02751 0.02302  45  HIS A CG  
341  N  ND1 . HIS A 45  ? 0.24762 0.25397 0.22725 0.04204  -0.02672 0.01606  45  HIS A ND1 
342  C  CD2 . HIS A 45  ? 0.25483 0.25942 0.22085 0.04355  -0.03223 0.02175  45  HIS A CD2 
343  C  CE1 . HIS A 45  ? 0.24759 0.26772 0.23453 0.04515  -0.03077 0.01060  45  HIS A CE1 
344  N  NE2 . HIS A 45  ? 0.25202 0.27124 0.23066 0.04629  -0.03462 0.01383  45  HIS A NE2 
345  N  N   . LYS A 46  ? 0.27006 0.25148 0.24490 0.04668  -0.02451 0.02116  46  LYS A N   
346  C  CA  . LYS A 46  ? 0.27653 0.26307 0.26059 0.04610  -0.02095 0.01470  46  LYS A CA  
347  C  C   . LYS A 46  ? 0.26686 0.26288 0.25500 0.03788  -0.01501 0.01103  46  LYS A C   
348  O  O   . LYS A 46  ? 0.26931 0.26388 0.25842 0.03411  -0.01009 0.00895  46  LYS A O   
349  C  CB  . LYS A 46  ? 0.29013 0.28644 0.28459 0.05453  -0.02517 0.00853  46  LYS A CB  
350  C  CG  . LYS A 46  ? 0.30510 0.29061 0.29564 0.06417  -0.03164 0.01206  46  LYS A CG  
351  C  CD  . LYS A 46  ? 0.30712 0.30117 0.31016 0.07251  -0.03428 0.00430  46  LYS A CD  
352  C  CE  . LYS A 46  ? 0.31870 0.30516 0.31902 0.08406  -0.04278 0.00735  46  LYS A CE  
353  N  NZ  . LYS A 46  ? 0.31283 0.31191 0.31528 0.08873  -0.04935 0.00643  46  LYS A NZ  
354  N  N   . GLN A 47  ? 0.24040 0.24512 0.22998 0.03501  -0.01542 0.01028  47  GLN A N   
355  C  CA  . GLN A 47  ? 0.23258 0.24361 0.22513 0.02700  -0.00968 0.00760  47  GLN A CA  
356  C  C   . GLN A 47  ? 0.22789 0.22765 0.21105 0.02111  -0.00595 0.01300  47  GLN A C   
357  O  O   . GLN A 47  ? 0.22430 0.22502 0.20798 0.01560  -0.00082 0.01157  47  GLN A O   
358  C  CB  . GLN A 47  ? 0.22946 0.25079 0.22589 0.02525  -0.01134 0.00514  47  GLN A CB  
359  C  CG  . GLN A 47  ? 0.23734 0.27431 0.24656 0.02922  -0.01400 -0.00258 47  GLN A CG  
360  C  CD  . GLN A 47  ? 0.24271 0.29103 0.25764 0.02519  -0.01428 -0.00679 47  GLN A CD  
361  O  OE1 . GLN A 47  ? 0.23477 0.28001 0.24653 0.01779  -0.00996 -0.00545 47  GLN A OE1 
362  N  NE2 . GLN A 47  ? 0.24306 0.30445 0.26682 0.03034  -0.01979 -0.01238 47  GLN A NE2 
363  N  N   . LYS A 48  ? 0.30011 0.28948 0.27459 0.02220  -0.00836 0.01917  48  LYS A N   
364  C  CA  . LYS A 48  ? 0.28827 0.26868 0.25581 0.01713  -0.00528 0.02337  48  LYS A CA  
365  C  C   . LYS A 48  ? 0.29486 0.26950 0.26190 0.01679  -0.00310 0.02253  48  LYS A C   
366  O  O   . LYS A 48  ? 0.28154 0.25364 0.24573 0.01212  0.00018  0.02304  48  LYS A O   
367  C  CB  . LYS A 48  ? 0.28097 0.25337 0.24072 0.01780  -0.00760 0.02940  48  LYS A CB  
368  C  CG  . LYS A 48  ? 0.27189 0.23848 0.22682 0.01244  -0.00463 0.03266  48  LYS A CG  
369  C  CD  . LYS A 48  ? 0.27868 0.23639 0.22713 0.01280  -0.00569 0.03808  48  LYS A CD  
370  C  CE  . LYS A 48  ? 0.27435 0.23426 0.21875 0.01439  -0.00773 0.04043  48  LYS A CE  
371  N  NZ  . LYS A 48  ? 0.27258 0.22391 0.20964 0.01369  -0.00737 0.04610  48  LYS A NZ  
372  N  N   . LEU A 49  ? 0.23745 0.20962 0.20683 0.02218  -0.00531 0.02094  49  LEU A N   
373  C  CA  . LEU A 49  ? 0.24529 0.21279 0.21491 0.02214  -0.00323 0.01847  49  LEU A CA  
374  C  C   . LEU A 49  ? 0.24519 0.22200 0.21929 0.01937  0.00123  0.01281  49  LEU A C   
375  O  O   . LEU A 49  ? 0.24216 0.21597 0.21260 0.01588  0.00443  0.01199  49  LEU A O   
376  C  CB  . LEU A 49  ? 0.25726 0.21965 0.22929 0.02924  -0.00664 0.01724  49  LEU A CB  
377  C  CG  . LEU A 49  ? 0.26245 0.21297 0.22847 0.03211  -0.01056 0.02362  49  LEU A CG  
378  C  CD1 . LEU A 49  ? 0.27243 0.21748 0.24125 0.04019  -0.01426 0.02213  49  LEU A CD1 
379  C  CD2 . LEU A 49  ? 0.25891 0.19852 0.21843 0.02679  -0.00856 0.02763  49  LEU A CD2 
380  N  N   . VAL A 50  ? 0.24007 0.22861 0.22185 0.02064  0.00160  0.00867  50  VAL A N   
381  C  CA  . VAL A 50  ? 0.24325 0.24107 0.22942 0.01687  0.00707  0.00347  50  VAL A CA  
382  C  C   . VAL A 50  ? 0.22853 0.22390 0.20818 0.00948  0.01080  0.00682  50  VAL A C   
383  O  O   . VAL A 50  ? 0.23046 0.22520 0.20649 0.00568  0.01541  0.00570  50  VAL A O   
384  C  CB  . VAL A 50  ? 0.24581 0.25796 0.24346 0.01906  0.00671  -0.00214 50  VAL A CB  
385  C  CG1 . VAL A 50  ? 0.23673 0.25848 0.23881 0.01324  0.01379  -0.00699 50  VAL A CG1 
386  C  CG2 . VAL A 50  ? 0.25975 0.27460 0.26435 0.02765  0.00268  -0.00609 50  VAL A CG2 
387  N  N   . LEU A 51  ? 0.25974 0.25313 0.23699 0.00781  0.00868  0.01098  51  LEU A N   
388  C  CA  . LEU A 51  ? 0.24335 0.23367 0.21521 0.00181  0.01159  0.01402  51  LEU A CA  
389  C  C   . LEU A 51  ? 0.24488 0.22573 0.20798 0.00019  0.01232  0.01736  51  LEU A C   
390  O  O   . LEU A 51  ? 0.24171 0.22142 0.20046 -0.00354 0.01609  0.01733  51  LEU A O   
391  C  CB  . LEU A 51  ? 0.23826 0.22791 0.20953 0.00146  0.00868  0.01703  51  LEU A CB  
392  C  CG  . LEU A 51  ? 0.23176 0.21652 0.19772 -0.00344 0.01071  0.02033  51  LEU A CG  
393  C  CD1 . LEU A 51  ? 0.22660 0.21401 0.19363 -0.00838 0.01598  0.01818  51  LEU A CD1 
394  C  CD2 . LEU A 51  ? 0.23083 0.21650 0.19744 -0.00320 0.00807  0.02159  51  LEU A CD2 
395  N  N   . VAL A 52  ? 0.31746 0.29145 0.27759 0.00279  0.00871  0.02021  52  VAL A N   
396  C  CA  . VAL A 52  ? 0.31384 0.28029 0.26722 0.00096  0.00865  0.02265  52  VAL A CA  
397  C  C   . VAL A 52  ? 0.32154 0.28793 0.27297 0.00084  0.01100  0.01889  52  VAL A C   
398  O  O   . VAL A 52  ? 0.31785 0.28259 0.26314 -0.00218 0.01302  0.01939  52  VAL A O   
399  C  CB  . VAL A 52  ? 0.30985 0.26972 0.26213 0.00291  0.00505  0.02569  52  VAL A CB  
400  C  CG1 . VAL A 52  ? 0.30960 0.26362 0.25720 0.00076  0.00474  0.02669  52  VAL A CG1 
401  C  CG2 . VAL A 52  ? 0.30058 0.26104 0.25296 0.00259  0.00355  0.02928  52  VAL A CG2 
402  N  N   . TRP A 53  ? 0.26626 0.23445 0.22233 0.00461  0.01065  0.01484  53  TRP A N   
403  C  CA  . TRP A 53  ? 0.27585 0.24352 0.22987 0.00501  0.01275  0.01035  53  TRP A CA  
404  C  C   . TRP A 53  ? 0.27474 0.24930 0.22707 0.00183  0.01822  0.00754  53  TRP A C   
405  O  O   . TRP A 53  ? 0.28322 0.25585 0.22824 -0.00021 0.02049  0.00630  53  TRP A O   
406  C  CB  . TRP A 53  ? 0.28850 0.25592 0.24881 0.01058  0.01101  0.00618  53  TRP A CB  
407  C  CG  . TRP A 53  ? 0.30344 0.26039 0.26224 0.01251  0.00684  0.00891  53  TRP A CG  
408  C  CD1 . TRP A 53  ? 0.29371 0.24349 0.24682 0.00926  0.00564  0.01198  53  TRP A CD1 
409  C  CD2 . TRP A 53  ? 0.30463 0.25675 0.26779 0.01789  0.00348  0.00897  53  TRP A CD2 
410  N  NE1 . TRP A 53  ? 0.29297 0.23389 0.24716 0.01120  0.00262  0.01374  53  TRP A NE1 
411  C  CE2 . TRP A 53  ? 0.31489 0.25577 0.27414 0.01664  0.00124  0.01252  53  TRP A CE2 
412  C  CE3 . TRP A 53  ? 0.32049 0.27664 0.29059 0.02387  0.00194  0.00633  53  TRP A CE3 
413  C  CZ2 . TRP A 53  ? 0.31635 0.24784 0.27692 0.02059  -0.00181 0.01440  53  TRP A CZ2 
414  C  CZ3 . TRP A 53  ? 0.32618 0.27316 0.29722 0.02902  -0.00213 0.00825  53  TRP A CZ3 
415  C  CH2 . TRP A 53  ? 0.32392 0.25766 0.28948 0.02709  -0.00364 0.01269  53  TRP A CH2 
416  N  N   . SER A 54  ? 0.31165 0.29432 0.27021 0.00100  0.02056  0.00634  54  SER A N   
417  C  CA  . SER A 54  ? 0.31325 0.30159 0.26999 -0.00353 0.02686  0.00442  54  SER A CA  
418  C  C   . SER A 54  ? 0.30194 0.28336 0.24783 -0.00830 0.02804  0.01001  54  SER A C   
419  O  O   . SER A 54  ? 0.31062 0.29109 0.24846 -0.01142 0.03238  0.00978  54  SER A O   
420  C  CB  . SER A 54  ? 0.30788 0.30648 0.27505 -0.00443 0.02893  0.00176  54  SER A CB  
421  O  OG  . SER A 54  ? 0.30987 0.31212 0.27478 -0.01052 0.03572  0.00116  54  SER A OG  
422  N  N   . ALA A 55  ? 0.25804 0.23438 0.20297 -0.00848 0.02413  0.01504  55  ALA A N   
423  C  CA  . ALA A 55  ? 0.24576 0.21544 0.18165 -0.01182 0.02445  0.02015  55  ALA A CA  
424  C  C   . ALA A 55  ? 0.25591 0.21945 0.18236 -0.01101 0.02234  0.02134  55  ALA A C   
425  O  O   . ALA A 55  ? 0.25832 0.21793 0.17492 -0.01336 0.02404  0.02378  55  ALA A O   
426  C  CB  . ALA A 55  ? 0.23896 0.20618 0.17778 -0.01156 0.02091  0.02392  55  ALA A CB  
427  N  N   . MET A 56  ? 0.28145 0.24359 0.21036 -0.00778 0.01842  0.01965  56  MET A N   
428  C  CA  . MET A 56  ? 0.28970 0.24737 0.21108 -0.00741 0.01617  0.01922  56  MET A CA  
429  C  C   . MET A 56  ? 0.29824 0.25780 0.21265 -0.00830 0.02015  0.01536  56  MET A C   
430  O  O   . MET A 56  ? 0.30600 0.26236 0.20964 -0.00948 0.01975  0.01654  56  MET A O   
431  C  CB  . MET A 56  ? 0.28961 0.24480 0.21609 -0.00473 0.01202  0.01738  56  MET A CB  
432  C  CG  . MET A 56  ? 0.28060 0.23409 0.21315 -0.00399 0.00897  0.02102  56  MET A CG  
433  S  SD  . MET A 56  ? 0.29484 0.24355 0.23259 -0.00159 0.00570  0.01933  56  MET A SD  
434  C  CE  . MET A 56  ? 0.30169 0.24725 0.23370 -0.00294 0.00417  0.01579  56  MET A CE  
435  N  N   . ARG A 57  ? 0.29985 0.26524 0.21998 -0.00737 0.02390  0.01040  57  ARG A N   
436  C  CA  . ARG A 57  ? 0.31165 0.28012 0.22553 -0.00826 0.02867  0.00577  57  ARG A CA  
437  C  C   . ARG A 57  ? 0.31069 0.27867 0.21429 -0.01278 0.03362  0.00939  57  ARG A C   
438  O  O   . ARG A 57  ? 0.32018 0.28618 0.21135 -0.01402 0.03556  0.00888  57  ARG A O   
439  C  CB  . ARG A 57  ? 0.31107 0.28753 0.23553 -0.00597 0.03198  -0.00081 57  ARG A CB  
440  C  CG  . ARG A 57  ? 0.32804 0.30232 0.25988 -0.00086 0.02734  -0.00462 57  ARG A CG  
441  C  CD  . ARG A 57  ? 0.33346 0.31555 0.27659 0.00282  0.02968  -0.01106 57  ARG A CD  
442  N  NE  . ARG A 57  ? 0.34868 0.32584 0.29775 0.00824  0.02491  -0.01388 57  ARG A NE  
443  C  CZ  . ARG A 57  ? 0.36289 0.34433 0.32127 0.01333  0.02535  -0.02016 57  ARG A CZ  
444  N  NH1 . ARG A 57  ? 0.34860 0.34174 0.31302 0.01365  0.03051  -0.02524 57  ARG A NH1 
445  N  NH2 . ARG A 57  ? 0.36384 0.33748 0.32608 0.01823  0.02062  -0.02153 57  ARG A NH2 
446  N  N   . GLN A 58  ? 0.30944 0.27830 0.21714 -0.01538 0.03567  0.01313  58  GLN A N   
447  C  CA  . GLN A 58  ? 0.31911 0.28476 0.21678 -0.02014 0.04059  0.01743  58  GLN A CA  
448  C  C   . GLN A 58  ? 0.31374 0.26944 0.19925 -0.01984 0.03597  0.02382  58  GLN A C   
449  O  O   . GLN A 58  ? 0.32360 0.27437 0.19487 -0.02198 0.03856  0.02689  58  GLN A O   
450  C  CB  . GLN A 58  ? 0.30200 0.27081 0.20885 -0.02335 0.04391  0.01870  58  GLN A CB  
451  C  CG  . GLN A 58  ? 0.30531 0.28604 0.22559 -0.02331 0.04794  0.01174  58  GLN A CG  
452  C  CD  . GLN A 58  ? 0.30406 0.28922 0.23447 -0.02672 0.05042  0.01194  58  GLN A CD  
453  O  OE1 . GLN A 58  ? 0.30091 0.28379 0.22692 -0.03259 0.05619  0.01442  58  GLN A OE1 
454  N  NE2 . GLN A 58  ? 0.29449 0.28544 0.23798 -0.02321 0.04601  0.00928  58  GLN A NE2 
455  N  N   . PHE A 59  ? 0.30679 0.25975 0.19747 -0.01696 0.02913  0.02585  59  PHE A N   
456  C  CA  . PHE A 59  ? 0.30735 0.25296 0.18905 -0.01578 0.02399  0.03074  59  PHE A CA  
457  C  C   . PHE A 59  ? 0.31828 0.26276 0.18900 -0.01425 0.02173  0.02864  59  PHE A C   
458  O  O   . PHE A 59  ? 0.32613 0.26507 0.18412 -0.01397 0.01963  0.03253  59  PHE A O   
459  C  CB  . PHE A 59  ? 0.29404 0.23939 0.18544 -0.01327 0.01799  0.03184  59  PHE A CB  
460  C  CG  . PHE A 59  ? 0.29995 0.23983 0.18535 -0.01170 0.01269  0.03612  59  PHE A CG  
461  C  CD1 . PHE A 59  ? 0.30124 0.23499 0.18029 -0.01261 0.01346  0.04149  59  PHE A CD1 
462  C  CD2 . PHE A 59  ? 0.29844 0.23931 0.18535 -0.00924 0.00687  0.03435  59  PHE A CD2 
463  C  CE1 . PHE A 59  ? 0.30790 0.23701 0.18226 -0.00996 0.00793  0.04502  59  PHE A CE1 
464  C  CE2 . PHE A 59  ? 0.30858 0.24660 0.19184 -0.00733 0.00162  0.03732  59  PHE A CE2 
465  C  CZ  . PHE A 59  ? 0.30472 0.23708 0.18170 -0.00712 0.00185  0.04267  59  PHE A CZ  
466  N  N   . ALA A 60  ? 0.29390 0.24322 0.16907 -0.01283 0.02169  0.02218  60  ALA A N   
467  C  CA  . ALA A 60  ? 0.30429 0.25323 0.16931 -0.01165 0.01983  0.01856  60  ALA A CA  
468  C  C   . ALA A 60  ? 0.31985 0.26817 0.16984 -0.01400 0.02577  0.01912  60  ALA A C   
469  O  O   . ALA A 60  ? 0.33276 0.27744 0.16790 -0.01341 0.02333  0.02063  60  ALA A O   
470  C  CB  . ALA A 60  ? 0.29973 0.25274 0.17377 -0.00969 0.01910  0.01088  60  ALA A CB  
471  N  N   . GLU A 61  ? 0.46301 0.41536 0.31635 -0.01677 0.03367  0.01779  61  GLU A N   
472  C  CA  . GLU A 61  ? 0.46845 0.42013 0.30736 -0.02019 0.04095  0.01887  61  GLU A CA  
473  C  C   . GLU A 61  ? 0.47372 0.41576 0.29936 -0.02210 0.04050  0.02813  61  GLU A C   
474  O  O   . GLU A 61  ? 0.48543 0.42295 0.29268 -0.02343 0.04303  0.03085  61  GLU A O   
475  C  CB  . GLU A 61  ? 0.47002 0.42951 0.31841 -0.02344 0.04990  0.01516  61  GLU A CB  
476  C  CG  . GLU A 61  ? 0.49195 0.46071 0.34855 -0.02111 0.05199  0.00532  61  GLU A CG  
477  C  CD  . GLU A 61  ? 0.51386 0.48195 0.35589 -0.01974 0.05175  0.00119  61  GLU A CD  
478  O  OE1 . GLU A 61  ? 0.52142 0.49190 0.35188 -0.02281 0.05943  -0.00015 61  GLU A OE1 
479  O  OE2 . GLU A 61  ? 0.50231 0.46785 0.34451 -0.01596 0.04419  -0.00122 61  GLU A OE2 
480  N  N   A ARG A 62  ? 0.39445 0.33249 0.22818 -0.02189 0.03725  0.03309  62  ARG A N   
481  N  N   B ARG A 62  ? 0.39438 0.33251 0.22826 -0.02188 0.03725  0.03302  62  ARG A N   
482  C  CA  A ARG A 62  ? 0.39799 0.32532 0.22006 -0.02261 0.03588  0.04168  62  ARG A CA  
483  C  CA  B ARG A 62  ? 0.39765 0.32513 0.22021 -0.02256 0.03578  0.04159  62  ARG A CA  
484  C  C   A ARG A 62  ? 0.40765 0.33014 0.21726 -0.01815 0.02760  0.04387  62  ARG A C   
485  C  C   B ARG A 62  ? 0.40756 0.33016 0.21729 -0.01818 0.02768  0.04379  62  ARG A C   
486  O  O   A ARG A 62  ? 0.41870 0.33253 0.21078 -0.01808 0.02735  0.04991  62  ARG A O   
487  O  O   B ARG A 62  ? 0.41875 0.33276 0.21083 -0.01820 0.02761  0.04977  62  ARG A O   
488  C  CB  A ARG A 62  ? 0.38880 0.31377 0.22385 -0.02279 0.03395  0.04491  62  ARG A CB  
489  C  CB  B ARG A 62  ? 0.38830 0.31368 0.22420 -0.02251 0.03349  0.04462  62  ARG A CB  
490  C  CG  A ARG A 62  ? 0.38484 0.31293 0.22942 -0.02786 0.04189  0.04398  62  ARG A CG  
491  C  CG  B ARG A 62  ? 0.38346 0.31259 0.23013 -0.02727 0.04102  0.04330  62  ARG A CG  
492  C  CD  A ARG A 62  ? 0.38211 0.30395 0.23276 -0.02875 0.04047  0.04864  62  ARG A CD  
493  C  CD  B ARG A 62  ? 0.37494 0.30344 0.23517 -0.02656 0.03771  0.04465  62  ARG A CD  
494  N  NE  A ARG A 62  ? 0.36755 0.29349 0.23188 -0.02477 0.03366  0.04653  62  ARG A NE  
495  N  NE  B ARG A 62  ? 0.37715 0.29381 0.22925 -0.02713 0.03657  0.05188  62  ARG A NE  
496  C  CZ  A ARG A 62  ? 0.35368 0.28908 0.23296 -0.02443 0.03385  0.04117  62  ARG A CZ  
497  C  CZ  B ARG A 62  ? 0.37352 0.28460 0.22305 -0.02259 0.02903  0.05525  62  ARG A CZ  
498  N  NH1 A ARG A 62  ? 0.35716 0.30037 0.24203 -0.02718 0.03981  0.03647  62  ARG A NH1 
499  N  NH1 B ARG A 62  ? 0.37146 0.28832 0.22707 -0.01817 0.02240  0.05208  62  ARG A NH1 
500  N  NH2 A ARG A 62  ? 0.34221 0.27950 0.23087 -0.02104 0.02795  0.04051  62  ARG A NH2 
501  N  NH2 B ARG A 62  ? 0.37768 0.27698 0.21906 -0.02253 0.02830  0.06172  62  ARG A NH2 
502  N  N   . LEU A 63  ? 0.38352 0.31131 0.20187 -0.01444 0.02061  0.03901  63  LEU A N   
503  C  CA  . LEU A 63  ? 0.39206 0.31778 0.20106 -0.01042 0.01225  0.03944  63  LEU A CA  
504  C  C   . LEU A 63  ? 0.40779 0.33368 0.19880 -0.01050 0.01380  0.03703  63  LEU A C   
505  O  O   . LEU A 63  ? 0.42596 0.34655 0.20053 -0.00813 0.00930  0.04090  63  LEU A O   
506  C  CB  . LEU A 63  ? 0.38904 0.32105 0.21318 -0.00787 0.00569  0.03387  63  LEU A CB  
507  C  CG  . LEU A 63  ? 0.38422 0.31623 0.22361 -0.00699 0.00260  0.03634  63  LEU A CG  
508  C  CD1 . LEU A 63  ? 0.37023 0.30823 0.22314 -0.00574 -0.00195 0.03055  63  LEU A CD1 
509  C  CD2 . LEU A 63  ? 0.38245 0.30838 0.21543 -0.00436 -0.00251 0.04278  63  LEU A CD2 
510  N  N   . ARG A 64  ? 0.49015 0.42239 0.28368 -0.01266 0.01988  0.03032  64  ARG A N   
511  C  CA  . ARG A 64  ? 0.50213 0.43562 0.27854 -0.01287 0.02223  0.02674  64  ARG A CA  
512  C  C   . ARG A 64  ? 0.51192 0.43759 0.26751 -0.01541 0.02781  0.03444  64  ARG A C   
513  O  O   . ARG A 64  ? 0.52915 0.45155 0.26429 -0.01391 0.02567  0.03569  64  ARG A O   
514  C  CB  . ARG A 64  ? 0.50117 0.44320 0.28634 -0.01448 0.02872  0.01761  64  ARG A CB  
515  C  CG  . ARG A 64  ? 0.50523 0.45247 0.30309 -0.01143 0.02267  0.00908  64  ARG A CG  
516  C  CD  . ARG A 64  ? 0.50629 0.46032 0.31778 -0.01212 0.02874  0.00138  64  ARG A CD  
517  N  NE  . ARG A 64  ? 0.50735 0.46351 0.33115 -0.00930 0.02315  -0.00590 64  ARG A NE  
518  C  CZ  . ARG A 64  ? 0.50300 0.46213 0.34404 -0.00837 0.02469  -0.01013 64  ARG A CZ  
519  N  NH1 . ARG A 64  ? 0.49697 0.45944 0.34639 -0.00963 0.03098  -0.00872 64  ARG A NH1 
520  N  NH2 . ARG A 64  ? 0.51175 0.47017 0.36181 -0.00610 0.01956  -0.01597 64  ARG A NH2 
521  N  N   . ALA A 65  ? 0.53806 0.46013 0.29790 -0.01947 0.03496  0.03971  65  ALA A N   
522  C  CA  . ALA A 65  ? 0.54596 0.45825 0.28630 -0.02283 0.04103  0.04800  65  ALA A CA  
523  C  C   . ALA A 65  ? 0.55916 0.45981 0.28495 -0.01868 0.03252  0.05660  65  ALA A C   
524  O  O   . ALA A 65  ? 0.57966 0.47093 0.28235 -0.01933 0.03466  0.06316  65  ALA A O   
525  C  CB  . ALA A 65  ? 0.52940 0.44018 0.28040 -0.02860 0.04991  0.05106  65  ALA A CB  
526  N  N   . ARG A 66  ? 0.61500 0.51614 0.35356 -0.01412 0.02292  0.05666  66  ARG A N   
527  C  CA  . ARG A 66  ? 0.61599 0.50830 0.34431 -0.00886 0.01360  0.06340  66  ARG A CA  
528  C  C   . ARG A 66  ? 0.63460 0.53108 0.35232 -0.00363 0.00443  0.05947  66  ARG A C   
529  O  O   . ARG A 66  ? 0.64727 0.53886 0.35790 0.00183  -0.00487 0.06374  66  ARG A O   
530  C  CB  . ARG A 66  ? 0.60739 0.49992 0.35560 -0.00645 0.00803  0.06440  66  ARG A CB  
531  C  CG  . ARG A 66  ? 0.61123 0.49439 0.36297 -0.00972 0.01374  0.07122  66  ARG A CG  
532  C  CD  . ARG A 66  ? 0.59710 0.48341 0.37037 -0.00781 0.00938  0.06982  66  ARG A CD  
533  N  NE  . ARG A 66  ? 0.61022 0.49481 0.38296 -0.00093 -0.00151 0.07157  66  ARG A NE  
534  C  CZ  . ARG A 66  ? 0.59873 0.49101 0.38929 0.00192  -0.00736 0.06746  66  ARG A CZ  
535  N  NH1 . ARG A 66  ? 0.57298 0.47355 0.38156 -0.00113 -0.00389 0.06224  66  ARG A NH1 
536  N  NH2 . ARG A 66  ? 0.60917 0.50108 0.39923 0.00812  -0.01687 0.06860  66  ARG A NH2 
537  N  N   . GLY A 67  ? 0.50251 0.40833 0.21979 -0.00482 0.00642  0.05076  67  GLY A N   
538  C  CA  . GLY A 67  ? 0.50910 0.41958 0.21640 -0.00059 -0.00192 0.04551  67  GLY A CA  
539  C  C   . GLY A 67  ? 0.50300 0.42366 0.23060 0.00172  -0.00959 0.03665  67  GLY A C   
540  O  O   . GLY A 67  ? 0.50737 0.43274 0.22906 0.00491  -0.01732 0.03119  67  GLY A O   
541  N  N   . PHE A 68  ? 0.45495 0.37892 0.20565 -0.00006 -0.00768 0.03497  68  PHE A N   
542  C  CA  . PHE A 68  ? 0.44284 0.37502 0.21242 0.00121  -0.01374 0.02730  68  PHE A CA  
543  C  C   . PHE A 68  ? 0.44526 0.38396 0.21762 -0.00069 -0.01051 0.01723  68  PHE A C   
544  O  O   . PHE A 68  ? 0.44790 0.38682 0.21758 -0.00363 -0.00152 0.01577  68  PHE A O   
545  C  CB  . PHE A 68  ? 0.42575 0.35842 0.21671 -0.00011 -0.01206 0.02926  68  PHE A CB  
546  C  CG  . PHE A 68  ? 0.42717 0.35555 0.22053 0.00276  -0.01746 0.03629  68  PHE A CG  
547  C  CD1 . PHE A 68  ? 0.42853 0.34763 0.21221 0.00256  -0.01397 0.04508  68  PHE A CD1 
548  C  CD2 . PHE A 68  ? 0.41602 0.34959 0.22222 0.00544  -0.02556 0.03362  68  PHE A CD2 
549  C  CE1 . PHE A 68  ? 0.43020 0.34455 0.21666 0.00590  -0.01907 0.05089  68  PHE A CE1 
550  C  CE2 . PHE A 68  ? 0.41917 0.34998 0.22884 0.00867  -0.03031 0.03909  68  PHE A CE2 
551  C  CZ  . PHE A 68  ? 0.41759 0.33843 0.21728 0.00936  -0.02734 0.04764  68  PHE A CZ  
552  N  N   . ASN A 69  ? 0.50182 0.44609 0.28051 0.00097  -0.01782 0.00961  69  ASN A N   
553  C  CA  . ASN A 69  ? 0.50426 0.45352 0.29043 -0.00061 -0.01565 -0.00077 69  ASN A CA  
554  C  C   . ASN A 69  ? 0.48940 0.43992 0.29929 -0.00208 -0.01460 -0.00224 69  ASN A C   
555  O  O   . ASN A 69  ? 0.48832 0.44037 0.30974 -0.00141 -0.02094 -0.00229 69  ASN A O   
556  C  CB  . ASN A 69  ? 0.51428 0.46790 0.29468 0.00125  -0.02390 -0.00886 69  ASN A CB  
557  C  CG  . ASN A 69  ? 0.52689 0.48408 0.31752 -0.00039 -0.02234 -0.02025 69  ASN A CG  
558  O  OD1 . ASN A 69  ? 0.53430 0.49478 0.33354 -0.00030 -0.02911 -0.02722 69  ASN A OD1 
559  N  ND2 . ASN A 69  ? 0.53783 0.49434 0.32838 -0.00190 -0.01331 -0.02262 69  ASN A ND2 
560  N  N   . VAL A 70  ? 0.39350 0.34383 0.21045 -0.00395 -0.00659 -0.00342 70  VAL A N   
561  C  CA  . VAL A 70  ? 0.38003 0.33039 0.21680 -0.00482 -0.00510 -0.00317 70  VAL A CA  
562  C  C   . VAL A 70  ? 0.38542 0.33732 0.23098 -0.00495 -0.00379 -0.01253 70  VAL A C   
563  O  O   . VAL A 70  ? 0.38842 0.34180 0.22901 -0.00492 0.00169  -0.01728 70  VAL A O   
564  C  CB  . VAL A 70  ? 0.37288 0.32179 0.21260 -0.00611 0.00198  0.00316  70  VAL A CB  
565  C  CG1 . VAL A 70  ? 0.36164 0.31061 0.21995 -0.00631 0.00187  0.00420  70  VAL A CG1 
566  C  CG2 . VAL A 70  ? 0.37094 0.31606 0.19937 -0.00615 0.00152  0.01198  70  VAL A CG2 
567  N  N   . ARG A 71  ? 0.33647 0.28767 0.19529 -0.00518 -0.00846 -0.01532 71  ARG A N   
568  C  CA  . ARG A 71  ? 0.33458 0.28421 0.20410 -0.00525 -0.00728 -0.02281 71  ARG A CA  
569  C  C   . ARG A 71  ? 0.32124 0.26862 0.20382 -0.00511 -0.00366 -0.01832 71  ARG A C   
570  O  O   . ARG A 71  ? 0.31558 0.26123 0.20734 -0.00597 -0.00633 -0.01398 71  ARG A O   
571  C  CB  . ARG A 71  ? 0.33652 0.28537 0.21226 -0.00642 -0.01395 -0.02828 71  ARG A CB  
572  C  CG  . ARG A 71  ? 0.33721 0.28156 0.22386 -0.00681 -0.01300 -0.03574 71  ARG A CG  
573  C  CD  . ARG A 71  ? 0.34285 0.28613 0.23636 -0.00937 -0.01920 -0.04099 71  ARG A CD  
574  N  NE  . ARG A 71  ? 0.34286 0.27886 0.24773 -0.01033 -0.01808 -0.04662 71  ARG A NE  
575  C  CZ  . ARG A 71  ? 0.35344 0.28674 0.25710 -0.01007 -0.01832 -0.05686 71  ARG A CZ  
576  N  NH1 . ARG A 71  ? 0.36457 0.30309 0.25553 -0.00903 -0.01950 -0.06315 71  ARG A NH1 
577  N  NH2 . ARG A 71  ? 0.35580 0.28013 0.27041 -0.01073 -0.01734 -0.06090 71  ARG A NH2 
578  N  N   . TYR A 72  ? 0.31604 0.26443 0.19935 -0.00389 0.00241  -0.01967 72  TYR A N   
579  C  CA  . TYR A 72  ? 0.30505 0.25266 0.19977 -0.00298 0.00537  -0.01604 72  TYR A CA  
580  C  C   . TYR A 72  ? 0.30646 0.25068 0.21081 -0.00077 0.00577  -0.02258 72  TYR A C   
581  O  O   . TYR A 72  ? 0.31445 0.26044 0.21655 0.00098  0.00885  -0.02969 72  TYR A O   
582  C  CB  . TYR A 72  ? 0.30402 0.25630 0.19497 -0.00305 0.01156  -0.01306 72  TYR A CB  
583  C  CG  . TYR A 72  ? 0.29208 0.24492 0.19398 -0.00249 0.01307  -0.00819 72  TYR A CG  
584  C  CD1 . TYR A 72  ? 0.28906 0.24265 0.20147 0.00030  0.01481  -0.01178 72  TYR A CD1 
585  C  CD2 . TYR A 72  ? 0.28509 0.23762 0.18669 -0.00416 0.01215  -0.00045 72  TYR A CD2 
586  C  CE1 . TYR A 72  ? 0.27956 0.23436 0.20101 0.00131  0.01525  -0.00763 72  TYR A CE1 
587  C  CE2 . TYR A 72  ? 0.27527 0.22886 0.18615 -0.00366 0.01318  0.00316  72  TYR A CE2 
588  C  CZ  . TYR A 72  ? 0.27260 0.22769 0.19298 -0.00097 0.01452  -0.00038 72  TYR A CZ  
589  O  OH  . TYR A 72  ? 0.26423 0.22106 0.19286 0.00001  0.01467  0.00291  72  TYR A OH  
590  N  N   . VAL A 73  ? 0.32214 0.26095 0.23668 -0.00067 0.00295  -0.02012 73  VAL A N   
591  C  CA  . VAL A 73  ? 0.31815 0.25055 0.24147 0.00167  0.00263  -0.02484 73  VAL A CA  
592  C  C   . VAL A 73  ? 0.32089 0.25361 0.25173 0.00479  0.00500  -0.02090 73  VAL A C   
593  O  O   . VAL A 73  ? 0.31500 0.24607 0.24979 0.00407  0.00365  -0.01382 73  VAL A O   
594  C  CB  . VAL A 73  ? 0.32408 0.24875 0.25253 -0.00083 -0.00181 -0.02463 73  VAL A CB  
595  C  CG1 . VAL A 73  ? 0.32545 0.24073 0.26113 0.00142  -0.00196 -0.02990 73  VAL A CG1 
596  C  CG2 . VAL A 73  ? 0.32251 0.24979 0.24444 -0.00410 -0.00516 -0.02824 73  VAL A CG2 
597  N  N   . THR A 74  ? 0.40272 0.33866 0.33573 0.00851  0.00840  -0.02611 74  THR A N   
598  C  CA  . THR A 74  ? 0.40501 0.34341 0.34601 0.01227  0.01000  -0.02386 74  THR A CA  
599  C  C   . THR A 74  ? 0.41100 0.33914 0.36015 0.01604  0.00683  -0.02405 74  THR A C   
600  O  O   . THR A 74  ? 0.41315 0.33200 0.36247 0.01555  0.00458  -0.02738 74  THR A O   
601  C  CB  . THR A 74  ? 0.41273 0.36043 0.35445 0.01489  0.01506  -0.03018 74  THR A CB  
602  O  OG1 . THR A 74  ? 0.42522 0.36920 0.36971 0.01864  0.01514  -0.03916 74  THR A OG1 
603  C  CG2 . THR A 74  ? 0.40482 0.35996 0.33562 0.01055  0.01888  -0.03016 74  THR A CG2 
604  N  N   . LEU A 75  ? 0.56081 0.49011 0.51642 0.01981  0.00650  -0.02043 75  LEU A N   
605  C  CA  . LEU A 75  ? 0.57043 0.48874 0.53197 0.02427  0.00327  -0.01931 75  LEU A CA  
606  C  C   . LEU A 75  ? 0.58137 0.49674 0.54801 0.03041  0.00367  -0.02800 75  LEU A C   
607  O  O   . LEU A 75  ? 0.58995 0.49303 0.56048 0.03444  0.00073  -0.02768 75  LEU A O   
608  C  CB  . LEU A 75  ? 0.56904 0.48966 0.53431 0.02699  0.00178  -0.01238 75  LEU A CB  
609  C  CG  . LEU A 75  ? 0.56683 0.50222 0.53507 0.02830  0.00422  -0.01279 75  LEU A CG  
610  C  CD1 . LEU A 75  ? 0.57803 0.52097 0.55271 0.03366  0.00655  -0.02157 75  LEU A CD1 
611  C  CD2 . LEU A 75  ? 0.56538 0.50106 0.53629 0.03045  0.00137  -0.00594 75  LEU A CD2 
612  N  N   . GLU A 76  ? 0.53369 0.45939 0.50009 0.03133  0.00751  -0.03570 76  GLU A N   
613  C  CA  . GLU A 76  ? 0.53879 0.46260 0.50999 0.03703  0.00842  -0.04561 76  GLU A CA  
614  C  C   . GLU A 76  ? 0.54235 0.45862 0.50816 0.03412  0.00834  -0.05207 76  GLU A C   
615  O  O   . GLU A 76  ? 0.54986 0.46158 0.51950 0.03876  0.00859  -0.06088 76  GLU A O   
616  C  CB  . GLU A 76  ? 0.57208 0.51230 0.54660 0.03950  0.01354  -0.05194 76  GLU A CB  
617  C  CG  . GLU A 76  ? 0.57485 0.52371 0.54000 0.03387  0.01856  -0.05614 76  GLU A CG  
618  C  CD  . GLU A 76  ? 0.56916 0.53056 0.53096 0.02933  0.02243  -0.05094 76  GLU A CD  
619  O  OE1 . GLU A 76  ? 0.55641 0.51727 0.52020 0.02805  0.02001  -0.04245 76  GLU A OE1 
620  O  OE2 . GLU A 76  ? 0.57697 0.54812 0.53354 0.02679  0.02821  -0.05546 76  GLU A OE2 
621  N  N   . ASP A 77  ? 0.45579 0.37114 0.41346 0.02702  0.00762  -0.04866 77  ASP A N   
622  C  CA  . ASP A 77  ? 0.44777 0.35727 0.40045 0.02377  0.00657  -0.05511 77  ASP A CA  
623  C  C   . ASP A 77  ? 0.45773 0.35037 0.41649 0.02565  0.00310  -0.05702 77  ASP A C   
624  O  O   . ASP A 77  ? 0.45657 0.34026 0.41744 0.02354  0.00038  -0.04897 77  ASP A O   
625  C  CB  . ASP A 77  ? 0.45673 0.36901 0.40129 0.01652  0.00512  -0.04987 77  ASP A CB  
626  C  CG  . ASP A 77  ? 0.46623 0.37755 0.40418 0.01324  0.00398  -0.05777 77  ASP A CG  
627  O  OD1 . ASP A 77  ? 0.47448 0.37859 0.41544 0.01541  0.00343  -0.06660 77  ASP A OD1 
628  O  OD2 . ASP A 77  ? 0.46344 0.38103 0.39302 0.00883  0.00318  -0.05544 77  ASP A OD2 
629  N  N   . PRO A 78  ? 0.39229 0.27943 0.35364 0.02933  0.00349  -0.06748 78  PRO A N   
630  C  CA  . PRO A 78  ? 0.40366 0.27210 0.37090 0.03115  0.00042  -0.06918 78  PRO A CA  
631  C  C   . PRO A 78  ? 0.40440 0.26336 0.36923 0.02321  -0.00225 -0.06742 78  PRO A C   
632  O  O   . PRO A 78  ? 0.40909 0.25120 0.37864 0.02294  -0.00430 -0.06599 78  PRO A O   
633  C  CB  . PRO A 78  ? 0.40582 0.27284 0.37567 0.03655  0.00198  -0.08265 78  PRO A CB  
634  C  CG  . PRO A 78  ? 0.39533 0.27954 0.35735 0.03420  0.00565  -0.08857 78  PRO A CG  
635  C  CD  . PRO A 78  ? 0.39485 0.29197 0.35350 0.03191  0.00727  -0.07846 78  PRO A CD  
636  N  N   . ASP A 79  ? 0.39350 0.26247 0.35147 0.01684  -0.00232 -0.06760 79  ASP A N   
637  C  CA  . ASP A 79  ? 0.39315 0.25644 0.35057 0.00925  -0.00517 -0.06685 79  ASP A CA  
638  C  C   . ASP A 79  ? 0.38624 0.25350 0.34293 0.00474  -0.00601 -0.05504 79  ASP A C   
639  O  O   . ASP A 79  ? 0.38511 0.25030 0.34268 -0.00177 -0.00811 -0.05403 79  ASP A O   
640  C  CB  . ASP A 79  ? 0.39718 0.26885 0.34781 0.00584  -0.00599 -0.07643 79  ASP A CB  
641  C  CG  . ASP A 79  ? 0.42198 0.28977 0.37290 0.00985  -0.00496 -0.08953 79  ASP A CG  
642  O  OD1 . ASP A 79  ? 0.42573 0.27918 0.38266 0.00895  -0.00668 -0.09519 79  ASP A OD1 
643  O  OD2 . ASP A 79  ? 0.42466 0.30335 0.36991 0.01365  -0.00198 -0.09443 79  ASP A OD2 
644  N  N   . ASN A 80  ? 0.35150 0.22531 0.30748 0.00799  -0.00437 -0.04704 80  ASN A N   
645  C  CA  . ASN A 80  ? 0.33984 0.21651 0.29555 0.00448  -0.00493 -0.03627 80  ASN A CA  
646  C  C   . ASN A 80  ? 0.34623 0.20805 0.30732 0.00199  -0.00609 -0.03136 80  ASN A C   
647  O  O   . ASN A 80  ? 0.35432 0.20468 0.31873 0.00654  -0.00592 -0.02984 80  ASN A O   
648  C  CB  . ASN A 80  ? 0.32911 0.21411 0.28398 0.00898  -0.00301 -0.03013 80  ASN A CB  
649  C  CG  . ASN A 80  ? 0.31656 0.20740 0.26966 0.00540  -0.00329 -0.02059 80  ASN A CG  
650  O  OD1 . ASN A 80  ? 0.31627 0.20285 0.27054 0.00046  -0.00473 -0.01703 80  ASN A OD1 
651  N  ND2 . ASN A 80  ? 0.30681 0.20782 0.25788 0.00768  -0.00156 -0.01706 80  ASN A ND2 
652  N  N   . THR A 81  ? 0.35374 0.21572 0.31562 -0.00516 -0.00717 -0.02889 81  THR A N   
653  C  CA  . THR A 81  ? 0.35885 0.20727 0.32541 -0.00912 -0.00704 -0.02393 81  THR A CA  
654  C  C   . THR A 81  ? 0.35315 0.20039 0.31870 -0.00729 -0.00580 -0.01251 81  THR A C   
655  O  O   . THR A 81  ? 0.35402 0.18749 0.32129 -0.00854 -0.00504 -0.00727 81  THR A O   
656  C  CB  . THR A 81  ? 0.35890 0.21033 0.32837 -0.01781 -0.00811 -0.02602 81  THR A CB  
657  O  OG1 . THR A 81  ? 0.35516 0.22245 0.32178 -0.01933 -0.00869 -0.02220 81  THR A OG1 
658  C  CG2 . THR A 81  ? 0.36167 0.21283 0.33219 -0.01973 -0.01009 -0.03822 81  THR A CG2 
659  N  N   . GLY A 82  ? 0.35284 0.21346 0.31490 -0.00459 -0.00545 -0.00863 82  GLY A N   
660  C  CA  . GLY A 82  ? 0.35139 0.21243 0.31205 -0.00202 -0.00469 0.00068  82  GLY A CA  
661  C  C   . GLY A 82  ? 0.34322 0.21115 0.30311 -0.00733 -0.00398 0.00715  82  GLY A C   
662  O  O   . GLY A 82  ? 0.33159 0.20401 0.28926 -0.00508 -0.00342 0.01365  82  GLY A O   
663  N  N   . SER A 83  ? 0.33752 0.20732 0.29994 -0.01405 -0.00419 0.00471  83  SER A N   
664  C  CA  . SER A 83  ? 0.32479 0.20170 0.28830 -0.01896 -0.00341 0.00972  83  SER A CA  
665  C  C   . SER A 83  ? 0.32540 0.21656 0.28856 -0.02064 -0.00528 0.00555  83  SER A C   
666  O  O   . SER A 83  ? 0.32913 0.22284 0.29110 -0.01999 -0.00715 -0.00168 83  SER A O   
667  C  CB  . SER A 83  ? 0.33028 0.19793 0.29868 -0.02586 -0.00183 0.01099  83  SER A CB  
668  O  OG  . SER A 83  ? 0.33777 0.20379 0.31072 -0.02996 -0.00330 0.00249  83  SER A OG  
669  N  N   . ILE A 84  ? 0.34197 0.24201 0.30545 -0.02239 -0.00493 0.01018  84  ILE A N   
670  C  CA  . ILE A 84  ? 0.34132 0.25366 0.30446 -0.02353 -0.00732 0.00725  84  ILE A CA  
671  C  C   . ILE A 84  ? 0.35454 0.26788 0.32344 -0.02881 -0.00946 0.00077  84  ILE A C   
672  O  O   . ILE A 84  ? 0.35439 0.27354 0.32121 -0.02833 -0.01275 -0.00539 84  ILE A O   
673  C  CB  . ILE A 84  ? 0.33470 0.25510 0.29817 -0.02371 -0.00650 0.01330  84  ILE A CB  
674  C  CG1 . ILE A 84  ? 0.32244 0.24229 0.28085 -0.01893 -0.00471 0.01863  84  ILE A CG1 
675  C  CG2 . ILE A 84  ? 0.33365 0.26530 0.29653 -0.02375 -0.00966 0.01067  84  ILE A CG2 
676  C  CD1 . ILE A 84  ? 0.33234 0.25515 0.28510 -0.01465 -0.00550 0.01600  84  ILE A CD1 
677  N  N   . GLY A 85  ? 0.29266 0.20054 0.26856 -0.03423 -0.00752 0.00187  85  GLY A N   
678  C  CA  . GLY A 85  ? 0.29900 0.20873 0.28260 -0.04032 -0.00927 -0.00504 85  GLY A CA  
679  C  C   . GLY A 85  ? 0.30993 0.21223 0.29275 -0.04023 -0.01116 -0.01315 85  GLY A C   
680  O  O   . GLY A 85  ? 0.31277 0.22168 0.29790 -0.04228 -0.01492 -0.02117 85  GLY A O   
681  N  N   . GLY A 86  ? 0.31725 0.20603 0.29686 -0.03735 -0.00899 -0.01173 86  GLY A N   
682  C  CA  . GLY A 86  ? 0.32841 0.20972 0.30729 -0.03631 -0.01052 -0.02016 86  GLY A CA  
683  C  C   . GLY A 86  ? 0.32459 0.21594 0.29640 -0.03161 -0.01359 -0.02575 86  GLY A C   
684  O  O   . GLY A 86  ? 0.33226 0.22479 0.30407 -0.03285 -0.01631 -0.03506 86  GLY A O   
685  N  N   . GLU A 87  ? 0.35872 0.25725 0.32385 -0.02655 -0.01296 -0.02031 87  GLU A N   
686  C  CA  . GLU A 87  ? 0.35892 0.26596 0.31572 -0.02260 -0.01474 -0.02438 87  GLU A CA  
687  C  C   . GLU A 87  ? 0.36167 0.28059 0.31689 -0.02488 -0.01884 -0.02696 87  GLU A C   
688  O  O   . GLU A 87  ? 0.36595 0.29004 0.31391 -0.02310 -0.02135 -0.03276 87  GLU A O   
689  C  CB  . GLU A 87  ? 0.34799 0.25801 0.29897 -0.01735 -0.01214 -0.01783 87  GLU A CB  
690  C  CG  . GLU A 87  ? 0.35600 0.25791 0.30666 -0.01286 -0.00948 -0.01883 87  GLU A CG  
691  C  CD  . GLU A 87  ? 0.36657 0.26478 0.31585 -0.01182 -0.01020 -0.02897 87  GLU A CD  
692  O  OE1 . GLU A 87  ? 0.37174 0.27794 0.31383 -0.01047 -0.01074 -0.03364 87  GLU A OE1 
693  O  OE2 . GLU A 87  ? 0.37292 0.25952 0.32758 -0.01236 -0.01005 -0.03229 87  GLU A OE2 
694  N  N   . LEU A 88  ? 0.33087 0.25461 0.29238 -0.02836 -0.01967 -0.02293 88  LEU A N   
695  C  CA  . LEU A 88  ? 0.33589 0.27111 0.29834 -0.03012 -0.02457 -0.02648 88  LEU A CA  
696  C  C   . LEU A 88  ? 0.33974 0.27467 0.30648 -0.03399 -0.02806 -0.03709 88  LEU A C   
697  O  O   . LEU A 88  ? 0.34999 0.29311 0.31165 -0.03283 -0.03308 -0.04302 88  LEU A O   
698  C  CB  . LEU A 88  ? 0.32383 0.26484 0.29470 -0.03300 -0.02421 -0.02113 88  LEU A CB  
699  C  CG  . LEU A 88  ? 0.33050 0.27822 0.29623 -0.02882 -0.02406 -0.01361 88  LEU A CG  
700  C  CD1 . LEU A 88  ? 0.32782 0.27845 0.30268 -0.03165 -0.02175 -0.00843 88  LEU A CD1 
701  C  CD2 . LEU A 88  ? 0.32222 0.27985 0.28157 -0.02583 -0.02975 -0.01633 88  LEU A CD2 
702  N  N   . ARG A 89  ? 0.49068 0.41548 0.46609 -0.03862 -0.02561 -0.03967 89  ARG A N   
703  C  CA  . ARG A 89  ? 0.50204 0.42492 0.48256 -0.04298 -0.02851 -0.05069 89  ARG A CA  
704  C  C   . ARG A 89  ? 0.50642 0.42680 0.47684 -0.03864 -0.03005 -0.05791 89  ARG A C   
705  O  O   . ARG A 89  ? 0.50995 0.43649 0.47865 -0.03970 -0.03489 -0.06744 89  ARG A O   
706  C  CB  . ARG A 89  ? 0.50244 0.41163 0.49340 -0.04895 -0.02450 -0.05083 89  ARG A CB  
707  C  CG  . ARG A 89  ? 0.51633 0.42969 0.51887 -0.05570 -0.02298 -0.04722 89  ARG A CG  
708  C  CD  . ARG A 89  ? 0.51473 0.41235 0.52587 -0.06251 -0.01838 -0.04737 89  ARG A CD  
709  N  NE  . ARG A 89  ? 0.51818 0.41850 0.53878 -0.06904 -0.01472 -0.04190 89  ARG A NE  
710  C  CZ  . ARG A 89  ? 0.52659 0.44137 0.55771 -0.07463 -0.01679 -0.04632 89  ARG A CZ  
711  N  NH1 . ARG A 89  ? 0.51332 0.44072 0.54692 -0.07455 -0.02344 -0.05639 89  ARG A NH1 
712  N  NH2 . ARG A 89  ? 0.52132 0.43869 0.56067 -0.08024 -0.01213 -0.04090 89  ARG A NH2 
713  N  N   . ARG A 90  ? 0.40814 0.32058 0.37200 -0.03360 -0.02603 -0.05411 90  ARG A N   
714  C  CA  . ARG A 90  ? 0.41703 0.32766 0.37203 -0.02940 -0.02623 -0.06140 90  ARG A CA  
715  C  C   . ARG A 90  ? 0.41990 0.34355 0.36272 -0.02621 -0.02956 -0.06290 90  ARG A C   
716  O  O   . ARG A 90  ? 0.42537 0.35155 0.36127 -0.02525 -0.03205 -0.07215 90  ARG A O   
717  C  CB  . ARG A 90  ? 0.40858 0.31030 0.36107 -0.02431 -0.02108 -0.05676 90  ARG A CB  
718  C  CG  . ARG A 90  ? 0.41606 0.30900 0.36753 -0.02185 -0.01994 -0.06603 90  ARG A CG  
719  C  CD  . ARG A 90  ? 0.41516 0.29771 0.36898 -0.01718 -0.01557 -0.06112 90  ARG A CD  
720  N  NE  . ARG A 90  ? 0.41342 0.30408 0.36082 -0.01228 -0.01312 -0.05408 90  ARG A NE  
721  C  CZ  . ARG A 90  ? 0.41578 0.31193 0.35595 -0.00756 -0.01117 -0.05798 90  ARG A CZ  
722  N  NH1 . ARG A 90  ? 0.41403 0.30891 0.35136 -0.00631 -0.01142 -0.06900 90  ARG A NH1 
723  N  NH2 . ARG A 90  ? 0.41265 0.31604 0.34859 -0.00442 -0.00849 -0.05121 90  ARG A NH2 
724  N  N   . ALA A 91  ? 0.33705 0.26817 0.27614 -0.02444 -0.02962 -0.05387 91  ALA A N   
725  C  CA  . ALA A 91  ? 0.33815 0.27941 0.26442 -0.02133 -0.03281 -0.05373 91  ALA A CA  
726  C  C   . ALA A 91  ? 0.34423 0.29416 0.27159 -0.02381 -0.04017 -0.06035 91  ALA A C   
727  O  O   . ALA A 91  ? 0.35263 0.30882 0.26762 -0.02124 -0.04404 -0.06442 91  ALA A O   
728  C  CB  . ALA A 91  ? 0.32623 0.27110 0.24908 -0.01881 -0.03092 -0.04232 91  ALA A CB  
729  N  N   . LEU A 92  ? 0.41653 0.36755 0.35833 -0.02884 -0.04218 -0.06170 92  LEU A N   
730  C  CA  . LEU A 92  ? 0.41663 0.37803 0.36225 -0.03136 -0.04964 -0.06910 92  LEU A CA  
731  C  C   . LEU A 92  ? 0.42770 0.38719 0.37280 -0.03364 -0.05251 -0.08232 92  LEU A C   
732  O  O   . LEU A 92  ? 0.43741 0.40676 0.37916 -0.03360 -0.05970 -0.08997 92  LEU A O   
733  C  CB  . LEU A 92  ? 0.41449 0.37935 0.37742 -0.03673 -0.04996 -0.06709 92  LEU A CB  
734  C  CG  . LEU A 92  ? 0.41822 0.38938 0.38214 -0.03425 -0.04941 -0.05654 92  LEU A CG  
735  C  CD1 . LEU A 92  ? 0.40888 0.38396 0.39070 -0.04020 -0.04851 -0.05595 92  LEU A CD1 
736  C  CD2 . LEU A 92  ? 0.40980 0.39214 0.36294 -0.02882 -0.05625 -0.05622 92  LEU A CD2 
737  N  N   . GLU A 93  ? 0.54307 0.48994 0.49135 -0.03518 -0.04751 -0.08562 93  GLU A N   
738  C  CA  . GLU A 93  ? 0.54858 0.49221 0.49547 -0.03669 -0.04968 -0.09888 93  GLU A CA  
739  C  C   . GLU A 93  ? 0.55109 0.49758 0.47937 -0.03070 -0.05019 -0.10245 93  GLU A C   
740  O  O   . GLU A 93  ? 0.55937 0.50836 0.48288 -0.03118 -0.05414 -0.11436 93  GLU A O   
741  C  CB  . GLU A 93  ? 0.54963 0.47699 0.50622 -0.03963 -0.04419 -0.10131 93  GLU A CB  
742  C  CG  . GLU A 93  ? 0.56205 0.48340 0.53514 -0.04610 -0.04186 -0.09668 93  GLU A CG  
743  C  CD  . GLU A 93  ? 0.57788 0.48035 0.55639 -0.04696 -0.03578 -0.09525 93  GLU A CD  
744  O  OE1 . GLU A 93  ? 0.59123 0.48549 0.56646 -0.04509 -0.03533 -0.10378 93  GLU A OE1 
745  O  OE2 . GLU A 93  ? 0.56384 0.45941 0.54922 -0.04902 -0.03162 -0.08571 93  GLU A OE2 
746  N  N   . ALA A 94  ? 0.47980 0.42625 0.39744 -0.02555 -0.04594 -0.09285 94  ALA A N   
747  C  CA  . ALA A 94  ? 0.48220 0.43037 0.38237 -0.02066 -0.04429 -0.09574 94  ALA A CA  
748  C  C   . ALA A 94  ? 0.49518 0.45481 0.38107 -0.01896 -0.05125 -0.09930 94  ALA A C   
749  O  O   . ALA A 94  ? 0.50089 0.46232 0.37358 -0.01693 -0.05195 -0.10751 94  ALA A O   
750  C  CB  . ALA A 94  ? 0.48396 0.42981 0.37817 -0.01670 -0.03750 -0.08449 94  ALA A CB  
751  N  N   . ARG A 95  ? 0.56023 0.52770 0.44789 -0.01922 -0.05658 -0.09351 95  ARG A N   
752  C  CA  . ARG A 95  ? 0.56445 0.54245 0.43830 -0.01653 -0.06447 -0.09595 95  ARG A CA  
753  C  C   . ARG A 95  ? 0.56673 0.55318 0.45273 -0.01830 -0.07156 -0.09392 95  ARG A C   
754  O  O   . ARG A 95  ? 0.56276 0.54690 0.46643 -0.02196 -0.06908 -0.09006 95  ARG A O   
755  C  CB  . ARG A 95  ? 0.56755 0.54593 0.42069 -0.01114 -0.06161 -0.08688 95  ARG A CB  
756  C  CG  . ARG A 95  ? 0.56851 0.54261 0.42585 -0.01018 -0.05567 -0.07312 95  ARG A CG  
757  C  CD  . ARG A 95  ? 0.57410 0.55091 0.41360 -0.00574 -0.05677 -0.06376 95  ARG A CD  
758  N  NE  . ARG A 95  ? 0.57149 0.55592 0.41199 -0.00416 -0.06606 -0.06192 95  ARG A NE  
759  C  CZ  . ARG A 95  ? 0.57705 0.56268 0.40556 0.00004  -0.06855 -0.05268 95  ARG A CZ  
760  N  NH1 . ARG A 95  ? 0.57118 0.55051 0.38546 0.00205  -0.06193 -0.04408 95  ARG A NH1 
761  N  NH2 . ARG A 95  ? 0.56521 0.55844 0.39677 0.00228  -0.07788 -0.05234 95  ARG A NH2 
762  N  N   . ALA A 96  ? 0.50126 0.49809 0.37727 -0.01534 -0.08045 -0.09673 96  ALA A N   
763  C  CA  . ALA A 96  ? 0.49142 0.49896 0.37943 -0.01605 -0.08842 -0.09676 96  ALA A CA  
764  C  C   . ALA A 96  ? 0.49471 0.50268 0.38186 -0.01234 -0.08702 -0.08268 96  ALA A C   
765  O  O   . ALA A 96  ? 0.50200 0.50625 0.37109 -0.00725 -0.08498 -0.07430 96  ALA A O   
766  C  CB  . ALA A 96  ? 0.50400 0.52316 0.38156 -0.01314 -0.09976 -0.10567 96  ALA A CB  
767  N  N   . PHE A 97  ? 0.39551 0.40781 0.30249 -0.01532 -0.08761 -0.08052 97  PHE A N   
768  C  CA  . PHE A 97  ? 0.39088 0.40469 0.30001 -0.01200 -0.08684 -0.06891 97  PHE A CA  
769  C  C   . PHE A 97  ? 0.39065 0.41809 0.31670 -0.01292 -0.09442 -0.07271 97  PHE A C   
770  O  O   . PHE A 97  ? 0.39833 0.43114 0.34130 -0.01907 -0.09592 -0.08216 97  PHE A O   
771  C  CB  . PHE A 97  ? 0.38090 0.38452 0.29826 -0.01480 -0.07630 -0.06050 97  PHE A CB  
772  C  CG  . PHE A 97  ? 0.38186 0.37471 0.28314 -0.01206 -0.06921 -0.05392 97  PHE A CG  
773  C  CD1 . PHE A 97  ? 0.38762 0.37910 0.27413 -0.00662 -0.06901 -0.04459 97  PHE A CD1 
774  C  CD2 . PHE A 97  ? 0.38223 0.36624 0.28408 -0.01498 -0.06257 -0.05735 97  PHE A CD2 
775  C  CE1 . PHE A 97  ? 0.38275 0.36553 0.25606 -0.00514 -0.06179 -0.03917 97  PHE A CE1 
776  C  CE2 . PHE A 97  ? 0.38675 0.36314 0.27595 -0.01246 -0.05593 -0.05229 97  PHE A CE2 
777  C  CZ  . PHE A 97  ? 0.39004 0.36647 0.26534 -0.00804 -0.05525 -0.04337 97  PHE A CZ  
778  N  N   . ASP A 98  ? 0.50019 0.53314 0.42237 -0.00684 -0.09896 -0.06562 98  ASP A N   
779  C  CA  . ASP A 98  ? 0.48948 0.53690 0.42903 -0.00655 -0.10599 -0.06900 98  ASP A CA  
780  C  C   . ASP A 98  ? 0.49051 0.53760 0.44947 -0.01069 -0.09882 -0.06392 98  ASP A C   
781  O  O   . ASP A 98  ? 0.47829 0.53694 0.45782 -0.01475 -0.10114 -0.07006 98  ASP A O   
782  C  CB  . ASP A 98  ? 0.50225 0.55582 0.42920 0.00304  -0.11521 -0.06439 98  ASP A CB  
783  C  CG  . ASP A 98  ? 0.51934 0.58434 0.44003 0.00619  -0.12748 -0.07455 98  ASP A CG  
784  O  OD1 . ASP A 98  ? 0.53538 0.60261 0.45957 0.00067  -0.12820 -0.08546 98  ASP A OD1 
785  O  OD2 . ASP A 98  ? 0.53175 0.60310 0.44369 0.01450  -0.13681 -0.07186 98  ASP A OD2 
786  N  N   . ARG A 99  ? 0.39736 0.43228 0.35037 -0.01009 -0.08998 -0.05344 99  ARG A N   
787  C  CA  . ARG A 99  ? 0.39802 0.43222 0.36627 -0.01318 -0.08321 -0.04792 99  ARG A CA  
788  C  C   . ARG A 99  ? 0.39897 0.41813 0.35730 -0.01304 -0.07369 -0.03840 99  ARG A C   
789  O  O   . ARG A 99  ? 0.39913 0.41006 0.33970 -0.00995 -0.07259 -0.03557 99  ARG A O   
790  C  CB  . ARG A 99  ? 0.43284 0.47759 0.40748 -0.00779 -0.08832 -0.04460 99  ARG A CB  
791  C  CG  . ARG A 99  ? 0.43413 0.47177 0.39078 0.00050  -0.08916 -0.03451 99  ARG A CG  
792  C  CD  . ARG A 99  ? 0.43460 0.48330 0.39495 0.00773  -0.09802 -0.03404 99  ARG A CD  
793  N  NE  . ARG A 99  ? 0.42857 0.49131 0.41369 0.00427  -0.09867 -0.03975 99  ARG A NE  
794  C  CZ  . ARG A 99  ? 0.42309 0.48867 0.41926 0.00549  -0.09520 -0.03532 99  ARG A CZ  
795  N  NH1 . ARG A 99  ? 0.42260 0.47742 0.40797 0.01008  -0.09133 -0.02531 99  ARG A NH1 
796  N  NH2 . ARG A 99  ? 0.41742 0.49732 0.43640 0.00159  -0.09518 -0.04168 99  ARG A NH2 
797  N  N   . VAL A 100 ? 0.32620 0.34283 0.29640 -0.01657 -0.06671 -0.03390 100 VAL A N   
798  C  CA  . VAL A 100 ? 0.32981 0.33446 0.29327 -0.01611 -0.05842 -0.02498 100 VAL A CA  
799  C  C   . VAL A 100 ? 0.32261 0.33020 0.28853 -0.01227 -0.05778 -0.01759 100 VAL A C   
800  O  O   . VAL A 100 ? 0.31811 0.33545 0.29848 -0.01340 -0.05937 -0.01950 100 VAL A O   
801  C  CB  . VAL A 100 ? 0.32310 0.32050 0.29606 -0.02293 -0.05086 -0.02568 100 VAL A CB  
802  C  CG1 . VAL A 100 ? 0.31400 0.30128 0.28123 -0.02163 -0.04346 -0.01667 100 VAL A CG1 
803  C  CG2 . VAL A 100 ? 0.32890 0.32129 0.29898 -0.02605 -0.05136 -0.03328 100 VAL A CG2 
804  N  N   . ILE A 101 ? 0.30368 0.30329 0.25620 -0.00794 -0.05523 -0.00989 101 ILE A N   
805  C  CA  . ILE A 101 ? 0.30250 0.30227 0.25610 -0.00430 -0.05393 -0.00290 101 ILE A CA  
806  C  C   . ILE A 101 ? 0.29866 0.28852 0.24961 -0.00615 -0.04530 0.00329  101 ILE A C   
807  O  O   . ILE A 101 ? 0.29232 0.27406 0.23299 -0.00663 -0.04206 0.00456  101 ILE A O   
808  C  CB  . ILE A 101 ? 0.30172 0.30064 0.24153 0.00301  -0.05974 0.00079  101 ILE A CB  
809  C  CG1 . ILE A 101 ? 0.30861 0.31771 0.24923 0.00582  -0.06965 -0.00574 101 ILE A CG1 
810  C  CG2 . ILE A 101 ? 0.30043 0.29866 0.24311 0.00681  -0.05860 0.00710  101 ILE A CG2 
811  C  CD1 . ILE A 101 ? 0.31763 0.32386 0.24121 0.01351  -0.07608 -0.00163 101 ILE A CD1 
812  N  N   . ARG A 102 ? 0.26837 0.25998 0.22888 -0.00699 -0.04171 0.00646  102 ARG A N   
813  C  CA  . ARG A 102 ? 0.26246 0.24613 0.22106 -0.00840 -0.03442 0.01186  102 ARG A CA  
814  C  C   . ARG A 102 ? 0.26573 0.25214 0.22949 -0.00620 -0.03298 0.01586  102 ARG A C   
815  O  O   . ARG A 102 ? 0.26275 0.25754 0.23367 -0.00394 -0.03703 0.01398  102 ARG A O   
816  C  CB  . ARG A 102 ? 0.26767 0.24853 0.23347 -0.01418 -0.02963 0.00985  102 ARG A CB  
817  C  CG  . ARG A 102 ? 0.27341 0.26182 0.25415 -0.01826 -0.02894 0.00701  102 ARG A CG  
818  C  CD  . ARG A 102 ? 0.27246 0.25477 0.25793 -0.02410 -0.02352 0.00664  102 ARG A CD  
819  N  NE  . ARG A 102 ? 0.27686 0.26485 0.27465 -0.02835 -0.02033 0.00643  102 ARG A NE  
820  C  CZ  . ARG A 102 ? 0.27607 0.26287 0.27472 -0.02849 -0.01534 0.01154  102 ARG A CZ  
821  N  NH1 . ARG A 102 ? 0.26297 0.24314 0.25210 -0.02478 -0.01338 0.01694  102 ARG A NH1 
822  N  NH2 . ARG A 102 ? 0.27874 0.27195 0.28823 -0.03276 -0.01203 0.01065  102 ARG A NH2 
823  N  N   . THR A 103 ? 0.25719 0.23712 0.21780 -0.00656 -0.02741 0.02064  103 THR A N   
824  C  CA  . THR A 103 ? 0.25508 0.23635 0.21954 -0.00480 -0.02518 0.02395  103 THR A CA  
825  C  C   . THR A 103 ? 0.25879 0.24040 0.23059 -0.00909 -0.01944 0.02447  103 THR A C   
826  O  O   . THR A 103 ? 0.25392 0.22958 0.22267 -0.01183 -0.01618 0.02532  103 THR A O   
827  C  CB  . THR A 103 ? 0.24107 0.21445 0.19474 -0.00165 -0.02376 0.02885  103 THR A CB  
828  O  OG1 . THR A 103 ? 0.24807 0.22034 0.19424 0.00272  -0.02898 0.02956  103 THR A OG1 
829  C  CG2 . THR A 103 ? 0.23638 0.20991 0.19424 -0.00077 -0.02049 0.03140  103 THR A CG2 
830  N  N   . ALA A 104 ? 0.35510 0.34362 0.33609 -0.00929 -0.01825 0.02388  104 ALA A N   
831  C  CA  . ALA A 104 ? 0.35949 0.34846 0.34574 -0.01342 -0.01242 0.02488  104 ALA A CA  
832  C  C   . ALA A 104 ? 0.34833 0.32865 0.32608 -0.01296 -0.00859 0.02941  104 ALA A C   
833  O  O   . ALA A 104 ? 0.33732 0.31530 0.31001 -0.00942 -0.00890 0.03157  104 ALA A O   
834  C  CB  . ALA A 104 ? 0.36979 0.36823 0.36565 -0.01281 -0.01120 0.02343  104 ALA A CB  
835  N  N   . CYS A 105 ? 0.32077 0.29611 0.29736 -0.01648 -0.00525 0.03058  105 CYS A N   
836  C  CA  . CYS A 105 ? 0.30338 0.27139 0.27255 -0.01553 -0.00273 0.03411  105 CYS A CA  
837  C  C   . CYS A 105 ? 0.30196 0.27168 0.27179 -0.01567 0.00097  0.03656  105 CYS A C   
838  O  O   . CYS A 105 ? 0.31818 0.29472 0.29388 -0.01624 0.00202  0.03539  105 CYS A O   
839  C  CB  . CYS A 105 ? 0.30038 0.26145 0.26751 -0.01789 -0.00179 0.03413  105 CYS A CB  
840  S  SG  . CYS A 105 ? 0.30727 0.26661 0.27985 -0.02336 0.00211  0.03492  105 CYS A SG  
841  N  N   . GLY A 106 ? 0.28969 0.25413 0.25361 -0.01483 0.00282  0.03936  106 GLY A N   
842  C  CA  . GLY A 106 ? 0.29452 0.26055 0.25698 -0.01447 0.00573  0.04133  106 GLY A CA  
843  C  C   . GLY A 106 ? 0.29616 0.25792 0.25581 -0.01684 0.00880  0.04425  106 GLY A C   
844  O  O   . GLY A 106 ? 0.28755 0.24853 0.24232 -0.01561 0.01038  0.04646  106 GLY A O   
845  N  N   . LYS A 107 ? 0.32438 0.28261 0.28638 -0.02021 0.00945  0.04429  107 LYS A N   
846  C  CA  . LYS A 107 ? 0.32689 0.27858 0.28560 -0.02299 0.01271  0.04786  107 LYS A CA  
847  C  C   . LYS A 107 ? 0.33227 0.28617 0.29815 -0.02877 0.01545  0.04650  107 LYS A C   
848  O  O   . LYS A 107 ? 0.33489 0.28882 0.30634 -0.03062 0.01337  0.04314  107 LYS A O   
849  C  CB  . LYS A 107 ? 0.32427 0.26573 0.27810 -0.02124 0.01087  0.04943  107 LYS A CB  
850  C  CG  . LYS A 107 ? 0.32491 0.25669 0.27372 -0.02313 0.01361  0.05409  107 LYS A CG  
851  C  CD  . LYS A 107 ? 0.32158 0.24412 0.26490 -0.01882 0.01094  0.05572  107 LYS A CD  
852  C  CE  . LYS A 107 ? 0.32536 0.24622 0.27301 -0.01807 0.00807  0.05119  107 LYS A CE  
853  N  NZ  . LYS A 107 ? 0.33985 0.24986 0.28404 -0.01496 0.00654  0.05227  107 LYS A NZ  
854  N  N   . TRP A 108 ? 0.27345 0.22992 0.23925 -0.03194 0.02033  0.04859  108 TRP A N   
855  C  CA  . TRP A 108 ? 0.28336 0.24482 0.25804 -0.03824 0.02397  0.04647  108 TRP A CA  
856  C  C   . TRP A 108 ? 0.29126 0.24293 0.26731 -0.04296 0.02465  0.04703  108 TRP A C   
857  O  O   . TRP A 108 ? 0.29551 0.25183 0.28169 -0.04734 0.02453  0.04251  108 TRP A O   
858  C  CB  . TRP A 108 ? 0.28233 0.24762 0.25493 -0.04118 0.03040  0.04904  108 TRP A CB  
859  C  CG  . TRP A 108 ? 0.29213 0.26524 0.27563 -0.04821 0.03523  0.04609  108 TRP A CG  
860  C  CD1 . TRP A 108 ? 0.29884 0.28717 0.29355 -0.04862 0.03603  0.04062  108 TRP A CD1 
861  C  CD2 . TRP A 108 ? 0.29273 0.25915 0.27812 -0.05599 0.04006  0.04793  108 TRP A CD2 
862  N  NE1 . TRP A 108 ? 0.29604 0.28961 0.30061 -0.05635 0.04113  0.03838  108 TRP A NE1 
863  C  CE2 . TRP A 108 ? 0.29913 0.27890 0.29798 -0.06158 0.04403  0.04294  108 TRP A CE2 
864  C  CE3 . TRP A 108 ? 0.29973 0.24967 0.27724 -0.05870 0.04145  0.05313  108 TRP A CE3 
865  C  CZ2 . TRP A 108 ? 0.31045 0.28810 0.31547 -0.07088 0.04991  0.04283  108 TRP A CZ2 
866  C  CZ3 . TRP A 108 ? 0.31419 0.25977 0.29660 -0.06758 0.04712  0.05366  108 TRP A CZ3 
867  C  CH2 . TRP A 108 ? 0.30742 0.26703 0.30362 -0.07414 0.05160  0.04848  108 TRP A CH2 
868  N  N   . GLY A 109 ? 0.34833 0.28637 0.31479 -0.04189 0.02500  0.05203  109 GLY A N   
869  C  CA  . GLY A 109 ? 0.34956 0.27581 0.31690 -0.04597 0.02571  0.05257  109 GLY A CA  
870  C  C   . GLY A 109 ? 0.34785 0.27495 0.32144 -0.04488 0.02052  0.04651  109 GLY A C   
871  O  O   . GLY A 109 ? 0.35135 0.27734 0.33259 -0.05032 0.02106  0.04278  109 GLY A O   
872  N  N   . LEU A 110 ? 0.28512 0.21440 0.25525 -0.03824 0.01569  0.04510  110 LEU A N   
873  C  CA  . LEU A 110 ? 0.28890 0.21982 0.26286 -0.03691 0.01105  0.03936  110 LEU A CA  
874  C  C   . LEU A 110 ? 0.29269 0.23652 0.27624 -0.03945 0.00954  0.03393  110 LEU A C   
875  O  O   . LEU A 110 ? 0.30192 0.24659 0.29135 -0.04227 0.00735  0.02873  110 LEU A O   
876  C  CB  . LEU A 110 ? 0.27869 0.20993 0.24630 -0.02991 0.00745  0.03945  110 LEU A CB  
877  C  CG  . LEU A 110 ? 0.28552 0.21749 0.25397 -0.02805 0.00330  0.03411  110 LEU A CG  
878  C  CD1 . LEU A 110 ? 0.28199 0.20352 0.25141 -0.03034 0.00323  0.03182  110 LEU A CD1 
879  C  CD2 . LEU A 110 ? 0.26684 0.19992 0.22906 -0.02213 0.00136  0.03471  110 LEU A CD2 
880  N  N   . GLU A 111 ? 0.27808 0.23231 0.26366 -0.03806 0.01025  0.03446  111 GLU A N   
881  C  CA  . GLU A 111 ? 0.29312 0.26037 0.28843 -0.03903 0.00806  0.02923  111 GLU A CA  
882  C  C   . GLU A 111 ? 0.30015 0.27085 0.30611 -0.04667 0.01102  0.02602  111 GLU A C   
883  O  O   . GLU A 111 ? 0.30412 0.28191 0.31866 -0.04842 0.00748  0.01985  111 GLU A O   
884  C  CB  . GLU A 111 ? 0.29008 0.26642 0.28587 -0.03563 0.00881  0.03039  111 GLU A CB  
885  C  CG  . GLU A 111 ? 0.30286 0.29270 0.30863 -0.03458 0.00556  0.02508  111 GLU A CG  
886  C  CD  . GLU A 111 ? 0.31909 0.30944 0.32266 -0.03018 -0.00144 0.02217  111 GLU A CD  
887  O  OE1 . GLU A 111 ? 0.31462 0.29645 0.30815 -0.02692 -0.00296 0.02474  111 GLU A OE1 
888  O  OE2 . GLU A 111 ? 0.32212 0.32200 0.33382 -0.02991 -0.00542 0.01715  111 GLU A OE2 
889  N  N   . SER A 112 ? 0.33633 0.30222 0.34163 -0.05159 0.01756  0.03003  112 SER A N   
890  C  CA  . SER A 112 ? 0.34138 0.30951 0.35697 -0.06029 0.02177  0.02730  112 SER A CA  
891  C  C   . SER A 112 ? 0.34694 0.30586 0.36463 -0.06375 0.01949  0.02398  112 SER A C   
892  O  O   . SER A 112 ? 0.35220 0.31781 0.38188 -0.06947 0.01905  0.01760  112 SER A O   
893  C  CB  . SER A 112 ? 0.33987 0.30179 0.35094 -0.06501 0.03004  0.03364  112 SER A CB  
894  O  OG  . SER A 112 ? 0.35704 0.32092 0.37835 -0.07462 0.03540  0.03123  112 SER A OG  
895  N  N   . HIS A 113 ? 0.40909 0.35346 0.41613 -0.06017 0.01779  0.02732  113 HIS A N   
896  C  CA  . HIS A 113 ? 0.40817 0.34271 0.41664 -0.06264 0.01561  0.02351  113 HIS A CA  
897  C  C   . HIS A 113 ? 0.41230 0.35695 0.42625 -0.06035 0.00871  0.01526  113 HIS A C   
898  O  O   . HIS A 113 ? 0.41849 0.36438 0.44089 -0.06548 0.00725  0.00861  113 HIS A O   
899  C  CB  . HIS A 113 ? 0.40124 0.31927 0.39753 -0.05781 0.01512  0.02845  113 HIS A CB  
900  C  CG  . HIS A 113 ? 0.40901 0.31658 0.40616 -0.05880 0.01254  0.02378  113 HIS A CG  
901  N  ND1 . HIS A 113 ? 0.42268 0.32088 0.42572 -0.06658 0.01557  0.02180  113 HIS A ND1 
902  C  CD2 . HIS A 113 ? 0.41574 0.32060 0.40868 -0.05324 0.00767  0.02015  113 HIS A CD2 
903  C  CE1 . HIS A 113 ? 0.41722 0.30700 0.41979 -0.06531 0.01216  0.01675  113 HIS A CE1 
904  N  NE2 . HIS A 113 ? 0.41727 0.31152 0.41356 -0.05711 0.00747  0.01557  113 HIS A NE2 
905  N  N   . LEU A 114 ? 0.32738 0.27889 0.33595 -0.05285 0.00435  0.01554  114 LEU A N   
906  C  CA  . LEU A 114 ? 0.33791 0.29784 0.34849 -0.04991 -0.00240 0.00889  114 LEU A CA  
907  C  C   . LEU A 114 ? 0.34254 0.31774 0.36641 -0.05361 -0.00425 0.00286  114 LEU A C   
908  O  O   . LEU A 114 ? 0.35137 0.33164 0.38047 -0.05496 -0.00912 -0.00450 114 LEU A O   
909  C  CB  . LEU A 114 ? 0.33471 0.29732 0.33583 -0.04172 -0.00560 0.01174  114 LEU A CB  
910  C  CG  . LEU A 114 ? 0.33459 0.28527 0.32426 -0.03756 -0.00480 0.01571  114 LEU A CG  
911  C  CD1 . LEU A 114 ? 0.32926 0.28391 0.31119 -0.03090 -0.00769 0.01728  114 LEU A CD1 
912  C  CD2 . LEU A 114 ? 0.33232 0.27428 0.32091 -0.03907 -0.00619 0.01124  114 LEU A CD2 
913  N  N   . LEU A 115 ? 0.32503 0.30875 0.35494 -0.05505 -0.00061 0.00514  115 LEU A N   
914  C  CA  . LEU A 115 ? 0.33079 0.33105 0.37552 -0.05820 -0.00207 -0.00122 115 LEU A CA  
915  C  C   . LEU A 115 ? 0.32684 0.32727 0.38327 -0.06775 0.00015  -0.00698 115 LEU A C   
916  O  O   . LEU A 115 ? 0.32979 0.34472 0.39965 -0.07032 -0.00321 -0.01484 115 LEU A O   
917  C  CB  . LEU A 115 ? 0.32614 0.33508 0.37524 -0.05805 0.00276  0.00203  115 LEU A CB  
918  C  CG  . LEU A 115 ? 0.33405 0.34780 0.37682 -0.04896 -0.00063 0.00477  115 LEU A CG  
919  C  CD1 . LEU A 115 ? 0.32311 0.34276 0.36899 -0.04945 0.00547  0.00783  115 LEU A CD1 
920  C  CD2 . LEU A 115 ? 0.33970 0.36579 0.38822 -0.04408 -0.00907 -0.00141 115 LEU A CD2 
921  N  N   . SER A 116 ? 0.44210 0.42658 0.49421 -0.07295 0.00547  -0.00352 116 SER A N   
922  C  CA  . SER A 116 ? 0.44166 0.42296 0.50432 -0.08301 0.00865  -0.00836 116 SER A CA  
923  C  C   . SER A 116 ? 0.44684 0.41839 0.50686 -0.08331 0.00388  -0.01368 116 SER A C   
924  O  O   . SER A 116 ? 0.45001 0.41713 0.51876 -0.09179 0.00596  -0.01866 116 SER A O   
925  C  CB  . SER A 116 ? 0.44374 0.41165 0.50320 -0.08937 0.01837  -0.00075 116 SER A CB  
926  O  OG  . SER A 116 ? 0.44264 0.38993 0.48824 -0.08653 0.01883  0.00492  116 SER A OG  
927  N  N   . LEU A 117 ? 0.42948 0.39761 0.47791 -0.07473 -0.00195 -0.01321 117 LEU A N   
928  C  CA  . LEU A 117 ? 0.43652 0.39573 0.48114 -0.07429 -0.00607 -0.01872 117 LEU A CA  
929  C  C   . LEU A 117 ? 0.43859 0.41061 0.49525 -0.07821 -0.01172 -0.03024 117 LEU A C   
930  O  O   . LEU A 117 ? 0.44576 0.43534 0.50818 -0.07563 -0.01647 -0.03375 117 LEU A O   
931  C  CB  . LEU A 117 ? 0.43380 0.38970 0.46369 -0.06436 -0.01040 -0.01609 117 LEU A CB  
932  C  CG  . LEU A 117 ? 0.43970 0.37737 0.45810 -0.06133 -0.00740 -0.01063 117 LEU A CG  
933  C  CD1 . LEU A 117 ? 0.43455 0.37050 0.44375 -0.05503 -0.01258 -0.01465 117 LEU A CD1 
934  C  CD2 . LEU A 117 ? 0.43201 0.35469 0.45483 -0.06857 -0.00263 -0.01091 117 LEU A CD2 
935  N  N   . ASP A 118 ? 0.61373 0.57670 0.67437 -0.08410 -0.01166 -0.03656 118 ASP A N   
936  C  CA  . ASP A 118 ? 0.61975 0.59391 0.69185 -0.08845 -0.01744 -0.04892 118 ASP A CA  
937  C  C   . ASP A 118 ? 0.62330 0.59445 0.68412 -0.08182 -0.02463 -0.05409 118 ASP A C   
938  O  O   . ASP A 118 ? 0.63744 0.59358 0.69392 -0.08334 -0.02360 -0.05675 118 ASP A O   
939  C  CB  . ASP A 118 ? 0.62897 0.59525 0.71385 -0.10044 -0.01231 -0.05373 118 ASP A CB  
940  C  CG  . ASP A 118 ? 0.64253 0.62413 0.74304 -0.10633 -0.01796 -0.06744 118 ASP A CG  
941  O  OD1 . ASP A 118 ? 0.64769 0.64669 0.74852 -0.10032 -0.02640 -0.07269 118 ASP A OD1 
942  O  OD2 . ASP A 118 ? 0.65132 0.62722 0.76369 -0.11702 -0.01416 -0.07302 118 ASP A OD2 
943  N  N   . LEU A 119 ? 0.38958 0.37441 0.44510 -0.07430 -0.03166 -0.05548 119 LEU A N   
944  C  CA  . LEU A 119 ? 0.39461 0.37830 0.43711 -0.06758 -0.03811 -0.05952 119 LEU A CA  
945  C  C   . LEU A 119 ? 0.38781 0.38545 0.43746 -0.06939 -0.04653 -0.07206 119 LEU A C   
946  O  O   . LEU A 119 ? 0.38590 0.39856 0.45029 -0.07327 -0.04886 -0.07648 119 LEU A O   
947  C  CB  . LEU A 119 ? 0.38986 0.37718 0.41861 -0.05775 -0.04006 -0.05151 119 LEU A CB  
948  C  CG  . LEU A 119 ? 0.38584 0.35994 0.40556 -0.05480 -0.03300 -0.04036 119 LEU A CG  
949  C  CD1 . LEU A 119 ? 0.38336 0.36220 0.39161 -0.04632 -0.03496 -0.03361 119 LEU A CD1 
950  C  CD2 . LEU A 119 ? 0.38547 0.34302 0.39763 -0.05480 -0.03026 -0.04128 119 LEU A CD2 
951  N  N   . PRO A 120 ? 0.38818 0.38234 0.42800 -0.06654 -0.05141 -0.07883 120 PRO A N   
952  C  CA  . PRO A 120 ? 0.39041 0.39863 0.43540 -0.06766 -0.06050 -0.09145 120 PRO A CA  
953  C  C   . PRO A 120 ? 0.38625 0.41244 0.42826 -0.06054 -0.06847 -0.09067 120 PRO A C   
954  O  O   . PRO A 120 ? 0.38680 0.42824 0.43716 -0.06167 -0.07650 -0.10063 120 PRO A O   
955  C  CB  . PRO A 120 ? 0.38936 0.38764 0.42044 -0.06497 -0.06275 -0.09736 120 PRO A CB  
956  C  CG  . PRO A 120 ? 0.39214 0.37050 0.41626 -0.06453 -0.05395 -0.08935 120 PRO A CG  
957  C  CD  . PRO A 120 ? 0.39146 0.36970 0.41581 -0.06234 -0.04880 -0.07632 120 PRO A CD  
958  N  N   . VAL A 121 ? 0.43419 0.45876 0.46490 -0.05310 -0.06691 -0.07956 121 VAL A N   
959  C  CA  . VAL A 121 ? 0.42679 0.46512 0.45276 -0.04529 -0.07433 -0.07746 121 VAL A CA  
960  C  C   . VAL A 121 ? 0.42096 0.46259 0.45488 -0.04457 -0.06955 -0.06843 121 VAL A C   
961  O  O   . VAL A 121 ? 0.42140 0.45231 0.45781 -0.04835 -0.06038 -0.06181 121 VAL A O   
962  C  CB  . VAL A 121 ? 0.42502 0.45733 0.42713 -0.03643 -0.07747 -0.07318 121 VAL A CB  
963  C  CG1 . VAL A 121 ? 0.43319 0.46036 0.42666 -0.03779 -0.08000 -0.08220 121 VAL A CG1 
964  C  CG2 . VAL A 121 ? 0.43203 0.45075 0.42411 -0.03370 -0.06905 -0.06099 121 VAL A CG2 
965  N  N   . PRO A 122 ? 0.37662 0.43301 0.41458 -0.03936 -0.07581 -0.06829 122 PRO A N   
966  C  CA  . PRO A 122 ? 0.37234 0.43207 0.41719 -0.03777 -0.07131 -0.06038 122 PRO A CA  
967  C  C   . PRO A 122 ? 0.37937 0.42456 0.40754 -0.03271 -0.06574 -0.04845 122 PRO A C   
968  O  O   . PRO A 122 ? 0.38018 0.41684 0.39046 -0.02784 -0.06766 -0.04582 122 PRO A O   
969  C  CB  . PRO A 122 ? 0.36276 0.44033 0.41257 -0.03099 -0.08120 -0.06378 122 PRO A CB  
970  C  CG  . PRO A 122 ? 0.36318 0.45020 0.41608 -0.03238 -0.09014 -0.07564 122 PRO A CG  
971  C  CD  . PRO A 122 ? 0.37558 0.44708 0.41357 -0.03469 -0.08772 -0.07639 122 PRO A CD  
972  N  N   . MET A 123 ? 0.45871 0.50190 0.49315 -0.03428 -0.05849 -0.04173 123 MET A N   
973  C  CA  . MET A 123 ? 0.45975 0.49073 0.48121 -0.03025 -0.05297 -0.03114 123 MET A CA  
974  C  C   . MET A 123 ? 0.45833 0.49712 0.48429 -0.02557 -0.05316 -0.02649 123 MET A C   
975  O  O   . MET A 123 ? 0.45369 0.49995 0.49452 -0.02957 -0.04928 -0.02741 123 MET A O   
976  C  CB  . MET A 123 ? 0.46862 0.48679 0.49103 -0.03649 -0.04349 -0.02739 123 MET A CB  
977  C  CG  . MET A 123 ? 0.46585 0.47427 0.47833 -0.03291 -0.03780 -0.01729 123 MET A CG  
978  S  SD  . MET A 123 ? 0.49399 0.48415 0.49509 -0.03445 -0.03219 -0.01390 123 MET A SD  
979  C  CE  . MET A 123 ? 0.46952 0.45448 0.48258 -0.04285 -0.02439 -0.01261 123 MET A CE  
980  N  N   . GLU A 124 ? 0.43875 0.47529 0.45172 -0.01731 -0.05720 -0.02167 124 GLU A N   
981  C  CA  . GLU A 124 ? 0.42806 0.46956 0.44358 -0.01170 -0.05788 -0.01723 124 GLU A CA  
982  C  C   . GLU A 124 ? 0.43499 0.46425 0.44237 -0.01128 -0.04998 -0.00837 124 GLU A C   
983  O  O   . GLU A 124 ? 0.43341 0.45065 0.42619 -0.01020 -0.04810 -0.00413 124 GLU A O   
984  C  CB  . GLU A 124 ? 0.43074 0.47539 0.43656 -0.00271 -0.06738 -0.01692 124 GLU A CB  
985  C  CG  . GLU A 124 ? 0.45046 0.48848 0.44714 0.00426  -0.06658 -0.00855 124 GLU A CG  
986  C  CD  . GLU A 124 ? 0.44812 0.48997 0.43803 0.01344  -0.07655 -0.00831 124 GLU A CD  
987  O  OE1 . GLU A 124 ? 0.46092 0.50218 0.44010 0.01551  -0.08296 -0.01064 124 GLU A OE1 
988  O  OE2 . GLU A 124 ? 0.44875 0.49357 0.44322 0.01903  -0.07814 -0.00579 124 GLU A OE2 
989  N  N   . THR A 125 ? 0.31126 0.34468 0.32855 -0.01225 -0.04531 -0.00636 125 THR A N   
990  C  CA  . THR A 125 ? 0.31755 0.34137 0.32863 -0.01194 -0.03827 0.00099  125 THR A CA  
991  C  C   . THR A 125 ? 0.31075 0.33727 0.32091 -0.00486 -0.04046 0.00405  125 THR A C   
992  O  O   . THR A 125 ? 0.31485 0.35303 0.33797 -0.00366 -0.04154 0.00082  125 THR A O   
993  C  CB  . THR A 125 ? 0.31648 0.34103 0.33740 -0.01906 -0.03025 0.00110  125 THR A CB  
994  O  OG1 . THR A 125 ? 0.32270 0.34071 0.34256 -0.02517 -0.02797 -0.00067 125 THR A OG1 
995  C  CG2 . THR A 125 ? 0.31750 0.33413 0.33187 -0.01779 -0.02416 0.00804  125 THR A CG2 
996  N  N   . ARG A 126 ? 0.32264 0.33836 0.31828 -0.00039 -0.04073 0.00982  126 ARG A N   
997  C  CA  . ARG A 126 ? 0.31321 0.32775 0.30605 0.00632  -0.04265 0.01325  126 ARG A CA  
998  C  C   . ARG A 126 ? 0.30933 0.31786 0.30130 0.00495  -0.03518 0.01766  126 ARG A C   
999  O  O   . ARG A 126 ? 0.31388 0.31505 0.30054 0.00068  -0.02980 0.02021  126 ARG A O   
1000 C  CB  . ARG A 126 ? 0.31071 0.31623 0.28734 0.01173  -0.04768 0.01693  126 ARG A CB  
1001 C  CG  . ARG A 126 ? 0.31560 0.32712 0.29044 0.01443  -0.05628 0.01269  126 ARG A CG  
1002 C  CD  . ARG A 126 ? 0.31337 0.31415 0.26872 0.01895  -0.05993 0.01732  126 ARG A CD  
1003 N  NE  . ARG A 126 ? 0.31632 0.32292 0.26779 0.02181  -0.06861 0.01311  126 ARG A NE  
1004 C  CZ  . ARG A 126 ? 0.32832 0.32728 0.26160 0.02535  -0.07254 0.01608  126 ARG A CZ  
1005 N  NH1 . ARG A 126 ? 0.32357 0.30866 0.24163 0.02590  -0.06798 0.02335  126 ARG A NH1 
1006 N  NH2 . ARG A 126 ? 0.33445 0.34031 0.26455 0.02807  -0.08108 0.01134  126 ARG A NH2 
1007 N  N   . GLU A 127 ? 0.29294 0.30505 0.29039 0.00912  -0.03535 0.01793  127 GLU A N   
1008 C  CA  . GLU A 127 ? 0.29286 0.30019 0.28937 0.00837  -0.02897 0.02108  127 GLU A CA  
1009 C  C   . GLU A 127 ? 0.28590 0.27928 0.26764 0.00995  -0.02795 0.02667  127 GLU A C   
1010 O  O   . GLU A 127 ? 0.28299 0.27040 0.25554 0.01373  -0.03251 0.02876  127 GLU A O   
1011 C  CB  . GLU A 127 ? 0.28502 0.29969 0.29122 0.01304  -0.02971 0.01882  127 GLU A CB  
1012 C  CG  . GLU A 127 ? 0.28970 0.31940 0.31224 0.00981  -0.02729 0.01315  127 GLU A CG  
1013 C  CD  . GLU A 127 ? 0.30289 0.33186 0.32615 0.00171  -0.01931 0.01403  127 GLU A CD  
1014 O  OE1 . GLU A 127 ? 0.29913 0.32361 0.31865 0.00092  -0.01386 0.01668  127 GLU A OE1 
1015 O  OE2 . GLU A 127 ? 0.32520 0.35741 0.35223 -0.00372 -0.01876 0.01203  127 GLU A OE2 
1016 N  N   . ASP A 128 ? 0.31857 0.30711 0.29787 0.00682  -0.02177 0.02899  128 ASP A N   
1017 C  CA  . ASP A 128 ? 0.30876 0.28596 0.27663 0.00722  -0.01983 0.03330  128 ASP A CA  
1018 C  C   . ASP A 128 ? 0.30703 0.28064 0.27454 0.01172  -0.02027 0.03452  128 ASP A C   
1019 O  O   . ASP A 128 ? 0.31333 0.28729 0.28405 0.01098  -0.01629 0.03413  128 ASP A O   
1020 C  CB  . ASP A 128 ? 0.30103 0.27590 0.26748 0.00246  -0.01407 0.03440  128 ASP A CB  
1021 C  CG  . ASP A 128 ? 0.29268 0.25823 0.24914 0.00215  -0.01225 0.03761  128 ASP A CG  
1022 O  OD1 . ASP A 128 ? 0.29086 0.25063 0.24075 0.00485  -0.01446 0.03952  128 ASP A OD1 
1023 O  OD2 . ASP A 128 ? 0.29217 0.25621 0.24737 -0.00078 -0.00857 0.03823  128 ASP A OD2 
1024 N  N   . ASP A 129 ? 0.50163 0.47082 0.46430 0.01667  -0.02537 0.03597  129 ASP A N   
1025 C  CA  . ASP A 129 ? 0.50446 0.46782 0.46647 0.02157  -0.02637 0.03728  129 ASP A CA  
1026 C  C   . ASP A 129 ? 0.49686 0.44759 0.44916 0.01979  -0.02250 0.04124  129 ASP A C   
1027 O  O   . ASP A 129 ? 0.49083 0.43301 0.44009 0.02346  -0.02351 0.04308  129 ASP A O   
1028 C  CB  . ASP A 129 ? 0.50387 0.46587 0.46371 0.02834  -0.03389 0.03791  129 ASP A CB  
1029 C  CG  . ASP A 129 ? 0.52295 0.47839 0.46957 0.02813  -0.03701 0.04139  129 ASP A CG  
1030 O  OD1 . ASP A 129 ? 0.52389 0.47026 0.46026 0.02434  -0.03292 0.04493  129 ASP A OD1 
1031 O  OD2 . ASP A 129 ? 0.54195 0.50224 0.48856 0.03192  -0.04366 0.04004  129 ASP A OD2 
1032 N  N   . ARG A 130 ? 0.34782 0.29714 0.29603 0.01433  -0.01817 0.04221  130 ARG A N   
1033 C  CA  . ARG A 130 ? 0.35035 0.29116 0.29317 0.01189  -0.01385 0.04432  130 ARG A CA  
1034 C  C   . ARG A 130 ? 0.34277 0.28619 0.29288 0.01159  -0.01077 0.04165  130 ARG A C   
1035 O  O   . ARG A 130 ? 0.34113 0.27737 0.28860 0.01070  -0.00830 0.04232  130 ARG A O   
1036 C  CB  . ARG A 130 ? 0.33531 0.27603 0.27353 0.00693  -0.01055 0.04506  130 ARG A CB  
1037 C  CG  . ARG A 130 ? 0.33351 0.27024 0.26230 0.00683  -0.01246 0.04734  130 ARG A CG  
1038 C  CD  . ARG A 130 ? 0.33311 0.27133 0.25947 0.00250  -0.00895 0.04671  130 ARG A CD  
1039 N  NE  . ARG A 130 ? 0.32752 0.27397 0.26163 0.00101  -0.00870 0.04372  130 ARG A NE  
1040 C  CZ  . ARG A 130 ? 0.32647 0.27458 0.26149 -0.00188 -0.00568 0.04270  130 ARG A CZ  
1041 N  NH1 . ARG A 130 ? 0.31220 0.25679 0.24261 -0.00363 -0.00261 0.04345  130 ARG A NH1 
1042 N  NH2 . ARG A 130 ? 0.32270 0.27600 0.26368 -0.00299 -0.00564 0.04085  130 ARG A NH2 
1043 N  N   . PHE A 131 ? 0.30573 0.25942 0.26472 0.01186  -0.01053 0.03826  131 PHE A N   
1044 C  CA  . PHE A 131 ? 0.30272 0.25982 0.26768 0.01219  -0.00772 0.03518  131 PHE A CA  
1045 C  C   . PHE A 131 ? 0.30510 0.26060 0.27442 0.01793  -0.01044 0.03342  131 PHE A C   
1046 O  O   . PHE A 131 ? 0.31100 0.26650 0.28119 0.02205  -0.01512 0.03408  131 PHE A O   
1047 C  CB  . PHE A 131 ? 0.30826 0.27659 0.27958 0.00967  -0.00531 0.03266  131 PHE A CB  
1048 C  CG  . PHE A 131 ? 0.30659 0.27487 0.27364 0.00493  -0.00259 0.03434  131 PHE A CG  
1049 C  CD1 . PHE A 131 ? 0.29957 0.26688 0.26428 0.00302  0.00063  0.03395  131 PHE A CD1 
1050 C  CD2 . PHE A 131 ? 0.31043 0.27964 0.27600 0.00292  -0.00378 0.03577  131 PHE A CD2 
1051 C  CE1 . PHE A 131 ? 0.29693 0.26423 0.25800 -0.00011 0.00223  0.03547  131 PHE A CE1 
1052 C  CE2 . PHE A 131 ? 0.30220 0.27038 0.26431 -0.00048 -0.00162 0.03709  131 PHE A CE2 
1053 C  CZ  . PHE A 131 ? 0.30208 0.26930 0.26199 -0.00163 0.00120  0.03719  131 PHE A CZ  
1054 N  N   . LEU A 132 ? 0.33080 0.28496 0.30289 0.01870  -0.00791 0.03067  132 LEU A N   
1055 C  CA  . LEU A 132 ? 0.32267 0.27345 0.29906 0.02464  -0.01015 0.02839  132 LEU A CA  
1056 C  C   . LEU A 132 ? 0.32568 0.28969 0.31343 0.02788  -0.01050 0.02328  132 LEU A C   
1057 O  O   . LEU A 132 ? 0.32494 0.28834 0.31802 0.03427  -0.01380 0.02111  132 LEU A O   
1058 C  CB  . LEU A 132 ? 0.32169 0.26422 0.29630 0.02387  -0.00717 0.02665  132 LEU A CB  
1059 C  CG  . LEU A 132 ? 0.32550 0.25627 0.29076 0.01965  -0.00581 0.03081  132 LEU A CG  
1060 C  CD1 . LEU A 132 ? 0.32734 0.25238 0.29293 0.01766  -0.00259 0.02761  132 LEU A CD1 
1061 C  CD2 . LEU A 132 ? 0.32744 0.24623 0.28587 0.02252  -0.00949 0.03603  132 LEU A CD2 
1062 N  N   . CYS A 133 ? 0.27937 0.25506 0.27103 0.02373  -0.00699 0.02132  133 CYS A N   
1063 C  CA  . CYS A 133 ? 0.27682 0.26659 0.27962 0.02521  -0.00588 0.01640  133 CYS A CA  
1064 C  C   . CYS A 133 ? 0.27773 0.27591 0.28296 0.02139  -0.00620 0.01763  133 CYS A C   
1065 O  O   . CYS A 133 ? 0.27961 0.27768 0.27988 0.01560  -0.00294 0.01999  133 CYS A O   
1066 C  CB  . CYS A 133 ? 0.27349 0.26906 0.27824 0.02296  0.00013  0.01242  133 CYS A CB  
1067 S  SG  . CYS A 133 ? 0.26970 0.28310 0.28845 0.02469  0.00315  0.00546  133 CYS A SG  
1068 N  N   . SER A 134 ? 0.27364 0.27882 0.28683 0.02489  -0.01054 0.01565  134 SER A N   
1069 C  CA  . SER A 134 ? 0.27445 0.28797 0.29148 0.02095  -0.01118 0.01559  134 SER A CA  
1070 C  C   . SER A 134 ? 0.27150 0.29665 0.29568 0.01555  -0.00453 0.01251  134 SER A C   
1071 O  O   . SER A 134 ? 0.26805 0.29808 0.29623 0.01633  -0.00027 0.00922  134 SER A O   
1072 C  CB  . SER A 134 ? 0.27631 0.29640 0.30140 0.02631  -0.01809 0.01301  134 SER A CB  
1073 O  OG  . SER A 134 ? 0.27245 0.30757 0.31258 0.02827  -0.01679 0.00655  134 SER A OG  
1074 N  N   . ARG A 135 ? 0.30210 0.33086 0.32704 0.00976  -0.00331 0.01359  135 ARG A N   
1075 C  CA  . ARG A 135 ? 0.30885 0.34703 0.33955 0.00375  0.00346  0.01163  135 ARG A CA  
1076 C  C   . ARG A 135 ? 0.31003 0.36386 0.35614 0.00582  0.00465  0.00491  135 ARG A C   
1077 O  O   . ARG A 135 ? 0.31883 0.38000 0.36862 0.00318  0.01149  0.00244  135 ARG A O   
1078 C  CB  . ARG A 135 ? 0.30155 0.33907 0.33127 -0.00268 0.00396  0.01373  135 ARG A CB  
1079 C  CG  . ARG A 135 ? 0.29984 0.32344 0.31560 -0.00489 0.00391  0.01959  135 ARG A CG  
1080 C  CD  . ARG A 135 ? 0.29453 0.31704 0.30988 -0.01164 0.00626  0.02114  135 ARG A CD  
1081 N  NE  . ARG A 135 ? 0.29491 0.31935 0.31474 -0.01178 0.00092  0.01914  135 ARG A NE  
1082 C  CZ  . ARG A 135 ? 0.29945 0.32352 0.32134 -0.01738 0.00181  0.01883  135 ARG A CZ  
1083 N  NH1 . ARG A 135 ? 0.30504 0.32544 0.32448 -0.02328 0.00795  0.02133  135 ARG A NH1 
1084 N  NH2 . ARG A 135 ? 0.29302 0.31966 0.31883 -0.01693 -0.00381 0.01590  135 ARG A NH2 
1085 N  N   . ALA A 136 ? 0.25690 0.31669 0.31198 0.01091  -0.00203 0.00158  136 ALA A N   
1086 C  CA  . ALA A 136 ? 0.25660 0.33310 0.32854 0.01394  -0.00172 -0.00582 136 ALA A CA  
1087 C  C   . ALA A 136 ? 0.26794 0.34413 0.34106 0.02037  -0.00033 -0.00855 136 ALA A C   
1088 O  O   . ALA A 136 ? 0.27204 0.36157 0.35635 0.02039  0.00469  -0.01452 136 ALA A O   
1089 C  CB  . ALA A 136 ? 0.24884 0.33184 0.32966 0.01890  -0.01074 -0.00884 136 ALA A CB  
1090 N  N   . GLN A 137 ? 0.28639 0.34742 0.34833 0.02548  -0.00421 -0.00474 137 GLN A N   
1091 C  CA  . GLN A 137 ? 0.30094 0.35946 0.36380 0.03156  -0.00326 -0.00777 137 GLN A CA  
1092 C  C   . GLN A 137 ? 0.30399 0.36443 0.36316 0.02655  0.00579  -0.00895 137 GLN A C   
1093 O  O   . GLN A 137 ? 0.30927 0.37693 0.37531 0.02977  0.00914  -0.01491 137 GLN A O   
1094 C  CB  . GLN A 137 ? 0.30812 0.34813 0.35920 0.03665  -0.00883 -0.00295 137 GLN A CB  
1095 C  CG  . GLN A 137 ? 0.30552 0.34324 0.35984 0.04451  -0.01811 -0.00265 137 GLN A CG  
1096 C  CD  . GLN A 137 ? 0.31484 0.33228 0.35497 0.04791  -0.02249 0.00361  137 GLN A CD  
1097 O  OE1 . GLN A 137 ? 0.30794 0.31451 0.33578 0.04246  -0.01956 0.00866  137 GLN A OE1 
1098 N  NE2 . GLN A 137 ? 0.32180 0.33398 0.36368 0.05702  -0.02945 0.00333  137 GLN A NE2 
1099 N  N   . PHE A 138 ? 0.24639 0.30053 0.29428 0.01920  0.00957  -0.00362 138 PHE A N   
1100 C  CA  . PHE A 138 ? 0.24885 0.30470 0.29123 0.01477  0.01745  -0.00416 138 PHE A CA  
1101 C  C   . PHE A 138 ? 0.24389 0.31648 0.29660 0.01070  0.02427  -0.00873 138 PHE A C   
1102 O  O   . PHE A 138 ? 0.24219 0.32142 0.29603 0.01077  0.03026  -0.01303 138 PHE A O   
1103 C  CB  . PHE A 138 ? 0.25284 0.29777 0.28074 0.00894  0.01882  0.00287  138 PHE A CB  
1104 C  CG  . PHE A 138 ? 0.25243 0.29659 0.27155 0.00602  0.02502  0.00297  138 PHE A CG  
1105 C  CD1 . PHE A 138 ? 0.25022 0.28627 0.26198 0.00915  0.02395  0.00228  138 PHE A CD1 
1106 C  CD2 . PHE A 138 ? 0.24054 0.29185 0.25827 -0.00003 0.03190  0.00362  138 PHE A CD2 
1107 C  CE1 . PHE A 138 ? 0.25041 0.28679 0.25359 0.00688  0.02876  0.00162  138 PHE A CE1 
1108 C  CE2 . PHE A 138 ? 0.23656 0.28693 0.24403 -0.00214 0.03707  0.00408  138 PHE A CE2 
1109 C  CZ  . PHE A 138 ? 0.24962 0.29323 0.24986 0.00162  0.03509  0.00274  138 PHE A CZ  
1110 N  N   . ALA A 139 ? 0.28398 0.36377 0.34423 0.00660  0.02392  -0.00831 139 ALA A N   
1111 C  CA  . ALA A 139 ? 0.27701 0.37330 0.34868 0.00156  0.03108  -0.01291 139 ALA A CA  
1112 C  C   . ALA A 139 ? 0.27728 0.38814 0.36428 0.00787  0.03156  -0.02193 139 ALA A C   
1113 O  O   . ALA A 139 ? 0.28169 0.40458 0.37401 0.00517  0.03985  -0.02665 139 ALA A O   
1114 C  CB  . ALA A 139 ? 0.26802 0.36912 0.34708 -0.00385 0.02953  -0.01193 139 ALA A CB  
1115 N  N   . ALA A 140 ? 0.28386 0.39351 0.37754 0.01670  0.02283  -0.02442 140 ALA A N   
1116 C  CA  . ALA A 140 ? 0.28245 0.40469 0.39116 0.02445  0.02211  -0.03323 140 ALA A CA  
1117 C  C   . ALA A 140 ? 0.29453 0.41301 0.39706 0.02737  0.02698  -0.03594 140 ALA A C   
1118 O  O   . ALA A 140 ? 0.30024 0.43310 0.41359 0.02909  0.03250  -0.04392 140 ALA A O   
1119 C  CB  . ALA A 140 ? 0.28300 0.40108 0.39711 0.03421  0.01066  -0.03386 140 ALA A CB  
1120 N  N   . TRP A 141 ? 0.26453 0.36471 0.35032 0.02779  0.02517  -0.03021 141 TRP A N   
1121 C  CA  . TRP A 141 ? 0.27744 0.37352 0.35683 0.03014  0.02919  -0.03343 141 TRP A CA  
1122 C  C   . TRP A 141 ? 0.27787 0.38252 0.35220 0.02249  0.03970  -0.03452 141 TRP A C   
1123 O  O   . TRP A 141 ? 0.28618 0.39786 0.36243 0.02450  0.04509  -0.04125 141 TRP A O   
1124 C  CB  . TRP A 141 ? 0.28175 0.35714 0.34561 0.03142  0.02459  -0.02745 141 TRP A CB  
1125 C  CG  . TRP A 141 ? 0.30087 0.37186 0.35666 0.03195  0.02886  -0.03073 141 TRP A CG  
1126 C  CD1 . TRP A 141 ? 0.30676 0.37430 0.36618 0.03916  0.02739  -0.03708 141 TRP A CD1 
1127 C  CD2 . TRP A 141 ? 0.29229 0.36172 0.33480 0.02528  0.03482  -0.02830 141 TRP A CD2 
1128 N  NE1 . TRP A 141 ? 0.30951 0.37427 0.35915 0.03687  0.03219  -0.03951 141 TRP A NE1 
1129 C  CE2 . TRP A 141 ? 0.30025 0.36660 0.33902 0.02864  0.03650  -0.03404 141 TRP A CE2 
1130 C  CE3 . TRP A 141 ? 0.28594 0.35561 0.31902 0.01727  0.03845  -0.02192 141 TRP A CE3 
1131 C  CZ2 . TRP A 141 ? 0.29866 0.36368 0.32428 0.02431  0.04122  -0.03384 141 TRP A CZ2 
1132 C  CZ3 . TRP A 141 ? 0.29203 0.35924 0.31164 0.01354  0.04303  -0.02088 141 TRP A CZ3 
1133 C  CH2 . TRP A 141 ? 0.29453 0.36018 0.31035 0.01709  0.04416  -0.02692 141 TRP A CH2 
1134 N  N   . ALA A 142 ? 0.30217 0.40545 0.36902 0.01392  0.04278  -0.02792 142 ALA A N   
1135 C  CA  . ALA A 142 ? 0.30198 0.41012 0.36049 0.00642  0.05249  -0.02688 142 ALA A CA  
1136 C  C   . ALA A 142 ? 0.29262 0.42067 0.36492 0.00285  0.06057  -0.03300 142 ALA A C   
1137 O  O   . ALA A 142 ? 0.29430 0.42780 0.35984 -0.00252 0.06989  -0.03349 142 ALA A O   
1138 C  CB  . ALA A 142 ? 0.29617 0.39336 0.34125 -0.00089 0.05251  -0.01707 142 ALA A CB  
1139 N  N   . GLU A 143 ? 0.24372 0.38325 0.33486 0.00563  0.05733  -0.03783 143 GLU A N   
1140 C  CA  . GLU A 143 ? 0.24124 0.40170 0.34823 0.00136  0.06512  -0.04430 143 GLU A CA  
1141 C  C   . GLU A 143 ? 0.24634 0.41871 0.35706 0.00429  0.07275  -0.05299 143 GLU A C   
1142 O  O   . GLU A 143 ? 0.24817 0.41925 0.36260 0.01381  0.06834  -0.05864 143 GLU A O   
1143 C  CB  . GLU A 143 ? 0.23616 0.40769 0.36408 0.00560  0.05817  -0.04917 143 GLU A CB  
1144 C  CG  . GLU A 143 ? 0.23498 0.42750 0.38018 -0.00169 0.06537  -0.05431 143 GLU A CG  
1145 C  CD  . GLU A 143 ? 0.23171 0.44172 0.40160 0.00556  0.05931  -0.06372 143 GLU A CD  
1146 O  OE1 . GLU A 143 ? 0.22860 0.44780 0.41092 0.00123  0.05722  -0.06472 143 GLU A OE1 
1147 O  OE2 . GLU A 143 ? 0.24335 0.45786 0.42053 0.01588  0.05625  -0.07052 143 GLU A OE2 
1148 N  N   . GLY A 144 ? 0.25274 0.43592 0.36178 -0.00409 0.08462  -0.05407 144 GLY A N   
1149 C  CA  . GLY A 144 ? 0.26040 0.45714 0.37266 -0.00251 0.09352  -0.06289 144 GLY A CA  
1150 C  C   . GLY A 144 ? 0.26756 0.45280 0.35878 -0.00103 0.09591  -0.06126 144 GLY A C   
1151 O  O   . GLY A 144 ? 0.27579 0.47200 0.36694 -0.00041 0.10418  -0.06868 144 GLY A O   
1152 N  N   . ARG A 145 ? 0.31721 0.48195 0.39108 -0.00047 0.08907  -0.05264 145 ARG A N   
1153 C  CA  . ARG A 145 ? 0.32326 0.47750 0.37786 0.00107  0.08997  -0.05165 145 ARG A CA  
1154 C  C   . ARG A 145 ? 0.32209 0.47423 0.35811 -0.00838 0.09855  -0.04467 145 ARG A C   
1155 O  O   . ARG A 145 ? 0.32803 0.47018 0.35579 -0.01408 0.09685  -0.03477 145 ARG A O   
1156 C  CB  . ARG A 145 ? 0.33412 0.46873 0.38029 0.00595  0.07873  -0.04639 145 ARG A CB  
1157 C  CG  . ARG A 145 ? 0.33535 0.46836 0.39572 0.01584  0.07044  -0.05248 145 ARG A CG  
1158 C  CD  . ARG A 145 ? 0.34112 0.45411 0.39096 0.01945  0.06133  -0.04742 145 ARG A CD  
1159 N  NE  . ARG A 145 ? 0.35274 0.46125 0.41499 0.02772  0.05284  -0.05010 145 ARG A NE  
1160 C  CZ  . ARG A 145 ? 0.35803 0.46664 0.42759 0.03587  0.05099  -0.05839 145 ARG A CZ  
1161 N  NH1 . ARG A 145 ? 0.36318 0.47711 0.42971 0.03687  0.05705  -0.06595 145 ARG A NH1 
1162 N  NH2 . ARG A 145 ? 0.37011 0.47262 0.44949 0.04350  0.04274  -0.05917 145 ARG A NH2 
1163 N  N   . ARG A 146 ? 0.46510 0.62593 0.49368 -0.00963 0.10766  -0.04984 146 ARG A N   
1164 C  CA  . ARG A 146 ? 0.47379 0.63244 0.48266 -0.01818 0.11630  -0.04293 146 ARG A CA  
1165 C  C   . ARG A 146 ? 0.47643 0.61580 0.46268 -0.01799 0.11009  -0.03394 146 ARG A C   
1166 O  O   . ARG A 146 ? 0.48253 0.61564 0.45176 -0.02459 0.11440  -0.02521 146 ARG A O   
1167 C  CB  . ARG A 146 ? 0.46922 0.64242 0.47427 -0.01898 0.12757  -0.05126 146 ARG A CB  
1168 C  CG  . ARG A 146 ? 0.46642 0.66101 0.49251 -0.02199 0.13672  -0.05893 146 ARG A CG  
1169 C  CD  . ARG A 146 ? 0.46947 0.67765 0.48709 -0.02610 0.15067  -0.06433 146 ARG A CD  
1170 N  NE  . ARG A 146 ? 0.47183 0.70155 0.50992 -0.03080 0.16082  -0.07105 146 ARG A NE  
1171 C  CZ  . ARG A 146 ? 0.46335 0.69671 0.50357 -0.04152 0.16833  -0.06469 146 ARG A CZ  
1172 N  NH1 . ARG A 146 ? 0.45871 0.67438 0.48139 -0.04818 0.16670  -0.05103 146 ARG A NH1 
1173 N  NH2 . ARG A 146 ? 0.45253 0.70789 0.51385 -0.04568 0.17779  -0.07273 146 ARG A NH2 
1174 N  N   . GLU A 147 ? 0.42739 0.55718 0.41339 -0.01061 0.10019  -0.03594 147 GLU A N   
1175 C  CA  . GLU A 147 ? 0.43166 0.54445 0.40080 -0.01030 0.09300  -0.02795 147 GLU A CA  
1176 C  C   . GLU A 147 ? 0.43287 0.53667 0.41171 -0.00376 0.08200  -0.02940 147 GLU A C   
1177 O  O   . GLU A 147 ? 0.42660 0.53523 0.41876 0.00228  0.07995  -0.03804 147 GLU A O   
1178 C  CB  . GLU A 147 ? 0.43777 0.54881 0.38681 -0.00962 0.09546  -0.02961 147 GLU A CB  
1179 C  CG  . GLU A 147 ? 0.45577 0.56328 0.40559 -0.00224 0.08902  -0.03765 147 GLU A CG  
1180 C  CD  . GLU A 147 ? 0.48409 0.59666 0.41882 -0.00146 0.09381  -0.04379 147 GLU A CD  
1181 O  OE1 . GLU A 147 ? 0.47781 0.58956 0.41474 0.00415  0.09009  -0.05268 147 GLU A OE1 
1182 O  OE2 . GLU A 147 ? 0.48108 0.59766 0.40092 -0.00659 0.10132  -0.03971 147 GLU A OE2 
1183 N  N   . LEU A 148 ? 0.30276 0.39297 0.27468 -0.00494 0.07525  -0.02074 148 LEU A N   
1184 C  CA  . LEU A 148 ? 0.30259 0.38307 0.28192 -0.00020 0.06560  -0.02025 148 LEU A CA  
1185 C  C   . LEU A 148 ? 0.30904 0.37954 0.27614 0.00251  0.06071  -0.02063 148 LEU A C   
1186 O  O   . LEU A 148 ? 0.30353 0.36683 0.25665 -0.00030 0.05919  -0.01403 148 LEU A O   
1187 C  CB  . LEU A 148 ? 0.29196 0.36553 0.27348 -0.00355 0.06182  -0.01152 148 LEU A CB  
1188 C  CG  . LEU A 148 ? 0.29566 0.37893 0.28720 -0.00838 0.06721  -0.01042 148 LEU A CG  
1189 C  CD1 . LEU A 148 ? 0.27959 0.35439 0.27150 -0.01184 0.06301  -0.00232 148 LEU A CD1 
1190 C  CD2 . LEU A 148 ? 0.28996 0.38559 0.30104 -0.00411 0.06755  -0.01926 148 LEU A CD2 
1191 N  N   . ARG A 149 ? 0.39634 0.46639 0.36949 0.00808  0.05805  -0.02876 149 ARG A N   
1192 C  CA  . ARG A 149 ? 0.40303 0.46477 0.36720 0.01023  0.05370  -0.03115 149 ARG A CA  
1193 C  C   . ARG A 149 ? 0.40902 0.45893 0.38041 0.01314  0.04578  -0.02957 149 ARG A C   
1194 O  O   . ARG A 149 ? 0.40911 0.45871 0.39373 0.01681  0.04392  -0.03206 149 ARG A O   
1195 C  CB  . ARG A 149 ? 0.45087 0.51933 0.41512 0.01364  0.05720  -0.04227 149 ARG A CB  
1196 C  CG  . ARG A 149 ? 0.45041 0.53110 0.40581 0.01063  0.06600  -0.04428 149 ARG A CG  
1197 C  CD  . ARG A 149 ? 0.45745 0.54146 0.40468 0.01310  0.06780  -0.05387 149 ARG A CD  
1198 N  NE  . ARG A 149 ? 0.45962 0.54714 0.38707 0.00918  0.07187  -0.05073 149 ARG A NE  
1199 C  CZ  . ARG A 149 ? 0.46435 0.54627 0.37730 0.00921  0.06748  -0.05032 149 ARG A CZ  
1200 N  NH1 . ARG A 149 ? 0.46657 0.53967 0.38351 0.01193  0.05970  -0.05331 149 ARG A NH1 
1201 N  NH2 . ARG A 149 ? 0.46792 0.55322 0.36179 0.00635  0.07096  -0.04682 149 ARG A NH2 
1202 N  N   . MET A 150 ? 0.42197 0.46250 0.38438 0.01164  0.04119  -0.02547 150 MET A N   
1203 C  CA  . MET A 150 ? 0.41648 0.44550 0.38399 0.01300  0.03473  -0.02275 150 MET A CA  
1204 C  C   . MET A 150 ? 0.42980 0.45397 0.40567 0.01773  0.03263  -0.03045 150 MET A C   
1205 O  O   . MET A 150 ? 0.43166 0.44730 0.41470 0.01987  0.02861  -0.02839 150 MET A O   
1206 C  CB  . MET A 150 ? 0.41174 0.43408 0.36886 0.01023  0.03116  -0.01836 150 MET A CB  
1207 C  CG  . MET A 150 ? 0.40147 0.41398 0.36194 0.00953  0.02622  -0.01228 150 MET A CG  
1208 S  SD  . MET A 150 ? 0.43384 0.43536 0.40025 0.01190  0.02212  -0.01712 150 MET A SD  
1209 C  CE  . MET A 150 ? 0.41702 0.42218 0.37708 0.01176  0.02315  -0.02605 150 MET A CE  
1210 N  N   . GLU A 151 ? 0.54685 0.57540 0.52114 0.01957  0.03530  -0.03933 151 GLU A N   
1211 C  CA  . GLU A 151 ? 0.55095 0.57262 0.53259 0.02399  0.03319  -0.04719 151 GLU A CA  
1212 C  C   . GLU A 151 ? 0.55824 0.58029 0.55348 0.02921  0.03293  -0.04890 151 GLU A C   
1213 O  O   . GLU A 151 ? 0.56950 0.57981 0.57089 0.03257  0.02858  -0.04892 151 GLU A O   
1214 C  CB  . GLU A 151 ? 0.59631 0.62371 0.57329 0.02493  0.03638  -0.05748 151 GLU A CB  
1215 C  CG  . GLU A 151 ? 0.59144 0.63374 0.56165 0.02325  0.04283  -0.05868 151 GLU A CG  
1216 C  CD  . GLU A 151 ? 0.58717 0.63141 0.54125 0.01869  0.04282  -0.05475 151 GLU A CD  
1217 O  OE1 . GLU A 151 ? 0.59575 0.64515 0.54119 0.01881  0.04480  -0.06179 151 GLU A OE1 
1218 O  OE2 . GLU A 151 ? 0.57532 0.61591 0.52511 0.01549  0.04046  -0.04495 151 GLU A OE2 
1219 N  N   . PHE A 152 ? 0.45098 0.48647 0.45111 0.03001  0.03752  -0.05037 152 PHE A N   
1220 C  CA  . PHE A 152 ? 0.44463 0.48311 0.45932 0.03559  0.03662  -0.05279 152 PHE A CA  
1221 C  C   . PHE A 152 ? 0.45466 0.48650 0.47279 0.03532  0.03140  -0.04364 152 PHE A C   
1222 O  O   . PHE A 152 ? 0.45966 0.48605 0.48708 0.04100  0.02707  -0.04428 152 PHE A O   
1223 C  CB  . PHE A 152 ? 0.44469 0.50159 0.46513 0.03561  0.04352  -0.05749 152 PHE A CB  
1224 C  CG  . PHE A 152 ? 0.46010 0.52498 0.47363 0.03468  0.04973  -0.06550 152 PHE A CG  
1225 C  CD1 . PHE A 152 ? 0.46349 0.53586 0.46437 0.02831  0.05504  -0.06214 152 PHE A CD1 
1226 C  CD2 . PHE A 152 ? 0.46616 0.53017 0.48483 0.04043  0.05011  -0.07643 152 PHE A CD2 
1227 C  CE1 . PHE A 152 ? 0.46610 0.54586 0.45834 0.02764  0.06060  -0.06932 152 PHE A CE1 
1228 C  CE2 . PHE A 152 ? 0.46909 0.54103 0.48047 0.03964  0.05581  -0.08468 152 PHE A CE2 
1229 C  CZ  . PHE A 152 ? 0.47659 0.55686 0.47410 0.03320  0.06105  -0.08101 152 PHE A CZ  
1230 N  N   . PHE A 153 ? 0.28510 0.31694 0.29524 0.02925  0.03146  -0.03525 153 PHE A N   
1231 C  CA  . PHE A 153 ? 0.28466 0.30927 0.29626 0.02867  0.02639  -0.02713 153 PHE A CA  
1232 C  C   . PHE A 153 ? 0.28881 0.29654 0.29709 0.03031  0.02099  -0.02494 153 PHE A C   
1233 O  O   . PHE A 153 ? 0.29643 0.29657 0.30907 0.03360  0.01631  -0.02173 153 PHE A O   
1234 C  CB  . PHE A 153 ? 0.27150 0.29888 0.27503 0.02193  0.02798  -0.01955 153 PHE A CB  
1235 C  CG  . PHE A 153 ? 0.26794 0.28749 0.27126 0.02089  0.02297  -0.01188 153 PHE A CG  
1236 C  CD1 . PHE A 153 ? 0.26567 0.28978 0.27830 0.02283  0.02093  -0.01068 153 PHE A CD1 
1237 C  CD2 . PHE A 153 ? 0.26346 0.27228 0.25762 0.01805  0.02028  -0.00665 153 PHE A CD2 
1238 C  CE1 . PHE A 153 ? 0.26911 0.28632 0.28024 0.02198  0.01622  -0.00426 153 PHE A CE1 
1239 C  CE2 . PHE A 153 ? 0.25396 0.25617 0.24726 0.01708  0.01633  -0.00024 153 PHE A CE2 
1240 C  CZ  . PHE A 153 ? 0.26010 0.26607 0.26105 0.01906  0.01426  0.00104  153 PHE A CZ  
1241 N  N   . TYR A 154 ? 0.26111 0.26303 0.26139 0.02781  0.02164  -0.02679 154 TYR A N   
1242 C  CA  . TYR A 154 ? 0.26494 0.25121 0.26261 0.02787  0.01770  -0.02526 154 TYR A CA  
1243 C  C   . TYR A 154 ? 0.27396 0.25145 0.27957 0.03439  0.01535  -0.02975 154 TYR A C   
1244 O  O   . TYR A 154 ? 0.27766 0.24133 0.28310 0.03571  0.01143  -0.02542 154 TYR A O   
1245 C  CB  . TYR A 154 ? 0.26777 0.25255 0.25762 0.02389  0.01905  -0.02855 154 TYR A CB  
1246 C  CG  . TYR A 154 ? 0.27367 0.24355 0.26268 0.02303  0.01623  -0.02923 154 TYR A CG  
1247 C  CD1 . TYR A 154 ? 0.27145 0.23088 0.25894 0.02112  0.01330  -0.02166 154 TYR A CD1 
1248 C  CD2 . TYR A 154 ? 0.28278 0.24907 0.27243 0.02357  0.01700  -0.03788 154 TYR A CD2 
1249 C  CE1 . TYR A 154 ? 0.27845 0.22412 0.26514 0.01924  0.01188  -0.02209 154 TYR A CE1 
1250 C  CE2 . TYR A 154 ? 0.28955 0.24171 0.27933 0.02165  0.01506  -0.03884 154 TYR A CE2 
1251 C  CZ  . TYR A 154 ? 0.28748 0.22932 0.27581 0.01922  0.01283  -0.03061 154 TYR A CZ  
1252 O  OH  . TYR A 154 ? 0.29574 0.22341 0.28419 0.01628  0.01201  -0.03138 154 TYR A OH  
1253 N  N   . ARG A 155 ? 0.40456 0.38938 0.41667 0.03880  0.01787  -0.03837 155 ARG A N   
1254 C  CA  . ARG A 155 ? 0.41073 0.38704 0.43130 0.04627  0.01535  -0.04322 155 ARG A CA  
1255 C  C   . ARG A 155 ? 0.41418 0.38925 0.44134 0.05123  0.01103  -0.03796 155 ARG A C   
1256 O  O   . ARG A 155 ? 0.41694 0.37706 0.44560 0.05591  0.00643  -0.03590 155 ARG A O   
1257 C  CB  . ARG A 155 ? 0.41394 0.40093 0.44097 0.05032  0.01941  -0.05452 155 ARG A CB  
1258 C  CG  . ARG A 155 ? 0.42566 0.40793 0.44748 0.04822  0.02158  -0.06203 155 ARG A CG  
1259 C  CD  . ARG A 155 ? 0.42459 0.42398 0.44619 0.04802  0.02757  -0.07075 155 ARG A CD  
1260 N  NE  . ARG A 155 ? 0.43866 0.43398 0.46336 0.05195  0.02871  -0.08242 155 ARG A NE  
1261 C  CZ  . ARG A 155 ? 0.44936 0.45788 0.47719 0.05476  0.03368  -0.09257 155 ARG A CZ  
1262 N  NH1 . ARG A 155 ? 0.45007 0.47695 0.47840 0.05361  0.03862  -0.09218 155 ARG A NH1 
1263 N  NH2 . ARG A 155 ? 0.45266 0.45560 0.48325 0.05848  0.03420  -0.10372 155 ARG A NH2 
1264 N  N   . GLU A 156 ? 0.42029 0.41049 0.45097 0.05016  0.01230  -0.03574 156 GLU A N   
1265 C  CA  . GLU A 156 ? 0.41412 0.40523 0.45113 0.05442  0.00751  -0.03131 156 GLU A CA  
1266 C  C   . GLU A 156 ? 0.40705 0.38307 0.43525 0.05209  0.00276  -0.02159 156 GLU A C   
1267 O  O   . GLU A 156 ? 0.40578 0.37246 0.43579 0.05770  -0.00282 -0.01845 156 GLU A O   
1268 C  CB  . GLU A 156 ? 0.40651 0.41714 0.44898 0.05167  0.01049  -0.03126 156 GLU A CB  
1269 C  CG  . GLU A 156 ? 0.40885 0.42626 0.46275 0.05758  0.00586  -0.03112 156 GLU A CG  
1270 C  CD  . GLU A 156 ? 0.41890 0.44520 0.48692 0.06598  0.00618  -0.04082 156 GLU A CD  
1271 O  OE1 . GLU A 156 ? 0.41743 0.46217 0.49342 0.06446  0.01204  -0.04708 156 GLU A OE1 
1272 O  OE2 . GLU A 156 ? 0.43185 0.44636 0.50290 0.07417  0.00084  -0.04221 156 GLU A OE2 
1273 N  N   . MET A 157 ? 0.34013 0.31381 0.35829 0.04423  0.00488  -0.01683 157 MET A N   
1274 C  CA  . MET A 157 ? 0.34334 0.30410 0.35317 0.04144  0.00148  -0.00835 157 MET A CA  
1275 C  C   . MET A 157 ? 0.34489 0.28638 0.35129 0.04373  -0.00078 -0.00780 157 MET A C   
1276 O  O   . MET A 157 ? 0.34140 0.27063 0.34287 0.04453  -0.00446 -0.00113 157 MET A O   
1277 C  CB  . MET A 157 ? 0.33212 0.29586 0.33357 0.03316  0.00449  -0.00473 157 MET A CB  
1278 C  CG  . MET A 157 ? 0.33092 0.30911 0.33362 0.03014  0.00624  -0.00274 157 MET A CG  
1279 S  SD  . MET A 157 ? 0.31211 0.29158 0.31812 0.03249  0.00130  0.00271  157 MET A SD  
1280 C  CE  . MET A 157 ? 0.29706 0.25774 0.29268 0.03137  -0.00240 0.00981  157 MET A CE  
1281 N  N   . ARG A 158 ? 0.29007 0.22800 0.29831 0.04440  0.00165  -0.01478 158 ARG A N   
1282 C  CA  . ARG A 158 ? 0.30447 0.22264 0.31054 0.04621  -0.00005 -0.01492 158 ARG A CA  
1283 C  C   . ARG A 158 ? 0.31614 0.22559 0.32723 0.05558  -0.00490 -0.01410 158 ARG A C   
1284 O  O   . ARG A 158 ? 0.32870 0.21917 0.33456 0.05708  -0.00787 -0.00879 158 ARG A O   
1285 C  CB  . ARG A 158 ? 0.30959 0.22688 0.31749 0.04480  0.00349  -0.02410 158 ARG A CB  
1286 C  CG  . ARG A 158 ? 0.30254 0.22398 0.30392 0.03599  0.00680  -0.02456 158 ARG A CG  
1287 C  CD  . ARG A 158 ? 0.30970 0.21410 0.30545 0.03095  0.00624  -0.02058 158 ARG A CD  
1288 N  NE  . ARG A 158 ? 0.32588 0.21458 0.32452 0.03320  0.00610  -0.02590 158 ARG A NE  
1289 C  CZ  . ARG A 158 ? 0.33063 0.22011 0.33161 0.03136  0.00839  -0.03536 158 ARG A CZ  
1290 N  NH1 . ARG A 158 ? 0.32101 0.22641 0.32056 0.02748  0.01073  -0.04017 158 ARG A NH1 
1291 N  NH2 . ARG A 158 ? 0.34710 0.22025 0.35128 0.03366  0.00807  -0.04019 158 ARG A NH2 
1292 N  N   . ARG A 159 ? 0.46351 0.38668 0.48464 0.06207  -0.00575 -0.01923 159 ARG A N   
1293 C  CA  . ARG A 159 ? 0.45349 0.37073 0.48074 0.07229  -0.01144 -0.01897 159 ARG A CA  
1294 C  C   . ARG A 159 ? 0.44556 0.36156 0.46835 0.07332  -0.01666 -0.00968 159 ARG A C   
1295 O  O   . ARG A 159 ? 0.45655 0.35716 0.47600 0.07939  -0.02224 -0.00485 159 ARG A O   
1296 C  CB  . ARG A 159 ? 0.46118 0.39634 0.50252 0.07886  -0.01049 -0.02853 159 ARG A CB  
1297 C  CG  . ARG A 159 ? 0.46759 0.40782 0.51248 0.07735  -0.00455 -0.03869 159 ARG A CG  
1298 C  CD  . ARG A 159 ? 0.48145 0.42457 0.53918 0.08787  -0.00571 -0.04820 159 ARG A CD  
1299 N  NE  . ARG A 159 ? 0.48548 0.44637 0.54949 0.08653  0.00092  -0.05881 159 ARG A NE  
1300 C  CZ  . ARG A 159 ? 0.49469 0.45223 0.56328 0.09060  0.00322  -0.06894 159 ARG A CZ  
1301 N  NH1 . ARG A 159 ? 0.48640 0.42235 0.55496 0.09618  -0.00057 -0.06998 159 ARG A NH1 
1302 N  NH2 . ARG A 159 ? 0.48037 0.45588 0.55298 0.08888  0.00975  -0.07831 159 ARG A NH2 
1303 N  N   . LYS A 160 ? 0.51580 0.44705 0.53767 0.06764  -0.01508 -0.00713 160 LYS A N   
1304 C  CA  . LYS A 160 ? 0.50519 0.43646 0.52276 0.06814  -0.01998 0.00053  160 LYS A CA  
1305 C  C   . LYS A 160 ? 0.50391 0.41492 0.50712 0.06462  -0.02133 0.00932  160 LYS A C   
1306 O  O   . LYS A 160 ? 0.50351 0.40327 0.50142 0.06964  -0.02701 0.01511  160 LYS A O   
1307 C  CB  . LYS A 160 ? 0.49450 0.44466 0.51402 0.06172  -0.01718 0.00075  160 LYS A CB  
1308 C  CG  . LYS A 160 ? 0.48277 0.43654 0.50078 0.06300  -0.02260 0.00616  160 LYS A CG  
1309 C  CD  . LYS A 160 ? 0.47144 0.43132 0.48323 0.05383  -0.01956 0.01017  160 LYS A CD  
1310 C  CE  . LYS A 160 ? 0.46910 0.44562 0.48762 0.04859  -0.01324 0.00499  160 LYS A CE  
1311 N  NZ  . LYS A 160 ? 0.46839 0.46221 0.50124 0.05271  -0.01382 -0.00118 160 LYS A NZ  
1312 N  N   . THR A 161 ? 0.35624 0.26292 0.35277 0.05602  -0.01608 0.01029  161 THR A N   
1313 C  CA  . THR A 161 ? 0.35533 0.24493 0.33945 0.05133  -0.01591 0.01784  161 THR A CA  
1314 C  C   . THR A 161 ? 0.36834 0.23605 0.34908 0.05443  -0.01671 0.01862  161 THR A C   
1315 O  O   . THR A 161 ? 0.36404 0.21518 0.33407 0.05213  -0.01727 0.02599  161 THR A O   
1316 C  CB  . THR A 161 ? 0.34170 0.23599 0.32182 0.04131  -0.01026 0.01768  161 THR A CB  
1317 O  OG1 . THR A 161 ? 0.35636 0.25229 0.34141 0.03964  -0.00641 0.01018  161 THR A OG1 
1318 C  CG2 . THR A 161 ? 0.33579 0.24850 0.31781 0.03818  -0.00947 0.01799  161 THR A CG2 
1319 N  N   . GLY A 162 ? 0.36339 0.28169 0.39399 0.01871  0.07774  0.03773  162 GLY A N   
1320 C  CA  . GLY A 162 ? 0.36289 0.26636 0.38797 0.02025  0.08259  0.03986  162 GLY A CA  
1321 C  C   . GLY A 162 ? 0.37313 0.26875 0.39303 0.01271  0.08744  0.03944  162 GLY A C   
1322 O  O   . GLY A 162 ? 0.37754 0.25979 0.39468 0.01320  0.09164  0.04175  162 GLY A O   
1323 N  N   . LEU A 163 ? 0.36174 0.26531 0.38205 0.00586  0.08695  0.03665  163 LEU A N   
1324 C  CA  . LEU A 163 ? 0.36649 0.26469 0.38361 -0.00129 0.09064  0.03555  163 LEU A CA  
1325 C  C   . LEU A 163 ? 0.37571 0.26889 0.39655 -0.00407 0.09470  0.02984  163 LEU A C   
1326 O  O   . LEU A 163 ? 0.38822 0.28871 0.41294 -0.00337 0.09446  0.02531  163 LEU A O   
1327 C  CB  . LEU A 163 ? 0.36048 0.26962 0.37779 -0.00675 0.08819  0.03398  163 LEU A CB  
1328 C  CG  . LEU A 163 ? 0.35668 0.26906 0.36954 -0.00536 0.08476  0.03789  163 LEU A CG  
1329 C  CD1 . LEU A 163 ? 0.33391 0.25853 0.35091 -0.00914 0.08124  0.03540  163 LEU A CD1 
1330 C  CD2 . LEU A 163 ? 0.33541 0.23865 0.34176 -0.00753 0.08864  0.04145  163 LEU A CD2 
1331 N  N   . LEU A 164 ? 0.32877 0.20990 0.34915 -0.00701 0.09865  0.02977  164 LEU A N   
1332 C  CA  . LEU A 164 ? 0.33496 0.21028 0.36001 -0.00979 0.10175  0.02247  164 LEU A CA  
1333 C  C   . LEU A 164 ? 0.34111 0.21433 0.36952 -0.00337 0.10234  0.01958  164 LEU A C   
1334 O  O   . LEU A 164 ? 0.34125 0.21828 0.37206 -0.00385 0.10311  0.01171  164 LEU A O   
1335 C  CB  . LEU A 164 ? 0.32567 0.21144 0.35096 -0.01587 0.10051  0.01561  164 LEU A CB  
1336 C  CG  . LEU A 164 ? 0.32138 0.20824 0.34587 -0.02263 0.10037  0.01669  164 LEU A CG  
1337 C  CD1 . LEU A 164 ? 0.31411 0.21159 0.33884 -0.02731 0.09842  0.00971  164 LEU A CD1 
1338 C  CD2 . LEU A 164 ? 0.33355 0.20599 0.36223 -0.02539 0.10454  0.01767  164 LEU A CD2 
1339 N  N   . MET A 165 ? 0.36816 0.23610 0.39622 0.00353  0.10187  0.02587  165 MET A N   
1340 C  CA  . MET A 165 ? 0.36899 0.23448 0.40151 0.01071  0.10235  0.02409  165 MET A CA  
1341 C  C   . MET A 165 ? 0.37150 0.21905 0.40596 0.01447  0.10552  0.02814  165 MET A C   
1342 O  O   . MET A 165 ? 0.37715 0.21810 0.40719 0.01608  0.10573  0.03700  165 MET A O   
1343 C  CB  . MET A 165 ? 0.35938 0.23615 0.39236 0.01691  0.09806  0.02788  165 MET A CB  
1344 C  CG  . MET A 165 ? 0.36140 0.25510 0.39522 0.01335  0.09542  0.02557  165 MET A CG  
1345 S  SD  . MET A 165 ? 0.37961 0.28171 0.41748 0.01173  0.09876  0.01678  165 MET A SD  
1346 C  CE  . MET A 165 ? 0.37489 0.27471 0.42006 0.02127  0.10015  0.01552  165 MET A CE  
1347 N  N   . ASP A 166 ? 0.48019 0.31981 0.52117 0.01637  0.10834  0.02186  166 ASP A N   
1348 C  CA  . ASP A 166 ? 0.49052 0.31259 0.53617 0.02149  0.11141  0.02564  166 ASP A CA  
1349 C  C   . ASP A 166 ? 0.48978 0.31540 0.53858 0.03118  0.10962  0.02548  166 ASP A C   
1350 O  O   . ASP A 166 ? 0.49697 0.32592 0.55122 0.03282  0.11063  0.01638  166 ASP A O   
1351 C  CB  . ASP A 166 ? 0.49318 0.30262 0.54695 0.01677  0.11556  0.01742  166 ASP A CB  
1352 C  CG  . ASP A 166 ? 0.49915 0.30407 0.55313 0.00752  0.11755  0.01849  166 ASP A CG  
1353 O  OD1 . ASP A 166 ? 0.48739 0.29296 0.53519 0.00660  0.11760  0.02868  166 ASP A OD1 
1354 O  OD2 . ASP A 166 ? 0.50657 0.30806 0.56743 0.00160  0.11890  0.00850  166 ASP A OD2 
1355 N  N   . GLY A 167 ? 0.54336 0.36941 0.58870 0.03818  0.10679  0.03509  167 GLY A N   
1356 C  CA  . GLY A 167 ? 0.53744 0.37032 0.58719 0.04740  0.10388  0.03484  167 GLY A CA  
1357 C  C   . GLY A 167 ? 0.53782 0.39112 0.58917 0.04532  0.10100  0.02901  167 GLY A C   
1358 O  O   . GLY A 167 ? 0.53283 0.39646 0.57926 0.04038  0.09823  0.03069  167 GLY A O   
1359 N  N   . ASP A 168 ? 0.57929 0.43845 0.63852 0.04934  0.10229  0.02241  168 ASP A N   
1360 C  CA  . ASP A 168 ? 0.58093 0.45910 0.64350 0.04760  0.10161  0.01760  168 ASP A CA  
1361 C  C   . ASP A 168 ? 0.58708 0.46817 0.64750 0.04097  0.10583  0.00892  168 ASP A C   
1362 O  O   . ASP A 168 ? 0.60011 0.49574 0.66327 0.04091  0.10725  0.00485  168 ASP A O   
1363 C  CB  . ASP A 168 ? 0.58077 0.46668 0.65378 0.05658  0.10122  0.01616  168 ASP A CB  
1364 C  CG  . ASP A 168 ? 0.60558 0.48469 0.68357 0.06030  0.10653  0.00831  168 ASP A CG  
1365 O  OD1 . ASP A 168 ? 0.62884 0.49172 0.70384 0.05836  0.10913  0.00576  168 ASP A OD1 
1366 O  OD2 . ASP A 168 ? 0.60607 0.49640 0.69230 0.06525  0.10833  0.00421  168 ASP A OD2 
1367 N  N   . GLN A 169 ? 0.53848 0.40681 0.59460 0.03578  0.10789  0.00616  169 GLN A N   
1368 C  CA  . GLN A 169 ? 0.53909 0.41004 0.59274 0.03027  0.11054  -0.00333 169 GLN A CA  
1369 C  C   . GLN A 169 ? 0.54309 0.41410 0.59022 0.02120  0.10905  -0.00158 169 GLN A C   
1370 O  O   . GLN A 169 ? 0.53796 0.39918 0.58359 0.01906  0.10809  0.00511  169 GLN A O   
1371 C  CB  . GLN A 169 ? 0.54603 0.40230 0.60414 0.03232  0.11377  -0.01166 169 GLN A CB  
1372 C  CG  . GLN A 169 ? 0.56120 0.41976 0.62576 0.04119  0.11608  -0.01694 169 GLN A CG  
1373 C  CD  . GLN A 169 ? 0.57096 0.44839 0.63307 0.04207  0.11793  -0.02330 169 GLN A CD  
1374 O  OE1 . GLN A 169 ? 0.56824 0.45827 0.63407 0.04684  0.11831  -0.01964 169 GLN A OE1 
1375 N  NE2 . GLN A 169 ? 0.58000 0.46009 0.63643 0.03786  0.11921  -0.03267 169 GLN A NE2 
1376 N  N   . PRO A 170 ? 0.36151 0.24391 0.40453 0.01646  0.10915  -0.00693 170 PRO A N   
1377 C  CA  . PRO A 170 ? 0.35475 0.23806 0.39280 0.00827  0.10742  -0.00576 170 PRO A CA  
1378 C  C   . PRO A 170 ? 0.36598 0.23481 0.40615 0.00402  0.10871  -0.01115 170 PRO A C   
1379 O  O   . PRO A 170 ? 0.37829 0.23960 0.42274 0.00634  0.11069  -0.01957 170 PRO A O   
1380 C  CB  . PRO A 170 ? 0.34657 0.24625 0.38022 0.00631  0.10734  -0.01025 170 PRO A CB  
1381 C  CG  . PRO A 170 ? 0.35522 0.25791 0.39050 0.01246  0.11047  -0.01775 170 PRO A CG  
1382 C  CD  . PRO A 170 ? 0.36060 0.25588 0.40294 0.01918  0.11132  -0.01392 170 PRO A CD  
1383 N  N   . ALA A 171 ? 0.40824 0.27337 0.44708 -0.00222 0.10772  -0.00664 171 ALA A N   
1384 C  CA  . ALA A 171 ? 0.40955 0.26145 0.45373 -0.00732 0.10939  -0.01069 171 ALA A CA  
1385 C  C   . ALA A 171 ? 0.41020 0.26697 0.45535 -0.01059 0.10844  -0.02426 171 ALA A C   
1386 O  O   . ALA A 171 ? 0.41645 0.28785 0.45516 -0.01261 0.10602  -0.02699 171 ALA A O   
1387 C  CB  . ALA A 171 ? 0.39634 0.24658 0.43920 -0.01327 0.10917  -0.00287 171 ALA A CB  
1388 N  N   . GLY A 172 ? 0.44551 0.28993 0.49900 -0.01052 0.11005  -0.03297 172 GLY A N   
1389 C  CA  . GLY A 172 ? 0.45552 0.30395 0.51043 -0.01262 0.10818  -0.04804 172 GLY A CA  
1390 C  C   . GLY A 172 ? 0.46497 0.32106 0.51523 -0.00527 0.10833  -0.05707 172 GLY A C   
1391 O  O   . GLY A 172 ? 0.46345 0.32312 0.51337 -0.00536 0.10654  -0.07108 172 GLY A O   
1392 N  N   . GLY A 173 ? 0.39831 0.25807 0.44530 0.00153  0.11034  -0.05008 173 GLY A N   
1393 C  CA  . GLY A 173 ? 0.40401 0.27142 0.44794 0.00914  0.11190  -0.05765 173 GLY A CA  
1394 C  C   . GLY A 173 ? 0.39417 0.28243 0.42691 0.01073  0.11156  -0.05724 173 GLY A C   
1395 O  O   . GLY A 173 ? 0.39953 0.29615 0.42895 0.01752  0.11406  -0.06264 173 GLY A O   
1396 N  N   . ARG A 174 ? 0.43396 0.33086 0.46140 0.00511  0.10919  -0.05058 174 ARG A N   
1397 C  CA  . ARG A 174 ? 0.43120 0.34690 0.44936 0.00657  0.10943  -0.04788 174 ARG A CA  
1398 C  C   . ARG A 174 ? 0.42949 0.34981 0.44687 0.00123  0.10733  -0.03580 174 ARG A C   
1399 O  O   . ARG A 174 ? 0.42347 0.33485 0.44429 -0.00448 0.10507  -0.03286 174 ARG A O   
1400 C  CB  . ARG A 174 ? 0.44897 0.37348 0.45865 0.00657  0.10776  -0.05970 174 ARG A CB  
1401 C  CG  . ARG A 174 ? 0.44691 0.37316 0.45450 -0.00098 0.10305  -0.06030 174 ARG A CG  
1402 C  CD  . ARG A 174 ? 0.44931 0.37787 0.45317 -0.00078 0.09977  -0.07619 174 ARG A CD  
1403 N  NE  . ARG A 174 ? 0.47312 0.41357 0.46651 0.00755  0.10192  -0.08337 174 ARG A NE  
1404 C  CZ  . ARG A 174 ? 0.47198 0.42978 0.45278 0.01079  0.10269  -0.07949 174 ARG A CZ  
1405 N  NH1 . ARG A 174 ? 0.45729 0.42217 0.43533 0.00625  0.10078  -0.06920 174 ARG A NH1 
1406 N  NH2 . ARG A 174 ? 0.46267 0.43089 0.43360 0.01929  0.10597  -0.08565 174 ARG A NH2 
1407 N  N   . TRP A 175 ? 0.40565 0.34013 0.41964 0.00337  0.10864  -0.02886 175 TRP A N   
1408 C  CA  . TRP A 175 ? 0.40886 0.34774 0.42418 -0.00077 0.10657  -0.01795 175 TRP A CA  
1409 C  C   . TRP A 175 ? 0.40741 0.35006 0.41767 -0.00689 0.10324  -0.01893 175 TRP A C   
1410 O  O   . TRP A 175 ? 0.40028 0.33853 0.41318 -0.01191 0.10065  -0.01382 175 TRP A O   
1411 C  CB  . TRP A 175 ? 0.40318 0.35579 0.41995 0.00291  0.10917  -0.01084 175 TRP A CB  
1412 C  CG  . TRP A 175 ? 0.40723 0.35834 0.43138 0.00896  0.11200  -0.00944 175 TRP A CG  
1413 C  CD1 . TRP A 175 ? 0.40891 0.36502 0.43311 0.01541  0.11660  -0.01428 175 TRP A CD1 
1414 C  CD2 . TRP A 175 ? 0.39834 0.34357 0.43092 0.00999  0.11014  -0.00309 175 TRP A CD2 
1415 N  NE1 . TRP A 175 ? 0.40505 0.35867 0.43893 0.02003  0.11776  -0.01118 175 TRP A NE1 
1416 C  CE2 . TRP A 175 ? 0.39984 0.34690 0.43865 0.01698  0.11335  -0.00435 175 TRP A CE2 
1417 C  CE3 . TRP A 175 ? 0.39269 0.33221 0.42751 0.00651  0.10591  0.00314  175 TRP A CE3 
1418 C  CZ2 . TRP A 175 ? 0.39755 0.34104 0.44528 0.02055  0.11162  0.00045  175 TRP A CZ2 
1419 C  CZ3 . TRP A 175 ? 0.39083 0.32689 0.43256 0.01046  0.10428  0.00772  175 TRP A CZ3 
1420 C  CH2 . TRP A 175 ? 0.39305 0.33117 0.44145 0.01740  0.10671  0.00639  175 TRP A CH2 
1421 N  N   . ASN A 176 ? 0.50221 0.45381 0.50483 -0.00576 0.10315  -0.02560 176 ASN A N   
1422 C  CA  . ASN A 176 ? 0.50170 0.46087 0.49906 -0.00994 0.09971  -0.02542 176 ASN A CA  
1423 C  C   . ASN A 176 ? 0.51377 0.47037 0.50781 -0.01120 0.09668  -0.03852 176 ASN A C   
1424 O  O   . ASN A 176 ? 0.50987 0.46914 0.49887 -0.00611 0.09785  -0.04792 176 ASN A O   
1425 C  CB  . ASN A 176 ? 0.50530 0.48058 0.49598 -0.00643 0.10180  -0.01960 176 ASN A CB  
1426 C  CG  . ASN A 176 ? 0.51236 0.49484 0.49988 -0.01047 0.09821  -0.01528 176 ASN A CG  
1427 O  OD1 . ASN A 176 ? 0.51635 0.49487 0.50392 -0.01495 0.09377  -0.02050 176 ASN A OD1 
1428 N  ND2 . ASN A 176 ? 0.51700 0.51010 0.50368 -0.00889 0.10036  -0.00548 176 ASN A ND2 
1429 N  N   . PHE A 177 ? 0.50124 0.45340 0.49921 -0.01773 0.09269  -0.03990 177 PHE A N   
1430 C  CA  . PHE A 177 ? 0.51622 0.46749 0.51438 -0.02005 0.08861  -0.05274 177 PHE A CA  
1431 C  C   . PHE A 177 ? 0.51011 0.47505 0.50145 -0.02138 0.08412  -0.05301 177 PHE A C   
1432 O  O   . PHE A 177 ? 0.52757 0.49216 0.52288 -0.02563 0.07938  -0.06079 177 PHE A O   
1433 C  CB  . PHE A 177 ? 0.51188 0.44791 0.52288 -0.02652 0.08788  -0.05508 177 PHE A CB  
1434 C  CG  . PHE A 177 ? 0.49886 0.42017 0.51674 -0.02463 0.09209  -0.05413 177 PHE A CG  
1435 C  CD1 . PHE A 177 ? 0.49525 0.40991 0.51607 -0.02148 0.09268  -0.06601 177 PHE A CD1 
1436 C  CD2 . PHE A 177 ? 0.50067 0.41495 0.52209 -0.02527 0.09497  -0.04184 177 PHE A CD2 
1437 C  CE1 . PHE A 177 ? 0.50075 0.40119 0.52884 -0.01915 0.09652  -0.06456 177 PHE A CE1 
1438 C  CE2 . PHE A 177 ? 0.49663 0.39776 0.52371 -0.02246 0.09837  -0.04018 177 PHE A CE2 
1439 C  CZ  . PHE A 177 ? 0.49802 0.39181 0.52889 -0.01947 0.09938  -0.05100 177 PHE A CZ  
1440 N  N   . ASP A 178 ? 0.77521 0.75231 0.75796 -0.01767 0.08565  -0.04413 178 ASP A N   
1441 C  CA  . ASP A 178 ? 0.77368 0.76394 0.74911 -0.01750 0.08172  -0.04277 178 ASP A CA  
1442 C  C   . ASP A 178 ? 0.78501 0.78242 0.75193 -0.01371 0.07752  -0.05709 178 ASP A C   
1443 O  O   . ASP A 178 ? 0.78083 0.78509 0.73704 -0.00630 0.07996  -0.06086 178 ASP A O   
1444 C  CB  . ASP A 178 ? 0.76502 0.76602 0.73386 -0.01324 0.08550  -0.03001 178 ASP A CB  
1445 C  CG  . ASP A 178 ? 0.77359 0.78036 0.74407 -0.01664 0.08261  -0.02107 178 ASP A CG  
1446 O  OD1 . ASP A 178 ? 0.77886 0.77860 0.75841 -0.02302 0.07962  -0.02099 178 ASP A OD1 
1447 O  OD2 . ASP A 178 ? 0.77505 0.79332 0.73819 -0.01255 0.08387  -0.01368 178 ASP A OD2 
1448 N  N   . ALA A 179 ? 1.14979 1.14633 1.12208 -0.01840 0.07117  -0.06588 179 ALA A N   
1449 C  CA  . ALA A 179 ? 1.16226 1.16615 1.12853 -0.01511 0.06521  -0.08173 179 ALA A CA  
1450 C  C   . ALA A 179 ? 1.17028 1.19189 1.12253 -0.01025 0.06141  -0.07829 179 ALA A C   
1451 O  O   . ALA A 179 ? 1.16832 1.19366 1.12445 -0.01422 0.05827  -0.07150 179 ALA A O   
1452 C  CB  . ALA A 179 ? 1.15990 1.15553 1.14177 -0.02262 0.05981  -0.09325 179 ALA A CB  
1453 N  N   . GLU A 180 ? 1.13272 1.16539 1.06842 -0.00097 0.06204  -0.08252 180 GLU A N   
1454 C  CA  . GLU A 180 ? 1.12655 1.17663 1.04647 0.00546  0.05865  -0.07909 180 GLU A CA  
1455 C  C   . GLU A 180 ? 1.12839 1.18446 1.05010 0.00399  0.04765  -0.09342 180 GLU A C   
1456 O  O   . GLU A 180 ? 1.12944 1.17579 1.06746 -0.00343 0.04357  -0.10401 180 GLU A O   
1457 C  CB  . GLU A 180 ? 1.14071 1.20138 1.04138 0.01671  0.06336  -0.07965 180 GLU A CB  
1458 C  CG  . GLU A 180 ? 1.13984 1.19484 1.04226 0.01816  0.07426  -0.06840 180 GLU A CG  
1459 C  CD  . GLU A 180 ? 1.12922 1.17885 1.04305 0.01184  0.07839  -0.05013 180 GLU A CD  
1460 O  OE1 . GLU A 180 ? 1.12562 1.18512 1.03297 0.01467  0.08049  -0.03687 180 GLU A OE1 
1461 O  OE2 . GLU A 180 ? 1.12455 1.16007 1.05389 0.00457  0.07951  -0.04909 180 GLU A OE2 
1462 N  N   . ASN A 181 ? 0.98497 1.05784 0.89065 0.01145  0.04283  -0.09335 181 ASN A N   
1463 C  CA  . ASN A 181 ? 0.99279 1.07486 0.89892 0.01171  0.03109  -0.10706 181 ASN A CA  
1464 C  C   . ASN A 181 ? 0.97555 1.05166 0.90205 0.00109  0.02712  -0.10398 181 ASN A C   
1465 O  O   . ASN A 181 ? 0.96591 1.04254 0.90430 -0.00316 0.01874  -0.11851 181 ASN A O   
1466 C  CB  . ASN A 181 ? 1.00371 1.08436 0.91147 0.01343  0.02543  -0.13057 181 ASN A CB  
1467 C  CG  . ASN A 181 ? 1.01549 1.09931 0.90563 0.02337  0.03101  -0.13454 181 ASN A CG  
1468 O  OD1 . ASN A 181 ? 1.02271 1.12206 0.89022 0.03429  0.03132  -0.13126 181 ASN A OD1 
1469 N  ND2 . ASN A 181 ? 1.01757 1.08691 0.91804 0.02023  0.03600  -0.14097 181 ASN A ND2 
1470 N  N   . ARG A 182 ? 1.33208 1.40293 1.26406 -0.00313 0.03324  -0.08572 182 ARG A N   
1471 C  CA  . ARG A 182 ? 1.32722 1.39440 1.27628 -0.01174 0.03022  -0.08161 182 ARG A CA  
1472 C  C   . ARG A 182 ? 1.31814 1.40127 1.26245 -0.00805 0.02064  -0.08438 182 ARG A C   
1473 O  O   . ARG A 182 ? 1.31639 1.41270 1.24189 0.00150  0.01918  -0.07959 182 ARG A O   
1474 C  CB  . ARG A 182 ? 1.32518 1.38496 1.27878 -0.01518 0.03830  -0.06240 182 ARG A CB  
1475 C  CG  . ARG A 182 ? 1.32527 1.36795 1.29043 -0.02143 0.04547  -0.06063 182 ARG A CG  
1476 C  CD  . ARG A 182 ? 1.32563 1.36515 1.28530 -0.01878 0.05404  -0.04545 182 ARG A CD  
1477 N  NE  . ARG A 182 ? 1.32982 1.35621 1.29478 -0.02082 0.05991  -0.04722 182 ARG A NE  
1478 C  CZ  . ARG A 182 ? 1.32585 1.33961 1.30362 -0.02724 0.06322  -0.04235 182 ARG A CZ  
1479 N  NH1 . ARG A 182 ? 1.31823 1.33069 1.30485 -0.03248 0.06187  -0.03580 182 ARG A NH1 
1480 N  NH2 . ARG A 182 ? 1.32960 1.33225 1.31076 -0.02758 0.06799  -0.04407 182 ARG A NH2 
1481 N  N   . ARG A 183 ? 0.87772 0.96020 0.83960 -0.01518 0.01437  -0.09163 183 ARG A N   
1482 C  CA  . ARG A 183 ? 0.88285 0.98101 0.84357 -0.01189 0.00358  -0.09780 183 ARG A CA  
1483 C  C   . ARG A 183 ? 0.86129 0.95814 0.83979 -0.01923 0.00252  -0.09029 183 ARG A C   
1484 O  O   . ARG A 183 ? 0.84539 0.92889 0.83764 -0.02731 0.00959  -0.08313 183 ARG A O   
1485 C  CB  . ARG A 183 ? 0.90099 1.00419 0.86700 -0.01170 -0.00597 -0.12110 183 ARG A CB  
1486 C  CG  . ARG A 183 ? 0.89054 0.98600 0.88538 -0.02328 -0.00890 -0.13154 183 ARG A CG  
1487 C  CD  . ARG A 183 ? 0.88693 0.96163 0.89560 -0.03219 0.00182  -0.12659 183 ARG A CD  
1488 N  NE  . ARG A 183 ? 0.89885 0.96527 0.89569 -0.02823 0.00776  -0.12830 183 ARG A NE  
1489 C  CZ  . ARG A 183 ? 0.91598 0.98403 0.90896 -0.02432 0.00345  -0.14552 183 ARG A CZ  
1490 N  NH1 . ARG A 183 ? 0.92400 1.00157 0.92462 -0.02409 -0.00763 -0.16392 183 ARG A NH1 
1491 N  NH2 . ARG A 183 ? 0.92509 0.98538 0.90770 -0.02036 0.01006  -0.14529 183 ARG A NH2 
1492 N  N   . LYS A 184 ? 0.51247 0.62424 0.48981 -0.01536 -0.00660 -0.09219 184 LYS A N   
1493 C  CA  . LYS A 184 ? 0.49193 0.60521 0.48641 -0.02102 -0.00873 -0.08681 184 LYS A CA  
1494 C  C   . LYS A 184 ? 0.48498 0.59267 0.50498 -0.03134 -0.01114 -0.10049 184 LYS A C   
1495 O  O   . LYS A 184 ? 0.48253 0.58679 0.50745 -0.03351 -0.01322 -0.11556 184 LYS A O   
1496 C  CB  . LYS A 184 ? 0.47707 0.60885 0.46331 -0.01278 -0.01851 -0.08566 184 LYS A CB  
1497 C  CG  . LYS A 184 ? 0.48503 0.63048 0.47146 -0.00916 -0.03120 -0.10593 184 LYS A CG  
1498 C  CD  . LYS A 184 ? 0.48742 0.65205 0.46587 -0.00019 -0.04174 -0.10423 184 LYS A CD  
1499 C  CE  . LYS A 184 ? 0.49514 0.66964 0.44227 0.01369  -0.04234 -0.09748 184 LYS A CE  
1500 N  NZ  . LYS A 184 ? 0.49040 0.68265 0.42831 0.02352  -0.05162 -0.09217 184 LYS A NZ  
1501 N  N   . LEU A 185 ? 0.41632 0.52315 0.45397 -0.03761 -0.01034 -0.09503 185 LEU A N   
1502 C  CA  . LEU A 185 ? 0.40464 0.50710 0.46857 -0.04757 -0.01109 -0.10575 185 LEU A CA  
1503 C  C   . LEU A 185 ? 0.40899 0.52560 0.48086 -0.04603 -0.02378 -0.12501 185 LEU A C   
1504 O  O   . LEU A 185 ? 0.40839 0.54143 0.46941 -0.03775 -0.03321 -0.12670 185 LEU A O   
1505 C  CB  . LEU A 185 ? 0.38371 0.48536 0.46371 -0.05309 -0.00763 -0.09589 185 LEU A CB  
1506 C  CG  . LEU A 185 ? 0.38679 0.47675 0.46121 -0.05424 0.00315  -0.07794 185 LEU A CG  
1507 C  CD1 . LEU A 185 ? 0.37645 0.46571 0.47015 -0.06042 0.00621  -0.07296 185 LEU A CD1 
1508 C  CD2 . LEU A 185 ? 0.39233 0.46558 0.46274 -0.05741 0.01219  -0.07619 185 LEU A CD2 
1509 N  N   . PRO A 186 ? 0.35728 0.46823 0.44865 -0.05336 -0.02474 -0.13994 186 PRO A N   
1510 C  CA  . PRO A 186 ? 0.36999 0.49499 0.47469 -0.05312 -0.03765 -0.15978 186 PRO A CA  
1511 C  C   . PRO A 186 ? 0.36245 0.49990 0.48496 -0.05563 -0.04297 -0.15837 186 PRO A C   
1512 O  O   . PRO A 186 ? 0.34678 0.47776 0.47975 -0.06124 -0.03462 -0.14513 186 PRO A O   
1513 C  CB  . PRO A 186 ? 0.37374 0.48557 0.50095 -0.06262 -0.03431 -0.17284 186 PRO A CB  
1514 C  CG  . PRO A 186 ? 0.35939 0.45175 0.49039 -0.06937 -0.01928 -0.15696 186 PRO A CG  
1515 C  CD  . PRO A 186 ? 0.35235 0.44361 0.45541 -0.06183 -0.01415 -0.13909 186 PRO A CD  
1516 N  N   . PRO A 187 ? 0.48172 0.63809 0.60814 -0.05088 -0.05721 -0.17235 187 PRO A N   
1517 C  CA  . PRO A 187 ? 0.47172 0.64230 0.61326 -0.05128 -0.06323 -0.17018 187 PRO A CA  
1518 C  C   . PRO A 187 ? 0.47137 0.63583 0.64783 -0.06412 -0.05692 -0.17074 187 PRO A C   
1519 O  O   . PRO A 187 ? 0.46837 0.63977 0.65527 -0.06507 -0.05649 -0.16255 187 PRO A O   
1520 C  CB  . PRO A 187 ? 0.48354 0.67509 0.62487 -0.04402 -0.08081 -0.18936 187 PRO A CB  
1521 C  CG  . PRO A 187 ? 0.50313 0.68907 0.63872 -0.04356 -0.08306 -0.20536 187 PRO A CG  
1522 C  CD  . PRO A 187 ? 0.50228 0.66926 0.61737 -0.04337 -0.06905 -0.19073 187 PRO A CD  
1523 N  N   . GLY A 188 ? 0.64639 0.79801 0.84153 -0.07356 -0.05129 -0.17933 188 GLY A N   
1524 C  CA  . GLY A 188 ? 0.64269 0.78927 0.87198 -0.08548 -0.04437 -0.17941 188 GLY A CA  
1525 C  C   . GLY A 188 ? 0.63125 0.75934 0.85914 -0.09100 -0.02742 -0.16065 188 GLY A C   
1526 O  O   . GLY A 188 ? 0.62265 0.74848 0.87434 -0.09896 -0.02019 -0.15623 188 GLY A O   
1527 N  N   . LEU A 189 ? 0.38656 0.50236 0.58692 -0.08636 -0.02094 -0.14969 189 LEU A N   
1528 C  CA  . LEU A 189 ? 0.38291 0.48094 0.58034 -0.09070 -0.00594 -0.13353 189 LEU A CA  
1529 C  C   . LEU A 189 ? 0.38035 0.48309 0.57238 -0.08820 -0.00248 -0.11815 189 LEU A C   
1530 O  O   . LEU A 189 ? 0.38675 0.49637 0.55737 -0.07961 -0.00697 -0.11148 189 LEU A O   
1531 C  CB  . LEU A 189 ? 0.40309 0.48784 0.57513 -0.08623 -0.00130 -0.12850 189 LEU A CB  
1532 C  CG  . LEU A 189 ? 0.40085 0.46730 0.56840 -0.08964 0.01295  -0.11307 189 LEU A CG  
1533 C  CD1 . LEU A 189 ? 0.38375 0.43903 0.57771 -0.09984 0.02100  -0.11566 189 LEU A CD1 
1534 C  CD2 . LEU A 189 ? 0.40269 0.45896 0.54597 -0.08416 0.01587  -0.10922 189 LEU A CD2 
1535 N  N   . ARG A 190 ? 0.44040 0.53928 0.65235 -0.09537 0.00603  -0.11237 190 ARG A N   
1536 C  CA  . ARG A 190 ? 0.43157 0.53343 0.64013 -0.09325 0.01040  -0.09878 190 ARG A CA  
1537 C  C   . ARG A 190 ? 0.43603 0.52051 0.63205 -0.09419 0.02322  -0.08458 190 ARG A C   
1538 O  O   . ARG A 190 ? 0.44117 0.51368 0.64835 -0.10087 0.03245  -0.08374 190 ARG A O   
1539 C  CB  . ARG A 190 ? 0.42419 0.53560 0.66210 -0.09916 0.01145  -0.10191 190 ARG A CB  
1540 C  CG  . ARG A 190 ? 0.41671 0.53678 0.65214 -0.09478 0.01160  -0.09201 190 ARG A CG  
1541 C  CD  . ARG A 190 ? 0.40541 0.53255 0.67023 -0.10109 0.01639  -0.09321 190 ARG A CD  
1542 N  NE  . ARG A 190 ? 0.41981 0.54749 0.68021 -0.09803 0.02245  -0.08084 190 ARG A NE  
1543 C  CZ  . ARG A 190 ? 0.40923 0.54755 0.66212 -0.09060 0.01530  -0.07745 190 ARG A CZ  
1544 N  NH1 . ARG A 190 ? 0.41249 0.56282 0.65986 -0.08483 0.00192  -0.08413 190 ARG A NH1 
1545 N  NH2 . ARG A 190 ? 0.39308 0.52996 0.64380 -0.08825 0.02166  -0.06716 190 ARG A NH2 
1546 N  N   . PRO A 191 ? 0.34138 0.42401 0.51562 -0.08753 0.02409  -0.07329 191 PRO A N   
1547 C  CA  . PRO A 191 ? 0.35153 0.41898 0.51440 -0.08781 0.03491  -0.06100 191 PRO A CA  
1548 C  C   . PRO A 191 ? 0.34314 0.40728 0.52179 -0.09313 0.04426  -0.05562 191 PRO A C   
1549 O  O   . PRO A 191 ? 0.33656 0.41200 0.52937 -0.09390 0.04245  -0.05667 191 PRO A O   
1550 C  CB  . PRO A 191 ? 0.34973 0.42042 0.49268 -0.07974 0.03189  -0.05171 191 PRO A CB  
1551 C  CG  . PRO A 191 ? 0.36654 0.45007 0.50335 -0.07445 0.02041  -0.05898 191 PRO A CG  
1552 C  CD  . PRO A 191 ? 0.34489 0.43916 0.50394 -0.07892 0.01481  -0.07145 191 PRO A CD  
1553 N  N   . PRO A 192 ? 0.31174 0.36120 0.48793 -0.09608 0.05458  -0.04949 192 PRO A N   
1554 C  CA  . PRO A 192 ? 0.30254 0.34903 0.49311 -0.10074 0.06469  -0.04436 192 PRO A CA  
1555 C  C   . PRO A 192 ? 0.30897 0.35925 0.49265 -0.09640 0.06724  -0.03529 192 PRO A C   
1556 O  O   . PRO A 192 ? 0.30790 0.35902 0.47486 -0.09026 0.06283  -0.03102 192 PRO A O   
1557 C  CB  . PRO A 192 ? 0.29802 0.32714 0.48298 -0.10305 0.07397  -0.03953 192 PRO A CB  
1558 C  CG  . PRO A 192 ? 0.32269 0.34598 0.48470 -0.09737 0.06959  -0.03788 192 PRO A CG  
1559 C  CD  . PRO A 192 ? 0.32218 0.35770 0.48234 -0.09460 0.05767  -0.04684 192 PRO A CD  
1560 N  N   . GLU A 193 ? 0.30813 0.36077 0.50643 -0.09963 0.07500  -0.03255 193 GLU A N   
1561 C  CA  . GLU A 193 ? 0.30835 0.36349 0.50101 -0.09542 0.07886  -0.02489 193 GLU A CA  
1562 C  C   . GLU A 193 ? 0.31629 0.35766 0.48898 -0.09205 0.08517  -0.01606 193 GLU A C   
1563 O  O   . GLU A 193 ? 0.30996 0.33981 0.47962 -0.09459 0.09140  -0.01379 193 GLU A O   
1564 C  CB  . GLU A 193 ? 0.34410 0.40604 0.55739 -0.09928 0.08672  -0.02460 193 GLU A CB  
1565 C  CG  . GLU A 193 ? 0.34027 0.41450 0.55767 -0.09499 0.08432  -0.02372 193 GLU A CG  
1566 C  CD  . GLU A 193 ? 0.33172 0.41282 0.56883 -0.09821 0.09393  -0.02282 193 GLU A CD  
1567 O  OE1 . GLU A 193 ? 0.32408 0.41520 0.58469 -0.10334 0.09256  -0.02952 193 GLU A OE1 
1568 O  OE2 . GLU A 193 ? 0.33264 0.40997 0.56219 -0.09525 0.10288  -0.01579 193 GLU A OE2 
1569 N  N   . ARG A 194 ? 0.28842 0.33107 0.44879 -0.08601 0.08308  -0.01140 194 ARG A N   
1570 C  CA  . ARG A 194 ? 0.29681 0.32846 0.43896 -0.08196 0.08679  -0.00449 194 ARG A CA  
1571 C  C   . ARG A 194 ? 0.30021 0.33274 0.44176 -0.07921 0.09387  0.00022  194 ARG A C   
1572 O  O   . ARG A 194 ? 0.30385 0.34662 0.45569 -0.07835 0.09337  -0.00152 194 ARG A O   
1573 C  CB  . ARG A 194 ? 0.30032 0.33181 0.42901 -0.07686 0.07850  -0.00346 194 ARG A CB  
1574 C  CG  . ARG A 194 ? 0.29865 0.33240 0.42633 -0.07790 0.07108  -0.00837 194 ARG A CG  
1575 C  CD  . ARG A 194 ? 0.31272 0.33594 0.43615 -0.08095 0.07444  -0.00969 194 ARG A CD  
1576 N  NE  . ARG A 194 ? 0.31145 0.32307 0.42265 -0.07871 0.08043  -0.00299 194 ARG A NE  
1577 C  CZ  . ARG A 194 ? 0.32103 0.32707 0.41829 -0.07491 0.07812  -0.00015 194 ARG A CZ  
1578 N  NH1 . ARG A 194 ? 0.32099 0.33133 0.41346 -0.07285 0.07123  -0.00236 194 ARG A NH1 
1579 N  NH2 . ARG A 194 ? 0.32378 0.32058 0.41183 -0.07262 0.08300  0.00527  194 ARG A NH2 
1580 N  N   . LEU A 195 ? 0.31218 0.33445 0.44112 -0.07703 0.10023  0.00580  195 LEU A N   
1581 C  CA  . LEU A 195 ? 0.30610 0.32900 0.43071 -0.07302 0.10702  0.00989  195 LEU A CA  
1582 C  C   . LEU A 195 ? 0.31894 0.34530 0.43581 -0.06674 0.10056  0.00922  195 LEU A C   
1583 O  O   . LEU A 195 ? 0.32687 0.34805 0.43318 -0.06414 0.09471  0.00992  195 LEU A O   
1584 C  CB  . LEU A 195 ? 0.31317 0.32446 0.42514 -0.07148 0.11489  0.01614  195 LEU A CB  
1585 C  CG  . LEU A 195 ? 0.31853 0.33023 0.42139 -0.06565 0.12198  0.02057  195 LEU A CG  
1586 C  CD1 . LEU A 195 ? 0.30472 0.32451 0.42152 -0.06796 0.13100  0.02131  195 LEU A CD1 
1587 C  CD2 . LEU A 195 ? 0.31798 0.31796 0.40506 -0.06257 0.12720  0.02706  195 LEU A CD2 
1588 N  N   . ARG A 196 ? 0.35999 0.39518 0.48410 -0.06434 0.10192  0.00765  196 ARG A N   
1589 C  CA  . ARG A 196 ? 0.37090 0.40847 0.48987 -0.05799 0.09721  0.00654  196 ARG A CA  
1590 C  C   . ARG A 196 ? 0.37054 0.40806 0.48256 -0.05310 0.10483  0.00794  196 ARG A C   
1591 O  O   . ARG A 196 ? 0.36251 0.40159 0.47734 -0.05470 0.11440  0.01024  196 ARG A O   
1592 C  CB  . ARG A 196 ? 0.35985 0.40818 0.49307 -0.05764 0.09110  0.00255  196 ARG A CB  
1593 C  CG  . ARG A 196 ? 0.36618 0.41685 0.50507 -0.06111 0.08330  0.00112  196 ARG A CG  
1594 C  CD  . ARG A 196 ? 0.37972 0.42120 0.50518 -0.06043 0.07878  0.00367  196 ARG A CD  
1595 N  NE  . ARG A 196 ? 0.40350 0.44427 0.52537 -0.05538 0.07275  0.00490  196 ARG A NE  
1596 C  CZ  . ARG A 196 ? 0.40408 0.43674 0.51502 -0.05294 0.07143  0.00747  196 ARG A CZ  
1597 N  NH1 . ARG A 196 ? 0.38894 0.41359 0.48954 -0.05428 0.07523  0.00922  196 ARG A NH1 
1598 N  NH2 . ARG A 196 ? 0.39921 0.43181 0.51148 -0.04899 0.06618  0.00836  196 ARG A NH2 
1599 N  N   . ILE A 197 ? 0.29367 0.32972 0.39703 -0.04677 0.10069  0.00643  197 ILE A N   
1600 C  CA  . ILE A 197 ? 0.29338 0.32973 0.38679 -0.04034 0.10616  0.00627  197 ILE A CA  
1601 C  C   . ILE A 197 ? 0.30124 0.34725 0.40422 -0.03629 0.10472  0.00083  197 ILE A C   
1602 O  O   . ILE A 197 ? 0.30680 0.35315 0.41323 -0.03354 0.09613  -0.00301 197 ILE A O   
1603 C  CB  . ILE A 197 ? 0.30714 0.33540 0.38462 -0.03533 0.10186  0.00653  197 ILE A CB  
1604 C  CG1 . ILE A 197 ? 0.29337 0.31225 0.36332 -0.03912 0.10239  0.01161  197 ILE A CG1 
1605 C  CG2 . ILE A 197 ? 0.30471 0.33441 0.36979 -0.02765 0.10714  0.00566  197 ILE A CG2 
1606 C  CD1 . ILE A 197 ? 0.29113 0.30692 0.35645 -0.04094 0.11310  0.01725  197 ILE A CD1 
1607 N  N   . PRO A 198 ? 0.29777 0.35164 0.40664 -0.03561 0.11330  0.00056  198 PRO A N   
1608 C  CA  . PRO A 198 ? 0.29944 0.36263 0.41656 -0.03042 0.11262  -0.00529 198 PRO A CA  
1609 C  C   . PRO A 198 ? 0.31049 0.37103 0.41403 -0.02168 0.10986  -0.00953 198 PRO A C   
1610 O  O   . PRO A 198 ? 0.31374 0.36948 0.40008 -0.01816 0.11403  -0.00712 198 PRO A O   
1611 C  CB  . PRO A 198 ? 0.29315 0.36487 0.41702 -0.03141 0.12497  -0.00334 198 PRO A CB  
1612 C  CG  . PRO A 198 ? 0.28954 0.35401 0.40319 -0.03483 0.13305  0.00420  198 PRO A CG  
1613 C  CD  . PRO A 198 ? 0.28397 0.33861 0.39443 -0.03969 0.12472  0.00588  198 PRO A CD  
1614 N  N   . PRO A 199 ? 0.30260 0.36610 0.41410 -0.01759 0.10233  -0.01618 199 PRO A N   
1615 C  CA  . PRO A 199 ? 0.30616 0.36668 0.40764 -0.00959 0.09764  -0.02226 199 PRO A CA  
1616 C  C   . PRO A 199 ? 0.30890 0.37427 0.39691 -0.00212 0.10628  -0.02462 199 PRO A C   
1617 O  O   . PRO A 199 ? 0.30888 0.38346 0.40278 -0.00046 0.11413  -0.02561 199 PRO A O   
1618 C  CB  . PRO A 199 ? 0.31365 0.37754 0.43201 -0.00739 0.08973  -0.02878 199 PRO A CB  
1619 C  CG  . PRO A 199 ? 0.30439 0.36932 0.43705 -0.01487 0.08699  -0.02381 199 PRO A CG  
1620 C  CD  . PRO A 199 ? 0.29670 0.36531 0.42766 -0.02015 0.09637  -0.01832 199 PRO A CD  
1621 N  N   . ASN A 200 ? 0.28491 0.34489 0.35458 0.00299  0.10490  -0.02538 200 ASN A N   
1622 C  CA  . ASN A 200 ? 0.30196 0.36669 0.35498 0.01245  0.11127  -0.02844 200 ASN A CA  
1623 C  C   . ASN A 200 ? 0.30579 0.37621 0.36392 0.02058  0.10544  -0.04103 200 ASN A C   
1624 O  O   . ASN A 200 ? 0.29513 0.36374 0.36984 0.01844  0.09621  -0.04614 200 ASN A O   
1625 C  CB  . ASN A 200 ? 0.31063 0.36804 0.34246 0.01575  0.11010  -0.02513 200 ASN A CB  
1626 C  CG  . ASN A 200 ? 0.30443 0.35515 0.33750 0.01667  0.09643  -0.03117 200 ASN A CG  
1627 O  OD1 . ASN A 200 ? 0.30357 0.35656 0.34464 0.02095  0.08856  -0.04145 200 ASN A OD1 
1628 N  ND2 . ASN A 200 ? 0.30081 0.34319 0.32770 0.01266  0.09393  -0.02487 200 ASN A ND2 
1629 N  N   . PRO A 201 ? 0.32729 0.28678 0.20465 0.06760  0.10001  -0.00333 201 PRO A N   
1630 C  CA  . PRO A 201 ? 0.34990 0.29391 0.20885 0.07713  0.10467  -0.00980 201 PRO A CA  
1631 C  C   . PRO A 201 ? 0.35425 0.27887 0.19999 0.07563  0.09282  -0.01659 201 PRO A C   
1632 O  O   . PRO A 201 ? 0.36289 0.27980 0.20683 0.08243  0.09374  -0.02111 201 PRO A O   
1633 C  CB  . PRO A 201 ? 0.37580 0.31065 0.20986 0.07984  0.11369  -0.00971 201 PRO A CB  
1634 C  CG  . PRO A 201 ? 0.36419 0.31869 0.21435 0.07545  0.11978  -0.00116 201 PRO A CG  
1635 C  CD  . PRO A 201 ? 0.33633 0.30023 0.20699 0.06563  0.10786  0.00189  201 PRO A CD  
1636 N  N   . THR A 202 ? 0.41892 0.33569 0.25631 0.06691  0.08167  -0.01693 202 THR A N   
1637 C  CA  . THR A 202 ? 0.43007 0.33088 0.25811 0.06414  0.06986  -0.02235 202 THR A CA  
1638 C  C   . THR A 202 ? 0.42700 0.33722 0.27841 0.06338  0.06471  -0.02186 202 THR A C   
1639 O  O   . THR A 202 ? 0.43843 0.33701 0.28514 0.06644  0.06119  -0.02643 202 THR A O   
1640 C  CB  . THR A 202 ? 0.42636 0.32105 0.24491 0.05485  0.05918  -0.02137 202 THR A CB  
1641 O  OG1 . THR A 202 ? 0.44890 0.32950 0.23981 0.05603  0.06197  -0.02311 202 THR A OG1 
1642 C  CG2 . THR A 202 ? 0.42584 0.31024 0.24310 0.05022  0.04627  -0.02509 202 THR A CG2 
1643 N  N   . THR A 203 ? 0.35320 0.28341 0.22882 0.05916  0.06413  -0.01628 203 THR A N   
1644 C  CA  . THR A 203 ? 0.34320 0.28297 0.23982 0.05813  0.05917  -0.01544 203 THR A CA  
1645 C  C   . THR A 203 ? 0.34933 0.29267 0.25350 0.06758  0.06655  -0.01628 203 THR A C   
1646 O  O   . THR A 203 ? 0.34824 0.28872 0.25854 0.06918  0.06173  -0.01795 203 THR A O   
1647 C  CB  . THR A 203 ? 0.31439 0.27340 0.23269 0.05161  0.05733  -0.00978 203 THR A CB  
1648 O  OG1 . THR A 203 ? 0.31165 0.26642 0.22253 0.04418  0.05131  -0.00874 203 THR A OG1 
1649 C  CG2 . THR A 203 ? 0.30401 0.27117 0.24059 0.04959  0.05088  -0.00927 203 THR A CG2 
1650 N  N   . GLN A 204 ? 0.33591 0.28587 0.24019 0.07422  0.07851  -0.01457 204 GLN A N   
1651 C  CA  A GLN A 204 ? 0.34137 0.29591 0.25399 0.08455  0.08645  -0.01485 204 GLN A CA  
1652 C  CA  B GLN A 204 ? 0.34132 0.29588 0.25405 0.08451  0.08636  -0.01485 204 GLN A CA  
1653 C  C   . GLN A 204 ? 0.37010 0.30119 0.26259 0.09124  0.08545  -0.02177 204 GLN A C   
1654 O  O   . GLN A 204 ? 0.36950 0.29980 0.27039 0.09720  0.08512  -0.02266 204 GLN A O   
1655 C  CB  A GLN A 204 ? 0.34270 0.30921 0.25853 0.09043  0.10051  -0.01135 204 GLN A CB  
1656 C  CB  B GLN A 204 ? 0.34214 0.30909 0.25868 0.09038  0.10039  -0.01126 204 GLN A CB  
1657 C  CG  A GLN A 204 ? 0.31950 0.30966 0.25742 0.08383  0.10219  -0.00390 204 GLN A CG  
1658 C  CG  B GLN A 204 ? 0.31892 0.31338 0.26618 0.08896  0.10358  -0.00402 204 GLN A CG  
1659 C  CD  A GLN A 204 ? 0.32343 0.32140 0.25821 0.08687  0.11532  -0.00021 204 GLN A CD  
1660 C  CD  B GLN A 204 ? 0.31033 0.31299 0.27682 0.09270  0.09966  -0.00334 204 GLN A CD  
1661 O  OE1 A GLN A 204 ? 0.34232 0.33219 0.26266 0.09622  0.12532  -0.00280 204 GLN A OE1 
1662 O  OE1 B GLN A 204 ? 0.29034 0.30841 0.27746 0.08647  0.09338  0.00062  204 GLN A OE1 
1663 N  NE2 A GLN A 204 ? 0.30674 0.31967 0.25435 0.07900  0.11573  0.00595  204 GLN A NE2 
1664 N  NE2 B GLN A 204 ? 0.32599 0.31738 0.28478 0.10307  0.10326  -0.00714 204 GLN A NE2 
1665 N  N   . THR A 205 ? 0.38663 0.29749 0.25179 0.09019  0.08447  -0.02660 205 THR A N   
1666 C  CA  . THR A 205 ? 0.41136 0.29686 0.25461 0.09541  0.08268  -0.03390 205 THR A CA  
1667 C  C   . THR A 205 ? 0.41076 0.28870 0.25883 0.08991  0.06974  -0.03542 205 THR A C   
1668 O  O   . THR A 205 ? 0.42352 0.29109 0.27076 0.09590  0.06929  -0.03827 205 THR A O   
1669 C  CB  . THR A 205 ? 0.43217 0.29799 0.24427 0.09356  0.08261  -0.03854 205 THR A CB  
1670 O  OG1 . THR A 205 ? 0.43877 0.31101 0.24489 0.09953  0.09606  -0.03681 205 THR A OG1 
1671 C  CG2 . THR A 205 ? 0.45952 0.29668 0.24722 0.09783  0.07957  -0.04680 205 THR A CG2 
1672 N  N   . VAL A 206 ? 0.44043 0.32341 0.29386 0.07879  0.05955  -0.03313 206 VAL A N   
1673 C  CA  . VAL A 206 ? 0.43929 0.31732 0.29848 0.07296  0.04798  -0.03367 206 VAL A CA  
1674 C  C   . VAL A 206 ? 0.42717 0.32018 0.31056 0.07628  0.04887  -0.02989 206 VAL A C   
1675 O  O   . VAL A 206 ? 0.43008 0.31453 0.31494 0.07702  0.04353  -0.03113 206 VAL A O   
1676 C  CB  . VAL A 206 ? 0.42734 0.31042 0.28901 0.06132  0.03846  -0.03135 206 VAL A CB  
1677 C  CG1 . VAL A 206 ? 0.41585 0.29804 0.28699 0.05536  0.02800  -0.03071 206 VAL A CG1 
1678 C  CG2 . VAL A 206 ? 0.44284 0.30940 0.27942 0.05804  0.03561  -0.03491 206 VAL A CG2 
1679 N  N   . LEU A 207 ? 0.45878 0.37402 0.36110 0.07804  0.05528  -0.02486 207 LEU A N   
1680 C  CA  . LEU A 207 ? 0.44242 0.37356 0.36796 0.08099  0.05559  -0.02079 207 LEU A CA  
1681 C  C   . LEU A 207 ? 0.44903 0.37098 0.37202 0.09240  0.06068  -0.02289 207 LEU A C   
1682 O  O   . LEU A 207 ? 0.44331 0.36412 0.37477 0.09380  0.05572  -0.02186 207 LEU A O   
1683 C  CB  . LEU A 207 ? 0.42073 0.37655 0.36553 0.08024  0.06158  -0.01520 207 LEU A CB  
1684 C  CG  . LEU A 207 ? 0.40828 0.38510 0.37922 0.07922  0.05934  -0.00993 207 LEU A CG  
1685 C  CD1 . LEU A 207 ? 0.39822 0.39532 0.38350 0.07450  0.06289  -0.00522 207 LEU A CD1 
1686 C  CD2 . LEU A 207 ? 0.39892 0.37944 0.37890 0.09021  0.06480  -0.00879 207 LEU A CD2 
1687 N  N   . GLU A 208 ? 0.55697 0.47157 0.46757 0.10114  0.07095  -0.02566 208 GLU A N   
1688 C  CA  . GLU A 208 ? 0.57230 0.47617 0.47910 0.11344  0.07682  -0.02816 208 GLU A CA  
1689 C  C   . GLU A 208 ? 0.58992 0.46638 0.47854 0.11254  0.06869  -0.03372 208 GLU A C   
1690 O  O   . GLU A 208 ? 0.58476 0.45465 0.47800 0.11891  0.06772  -0.03374 208 GLU A O   
1691 C  CB  . GLU A 208 ? 0.57952 0.47987 0.47408 0.12303  0.09045  -0.03055 208 GLU A CB  
1692 C  CG  . GLU A 208 ? 0.61513 0.51125 0.51206 0.13804  0.09969  -0.03165 208 GLU A CG  
1693 C  CD  . GLU A 208 ? 0.65084 0.51400 0.52268 0.14302  0.09717  -0.03948 208 GLU A CD  
1694 O  OE1 . GLU A 208 ? 0.64866 0.49139 0.49571 0.13659  0.09218  -0.04512 208 GLU A OE1 
1695 O  OE2 . GLU A 208 ? 0.64904 0.50679 0.52646 0.15265  0.09931  -0.03964 208 GLU A OE2 
1696 N  N   . GLN A 209 ? 0.59480 0.45510 0.46323 0.10432  0.06229  -0.03795 209 GLN A N   
1697 C  CA  . GLN A 209 ? 0.60432 0.43867 0.45578 0.10158  0.05359  -0.04294 209 GLN A CA  
1698 C  C   . GLN A 209 ? 0.58588 0.42617 0.45370 0.09513  0.04347  -0.03891 209 GLN A C   
1699 O  O   . GLN A 209 ? 0.58869 0.41287 0.45215 0.09750  0.03948  -0.04056 209 GLN A O   
1700 C  CB  . GLN A 209 ? 0.62061 0.43987 0.44921 0.09305  0.04800  -0.04736 209 GLN A CB  
1701 C  CG  . GLN A 209 ? 0.66181 0.46621 0.46586 0.09979  0.05675  -0.05299 209 GLN A CG  
1702 C  CD  . GLN A 209 ? 0.68422 0.47564 0.46608 0.09059  0.04990  -0.05645 209 GLN A CD  
1703 O  OE1 . GLN A 209 ? 0.67058 0.46161 0.45504 0.07960  0.03806  -0.05518 209 GLN A OE1 
1704 N  NE2 . GLN A 209 ? 0.69895 0.48023 0.45885 0.09526  0.05742  -0.06047 209 GLN A NE2 
1705 N  N   . VAL A 210 ? 0.40920 0.27143 0.29490 0.08705  0.03948  -0.03357 210 VAL A N   
1706 C  CA  . VAL A 210 ? 0.38100 0.24978 0.28108 0.08096  0.03068  -0.02962 210 VAL A CA  
1707 C  C   . VAL A 210 ? 0.36620 0.24451 0.28310 0.08934  0.03396  -0.02573 210 VAL A C   
1708 O  O   . VAL A 210 ? 0.36538 0.23679 0.28528 0.08890  0.02812  -0.02424 210 VAL A O   
1709 C  CB  . VAL A 210 ? 0.36538 0.25338 0.27775 0.07070  0.02620  -0.02575 210 VAL A CB  
1710 C  CG1 . VAL A 210 ? 0.33343 0.23247 0.26272 0.06627  0.01966  -0.02106 210 VAL A CG1 
1711 C  CG2 . VAL A 210 ? 0.36732 0.24409 0.26405 0.06202  0.02030  -0.02879 210 VAL A CG2 
1712 N  N   . SER A 211 ? 0.48034 0.37495 0.40882 0.09701  0.04316  -0.02339 211 SER A N   
1713 C  CA  . SER A 211 ? 0.46995 0.37518 0.41561 0.10585  0.04624  -0.01914 211 SER A CA  
1714 C  C   . SER A 211 ? 0.48330 0.36536 0.41745 0.11494  0.04703  -0.02225 211 SER A C   
1715 O  O   . SER A 211 ? 0.47860 0.36222 0.42359 0.11894  0.04409  -0.01853 211 SER A O   
1716 C  CB  . SER A 211 ? 0.46474 0.38990 0.42328 0.11311  0.05701  -0.01647 211 SER A CB  
1717 O  OG  . SER A 211 ? 0.45665 0.40501 0.43067 0.10492  0.05537  -0.01215 211 SER A OG  
1718 N  N   . ARG A 212 ? 0.61663 0.47578 0.52766 0.11826  0.05066  -0.02905 212 ARG A N   
1719 C  CA  . ARG A 212 ? 0.63323 0.46776 0.53090 0.12838  0.05322  -0.03311 212 ARG A CA  
1720 C  C   . ARG A 212 ? 0.64465 0.45370 0.52706 0.12119  0.04257  -0.03619 212 ARG A C   
1721 O  O   . ARG A 212 ? 0.64903 0.44196 0.52883 0.12735  0.04115  -0.03642 212 ARG A O   
1722 C  CB  . ARG A 212 ? 0.65964 0.48151 0.53839 0.13680  0.06393  -0.03946 212 ARG A CB  
1723 C  CG  . ARG A 212 ? 0.70012 0.49938 0.56726 0.15064  0.06995  -0.04367 212 ARG A CG  
1724 C  CD  . ARG A 212 ? 0.70747 0.51659 0.57474 0.15898  0.08282  -0.04457 212 ARG A CD  
1725 N  NE  . ARG A 212 ? 0.72014 0.52947 0.57224 0.15388  0.08646  -0.04805 212 ARG A NE  
1726 C  CZ  . ARG A 212 ? 0.74617 0.53219 0.57130 0.14717  0.08176  -0.05475 212 ARG A CZ  
1727 N  NH1 . ARG A 212 ? 0.75858 0.51866 0.56867 0.14401  0.07330  -0.05915 212 ARG A NH1 
1728 N  NH2 . ARG A 212 ? 0.75531 0.54467 0.56871 0.14295  0.08513  -0.05652 212 ARG A NH2 
1729 N  N   . GLY A 213 ? 0.47619 0.28170 0.34963 0.10825  0.03494  -0.03794 213 GLY A N   
1730 C  CA  . GLY A 213 ? 0.48811 0.26931 0.34623 0.10059  0.02516  -0.04103 213 GLY A CA  
1731 C  C   . GLY A 213 ? 0.46181 0.25237 0.33340 0.08977  0.01496  -0.03531 213 GLY A C   
1732 O  O   . GLY A 213 ? 0.47104 0.24298 0.33379 0.08394  0.00707  -0.03622 213 GLY A O   
1733 N  N   . PHE A 214 ? 0.43005 0.24872 0.32235 0.08670  0.01515  -0.02939 214 PHE A N   
1734 C  CA  . PHE A 214 ? 0.40222 0.23162 0.30681 0.07691  0.00671  -0.02401 214 PHE A CA  
1735 C  C   . PHE A 214 ? 0.38571 0.23668 0.31187 0.08141  0.00850  -0.01739 214 PHE A C   
1736 O  O   . PHE A 214 ? 0.36613 0.23680 0.30561 0.07463  0.00532  -0.01317 214 PHE A O   
1737 C  CB  . PHE A 214 ? 0.38973 0.23054 0.29516 0.06563  0.00289  -0.02401 214 PHE A CB  
1738 C  CG  . PHE A 214 ? 0.40765 0.22895 0.29310 0.05964  -0.00113 -0.02947 214 PHE A CG  
1739 C  CD1 . PHE A 214 ? 0.43156 0.24493 0.30235 0.06367  0.00424  -0.03482 214 PHE A CD1 
1740 C  CD2 . PHE A 214 ? 0.40375 0.21520 0.28500 0.04964  -0.01046 -0.02883 214 PHE A CD2 
1741 C  CE1 . PHE A 214 ? 0.45389 0.24898 0.30497 0.05778  -0.00057 -0.03979 214 PHE A CE1 
1742 C  CE2 . PHE A 214 ? 0.42285 0.21733 0.28669 0.04338  -0.01539 -0.03347 214 PHE A CE2 
1743 C  CZ  . PHE A 214 ? 0.45010 0.23595 0.29821 0.04741  -0.01092 -0.03914 214 PHE A CZ  
1744 N  N   . ASP A 215 ? 0.64396 0.49105 0.57348 0.09318  0.01335  -0.01641 215 ASP A N   
1745 C  CA  . ASP A 215 ? 0.63048 0.49895 0.58095 0.09816  0.01461  -0.00976 215 ASP A CA  
1746 C  C   . ASP A 215 ? 0.59840 0.47107 0.55663 0.09112  0.00583  -0.00405 215 ASP A C   
1747 O  O   . ASP A 215 ? 0.58083 0.47503 0.55574 0.09081  0.00469  0.00146  215 ASP A O   
1748 C  CB  . ASP A 215 ? 0.63375 0.49571 0.58625 0.11302  0.02114  -0.00942 215 ASP A CB  
1749 C  CG  . ASP A 215 ? 0.62186 0.51067 0.59770 0.11915  0.02404  -0.00282 215 ASP A CG  
1750 O  OD1 . ASP A 215 ? 0.62227 0.53329 0.60889 0.11595  0.02689  -0.00168 215 ASP A OD1 
1751 O  OD2 . ASP A 215 ? 0.62621 0.51376 0.60986 0.12671  0.02279  0.00163  215 ASP A OD2 
1752 N  N   . ASP A 216 ? 0.65288 0.50560 0.59897 0.08502  -0.00045 -0.00507 216 ASP A N   
1753 C  CA  . ASP A 216 ? 0.63710 0.49155 0.58859 0.07861  -0.00797 0.00077  216 ASP A CA  
1754 C  C   . ASP A 216 ? 0.62008 0.48812 0.57511 0.06580  -0.01250 0.00197  216 ASP A C   
1755 O  O   . ASP A 216 ? 0.61087 0.47909 0.56782 0.05907  -0.01832 0.00631  216 ASP A O   
1756 C  CB  . ASP A 216 ? 0.64536 0.47112 0.58310 0.07855  -0.01202 0.00001  216 ASP A CB  
1757 C  CG  . ASP A 216 ? 0.68951 0.50102 0.61365 0.06732  -0.01675 -0.00398 216 ASP A CG  
1758 O  OD1 . ASP A 216 ? 0.70574 0.51063 0.61947 0.06716  -0.01397 -0.01047 216 ASP A OD1 
1759 O  OD2 . ASP A 216 ? 0.68915 0.49566 0.61272 0.05875  -0.02336 -0.00024 216 ASP A OD2 
1760 N  N   . HIS A 217 ? 0.40501 0.28441 0.36100 0.06281  -0.00946 -0.00139 217 HIS A N   
1761 C  CA  . HIS A 217 ? 0.38429 0.27859 0.34564 0.05258  -0.01259 -0.00018 217 HIS A CA  
1762 C  C   . HIS A 217 ? 0.37499 0.29368 0.35251 0.05372  -0.01122 0.00383  217 HIS A C   
1763 O  O   . HIS A 217 ? 0.37062 0.29764 0.35597 0.06191  -0.00691 0.00484  217 HIS A O   
1764 C  CB  . HIS A 217 ? 0.39809 0.29083 0.35170 0.04868  -0.01070 -0.00540 217 HIS A CB  
1765 C  CG  . HIS A 217 ? 0.41742 0.29007 0.35629 0.04275  -0.01520 -0.00857 217 HIS A CG  
1766 N  ND1 . HIS A 217 ? 0.40242 0.27793 0.33866 0.03366  -0.01856 -0.00976 217 HIS A ND1 
1767 C  CD2 . HIS A 217 ? 0.42910 0.27829 0.35541 0.04437  -0.01744 -0.01064 217 HIS A CD2 
1768 C  CE1 . HIS A 217 ? 0.41709 0.27326 0.34060 0.02936  -0.02316 -0.01216 217 HIS A CE1 
1769 N  NE2 . HIS A 217 ? 0.43233 0.27132 0.34888 0.03535  -0.02264 -0.01303 217 HIS A NE2 
1770 N  N   . PHE A 218 ? 0.30360 0.23374 0.28613 0.04530  -0.01497 0.00612  218 PHE A N   
1771 C  CA  . PHE A 218 ? 0.28755 0.23877 0.28316 0.04477  -0.01499 0.00940  218 PHE A CA  
1772 C  C   . PHE A 218 ? 0.28529 0.24924 0.28672 0.04609  -0.01001 0.00676  218 PHE A C   
1773 O  O   . PHE A 218 ? 0.29033 0.24966 0.28526 0.04381  -0.00771 0.00279  218 PHE A O   
1774 C  CB  . PHE A 218 ? 0.27331 0.23086 0.26992 0.03559  -0.01953 0.01161  218 PHE A CB  
1775 C  CG  . PHE A 218 ? 0.25932 0.23648 0.26631 0.03371  -0.01996 0.01362  218 PHE A CG  
1776 C  CD1 . PHE A 218 ? 0.25516 0.23943 0.26779 0.03576  -0.02289 0.01837  218 PHE A CD1 
1777 C  CD2 . PHE A 218 ? 0.25203 0.23927 0.26213 0.02953  -0.01808 0.01084  218 PHE A CD2 
1778 C  CE1 . PHE A 218 ? 0.24471 0.24569 0.26514 0.03325  -0.02427 0.01973  218 PHE A CE1 
1779 C  CE2 . PHE A 218 ? 0.24217 0.24501 0.26040 0.02722  -0.01896 0.01209  218 PHE A CE2 
1780 C  CZ  . PHE A 218 ? 0.23880 0.24846 0.26180 0.02880  -0.02226 0.01625  218 PHE A CZ  
1781 N  N   . GLY A 219 ? 0.31132 0.29145 0.32518 0.04942  -0.00880 0.00953  219 GLY A N   
1782 C  CA  . GLY A 219 ? 0.31646 0.31144 0.33827 0.04835  -0.00516 0.00838  219 GLY A CA  
1783 C  C   . GLY A 219 ? 0.33299 0.33009 0.35855 0.05683  0.00166  0.00762  219 GLY A C   
1784 O  O   . GLY A 219 ? 0.35069 0.33427 0.36900 0.06370  0.00457  0.00617  219 GLY A O   
1785 N  N   . GLU A 220 ? 0.26430 0.27841 0.30125 0.05619  0.00456  0.00866  220 GLU A N   
1786 C  CA  . GLU A 220 ? 0.27947 0.29942 0.32199 0.06323  0.01223  0.00861  220 GLU A CA  
1787 C  C   . GLU A 220 ? 0.29154 0.30580 0.32458 0.06052  0.01706  0.00458  220 GLU A C   
1788 O  O   . GLU A 220 ? 0.28378 0.29893 0.31384 0.05228  0.01428  0.00328  220 GLU A O   
1789 C  CB  . GLU A 220 ? 0.26509 0.30791 0.32673 0.06315  0.01243  0.01297  220 GLU A CB  
1790 C  CG  . GLU A 220 ? 0.27576 0.32752 0.34800 0.07287  0.01975  0.01530  220 GLU A CG  
1791 C  CD  . GLU A 220 ? 0.29058 0.34606 0.37193 0.08068  0.01727  0.01964  220 GLU A CD  
1792 O  OE1 . GLU A 220 ? 0.27924 0.32570 0.35470 0.07912  0.01041  0.02033  220 GLU A OE1 
1793 O  OE2 . GLU A 220 ? 0.28691 0.35487 0.38189 0.08855  0.02236  0.02295  220 GLU A OE2 
1794 N  N   . VAL A 221 ? 0.48299 0.49099 0.51066 0.06800  0.02449  0.00279  221 VAL A N   
1795 C  CA  . VAL A 221 ? 0.50500 0.50729 0.52206 0.06630  0.02954  -0.00053 221 VAL A CA  
1796 C  C   . VAL A 221 ? 0.50189 0.52252 0.53194 0.06716  0.03614  0.00228  221 VAL A C   
1797 O  O   . VAL A 221 ? 0.51246 0.53447 0.53856 0.06249  0.03869  0.00143  221 VAL A O   
1798 C  CB  . VAL A 221 ? 0.53294 0.51504 0.53248 0.07333  0.03396  -0.00478 221 VAL A CB  
1799 C  CG1 . VAL A 221 ? 0.53976 0.50501 0.53021 0.07342  0.02754  -0.00638 221 VAL A CG1 
1800 C  CG2 . VAL A 221 ? 0.54236 0.52967 0.54780 0.08451  0.04310  -0.00361 221 VAL A CG2 
1801 N  N   . GLU A 222 ? 0.89148 0.92665 0.93779 0.07295  0.03871  0.00629  222 GLU A N   
1802 C  CA  . GLU A 222 ? 0.88560 0.93948 0.94628 0.07391  0.04543  0.00976  222 GLU A CA  
1803 C  C   . GLU A 222 ? 0.87467 0.94146 0.94495 0.06295  0.04045  0.01178  222 GLU A C   
1804 O  O   . GLU A 222 ? 0.86568 0.93418 0.93918 0.05734  0.03191  0.01221  222 GLU A O   
1805 C  CB  . GLU A 222 ? 0.88576 0.95363 0.96373 0.08280  0.04849  0.01423  222 GLU A CB  
1806 C  CG  . GLU A 222 ? 0.87911 0.97235 0.97904 0.08074  0.05154  0.01973  222 GLU A CG  
1807 C  CD  . GLU A 222 ? 0.86358 0.97109 0.97880 0.07406  0.04167  0.02338  222 GLU A CD  
1808 O  OE1 . GLU A 222 ? 0.85734 0.96542 0.97732 0.07864  0.03679  0.02524  222 GLU A OE1 
1809 O  OE2 . GLU A 222 ? 0.85529 0.97222 0.97660 0.06428  0.03861  0.02438  222 GLU A OE2 
1810 N  N   . GLY A 223 ? 0.40497 0.47957 0.47854 0.05995  0.04613  0.01299  223 GLY A N   
1811 C  CA  . GLY A 223 ? 0.39768 0.48006 0.47707 0.04945  0.04205  0.01414  223 GLY A CA  
1812 C  C   . GLY A 223 ? 0.40025 0.46728 0.46306 0.04322  0.03863  0.01019  223 GLY A C   
1813 O  O   . GLY A 223 ? 0.39950 0.47029 0.46586 0.03494  0.03437  0.01058  223 GLY A O   
1814 N  N   . PHE A 224 ? 0.27637 0.32595 0.32139 0.04700  0.03996  0.00644  224 PHE A N   
1815 C  CA  . PHE A 224 ? 0.28271 0.31858 0.31257 0.04161  0.03661  0.00328  224 PHE A CA  
1816 C  C   . PHE A 224 ? 0.28055 0.32138 0.31165 0.03631  0.03979  0.00501  224 PHE A C   
1817 O  O   . PHE A 224 ? 0.28020 0.32439 0.31084 0.03942  0.04778  0.00672  224 PHE A O   
1818 C  CB  . PHE A 224 ? 0.30668 0.32439 0.31765 0.04697  0.03877  -0.00050 224 PHE A CB  
1819 C  CG  . PHE A 224 ? 0.31158 0.31574 0.30741 0.04158  0.03431  -0.00330 224 PHE A CG  
1820 C  CD1 . PHE A 224 ? 0.32225 0.32255 0.30863 0.03997  0.03805  -0.00337 224 PHE A CD1 
1821 C  CD2 . PHE A 224 ? 0.30591 0.30193 0.29746 0.03817  0.02634  -0.00515 224 PHE A CD2 
1822 C  CE1 . PHE A 224 ? 0.32158 0.31053 0.29516 0.03528  0.03308  -0.00525 224 PHE A CE1 
1823 C  CE2 . PHE A 224 ? 0.31344 0.29917 0.29348 0.03330  0.02197  -0.00701 224 PHE A CE2 
1824 C  CZ  . PHE A 224 ? 0.32710 0.30944 0.29842 0.03200  0.02495  -0.00707 224 PHE A CZ  
1825 N  N   . GLY A 225 ? 0.23449 0.27532 0.26690 0.02861  0.03398  0.00483  225 GLY A N   
1826 C  CA  . GLY A 225 ? 0.22078 0.26509 0.25509 0.02325  0.03617  0.00687  225 GLY A CA  
1827 C  C   . GLY A 225 ? 0.22117 0.25457 0.24507 0.01827  0.03138  0.00501  225 GLY A C   
1828 O  O   . GLY A 225 ? 0.21059 0.24637 0.23803 0.01290  0.03092  0.00669  225 GLY A O   
1829 N  N   . TRP A 226 ? 0.23980 0.26118 0.25159 0.01998  0.02763  0.00190  226 TRP A N   
1830 C  CA  . TRP A 226 ? 0.23673 0.24933 0.24023 0.01579  0.02281  0.00071  226 TRP A CA  
1831 C  C   . TRP A 226 ? 0.23907 0.24362 0.22976 0.01639  0.02617  0.00137  226 TRP A C   
1832 O  O   . TRP A 226 ? 0.25369 0.25435 0.23603 0.02114  0.03135  0.00095  226 TRP A O   
1833 C  CB  . TRP A 226 ? 0.24581 0.25021 0.24302 0.01634  0.01693  -0.00207 226 TRP A CB  
1834 C  CG  . TRP A 226 ? 0.24748 0.25859 0.25498 0.01512  0.01308  -0.00222 226 TRP A CG  
1835 C  CD1 . TRP A 226 ? 0.25698 0.26906 0.26688 0.01876  0.01249  -0.00261 226 TRP A CD1 
1836 C  CD2 . TRP A 226 ? 0.23691 0.25369 0.25221 0.01020  0.00935  -0.00188 226 TRP A CD2 
1837 N  NE1 . TRP A 226 ? 0.23695 0.25558 0.25526 0.01599  0.00828  -0.00210 226 TRP A NE1 
1838 C  CE2 . TRP A 226 ? 0.23483 0.25622 0.25596 0.01075  0.00654  -0.00206 226 TRP A CE2 
1839 C  CE3 . TRP A 226 ? 0.21830 0.23561 0.23529 0.00582  0.00827  -0.00148 226 TRP A CE3 
1840 C  CZ2 . TRP A 226 ? 0.21955 0.24606 0.24663 0.00681  0.00290  -0.00224 226 TRP A CZ2 
1841 C  CZ3 . TRP A 226 ? 0.20815 0.22988 0.23172 0.00242  0.00501  -0.00207 226 TRP A CZ3 
1842 C  CH2 . TRP A 226 ? 0.21553 0.24182 0.24336 0.00280  0.00245  -0.00264 226 TRP A CH2 
1843 N  N   . PRO A 227 ? 0.24498 0.24646 0.23319 0.01206  0.02346  0.00254  227 PRO A N   
1844 C  CA  . PRO A 227 ? 0.24732 0.24052 0.22195 0.01239  0.02549  0.00379  227 PRO A CA  
1845 C  C   . PRO A 227 ? 0.25570 0.23652 0.21500 0.01408  0.02120  0.00086  227 PRO A C   
1846 O  O   . PRO A 227 ? 0.25401 0.23252 0.21481 0.01260  0.01487  -0.00108 227 PRO A O   
1847 C  CB  . PRO A 227 ? 0.23046 0.22456 0.20955 0.00740  0.02273  0.00639  227 PRO A CB  
1848 C  CG  . PRO A 227 ? 0.21698 0.21510 0.20659 0.00503  0.01726  0.00458  227 PRO A CG  
1849 C  CD  . PRO A 227 ? 0.23421 0.23954 0.23170 0.00717  0.01886  0.00303  227 PRO A CD  
1850 N  N   . THR A 228 ? 0.26668 0.23930 0.21055 0.01677  0.02468  0.00069  228 THR A N   
1851 C  CA  . THR A 228 ? 0.27835 0.23751 0.20535 0.01815  0.02054  -0.00263 228 THR A CA  
1852 C  C   . THR A 228 ? 0.27521 0.22539 0.18670 0.01617  0.01789  -0.00124 228 THR A C   
1853 O  O   . THR A 228 ? 0.29065 0.22881 0.18633 0.01657  0.01369  -0.00404 228 THR A O   
1854 C  CB  . THR A 228 ? 0.30020 0.25398 0.21840 0.02439  0.02641  -0.00570 228 THR A CB  
1855 O  OG1 . THR A 228 ? 0.30202 0.25705 0.21386 0.02737  0.03526  -0.00367 228 THR A OG1 
1856 C  CG2 . THR A 228 ? 0.30153 0.26422 0.23523 0.02696  0.02822  -0.00639 228 THR A CG2 
1857 N  N   . ASN A 229 ? 0.29656 0.25129 0.21141 0.01381  0.01963  0.00317  229 ASN A N   
1858 C  CA  . ASN A 229 ? 0.29439 0.24108 0.19496 0.01202  0.01651  0.00559  229 ASN A CA  
1859 C  C   . ASN A 229 ? 0.27694 0.23008 0.18942 0.00830  0.01460  0.01038  229 ASN A C   
1860 O  O   . ASN A 229 ? 0.26920 0.23191 0.19865 0.00717  0.01695  0.01126  229 ASN A O   
1861 C  CB  . ASN A 229 ? 0.30912 0.24974 0.19247 0.01532  0.02414  0.00635  229 ASN A CB  
1862 C  CG  . ASN A 229 ? 0.31295 0.26391 0.20650 0.01641  0.03424  0.01007  229 ASN A CG  
1863 O  OD1 . ASN A 229 ? 0.29188 0.24967 0.19711 0.01288  0.03435  0.01452  229 ASN A OD1 
1864 N  ND2 . ASN A 229 ? 0.32003 0.27190 0.20942 0.02135  0.04290  0.00843  229 ASN A ND2 
1865 N  N   . PRO A 230 ? 0.37423 0.32151 0.27782 0.00639  0.00972  0.01353  230 PRO A N   
1866 C  CA  . PRO A 230 ? 0.37268 0.32444 0.28772 0.00367  0.00778  0.01816  230 PRO A CA  
1867 C  C   . PRO A 230 ? 0.36288 0.32015 0.28576 0.00306  0.01588  0.02168  230 PRO A C   
1868 O  O   . PRO A 230 ? 0.35603 0.31858 0.29376 0.00087  0.01536  0.02321  230 PRO A O   
1869 C  CB  . PRO A 230 ? 0.38624 0.32965 0.28712 0.00283  0.00181  0.02160  230 PRO A CB  
1870 C  CG  . PRO A 230 ? 0.39195 0.32826 0.27915 0.00350  -0.00325 0.01738  230 PRO A CG  
1871 C  CD  . PRO A 230 ? 0.37984 0.31582 0.26354 0.00641  0.00410  0.01285  230 PRO A CD  
1872 N  N   . ASP A 231 ? 0.44497 0.40092 0.35816 0.00476  0.02355  0.02305  231 ASP A N   
1873 C  CA  . ASP A 231 ? 0.43994 0.40225 0.36180 0.00324  0.03134  0.02737  231 ASP A CA  
1874 C  C   . ASP A 231 ? 0.42967 0.40318 0.37058 0.00268  0.03427  0.02497  231 ASP A C   
1875 O  O   . ASP A 231 ? 0.41721 0.39626 0.37186 -0.00083 0.03537  0.02759  231 ASP A O   
1876 C  CB  . ASP A 231 ? 0.45216 0.41167 0.35913 0.00549  0.03976  0.02989  231 ASP A CB  
1877 C  CG  . ASP A 231 ? 0.47148 0.42108 0.36125 0.00456  0.03776  0.03476  231 ASP A CG  
1878 O  OD1 . ASP A 231 ? 0.48730 0.43139 0.37464 0.00322  0.02856  0.03516  231 ASP A OD1 
1879 O  OD2 . ASP A 231 ? 0.48928 0.43724 0.36819 0.00533  0.04549  0.03869  231 ASP A OD2 
1880 N  N   . GLU A 232 ? 0.26861 0.24468 0.20998 0.00592  0.03501  0.02010  232 GLU A N   
1881 C  CA  . GLU A 232 ? 0.25757 0.24450 0.21654 0.00559  0.03652  0.01817  232 GLU A CA  
1882 C  C   . GLU A 232 ? 0.25432 0.24295 0.22467 0.00243  0.02910  0.01648  232 GLU A C   
1883 O  O   . GLU A 232 ? 0.24930 0.24584 0.23429 -0.00021 0.02965  0.01678  232 GLU A O   
1884 C  CB  . GLU A 232 ? 0.25675 0.24448 0.21252 0.01060  0.03862  0.01386  232 GLU A CB  
1885 C  CG  . GLU A 232 ? 0.26519 0.25103 0.20926 0.01515  0.04733  0.01471  232 GLU A CG  
1886 C  CD  . GLU A 232 ? 0.26860 0.25229 0.20814 0.02110  0.04905  0.00990  232 GLU A CD  
1887 O  OE1 . GLU A 232 ? 0.26930 0.24989 0.21068 0.02113  0.04218  0.00606  232 GLU A OE1 
1888 O  OE2 . GLU A 232 ? 0.27076 0.25559 0.20496 0.02601  0.05773  0.01023  232 GLU A OE2 
1889 N  N   . ALA A 233 ? 0.26894 0.25047 0.23261 0.00254  0.02213  0.01475  233 ALA A N   
1890 C  CA  . ALA A 233 ? 0.26802 0.25149 0.24195 0.00031  0.01619  0.01337  233 ALA A CA  
1891 C  C   . ALA A 233 ? 0.27526 0.25822 0.25535 -0.00281 0.01610  0.01694  233 ALA A C   
1892 O  O   . ALA A 233 ? 0.26817 0.25479 0.25972 -0.00487 0.01463  0.01575  233 ALA A O   
1893 C  CB  . ALA A 233 ? 0.26890 0.24653 0.23565 0.00116  0.00925  0.01153  233 ALA A CB  
1894 N  N   . THR A 234 ? 0.26826 0.24536 0.23961 -0.00313 0.01754  0.02132  234 THR A N   
1895 C  CA  . THR A 234 ? 0.27582 0.25061 0.25245 -0.00598 0.01789  0.02538  234 THR A CA  
1896 C  C   . THR A 234 ? 0.27391 0.25513 0.26180 -0.00919 0.02318  0.02621  234 THR A C   
1897 O  O   . THR A 234 ? 0.27226 0.25280 0.26935 -0.01228 0.02196  0.02667  234 THR A O   
1898 C  CB  . THR A 234 ? 0.28656 0.25351 0.25019 -0.00563 0.01855  0.03082  234 THR A CB  
1899 O  OG1 . THR A 234 ? 0.28632 0.24790 0.24158 -0.00354 0.01170  0.03046  234 THR A OG1 
1900 C  CG2 . THR A 234 ? 0.28804 0.25135 0.25697 -0.00864 0.01972  0.03586  234 THR A CG2 
1901 N  N   . ALA A 235 ? 0.27657 0.26403 0.26417 -0.00846 0.02894  0.02635  235 ALA A N   
1902 C  CA  . ALA A 235 ? 0.27336 0.26957 0.27390 -0.01190 0.03341  0.02764  235 ALA A CA  
1903 C  C   . ALA A 235 ? 0.26645 0.26819 0.27947 -0.01352 0.02927  0.02311  235 ALA A C   
1904 O  O   . ALA A 235 ? 0.26334 0.26814 0.28703 -0.01821 0.02924  0.02385  235 ALA A O   
1905 C  CB  . ALA A 235 ? 0.26230 0.26593 0.26131 -0.00944 0.04066  0.02881  235 ALA A CB  
1906 N  N   . ILE A 236 ? 0.31526 0.31759 0.32615 -0.01016 0.02551  0.01851  236 ILE A N   
1907 C  CA  . ILE A 236 ? 0.30700 0.31368 0.32726 -0.01145 0.02145  0.01447  236 ILE A CA  
1908 C  C   . ILE A 236 ? 0.31585 0.31592 0.33789 -0.01380 0.01736  0.01371  236 ILE A C   
1909 O  O   . ILE A 236 ? 0.31575 0.31770 0.34594 -0.01713 0.01586  0.01191  236 ILE A O   
1910 C  CB  . ILE A 236 ? 0.31107 0.31900 0.32758 -0.00737 0.01883  0.01067  236 ILE A CB  
1911 C  CG1 . ILE A 236 ? 0.29929 0.31429 0.31714 -0.00466 0.02309  0.01075  236 ILE A CG1 
1912 C  CG2 . ILE A 236 ? 0.29856 0.30857 0.32145 -0.00857 0.01408  0.00702  236 ILE A CG2 
1913 C  CD1 . ILE A 236 ? 0.29617 0.32212 0.32782 -0.00735 0.02466  0.01140  236 ILE A CD1 
1914 N  N   . LEU A 237 ? 0.20521 0.19714 0.21934 -0.01186 0.01534  0.01508  237 LEU A N   
1915 C  CA  . LEU A 237 ? 0.21252 0.19804 0.22885 -0.01263 0.01210  0.01473  237 LEU A CA  
1916 C  C   . LEU A 237 ? 0.22300 0.20403 0.24321 -0.01669 0.01427  0.01777  237 LEU A C   
1917 O  O   . LEU A 237 ? 0.22365 0.20120 0.24926 -0.01877 0.01259  0.01562  237 LEU A O   
1918 C  CB  . LEU A 237 ? 0.22013 0.19972 0.22871 -0.00922 0.00902  0.01649  237 LEU A CB  
1919 C  CG  . LEU A 237 ? 0.22935 0.20308 0.24103 -0.00827 0.00599  0.01671  237 LEU A CG  
1920 C  CD1 . LEU A 237 ? 0.22831 0.20576 0.24653 -0.00768 0.00417  0.01156  237 LEU A CD1 
1921 C  CD2 . LEU A 237 ? 0.23461 0.20441 0.23984 -0.00508 0.00259  0.02000  237 LEU A CD2 
1922 N  N   . ASP A 238 ? 0.32878 0.30889 0.34544 -0.01804 0.01820  0.02278  238 ASP A N   
1923 C  CA  . ASP A 238 ? 0.33968 0.31584 0.36077 -0.02299 0.02059  0.02650  238 ASP A CA  
1924 C  C   . ASP A 238 ? 0.33690 0.31924 0.36923 -0.02784 0.02062  0.02357  238 ASP A C   
1925 O  O   . ASP A 238 ? 0.34171 0.31774 0.37859 -0.03194 0.01907  0.02308  238 ASP A O   
1926 C  CB  . ASP A 238 ? 0.33927 0.31626 0.35509 -0.02389 0.02599  0.03274  238 ASP A CB  
1927 C  CG  . ASP A 238 ? 0.34775 0.31590 0.35101 -0.02050 0.02508  0.03669  238 ASP A CG  
1928 O  OD1 . ASP A 238 ? 0.36475 0.32617 0.36615 -0.01805 0.02008  0.03551  238 ASP A OD1 
1929 O  OD2 . ASP A 238 ? 0.35940 0.32779 0.35455 -0.02011 0.02942  0.04122  238 ASP A OD2 
1930 N  N   . HIS A 239 ? 0.30101 0.29497 0.33750 -0.02737 0.02186  0.02158  239 HIS A N   
1931 C  CA  . HIS A 239 ? 0.29070 0.29237 0.33823 -0.03206 0.02090  0.01937  239 HIS A CA  
1932 C  C   . HIS A 239 ? 0.29865 0.29546 0.34738 -0.03282 0.01548  0.01361  239 HIS A C   
1933 O  O   . HIS A 239 ? 0.30162 0.29661 0.35616 -0.03840 0.01354  0.01221  239 HIS A O   
1934 C  CB  . HIS A 239 ? 0.27637 0.29150 0.32782 -0.02970 0.02288  0.01877  239 HIS A CB  
1935 C  CG  . HIS A 239 ? 0.27613 0.30022 0.33817 -0.03315 0.01986  0.01589  239 HIS A CG  
1936 N  ND1 . HIS A 239 ? 0.27828 0.30695 0.35080 -0.04027 0.01977  0.01794  239 HIS A ND1 
1937 C  CD2 . HIS A 239 ? 0.26827 0.29752 0.33166 -0.03089 0.01623  0.01155  239 HIS A CD2 
1938 C  CE1 . HIS A 239 ? 0.26685 0.30344 0.34646 -0.04218 0.01565  0.01475  239 HIS A CE1 
1939 N  NE2 . HIS A 239 ? 0.26602 0.30292 0.33983 -0.03629 0.01368  0.01099  239 HIS A NE2 
1940 N  N   . PHE A 240 ? 0.21253 0.20685 0.25533 -0.02755 0.01307  0.01025  240 PHE A N   
1941 C  CA  . PHE A 240 ? 0.22188 0.21211 0.26484 -0.02747 0.00916  0.00494  240 PHE A CA  
1942 C  C   . PHE A 240 ? 0.23906 0.21618 0.28045 -0.02899 0.00848  0.00491  240 PHE A C   
1943 O  O   . PHE A 240 ? 0.24340 0.21590 0.28695 -0.03262 0.00653  0.00134  240 PHE A O   
1944 C  CB  . PHE A 240 ? 0.21696 0.20860 0.25502 -0.02167 0.00751  0.00248  240 PHE A CB  
1945 C  CG  . PHE A 240 ? 0.22424 0.21057 0.26117 -0.02046 0.00502  -0.00195 240 PHE A CG  
1946 C  CD1 . PHE A 240 ? 0.22264 0.21149 0.26166 -0.02300 0.00307  -0.00641 240 PHE A CD1 
1947 C  CD2 . PHE A 240 ? 0.23322 0.21230 0.26684 -0.01657 0.00476  -0.00140 240 PHE A CD2 
1948 C  CE1 . PHE A 240 ? 0.23472 0.21807 0.27085 -0.02144 0.00180  -0.01075 240 PHE A CE1 
1949 C  CE2 . PHE A 240 ? 0.24041 0.21532 0.27353 -0.01457 0.00375  -0.00534 240 PHE A CE2 
1950 C  CZ  . PHE A 240 ? 0.23731 0.21386 0.27085 -0.01692 0.00272  -0.01027 240 PHE A CZ  
1951 N  N   . ILE A 241 ? 0.29109 0.26108 0.32783 -0.02601 0.00972  0.00878  241 ILE A N   
1952 C  CA  . ILE A 241 ? 0.30800 0.26449 0.34316 -0.02581 0.00904  0.00923  241 ILE A CA  
1953 C  C   . ILE A 241 ? 0.31656 0.26683 0.35563 -0.03292 0.00957  0.01008  241 ILE A C   
1954 O  O   . ILE A 241 ? 0.32723 0.26724 0.36634 -0.03457 0.00787  0.00647  241 ILE A O   
1955 C  CB  . ILE A 241 ? 0.31894 0.27021 0.34888 -0.02166 0.00977  0.01481  241 ILE A CB  
1956 C  CG1 . ILE A 241 ? 0.30360 0.26032 0.33031 -0.01559 0.00794  0.01372  241 ILE A CG1 
1957 C  CG2 . ILE A 241 ? 0.32310 0.25984 0.35235 -0.02104 0.00921  0.01634  241 ILE A CG2 
1958 C  CD1 . ILE A 241 ? 0.31623 0.27084 0.34484 -0.01197 0.00591  0.00911  241 ILE A CD1 
1959 N  N   . ALA A 242 ? 0.34657 0.30272 0.38889 -0.03739 0.01212  0.01483  242 ALA A N   
1960 C  CA  . ALA A 242 ? 0.35451 0.30507 0.40163 -0.04516 0.01267  0.01721  242 ALA A CA  
1961 C  C   . ALA A 242 ? 0.35342 0.30931 0.40728 -0.05121 0.00982  0.01235  242 ALA A C   
1962 O  O   . ALA A 242 ? 0.36340 0.30928 0.41895 -0.05713 0.00764  0.01068  242 ALA A O   
1963 C  CB  . ALA A 242 ? 0.34049 0.29674 0.38940 -0.04790 0.01724  0.02504  242 ALA A CB  
1964 N  N   . ASP A 243 ? 0.44152 0.41207 0.49865 -0.04995 0.00922  0.01008  243 ASP A N   
1965 C  CA  . ASP A 243 ? 0.43961 0.41828 0.50436 -0.05623 0.00618  0.00734  243 ASP A CA  
1966 C  C   . ASP A 243 ? 0.43932 0.41826 0.50067 -0.05424 0.00173  -0.00016 243 ASP A C   
1967 O  O   . ASP A 243 ? 0.43509 0.41572 0.50004 -0.06026 -0.00231 -0.00331 243 ASP A O   
1968 C  CB  . ASP A 243 ? 0.42200 0.41884 0.49514 -0.05698 0.00891  0.01165  243 ASP A CB  
1969 C  CG  . ASP A 243 ? 0.42724 0.42564 0.50440 -0.06011 0.01414  0.01942  243 ASP A CG  
1970 O  OD1 . ASP A 243 ? 0.44638 0.43193 0.52158 -0.06401 0.01442  0.02171  243 ASP A OD1 
1971 O  OD2 . ASP A 243 ? 0.42946 0.44135 0.51121 -0.05834 0.01839  0.02344  243 ASP A OD2 
1972 N  N   . MET A 244 ? 0.31786 0.29549 0.37226 -0.04653 0.00213  -0.00274 244 MET A N   
1973 C  CA  . MET A 244 ? 0.31398 0.29330 0.36480 -0.04448 -0.00115 -0.00896 244 MET A CA  
1974 C  C   . MET A 244 ? 0.33295 0.29933 0.37556 -0.04002 -0.00130 -0.01331 244 MET A C   
1975 O  O   . MET A 244 ? 0.34167 0.30477 0.38017 -0.04065 -0.00383 -0.01909 244 MET A O   
1976 C  CB  . MET A 244 ? 0.30221 0.29488 0.35372 -0.03953 -0.00052 -0.00814 244 MET A CB  
1977 C  CG  . MET A 244 ? 0.29240 0.29759 0.35169 -0.04120 0.00146  -0.00313 244 MET A CG  
1978 S  SD  . MET A 244 ? 0.29285 0.31055 0.36098 -0.04703 -0.00285 -0.00446 244 MET A SD  
1979 C  CE  . MET A 244 ? 0.26821 0.29415 0.34823 -0.05254 0.00048  0.00248  244 MET A CE  
1980 N  N   . LEU A 245 ? 0.26091 0.22035 0.30092 -0.03524 0.00140  -0.01048 245 LEU A N   
1981 C  CA  . LEU A 245 ? 0.27578 0.22444 0.31019 -0.03000 0.00183  -0.01381 245 LEU A CA  
1982 C  C   . LEU A 245 ? 0.29151 0.22625 0.32228 -0.03324 0.00038  -0.01922 245 LEU A C   
1983 O  O   . LEU A 245 ? 0.29609 0.22634 0.32149 -0.02928 0.00050  -0.02456 245 LEU A O   
1984 C  CB  . LEU A 245 ? 0.27761 0.22077 0.31150 -0.02535 0.00410  -0.00856 245 LEU A CB  
1985 C  CG  . LEU A 245 ? 0.29743 0.23117 0.32812 -0.01871 0.00491  -0.01055 245 LEU A CG  
1986 C  CD1 . LEU A 245 ? 0.27768 0.21993 0.30716 -0.01402 0.00486  -0.01423 245 LEU A CD1 
1987 C  CD2 . LEU A 245 ? 0.28799 0.21793 0.31915 -0.01454 0.00596  -0.00415 245 LEU A CD2 
1988 N  N   . PRO A 246 ? 0.31571 0.24251 0.34842 -0.04032 -0.00080 -0.01832 246 PRO A N   
1989 C  CA  . PRO A 246 ? 0.33281 0.24378 0.36009 -0.04372 -0.00283 -0.02450 246 PRO A CA  
1990 C  C   . PRO A 246 ? 0.32989 0.24448 0.35253 -0.04588 -0.00607 -0.03161 246 PRO A C   
1991 O  O   . PRO A 246 ? 0.34203 0.24256 0.35634 -0.04595 -0.00702 -0.03824 246 PRO A O   
1992 C  CB  . PRO A 246 ? 0.32525 0.23055 0.35742 -0.05287 -0.00428 -0.02089 246 PRO A CB  
1993 C  CG  . PRO A 246 ? 0.31831 0.23029 0.35590 -0.05086 -0.00092 -0.01230 246 PRO A CG  
1994 C  CD  . PRO A 246 ? 0.30711 0.23636 0.34599 -0.04520 0.00024  -0.01134 246 PRO A CD  
1995 N  N   . SER A 247 ? 0.36223 0.29415 0.38886 -0.04723 -0.00773 -0.03044 247 SER A N   
1996 C  CA  . SER A 247 ? 0.36709 0.30346 0.38895 -0.04943 -0.01146 -0.03610 247 SER A CA  
1997 C  C   . SER A 247 ? 0.36468 0.30912 0.38242 -0.04170 -0.00948 -0.03748 247 SER A C   
1998 O  O   . SER A 247 ? 0.36719 0.31713 0.38058 -0.04289 -0.01228 -0.04099 247 SER A O   
1999 C  CB  . SER A 247 ? 0.35505 0.30525 0.38521 -0.05705 -0.01566 -0.03336 247 SER A CB  
2000 O  OG  . SER A 247 ? 0.36311 0.30581 0.39663 -0.06605 -0.01866 -0.03317 247 SER A OG  
2001 N  N   . PHE A 248 ? 0.37081 0.31610 0.38980 -0.03430 -0.00515 -0.03436 248 PHE A N   
2002 C  CA  . PHE A 248 ? 0.36101 0.31579 0.37836 -0.02805 -0.00348 -0.03425 248 PHE A CA  
2003 C  C   . PHE A 248 ? 0.37398 0.32326 0.38167 -0.02566 -0.00304 -0.04082 248 PHE A C   
2004 O  O   . PHE A 248 ? 0.37111 0.32936 0.37597 -0.02480 -0.00392 -0.04185 248 PHE A O   
2005 C  CB  . PHE A 248 ? 0.36168 0.31709 0.38240 -0.02151 0.00016  -0.02971 248 PHE A CB  
2006 C  CG  . PHE A 248 ? 0.35256 0.31963 0.37415 -0.01684 0.00107  -0.02790 248 PHE A CG  
2007 C  CD1 . PHE A 248 ? 0.33767 0.31650 0.36307 -0.01838 -0.00046 -0.02449 248 PHE A CD1 
2008 C  CD2 . PHE A 248 ? 0.35861 0.32462 0.37763 -0.01090 0.00369  -0.02941 248 PHE A CD2 
2009 C  CE1 . PHE A 248 ? 0.32604 0.31339 0.35159 -0.01469 -0.00004 -0.02288 248 PHE A CE1 
2010 C  CE2 . PHE A 248 ? 0.35257 0.32919 0.37316 -0.00775 0.00421  -0.02720 248 PHE A CE2 
2011 C  CZ  . PHE A 248 ? 0.33436 0.32067 0.35766 -0.00996 0.00200  -0.02406 248 PHE A CZ  
2012 N  N   . GLY A 249 ? 0.54829 0.48207 0.54998 -0.02420 -0.00128 -0.04517 249 GLY A N   
2013 C  CA  . GLY A 249 ? 0.55972 0.48717 0.55078 -0.02064 0.00066  -0.05166 249 GLY A CA  
2014 C  C   . GLY A 249 ? 0.56379 0.48913 0.54557 -0.02684 -0.00380 -0.05738 249 GLY A C   
2015 O  O   . GLY A 249 ? 0.57554 0.49677 0.54629 -0.02400 -0.00209 -0.06275 249 GLY A O   
2016 N  N   . ASP A 250 ? 0.45197 0.38073 0.43790 -0.03519 -0.00946 -0.05603 250 ASP A N   
2017 C  CA  . ASP A 250 ? 0.45108 0.37768 0.42881 -0.04212 -0.01528 -0.06113 250 ASP A CA  
2018 C  C   . ASP A 250 ? 0.45136 0.39429 0.42892 -0.04241 -0.01803 -0.05932 250 ASP A C   
2019 O  O   . ASP A 250 ? 0.45501 0.39549 0.42049 -0.04350 -0.02033 -0.06430 250 ASP A O   
2020 C  CB  . ASP A 250 ? 0.45588 0.37953 0.43993 -0.05174 -0.02076 -0.05996 250 ASP A CB  
2021 C  CG  . ASP A 250 ? 0.47651 0.38004 0.45765 -0.05302 -0.01925 -0.06274 250 ASP A CG  
2022 O  OD1 . ASP A 250 ? 0.49791 0.38669 0.46786 -0.04766 -0.01562 -0.06849 250 ASP A OD1 
2023 O  OD2 . ASP A 250 ? 0.47271 0.37495 0.46285 -0.05918 -0.02130 -0.05889 250 ASP A OD2 
2024 N  N   . TRP A 251 ? 0.42329 0.38165 0.41273 -0.04120 -0.01779 -0.05231 251 TRP A N   
2025 C  CA  . TRP A 251 ? 0.42480 0.39798 0.41587 -0.04204 -0.02120 -0.04969 251 TRP A CA  
2026 C  C   . TRP A 251 ? 0.41575 0.39839 0.41072 -0.03489 -0.01673 -0.04512 251 TRP A C   
2027 O  O   . TRP A 251 ? 0.40763 0.40273 0.40990 -0.03479 -0.01834 -0.04024 251 TRP A O   
2028 C  CB  . TRP A 251 ? 0.40318 0.38633 0.40564 -0.04860 -0.02645 -0.04558 251 TRP A CB  
2029 C  CG  . TRP A 251 ? 0.40746 0.38130 0.41020 -0.05657 -0.03039 -0.04844 251 TRP A CG  
2030 C  CD1 . TRP A 251 ? 0.40305 0.37521 0.41603 -0.06019 -0.02966 -0.04511 251 TRP A CD1 
2031 C  CD2 . TRP A 251 ? 0.42214 0.38608 0.41359 -0.06255 -0.03594 -0.05508 251 TRP A CD2 
2032 N  NE1 . TRP A 251 ? 0.41016 0.37212 0.42026 -0.06850 -0.03452 -0.04894 251 TRP A NE1 
2033 C  CE2 . TRP A 251 ? 0.42260 0.37884 0.41909 -0.07017 -0.03880 -0.05550 251 TRP A CE2 
2034 C  CE3 . TRP A 251 ? 0.43211 0.39222 0.40847 -0.06253 -0.03885 -0.06065 251 TRP A CE3 
2035 C  CZ2 . TRP A 251 ? 0.42702 0.37116 0.41419 -0.07812 -0.04514 -0.06175 251 TRP A CZ2 
2036 C  CZ3 . TRP A 251 ? 0.44245 0.39058 0.40814 -0.06989 -0.04492 -0.06713 251 TRP A CZ3 
2037 C  CH2 . TRP A 251 ? 0.44474 0.38462 0.41597 -0.07778 -0.04834 -0.06788 251 TRP A CH2 
2038 N  N   . GLN A 252 ? 0.61343 0.59008 0.60392 -0.02879 -0.01116 -0.04656 252 GLN A N   
2039 C  CA  . GLN A 252 ? 0.61267 0.59789 0.60766 -0.02300 -0.00752 -0.04200 252 GLN A CA  
2040 C  C   . GLN A 252 ? 0.60025 0.59397 0.59030 -0.02231 -0.00887 -0.04125 252 GLN A C   
2041 O  O   . GLN A 252 ? 0.58137 0.58385 0.57664 -0.01973 -0.00804 -0.03648 252 GLN A O   
2042 C  CB  . GLN A 252 ? 0.61796 0.59624 0.61147 -0.01696 -0.00163 -0.04307 252 GLN A CB  
2043 C  CG  . GLN A 252 ? 0.60898 0.59313 0.61214 -0.01301 0.00079  -0.03725 252 GLN A CG  
2044 C  CD  . GLN A 252 ? 0.63155 0.61253 0.63472 -0.00666 0.00597  -0.03740 252 GLN A CD  
2045 O  OE1 . GLN A 252 ? 0.62008 0.60853 0.62892 -0.00335 0.00749  -0.03304 252 GLN A OE1 
2046 N  NE2 . GLN A 252 ? 0.63870 0.60841 0.63585 -0.00489 0.00855  -0.04237 252 GLN A NE2 
2047 N  N   . ASP A 253 ? 0.39433 0.38451 0.37327 -0.02480 -0.01124 -0.04579 253 ASP A N   
2048 C  CA  . ASP A 253 ? 0.39519 0.39208 0.36723 -0.02421 -0.01250 -0.04483 253 ASP A CA  
2049 C  C   . ASP A 253 ? 0.38829 0.39019 0.35867 -0.02987 -0.02014 -0.04454 253 ASP A C   
2050 O  O   . ASP A 253 ? 0.38703 0.39332 0.34993 -0.02993 -0.02227 -0.04372 253 ASP A O   
2051 C  CB  . ASP A 253 ? 0.41128 0.40071 0.36929 -0.02132 -0.00819 -0.04974 253 ASP A CB  
2052 C  CG  . ASP A 253 ? 0.41449 0.40372 0.37628 -0.01475 -0.00048 -0.04823 253 ASP A CG  
2053 O  OD1 . ASP A 253 ? 0.40660 0.39972 0.38075 -0.01305 0.00057  -0.04394 253 ASP A OD1 
2054 O  OD2 . ASP A 253 ? 0.42331 0.40898 0.37563 -0.01124 0.00452  -0.05114 253 ASP A OD2 
2055 N  N   . ALA A 254 ? 0.30938 0.31145 0.28712 -0.03474 -0.02443 -0.04452 254 ALA A N   
2056 C  CA  . ALA A 254 ? 0.31709 0.32584 0.29583 -0.04035 -0.03228 -0.04363 254 ALA A CA  
2057 C  C   . ALA A 254 ? 0.29285 0.31572 0.28324 -0.03850 -0.03380 -0.03644 254 ALA A C   
2058 O  O   . ALA A 254 ? 0.28314 0.30906 0.28159 -0.03417 -0.02923 -0.03271 254 ALA A O   
2059 C  CB  . ALA A 254 ? 0.31320 0.31761 0.29681 -0.04702 -0.03629 -0.04591 254 ALA A CB  
2060 N  N   . MET A 255 ? 0.28274 0.31354 0.27321 -0.04161 -0.04064 -0.03459 255 MET A N   
2061 C  CA  . MET A 255 ? 0.26442 0.30820 0.26637 -0.03960 -0.04272 -0.02788 255 MET A CA  
2062 C  C   . MET A 255 ? 0.26380 0.31617 0.27361 -0.04534 -0.05059 -0.02635 255 MET A C   
2063 O  O   . MET A 255 ? 0.27368 0.32404 0.27468 -0.05034 -0.05694 -0.02947 255 MET A O   
2064 C  CB  . MET A 255 ? 0.27047 0.31730 0.26513 -0.03556 -0.04289 -0.02503 255 MET A CB  
2065 C  CG  . MET A 255 ? 0.27339 0.31283 0.25948 -0.03116 -0.03589 -0.02646 255 MET A CG  
2066 S  SD  . MET A 255 ? 0.28029 0.32280 0.25710 -0.02801 -0.03627 -0.02249 255 MET A SD  
2067 C  CE  . MET A 255 ? 0.28968 0.32247 0.24697 -0.02936 -0.03401 -0.02884 255 MET A CE  
2068 N  N   . SER A 256 ? 0.30598 0.36824 0.33216 -0.04469 -0.05020 -0.02146 256 SER A N   
2069 C  CA  . SER A 256 ? 0.30145 0.37527 0.33930 -0.04969 -0.05707 -0.01857 256 SER A CA  
2070 C  C   . SER A 256 ? 0.28927 0.37676 0.33879 -0.04440 -0.05746 -0.01153 256 SER A C   
2071 O  O   . SER A 256 ? 0.28033 0.36818 0.33485 -0.03832 -0.05084 -0.00894 256 SER A O   
2072 C  CB  . SER A 256 ? 0.29613 0.36975 0.34483 -0.05455 -0.05558 -0.01900 256 SER A CB  
2073 O  OG  . SER A 256 ? 0.29480 0.38196 0.35724 -0.05977 -0.06208 -0.01528 256 SER A OG  
2074 N  N   . TRP A 257 ? 0.25012 0.34808 0.30339 -0.04659 -0.06556 -0.00853 257 TRP A N   
2075 C  CA  . TRP A 257 ? 0.23383 0.34432 0.29771 -0.04082 -0.06672 -0.00163 257 TRP A CA  
2076 C  C   . TRP A 257 ? 0.22964 0.34896 0.31181 -0.03775 -0.06127 0.00242  257 TRP A C   
2077 O  O   . TRP A 257 ? 0.21999 0.34704 0.31444 -0.04294 -0.06287 0.00336  257 TRP A O   
2078 C  CB  . TRP A 257 ? 0.23277 0.35409 0.29935 -0.04475 -0.07756 0.00118  257 TRP A CB  
2079 C  CG  . TRP A 257 ? 0.23504 0.36991 0.31369 -0.03849 -0.07979 0.00887  257 TRP A CG  
2080 C  CD1 . TRP A 257 ? 0.23367 0.36631 0.30536 -0.03172 -0.07946 0.01197  257 TRP A CD1 
2081 C  CD2 . TRP A 257 ? 0.21988 0.37260 0.32029 -0.03820 -0.08265 0.01485  257 TRP A CD2 
2082 N  NE1 . TRP A 257 ? 0.22358 0.37007 0.31065 -0.02661 -0.08199 0.01921  257 TRP A NE1 
2083 C  CE2 . TRP A 257 ? 0.21216 0.37208 0.31756 -0.03009 -0.08374 0.02112  257 TRP A CE2 
2084 C  CE3 . TRP A 257 ? 0.21101 0.37458 0.32796 -0.04398 -0.08407 0.01599  257 TRP A CE3 
2085 C  CZ2 . TRP A 257 ? 0.20394 0.38196 0.33061 -0.02655 -0.08581 0.02822  257 TRP A CZ2 
2086 C  CZ3 . TRP A 257 ? 0.20203 0.38509 0.34085 -0.04122 -0.08599 0.02340  257 TRP A CZ3 
2087 C  CH2 . TRP A 257 ? 0.20216 0.39251 0.34584 -0.03206 -0.08667 0.02931  257 TRP A CH2 
2088 N  N   . ARG A 258 ? 0.28050 0.39800 0.36361 -0.02961 -0.05464 0.00479  258 ARG A N   
2089 C  CA  . ARG A 258 ? 0.27259 0.39703 0.36990 -0.02490 -0.04838 0.00854  258 ARG A CA  
2090 C  C   . ARG A 258 ? 0.27407 0.39459 0.37457 -0.02864 -0.04290 0.00611  258 ARG A C   
2091 O  O   . ARG A 258 ? 0.26746 0.39660 0.38141 -0.02734 -0.03881 0.00954  258 ARG A O   
2092 C  CB  . ARG A 258 ? 0.26416 0.40679 0.37910 -0.02366 -0.05256 0.01474  258 ARG A CB  
2093 C  CG  . ARG A 258 ? 0.26705 0.41348 0.37942 -0.01930 -0.05840 0.01820  258 ARG A CG  
2094 C  CD  . ARG A 258 ? 0.25907 0.41731 0.38667 -0.01085 -0.05612 0.02473  258 ARG A CD  
2095 N  NE  . ARG A 258 ? 0.27192 0.43045 0.39519 -0.00572 -0.06115 0.02829  258 ARG A NE  
2096 C  CZ  . ARG A 258 ? 0.26843 0.44161 0.40502 -0.00241 -0.06659 0.03467  258 ARG A CZ  
2097 N  NH1 . ARG A 258 ? 0.26712 0.45776 0.42379 -0.00376 -0.06762 0.03837  258 ARG A NH1 
2098 N  NH2 . ARG A 258 ? 0.27775 0.44858 0.40812 0.00230  -0.07115 0.03807  258 ARG A NH2 
2099 N  N   . ARG A 259 ? 0.36921 0.47666 0.45740 -0.03284 -0.04229 0.00063  259 ARG A N   
2100 C  CA  . ARG A 259 ? 0.36425 0.46425 0.45238 -0.03491 -0.03644 -0.00151 259 ARG A CA  
2101 C  C   . ARG A 259 ? 0.37494 0.46151 0.44989 -0.03016 -0.03139 -0.00441 259 ARG A C   
2102 O  O   . ARG A 259 ? 0.38367 0.45956 0.44744 -0.03257 -0.03194 -0.00897 259 ARG A O   
2103 C  CB  . ARG A 259 ? 0.37832 0.47415 0.46501 -0.04399 -0.04045 -0.00507 259 ARG A CB  
2104 C  CG  . ARG A 259 ? 0.37300 0.48252 0.47283 -0.05045 -0.04731 -0.00221 259 ARG A CG  
2105 C  CD  . ARG A 259 ? 0.36646 0.49082 0.48535 -0.04862 -0.04330 0.00426  259 ARG A CD  
2106 N  NE  . ARG A 259 ? 0.36635 0.48448 0.48543 -0.04591 -0.03411 0.00468  259 ARG A NE  
2107 C  CZ  . ARG A 259 ? 0.36303 0.48212 0.48994 -0.05130 -0.03141 0.00613  259 ARG A CZ  
2108 N  NH1 . ARG A 259 ? 0.36427 0.49014 0.50061 -0.06038 -0.03719 0.00711  259 ARG A NH1 
2109 N  NH2 . ARG A 259 ? 0.36479 0.47753 0.48960 -0.04802 -0.02312 0.00696  259 ARG A NH2 
2110 N  N   . PRO A 260 ? 0.27322 0.35996 0.34927 -0.02332 -0.02645 -0.00186 260 PRO A N   
2111 C  CA  . PRO A 260 ? 0.28572 0.36168 0.35005 -0.01919 -0.02360 -0.00381 260 PRO A CA  
2112 C  C   . PRO A 260 ? 0.29006 0.35571 0.34896 -0.02013 -0.01919 -0.00657 260 PRO A C   
2113 O  O   . PRO A 260 ? 0.29113 0.34881 0.34123 -0.01782 -0.01768 -0.00825 260 PRO A O   
2114 C  CB  . PRO A 260 ? 0.27621 0.35520 0.34401 -0.01231 -0.02065 -0.00018 260 PRO A CB  
2115 C  CG  . PRO A 260 ? 0.27398 0.36244 0.35449 -0.01217 -0.01814 0.00281  260 PRO A CG  
2116 C  CD  . PRO A 260 ? 0.26719 0.36402 0.35506 -0.01893 -0.02343 0.00291  260 PRO A CD  
2117 N  N   . PHE A 261 ? 0.26917 0.33507 0.33361 -0.02351 -0.01725 -0.00646 261 PHE A N   
2118 C  CA  . PHE A 261 ? 0.27315 0.32930 0.33310 -0.02355 -0.01304 -0.00788 261 PHE A CA  
2119 C  C   . PHE A 261 ? 0.28148 0.33000 0.33758 -0.02877 -0.01471 -0.01160 261 PHE A C   
2120 O  O   . PHE A 261 ? 0.28981 0.32862 0.33886 -0.02738 -0.01257 -0.01379 261 PHE A O   
2121 C  CB  . PHE A 261 ? 0.26925 0.32871 0.33628 -0.02271 -0.00837 -0.00435 261 PHE A CB  
2122 C  CG  . PHE A 261 ? 0.26187 0.32620 0.33072 -0.01657 -0.00557 -0.00145 261 PHE A CG  
2123 C  CD1 . PHE A 261 ? 0.27036 0.32981 0.33144 -0.01192 -0.00591 -0.00238 261 PHE A CD1 
2124 C  CD2 . PHE A 261 ? 0.25977 0.33308 0.33805 -0.01543 -0.00227 0.00226  261 PHE A CD2 
2125 C  CE1 . PHE A 261 ? 0.26721 0.32839 0.32853 -0.00629 -0.00356 -0.00030 261 PHE A CE1 
2126 C  CE2 . PHE A 261 ? 0.26098 0.33705 0.33964 -0.00882 0.00099  0.00430  261 PHE A CE2 
2127 C  CZ  . PHE A 261 ? 0.26269 0.33155 0.33216 -0.00426 0.00006  0.00270  261 PHE A CZ  
2128 N  N   . LEU A 262 ? 0.19049 0.24280 0.25113 -0.03467 -0.01877 -0.01237 262 LEU A N   
2129 C  CA  . LEU A 262 ? 0.19931 0.24225 0.25512 -0.04020 -0.02097 -0.01662 262 LEU A CA  
2130 C  C   . LEU A 262 ? 0.20268 0.23644 0.25824 -0.04008 -0.01616 -0.01617 262 LEU A C   
2131 O  O   . LEU A 262 ? 0.20025 0.23860 0.26390 -0.04077 -0.01334 -0.01197 262 LEU A O   
2132 C  CB  . LEU A 262 ? 0.20759 0.24406 0.25132 -0.03903 -0.02328 -0.02132 262 LEU A CB  
2133 C  CG  . LEU A 262 ? 0.20564 0.25049 0.24805 -0.03954 -0.02860 -0.02109 262 LEU A CG  
2134 C  CD1 . LEU A 262 ? 0.21049 0.24760 0.23884 -0.03879 -0.02988 -0.02576 262 LEU A CD1 
2135 C  CD2 . LEU A 262 ? 0.19401 0.24658 0.24443 -0.04632 -0.03448 -0.02017 262 LEU A CD2 
2136 N  N   . TRP A 263 ? 0.24337 0.26464 0.29002 -0.03875 -0.01476 -0.01983 263 TRP A N   
2137 C  CA  . TRP A 263 ? 0.24993 0.26167 0.29612 -0.03828 -0.01094 -0.01895 263 TRP A CA  
2138 C  C   . TRP A 263 ? 0.25352 0.26210 0.29532 -0.03133 -0.00717 -0.01789 263 TRP A C   
2139 O  O   . TRP A 263 ? 0.26267 0.26210 0.30217 -0.02988 -0.00477 -0.01769 263 TRP A O   
2140 C  CB  . TRP A 263 ? 0.26857 0.26717 0.30934 -0.04220 -0.01252 -0.02361 263 TRP A CB  
2141 C  CG  . TRP A 263 ? 0.26400 0.26297 0.31015 -0.05067 -0.01625 -0.02371 263 TRP A CG  
2142 C  CD1 . TRP A 263 ? 0.26713 0.26153 0.31884 -0.05534 -0.01510 -0.02097 263 TRP A CD1 
2143 C  CD2 . TRP A 263 ? 0.26058 0.26498 0.30730 -0.05617 -0.02232 -0.02617 263 TRP A CD2 
2144 N  NE1 . TRP A 263 ? 0.26368 0.26073 0.32052 -0.06391 -0.02005 -0.02159 263 TRP A NE1 
2145 C  CE2 . TRP A 263 ? 0.26535 0.26878 0.31921 -0.06456 -0.02496 -0.02489 263 TRP A CE2 
2146 C  CE3 . TRP A 263 ? 0.26321 0.27325 0.30490 -0.05518 -0.02619 -0.02880 263 TRP A CE3 
2147 C  CZ2 . TRP A 263 ? 0.26274 0.27130 0.31957 -0.07224 -0.03201 -0.02642 263 TRP A CZ2 
2148 C  CZ3 . TRP A 263 ? 0.25841 0.27305 0.30176 -0.06220 -0.03311 -0.03026 263 TRP A CZ3 
2149 C  CH2 . TRP A 263 ? 0.26583 0.28004 0.31705 -0.07077 -0.03630 -0.02919 263 TRP A CH2 
2150 N  N   . HIS A 264 ? 0.22842 0.24412 0.26935 -0.02727 -0.00713 -0.01684 264 HIS A N   
2151 C  CA  . HIS A 264 ? 0.22645 0.23977 0.26377 -0.02181 -0.00465 -0.01568 264 HIS A CA  
2152 C  C   . HIS A 264 ? 0.21526 0.22874 0.25516 -0.02032 -0.00188 -0.01140 264 HIS A C   
2153 O  O   . HIS A 264 ? 0.21424 0.23222 0.25914 -0.02254 -0.00099 -0.00887 264 HIS A O   
2154 C  CB  . HIS A 264 ? 0.21799 0.23746 0.25311 -0.01896 -0.00592 -0.01572 264 HIS A CB  
2155 C  CG  . HIS A 264 ? 0.22710 0.24622 0.25757 -0.02014 -0.00821 -0.01940 264 HIS A CG  
2156 N  ND1 . HIS A 264 ? 0.23409 0.24803 0.25882 -0.01788 -0.00680 -0.02185 264 HIS A ND1 
2157 C  CD2 . HIS A 264 ? 0.22435 0.24786 0.25447 -0.02326 -0.01176 -0.02083 264 HIS A CD2 
2158 C  CE1 . HIS A 264 ? 0.23750 0.25176 0.25696 -0.01945 -0.00873 -0.02497 264 HIS A CE1 
2159 N  NE2 . HIS A 264 ? 0.23585 0.25555 0.25798 -0.02296 -0.01235 -0.02443 264 HIS A NE2 
2160 N  N   . SER A 265 ? 0.23273 0.24172 0.26902 -0.01655 -0.00049 -0.01032 265 SER A N   
2161 C  CA  . SER A 265 ? 0.23461 0.24149 0.27043 -0.01525 0.00168  -0.00648 265 SER A CA  
2162 C  C   . SER A 265 ? 0.22179 0.23458 0.25697 -0.01316 0.00247  -0.00439 265 SER A C   
2163 O  O   . SER A 265 ? 0.21980 0.23266 0.25470 -0.01305 0.00500  -0.00144 265 SER A O   
2164 C  CB  . SER A 265 ? 0.23947 0.23983 0.27175 -0.01212 0.00173  -0.00572 265 SER A CB  
2165 O  OG  . SER A 265 ? 0.23247 0.23574 0.26287 -0.00926 0.00029  -0.00657 265 SER A OG  
2166 N  N   . LEU A 266 ? 0.23912 0.25588 0.27321 -0.01130 0.00075  -0.00576 266 LEU A N   
2167 C  CA  . LEU A 266 ? 0.23792 0.25787 0.27029 -0.00860 0.00133  -0.00435 266 LEU A CA  
2168 C  C   . LEU A 266 ? 0.23743 0.25168 0.26338 -0.00619 0.00221  -0.00258 266 LEU A C   
2169 O  O   . LEU A 266 ? 0.24281 0.25699 0.26562 -0.00425 0.00415  -0.00125 266 LEU A O   
2170 C  CB  . LEU A 266 ? 0.23570 0.26226 0.27343 -0.00930 0.00343  -0.00285 266 LEU A CB  
2171 C  CG  . LEU A 266 ? 0.23494 0.26788 0.28024 -0.01311 0.00182  -0.00373 266 LEU A CG  
2172 C  CD1 . LEU A 266 ? 0.22924 0.27137 0.28190 -0.01289 0.00386  -0.00114 266 LEU A CD1 
2173 C  CD2 . LEU A 266 ? 0.23119 0.26557 0.27523 -0.01324 -0.00206 -0.00637 266 LEU A CD2 
2174 N  N   . ILE A 267 ? 0.21672 0.22615 0.24033 -0.00602 0.00070  -0.00252 267 ILE A N   
2175 C  CA  . ILE A 267 ? 0.22398 0.22823 0.24141 -0.00439 0.00014  -0.00044 267 ILE A CA  
2176 C  C   . ILE A 267 ? 0.22206 0.22554 0.23627 -0.00311 -0.00316 -0.00091 267 ILE A C   
2177 O  O   . ILE A 267 ? 0.23366 0.23279 0.24182 -0.00232 -0.00485 0.00059  267 ILE A O   
2178 C  CB  . ILE A 267 ? 0.22985 0.22953 0.24775 -0.00486 0.00003  0.00129  267 ILE A CB  
2179 C  CG1 . ILE A 267 ? 0.23264 0.23289 0.25479 -0.00449 -0.00179 -0.00026 267 ILE A CG1 
2180 C  CG2 . ILE A 267 ? 0.23192 0.23067 0.25262 -0.00707 0.00310  0.00232  267 ILE A CG2 
2181 C  CD1 . ILE A 267 ? 0.23575 0.23103 0.25906 -0.00356 -0.00195 0.00162  267 ILE A CD1 
2182 N  N   . SER A 268 ? 0.18089 0.18816 0.19838 -0.00342 -0.00447 -0.00261 268 SER A N   
2183 C  CA  . SER A 268 ? 0.18123 0.18805 0.19698 -0.00319 -0.00759 -0.00227 268 SER A CA  
2184 C  C   . SER A 268 ? 0.18920 0.19151 0.19775 -0.00240 -0.00903 -0.00191 268 SER A C   
2185 O  O   . SER A 268 ? 0.19519 0.19428 0.20041 -0.00302 -0.01238 -0.00082 268 SER A O   
2186 C  CB  . SER A 268 ? 0.17964 0.19123 0.19928 -0.00386 -0.00796 -0.00357 268 SER A CB  
2187 O  OG  . SER A 268 ? 0.17860 0.19247 0.19847 -0.00372 -0.00695 -0.00467 268 SER A OG  
2188 N  N   . PRO A 269 ? 0.23614 0.23769 0.24204 -0.00093 -0.00687 -0.00276 269 PRO A N   
2189 C  CA  . PRO A 269 ? 0.24679 0.24145 0.24384 0.00059  -0.00781 -0.00310 269 PRO A CA  
2190 C  C   . PRO A 269 ? 0.24447 0.23284 0.23321 0.00078  -0.00814 -0.00221 269 PRO A C   
2191 O  O   . PRO A 269 ? 0.25134 0.23250 0.23147 0.00059  -0.01134 -0.00261 269 PRO A O   
2192 C  CB  . PRO A 269 ? 0.24163 0.23827 0.23954 0.00331  -0.00407 -0.00392 269 PRO A CB  
2193 C  CG  . PRO A 269 ? 0.23360 0.23890 0.24137 0.00207  -0.00356 -0.00391 269 PRO A CG  
2194 C  CD  . PRO A 269 ? 0.22848 0.23539 0.23948 -0.00039 -0.00381 -0.00344 269 PRO A CD  
2195 N  N   . ALA A 270 ? 0.23240 0.22244 0.22260 0.00073  -0.00536 -0.00083 270 ALA A N   
2196 C  CA  . ALA A 270 ? 0.23764 0.22162 0.21897 0.00085  -0.00586 0.00084  270 ALA A CA  
2197 C  C   . ALA A 270 ? 0.23851 0.22195 0.22133 -0.00100 -0.01103 0.00270  270 ALA A C   
2198 O  O   . ALA A 270 ? 0.24003 0.21770 0.21410 -0.00143 -0.01465 0.00386  270 ALA A O   
2199 C  CB  . ALA A 270 ? 0.22888 0.21454 0.21130 0.00125  -0.00066 0.00262  270 ALA A CB  
2200 N  N   . LEU A 271 ? 0.21854 0.20805 0.21215 -0.00187 -0.01148 0.00309  271 LEU A N   
2201 C  CA  . LEU A 271 ? 0.21895 0.20977 0.21642 -0.00262 -0.01565 0.00528  271 LEU A CA  
2202 C  C   . LEU A 271 ? 0.21866 0.20919 0.21458 -0.00418 -0.02088 0.00527  271 LEU A C   
2203 O  O   . LEU A 271 ? 0.21639 0.20574 0.21067 -0.00520 -0.02580 0.00769  271 LEU A O   
2204 C  CB  . LEU A 271 ? 0.21527 0.21196 0.22383 -0.00230 -0.01370 0.00503  271 LEU A CB  
2205 C  CG  . LEU A 271 ? 0.21291 0.21264 0.22807 -0.00173 -0.01658 0.00746  271 LEU A CG  
2206 C  CD1 . LEU A 271 ? 0.21487 0.21032 0.22598 -0.00099 -0.01915 0.01109  271 LEU A CD1 
2207 C  CD2 . LEU A 271 ? 0.21489 0.21819 0.23861 -0.00046 -0.01314 0.00621  271 LEU A CD2 
2208 N  N   . ASN A 272 ? 0.23047 0.22189 0.22705 -0.00475 -0.02042 0.00306  272 ASN A N   
2209 C  CA  . ASN A 272 ? 0.23614 0.22719 0.23274 -0.00715 -0.02528 0.00349  272 ASN A CA  
2210 C  C   . ASN A 272 ? 0.23837 0.21979 0.22250 -0.00839 -0.02955 0.00302  272 ASN A C   
2211 O  O   . ASN A 272 ? 0.25170 0.23174 0.23548 -0.01154 -0.03507 0.00390  272 ASN A O   
2212 C  CB  . ASN A 272 ? 0.22916 0.22282 0.22942 -0.00740 -0.02343 0.00188  272 ASN A CB  
2213 C  CG  . ASN A 272 ? 0.23091 0.23368 0.24202 -0.00724 -0.02096 0.00247  272 ASN A CG  
2214 O  OD1 . ASN A 272 ? 0.22661 0.23349 0.24342 -0.00673 -0.02074 0.00398  272 ASN A OD1 
2215 N  ND2 . ASN A 272 ? 0.22231 0.22755 0.23541 -0.00725 -0.01905 0.00131  272 ASN A ND2 
2216 N  N   . ILE A 273 ? 0.27166 0.24614 0.24511 -0.00631 -0.02712 0.00171  273 ILE A N   
2217 C  CA  . ILE A 273 ? 0.27948 0.24306 0.23802 -0.00711 -0.03088 0.00069  273 ILE A CA  
2218 C  C   . ILE A 273 ? 0.28827 0.24951 0.24029 -0.00712 -0.03284 0.00312  273 ILE A C   
2219 O  O   . ILE A 273 ? 0.29883 0.25017 0.23565 -0.00755 -0.03560 0.00220  273 ILE A O   
2220 C  CB  . ILE A 273 ? 0.28448 0.23998 0.23261 -0.00406 -0.02631 -0.00289 273 ILE A CB  
2221 C  CG1 . ILE A 273 ? 0.29309 0.25096 0.24040 -0.00048 -0.01894 -0.00266 273 ILE A CG1 
2222 C  CG2 . ILE A 273 ? 0.28987 0.24747 0.24468 -0.00369 -0.02503 -0.00444 273 ILE A CG2 
2223 C  CD1 . ILE A 273 ? 0.29356 0.24538 0.23215 0.00346  -0.01350 -0.00557 273 ILE A CD1 
2224 N  N   . GLY A 274 ? 0.30844 0.27733 0.27036 -0.00650 -0.03161 0.00623  274 GLY A N   
2225 C  CA  . GLY A 274 ? 0.31512 0.28219 0.27246 -0.00652 -0.03451 0.00975  274 GLY A CA  
2226 C  C   . GLY A 274 ? 0.31614 0.27915 0.26555 -0.00408 -0.02880 0.01047  274 GLY A C   
2227 O  O   . GLY A 274 ? 0.32552 0.28523 0.26827 -0.00409 -0.03130 0.01385  274 GLY A O   
2228 N  N   . LEU A 275 ? 0.25954 0.22338 0.21001 -0.00217 -0.02140 0.00809  275 LEU A N   
2229 C  CA  . LEU A 275 ? 0.25936 0.22087 0.20397 -0.00043 -0.01526 0.00949  275 LEU A CA  
2230 C  C   . LEU A 275 ? 0.26149 0.22757 0.21602 -0.00062 -0.01368 0.01324  275 LEU A C   
2231 O  O   . LEU A 275 ? 0.26329 0.22649 0.21253 -0.00013 -0.01002 0.01602  275 LEU A O   
2232 C  CB  . LEU A 275 ? 0.25767 0.22077 0.20312 0.00153  -0.00811 0.00647  275 LEU A CB  
2233 C  CG  . LEU A 275 ? 0.26903 0.22445 0.20140 0.00320  -0.00788 0.00289  275 LEU A CG  
2234 C  CD1 . LEU A 275 ? 0.26075 0.21937 0.19621 0.00632  -0.00016 0.00090  275 LEU A CD1 
2235 C  CD2 . LEU A 275 ? 0.27327 0.21839 0.18661 0.00355  -0.00926 0.00368  275 LEU A CD2 
2236 N  N   . LEU A 276 ? 0.29291 0.26516 0.26101 -0.00119 -0.01590 0.01343  276 LEU A N   
2237 C  CA  . LEU A 276 ? 0.29699 0.27137 0.27385 -0.00081 -0.01522 0.01652  276 LEU A CA  
2238 C  C   . LEU A 276 ? 0.30280 0.28045 0.28665 -0.00060 -0.02141 0.01837  276 LEU A C   
2239 O  O   . LEU A 276 ? 0.29130 0.27168 0.27629 -0.00163 -0.02546 0.01691  276 LEU A O   
2240 C  CB  . LEU A 276 ? 0.29335 0.27235 0.28102 -0.00097 -0.00999 0.01430  276 LEU A CB  
2241 C  CG  . LEU A 276 ? 0.29430 0.27319 0.27962 -0.00152 -0.00382 0.01332  276 LEU A CG  
2242 C  CD1 . LEU A 276 ? 0.28640 0.27100 0.28286 -0.00252 -0.00103 0.01055  276 LEU A CD1 
2243 C  CD2 . LEU A 276 ? 0.29395 0.26802 0.27413 -0.00190 -0.00104 0.01759  276 LEU A CD2 
2244 N  N   . ASP A 277 ? 0.31314 0.29062 0.30251 0.00082  -0.02196 0.02204  277 ASP A N   
2245 C  CA  . ASP A 277 ? 0.31226 0.29424 0.31016 0.00207  -0.02724 0.02477  277 ASP A CA  
2246 C  C   . ASP A 277 ? 0.31249 0.29912 0.32416 0.00413  -0.02374 0.02349  277 ASP A C   
2247 O  O   . ASP A 277 ? 0.31619 0.29891 0.32924 0.00492  -0.01908 0.02306  277 ASP A O   
2248 C  CB  . ASP A 277 ? 0.32293 0.30064 0.31604 0.00329  -0.03151 0.03072  277 ASP A CB  
2249 C  CG  . ASP A 277 ? 0.32087 0.30496 0.32549 0.00541  -0.03691 0.03447  277 ASP A CG  
2250 O  OD1 . ASP A 277 ? 0.32540 0.31381 0.32995 0.00371  -0.04348 0.03555  277 ASP A OD1 
2251 O  OD2 . ASP A 277 ? 0.32450 0.30919 0.33864 0.00879  -0.03460 0.03645  277 ASP A OD2 
2252 N  N   . PRO A 278 ? 0.25043 0.24483 0.27180 0.00478  -0.02566 0.02287  278 PRO A N   
2253 C  CA  . PRO A 278 ? 0.24838 0.24650 0.28072 0.00723  -0.02133 0.02089  278 PRO A CA  
2254 C  C   . PRO A 278 ? 0.25332 0.24754 0.29044 0.01110  -0.02003 0.02381  278 PRO A C   
2255 O  O   . PRO A 278 ? 0.26299 0.25327 0.30231 0.01226  -0.01506 0.02105  278 PRO A O   
2256 C  CB  . PRO A 278 ? 0.23831 0.24633 0.27939 0.00727  -0.02397 0.02131  278 PRO A CB  
2257 C  CG  . PRO A 278 ? 0.23865 0.24673 0.27223 0.00333  -0.02897 0.02156  278 PRO A CG  
2258 C  CD  . PRO A 278 ? 0.24519 0.24488 0.26709 0.00274  -0.03137 0.02362  278 PRO A CD  
2259 N  N   . LEU A 279 ? 0.22183 0.21624 0.26028 0.01309  -0.02489 0.02943  279 LEU A N   
2260 C  CA  . LEU A 279 ? 0.22670 0.21654 0.27018 0.01762  -0.02391 0.03293  279 LEU A CA  
2261 C  C   . LEU A 279 ? 0.23583 0.21391 0.27045 0.01638  -0.02073 0.03308  279 LEU A C   
2262 O  O   . LEU A 279 ? 0.23952 0.21124 0.27768 0.01870  -0.01683 0.03240  279 LEU A O   
2263 C  CB  . LEU A 279 ? 0.22731 0.22095 0.27450 0.02004  -0.03086 0.03991  279 LEU A CB  
2264 C  CG  . LEU A 279 ? 0.24001 0.23041 0.29530 0.02628  -0.03036 0.04443  279 LEU A CG  
2265 C  CD1 . LEU A 279 ? 0.22466 0.21888 0.29225 0.03083  -0.02457 0.04091  279 LEU A CD1 
2266 C  CD2 . LEU A 279 ? 0.22125 0.21726 0.28091 0.02851  -0.03847 0.05217  279 LEU A CD2 
2267 N  N   . ASP A 280 ? 0.32287 0.29745 0.34568 0.01262  -0.02202 0.03398  280 ASP A N   
2268 C  CA  . ASP A 280 ? 0.33042 0.29550 0.34554 0.01083  -0.01833 0.03498  280 ASP A CA  
2269 C  C   . ASP A 280 ? 0.32804 0.29193 0.34588 0.00867  -0.01225 0.02932  280 ASP A C   
2270 O  O   . ASP A 280 ? 0.33102 0.28722 0.34889 0.00796  -0.00893 0.02993  280 ASP A O   
2271 C  CB  . ASP A 280 ? 0.31915 0.28202 0.32056 0.00778  -0.01991 0.03690  280 ASP A CB  
2272 C  CG  . ASP A 280 ? 0.33786 0.29333 0.33224 0.00535  -0.01467 0.03799  280 ASP A CG  
2273 O  OD1 . ASP A 280 ? 0.34611 0.29426 0.33693 0.00612  -0.01501 0.04364  280 ASP A OD1 
2274 O  OD2 . ASP A 280 ? 0.34597 0.30349 0.33914 0.00260  -0.01024 0.03382  280 ASP A OD2 
2275 N  N   . ILE A 281 ? 0.22404 0.19505 0.24396 0.00716  -0.01131 0.02415  281 ILE A N   
2276 C  CA  . ILE A 281 ? 0.22109 0.19206 0.24362 0.00498  -0.00674 0.01895  281 ILE A CA  
2277 C  C   . ILE A 281 ? 0.22997 0.19691 0.25965 0.00747  -0.00476 0.01725  281 ILE A C   
2278 O  O   . ILE A 281 ? 0.23421 0.19442 0.26374 0.00551  -0.00177 0.01552  281 ILE A O   
2279 C  CB  . ILE A 281 ? 0.21152 0.19083 0.23477 0.00359  -0.00692 0.01459  281 ILE A CB  
2280 C  CG1 . ILE A 281 ? 0.20889 0.18917 0.22382 0.00113  -0.00719 0.01493  281 ILE A CG1 
2281 C  CG2 . ILE A 281 ? 0.20867 0.18896 0.23603 0.00226  -0.00352 0.00948  281 ILE A CG2 
2282 C  CD1 . ILE A 281 ? 0.20171 0.18834 0.21635 0.00058  -0.00881 0.01198  281 ILE A CD1 
2283 N  N   . CYS A 282 ? 0.20967 0.18041 0.24572 0.01181  -0.00632 0.01776  282 CYS A N   
2284 C  CA  . CYS A 282 ? 0.22142 0.18802 0.26350 0.01547  -0.00350 0.01543  282 CYS A CA  
2285 C  C   . CYS A 282 ? 0.23017 0.18481 0.27170 0.01751  -0.00304 0.01905  282 CYS A C   
2286 O  O   . CYS A 282 ? 0.23982 0.18538 0.28200 0.01807  0.00013  0.01594  282 CYS A O   
2287 C  CB  . CYS A 282 ? 0.21453 0.19001 0.26479 0.02028  -0.00442 0.01597  282 CYS A CB  
2288 S  SG  . CYS A 282 ? 0.21289 0.19991 0.26435 0.01786  -0.00343 0.01111  282 CYS A SG  
2289 N  N   . ARG A 283 ? 0.37004 0.32327 0.40927 0.01844  -0.00652 0.02570  283 ARG A N   
2290 C  CA  . ARG A 283 ? 0.38066 0.32179 0.41886 0.02046  -0.00639 0.03031  283 ARG A CA  
2291 C  C   . ARG A 283 ? 0.38159 0.31308 0.41371 0.01482  -0.00329 0.02912  283 ARG A C   
2292 O  O   . ARG A 283 ? 0.39633 0.31559 0.42909 0.01541  -0.00136 0.02952  283 ARG A O   
2293 C  CB  . ARG A 283 ? 0.37048 0.31278 0.40592 0.02219  -0.01149 0.03829  283 ARG A CB  
2294 C  CG  . ARG A 283 ? 0.37765 0.32489 0.42245 0.02918  -0.01480 0.04195  283 ARG A CG  
2295 C  CD  . ARG A 283 ? 0.37768 0.33014 0.41933 0.02938  -0.02170 0.04898  283 ARG A CD  
2296 N  NE  . ARG A 283 ? 0.38482 0.34173 0.43719 0.03627  -0.02541 0.05414  283 ARG A NE  
2297 C  CZ  . ARG A 283 ? 0.39428 0.35863 0.44760 0.03718  -0.03276 0.06029  283 ARG A CZ  
2298 N  NH1 . ARG A 283 ? 0.38197 0.34789 0.42372 0.03173  -0.03719 0.06163  283 ARG A NH1 
2299 N  NH2 . ARG A 283 ? 0.39033 0.36048 0.45630 0.04389  -0.03588 0.06526  283 ARG A NH2 
2300 N  N   . ARG A 284 ? 0.37331 0.31010 0.40013 0.00932  -0.00269 0.02785  284 ARG A N   
2301 C  CA  . ARG A 284 ? 0.37763 0.30851 0.40113 0.00348  0.00049  0.02715  284 ARG A CA  
2302 C  C   . ARG A 284 ? 0.38905 0.31617 0.41677 0.00171  0.00295  0.02050  284 ARG A C   
2303 O  O   . ARG A 284 ? 0.39471 0.31159 0.42201 -0.00179 0.00466  0.02057  284 ARG A O   
2304 C  CB  . ARG A 284 ? 0.37039 0.30985 0.38894 -0.00073 0.00120  0.02700  284 ARG A CB  
2305 C  CG  . ARG A 284 ? 0.37848 0.31799 0.38893 -0.00024 -0.00047 0.03339  284 ARG A CG  
2306 C  CD  . ARG A 284 ? 0.37309 0.31765 0.37781 -0.00436 0.00239  0.03316  284 ARG A CD  
2307 N  NE  . ARG A 284 ? 0.38799 0.32896 0.39492 -0.00922 0.00673  0.03367  284 ARG A NE  
2308 C  CZ  . ARG A 284 ? 0.37248 0.31853 0.37744 -0.01293 0.01050  0.03410  284 ARG A CZ  
2309 N  NH1 . ARG A 284 ? 0.36071 0.31393 0.35991 -0.01168 0.01097  0.03341  284 ARG A NH1 
2310 N  NH2 . ARG A 284 ? 0.36836 0.31214 0.37766 -0.01799 0.01393  0.03529  284 ARG A NH2 
2311 N  N   . ALA A 285 ? 0.23050 0.16516 0.26144 0.00359  0.00291  0.01485  285 ALA A N   
2312 C  CA  . ALA A 285 ? 0.23872 0.16917 0.27131 0.00225  0.00484  0.00813  285 ALA A CA  
2313 C  C   . ALA A 285 ? 0.24826 0.16517 0.28220 0.00653  0.00592  0.00767  285 ALA A C   
2314 O  O   . ALA A 285 ? 0.25659 0.16201 0.28880 0.00340  0.00721  0.00444  285 ALA A O   
2315 C  CB  . ALA A 285 ? 0.22977 0.17124 0.26407 0.00383  0.00483  0.00308  285 ALA A CB  
2316 N  N   . GLU A 286 ? 0.30972 0.22744 0.34705 0.01375  0.00515  0.01098  286 GLU A N   
2317 C  CA  . GLU A 286 ? 0.32631 0.23092 0.36569 0.01944  0.00656  0.01121  286 GLU A CA  
2318 C  C   . GLU A 286 ? 0.33684 0.22618 0.37282 0.01638  0.00630  0.01551  286 GLU A C   
2319 O  O   . GLU A 286 ? 0.34590 0.21979 0.38056 0.01669  0.00807  0.01265  286 GLU A O   
2320 C  CB  . GLU A 286 ? 0.31545 0.22659 0.36128 0.02788  0.00525  0.01575  286 GLU A CB  
2321 C  CG  . GLU A 286 ? 0.33734 0.23502 0.38573 0.03431  0.00555  0.01996  286 GLU A CG  
2322 C  CD  . GLU A 286 ? 0.33446 0.24003 0.39214 0.04389  0.00529  0.02268  286 GLU A CD  
2323 O  OE1 . GLU A 286 ? 0.33062 0.25283 0.39256 0.04419  0.00284  0.02467  286 GLU A OE1 
2324 O  OE2 . GLU A 286 ? 0.35407 0.24913 0.41540 0.05115  0.00753  0.02304  286 GLU A OE2 
2325 N  N   . ALA A 287 ? 0.31602 0.20843 0.34949 0.01317  0.00428  0.02237  287 ALA A N   
2326 C  CA  . ALA A 287 ? 0.32935 0.20812 0.35924 0.00950  0.00449  0.02760  287 ALA A CA  
2327 C  C   . ALA A 287 ? 0.33396 0.20541 0.36200 0.00134  0.00649  0.02296  287 ALA A C   
2328 O  O   . ALA A 287 ? 0.33975 0.19525 0.36630 -0.00120 0.00713  0.02484  287 ALA A O   
2329 C  CB  . ALA A 287 ? 0.31342 0.19851 0.33909 0.00717  0.00272  0.03543  287 ALA A CB  
2330 N  N   . ALA A 288 ? 0.26834 0.15100 0.29681 -0.00313 0.00695  0.01730  288 ALA A N   
2331 C  CA  . ALA A 288 ? 0.26608 0.14375 0.29406 -0.01120 0.00773  0.01284  288 ALA A CA  
2332 C  C   . ALA A 288 ? 0.27905 0.14095 0.30585 -0.00966 0.00816  0.00655  288 ALA A C   
2333 O  O   . ALA A 288 ? 0.29055 0.13895 0.31579 -0.01576 0.00801  0.00557  288 ALA A O   
2334 C  CB  . ALA A 288 ? 0.25383 0.14766 0.28304 -0.01495 0.00748  0.00840  288 ALA A CB  
2335 N  N   . TRP A 289 ? 0.32321 0.18612 0.35043 -0.00166 0.00891  0.00222  289 TRP A N   
2336 C  CA  . TRP A 289 ? 0.34069 0.18708 0.36510 0.00147  0.01034  -0.00406 289 TRP A CA  
2337 C  C   . TRP A 289 ? 0.35337 0.18180 0.37776 0.00603  0.01087  0.00087  289 TRP A C   
2338 O  O   . TRP A 289 ? 0.36885 0.17762 0.38936 0.00377  0.01128  -0.00225 289 TRP A O   
2339 C  CB  . TRP A 289 ? 0.34009 0.19405 0.36516 0.00932  0.01228  -0.00964 289 TRP A CB  
2340 C  CG  . TRP A 289 ? 0.35997 0.19642 0.38206 0.01590  0.01504  -0.01464 289 TRP A CG  
2341 C  CD1 . TRP A 289 ? 0.37267 0.19285 0.38726 0.01257  0.01574  -0.02263 289 TRP A CD1 
2342 C  CD2 . TRP A 289 ? 0.35767 0.19022 0.38391 0.02726  0.01746  -0.01197 289 TRP A CD2 
2343 N  NE1 . TRP A 289 ? 0.38625 0.19126 0.39872 0.02169  0.01918  -0.02577 289 TRP A NE1 
2344 C  CE2 . TRP A 289 ? 0.37829 0.19146 0.39895 0.03120  0.02056  -0.01899 289 TRP A CE2 
2345 C  CE3 . TRP A 289 ? 0.34764 0.19142 0.38194 0.03450  0.01697  -0.00429 289 TRP A CE3 
2346 C  CZ2 . TRP A 289 ? 0.38462 0.18988 0.40847 0.04314  0.02415  -0.01836 289 TRP A CZ2 
2347 C  CZ3 . TRP A 289 ? 0.36077 0.19832 0.39957 0.04564  0.01963  -0.00307 289 TRP A CZ3 
2348 C  CH2 . TRP A 289 ? 0.38001 0.19872 0.41409 0.05037  0.02367  -0.00996 289 TRP A CH2 
2349 N  N   . ARG A 290 ? 0.42395 0.25801 0.45219 0.01234  0.01030  0.00870  290 ARG A N   
2350 C  CA  . ARG A 290 ? 0.44104 0.25888 0.46980 0.01789  0.01033  0.01447  290 ARG A CA  
2351 C  C   . ARG A 290 ? 0.45115 0.25312 0.47602 0.00962  0.00954  0.01848  290 ARG A C   
2352 O  O   . ARG A 290 ? 0.46848 0.24961 0.49159 0.01203  0.01005  0.01959  290 ARG A O   
2353 C  CB  . ARG A 290 ? 0.43514 0.26441 0.46844 0.02452  0.00840  0.02325  290 ARG A CB  
2354 C  CG  . ARG A 290 ? 0.43354 0.27662 0.47303 0.03355  0.00901  0.02095  290 ARG A CG  
2355 C  CD  . ARG A 290 ? 0.44969 0.28152 0.49367 0.04457  0.01061  0.02223  290 ARG A CD  
2356 N  NE  . ARG A 290 ? 0.44086 0.28861 0.49312 0.05317  0.01146  0.02168  290 ARG A NE  
2357 C  CZ  . ARG A 290 ? 0.45015 0.29308 0.50784 0.06354  0.01488  0.01964  290 ARG A CZ  
2358 N  NH1 . ARG A 290 ? 0.45982 0.28036 0.51417 0.06729  0.01769  0.01715  290 ARG A NH1 
2359 N  NH2 . ARG A 290 ? 0.44025 0.30098 0.50716 0.07037  0.01579  0.02023  290 ARG A NH2 
2360 N  N   . GLU A 291 ? 0.50477 0.31602 0.52870 0.00002  0.00864  0.02099  291 GLU A N   
2361 C  CA  . GLU A 291 ? 0.51593 0.31533 0.53764 -0.00885 0.00841  0.02601  291 GLU A CA  
2362 C  C   . GLU A 291 ? 0.51433 0.30830 0.53504 -0.01888 0.00828  0.01894  291 GLU A C   
2363 O  O   . GLU A 291 ? 0.51800 0.30819 0.53903 -0.02854 0.00803  0.02303  291 GLU A O   
2364 C  CB  . GLU A 291 ? 0.50022 0.31335 0.52185 -0.01263 0.00822  0.03481  291 GLU A CB  
2365 C  CG  . GLU A 291 ? 0.50827 0.31918 0.52841 -0.00531 0.00713  0.04411  291 GLU A CG  
2366 C  CD  . GLU A 291 ? 0.50266 0.33092 0.52053 -0.00644 0.00666  0.05008  291 GLU A CD  
2367 O  OE1 . GLU A 291 ? 0.49309 0.33268 0.51075 -0.01356 0.00818  0.04840  291 GLU A OE1 
2368 O  OE2 . GLU A 291 ? 0.50942 0.33972 0.52545 0.00003  0.00456  0.05641  291 GLU A OE2 
2369 N  N   . GLY A 292 ? 0.39386 0.18795 0.41332 -0.01709 0.00828  0.00882  292 GLY A N   
2370 C  CA  . GLY A 292 ? 0.40285 0.18843 0.41974 -0.02611 0.00696  0.00151  292 GLY A CA  
2371 C  C   . GLY A 292 ? 0.38838 0.19192 0.40864 -0.03586 0.00553  0.00080  292 GLY A C   
2372 O  O   . GLY A 292 ? 0.39775 0.19483 0.41777 -0.04579 0.00343  -0.00221 292 GLY A O   
2373 N  N   . ARG A 293 ? 0.42642 0.25207 0.45013 -0.03336 0.00627  0.00350  293 ARG A N   
2374 C  CA  . ARG A 293 ? 0.41844 0.26178 0.44622 -0.04117 0.00541  0.00348  293 ARG A CA  
2375 C  C   . ARG A 293 ? 0.41249 0.26791 0.43957 -0.03962 0.00420  -0.00471 293 ARG A C   
2376 O  O   . ARG A 293 ? 0.40124 0.26993 0.43191 -0.04604 0.00281  -0.00564 293 ARG A O   
2377 C  CB  . ARG A 293 ? 0.40551 0.26402 0.43631 -0.04012 0.00732  0.01214  293 ARG A CB  
2378 C  CG  . ARG A 293 ? 0.41405 0.26357 0.44513 -0.04430 0.00874  0.02134  293 ARG A CG  
2379 C  CD  . ARG A 293 ? 0.41197 0.27676 0.44362 -0.04350 0.01110  0.02902  293 ARG A CD  
2380 N  NE  . ARG A 293 ? 0.40737 0.27852 0.43557 -0.03361 0.01087  0.02950  293 ARG A NE  
2381 C  CZ  . ARG A 293 ? 0.41491 0.27783 0.43932 -0.02756 0.01061  0.03505  293 ARG A CZ  
2382 N  NH1 . ARG A 293 ? 0.42935 0.27615 0.45201 -0.02958 0.01100  0.04084  293 ARG A NH1 
2383 N  NH2 . ARG A 293 ? 0.40309 0.27411 0.42573 -0.01960 0.00945  0.03529  293 ARG A NH2 
2384 N  N   . ALA A 294 ? 0.29685 0.14852 0.31986 -0.03114 0.00492  -0.01005 294 ALA A N   
2385 C  CA  . ALA A 294 ? 0.29116 0.15318 0.31219 -0.02942 0.00424  -0.01730 294 ALA A CA  
2386 C  C   . ALA A 294 ? 0.31128 0.15929 0.32583 -0.02267 0.00562  -0.02431 294 ALA A C   
2387 O  O   . ALA A 294 ? 0.31378 0.15113 0.32805 -0.01550 0.00783  -0.02197 294 ALA A O   
2388 C  CB  . ALA A 294 ? 0.27774 0.16000 0.30224 -0.02435 0.00524  -0.01415 294 ALA A CB  
2389 N  N   . PRO A 295 ? 0.37853 0.22611 0.38744 -0.02430 0.00458  -0.03266 295 PRO A N   
2390 C  CA  . PRO A 295 ? 0.39087 0.22529 0.39203 -0.01705 0.00713  -0.03984 295 PRO A CA  
2391 C  C   . PRO A 295 ? 0.38617 0.23290 0.39016 -0.00629 0.01088  -0.03844 295 PRO A C   
2392 O  O   . PRO A 295 ? 0.37306 0.23889 0.38288 -0.00578 0.01044  -0.03400 295 PRO A O   
2393 C  CB  . PRO A 295 ? 0.39628 0.22893 0.38924 -0.02332 0.00435  -0.04854 295 PRO A CB  
2394 C  CG  . PRO A 295 ? 0.37592 0.22963 0.37509 -0.02985 0.00116  -0.04506 295 PRO A CG  
2395 C  CD  . PRO A 295 ? 0.36409 0.22333 0.37295 -0.03245 0.00110  -0.03565 295 PRO A CD  
2396 N  N   . LEU A 296 ? 0.34827 0.18329 0.34829 0.00242  0.01473  -0.04231 296 LEU A N   
2397 C  CA  . LEU A 296 ? 0.34067 0.18712 0.34581 0.01297  0.01861  -0.03986 296 LEU A CA  
2398 C  C   . LEU A 296 ? 0.33609 0.19935 0.33948 0.01319  0.01940  -0.04335 296 LEU A C   
2399 O  O   . LEU A 296 ? 0.31923 0.19985 0.32985 0.01679  0.02007  -0.03853 296 LEU A O   
2400 C  CB  . LEU A 296 ? 0.35291 0.18294 0.35546 0.02290  0.02332  -0.04286 296 LEU A CB  
2401 C  CG  . LEU A 296 ? 0.35130 0.19335 0.36108 0.03452  0.02792  -0.04016 296 LEU A CG  
2402 C  CD1 . LEU A 296 ? 0.33838 0.19709 0.35998 0.03537  0.02533  -0.02989 296 LEU A CD1 
2403 C  CD2 . LEU A 296 ? 0.35649 0.18113 0.36502 0.04491  0.03290  -0.04247 296 LEU A CD2 
2404 N  N   . ASN A 297 ? 0.44808 0.30587 0.44128 0.00891  0.01881  -0.05141 297 ASN A N   
2405 C  CA  . ASN A 297 ? 0.43826 0.31097 0.42850 0.00903  0.01948  -0.05420 297 ASN A CA  
2406 C  C   . ASN A 297 ? 0.41913 0.31092 0.41639 0.00321  0.01545  -0.04855 297 ASN A C   
2407 O  O   . ASN A 297 ? 0.40816 0.31529 0.40764 0.00556  0.01647  -0.04711 297 ASN A O   
2408 C  CB  . ASN A 297 ? 0.44618 0.30801 0.42217 0.00480  0.01859  -0.06370 297 ASN A CB  
2409 C  CG  . ASN A 297 ? 0.46740 0.31848 0.43998 -0.00601 0.01251  -0.06557 297 ASN A CG  
2410 O  OD1 . ASN A 297 ? 0.45793 0.31656 0.43942 -0.01190 0.00883  -0.05935 297 ASN A OD1 
2411 N  ND2 . ASN A 297 ? 0.48973 0.32286 0.44909 -0.00884 0.01155  -0.07415 297 ASN A ND2 
2412 N  N   . ALA A 298 ? 0.26284 0.15357 0.26370 -0.00418 0.01130  -0.04511 298 ALA A N   
2413 C  CA  . ALA A 298 ? 0.24815 0.15602 0.25558 -0.00859 0.00838  -0.03978 298 ALA A CA  
2414 C  C   . ALA A 298 ? 0.24154 0.15902 0.25716 -0.00312 0.00989  -0.03246 298 ALA A C   
2415 O  O   . ALA A 298 ? 0.22648 0.15888 0.24529 -0.00244 0.00934  -0.02987 298 ALA A O   
2416 C  CB  . ALA A 298 ? 0.24161 0.14640 0.25103 -0.01779 0.00450  -0.03804 298 ALA A CB  
2417 N  N   . VAL A 299 ? 0.26576 0.17399 0.28427 0.00063  0.01122  -0.02893 299 VAL A N   
2418 C  CA  . VAL A 299 ? 0.26073 0.17731 0.28614 0.00524  0.01142  -0.02164 299 VAL A CA  
2419 C  C   . VAL A 299 ? 0.25841 0.18396 0.28662 0.01280  0.01389  -0.02193 299 VAL A C   
2420 O  O   . VAL A 299 ? 0.24057 0.17964 0.27353 0.01394  0.01271  -0.01759 299 VAL A O   
2421 C  CB  . VAL A 299 ? 0.26918 0.17289 0.29639 0.00720  0.01160  -0.01715 299 VAL A CB  
2422 C  CG1 . VAL A 299 ? 0.25798 0.16923 0.29129 0.01349  0.01138  -0.01015 299 VAL A CG1 
2423 C  CG2 . VAL A 299 ? 0.26865 0.16783 0.29498 -0.00112 0.00934  -0.01442 299 VAL A CG2 
2424 N  N   . GLU A 300 ? 0.27951 0.19746 0.30471 0.01792  0.01755  -0.02700 300 GLU A N   
2425 C  CA  . GLU A 300 ? 0.27251 0.20047 0.30145 0.02504  0.02096  -0.02696 300 GLU A CA  
2426 C  C   . GLU A 300 ? 0.25904 0.20125 0.28627 0.02151  0.02020  -0.02837 300 GLU A C   
2427 O  O   . GLU A 300 ? 0.24787 0.20375 0.28134 0.02414  0.02053  -0.02451 300 GLU A O   
2428 C  CB  . GLU A 300 ? 0.27435 0.19047 0.29892 0.03160  0.02628  -0.03275 300 GLU A CB  
2429 C  CG  . GLU A 300 ? 0.26949 0.19633 0.30056 0.04040  0.03117  -0.03132 300 GLU A CG  
2430 C  CD  . GLU A 300 ? 0.26891 0.20658 0.29545 0.03892  0.03337  -0.03499 300 GLU A CD  
2431 O  OE1 . GLU A 300 ? 0.27566 0.20470 0.29024 0.03570  0.03425  -0.04219 300 GLU A OE1 
2432 O  OE2 . GLU A 300 ? 0.25384 0.20822 0.28830 0.04047  0.03375  -0.03036 300 GLU A OE2 
2433 N  N   . GLY A 301 ? 0.33903 0.27803 0.35810 0.01527  0.01867  -0.03347 301 GLY A N   
2434 C  CA  . GLY A 301 ? 0.33142 0.28298 0.34854 0.01187  0.01733  -0.03409 301 GLY A CA  
2435 C  C   . GLY A 301 ? 0.32368 0.28726 0.34732 0.00910  0.01380  -0.02786 301 GLY A C   
2436 O  O   . GLY A 301 ? 0.30980 0.28502 0.33520 0.00936  0.01359  -0.02611 301 GLY A O   
2437 N  N   . PHE A 302 ? 0.28047 0.24040 0.30684 0.00641  0.01127  -0.02441 302 PHE A N   
2438 C  CA  . PHE A 302 ? 0.26980 0.23911 0.30029 0.00441  0.00848  -0.01895 302 PHE A CA  
2439 C  C   . PHE A 302 ? 0.26848 0.24399 0.30489 0.00956  0.00871  -0.01412 302 PHE A C   
2440 O  O   . PHE A 302 ? 0.25187 0.23757 0.29028 0.00910  0.00714  -0.01170 302 PHE A O   
2441 C  CB  . PHE A 302 ? 0.27174 0.23514 0.30231 0.00030  0.00671  -0.01647 302 PHE A CB  
2442 C  CG  . PHE A 302 ? 0.25604 0.22714 0.28863 -0.00112 0.00471  -0.01133 302 PHE A CG  
2443 C  CD1 . PHE A 302 ? 0.24056 0.22070 0.27241 -0.00388 0.00338  -0.01171 302 PHE A CD1 
2444 C  CD2 . PHE A 302 ? 0.25642 0.22461 0.29048 0.00064  0.00414  -0.00613 302 PHE A CD2 
2445 C  CE1 . PHE A 302 ? 0.23298 0.21818 0.26505 -0.00452 0.00211  -0.00774 302 PHE A CE1 
2446 C  CE2 . PHE A 302 ? 0.24625 0.21991 0.27947 -0.00056 0.00249  -0.00207 302 PHE A CE2 
2447 C  CZ  . PHE A 302 ? 0.23763 0.21932 0.26961 -0.00298 0.00177  -0.00325 302 PHE A CZ  
2448 N  N   . ILE A 303 ? 0.29376 0.26290 0.33336 0.01437  0.01018  -0.01242 303 ILE A N   
2449 C  CA  . ILE A 303 ? 0.28308 0.25909 0.32988 0.01914  0.00941  -0.00703 303 ILE A CA  
2450 C  C   . ILE A 303 ? 0.27433 0.26117 0.32506 0.02205  0.01153  -0.00782 303 ILE A C   
2451 O  O   . ILE A 303 ? 0.26266 0.25985 0.31933 0.02278  0.00937  -0.00330 303 ILE A O   
2452 C  CB  . ILE A 303 ? 0.29239 0.25896 0.34248 0.02438  0.01049  -0.00467 303 ILE A CB  
2453 C  CG1 . ILE A 303 ? 0.29669 0.25604 0.34423 0.02117  0.00740  -0.00064 303 ILE A CG1 
2454 C  CG2 . ILE A 303 ? 0.28018 0.25543 0.33977 0.03085  0.01053  -0.00002 303 ILE A CG2 
2455 C  CD1 . ILE A 303 ? 0.30044 0.24648 0.34887 0.02506  0.00849  0.00113  303 ILE A CD1 
2456 N  N   . ARG A 304 ? 0.32455 0.30905 0.37136 0.02316  0.01562  -0.01338 304 ARG A N   
2457 C  CA  . ARG A 304 ? 0.31609 0.31108 0.36578 0.02572  0.01868  -0.01372 304 ARG A CA  
2458 C  C   . ARG A 304 ? 0.30099 0.30646 0.35021 0.02063  0.01554  -0.01182 304 ARG A C   
2459 O  O   . ARG A 304 ? 0.28939 0.30572 0.34426 0.02184  0.01634  -0.00892 304 ARG A O   
2460 C  CB  . ARG A 304 ? 0.32674 0.31537 0.36880 0.02754  0.02385  -0.02054 304 ARG A CB  
2461 C  CG  . ARG A 304 ? 0.33002 0.32816 0.37569 0.03245  0.02925  -0.02032 304 ARG A CG  
2462 C  CD  . ARG A 304 ? 0.34185 0.33534 0.37572 0.03192  0.03334  -0.02714 304 ARG A CD  
2463 N  NE  . ARG A 304 ? 0.36029 0.33674 0.38516 0.03289  0.03467  -0.03349 304 ARG A NE  
2464 C  CZ  . ARG A 304 ? 0.37760 0.34542 0.38983 0.02799  0.03326  -0.03958 304 ARG A CZ  
2465 N  NH1 . ARG A 304 ? 0.36950 0.34451 0.37665 0.02259  0.03074  -0.03992 304 ARG A NH1 
2466 N  NH2 . ARG A 304 ? 0.37950 0.33060 0.38406 0.02834  0.03385  -0.04520 304 ARG A NH2 
2467 N  N   . GLN A 305 ? 0.33780 0.34023 0.38104 0.01501  0.01213  -0.01306 305 GLN A N   
2468 C  CA  . GLN A 305 ? 0.32908 0.33957 0.37144 0.01099  0.00925  -0.01133 305 GLN A CA  
2469 C  C   . GLN A 305 ? 0.32233 0.33844 0.37052 0.01080  0.00558  -0.00563 305 GLN A C   
2470 O  O   . GLN A 305 ? 0.30735 0.33084 0.35698 0.00891  0.00385  -0.00350 305 GLN A O   
2471 C  CB  . GLN A 305 ? 0.32568 0.33208 0.36147 0.00607  0.00694  -0.01381 305 GLN A CB  
2472 C  CG  . GLN A 305 ? 0.33836 0.33828 0.36770 0.00481  0.00874  -0.01946 305 GLN A CG  
2473 C  CD  . GLN A 305 ? 0.34820 0.35027 0.37438 0.00727  0.01246  -0.02237 305 GLN A CD  
2474 O  OE1 . GLN A 305 ? 0.33931 0.34941 0.36510 0.00657  0.01249  -0.02096 305 GLN A OE1 
2475 N  NE2 . GLN A 305 ? 0.35941 0.35329 0.38237 0.01024  0.01595  -0.02642 305 GLN A NE2 
2476 N  N   . ILE A 306 ? 0.25753 0.26936 0.30824 0.01242  0.00393  -0.00296 306 ILE A N   
2477 C  CA  . ILE A 306 ? 0.25701 0.27202 0.31008 0.01139  -0.00072 0.00203  306 ILE A CA  
2478 C  C   . ILE A 306 ? 0.25041 0.27280 0.31318 0.01504  -0.00145 0.00636  306 ILE A C   
2479 O  O   . ILE A 306 ? 0.24419 0.27468 0.31069 0.01319  -0.00450 0.00941  306 ILE A O   
2480 C  CB  . ILE A 306 ? 0.27452 0.28100 0.32329 0.01053  -0.00258 0.00329  306 ILE A CB  
2481 C  CG1 . ILE A 306 ? 0.26419 0.26695 0.30571 0.00633  -0.00222 0.00024  306 ILE A CG1 
2482 C  CG2 . ILE A 306 ? 0.25917 0.26768 0.30868 0.01027  -0.00747 0.00849  306 ILE A CG2 
2483 C  CD1 . ILE A 306 ? 0.27119 0.26577 0.30913 0.00521  -0.00210 0.00114  306 ILE A CD1 
2484 N  N   . ILE A 307 ? 0.16535 0.18496 0.23301 0.02021  0.00108  0.00701  307 ILE A N   
2485 C  CA  . ILE A 307 ? 0.16029 0.18880 0.23963 0.02466  0.00081  0.01170  307 ILE A CA  
2486 C  C   . ILE A 307 ? 0.15409 0.19172 0.23927 0.02691  0.00596  0.01039  307 ILE A C   
2487 O  O   . ILE A 307 ? 0.14235 0.19119 0.23922 0.02965  0.00594  0.01496  307 ILE A O   
2488 C  CB  . ILE A 307 ? 0.16576 0.18788 0.24915 0.03062  0.00180  0.01366  307 ILE A CB  
2489 C  CG1 . ILE A 307 ? 0.18064 0.19688 0.26362 0.03564  0.00914  0.00871  307 ILE A CG1 
2490 C  CG2 . ILE A 307 ? 0.17489 0.18576 0.25004 0.02808  -0.00169 0.01444  307 ILE A CG2 
2491 C  CD1 . ILE A 307 ? 0.18676 0.19626 0.27501 0.04280  0.01073  0.01084  307 ILE A CD1 
2492 N  N   . GLY A 308 ? 0.28553 0.31941 0.36299 0.02565  0.01030  0.00473  308 GLY A N   
2493 C  CA  . GLY A 308 ? 0.27362 0.31552 0.35386 0.02739  0.01568  0.00352  308 GLY A CA  
2494 C  C   . GLY A 308 ? 0.26643 0.31531 0.34425 0.02144  0.01354  0.00444  308 GLY A C   
2495 O  O   . GLY A 308 ? 0.25673 0.31657 0.34326 0.02009  0.01159  0.00950  308 GLY A O   
2496 N  N   . TRP A 309 ? 0.25650 0.29892 0.32306 0.01759  0.01331  0.00003  309 TRP A N   
2497 C  CA  . TRP A 309 ? 0.25470 0.30235 0.31812 0.01287  0.01204  0.00076  309 TRP A CA  
2498 C  C   . TRP A 309 ? 0.24389 0.29444 0.31021 0.00860  0.00543  0.00516  309 TRP A C   
2499 O  O   . TRP A 309 ? 0.23629 0.29449 0.30660 0.00590  0.00427  0.00860  309 TRP A O   
2500 C  CB  . TRP A 309 ? 0.25750 0.29763 0.30894 0.01024  0.01237  -0.00442 309 TRP A CB  
2501 C  CG  . TRP A 309 ? 0.27180 0.31123 0.31783 0.01253  0.01827  -0.00839 309 TRP A CG  
2502 C  CD1 . TRP A 309 ? 0.27613 0.30618 0.31444 0.01413  0.02066  -0.01413 309 TRP A CD1 
2503 C  CD2 . TRP A 309 ? 0.26578 0.31339 0.31232 0.01314  0.02257  -0.00697 309 TRP A CD2 
2504 N  NE1 . TRP A 309 ? 0.28256 0.31360 0.31499 0.01603  0.02601  -0.01701 309 TRP A NE1 
2505 C  CE2 . TRP A 309 ? 0.27752 0.31982 0.31490 0.01569  0.02776  -0.01242 309 TRP A CE2 
2506 C  CE3 . TRP A 309 ? 0.25345 0.31187 0.30680 0.01129  0.02252  -0.00142 309 TRP A CE3 
2507 C  CZ2 . TRP A 309 ? 0.27525 0.32303 0.30903 0.01711  0.03357  -0.01247 309 TRP A CZ2 
2508 C  CZ3 . TRP A 309 ? 0.25564 0.32038 0.30728 0.01226  0.02837  -0.00077 309 TRP A CZ3 
2509 C  CH2 . TRP A 309 ? 0.26530 0.32489 0.30672 0.01547  0.03416  -0.00625 309 TRP A CH2 
2510 N  N   . ARG A 310 ? 0.17598 0.21967 0.23941 0.00768  0.00117  0.00513  310 ARG A N   
2511 C  CA  . ARG A 310 ? 0.17368 0.21754 0.23639 0.00375  -0.00502 0.00820  310 ARG A CA  
2512 C  C   . ARG A 310 ? 0.16769 0.22044 0.24095 0.00364  -0.00797 0.01371  310 ARG A C   
2513 O  O   . ARG A 310 ? 0.16401 0.22048 0.23854 -0.00060 -0.01179 0.01638  310 ARG A O   
2514 C  CB  . ARG A 310 ? 0.18278 0.21752 0.23916 0.00347  -0.00783 0.00716  310 ARG A CB  
2515 C  CG  . ARG A 310 ? 0.17383 0.20561 0.22472 -0.00034 -0.01318 0.00851  310 ARG A CG  
2516 C  CD  . ARG A 310 ? 0.18228 0.20532 0.22537 -0.00024 -0.01395 0.00707  310 ARG A CD  
2517 N  NE  . ARG A 310 ? 0.18276 0.20180 0.21889 -0.00293 -0.01828 0.00791  310 ARG A NE  
2518 C  CZ  . ARG A 310 ? 0.18759 0.20480 0.22199 -0.00360 -0.02298 0.01082  310 ARG A CZ  
2519 N  NH1 . ARG A 310 ? 0.18843 0.20874 0.22918 -0.00163 -0.02442 0.01405  310 ARG A NH1 
2520 N  NH2 . ARG A 310 ? 0.18425 0.19580 0.20969 -0.00600 -0.02651 0.01049  310 ARG A NH2 
2521 N  N   . GLU A 311 ? 0.17330 0.22941 0.25481 0.00818  -0.00664 0.01579  311 GLU A N   
2522 C  CA  . GLU A 311 ? 0.16373 0.23089 0.25796 0.00839  -0.00961 0.02178  311 GLU A CA  
2523 C  C   . GLU A 311 ? 0.15818 0.23712 0.26086 0.00804  -0.00535 0.02367  311 GLU A C   
2524 O  O   . GLU A 311 ? 0.14669 0.23548 0.25860 0.00471  -0.00901 0.02886  311 GLU A O   
2525 C  CB  . GLU A 311 ? 0.16747 0.23558 0.26935 0.01443  -0.00905 0.02407  311 GLU A CB  
2526 C  CG  . GLU A 311 ? 0.17826 0.23470 0.27170 0.01475  -0.01286 0.02331  311 GLU A CG  
2527 C  CD  . GLU A 311 ? 0.18047 0.23642 0.27098 0.00998  -0.02159 0.02685  311 GLU A CD  
2528 O  OE1 . GLU A 311 ? 0.16751 0.23347 0.26670 0.00749  -0.02592 0.03124  311 GLU A OE1 
2529 O  OE2 . GLU A 311 ? 0.18397 0.22940 0.26313 0.00850  -0.02408 0.02528  311 GLU A OE2 
2530 N  N   . PHE A 312 ? 0.16461 0.24252 0.26367 0.01091  0.00222  0.01974  312 PHE A N   
2531 C  CA  . PHE A 312 ? 0.15987 0.24866 0.26515 0.01104  0.00765  0.02163  312 PHE A CA  
2532 C  C   . PHE A 312 ? 0.15924 0.24982 0.26113 0.00376  0.00428  0.02347  312 PHE A C   
2533 O  O   . PHE A 312 ? 0.14557 0.24756 0.25740 0.00106  0.00424  0.02876  312 PHE A O   
2534 C  CB  . PHE A 312 ? 0.16430 0.24872 0.26228 0.01565  0.01611  0.01613  312 PHE A CB  
2535 C  CG  . PHE A 312 ? 0.16645 0.26185 0.26958 0.01725  0.02341  0.01801  312 PHE A CG  
2536 C  CD1 . PHE A 312 ? 0.15840 0.26650 0.27684 0.02203  0.02755  0.02257  312 PHE A CD1 
2537 C  CD2 . PHE A 312 ? 0.16236 0.25591 0.25509 0.01437  0.02649  0.01567  312 PHE A CD2 
2538 C  CE1 . PHE A 312 ? 0.16020 0.27940 0.28355 0.02383  0.03556  0.02468  312 PHE A CE1 
2539 C  CE2 . PHE A 312 ? 0.16701 0.27042 0.26289 0.01582  0.03394  0.01778  312 PHE A CE2 
2540 C  CZ  . PHE A 312 ? 0.16130 0.27773 0.27250 0.02055  0.03897  0.02223  312 PHE A CZ  
2541 N  N   . VAL A 313 ? 0.16550 0.24497 0.25415 0.00055  0.00154  0.01958  313 VAL A N   
2542 C  CA  . VAL A 313 ? 0.16637 0.24534 0.25080 -0.00550 -0.00135 0.02114  313 VAL A CA  
2543 C  C   . VAL A 313 ? 0.16072 0.24134 0.25046 -0.01049 -0.00923 0.02564  313 VAL A C   
2544 O  O   . VAL A 313 ? 0.16103 0.24635 0.25449 -0.01554 -0.01116 0.02958  313 VAL A O   
2545 C  CB  . VAL A 313 ? 0.16944 0.23672 0.23950 -0.00651 -0.00201 0.01609  313 VAL A CB  
2546 C  CG1 . VAL A 313 ? 0.17376 0.23986 0.23816 -0.00287 0.00466  0.01188  313 VAL A CG1 
2547 C  CG2 . VAL A 313 ? 0.17891 0.23677 0.24368 -0.00613 -0.00656 0.01360  313 VAL A CG2 
2548 N  N   . ARG A 314 ? 0.22461 0.30076 0.31406 -0.00960 -0.01418 0.02534  314 ARG A N   
2549 C  CA  . ARG A 314 ? 0.22048 0.29778 0.31374 -0.01447 -0.02244 0.02938  314 ARG A CA  
2550 C  C   . ARG A 314 ? 0.21873 0.31175 0.32920 -0.01546 -0.02279 0.03586  314 ARG A C   
2551 O  O   . ARG A 314 ? 0.21167 0.30866 0.32705 -0.02187 -0.02842 0.04007  314 ARG A O   
2552 C  CB  . ARG A 314 ? 0.22368 0.29317 0.31165 -0.01284 -0.02730 0.02804  314 ARG A CB  
2553 C  CG  . ARG A 314 ? 0.22554 0.29714 0.31752 -0.01737 -0.03642 0.03244  314 ARG A CG  
2554 C  CD  . ARG A 314 ? 0.24084 0.30091 0.32131 -0.01687 -0.04148 0.03036  314 ARG A CD  
2555 N  NE  . ARG A 314 ? 0.24302 0.30458 0.32565 -0.02117 -0.05096 0.03442  314 ARG A NE  
2556 C  CZ  . ARG A 314 ? 0.23406 0.30529 0.32836 -0.01952 -0.05433 0.03940  314 ARG A CZ  
2557 N  NH1 . ARG A 314 ? 0.22957 0.30924 0.33482 -0.01296 -0.04828 0.04086  314 ARG A NH1 
2558 N  NH2 . ARG A 314 ? 0.22669 0.29856 0.32132 -0.02439 -0.06435 0.04297  314 ARG A NH2 
2559 N  N   . GLY A 315 ? 0.16591 0.26793 0.28623 -0.00917 -0.01679 0.03688  315 GLY A N   
2560 C  CA  . GLY A 315 ? 0.14847 0.26774 0.28739 -0.00898 -0.01587 0.04355  315 GLY A CA  
2561 C  C   . GLY A 315 ? 0.14543 0.27320 0.28912 -0.01359 -0.01243 0.04670  315 GLY A C   
2562 O  O   . GLY A 315 ? 0.13984 0.27895 0.29631 -0.01883 -0.01637 0.05319  315 GLY A O   
2563 N  N   . ILE A 316 ? 0.18944 0.31185 0.32277 -0.01225 -0.00550 0.04264  316 ILE A N   
2564 C  CA  . ILE A 316 ? 0.18876 0.31838 0.32478 -0.01637 -0.00151 0.04609  316 ILE A CA  
2565 C  C   . ILE A 316 ? 0.18984 0.31327 0.32143 -0.02561 -0.00971 0.04831  316 ILE A C   
2566 O  O   . ILE A 316 ? 0.18592 0.31863 0.32706 -0.03154 -0.01067 0.05455  316 ILE A O   
2567 C  CB  . ILE A 316 ? 0.19274 0.31696 0.31649 -0.01238 0.00720  0.04108  316 ILE A CB  
2568 C  CG1 . ILE A 316 ? 0.19749 0.33001 0.32770 -0.00396 0.01657  0.04013  316 ILE A CG1 
2569 C  CG2 . ILE A 316 ? 0.19636 0.32283 0.31704 -0.01796 0.00931  0.04430  316 ILE A CG2 
2570 C  CD1 . ILE A 316 ? 0.20567 0.33155 0.32195 -0.00007 0.02449  0.03443  316 ILE A CD1 
2571 N  N   . TYR A 317 ? 0.16492 0.27222 0.28209 -0.02693 -0.01539 0.04339  317 TYR A N   
2572 C  CA  . TYR A 317 ? 0.16880 0.26694 0.27963 -0.03467 -0.02314 0.04445  317 TYR A CA  
2573 C  C   . TYR A 317 ? 0.16755 0.27389 0.29134 -0.04109 -0.03064 0.05070  317 TYR A C   
2574 O  O   . TYR A 317 ? 0.16238 0.27330 0.29210 -0.04802 -0.03234 0.05581  317 TYR A O   
2575 C  CB  . TYR A 317 ? 0.18205 0.26305 0.27714 -0.03330 -0.02755 0.03817  317 TYR A CB  
2576 C  CG  . TYR A 317 ? 0.18924 0.25763 0.27507 -0.03975 -0.03479 0.03793  317 TYR A CG  
2577 C  CD1 . TYR A 317 ? 0.19429 0.25578 0.27241 -0.04192 -0.03301 0.03757  317 TYR A CD1 
2578 C  CD2 . TYR A 317 ? 0.19464 0.25669 0.27815 -0.04334 -0.04356 0.03797  317 TYR A CD2 
2579 C  CE1 . TYR A 317 ? 0.20414 0.25213 0.27336 -0.04700 -0.03931 0.03714  317 TYR A CE1 
2580 C  CE2 . TYR A 317 ? 0.19988 0.24793 0.27298 -0.04881 -0.04991 0.03688  317 TYR A CE2 
2581 C  CZ  . TYR A 317 ? 0.21189 0.25262 0.27829 -0.05036 -0.04751 0.03641  317 TYR A CZ  
2582 O  OH  . TYR A 317 ? 0.22003 0.24507 0.27580 -0.05504 -0.05350 0.03519  317 TYR A OH  
2583 N  N   . TRP A 318 ? 0.19701 0.30564 0.32572 -0.03926 -0.03558 0.05093  318 TRP A N   
2584 C  CA  . TRP A 318 ? 0.19239 0.30859 0.33278 -0.04584 -0.04451 0.05681  318 TRP A CA  
2585 C  C   . TRP A 318 ? 0.17959 0.31801 0.34225 -0.04674 -0.04069 0.06464  318 TRP A C   
2586 O  O   . TRP A 318 ? 0.17362 0.32049 0.34818 -0.05438 -0.04784 0.07085  318 TRP A O   
2587 C  CB  . TRP A 318 ? 0.18778 0.30021 0.32597 -0.04324 -0.05120 0.05531  318 TRP A CB  
2588 C  CG  . TRP A 318 ? 0.20572 0.29726 0.32281 -0.04426 -0.05611 0.04895  318 TRP A CG  
2589 C  CD1 . TRP A 318 ? 0.21606 0.29710 0.32060 -0.03779 -0.05310 0.04312  318 TRP A CD1 
2590 C  CD2 . TRP A 318 ? 0.21591 0.29424 0.32196 -0.05207 -0.06425 0.04784  318 TRP A CD2 
2591 N  NE1 . TRP A 318 ? 0.22108 0.28485 0.30824 -0.04056 -0.05816 0.03877  318 TRP A NE1 
2592 C  CE2 . TRP A 318 ? 0.22401 0.28481 0.31092 -0.04889 -0.06500 0.04112  318 TRP A CE2 
2593 C  CE3 . TRP A 318 ? 0.21043 0.28939 0.32086 -0.06158 -0.07086 0.05192  318 TRP A CE3 
2594 C  CZ2 . TRP A 318 ? 0.23573 0.27935 0.30704 -0.05376 -0.07143 0.03789  318 TRP A CZ2 
2595 C  CZ3 . TRP A 318 ? 0.22428 0.28444 0.31849 -0.06711 -0.07814 0.04844  318 TRP A CZ3 
2596 C  CH2 . TRP A 318 ? 0.23187 0.27440 0.30635 -0.06264 -0.07805 0.04124  318 TRP A CH2 
2597 N  N   . LEU A 319 ? 0.17230 0.32032 0.34074 -0.03931 -0.02950 0.06452  319 LEU A N   
2598 C  CA  . LEU A 319 ? 0.15897 0.32889 0.34853 -0.03912 -0.02396 0.07203  319 LEU A CA  
2599 C  C   . LEU A 319 ? 0.15806 0.33159 0.34911 -0.04638 -0.02104 0.07617  319 LEU A C   
2600 O  O   . LEU A 319 ? 0.15362 0.34382 0.36289 -0.05176 -0.02171 0.08440  319 LEU A O   
2601 C  CB  . LEU A 319 ? 0.15662 0.33377 0.34991 -0.02781 -0.01230 0.06985  319 LEU A CB  
2602 C  CG  . LEU A 319 ? 0.15040 0.35066 0.36507 -0.02500 -0.00393 0.07699  319 LEU A CG  
2603 C  CD1 . LEU A 319 ? 0.13283 0.34966 0.36978 -0.02710 -0.01121 0.08471  319 LEU A CD1 
2604 C  CD2 . LEU A 319 ? 0.15050 0.35200 0.36276 -0.01316 0.00831  0.07262  319 LEU A CD2 
2605 N  N   . LYS A 320 ? 0.16713 0.32575 0.33997 -0.04688 -0.01803 0.07131  320 LYS A N   
2606 C  CA  . LYS A 320 ? 0.17106 0.33215 0.34342 -0.05232 -0.01369 0.07539  320 LYS A CA  
2607 C  C   . LYS A 320 ? 0.17988 0.32599 0.34225 -0.06202 -0.02259 0.07584  320 LYS A C   
2608 O  O   . LYS A 320 ? 0.18086 0.32981 0.34583 -0.06842 -0.02085 0.08125  320 LYS A O   
2609 C  CB  . LYS A 320 ? 0.17503 0.33157 0.33445 -0.04541 -0.00285 0.07074  320 LYS A CB  
2610 C  CG  . LYS A 320 ? 0.17289 0.34172 0.33964 -0.03558 0.00729  0.06962  320 LYS A CG  
2611 C  CD  . LYS A 320 ? 0.16049 0.35237 0.34917 -0.03667 0.01281  0.07852  320 LYS A CD  
2612 C  CE  . LYS A 320 ? 0.15472 0.35602 0.34530 -0.02656 0.02640  0.07696  320 LYS A CE  
2613 N  NZ  . LYS A 320 ? 0.14751 0.37297 0.36279 -0.02480 0.03178  0.08512  320 LYS A NZ  
2614 N  N   . MET A 321 ? 0.17127 0.30076 0.32159 -0.06300 -0.03149 0.07043  321 MET A N   
2615 C  CA  . MET A 321 ? 0.17956 0.29292 0.31957 -0.07144 -0.03986 0.07026  321 MET A CA  
2616 C  C   . MET A 321 ? 0.17172 0.29390 0.32688 -0.08209 -0.04757 0.07812  321 MET A C   
2617 O  O   . MET A 321 ? 0.16419 0.30252 0.33612 -0.08234 -0.04972 0.08217  321 MET A O   
2618 C  CB  . MET A 321 ? 0.18880 0.28310 0.31241 -0.06919 -0.04675 0.06252  321 MET A CB  
2619 C  CG  . MET A 321 ? 0.19716 0.27863 0.30373 -0.06176 -0.04118 0.05530  321 MET A CG  
2620 S  SD  . MET A 321 ? 0.21440 0.28391 0.30957 -0.06519 -0.03900 0.05607  321 MET A SD  
2621 C  CE  . MET A 321 ? 0.22269 0.26987 0.30502 -0.07120 -0.05042 0.05316  321 MET A CE  
2622 N  N   . PRO A 322 ? 0.17201 0.28350 0.32208 -0.09127 -0.05245 0.08072  322 PRO A N   
2623 C  CA  . PRO A 322 ? 0.18304 0.27422 0.31412 -0.09157 -0.05158 0.07695  322 PRO A CA  
2624 C  C   . PRO A 322 ? 0.18283 0.28047 0.31452 -0.08997 -0.04116 0.08076  322 PRO A C   
2625 O  O   . PRO A 322 ? 0.19406 0.27709 0.31029 -0.08785 -0.03911 0.07765  322 PRO A O   
2626 C  CB  . PRO A 322 ? 0.19395 0.27214 0.32260 -0.10316 -0.06278 0.07946  322 PRO A CB  
2627 C  CG  . PRO A 322 ? 0.18950 0.28863 0.34122 -0.11118 -0.06521 0.08867  322 PRO A CG  
2628 C  CD  . PRO A 322 ? 0.17583 0.29494 0.34056 -0.10304 -0.06062 0.08849  322 PRO A CD  
2629 N  N   . GLU A 323 ? 0.29518 0.41488 0.44426 -0.09056 -0.03430 0.08775  323 GLU A N   
2630 C  CA  . GLU A 323 ? 0.30169 0.42761 0.45002 -0.08973 -0.02416 0.09204  323 GLU A CA  
2631 C  C   . GLU A 323 ? 0.30935 0.42900 0.44224 -0.07907 -0.01642 0.08488  323 GLU A C   
2632 O  O   . GLU A 323 ? 0.31852 0.43443 0.44223 -0.07853 -0.01079 0.08634  323 GLU A O   
2633 C  CB  . GLU A 323 ? 0.28501 0.43727 0.45521 -0.09092 -0.01697 0.10041  323 GLU A CB  
2634 C  CG  . GLU A 323 ? 0.28049 0.44101 0.46723 -0.10292 -0.02366 0.10939  323 GLU A CG  
2635 C  CD  . GLU A 323 ? 0.28530 0.44951 0.48125 -0.10292 -0.03260 0.10747  323 GLU A CD  
2636 O  OE1 . GLU A 323 ? 0.26760 0.43523 0.46456 -0.09565 -0.03234 0.10261  323 GLU A OE1 
2637 O  OE2 . GLU A 323 ? 0.30401 0.46753 0.50572 -0.11024 -0.04002 0.11114  323 GLU A OE2 
2638 N  N   . TYR A 324 ? 0.18806 0.30629 0.31772 -0.07105 -0.01652 0.07754  324 TYR A N   
2639 C  CA  . TYR A 324 ? 0.19210 0.30441 0.30796 -0.06182 -0.01009 0.07062  324 TYR A CA  
2640 C  C   . TYR A 324 ? 0.21367 0.30617 0.31125 -0.06253 -0.01348 0.06709  324 TYR A C   
2641 O  O   . TYR A 324 ? 0.21168 0.30136 0.29894 -0.05855 -0.00778 0.06550  324 TYR A O   
2642 C  CB  . TYR A 324 ? 0.18610 0.29871 0.30243 -0.05451 -0.01094 0.06401  324 TYR A CB  
2643 C  CG  . TYR A 324 ? 0.18795 0.29757 0.29346 -0.04551 -0.00375 0.05749  324 TYR A CG  
2644 C  CD1 . TYR A 324 ? 0.18264 0.30536 0.29392 -0.03982 0.00579  0.05792  324 TYR A CD1 
2645 C  CD2 . TYR A 324 ? 0.20178 0.29536 0.29143 -0.04277 -0.00655 0.05087  324 TYR A CD2 
2646 C  CE1 . TYR A 324 ? 0.18615 0.30425 0.28617 -0.03243 0.01150  0.05143  324 TYR A CE1 
2647 C  CE2 . TYR A 324 ? 0.19436 0.28556 0.27495 -0.03576 -0.00105 0.04519  324 TYR A CE2 
2648 C  CZ  . TYR A 324 ? 0.19705 0.29964 0.28211 -0.03102 0.00753  0.04524  324 TYR A CZ  
2649 O  OH  . TYR A 324 ? 0.20135 0.29967 0.27598 -0.02485 0.01217  0.03907  324 TYR A OH  
2650 N  N   . ALA A 325 ? 0.20710 0.28547 0.30013 -0.06736 -0.02290 0.06593  325 ALA A N   
2651 C  CA  . ALA A 325 ? 0.22541 0.28438 0.30215 -0.06703 -0.02624 0.06261  325 ALA A CA  
2652 C  C   . ALA A 325 ? 0.22854 0.28443 0.30168 -0.07155 -0.02407 0.06880  325 ALA A C   
2653 O  O   . ALA A 325 ? 0.23800 0.27916 0.29799 -0.06991 -0.02563 0.06683  325 ALA A O   
2654 C  CB  . ALA A 325 ? 0.23071 0.27450 0.30298 -0.07096 -0.03626 0.05990  325 ALA A CB  
2655 N  N   . GLN A 326 ? 0.23986 0.30957 0.32475 -0.07698 -0.02040 0.07679  326 GLN A N   
2656 C  CA  . GLN A 326 ? 0.24889 0.31612 0.33089 -0.08234 -0.01824 0.08409  326 GLN A CA  
2657 C  C   . GLN A 326 ? 0.24890 0.32984 0.33059 -0.07837 -0.00730 0.08712  326 GLN A C   
2658 O  O   . GLN A 326 ? 0.25041 0.33042 0.32840 -0.08229 -0.00435 0.09380  326 GLN A O   
2659 C  CB  . GLN A 326 ? 0.25135 0.32223 0.34635 -0.09368 -0.02296 0.09229  326 GLN A CB  
2660 C  CG  . GLN A 326 ? 0.25901 0.31285 0.35117 -0.09919 -0.03474 0.08953  326 GLN A CG  
2661 C  CD  . GLN A 326 ? 0.29294 0.32249 0.36602 -0.09578 -0.03880 0.08395  326 GLN A CD  
2662 O  OE1 . GLN A 326 ? 0.29683 0.32011 0.36070 -0.09381 -0.03518 0.08604  326 GLN A OE1 
2663 N  NE2 . GLN A 326 ? 0.29838 0.31450 0.36531 -0.09464 -0.04620 0.07712  326 GLN A NE2 
2664 N  N   . ARG A 327 ? 0.35293 0.44520 0.43703 -0.07070 -0.00117 0.08240  327 ARG A N   
2665 C  CA  . ARG A 327 ? 0.35008 0.45433 0.43219 -0.06654 0.00962  0.08435  327 ARG A CA  
2666 C  C   . ARG A 327 ? 0.35681 0.44924 0.41959 -0.06248 0.01098  0.08130  327 ARG A C   
2667 O  O   . ARG A 327 ? 0.36319 0.44304 0.41626 -0.05841 0.00600  0.07434  327 ARG A O   
2668 C  CB  . ARG A 327 ? 0.33707 0.45413 0.42632 -0.05906 0.01538  0.07942  327 ARG A CB  
2669 C  CG  . ARG A 327 ? 0.32565 0.45720 0.43573 -0.06203 0.01434  0.08332  327 ARG A CG  
2670 C  CD  . ARG A 327 ? 0.33046 0.48253 0.45265 -0.06166 0.02506  0.09012  327 ARG A CD  
2671 N  NE  . ARG A 327 ? 0.30944 0.47768 0.45405 -0.06403 0.02383  0.09458  327 ARG A NE  
2672 C  CZ  . ARG A 327 ? 0.31615 0.49786 0.47701 -0.07205 0.02444  0.10459  327 ARG A CZ  
2673 N  NH1 . ARG A 327 ? 0.30350 0.48367 0.46026 -0.07876 0.02680  0.11149  327 ARG A NH1 
2674 N  NH2 . ARG A 327 ? 0.29595 0.49347 0.47830 -0.07365 0.02234  0.10841  327 ARG A NH2 
2675 N  N   . ASN A 328 ? 0.25068 0.34807 0.30815 -0.06372 0.01779  0.08716  328 ASN A N   
2676 C  CA  . ASN A 328 ? 0.25916 0.34744 0.29816 -0.06041 0.01914  0.08584  328 ASN A CA  
2677 C  C   . ASN A 328 ? 0.26519 0.36633 0.30038 -0.05834 0.03035  0.08921  328 ASN A C   
2678 O  O   . ASN A 328 ? 0.26320 0.36597 0.29413 -0.06266 0.03393  0.09741  328 ASN A O   
2679 C  CB  . ASN A 328 ? 0.27167 0.34550 0.30382 -0.06610 0.01264  0.09146  328 ASN A CB  
2680 C  CG  . ASN A 328 ? 0.29325 0.35697 0.30706 -0.06185 0.01194  0.08982  328 ASN A CG  
2681 O  OD1 . ASN A 328 ? 0.28194 0.34845 0.28760 -0.05522 0.01513  0.08357  328 ASN A OD1 
2682 N  ND2 . ASN A 328 ? 0.29015 0.34156 0.29749 -0.06582 0.00720  0.09569  328 ASN A ND2 
2683 N  N   . ALA A 329 ? 0.30437 0.41369 0.33993 -0.05133 0.03632  0.08265  329 ALA A N   
2684 C  CA  . ALA A 329 ? 0.29861 0.42094 0.33203 -0.04846 0.04820  0.08488  329 ALA A CA  
2685 C  C   . ALA A 329 ? 0.30552 0.42186 0.31801 -0.04756 0.05143  0.08635  329 ALA A C   
2686 O  O   . ALA A 329 ? 0.31836 0.44383 0.32758 -0.04836 0.06072  0.09222  329 ALA A O   
2687 C  CB  . ALA A 329 ? 0.28292 0.41133 0.31914 -0.04027 0.05309  0.07630  329 ALA A CB  
2688 N  N   . LEU A 330 ? 0.24047 0.34243 0.23874 -0.04578 0.04408  0.08158  330 LEU A N   
2689 C  CA  . LEU A 330 ? 0.26444 0.36055 0.24214 -0.04465 0.04552  0.08272  330 LEU A CA  
2690 C  C   . LEU A 330 ? 0.26712 0.35419 0.23991 -0.05067 0.03972  0.09144  330 LEU A C   
2691 O  O   . LEU A 330 ? 0.28288 0.36396 0.23842 -0.04999 0.03916  0.09346  330 LEU A O   
2692 C  CB  . LEU A 330 ? 0.25952 0.34705 0.22464 -0.03862 0.04113  0.07244  330 LEU A CB  
2693 C  CG  . LEU A 330 ? 0.25649 0.34967 0.22419 -0.03250 0.04636  0.06329  330 LEU A CG  
2694 C  CD1 . LEU A 330 ? 0.26191 0.34580 0.21627 -0.02809 0.04147  0.05403  330 LEU A CD1 
2695 C  CD2 . LEU A 330 ? 0.25695 0.36128 0.22132 -0.03048 0.05892  0.06534  330 LEU A CD2 
2696 N  N   . ASP A 331 ? 0.40476 0.48984 0.39162 -0.05662 0.03500  0.09675  331 ASP A N   
2697 C  CA  . ASP A 331 ? 0.41766 0.49186 0.40087 -0.06259 0.02924  0.10517  331 ASP A CA  
2698 C  C   . ASP A 331 ? 0.42412 0.48318 0.39331 -0.05884 0.02099  0.10143  331 ASP A C   
2699 O  O   . ASP A 331 ? 0.43385 0.48583 0.39061 -0.06012 0.01941  0.10754  331 ASP A O   
2700 C  CB  . ASP A 331 ? 0.42255 0.50304 0.40022 -0.06719 0.03687  0.11602  331 ASP A CB  
2701 C  CG  . ASP A 331 ? 0.42077 0.51584 0.41658 -0.07294 0.04343  0.12264  331 ASP A CG  
2702 O  OD1 . ASP A 331 ? 0.44208 0.54965 0.43579 -0.07339 0.05407  0.12796  331 ASP A OD1 
2703 O  OD2 . ASP A 331 ? 0.41505 0.50954 0.42720 -0.07703 0.03795  0.12268  331 ASP A OD2 
2704 N  N   . ALA A 332 ? 0.26655 0.32138 0.23847 -0.05403 0.01579  0.09190  332 ALA A N   
2705 C  CA  . ALA A 332 ? 0.27261 0.31517 0.23497 -0.05010 0.00797  0.08827  332 ALA A CA  
2706 C  C   . ALA A 332 ? 0.27598 0.30501 0.24216 -0.05359 0.00039  0.09296  332 ALA A C   
2707 O  O   . ALA A 332 ? 0.26617 0.29278 0.24423 -0.05636 -0.00218 0.09177  332 ALA A O   
2708 C  CB  . ALA A 332 ? 0.25841 0.30189 0.22357 -0.04423 0.00582  0.07715  332 ALA A CB  
2709 N  N   . GLN A 333 ? 0.35989 0.37914 0.31509 -0.05326 -0.00352 0.09828  333 GLN A N   
2710 C  CA  . GLN A 333 ? 0.36948 0.37363 0.32633 -0.05620 -0.01008 0.10364  333 GLN A CA  
2711 C  C   . GLN A 333 ? 0.38510 0.37753 0.33429 -0.05008 -0.01722 0.10158  333 GLN A C   
2712 O  O   . GLN A 333 ? 0.39142 0.36944 0.33969 -0.05108 -0.02246 0.10634  333 GLN A O   
2713 C  CB  . GLN A 333 ? 0.37941 0.38162 0.33268 -0.06313 -0.00753 0.11573  333 GLN A CB  
2714 C  CG  . GLN A 333 ? 0.37071 0.38573 0.33421 -0.06985 -0.00027 0.11960  333 GLN A CG  
2715 C  CD  . GLN A 333 ? 0.36805 0.37964 0.34683 -0.07476 -0.00387 0.11826  333 GLN A CD  
2716 O  OE1 . GLN A 333 ? 0.38494 0.38029 0.36396 -0.07597 -0.01141 0.11847  333 GLN A OE1 
2717 N  NE2 . GLN A 333 ? 0.35807 0.38454 0.34921 -0.07736 0.00132  0.11685  333 GLN A NE2 
2718 N  N   . GLY A 334 ? 0.27276 0.27084 0.21710 -0.04378 -0.01768 0.09487  334 GLY A N   
2719 C  CA  . GLY A 334 ? 0.27537 0.26553 0.21410 -0.03795 -0.02426 0.09404  334 GLY A CA  
2720 C  C   . GLY A 334 ? 0.27088 0.25295 0.21821 -0.03413 -0.02891 0.08790  334 GLY A C   
2721 O  O   . GLY A 334 ? 0.26712 0.25045 0.22337 -0.03559 -0.02741 0.08264  334 GLY A O   
2722 N  N   . LYS A 335 ? 0.34882 0.32269 0.29303 -0.02876 -0.03457 0.08897  335 LYS A N   
2723 C  CA  . LYS A 335 ? 0.35512 0.32151 0.30599 -0.02358 -0.03823 0.08329  335 LYS A CA  
2724 C  C   . LYS A 335 ? 0.34392 0.32126 0.29761 -0.01846 -0.03813 0.07511  335 LYS A C   
2725 O  O   . LYS A 335 ? 0.33928 0.32671 0.28772 -0.01781 -0.03761 0.07483  335 LYS A O   
2726 C  CB  . LYS A 335 ? 0.40983 0.36220 0.35749 -0.01929 -0.04371 0.08888  335 LYS A CB  
2727 C  CG  . LYS A 335 ? 0.42035 0.35639 0.36721 -0.02377 -0.04489 0.09496  335 LYS A CG  
2728 C  CD  . LYS A 335 ? 0.43260 0.36001 0.37126 -0.02320 -0.04809 0.10536  335 LYS A CD  
2729 C  CE  . LYS A 335 ? 0.43829 0.35492 0.37718 -0.01414 -0.05339 0.10569  335 LYS A CE  
2730 N  NZ  . LYS A 335 ? 0.44972 0.35844 0.38062 -0.01285 -0.05709 0.11654  335 LYS A NZ  
2731 N  N   . LEU A 336 ? 0.27590 0.25044 0.23704 -0.01525 -0.03874 0.06851  336 LEU A N   
2732 C  CA  . LEU A 336 ? 0.26705 0.25111 0.23206 -0.01075 -0.03874 0.06139  336 LEU A CA  
2733 C  C   . LEU A 336 ? 0.26710 0.25032 0.23155 -0.00431 -0.04352 0.06358  336 LEU A C   
2734 O  O   . LEU A 336 ? 0.27980 0.25164 0.24528 -0.00062 -0.04624 0.06673  336 LEU A O   
2735 C  CB  . LEU A 336 ? 0.26087 0.24262 0.23347 -0.00965 -0.03721 0.05433  336 LEU A CB  
2736 C  CG  . LEU A 336 ? 0.25261 0.24472 0.22997 -0.00659 -0.03603 0.04708  336 LEU A CG  
2737 C  CD1 . LEU A 336 ? 0.24203 0.24533 0.21785 -0.01054 -0.03247 0.04456  336 LEU A CD1 
2738 C  CD2 . LEU A 336 ? 0.25040 0.23755 0.23360 -0.00462 -0.03502 0.04157  336 LEU A CD2 
2739 N  N   . PRO A 337 ? 0.31284 0.30750 0.27586 -0.00277 -0.04496 0.06215  337 PRO A N   
2740 C  CA  . PRO A 337 ? 0.30987 0.30611 0.27418 0.00309  -0.05039 0.06516  337 PRO A CA  
2741 C  C   . PRO A 337 ? 0.31333 0.30737 0.28808 0.00939  -0.05087 0.06126  337 PRO A C   
2742 O  O   . PRO A 337 ? 0.30999 0.30557 0.29014 0.00900  -0.04734 0.05453  337 PRO A O   
2743 C  CB  . PRO A 337 ? 0.30368 0.31356 0.26451 0.00157  -0.05183 0.06285  337 PRO A CB  
2744 C  CG  . PRO A 337 ? 0.30499 0.31742 0.25883 -0.00477 -0.04673 0.06070  337 PRO A CG  
2745 C  CD  . PRO A 337 ? 0.30143 0.30752 0.26116 -0.00645 -0.04209 0.05800  337 PRO A CD  
2746 N  N   . GLY A 338 ? 0.28472 0.27535 0.26208 0.01573  -0.05504 0.06600  338 GLY A N   
2747 C  CA  . GLY A 338 ? 0.28441 0.27210 0.27127 0.02293  -0.05451 0.06316  338 GLY A CA  
2748 C  C   . GLY A 338 ? 0.27367 0.27570 0.26955 0.02459  -0.05349 0.05713  338 GLY A C   
2749 O  O   . GLY A 338 ? 0.27331 0.27378 0.27627 0.02868  -0.05046 0.05280  338 GLY A O   
2750 N  N   . PHE A 339 ? 0.25145 0.26681 0.24634 0.02116  -0.05594 0.05676  339 PHE A N   
2751 C  CA  . PHE A 339 ? 0.24469 0.27312 0.24857 0.02170  -0.05557 0.05150  339 PHE A CA  
2752 C  C   . PHE A 339 ? 0.24034 0.26837 0.24503 0.01785  -0.04977 0.04387  339 PHE A C   
2753 O  O   . PHE A 339 ? 0.23268 0.26945 0.24517 0.01829  -0.04861 0.03953  339 PHE A O   
2754 C  CB  . PHE A 339 ? 0.24484 0.28584 0.24626 0.01841  -0.06084 0.05283  339 PHE A CB  
2755 C  CG  . PHE A 339 ? 0.24393 0.28338 0.23165 0.01135  -0.06031 0.05237  339 PHE A CG  
2756 C  CD1 . PHE A 339 ? 0.23641 0.27624 0.22131 0.00639  -0.05521 0.04575  339 PHE A CD1 
2757 C  CD2 . PHE A 339 ? 0.25078 0.28883 0.22827 0.01020  -0.06468 0.05892  339 PHE A CD2 
2758 C  CE1 . PHE A 339 ? 0.24315 0.28220 0.21601 0.00100  -0.05365 0.04534  339 PHE A CE1 
2759 C  CE2 . PHE A 339 ? 0.25223 0.28929 0.21624 0.00421  -0.06308 0.05859  339 PHE A CE2 
2760 C  CZ  . PHE A 339 ? 0.24520 0.28301 0.20728 -0.00011 -0.05718 0.05160  339 PHE A CZ  
2761 N  N   . TYR A 340 ? 0.23125 0.24995 0.22889 0.01392  -0.04638 0.04278  340 TYR A N   
2762 C  CA  . TYR A 340 ? 0.22828 0.24596 0.22779 0.01132  -0.04144 0.03637  340 TYR A CA  
2763 C  C   . TYR A 340 ? 0.23516 0.24767 0.24122 0.01656  -0.03915 0.03388  340 TYR A C   
2764 O  O   . TYR A 340 ? 0.22936 0.24513 0.23941 0.01602  -0.03592 0.02867  340 TYR A O   
2765 C  CB  . TYR A 340 ? 0.22830 0.23850 0.22061 0.00608  -0.03898 0.03682  340 TYR A CB  
2766 C  CG  . TYR A 340 ? 0.22561 0.24323 0.21282 0.00063  -0.03767 0.03552  340 TYR A CG  
2767 C  CD1 . TYR A 340 ? 0.23276 0.25361 0.21261 -0.00101 -0.04024 0.03979  340 TYR A CD1 
2768 C  CD2 . TYR A 340 ? 0.21899 0.23968 0.20781 -0.00234 -0.03369 0.03008  340 TYR A CD2 
2769 C  CE1 . TYR A 340 ? 0.22544 0.25184 0.19866 -0.00531 -0.03821 0.03799  340 TYR A CE1 
2770 C  CE2 . TYR A 340 ? 0.21399 0.24038 0.19781 -0.00618 -0.03170 0.02852  340 TYR A CE2 
2771 C  CZ  . TYR A 340 ? 0.21796 0.24691 0.19349 -0.00758 -0.03364 0.03214  340 TYR A CZ  
2772 O  OH  . TYR A 340 ? 0.22095 0.25435 0.18955 -0.01078 -0.03088 0.03003  340 TYR A OH  
2773 N  N   . TRP A 341 ? 0.28657 0.29015 0.29284 0.02196  -0.04048 0.03759  341 TRP A N   
2774 C  CA  . TRP A 341 ? 0.29082 0.28806 0.30143 0.02815  -0.03772 0.03512  341 TRP A CA  
2775 C  C   . TRP A 341 ? 0.28691 0.29439 0.30780 0.03512  -0.03837 0.03642  341 TRP A C   
2776 O  O   . TRP A 341 ? 0.28963 0.29911 0.31631 0.03903  -0.03446 0.03288  341 TRP A O   
2777 C  CB  . TRP A 341 ? 0.30945 0.28851 0.31377 0.03068  -0.03821 0.03771  341 TRP A CB  
2778 C  CG  . TRP A 341 ? 0.31057 0.28009 0.30667 0.02331  -0.03805 0.03741  341 TRP A CG  
2779 C  CD1 . TRP A 341 ? 0.31096 0.27501 0.30112 0.01911  -0.04067 0.04278  341 TRP A CD1 
2780 C  CD2 . TRP A 341 ? 0.30555 0.27101 0.29940 0.01906  -0.03524 0.03219  341 TRP A CD2 
2781 N  NE1 . TRP A 341 ? 0.30924 0.26720 0.29511 0.01231  -0.03940 0.04131  341 TRP A NE1 
2782 C  CE2 . TRP A 341 ? 0.30416 0.26296 0.29234 0.01226  -0.03654 0.03480  341 TRP A CE2 
2783 C  CE3 . TRP A 341 ? 0.30791 0.27520 0.30412 0.02021  -0.03191 0.02620  341 TRP A CE3 
2784 C  CZ2 . TRP A 341 ? 0.30459 0.25963 0.29083 0.00671  -0.03525 0.03161  341 TRP A CZ2 
2785 C  CZ3 . TRP A 341 ? 0.30249 0.26466 0.29492 0.01489  -0.03085 0.02296  341 TRP A CZ3 
2786 C  CH2 . TRP A 341 ? 0.30403 0.26065 0.29222 0.00827  -0.03283 0.02566  341 TRP A CH2 
2787 N  N   . THR A 342 ? 0.33733 0.35213 0.36088 0.03670  -0.04326 0.04191  342 THR A N   
2788 C  CA  . THR A 342 ? 0.34048 0.36652 0.37590 0.04353  -0.04482 0.04453  342 THR A CA  
2789 C  C   . THR A 342 ? 0.32904 0.37375 0.37177 0.03951  -0.04722 0.04347  342 THR A C   
2790 O  O   . THR A 342 ? 0.31441 0.37103 0.36980 0.04395  -0.04742 0.04455  342 THR A O   
2791 C  CB  . THR A 342 ? 0.33821 0.36088 0.37343 0.04874  -0.04991 0.05227  342 THR A CB  
2792 O  OG1 . THR A 342 ? 0.33800 0.36744 0.36804 0.04293  -0.05574 0.05595  342 THR A OG1 
2793 C  CG2 . THR A 342 ? 0.35084 0.35239 0.37681 0.05108  -0.04846 0.05368  342 THR A CG2 
2794 N  N   . GLY A 343 ? 0.30604 0.35339 0.34137 0.03126  -0.04891 0.04146  343 GLY A N   
2795 C  CA  . GLY A 343 ? 0.29523 0.35757 0.33526 0.02690  -0.05219 0.04022  343 GLY A CA  
2796 C  C   . GLY A 343 ? 0.30394 0.37620 0.34766 0.02842  -0.05985 0.04630  343 GLY A C   
2797 O  O   . GLY A 343 ? 0.29784 0.38330 0.34718 0.02501  -0.06369 0.04555  343 GLY A O   
2798 N  N   . GLN A 344 ? 0.37575 0.44151 0.41621 0.03310  -0.06281 0.05259  344 GLN A N   
2799 C  CA  . GLN A 344 ? 0.38290 0.45784 0.42697 0.03547  -0.07089 0.05959  344 GLN A CA  
2800 C  C   . GLN A 344 ? 0.38251 0.45625 0.41150 0.02838  -0.07595 0.06118  344 GLN A C   
2801 O  O   . GLN A 344 ? 0.39442 0.45963 0.41370 0.02928  -0.07840 0.06672  344 GLN A O   
2802 C  CB  . GLN A 344 ? 0.38824 0.45595 0.43631 0.04494  -0.07152 0.06615  344 GLN A CB  
2803 C  CG  . GLN A 344 ? 0.38341 0.45451 0.44681 0.05343  -0.06673 0.06516  344 GLN A CG  
2804 C  CD  . GLN A 344 ? 0.38876 0.48094 0.46810 0.05308  -0.06878 0.06474  344 GLN A CD  
2805 O  OE1 . GLN A 344 ? 0.38923 0.49449 0.47521 0.05339  -0.07658 0.07026  344 GLN A OE1 
2806 N  NE2 . GLN A 344 ? 0.37647 0.47221 0.46202 0.05186  -0.06224 0.05865  344 GLN A NE2 
2807 N  N   . THR A 345 ? 0.26615 0.34784 0.29244 0.02121  -0.07718 0.05617  345 THR A N   
2808 C  CA  . THR A 345 ? 0.27154 0.35271 0.28229 0.01449  -0.08130 0.05628  345 THR A CA  
2809 C  C   . THR A 345 ? 0.26961 0.36453 0.28375 0.00988  -0.08775 0.05412  345 THR A C   
2810 O  O   . THR A 345 ? 0.26390 0.36665 0.29026 0.00900  -0.08624 0.04985  345 THR A O   
2811 C  CB  . THR A 345 ? 0.28183 0.35305 0.28016 0.00918  -0.07439 0.05052  345 THR A CB  
2812 O  OG1 . THR A 345 ? 0.28587 0.35851 0.26972 0.00293  -0.07750 0.04923  345 THR A OG1 
2813 C  CG2 . THR A 345 ? 0.26685 0.33953 0.27342 0.00783  -0.06832 0.04286  345 THR A CG2 
2814 N  N   . ASP A 346 ? 0.44817 0.54535 0.45053 0.00641  -0.09520 0.05730  346 ASP A N   
2815 C  CA  . ASP A 346 ? 0.44404 0.55230 0.44619 0.00067  -0.10281 0.05500  346 ASP A CA  
2816 C  C   . ASP A 346 ? 0.44455 0.54834 0.43543 -0.00693 -0.09905 0.04573  346 ASP A C   
2817 O  O   . ASP A 346 ? 0.45286 0.56305 0.44145 -0.01269 -0.10513 0.04245  346 ASP A O   
2818 C  CB  . ASP A 346 ? 0.45229 0.56361 0.44377 -0.00021 -0.11303 0.06187  346 ASP A CB  
2819 C  CG  . ASP A 346 ? 0.46316 0.58557 0.47122 0.00632  -0.12033 0.07057  346 ASP A CG  
2820 O  OD1 . ASP A 346 ? 0.45710 0.58734 0.48571 0.01065  -0.11776 0.07029  346 ASP A OD1 
2821 O  OD2 . ASP A 346 ? 0.48438 0.60800 0.48493 0.00750  -0.12840 0.07806  346 ASP A OD2 
2822 N  N   . MET A 347 ? 0.32765 0.42038 0.31174 -0.00706 -0.08961 0.04159  347 MET A N   
2823 C  CA  . MET A 347 ? 0.33679 0.42503 0.31260 -0.01271 -0.08487 0.03290  347 MET A CA  
2824 C  C   . MET A 347 ? 0.32582 0.41894 0.31806 -0.01288 -0.08184 0.02819  347 MET A C   
2825 O  O   . MET A 347 ? 0.31932 0.40961 0.32101 -0.00873 -0.07524 0.02816  347 MET A O   
2826 C  CB  . MET A 347 ? 0.34519 0.42185 0.31009 -0.01232 -0.07609 0.03137  347 MET A CB  
2827 C  CG  . MET A 347 ? 0.34946 0.42082 0.30136 -0.01110 -0.07705 0.03800  347 MET A CG  
2828 S  SD  . MET A 347 ? 0.36987 0.43160 0.30458 -0.01445 -0.06811 0.03417  347 MET A SD  
2829 C  CE  . MET A 347 ? 0.35731 0.41189 0.29469 -0.01053 -0.06365 0.04182  347 MET A CE  
2830 N  N   . ALA A 348 ? 0.27738 0.37709 0.27214 -0.01812 -0.08685 0.02436  348 ALA A N   
2831 C  CA  . ALA A 348 ? 0.27209 0.37739 0.28312 -0.01898 -0.08443 0.02104  348 ALA A CA  
2832 C  C   . ALA A 348 ? 0.26864 0.36422 0.27751 -0.01899 -0.07444 0.01515  348 ALA A C   
2833 O  O   . ALA A 348 ? 0.26424 0.36138 0.28609 -0.01603 -0.06935 0.01500  348 ALA A O   
2834 C  CB  . ALA A 348 ? 0.26746 0.37985 0.27968 -0.02626 -0.09221 0.01796  348 ALA A CB  
2835 N  N   . CYS A 349 ? 0.25235 0.33816 0.24473 -0.02188 -0.07137 0.01057  349 CYS A N   
2836 C  CA  . CYS A 349 ? 0.25090 0.32845 0.24192 -0.02170 -0.06252 0.00546  349 CYS A CA  
2837 C  C   . CYS A 349 ? 0.25145 0.32570 0.24804 -0.01598 -0.05644 0.00894  349 CYS A C   
2838 O  O   . CYS A 349 ? 0.24299 0.31557 0.24803 -0.01444 -0.05117 0.00699  349 CYS A O   
2839 C  CB  . CYS A 349 ? 0.25758 0.32642 0.23031 -0.02475 -0.06010 0.00070  349 CYS A CB  
2840 S  SG  . CYS A 349 ? 0.27809 0.34407 0.23464 -0.02328 -0.06141 0.00583  349 CYS A SG  
2841 N  N   . VAL A 350 ? 0.22890 0.30113 0.21977 -0.01317 -0.05748 0.01426  350 VAL A N   
2842 C  CA  . VAL A 350 ? 0.21829 0.28542 0.21311 -0.00852 -0.05267 0.01750  350 VAL A CA  
2843 C  C   . VAL A 350 ? 0.21910 0.29098 0.22914 -0.00393 -0.05330 0.02011  350 VAL A C   
2844 O  O   . VAL A 350 ? 0.21442 0.28202 0.23000 -0.00112 -0.04803 0.01915  350 VAL A O   
2845 C  CB  . VAL A 350 ? 0.22725 0.29002 0.21183 -0.00736 -0.05403 0.02312  350 VAL A CB  
2846 C  CG1 . VAL A 350 ? 0.22516 0.28104 0.21372 -0.00340 -0.04999 0.02645  350 VAL A CG1 
2847 C  CG2 . VAL A 350 ? 0.23326 0.29203 0.20252 -0.01145 -0.05172 0.02061  350 VAL A CG2 
2848 N  N   . ALA A 351 ? 0.20394 0.28509 0.22079 -0.00290 -0.05969 0.02356  351 ALA A N   
2849 C  CA  . ALA A 351 ? 0.20148 0.28872 0.23386 0.00250  -0.05951 0.02658  351 ALA A CA  
2850 C  C   . ALA A 351 ? 0.19149 0.28140 0.23341 0.00149  -0.05464 0.02195  351 ALA A C   
2851 O  O   . ALA A 351 ? 0.19270 0.28162 0.24281 0.00643  -0.04999 0.02267  351 ALA A O   
2852 C  CB  . ALA A 351 ? 0.20087 0.30015 0.24061 0.00343  -0.06775 0.03163  351 ALA A CB  
2853 N  N   . ASP A 352 ? 0.22215 0.31417 0.26186 -0.00484 -0.05546 0.01717  352 ASP A N   
2854 C  CA  . ASP A 352 ? 0.21994 0.31366 0.26805 -0.00640 -0.05100 0.01343  352 ASP A CA  
2855 C  C   . ASP A 352 ? 0.21928 0.30203 0.26239 -0.00485 -0.04339 0.01036  352 ASP A C   
2856 O  O   . ASP A 352 ? 0.21672 0.29968 0.26730 -0.00300 -0.03872 0.00948  352 ASP A O   
2857 C  CB  . ASP A 352 ? 0.21969 0.31616 0.26572 -0.01393 -0.05444 0.00919  352 ASP A CB  
2858 C  CG  . ASP A 352 ? 0.21308 0.31479 0.27152 -0.01606 -0.05188 0.00756  352 ASP A CG  
2859 O  OD1 . ASP A 352 ? 0.20733 0.31801 0.27973 -0.01235 -0.05085 0.01150  352 ASP A OD1 
2860 O  OD2 . ASP A 352 ? 0.22352 0.32006 0.27768 -0.02116 -0.05047 0.00261  352 ASP A OD2 
2861 N  N   . THR A 353 ? 0.21992 0.29379 0.25063 -0.00571 -0.04213 0.00915  353 THR A N   
2862 C  CA  . THR A 353 ? 0.21757 0.28238 0.24469 -0.00463 -0.03597 0.00694  353 THR A CA  
2863 C  C   . THR A 353 ? 0.22230 0.28342 0.25309 0.00101  -0.03365 0.01010  353 THR A C   
2864 O  O   . THR A 353 ? 0.21989 0.27723 0.25348 0.00265  -0.02924 0.00842  353 THR A O   
2865 C  CB  . THR A 353 ? 0.22924 0.28771 0.24413 -0.00703 -0.03512 0.00572  353 THR A CB  
2866 O  OG1 . THR A 353 ? 0.24128 0.30092 0.25115 -0.01158 -0.03625 0.00158  353 THR A OG1 
2867 C  CG2 . THR A 353 ? 0.22404 0.27499 0.23731 -0.00610 -0.02967 0.00442  353 THR A CG2 
2868 N  N   . VAL A 354 ? 0.18550 0.24642 0.21514 0.00413  -0.03679 0.01469  354 VAL A N   
2869 C  CA  . VAL A 354 ? 0.18670 0.24198 0.21885 0.00997  -0.03489 0.01741  354 VAL A CA  
2870 C  C   . VAL A 354 ? 0.18372 0.24515 0.22737 0.01409  -0.03282 0.01739  354 VAL A C   
2871 O  O   . VAL A 354 ? 0.19236 0.24753 0.23685 0.01815  -0.02851 0.01667  354 VAL A O   
2872 C  CB  . VAL A 354 ? 0.19612 0.24931 0.22481 0.01264  -0.03910 0.02291  354 VAL A CB  
2873 C  CG1 . VAL A 354 ? 0.20299 0.24845 0.23408 0.01933  -0.03727 0.02543  354 VAL A CG1 
2874 C  CG2 . VAL A 354 ? 0.19878 0.24588 0.21565 0.00836  -0.03980 0.02351  354 VAL A CG2 
2875 N  N   . ARG A 355 ? 0.28010 0.35397 0.33243 0.01281  -0.03577 0.01825  355 ARG A N   
2876 C  CA  . ARG A 355 ? 0.27549 0.35782 0.34072 0.01624  -0.03314 0.01900  355 ARG A CA  
2877 C  C   . ARG A 355 ? 0.27435 0.35287 0.33931 0.01465  -0.02696 0.01478  355 ARG A C   
2878 O  O   . ARG A 355 ? 0.27600 0.35367 0.34534 0.01952  -0.02194 0.01504  355 ARG A O   
2879 C  CB  . ARG A 355 ? 0.27307 0.37059 0.34851 0.01318  -0.03838 0.02097  355 ARG A CB  
2880 C  CG  . ARG A 355 ? 0.25892 0.36816 0.35003 0.01543  -0.03539 0.02240  355 ARG A CG  
2881 C  CD  . ARG A 355 ? 0.26915 0.39225 0.36925 0.00894  -0.04103 0.02312  355 ARG A CD  
2882 N  NE  . ARG A 355 ? 0.27413 0.41132 0.39195 0.01068  -0.03856 0.02598  355 ARG A NE  
2883 C  CZ  . ARG A 355 ? 0.26343 0.41292 0.39495 0.01662  -0.04000 0.03165  355 ARG A CZ  
2884 N  NH1 . ARG A 355 ? 0.26438 0.41264 0.39344 0.02168  -0.04443 0.03522  355 ARG A NH1 
2885 N  NH2 . ARG A 355 ? 0.25902 0.42278 0.40778 0.01772  -0.03669 0.03439  355 ARG A NH2 
2886 N  N   . ALA A 356 ? 0.14471 0.22026 0.20372 0.00834  -0.02700 0.01102  356 ALA A N   
2887 C  CA  . ALA A 356 ? 0.14634 0.21740 0.20432 0.00686  -0.02175 0.00768  356 ALA A CA  
2888 C  C   . ALA A 356 ? 0.15479 0.21363 0.20465 0.01023  -0.01814 0.00675  356 ALA A C   
2889 O  O   . ALA A 356 ? 0.15614 0.21172 0.20635 0.01226  -0.01352 0.00564  356 ALA A O   
2890 C  CB  . ALA A 356 ? 0.14238 0.21213 0.19597 0.00011  -0.02295 0.00413  356 ALA A CB  
2891 N  N   . ALA A 357 ? 0.19134 0.24310 0.23327 0.01033  -0.02043 0.00744  357 ALA A N   
2892 C  CA  . ALA A 357 ? 0.20448 0.24436 0.23915 0.01256  -0.01825 0.00692  357 ALA A CA  
2893 C  C   . ALA A 357 ? 0.20958 0.24624 0.24641 0.01932  -0.01595 0.00834  357 ALA A C   
2894 O  O   . ALA A 357 ? 0.21553 0.24369 0.24770 0.02129  -0.01256 0.00645  357 ALA A O   
2895 C  CB  . ALA A 357 ? 0.20965 0.24381 0.23702 0.01070  -0.02133 0.00845  357 ALA A CB  
2896 N  N   . HIS A 358 ? 0.23971 0.28288 0.28316 0.02329  -0.01779 0.01167  358 HIS A N   
2897 C  CA  . HIS A 358 ? 0.24677 0.28683 0.29285 0.03114  -0.01493 0.01314  358 HIS A CA  
2898 C  C   . HIS A 358 ? 0.24411 0.29018 0.29666 0.03355  -0.00923 0.01175  358 HIS A C   
2899 O  O   . HIS A 358 ? 0.24744 0.28509 0.29546 0.03834  -0.00444 0.01019  358 HIS A O   
2900 C  CB  . HIS A 358 ? 0.24282 0.28968 0.29591 0.03532  -0.01869 0.01794  358 HIS A CB  
2901 C  CG  . HIS A 358 ? 0.25877 0.30268 0.31572 0.04475  -0.01538 0.01977  358 HIS A CG  
2902 N  ND1 . HIS A 358 ? 0.25585 0.31062 0.32416 0.04953  -0.01093 0.02053  358 HIS A ND1 
2903 C  CD2 . HIS A 358 ? 0.26294 0.29368 0.31386 0.05060  -0.01541 0.02105  358 HIS A CD2 
2904 C  CE1 . HIS A 358 ? 0.25056 0.29936 0.31955 0.05877  -0.00780 0.02194  358 HIS A CE1 
2905 N  NE2 . HIS A 358 ? 0.26876 0.30189 0.32676 0.05959  -0.01073 0.02203  358 HIS A NE2 
2906 N  N   . ASP A 359 ? 0.28921 0.34913 0.35144 0.02992  -0.00961 0.01234  359 ASP A N   
2907 C  CA  . ASP A 359 ? 0.28199 0.35008 0.35272 0.03197  -0.00403 0.01253  359 ASP A CA  
2908 C  C   . ASP A 359 ? 0.27929 0.34073 0.34287 0.02853  0.00016  0.00902  359 ASP A C   
2909 O  O   . ASP A 359 ? 0.27975 0.34094 0.34392 0.03216  0.00638  0.00879  359 ASP A O   
2910 C  CB  . ASP A 359 ? 0.26329 0.34907 0.34844 0.02849  -0.00683 0.01528  359 ASP A CB  
2911 C  CG  . ASP A 359 ? 0.26364 0.35910 0.35895 0.03353  -0.01023 0.01995  359 ASP A CG  
2912 O  OD1 . ASP A 359 ? 0.28234 0.36995 0.37366 0.04062  -0.00945 0.02110  359 ASP A OD1 
2913 O  OD2 . ASP A 359 ? 0.26186 0.37230 0.36914 0.03027  -0.01421 0.02266  359 ASP A OD2 
2914 N  N   . HIS A 360 ? 0.24097 0.29715 0.29758 0.02209  -0.00284 0.00663  360 HIS A N   
2915 C  CA  . HIS A 360 ? 0.24245 0.29370 0.29381 0.01866  0.00020  0.00412  360 HIS A CA  
2916 C  C   . HIS A 360 ? 0.25250 0.29039 0.29138 0.01705  -0.00126 0.00165  360 HIS A C   
2917 O  O   . HIS A 360 ? 0.24956 0.28286 0.28368 0.01473  0.00062  0.00003  360 HIS A O   
2918 C  CB  . HIS A 360 ? 0.22624 0.28560 0.28381 0.01199  -0.00149 0.00387  360 HIS A CB  
2919 C  CG  . HIS A 360 ? 0.21819 0.29201 0.28941 0.01152  -0.00188 0.00666  360 HIS A CG  
2920 N  ND1 . HIS A 360 ? 0.21501 0.29620 0.29446 0.01415  0.00350  0.00887  360 HIS A ND1 
2921 C  CD2 . HIS A 360 ? 0.21120 0.29420 0.28951 0.00838  -0.00728 0.00794  360 HIS A CD2 
2922 C  CE1 . HIS A 360 ? 0.21432 0.30983 0.30738 0.01241  0.00127  0.01176  360 HIS A CE1 
2923 N  NE2 . HIS A 360 ? 0.20493 0.30134 0.29701 0.00873  -0.00583 0.01108  360 HIS A NE2 
2924 N  N   . ALA A 361 ? 0.15907 0.19114 0.19324 0.01793  -0.00480 0.00198  361 ALA A N   
2925 C  CA  . ALA A 361 ? 0.17575 0.19728 0.20039 0.01531  -0.00683 0.00047  361 ALA A CA  
2926 C  C   . ALA A 361 ? 0.16977 0.19421 0.19485 0.00953  -0.00797 -0.00078 361 ALA A C   
2927 O  O   . ALA A 361 ? 0.16623 0.18463 0.18606 0.00755  -0.00781 -0.00205 361 ALA A O   
2928 C  CB  . ALA A 361 ? 0.18292 0.19314 0.19886 0.01789  -0.00431 -0.00118 361 ALA A CB  
2929 N  N   . TYR A 362 ? 0.16667 0.20010 0.19792 0.00702  -0.00943 -0.00041 362 TYR A N   
2930 C  CA  . TYR A 362 ? 0.15719 0.19226 0.18853 0.00234  -0.00990 -0.00214 362 TYR A CA  
2931 C  C   . TYR A 362 ? 0.14990 0.19125 0.18352 -0.00027 -0.01311 -0.00208 362 TYR A C   
2932 O  O   . TYR A 362 ? 0.15412 0.20206 0.19265 0.00074  -0.01491 -0.00044 362 TYR A O   
2933 C  CB  . TYR A 362 ? 0.15012 0.18736 0.18515 0.00120  -0.00685 -0.00293 362 TYR A CB  
2934 C  CG  . TYR A 362 ? 0.14577 0.18329 0.18119 -0.00317 -0.00739 -0.00478 362 TYR A CG  
2935 C  CD1 . TYR A 362 ? 0.15061 0.18183 0.18155 -0.00399 -0.00656 -0.00583 362 TYR A CD1 
2936 C  CD2 . TYR A 362 ? 0.14328 0.18682 0.18345 -0.00632 -0.00909 -0.00547 362 TYR A CD2 
2937 C  CE1 . TYR A 362 ? 0.14583 0.17616 0.17717 -0.00682 -0.00652 -0.00756 362 TYR A CE1 
2938 C  CE2 . TYR A 362 ? 0.14468 0.18587 0.18363 -0.00995 -0.00942 -0.00785 362 TYR A CE2 
2939 C  CZ  . TYR A 362 ? 0.14941 0.18369 0.18400 -0.00967 -0.00769 -0.00891 362 TYR A CZ  
2940 O  OH  . TYR A 362 ? 0.15225 0.18314 0.18573 -0.01217 -0.00751 -0.01131 362 TYR A OH  
2941 N  N   . ALA A 363 ? 0.19639 0.23574 0.22610 -0.00337 -0.01381 -0.00380 363 ALA A N   
2942 C  CA  . ALA A 363 ? 0.19846 0.24181 0.22750 -0.00645 -0.01617 -0.00506 363 ALA A CA  
2943 C  C   . ALA A 363 ? 0.19618 0.23548 0.22178 -0.00871 -0.01434 -0.00794 363 ALA A C   
2944 O  O   . ALA A 363 ? 0.20109 0.23611 0.22414 -0.00774 -0.01260 -0.00765 363 ALA A O   
2945 C  CB  . ALA A 363 ? 0.19743 0.24180 0.22226 -0.00597 -0.01911 -0.00308 363 ALA A CB  
2946 N  N   . HIS A 364 ? 0.21216 0.25254 0.23812 -0.01167 -0.01495 -0.01059 364 HIS A N   
2947 C  CA  . HIS A 364 ? 0.22198 0.25707 0.24501 -0.01265 -0.01255 -0.01342 364 HIS A CA  
2948 C  C   . HIS A 364 ? 0.22993 0.26365 0.24617 -0.01237 -0.01208 -0.01437 364 HIS A C   
2949 O  O   . HIS A 364 ? 0.22566 0.26215 0.23856 -0.01224 -0.01397 -0.01274 364 HIS A O   
2950 C  CB  . HIS A 364 ? 0.22634 0.26016 0.25104 -0.01595 -0.01303 -0.01628 364 HIS A CB  
2951 C  CG  . HIS A 364 ? 0.23013 0.26752 0.25321 -0.01922 -0.01712 -0.01776 364 HIS A CG  
2952 N  ND1 . HIS A 364 ? 0.23840 0.27335 0.25276 -0.02038 -0.01836 -0.02060 364 HIS A ND1 
2953 C  CD2 . HIS A 364 ? 0.22273 0.26633 0.25172 -0.02181 -0.02050 -0.01663 364 HIS A CD2 
2954 C  CE1 . HIS A 364 ? 0.24156 0.28012 0.25512 -0.02386 -0.02316 -0.02140 364 HIS A CE1 
2955 N  NE2 . HIS A 364 ? 0.23189 0.27650 0.25546 -0.02491 -0.02481 -0.01877 364 HIS A NE2 
2956 N  N   . HIS A 365 ? 0.21649 0.24599 0.23090 -0.01191 -0.00908 -0.01656 365 HIS A N   
2957 C  CA  . HIS A 365 ? 0.21549 0.24484 0.22585 -0.01045 -0.00671 -0.01629 365 HIS A CA  
2958 C  C   . HIS A 365 ? 0.22799 0.25887 0.23045 -0.01169 -0.00775 -0.01748 365 HIS A C   
2959 O  O   . HIS A 365 ? 0.22684 0.26038 0.22650 -0.01112 -0.00743 -0.01465 365 HIS A O   
2960 C  CB  . HIS A 365 ? 0.21905 0.24429 0.23015 -0.00887 -0.00297 -0.01852 365 HIS A CB  
2961 C  CG  . HIS A 365 ? 0.22486 0.25193 0.23421 -0.00679 0.00050  -0.01769 365 HIS A CG  
2962 N  ND1 . HIS A 365 ? 0.21660 0.24763 0.23030 -0.00590 0.00091  -0.01335 365 HIS A ND1 
2963 C  CD2 . HIS A 365 ? 0.23278 0.25853 0.23662 -0.00553 0.00404  -0.02049 365 HIS A CD2 
2964 C  CE1 . HIS A 365 ? 0.21693 0.25072 0.22975 -0.00444 0.00467  -0.01281 365 HIS A CE1 
2965 N  NE2 . HIS A 365 ? 0.22733 0.25798 0.23378 -0.00364 0.00717  -0.01720 365 HIS A NE2 
2966 N  N   . ILE A 366 ? 0.25229 0.28084 0.25018 -0.01388 -0.00933 -0.02145 366 ILE A N   
2967 C  CA  . ILE A 366 ? 0.26755 0.29611 0.25504 -0.01511 -0.01033 -0.02321 366 ILE A CA  
2968 C  C   . ILE A 366 ? 0.25907 0.29326 0.24560 -0.01602 -0.01473 -0.01913 366 ILE A C   
2969 O  O   . ILE A 366 ? 0.26340 0.29852 0.24125 -0.01620 -0.01494 -0.01818 366 ILE A O   
2970 C  CB  . ILE A 366 ? 0.27738 0.30036 0.25878 -0.01795 -0.01205 -0.02899 366 ILE A CB  
2971 C  CG1 . ILE A 366 ? 0.29174 0.31106 0.25904 -0.01784 -0.01030 -0.03246 366 ILE A CG1 
2972 C  CG2 . ILE A 366 ? 0.26999 0.29656 0.25468 -0.02183 -0.01857 -0.02843 366 ILE A CG2 
2973 C  CD1 . ILE A 366 ? 0.30361 0.31948 0.26880 -0.01368 -0.00278 -0.03390 366 ILE A CD1 
2974 N  N   . GLN A 367 ? 0.30336 0.34113 0.29837 -0.01606 -0.01784 -0.01627 367 GLN A N   
2975 C  CA  . GLN A 367 ? 0.29832 0.34078 0.29361 -0.01557 -0.02161 -0.01178 367 GLN A CA  
2976 C  C   . GLN A 367 ? 0.29734 0.33911 0.29227 -0.01322 -0.01917 -0.00768 367 GLN A C   
2977 O  O   . GLN A 367 ? 0.30288 0.34583 0.29236 -0.01320 -0.02074 -0.00448 367 GLN A O   
2978 C  CB  . GLN A 367 ? 0.29114 0.33783 0.29635 -0.01524 -0.02462 -0.00991 367 GLN A CB  
2979 C  CG  . GLN A 367 ? 0.29808 0.34707 0.30612 -0.01867 -0.02770 -0.01280 367 GLN A CG  
2980 C  CD  . GLN A 367 ? 0.29605 0.35106 0.31610 -0.01797 -0.02908 -0.01017 367 GLN A CD  
2981 O  OE1 . GLN A 367 ? 0.29868 0.36082 0.32288 -0.01886 -0.03381 -0.00799 367 GLN A OE1 
2982 N  NE2 . GLN A 367 ? 0.28973 0.34249 0.31541 -0.01613 -0.02486 -0.00999 367 GLN A NE2 
2983 N  N   . ARG A 368 ? 0.21913 0.25868 0.21960 -0.01172 -0.01590 -0.00732 368 ARG A N   
2984 C  CA  . ARG A 368 ? 0.21683 0.25530 0.21738 -0.01069 -0.01419 -0.00359 368 ARG A CA  
2985 C  C   . ARG A 368 ? 0.22784 0.26706 0.22169 -0.01150 -0.01126 -0.00321 368 ARG A C   
2986 O  O   . ARG A 368 ? 0.22914 0.26890 0.22079 -0.01186 -0.01112 0.00107  368 ARG A O   
2987 C  CB  . ARG A 368 ? 0.20732 0.24339 0.21420 -0.00965 -0.01203 -0.00375 368 ARG A CB  
2988 C  CG  . ARG A 368 ? 0.20455 0.23927 0.21651 -0.00839 -0.01371 -0.00367 368 ARG A CG  
2989 C  CD  . ARG A 368 ? 0.20204 0.23316 0.21696 -0.00758 -0.01246 -0.00276 368 ARG A CD  
2990 N  NE  . ARG A 368 ? 0.20934 0.23897 0.22758 -0.00656 -0.01202 -0.00434 368 ARG A NE  
2991 C  CZ  . ARG A 368 ? 0.20920 0.23489 0.22823 -0.00558 -0.01176 -0.00364 368 ARG A CZ  
2992 N  NH1 . ARG A 368 ? 0.20312 0.22569 0.22064 -0.00597 -0.01271 -0.00166 368 ARG A NH1 
2993 N  NH2 . ARG A 368 ? 0.20861 0.23326 0.22942 -0.00466 -0.01071 -0.00474 368 ARG A NH2 
2994 N  N   . LEU A 369 ? 0.23257 0.27124 0.22273 -0.01169 -0.00848 -0.00750 369 LEU A N   
2995 C  CA  . LEU A 369 ? 0.24243 0.28196 0.22593 -0.01148 -0.00405 -0.00765 369 LEU A CA  
2996 C  C   . LEU A 369 ? 0.25191 0.29177 0.22354 -0.01289 -0.00586 -0.00773 369 LEU A C   
2997 O  O   . LEU A 369 ? 0.25473 0.29655 0.22135 -0.01329 -0.00459 -0.00357 369 LEU A O   
2998 C  CB  . LEU A 369 ? 0.24289 0.28008 0.22682 -0.00992 0.00042  -0.01257 369 LEU A CB  
2999 C  CG  . LEU A 369 ? 0.25054 0.28898 0.22864 -0.00829 0.00675  -0.01319 369 LEU A CG  
3000 C  CD1 . LEU A 369 ? 0.24262 0.28672 0.22820 -0.00771 0.00989  -0.00742 369 LEU A CD1 
3001 C  CD2 . LEU A 369 ? 0.25509 0.28900 0.23228 -0.00585 0.01071  -0.01900 369 LEU A CD2 
3002 N  N   . MET A 370 ? 0.27908 0.31693 0.24587 -0.01417 -0.00928 -0.01201 370 MET A N   
3003 C  CA  . MET A 370 ? 0.29074 0.32776 0.24383 -0.01582 -0.01121 -0.01351 370 MET A CA  
3004 C  C   . MET A 370 ? 0.29210 0.33225 0.24361 -0.01731 -0.01821 -0.00923 370 MET A C   
3005 O  O   . MET A 370 ? 0.29402 0.33411 0.23319 -0.01866 -0.02037 -0.00862 370 MET A O   
3006 C  CB  . MET A 370 ? 0.29265 0.32462 0.24018 -0.01720 -0.01204 -0.02088 370 MET A CB  
3007 C  CG  . MET A 370 ? 0.29979 0.32686 0.24391 -0.01486 -0.00464 -0.02555 370 MET A CG  
3008 S  SD  . MET A 370 ? 0.31600 0.34663 0.25685 -0.01170 0.00373  -0.02173 370 MET A SD  
3009 C  CE  . MET A 370 ? 0.33241 0.35989 0.25131 -0.01301 0.00386  -0.02427 370 MET A CE  
3010 N  N   . VAL A 371 ? 0.23998 0.28261 0.20294 -0.01662 -0.02167 -0.00611 371 VAL A N   
3011 C  CA  . VAL A 371 ? 0.23965 0.28563 0.20290 -0.01683 -0.02811 -0.00164 371 VAL A CA  
3012 C  C   . VAL A 371 ? 0.23838 0.28404 0.20380 -0.01493 -0.02720 0.00500  371 VAL A C   
3013 O  O   . VAL A 371 ? 0.24587 0.29117 0.20220 -0.01549 -0.02746 0.00885  371 VAL A O   
3014 C  CB  . VAL A 371 ? 0.23859 0.28789 0.21303 -0.01679 -0.03249 -0.00246 371 VAL A CB  
3015 C  CG1 . VAL A 371 ? 0.22403 0.27820 0.20018 -0.01608 -0.03910 0.00265  371 VAL A CG1 
3016 C  CG2 . VAL A 371 ? 0.22810 0.27664 0.20088 -0.01986 -0.03367 -0.00873 371 VAL A CG2 
3017 N  N   . THR A 372 ? 0.28252 0.32720 0.25880 -0.01298 -0.02619 0.00645  372 THR A N   
3018 C  CA  . THR A 372 ? 0.27434 0.31644 0.25240 -0.01159 -0.02625 0.01231  372 THR A CA  
3019 C  C   . THR A 372 ? 0.28096 0.32103 0.25584 -0.01296 -0.02110 0.01396  372 THR A C   
3020 O  O   . THR A 372 ? 0.28430 0.32251 0.25566 -0.01360 -0.02132 0.01951  372 THR A O   
3021 C  CB  . THR A 372 ? 0.26534 0.30545 0.25391 -0.00904 -0.02689 0.01257  372 THR A CB  
3022 O  OG1 . THR A 372 ? 0.26043 0.30045 0.25415 -0.00931 -0.02360 0.00778  372 THR A OG1 
3023 C  CG2 . THR A 372 ? 0.26498 0.30856 0.25790 -0.00687 -0.03179 0.01366  372 THR A CG2 
3024 N  N   . GLY A 373 ? 0.25630 0.29709 0.23332 -0.01343 -0.01645 0.00984  373 GLY A N   
3025 C  CA  . GLY A 373 ? 0.25326 0.29467 0.22965 -0.01451 -0.01129 0.01191  373 GLY A CA  
3026 C  C   . GLY A 373 ? 0.26954 0.31302 0.23454 -0.01569 -0.00876 0.01340  373 GLY A C   
3027 O  O   . GLY A 373 ? 0.26624 0.31037 0.22889 -0.01709 -0.00670 0.01895  373 GLY A O   
3028 N  N   . ASN A 374 ? 0.25473 0.29859 0.21158 -0.01550 -0.00889 0.00853  374 ASN A N   
3029 C  CA  . ASN A 374 ? 0.26460 0.30915 0.20727 -0.01641 -0.00664 0.00914  374 ASN A CA  
3030 C  C   . ASN A 374 ? 0.26137 0.30560 0.19755 -0.01762 -0.01102 0.01597  374 ASN A C   
3031 O  O   . ASN A 374 ? 0.26719 0.31223 0.19510 -0.01871 -0.00762 0.02046  374 ASN A O   
3032 C  CB  . ASN A 374 ? 0.26203 0.30467 0.19581 -0.01648 -0.00792 0.00191  374 ASN A CB  
3033 C  CG  . ASN A 374 ? 0.27701 0.31875 0.19270 -0.01747 -0.00675 0.00179  374 ASN A CG  
3034 O  OD1 . ASN A 374 ? 0.28299 0.32604 0.19286 -0.01697 0.00003  0.00412  374 ASN A OD1 
3035 N  ND2 . ASN A 374 ? 0.28182 0.32179 0.18832 -0.01908 -0.01340 -0.00069 374 ASN A ND2 
3036 N  N   . LEU A 375 ? 0.26733 0.31060 0.20775 -0.01712 -0.01819 0.01746  375 LEU A N   
3037 C  CA  . LEU A 375 ? 0.28082 0.32319 0.21566 -0.01741 -0.02308 0.02432  375 LEU A CA  
3038 C  C   . LEU A 375 ? 0.27908 0.31893 0.21730 -0.01802 -0.02059 0.03146  375 LEU A C   
3039 O  O   . LEU A 375 ? 0.28031 0.31922 0.20942 -0.01941 -0.02039 0.03758  375 LEU A O   
3040 C  CB  . LEU A 375 ? 0.27054 0.31344 0.21220 -0.01565 -0.03069 0.02454  375 LEU A CB  
3041 C  CG  . LEU A 375 ? 0.27707 0.31889 0.21518 -0.01470 -0.03655 0.03213  375 LEU A CG  
3042 C  CD1 . LEU A 375 ? 0.27618 0.31978 0.19847 -0.01656 -0.03959 0.03348  375 LEU A CD1 
3043 C  CD2 . LEU A 375 ? 0.26512 0.30836 0.21461 -0.01153 -0.04238 0.03273  375 LEU A CD2 
3044 N  N   . ALA A 376 ? 0.29853 0.33663 0.24906 -0.01750 -0.01906 0.03101  376 ALA A N   
3045 C  CA  . ALA A 376 ? 0.30029 0.33489 0.25438 -0.01916 -0.01753 0.03737  376 ALA A CA  
3046 C  C   . ALA A 376 ? 0.30376 0.34205 0.25295 -0.02203 -0.01087 0.04018  376 ALA A C   
3047 O  O   . ALA A 376 ? 0.31550 0.35187 0.26217 -0.02452 -0.01009 0.04753  376 ALA A O   
3048 C  CB  . ALA A 376 ? 0.28649 0.31818 0.25303 -0.01858 -0.01755 0.03522  376 ALA A CB  
3049 N  N   . MET A 377 ? 0.30450 0.34794 0.25263 -0.02152 -0.00558 0.03471  377 MET A N   
3050 C  CA  . MET A 377 ? 0.30292 0.35127 0.24608 -0.02306 0.00202  0.03702  377 MET A CA  
3051 C  C   . MET A 377 ? 0.32215 0.37010 0.24883 -0.02394 0.00211  0.04085  377 MET A C   
3052 O  O   . MET A 377 ? 0.32370 0.37298 0.24661 -0.02643 0.00566  0.04812  377 MET A O   
3053 C  CB  . MET A 377 ? 0.30172 0.35422 0.24649 -0.02085 0.00764  0.02958  377 MET A CB  
3054 C  CG  . MET A 377 ? 0.31336 0.37129 0.25101 -0.02082 0.01657  0.03076  377 MET A CG  
3055 S  SD  . MET A 377 ? 0.30895 0.37242 0.25640 -0.01763 0.02453  0.02490  377 MET A SD  
3056 C  CE  . MET A 377 ? 0.31174 0.36947 0.24574 -0.01445 0.02355  0.01464  377 MET A CE  
3057 N  N   . LEU A 378 ? 0.29587 0.34211 0.21226 -0.02240 -0.00207 0.03640  378 LEU A N   
3058 C  CA  . LEU A 378 ? 0.30473 0.35022 0.20319 -0.02330 -0.00297 0.03954  378 LEU A CA  
3059 C  C   . LEU A 378 ? 0.30974 0.35188 0.20659 -0.02487 -0.00776 0.04927  378 LEU A C   
3060 O  O   . LEU A 378 ? 0.31690 0.35892 0.20126 -0.02664 -0.00557 0.05552  378 LEU A O   
3061 C  CB  . LEU A 378 ? 0.30552 0.34954 0.19479 -0.02215 -0.00874 0.03286  378 LEU A CB  
3062 C  CG  . LEU A 378 ? 0.31416 0.35862 0.20207 -0.02085 -0.00503 0.02278  378 LEU A CG  
3063 C  CD1 . LEU A 378 ? 0.31498 0.35706 0.19362 -0.02126 -0.01257 0.01731  378 LEU A CD1 
3064 C  CD2 . LEU A 378 ? 0.32153 0.36757 0.19946 -0.02036 0.00520  0.02145  378 LEU A CD2 
3065 N  N   . LEU A 379 ? 0.29937 0.33788 0.20796 -0.02392 -0.01395 0.05085  379 LEU A N   
3066 C  CA  . LEU A 379 ? 0.30539 0.33853 0.21309 -0.02459 -0.01866 0.05987  379 LEU A CA  
3067 C  C   . LEU A 379 ? 0.30650 0.33784 0.21841 -0.02801 -0.01362 0.06693  379 LEU A C   
3068 O  O   . LEU A 379 ? 0.32121 0.34752 0.22816 -0.02965 -0.01581 0.07567  379 LEU A O   
3069 C  CB  . LEU A 379 ? 0.29450 0.32344 0.21330 -0.02156 -0.02587 0.05880  379 LEU A CB  
3070 C  CG  . LEU A 379 ? 0.29762 0.32894 0.21402 -0.01864 -0.03276 0.05508  379 LEU A CG  
3071 C  CD1 . LEU A 379 ? 0.28667 0.31588 0.21734 -0.01516 -0.03702 0.05305  379 LEU A CD1 
3072 C  CD2 . LEU A 379 ? 0.30576 0.33598 0.20924 -0.01862 -0.03815 0.06199  379 LEU A CD2 
3073 N  N   . GLY A 380 ? 0.29444 0.32988 0.21592 -0.02940 -0.00738 0.06394  380 GLY A N   
3074 C  CA  . GLY A 380 ? 0.28949 0.32457 0.21763 -0.03357 -0.00345 0.07079  380 GLY A CA  
3075 C  C   . GLY A 380 ? 0.29658 0.32330 0.23611 -0.03449 -0.00872 0.07299  380 GLY A C   
3076 O  O   . GLY A 380 ? 0.29801 0.32005 0.23933 -0.03860 -0.00870 0.08084  380 GLY A O   
3077 N  N   . VAL A 381 ? 0.26176 0.28561 0.20821 -0.03094 -0.01310 0.06627  381 VAL A N   
3078 C  CA  . VAL A 381 ? 0.26176 0.27638 0.21714 -0.03110 -0.01754 0.06706  381 VAL A CA  
3079 C  C   . VAL A 381 ? 0.26047 0.27694 0.22589 -0.03561 -0.01403 0.06768  381 VAL A C   
3080 O  O   . VAL A 381 ? 0.25015 0.27606 0.22041 -0.03584 -0.00919 0.06351  381 VAL A O   
3081 C  CB  . VAL A 381 ? 0.25934 0.27207 0.21906 -0.02588 -0.02165 0.05954  381 VAL A CB  
3082 C  CG1 . VAL A 381 ? 0.26073 0.26275 0.22753 -0.02536 -0.02536 0.05959  381 VAL A CG1 
3083 C  CG2 . VAL A 381 ? 0.25511 0.26822 0.20711 -0.02195 -0.02584 0.05973  381 VAL A CG2 
3084 N  N   . HIS A 382 ? 0.30170 0.30879 0.27044 -0.03927 -0.01690 0.07312  382 HIS A N   
3085 C  CA  . HIS A 382 ? 0.29138 0.29985 0.27027 -0.04470 -0.01529 0.07446  382 HIS A CA  
3086 C  C   . HIS A 382 ? 0.28021 0.29191 0.26730 -0.04219 -0.01568 0.06591  382 HIS A C   
3087 O  O   . HIS A 382 ? 0.28439 0.28940 0.27040 -0.03761 -0.01964 0.06057  382 HIS A O   
3088 C  CB  . HIS A 382 ? 0.29463 0.28864 0.27441 -0.04894 -0.02031 0.08021  382 HIS A CB  
3089 C  CG  . HIS A 382 ? 0.29427 0.29014 0.28380 -0.05660 -0.01946 0.08370  382 HIS A CG  
3090 N  ND1 . HIS A 382 ? 0.29586 0.29446 0.29482 -0.05751 -0.02057 0.07826  382 HIS A ND1 
3091 C  CD2 . HIS A 382 ? 0.29894 0.29496 0.29082 -0.06421 -0.01807 0.09270  382 HIS A CD2 
3092 C  CE1 . HIS A 382 ? 0.28665 0.28764 0.29394 -0.06539 -0.02052 0.08359  382 HIS A CE1 
3093 N  NE2 . HIS A 382 ? 0.29466 0.29438 0.29846 -0.06981 -0.01877 0.09244  382 HIS A NE2 
3094 N  N   . PRO A 383 ? 0.22076 0.24308 0.21637 -0.04468 -0.01145 0.06492  383 PRO A N   
3095 C  CA  . PRO A 383 ? 0.21385 0.23941 0.21640 -0.04189 -0.01188 0.05733  383 PRO A CA  
3096 C  C   . PRO A 383 ? 0.21769 0.23153 0.22315 -0.04257 -0.01820 0.05499  383 PRO A C   
3097 O  O   . PRO A 383 ? 0.21454 0.22785 0.22180 -0.03884 -0.01942 0.04837  383 PRO A O   
3098 C  CB  . PRO A 383 ? 0.20366 0.24268 0.21591 -0.04496 -0.00644 0.05920  383 PRO A CB  
3099 C  CG  . PRO A 383 ? 0.21259 0.25379 0.22524 -0.05093 -0.00421 0.06840  383 PRO A CG  
3100 C  CD  . PRO A 383 ? 0.21732 0.25028 0.21695 -0.04956 -0.00555 0.07121  383 PRO A CD  
3101 N  N   . ASP A 384 ? 0.28095 0.28431 0.28583 -0.04734 -0.02212 0.06015  384 ASP A N   
3102 C  CA  . ASP A 384 ? 0.28922 0.27830 0.29342 -0.04738 -0.02818 0.05710  384 ASP A CA  
3103 C  C   . ASP A 384 ? 0.29891 0.27979 0.29577 -0.03980 -0.03002 0.05216  384 ASP A C   
3104 O  O   . ASP A 384 ? 0.29773 0.27338 0.29466 -0.03663 -0.03211 0.04624  384 ASP A O   
3105 C  CB  . ASP A 384 ? 0.30337 0.28028 0.30657 -0.05408 -0.03216 0.06360  384 ASP A CB  
3106 C  CG  . ASP A 384 ? 0.30450 0.28884 0.31780 -0.06261 -0.03204 0.06795  384 ASP A CG  
3107 O  OD1 . ASP A 384 ? 0.29845 0.29863 0.31998 -0.06246 -0.02816 0.06651  384 ASP A OD1 
3108 O  OD2 . ASP A 384 ? 0.31389 0.28822 0.32755 -0.06954 -0.03596 0.07321  384 ASP A OD2 
3109 N  N   . ALA A 385 ? 0.27561 0.25613 0.26632 -0.03680 -0.02925 0.05501  385 ALA A N   
3110 C  CA  . ALA A 385 ? 0.27676 0.25167 0.26274 -0.02958 -0.03126 0.05148  385 ALA A CA  
3111 C  C   . ALA A 385 ? 0.26951 0.25531 0.25788 -0.02503 -0.02876 0.04479  385 ALA A C   
3112 O  O   . ALA A 385 ? 0.27184 0.25403 0.26001 -0.01984 -0.03024 0.04030  385 ALA A O   
3113 C  CB  . ALA A 385 ? 0.27683 0.24925 0.25622 -0.02798 -0.03218 0.05737  385 ALA A CB  
3114 N  N   . VAL A 386 ? 0.22446 0.22310 0.21512 -0.02680 -0.02461 0.04417  386 VAL A N   
3115 C  CA  . VAL A 386 ? 0.21822 0.22536 0.21085 -0.02318 -0.02239 0.03776  386 VAL A CA  
3116 C  C   . VAL A 386 ? 0.21277 0.21839 0.21123 -0.02298 -0.02280 0.03300  386 VAL A C   
3117 O  O   . VAL A 386 ? 0.21105 0.21723 0.21031 -0.01905 -0.02293 0.02785  386 VAL A O   
3118 C  CB  . VAL A 386 ? 0.21764 0.23652 0.20946 -0.02456 -0.01748 0.03810  386 VAL A CB  
3119 C  CG1 . VAL A 386 ? 0.20122 0.22615 0.19341 -0.02090 -0.01583 0.03138  386 VAL A CG1 
3120 C  CG2 . VAL A 386 ? 0.21506 0.23448 0.19882 -0.02548 -0.01714 0.04359  386 VAL A CG2 
3121 N  N   . ASP A 387 ? 0.30951 0.31359 0.31214 -0.02764 -0.02332 0.03515  387 ASP A N   
3122 C  CA  . ASP A 387 ? 0.31183 0.31376 0.31864 -0.02789 -0.02482 0.03125  387 ASP A CA  
3123 C  C   . ASP A 387 ? 0.32179 0.31084 0.32386 -0.02469 -0.02841 0.02824  387 ASP A C   
3124 O  O   . ASP A 387 ? 0.31522 0.30345 0.31773 -0.02193 -0.02846 0.02340  387 ASP A O   
3125 C  CB  . ASP A 387 ? 0.31383 0.31680 0.32630 -0.03433 -0.02607 0.03506  387 ASP A CB  
3126 C  CG  . ASP A 387 ? 0.31106 0.32898 0.33138 -0.03567 -0.02159 0.03604  387 ASP A CG  
3127 O  OD1 . ASP A 387 ? 0.30897 0.33148 0.33621 -0.04100 -0.02185 0.04050  387 ASP A OD1 
3128 O  OD2 . ASP A 387 ? 0.30417 0.32912 0.32412 -0.03137 -0.01777 0.03248  387 ASP A OD2 
3129 N  N   . ASP A 388 ? 0.37575 0.35414 0.37280 -0.02460 -0.03098 0.03129  388 ASP A N   
3130 C  CA  . ASP A 388 ? 0.38848 0.35340 0.38049 -0.02054 -0.03357 0.02843  388 ASP A CA  
3131 C  C   . ASP A 388 ? 0.37880 0.34819 0.37074 -0.01347 -0.03150 0.02455  388 ASP A C   
3132 O  O   . ASP A 388 ? 0.38645 0.35042 0.37676 -0.00971 -0.03148 0.02031  388 ASP A O   
3133 C  CB  . ASP A 388 ? 0.39415 0.34600 0.38108 -0.02127 -0.03647 0.03301  388 ASP A CB  
3134 C  CG  . ASP A 388 ? 0.41801 0.35539 0.39927 -0.01530 -0.03813 0.02994  388 ASP A CG  
3135 O  OD1 . ASP A 388 ? 0.42799 0.35456 0.40567 -0.01616 -0.03998 0.02642  388 ASP A OD1 
3136 O  OD2 . ASP A 388 ? 0.43214 0.36921 0.41232 -0.00944 -0.03756 0.03108  388 ASP A OD2 
3137 N  N   . TRP A 389 ? 0.25016 0.22955 0.24352 -0.01192 -0.02979 0.02610  389 TRP A N   
3138 C  CA  . TRP A 389 ? 0.24971 0.23477 0.24456 -0.00637 -0.02862 0.02300  389 TRP A CA  
3139 C  C   . TRP A 389 ? 0.23794 0.22953 0.23649 -0.00611 -0.02621 0.01788  389 TRP A C   
3140 O  O   . TRP A 389 ? 0.24215 0.23231 0.24154 -0.00213 -0.02548 0.01462  389 TRP A O   
3141 C  CB  . TRP A 389 ? 0.24272 0.23662 0.23713 -0.00601 -0.02855 0.02578  389 TRP A CB  
3142 C  CG  . TRP A 389 ? 0.24042 0.23994 0.23730 -0.00101 -0.02888 0.02375  389 TRP A CG  
3143 C  CD1 . TRP A 389 ? 0.24530 0.24086 0.24292 0.00428  -0.03076 0.02519  389 TRP A CD1 
3144 C  CD2 . TRP A 389 ? 0.23088 0.24129 0.23092 -0.00100 -0.02740 0.02023  389 TRP A CD2 
3145 N  NE1 . TRP A 389 ? 0.24598 0.25135 0.24845 0.00721  -0.03066 0.02330  389 TRP A NE1 
3146 C  CE2 . TRP A 389 ? 0.23230 0.24608 0.23576 0.00351  -0.02892 0.02010  389 TRP A CE2 
3147 C  CE3 . TRP A 389 ? 0.22553 0.24265 0.22615 -0.00424 -0.02496 0.01732  389 TRP A CE3 
3148 C  CZ2 . TRP A 389 ? 0.22731 0.25102 0.23485 0.00361  -0.02868 0.01730  389 TRP A CZ2 
3149 C  CZ3 . TRP A 389 ? 0.22112 0.24586 0.22420 -0.00357 -0.02452 0.01399  389 TRP A CZ3 
3150 C  CH2 . TRP A 389 ? 0.21748 0.24550 0.22402 -0.00029 -0.02668 0.01406  389 TRP A CH2 
3151 N  N   . TYR A 390 ? 0.19805 0.19677 0.19903 -0.01000 -0.02452 0.01755  390 TYR A N   
3152 C  CA  . TYR A 390 ? 0.19829 0.20252 0.20274 -0.00951 -0.02236 0.01331  390 TYR A CA  
3153 C  C   . TYR A 390 ? 0.20372 0.20051 0.20746 -0.00945 -0.02339 0.01121  390 TYR A C   
3154 O  O   . TYR A 390 ? 0.19727 0.19562 0.20213 -0.00742 -0.02197 0.00786  390 TYR A O   
3155 C  CB  . TYR A 390 ? 0.18576 0.19860 0.19306 -0.01262 -0.01998 0.01374  390 TYR A CB  
3156 C  CG  . TYR A 390 ? 0.18745 0.20758 0.19341 -0.01175 -0.01823 0.01328  390 TYR A CG  
3157 C  CD1 . TYR A 390 ? 0.18522 0.20655 0.18721 -0.01302 -0.01857 0.01707  390 TYR A CD1 
3158 C  CD2 . TYR A 390 ? 0.17872 0.20344 0.18619 -0.01009 -0.01667 0.00915  390 TYR A CD2 
3159 C  CE1 . TYR A 390 ? 0.18338 0.21039 0.18179 -0.01250 -0.01765 0.01632  390 TYR A CE1 
3160 C  CE2 . TYR A 390 ? 0.18239 0.21219 0.18711 -0.00999 -0.01601 0.00812  390 TYR A CE2 
3161 C  CZ  . TYR A 390 ? 0.18296 0.21391 0.18255 -0.01112 -0.01664 0.01148  390 TYR A CZ  
3162 O  OH  . TYR A 390 ? 0.18065 0.21577 0.17529 -0.01130 -0.01660 0.01012  390 TYR A OH  
3163 N  N   . MET A 391 ? 0.25302 0.24094 0.25394 -0.01210 -0.02615 0.01326  391 MET A N   
3164 C  CA  . MET A 391 ? 0.25891 0.23753 0.25629 -0.01224 -0.02809 0.01086  391 MET A CA  
3165 C  C   . MET A 391 ? 0.26635 0.23696 0.25865 -0.00653 -0.02739 0.00808  391 MET A C   
3166 O  O   . MET A 391 ? 0.27131 0.23787 0.26036 -0.00478 -0.02681 0.00480  391 MET A O   
3167 C  CB  . MET A 391 ? 0.26706 0.23696 0.26208 -0.01744 -0.03211 0.01365  391 MET A CB  
3168 C  CG  . MET A 391 ? 0.26116 0.23841 0.26222 -0.02319 -0.03327 0.01568  391 MET A CG  
3169 S  SD  . MET A 391 ? 0.25987 0.24363 0.26391 -0.02193 -0.03231 0.01214  391 MET A SD  
3170 C  CE  . MET A 391 ? 0.26320 0.23089 0.25733 -0.02265 -0.03715 0.00931  391 MET A CE  
3171 N  N   . VAL A 392 ? 0.18639 0.15518 0.17802 -0.00317 -0.02715 0.00976  392 VAL A N   
3172 C  CA  . VAL A 392 ? 0.19946 0.16032 0.18730 0.00307  -0.02615 0.00786  392 VAL A CA  
3173 C  C   . VAL A 392 ? 0.19324 0.16453 0.18608 0.00744  -0.02247 0.00579  392 VAL A C   
3174 O  O   . VAL A 392 ? 0.19684 0.16463 0.18734 0.01131  -0.02008 0.00292  392 VAL A O   
3175 C  CB  . VAL A 392 ? 0.21336 0.16735 0.19937 0.00541  -0.02790 0.01136  392 VAL A CB  
3176 C  CG1 . VAL A 392 ? 0.20887 0.16137 0.19543 0.01363  -0.02563 0.01030  392 VAL A CG1 
3177 C  CG2 . VAL A 392 ? 0.21934 0.15726 0.19823 0.00200  -0.03141 0.01242  392 VAL A CG2 
3178 N  N   . VAL A 393 ? 0.21195 0.19588 0.21115 0.00648  -0.02191 0.00725  393 VAL A N   
3179 C  CA  . VAL A 393 ? 0.21309 0.20628 0.21794 0.01038  -0.01967 0.00646  393 VAL A CA  
3180 C  C   . VAL A 393 ? 0.20768 0.20782 0.21576 0.00914  -0.01699 0.00353  393 VAL A C   
3181 O  O   . VAL A 393 ? 0.20593 0.21310 0.21917 0.01180  -0.01493 0.00297  393 VAL A O   
3182 C  CB  . VAL A 393 ? 0.20265 0.20480 0.21142 0.00974  -0.02150 0.00942  393 VAL A CB  
3183 C  CG1 . VAL A 393 ? 0.21112 0.20599 0.21645 0.01119  -0.02426 0.01334  393 VAL A CG1 
3184 C  CG2 . VAL A 393 ? 0.19200 0.20077 0.20112 0.00430  -0.02168 0.00907  393 VAL A CG2 
3185 N  N   . PHE A 394 ? 0.23440 0.23311 0.24049 0.00520  -0.01708 0.00225  394 PHE A N   
3186 C  CA  . PHE A 394 ? 0.23393 0.23830 0.24294 0.00399  -0.01484 0.00015  394 PHE A CA  
3187 C  C   . PHE A 394 ? 0.23401 0.23083 0.23788 0.00426  -0.01411 -0.00151 394 PHE A C   
3188 O  O   . PHE A 394 ? 0.23511 0.22437 0.23400 0.00229  -0.01661 -0.00123 394 PHE A O   
3189 C  CB  . PHE A 394 ? 0.21331 0.22373 0.22500 -0.00010 -0.01538 0.00035  394 PHE A CB  
3190 C  CG  . PHE A 394 ? 0.20771 0.22507 0.22195 -0.00061 -0.01603 0.00134  394 PHE A CG  
3191 C  CD1 . PHE A 394 ? 0.20198 0.22516 0.22009 0.00109  -0.01561 0.00084  394 PHE A CD1 
3192 C  CD2 . PHE A 394 ? 0.20629 0.22474 0.21882 -0.00309 -0.01724 0.00316  394 PHE A CD2 
3193 C  CE1 . PHE A 394 ? 0.20311 0.23233 0.22236 0.00011  -0.01743 0.00175  394 PHE A CE1 
3194 C  CE2 . PHE A 394 ? 0.20100 0.22493 0.21334 -0.00360 -0.01809 0.00403  394 PHE A CE2 
3195 C  CZ  . PHE A 394 ? 0.20365 0.23256 0.21884 -0.00210 -0.01872 0.00314  394 PHE A CZ  
3196 N  N   . ALA A 395 ? 0.23337 0.23239 0.23817 0.00617  -0.01098 -0.00288 395 ALA A N   
3197 C  CA  . ALA A 395 ? 0.23756 0.22911 0.23543 0.00702  -0.00991 -0.00428 395 ALA A CA  
3198 C  C   . ALA A 395 ? 0.23601 0.22667 0.23252 0.00306  -0.01204 -0.00421 395 ALA A C   
3199 O  O   . ALA A 395 ? 0.23325 0.21666 0.22241 0.00299  -0.01279 -0.00496 395 ALA A O   
3200 C  CB  . ALA A 395 ? 0.24441 0.23984 0.24411 0.01005  -0.00516 -0.00479 395 ALA A CB  
3201 N  N   . ASP A 396 ? 0.26758 0.26526 0.27049 0.00018  -0.01299 -0.00329 396 ASP A N   
3202 C  CA  . ASP A 396 ? 0.26236 0.26061 0.26617 -0.00267 -0.01483 -0.00259 396 ASP A CA  
3203 C  C   . ASP A 396 ? 0.26330 0.26077 0.26779 -0.00557 -0.01836 -0.00092 396 ASP A C   
3204 O  O   . ASP A 396 ? 0.25247 0.25362 0.26088 -0.00780 -0.01963 0.00041  396 ASP A O   
3205 C  CB  . ASP A 396 ? 0.25299 0.25884 0.26351 -0.00327 -0.01265 -0.00275 396 ASP A CB  
3206 C  CG  . ASP A 396 ? 0.25238 0.26431 0.26734 -0.00372 -0.01191 -0.00297 396 ASP A CG  
3207 O  OD1 . ASP A 396 ? 0.25392 0.26517 0.26759 -0.00373 -0.01331 -0.00212 396 ASP A OD1 
3208 O  OD2 . ASP A 396 ? 0.25535 0.27167 0.27403 -0.00419 -0.01020 -0.00398 396 ASP A OD2 
3209 N  N   . ALA A 397 ? 0.18080 0.17376 0.18232 -0.00551 -0.01980 -0.00044 397 ALA A N   
3210 C  CA  . ALA A 397 ? 0.18105 0.17431 0.18440 -0.00892 -0.02257 0.00200  397 ALA A CA  
3211 C  C   . ALA A 397 ? 0.18828 0.17453 0.18783 -0.01216 -0.02698 0.00279  397 ALA A C   
3212 O  O   . ALA A 397 ? 0.19502 0.17024 0.18611 -0.01147 -0.02890 0.00128  397 ALA A O   
3213 C  CB  . ALA A 397 ? 0.18543 0.17569 0.18693 -0.00780 -0.02272 0.00295  397 ALA A CB  
3214 N  N   . TYR A 398 ? 0.24669 0.23936 0.25248 -0.01558 -0.02864 0.00509  398 TYR A N   
3215 C  CA  . TYR A 398 ? 0.24911 0.23805 0.25427 -0.02019 -0.03402 0.00705  398 TYR A CA  
3216 C  C   . TYR A 398 ? 0.24281 0.24187 0.25817 -0.02379 -0.03407 0.01115  398 TYR A C   
3217 O  O   . TYR A 398 ? 0.23616 0.24528 0.25821 -0.02192 -0.02971 0.01170  398 TYR A O   
3218 C  CB  . TYR A 398 ? 0.24820 0.23600 0.25124 -0.02026 -0.03646 0.00632  398 TYR A CB  
3219 C  CG  . TYR A 398 ? 0.25945 0.23789 0.25156 -0.01644 -0.03500 0.00264  398 TYR A CG  
3220 C  CD1 . TYR A 398 ? 0.25073 0.23340 0.24412 -0.01217 -0.02974 0.00112  398 TYR A CD1 
3221 C  CD2 . TYR A 398 ? 0.27199 0.23690 0.25213 -0.01720 -0.03847 0.00068  398 TYR A CD2 
3222 C  CE1 . TYR A 398 ? 0.25886 0.23465 0.24350 -0.00877 -0.02744 -0.00145 398 TYR A CE1 
3223 C  CE2 . TYR A 398 ? 0.27556 0.23234 0.24518 -0.01297 -0.03579 -0.00262 398 TYR A CE2 
3224 C  CZ  . TYR A 398 ? 0.27302 0.23634 0.24574 -0.00875 -0.02997 -0.00328 398 TYR A CZ  
3225 O  OH  . TYR A 398 ? 0.28013 0.23705 0.24365 -0.00464 -0.02641 -0.00578 398 TYR A OH  
3226 N  N   . GLU A 399 ? 0.23378 0.22961 0.24979 -0.02911 -0.03875 0.01400  399 GLU A N   
3227 C  CA  . GLU A 399 ? 0.23089 0.23589 0.25607 -0.03274 -0.03779 0.01864  399 GLU A CA  
3228 C  C   . GLU A 399 ? 0.22086 0.24084 0.25789 -0.03234 -0.03526 0.02094  399 GLU A C   
3229 O  O   . GLU A 399 ? 0.21571 0.24536 0.25926 -0.03196 -0.03062 0.02325  399 GLU A O   
3230 C  CB  . GLU A 399 ? 0.24183 0.24027 0.26639 -0.03962 -0.04384 0.02183  399 GLU A CB  
3231 C  CG  . GLU A 399 ? 0.24203 0.25001 0.27611 -0.04395 -0.04222 0.02760  399 GLU A CG  
3232 C  CD  . GLU A 399 ? 0.24904 0.24858 0.28193 -0.05149 -0.04818 0.03109  399 GLU A CD  
3233 O  OE1 . GLU A 399 ? 0.24295 0.24614 0.28252 -0.05734 -0.05338 0.03395  399 GLU A OE1 
3234 O  OE2 . GLU A 399 ? 0.26900 0.25810 0.29464 -0.05177 -0.04806 0.03131  399 GLU A OE2 
3235 N  N   . TRP A 400 ? 0.16849 0.19017 0.20776 -0.03186 -0.03795 0.02047  400 TRP A N   
3236 C  CA  . TRP A 400 ? 0.15700 0.19251 0.20853 -0.03054 -0.03567 0.02309  400 TRP A CA  
3237 C  C   . TRP A 400 ? 0.15210 0.19276 0.20483 -0.02473 -0.02804 0.02066  400 TRP A C   
3238 O  O   . TRP A 400 ? 0.14613 0.19795 0.20838 -0.02325 -0.02390 0.02281  400 TRP A O   
3239 C  CB  . TRP A 400 ? 0.15534 0.19025 0.20769 -0.03042 -0.04061 0.02327  400 TRP A CB  
3240 C  CG  . TRP A 400 ? 0.15829 0.18480 0.20068 -0.02578 -0.03935 0.01870  400 TRP A CG  
3241 C  CD1 . TRP A 400 ? 0.16640 0.17971 0.19559 -0.02600 -0.04231 0.01550  400 TRP A CD1 
3242 C  CD2 . TRP A 400 ? 0.15658 0.18694 0.20131 -0.02032 -0.03431 0.01709  400 TRP A CD2 
3243 N  NE1 . TRP A 400 ? 0.17481 0.18522 0.19895 -0.02125 -0.03906 0.01261  400 TRP A NE1 
3244 C  CE2 . TRP A 400 ? 0.16521 0.18541 0.19880 -0.01816 -0.03459 0.01359  400 TRP A CE2 
3245 C  CE3 . TRP A 400 ? 0.15019 0.19069 0.20484 -0.01696 -0.02927 0.01819  400 TRP A CE3 
3246 C  CZ2 . TRP A 400 ? 0.16472 0.18496 0.19773 -0.01378 -0.03056 0.01179  400 TRP A CZ2 
3247 C  CZ3 . TRP A 400 ? 0.15213 0.19077 0.20500 -0.01222 -0.02561 0.01562  400 TRP A CZ3 
3248 C  CH2 . TRP A 400 ? 0.15755 0.18631 0.20013 -0.01116 -0.02654 0.01275  400 TRP A CH2 
3249 N  N   . VAL A 401 ? 0.22455 0.25725 0.26785 -0.02145 -0.02606 0.01619  401 VAL A N   
3250 C  CA  . VAL A 401 ? 0.22565 0.26162 0.26893 -0.01703 -0.02007 0.01345  401 VAL A CA  
3251 C  C   . VAL A 401 ? 0.22639 0.26117 0.26495 -0.01705 -0.01734 0.01256  401 VAL A C   
3252 O  O   . VAL A 401 ? 0.22175 0.26190 0.26166 -0.01508 -0.01265 0.01173  401 VAL A O   
3253 C  CB  . VAL A 401 ? 0.22274 0.25274 0.26083 -0.01373 -0.01984 0.00981  401 VAL A CB  
3254 C  CG1 . VAL A 401 ? 0.23051 0.25028 0.25897 -0.01430 -0.02254 0.00788  401 VAL A CG1 
3255 C  CG2 . VAL A 401 ? 0.21725 0.24948 0.25536 -0.01026 -0.01451 0.00686  401 VAL A CG2 
3256 N  N   . GLU A 402 ? 0.22113 0.24828 0.25344 -0.01900 -0.02034 0.01279  402 GLU A N   
3257 C  CA  . GLU A 402 ? 0.22631 0.25219 0.25424 -0.01870 -0.01857 0.01282  402 GLU A CA  
3258 C  C   . GLU A 402 ? 0.22998 0.26325 0.26215 -0.02128 -0.01638 0.01689  402 GLU A C   
3259 O  O   . GLU A 402 ? 0.22558 0.26264 0.25562 -0.01986 -0.01264 0.01656  402 GLU A O   
3260 C  CB  . GLU A 402 ? 0.23790 0.25290 0.25878 -0.01940 -0.02230 0.01267  402 GLU A CB  
3261 C  CG  . GLU A 402 ? 0.24091 0.25383 0.25791 -0.01938 -0.02178 0.01434  402 GLU A CG  
3262 C  CD  . GLU A 402 ? 0.25294 0.26656 0.27191 -0.02411 -0.02299 0.01947  402 GLU A CD  
3263 O  OE1 . GLU A 402 ? 0.25669 0.26632 0.27734 -0.02798 -0.02665 0.02134  402 GLU A OE1 
3264 O  OE2 . GLU A 402 ? 0.24943 0.26749 0.26780 -0.02442 -0.02049 0.02188  402 GLU A OE2 
3265 N  N   . MET A 403 ? 0.21015 0.24578 0.24801 -0.02549 -0.01876 0.02103  403 MET A N   
3266 C  CA  . MET A 403 ? 0.21421 0.25654 0.25604 -0.02876 -0.01650 0.02602  403 MET A CA  
3267 C  C   . MET A 403 ? 0.20694 0.26150 0.25466 -0.02626 -0.00993 0.02648  403 MET A C   
3268 O  O   . MET A 403 ? 0.20325 0.26116 0.24779 -0.02607 -0.00570 0.02791  403 MET A O   
3269 C  CB  . MET A 403 ? 0.20812 0.24996 0.25562 -0.03493 -0.02129 0.03080  403 MET A CB  
3270 C  CG  . MET A 403 ? 0.21412 0.26185 0.26565 -0.03942 -0.01919 0.03700  403 MET A CG  
3271 S  SD  . MET A 403 ? 0.22061 0.26798 0.28043 -0.04815 -0.02584 0.04287  403 MET A SD  
3272 C  CE  . MET A 403 ? 0.22889 0.25558 0.27510 -0.05045 -0.03173 0.04151  403 MET A CE  
3273 N  N   . PRO A 404 ? 0.20068 0.26154 0.25599 -0.02390 -0.00854 0.02549  404 PRO A N   
3274 C  CA  . PRO A 404 ? 0.19400 0.26478 0.25373 -0.02029 -0.00132 0.02533  404 PRO A CA  
3275 C  C   . PRO A 404 ? 0.19935 0.26592 0.24896 -0.01622 0.00252  0.02006  404 PRO A C   
3276 O  O   . PRO A 404 ? 0.20240 0.27425 0.25041 -0.01426 0.00861  0.01989  404 PRO A O   
3277 C  CB  . PRO A 404 ? 0.18474 0.26043 0.25421 -0.01782 -0.00189 0.02517  404 PRO A CB  
3278 C  CG  . PRO A 404 ? 0.18836 0.25973 0.26002 -0.02210 -0.00980 0.02722  404 PRO A CG  
3279 C  CD  . PRO A 404 ? 0.19539 0.25443 0.25511 -0.02408 -0.01330 0.02489  404 PRO A CD  
3280 N  N   . ASN A 405 ? 0.15809 0.21542 0.20053 -0.01515 -0.00089 0.01584  405 ASN A N   
3281 C  CA  . ASN A 405 ? 0.16238 0.21607 0.19605 -0.01251 0.00129  0.01123  405 ASN A CA  
3282 C  C   . ASN A 405 ? 0.17053 0.22242 0.19629 -0.01444 0.00083  0.01282  405 ASN A C   
3283 O  O   . ASN A 405 ? 0.17371 0.22580 0.19235 -0.01299 0.00347  0.01042  405 ASN A O   
3284 C  CB  . ASN A 405 ? 0.16342 0.20986 0.19445 -0.01105 -0.00202 0.00718  405 ASN A CB  
3285 C  CG  . ASN A 405 ? 0.16323 0.21026 0.19871 -0.00810 -0.00022 0.00462  405 ASN A CG  
3286 O  OD1 . ASN A 405 ? 0.16403 0.21291 0.19885 -0.00553 0.00417  0.00216  405 ASN A OD1 
3287 N  ND2 . ASN A 405 ? 0.15533 0.19955 0.19416 -0.00828 -0.00365 0.00521  405 ASN A ND2 
3288 N  N   . THR A 406 ? 0.23692 0.28595 0.26289 -0.01777 -0.00294 0.01688  406 THR A N   
3289 C  CA  . THR A 406 ? 0.24549 0.29128 0.26404 -0.01929 -0.00421 0.01925  406 THR A CA  
3290 C  C   . THR A 406 ? 0.24318 0.29470 0.26261 -0.02228 -0.00105 0.02496  406 THR A C   
3291 O  O   . THR A 406 ? 0.24782 0.30191 0.26039 -0.02166 0.00235  0.02550  406 THR A O   
3292 C  CB  . THR A 406 ? 0.24815 0.28490 0.26517 -0.02047 -0.00999 0.02021  406 THR A CB  
3293 O  OG1 . THR A 406 ? 0.23955 0.27221 0.25566 -0.01741 -0.01174 0.01535  406 THR A OG1 
3294 C  CG2 . THR A 406 ? 0.24476 0.27752 0.25471 -0.02120 -0.01157 0.02324  406 THR A CG2 
3295 N  N   . ARG A 407 ? 0.27864 0.33229 0.30607 -0.02600 -0.00229 0.02953  407 ARG A N   
3296 C  CA  . ARG A 407 ? 0.27608 0.33691 0.30664 -0.02953 0.00129  0.03590  407 ARG A CA  
3297 C  C   . ARG A 407 ? 0.26658 0.33866 0.30033 -0.02669 0.00915  0.03527  407 ARG A C   
3298 O  O   . ARG A 407 ? 0.27311 0.35141 0.30536 -0.02804 0.01428  0.03959  407 ARG A O   
3299 C  CB  . ARG A 407 ? 0.26850 0.32990 0.30884 -0.03497 -0.00252 0.04091  407 ARG A CB  
3300 C  CG  . ARG A 407 ? 0.27994 0.34738 0.32390 -0.04027 0.00009  0.04889  407 ARG A CG  
3301 C  CD  . ARG A 407 ? 0.27601 0.34046 0.32781 -0.04713 -0.00589 0.05369  407 ARG A CD  
3302 N  NE  . ARG A 407 ? 0.28942 0.33768 0.33227 -0.04891 -0.01253 0.05303  407 ARG A NE  
3303 C  CZ  . ARG A 407 ? 0.29248 0.33408 0.33172 -0.05375 -0.01444 0.05870  407 ARG A CZ  
3304 N  NH1 . ARG A 407 ? 0.29108 0.34141 0.33473 -0.05815 -0.01020 0.06599  407 ARG A NH1 
3305 N  NH2 . ARG A 407 ? 0.29341 0.31888 0.32438 -0.05389 -0.02028 0.05732  407 ARG A NH2 
3306 N  N   . GLY A 408 ? 0.19540 0.26945 0.23278 -0.02243 0.01064  0.03014  408 GLY A N   
3307 C  CA  . GLY A 408 ? 0.20377 0.28674 0.24410 -0.01859 0.01841  0.02894  408 GLY A CA  
3308 C  C   . GLY A 408 ? 0.20167 0.28029 0.22974 -0.01415 0.02177  0.02254  408 GLY A C   
3309 O  O   . GLY A 408 ? 0.20679 0.28688 0.22573 -0.01387 0.02627  0.02318  408 GLY A O   
3310 N  N   . MET A 409 ? 0.26474 0.33739 0.29168 -0.01119 0.01929  0.01649  409 MET A N   
3311 C  CA  . MET A 409 ? 0.26824 0.33660 0.28512 -0.00748 0.02227  0.00999  409 MET A CA  
3312 C  C   . MET A 409 ? 0.28289 0.34572 0.28613 -0.00932 0.01959  0.00886  409 MET A C   
3313 O  O   . MET A 409 ? 0.28741 0.34935 0.27977 -0.00785 0.02333  0.00604  409 MET A O   
3314 C  CB  . MET A 409 ? 0.26820 0.33101 0.28818 -0.00503 0.01954  0.00486  409 MET A CB  
3315 C  CG  . MET A 409 ? 0.29171 0.34939 0.30348 -0.00145 0.02284  -0.00198 409 MET A CG  
3316 S  SD  . MET A 409 ? 0.29668 0.34523 0.30864 -0.00113 0.01740  -0.00713 409 MET A SD  
3317 C  CE  . MET A 409 ? 0.27578 0.32748 0.30202 0.00154  0.01826  -0.00492 409 MET A CE  
3318 N  N   . ALA A 410 ? 0.20118 0.25994 0.20423 -0.01224 0.01302  0.01111  410 ALA A N   
3319 C  CA  . ALA A 410 ? 0.20142 0.25532 0.19339 -0.01313 0.00937  0.01005  410 ALA A CA  
3320 C  C   . ALA A 410 ? 0.21542 0.27157 0.19974 -0.01523 0.01107  0.01526  410 ALA A C   
3321 O  O   . ALA A 410 ? 0.22310 0.27722 0.19538 -0.01510 0.01050  0.01386  410 ALA A O   
3322 C  CB  . ALA A 410 ? 0.20305 0.25176 0.19820 -0.01411 0.00243  0.01047  410 ALA A CB  
3323 N  N   . THR A 411 ? 0.20921 0.26934 0.19989 -0.01772 0.01268  0.02169  411 THR A N   
3324 C  CA  . THR A 411 ? 0.21488 0.27590 0.19880 -0.02055 0.01350  0.02804  411 THR A CA  
3325 C  C   . THR A 411 ? 0.22457 0.29442 0.21128 -0.02163 0.02136  0.03271  411 THR A C   
3326 O  O   . THR A 411 ? 0.22456 0.29559 0.20547 -0.02442 0.02291  0.03888  411 THR A O   
3327 C  CB  . THR A 411 ? 0.21200 0.26759 0.19971 -0.02378 0.00711  0.03316  411 THR A CB  
3328 O  OG1 . THR A 411 ? 0.21053 0.26862 0.21103 -0.02609 0.00712  0.03583  411 THR A OG1 
3329 C  CG2 . THR A 411 ? 0.21256 0.26065 0.19855 -0.02182 0.00043  0.02904  411 THR A CG2 
3330 N  N   . PHE A 412 ? 0.28326 0.35980 0.27928 -0.01933 0.02655  0.03067  412 PHE A N   
3331 C  CA  . PHE A 412 ? 0.28326 0.37047 0.28389 -0.01927 0.03527  0.03505  412 PHE A CA  
3332 C  C   . PHE A 412 ? 0.28402 0.37609 0.29343 -0.02516 0.03446  0.04457  412 PHE A C   
3333 O  O   . PHE A 412 ? 0.27607 0.37726 0.28732 -0.02646 0.04165  0.05021  412 PHE A O   
3334 C  CB  . PHE A 412 ? 0.30219 0.38992 0.28669 -0.01684 0.04207  0.03341  412 PHE A CB  
3335 C  CG  . PHE A 412 ? 0.29891 0.39691 0.28723 -0.01335 0.05313  0.03396  412 PHE A CG  
3336 C  CD1 . PHE A 412 ? 0.29028 0.38954 0.28396 -0.00771 0.05680  0.02760  412 PHE A CD1 
3337 C  CD2 . PHE A 412 ? 0.30343 0.40974 0.29004 -0.01533 0.06039  0.04126  412 PHE A CD2 
3338 C  CE1 . PHE A 412 ? 0.29078 0.39950 0.28864 -0.00324 0.06764  0.02816  412 PHE A CE1 
3339 C  CE2 . PHE A 412 ? 0.29655 0.41361 0.28756 -0.01130 0.07173  0.04205  412 PHE A CE2 
3340 C  CZ  . PHE A 412 ? 0.28831 0.40660 0.28517 -0.00480 0.07543  0.03529  412 PHE A CZ  
3341 N  N   . ALA A 413 ? 0.23077 0.31642 0.24539 -0.02895 0.02608  0.04655  413 ALA A N   
3342 C  CA  . ALA A 413 ? 0.22805 0.31580 0.25045 -0.03544 0.02424  0.05522  413 ALA A CA  
3343 C  C   . ALA A 413 ? 0.22129 0.32150 0.26144 -0.03725 0.02754  0.05891  413 ALA A C   
3344 O  O   . ALA A 413 ? 0.21603 0.32161 0.26384 -0.04322 0.02811  0.06708  413 ALA A O   
3345 C  CB  . ALA A 413 ? 0.22708 0.30232 0.24889 -0.03840 0.01436  0.05526  413 ALA A CB  
3346 N  N   . ASP A 414 ? 0.24282 0.34797 0.29035 -0.03246 0.02939  0.05370  414 ASP A N   
3347 C  CA  . ASP A 414 ? 0.22600 0.34479 0.29157 -0.03295 0.03255  0.05738  414 ASP A CA  
3348 C  C   . ASP A 414 ? 0.22778 0.35983 0.29561 -0.02872 0.04439  0.05897  414 ASP A C   
3349 O  O   . ASP A 414 ? 0.21656 0.36168 0.30042 -0.02708 0.04833  0.06150  414 ASP A O   
3350 C  CB  . ASP A 414 ? 0.22062 0.33746 0.29367 -0.02960 0.02787  0.05186  414 ASP A CB  
3351 C  CG  . ASP A 414 ? 0.22972 0.34403 0.29551 -0.02145 0.03235  0.04370  414 ASP A CG  
3352 O  OD1 . ASP A 414 ? 0.23331 0.34420 0.28536 -0.01877 0.03716  0.04076  414 ASP A OD1 
3353 O  OD2 . ASP A 414 ? 0.22085 0.33563 0.29398 -0.01804 0.03054  0.04029  414 ASP A OD2 
3354 N  N   . GLY A 415 ? 0.35059 0.47960 0.40240 -0.02652 0.05013  0.05758  415 GLY A N   
3355 C  CA  . GLY A 415 ? 0.35439 0.49440 0.40517 -0.02212 0.06230  0.05868  415 GLY A CA  
3356 C  C   . GLY A 415 ? 0.35058 0.49167 0.40131 -0.01328 0.06764  0.05071  415 GLY A C   
3357 O  O   . GLY A 415 ? 0.35948 0.50957 0.41029 -0.00840 0.07865  0.05109  415 GLY A O   
3358 N  N   . GLY A 416 ? 0.29768 0.42932 0.34794 -0.01086 0.06073  0.04370  416 GLY A N   
3359 C  CA  . GLY A 416 ? 0.30483 0.43469 0.35437 -0.00290 0.06481  0.03614  416 GLY A CA  
3360 C  C   . GLY A 416 ? 0.29860 0.43554 0.36778 -0.00035 0.06321  0.03697  416 GLY A C   
3361 O  O   . GLY A 416 ? 0.29555 0.43391 0.36707 0.00714  0.06902  0.03266  416 GLY A O   
3362 N  N   . ILE A 417 ? 0.25437 0.39478 0.33678 -0.00621 0.05524  0.04233  417 ILE A N   
3363 C  CA  . ILE A 417 ? 0.24242 0.38946 0.34261 -0.00426 0.05226  0.04358  417 ILE A CA  
3364 C  C   . ILE A 417 ? 0.24754 0.38201 0.34119 0.00052  0.04820  0.03528  417 ILE A C   
3365 O  O   . ILE A 417 ? 0.24592 0.38364 0.34755 0.00691  0.05121  0.03336  417 ILE A O   
3366 C  CB  . ILE A 417 ? 0.24024 0.39128 0.35262 -0.01271 0.04319  0.05052  417 ILE A CB  
3367 C  CG1 . ILE A 417 ? 0.22433 0.39120 0.34866 -0.01730 0.04813  0.06003  417 ILE A CG1 
3368 C  CG2 . ILE A 417 ? 0.22709 0.38061 0.35301 -0.01130 0.03700  0.05046  417 ILE A CG2 
3369 C  CD1 . ILE A 417 ? 0.21456 0.38274 0.34801 -0.02730 0.03876  0.06678  417 ILE A CD1 
3370 N  N   . VAL A 418 ? 0.21415 0.33431 0.29372 -0.00229 0.04167  0.03073  418 VAL A N   
3371 C  CA  . VAL A 418 ? 0.22090 0.32937 0.29474 0.00089  0.03740  0.02373  418 VAL A CA  
3372 C  C   . VAL A 418 ? 0.23061 0.33164 0.29091 0.00646  0.04342  0.01638  418 VAL A C   
3373 O  O   . VAL A 418 ? 0.23709 0.33466 0.29892 0.01204  0.04551  0.01205  418 VAL A O   
3374 C  CB  . VAL A 418 ? 0.21933 0.31720 0.28616 -0.00456 0.02785  0.02273  418 VAL A CB  
3375 C  CG1 . VAL A 418 ? 0.22309 0.30941 0.28256 -0.00162 0.02472  0.01572  418 VAL A CG1 
3376 C  CG2 . VAL A 418 ? 0.20908 0.31116 0.28775 -0.00958 0.02115  0.02849  418 VAL A CG2 
3377 N  N   . GLY A 419 ? 0.31789 0.41538 0.36401 0.00480  0.04582  0.01497  419 GLY A N   
3378 C  CA  . GLY A 419 ? 0.33951 0.42741 0.36973 0.00846  0.04917  0.00731  419 GLY A CA  
3379 C  C   . GLY A 419 ? 0.35269 0.44480 0.37747 0.01361  0.06011  0.00592  419 GLY A C   
3380 O  O   . GLY A 419 ? 0.37844 0.46108 0.38928 0.01715  0.06310  -0.00139 419 GLY A O   
3381 N  N   . SER A 420 ? 0.47547 0.58141 0.51048 0.01377  0.06624  0.01286  420 SER A N   
3382 C  CA  . SER A 420 ? 0.49019 0.60271 0.52224 0.01945  0.07840  0.01270  420 SER A CA  
3383 C  C   . SER A 420 ? 0.50798 0.61435 0.51777 0.01836  0.08216  0.00995  420 SER A C   
3384 O  O   . SER A 420 ? 0.51256 0.62523 0.51765 0.02188  0.09271  0.01119  420 SER A O   
3385 C  CB  . SER A 420 ? 0.49457 0.60295 0.52874 0.02826  0.08363  0.00638  420 SER A CB  
3386 O  OG  . SER A 420 ? 0.52016 0.61180 0.53431 0.03004  0.08275  -0.00316 420 SER A OG  
3387 N  N   . LYS A 421 ? 0.44557 0.54034 0.44151 0.01375  0.07378  0.00660  421 LYS A N   
3388 C  CA  . LYS A 421 ? 0.45171 0.54050 0.42605 0.01196  0.07518  0.00466  421 LYS A CA  
3389 C  C   . LYS A 421 ? 0.45118 0.53190 0.41917 0.00572  0.06348  0.00458  421 LYS A C   
3390 O  O   . LYS A 421 ? 0.44634 0.52215 0.42166 0.00474  0.05591  0.00216  421 LYS A O   
3391 C  CB  . LYS A 421 ? 0.47043 0.54908 0.42752 0.01785  0.08091  -0.00496 421 LYS A CB  
3392 C  CG  . LYS A 421 ? 0.47198 0.53682 0.42465 0.01823  0.07337  -0.01338 421 LYS A CG  
3393 C  CD  . LYS A 421 ? 0.50242 0.55406 0.43030 0.01878  0.07365  -0.02175 421 LYS A CD  
3394 C  CE  . LYS A 421 ? 0.51667 0.55513 0.44152 0.01780  0.06560  -0.02939 421 LYS A CE  
3395 N  NZ  . LYS A 421 ? 0.52666 0.55820 0.45353 0.02458  0.07141  -0.03587 421 LYS A NZ  
3396 N  N   . PRO A 422 ? 0.33119 0.41070 0.28597 0.00183  0.06202  0.00769  422 PRO A N   
3397 C  CA  . PRO A 422 ? 0.33221 0.40474 0.28215 -0.00311 0.05104  0.00813  422 PRO A CA  
3398 C  C   . PRO A 422 ? 0.34601 0.40722 0.28316 -0.00197 0.04630  -0.00089 422 PRO A C   
3399 O  O   . PRO A 422 ? 0.35707 0.41344 0.27966 0.00094  0.05108  -0.00680 422 PRO A O   
3400 C  CB  . PRO A 422 ? 0.33713 0.41206 0.27615 -0.00670 0.05200  0.01479  422 PRO A CB  
3401 C  CG  . PRO A 422 ? 0.34641 0.42500 0.27508 -0.00303 0.06334  0.01375  422 PRO A CG  
3402 C  CD  . PRO A 422 ? 0.34598 0.43044 0.28919 0.00219  0.07058  0.01133  422 PRO A CD  
3403 N  N   . TYR A 423 ? 0.50629 0.56306 0.44882 -0.00446 0.03695  -0.00194 423 TYR A N   
3404 C  CA  . TYR A 423 ? 0.51092 0.55839 0.44488 -0.00454 0.03139  -0.00953 423 TYR A CA  
3405 C  C   . TYR A 423 ? 0.51398 0.55829 0.43473 -0.00822 0.02453  -0.00842 423 TYR A C   
3406 O  O   . TYR A 423 ? 0.51611 0.55716 0.43870 -0.01036 0.01626  -0.00977 423 TYR A O   
3407 C  CB  . TYR A 423 ? 0.50401 0.54967 0.45245 -0.00467 0.02616  -0.01112 423 TYR A CB  
3408 C  CG  . TYR A 423 ? 0.50411 0.54941 0.46105 -0.00041 0.03165  -0.01464 423 TYR A CG  
3409 C  CD1 . TYR A 423 ? 0.49042 0.54404 0.46041 0.00168  0.03694  -0.00984 423 TYR A CD1 
3410 C  CD2 . TYR A 423 ? 0.51613 0.55271 0.46855 0.00136  0.03115  -0.02229 423 TYR A CD2 
3411 C  CE1 . TYR A 423 ? 0.49971 0.55376 0.47846 0.00626  0.04155  -0.01228 423 TYR A CE1 
3412 C  CE2 . TYR A 423 ? 0.52553 0.56059 0.48559 0.00587  0.03608  -0.02498 423 TYR A CE2 
3413 C  CZ  . TYR A 423 ? 0.51448 0.55869 0.48787 0.00874  0.04127  -0.01983 423 TYR A CZ  
3414 O  OH  . TYR A 423 ? 0.51250 0.55599 0.49451 0.01388  0.04575  -0.02175 423 TYR A OH  
3415 N  N   . ALA A 424 ? 0.30654 0.35261 0.21414 -0.00878 0.02814  -0.00529 424 ALA A N   
3416 C  CA  . ALA A 424 ? 0.31367 0.35692 0.20720 -0.01194 0.02151  -0.00347 424 ALA A CA  
3417 C  C   . ALA A 424 ? 0.32663 0.36177 0.20493 -0.01221 0.01788  -0.01206 424 ALA A C   
3418 O  O   . ALA A 424 ? 0.33265 0.36310 0.20360 -0.00954 0.02368  -0.01902 424 ALA A O   
3419 C  CB  . ALA A 424 ? 0.31830 0.36530 0.20075 -0.01265 0.02679  0.00302  424 ALA A CB  
3420 N  N   . ALA A 425 ? 0.39200 0.42522 0.26600 -0.01546 0.00787  -0.01145 425 ALA A N   
3421 C  CA  . ALA A 425 ? 0.40027 0.42646 0.26030 -0.01729 0.00228  -0.01876 425 ALA A CA  
3422 C  C   . ALA A 425 ? 0.39642 0.42419 0.25003 -0.02083 -0.00795 -0.01434 425 ALA A C   
3423 O  O   . ALA A 425 ? 0.39341 0.42654 0.25889 -0.02127 -0.01199 -0.00706 425 ALA A O   
3424 C  CB  . ALA A 425 ? 0.40067 0.42310 0.27194 -0.01740 -0.00061 -0.02530 425 ALA A CB  
3425 N  N   . SER A 426 ? 0.37277 0.39519 0.20702 -0.02314 -0.01236 -0.01883 426 SER A N   
3426 C  CA  . SER A 426 ? 0.37372 0.39803 0.20098 -0.02655 -0.02327 -0.01484 426 SER A CA  
3427 C  C   . SER A 426 ? 0.36707 0.39276 0.20747 -0.02908 -0.03293 -0.01753 426 SER A C   
3428 O  O   . SER A 426 ? 0.36352 0.38871 0.21877 -0.02821 -0.03071 -0.02128 426 SER A O   
3429 C  CB  . SER A 426 ? 0.39037 0.40854 0.18970 -0.02840 -0.02438 -0.01814 426 SER A CB  
3430 O  OG  . SER A 426 ? 0.39884 0.40835 0.18891 -0.02997 -0.02562 -0.02886 426 SER A OG  
3431 N  N   . GLY A 427 ? 0.45303 0.48125 0.28849 -0.03231 -0.04387 -0.01498 427 GLY A N   
3432 C  CA  . GLY A 427 ? 0.44563 0.47673 0.29335 -0.03529 -0.05305 -0.01728 427 GLY A CA  
3433 C  C   . GLY A 427 ? 0.46323 0.48620 0.30316 -0.03863 -0.05410 -0.02767 427 GLY A C   
3434 O  O   . GLY A 427 ? 0.44185 0.46678 0.29494 -0.04137 -0.05959 -0.03007 427 GLY A O   
3435 N  N   . ALA A 428 ? 0.41279 0.42604 0.23127 -0.03841 -0.04854 -0.03380 428 ALA A N   
3436 C  CA  . ALA A 428 ? 0.41973 0.42198 0.22846 -0.04123 -0.04906 -0.04445 428 ALA A CA  
3437 C  C   . ALA A 428 ? 0.40379 0.40430 0.23144 -0.03939 -0.04362 -0.04792 428 ALA A C   
3438 O  O   . ALA A 428 ? 0.40613 0.40166 0.23726 -0.04334 -0.04848 -0.05363 428 ALA A O   
3439 C  CB  . ALA A 428 ? 0.43830 0.42953 0.22016 -0.03947 -0.04171 -0.05031 428 ALA A CB  
3440 N  N   . TYR A 429 ? 0.43178 0.43623 0.27175 -0.03393 -0.03406 -0.04408 429 TYR A N   
3441 C  CA  . TYR A 429 ? 0.42325 0.42639 0.28070 -0.03190 -0.02926 -0.04644 429 TYR A CA  
3442 C  C   . TYR A 429 ? 0.40208 0.41217 0.27907 -0.03499 -0.03712 -0.04340 429 TYR A C   
3443 O  O   . TYR A 429 ? 0.38814 0.39376 0.27166 -0.03744 -0.03892 -0.04809 429 TYR A O   
3444 C  CB  . TYR A 429 ? 0.42095 0.42848 0.28795 -0.02603 -0.01895 -0.04190 429 TYR A CB  
3445 C  CG  . TYR A 429 ? 0.41429 0.42103 0.29893 -0.02376 -0.01473 -0.04339 429 TYR A CG  
3446 C  CD1 . TYR A 429 ? 0.42167 0.41947 0.30239 -0.02090 -0.00755 -0.04987 429 TYR A CD1 
3447 C  CD2 . TYR A 429 ? 0.39258 0.40679 0.29683 -0.02405 -0.01788 -0.03822 429 TYR A CD2 
3448 C  CE1 . TYR A 429 ? 0.40321 0.40003 0.29951 -0.01873 -0.00436 -0.05046 429 TYR A CE1 
3449 C  CE2 . TYR A 429 ? 0.37885 0.39185 0.29714 -0.02221 -0.01441 -0.03926 429 TYR A CE2 
3450 C  CZ  . TYR A 429 ? 0.39127 0.39583 0.30579 -0.01972 -0.00800 -0.04501 429 TYR A CZ  
3451 O  OH  . TYR A 429 ? 0.37044 0.37366 0.29863 -0.01774 -0.00509 -0.04523 429 TYR A OH  
3452 N  N   . ILE A 430 ? 0.41478 0.43555 0.30142 -0.03461 -0.04132 -0.03522 430 ILE A N   
3453 C  CA  . ILE A 430 ? 0.38963 0.41828 0.29520 -0.03646 -0.04770 -0.03177 430 ILE A CA  
3454 C  C   . ILE A 430 ? 0.38637 0.41416 0.28867 -0.04287 -0.05742 -0.03563 430 ILE A C   
3455 O  O   . ILE A 430 ? 0.37742 0.40827 0.29446 -0.04544 -0.06053 -0.03610 430 ILE A O   
3456 C  CB  . ILE A 430 ? 0.37801 0.41667 0.29191 -0.03399 -0.05031 -0.02253 430 ILE A CB  
3457 C  CG1 . ILE A 430 ? 0.37355 0.41229 0.29282 -0.02887 -0.04137 -0.01884 430 ILE A CG1 
3458 C  CG2 . ILE A 430 ? 0.35174 0.39921 0.28425 -0.03510 -0.05662 -0.01900 430 ILE A CG2 
3459 C  CD1 . ILE A 430 ? 0.37502 0.41781 0.29085 -0.02689 -0.04225 -0.01113 430 ILE A CD1 
3460 N  N   . ASP A 431 ? 0.50696 0.53053 0.38955 -0.04605 -0.06247 -0.03827 431 ASP A N   
3461 C  CA  . ASP A 431 ? 0.50879 0.53087 0.38679 -0.05328 -0.07300 -0.04225 431 ASP A CA  
3462 C  C   . ASP A 431 ? 0.51181 0.52207 0.38812 -0.05632 -0.07063 -0.05114 431 ASP A C   
3463 O  O   . ASP A 431 ? 0.49573 0.50799 0.38328 -0.06172 -0.07694 -0.05228 431 ASP A O   
3464 C  CB  . ASP A 431 ? 0.52304 0.54150 0.37698 -0.05599 -0.07904 -0.04345 431 ASP A CB  
3465 C  CG  . ASP A 431 ? 0.52023 0.54002 0.37114 -0.06423 -0.09257 -0.04569 431 ASP A CG  
3466 O  OD1 . ASP A 431 ? 0.50563 0.53583 0.37785 -0.06699 -0.09854 -0.04206 431 ASP A OD1 
3467 O  OD2 . ASP A 431 ? 0.54369 0.55437 0.37073 -0.06811 -0.09724 -0.05097 431 ASP A OD2 
3468 N  N   . ARG A 432 ? 0.65388 0.65180 0.51698 -0.05275 -0.06128 -0.05705 432 ARG A N   
3469 C  CA  . ARG A 432 ? 0.65441 0.63894 0.51518 -0.05458 -0.05845 -0.06541 432 ARG A CA  
3470 C  C   . ARG A 432 ? 0.62726 0.61603 0.51196 -0.05332 -0.05509 -0.06274 432 ARG A C   
3471 O  O   . ARG A 432 ? 0.62013 0.60100 0.50844 -0.05728 -0.05669 -0.06741 432 ARG A O   
3472 C  CB  . ARG A 432 ? 0.67690 0.64825 0.51929 -0.04927 -0.04808 -0.07160 432 ARG A CB  
3473 C  CG  . ARG A 432 ? 0.67096 0.62829 0.51425 -0.04816 -0.04227 -0.07894 432 ARG A CG  
3474 C  CD  . ARG A 432 ? 0.71141 0.65495 0.53400 -0.04273 -0.03276 -0.08593 432 ARG A CD  
3475 N  NE  . ARG A 432 ? 0.71560 0.66281 0.54895 -0.03424 -0.02084 -0.08274 432 ARG A NE  
3476 C  CZ  . ARG A 432 ? 0.72914 0.68525 0.56141 -0.02895 -0.01427 -0.07748 432 ARG A CZ  
3477 N  NH1 . ARG A 432 ? 0.72825 0.68953 0.54779 -0.03060 -0.01760 -0.07464 432 ARG A NH1 
3478 N  NH2 . ARG A 432 ? 0.72080 0.68087 0.56530 -0.02224 -0.00456 -0.07445 432 ARG A NH2 
3479 N  N   . MET A 433 ? 0.48736 0.48761 0.38761 -0.04832 -0.05088 -0.05517 433 MET A N   
3480 C  CA  . MET A 433 ? 0.47267 0.47523 0.39184 -0.04582 -0.04585 -0.05293 433 MET A CA  
3481 C  C   . MET A 433 ? 0.44158 0.45698 0.38054 -0.04829 -0.05143 -0.04667 433 MET A C   
3482 O  O   . MET A 433 ? 0.42709 0.44491 0.38090 -0.04623 -0.04730 -0.04427 433 MET A O   
3483 C  CB  . MET A 433 ? 0.47377 0.47836 0.39559 -0.03821 -0.03625 -0.04960 433 MET A CB  
3484 C  CG  . MET A 433 ? 0.49715 0.49041 0.40480 -0.03430 -0.02803 -0.05527 433 MET A CG  
3485 S  SD  . MET A 433 ? 0.49767 0.47288 0.39684 -0.03535 -0.02520 -0.06522 433 MET A SD  
3486 C  CE  . MET A 433 ? 0.47738 0.45419 0.39720 -0.03898 -0.02865 -0.06325 433 MET A CE  
3487 N  N   . SER A 434 ? 0.34177 0.36581 0.28134 -0.05223 -0.06046 -0.04366 434 SER A N   
3488 C  CA  . SER A 434 ? 0.32581 0.36396 0.28540 -0.05297 -0.06457 -0.03686 434 SER A CA  
3489 C  C   . SER A 434 ? 0.32626 0.37126 0.28679 -0.06000 -0.07618 -0.03611 434 SER A C   
3490 O  O   . SER A 434 ? 0.33663 0.37475 0.28039 -0.06455 -0.08177 -0.04087 434 SER A O   
3491 C  CB  . SER A 434 ? 0.32461 0.37169 0.29023 -0.04632 -0.06155 -0.02964 434 SER A CB  
3492 O  OG  . SER A 434 ? 0.33569 0.38715 0.29193 -0.04670 -0.06763 -0.02680 434 SER A OG  
3493 N  N   . ASP A 435 ? 0.34577 0.40484 0.32626 -0.06076 -0.07978 -0.02993 435 ASP A N   
3494 C  CA  . ASP A 435 ? 0.34652 0.41710 0.33327 -0.06641 -0.09113 -0.02674 435 ASP A CA  
3495 C  C   . ASP A 435 ? 0.34592 0.43000 0.33953 -0.06107 -0.09384 -0.01846 435 ASP A C   
3496 O  O   . ASP A 435 ? 0.33925 0.43806 0.34880 -0.06254 -0.10034 -0.01277 435 ASP A O   
3497 C  CB  . ASP A 435 ? 0.31921 0.39703 0.32541 -0.07194 -0.09356 -0.02552 435 ASP A CB  
3498 C  CG  . ASP A 435 ? 0.30642 0.39270 0.33216 -0.06594 -0.08558 -0.01999 435 ASP A CG  
3499 O  OD1 . ASP A 435 ? 0.31070 0.39536 0.33423 -0.05789 -0.07849 -0.01797 435 ASP A OD1 
3500 O  OD2 . ASP A 435 ? 0.28974 0.38393 0.33251 -0.06970 -0.08638 -0.01765 435 ASP A OD2 
3501 N  N   . TYR A 436 ? 0.31381 0.39298 0.29608 -0.05477 -0.08882 -0.01731 436 TYR A N   
3502 C  CA  . TYR A 436 ? 0.32137 0.41008 0.30889 -0.04899 -0.09031 -0.00934 436 TYR A CA  
3503 C  C   . TYR A 436 ? 0.33774 0.42971 0.31317 -0.05153 -0.10036 -0.00703 436 TYR A C   
3504 O  O   . TYR A 436 ? 0.33269 0.43710 0.31868 -0.04963 -0.10665 0.00028  436 TYR A O   
3505 C  CB  . TYR A 436 ? 0.32003 0.40146 0.30148 -0.04188 -0.08055 -0.00839 436 TYR A CB  
3506 C  CG  . TYR A 436 ? 0.30806 0.38945 0.30369 -0.03748 -0.07190 -0.00760 436 TYR A CG  
3507 C  CD1 . TYR A 436 ? 0.29317 0.38538 0.30838 -0.03541 -0.07256 -0.00290 436 TYR A CD1 
3508 C  CD2 . TYR A 436 ? 0.30722 0.37817 0.29627 -0.03506 -0.06302 -0.01125 436 TYR A CD2 
3509 C  CE1 . TYR A 436 ? 0.27898 0.37001 0.30434 -0.03136 -0.06459 -0.00243 436 TYR A CE1 
3510 C  CE2 . TYR A 436 ? 0.29466 0.36517 0.29503 -0.03141 -0.05612 -0.01039 436 TYR A CE2 
3511 C  CZ  . TYR A 436 ? 0.27905 0.35882 0.29629 -0.02969 -0.05695 -0.00622 436 TYR A CZ  
3512 O  OH  . TYR A 436 ? 0.27149 0.34972 0.29734 -0.02607 -0.05005 -0.00564 436 TYR A OH  
3513 N  N   . CYS A 437 ? 0.38874 0.46940 0.34153 -0.05537 -0.10190 -0.01301 437 CYS A N   
3514 C  CA  . CYS A 437 ? 0.41477 0.49550 0.35060 -0.05588 -0.10874 -0.01036 437 CYS A CA  
3515 C  C   . CYS A 437 ? 0.40168 0.49305 0.34154 -0.06190 -0.12297 -0.00759 437 CYS A C   
3516 O  O   . CYS A 437 ? 0.40753 0.50557 0.34355 -0.06034 -0.12995 -0.00107 437 CYS A O   
3517 C  CB  . CYS A 437 ? 0.42689 0.49185 0.33569 -0.05761 -0.10483 -0.01790 437 CYS A CB  
3518 S  SG  . CYS A 437 ? 0.43091 0.48633 0.33534 -0.05016 -0.08889 -0.01927 437 CYS A SG  
3519 N  N   . LYS A 438 ? 0.46462 0.55789 0.41244 -0.06912 -0.12803 -0.01182 438 LYS A N   
3520 C  CA  . LYS A 438 ? 0.47119 0.57615 0.42501 -0.07550 -0.14224 -0.00865 438 LYS A CA  
3521 C  C   . LYS A 438 ? 0.46112 0.58549 0.44148 -0.07029 -0.14466 0.00180  438 LYS A C   
3522 O  O   . LYS A 438 ? 0.46608 0.59917 0.45043 -0.06947 -0.15243 0.00675  438 LYS A O   
3523 C  CB  . LYS A 438 ? 0.51179 0.61249 0.46989 -0.08360 -0.14495 -0.01566 438 LYS A CB  
3524 C  CG  . LYS A 438 ? 0.52997 0.60993 0.46085 -0.08845 -0.14392 -0.02662 438 LYS A CG  
3525 C  CD  . LYS A 438 ? 0.52873 0.59440 0.44920 -0.08572 -0.13210 -0.03250 438 LYS A CD  
3526 C  CE  . LYS A 438 ? 0.55450 0.60029 0.44325 -0.08787 -0.13066 -0.04197 438 LYS A CE  
3527 N  NZ  . LYS A 438 ? 0.57197 0.61737 0.44141 -0.08437 -0.13280 -0.03911 438 LYS A NZ  
3528 N  N   . GLY A 439 ? 0.48926 0.61816 0.48778 -0.06459 -0.13548 0.00455  439 GLY A N   
3529 C  CA  . GLY A 439 ? 0.48742 0.63293 0.50879 -0.05804 -0.13621 0.01417  439 GLY A CA  
3530 C  C   . GLY A 439 ? 0.49121 0.63481 0.50637 -0.04893 -0.13303 0.02006  439 GLY A C   
3531 O  O   . GLY A 439 ? 0.49043 0.64607 0.52277 -0.04254 -0.13400 0.02817  439 GLY A O   
3532 N  N   . CYS A 440 ? 0.32806 0.45665 0.31943 -0.04810 -0.12896 0.01644  440 CYS A N   
3533 C  CA  . CYS A 440 ? 0.33004 0.45503 0.31437 -0.04049 -0.12538 0.02217  440 CYS A CA  
3534 C  C   . CYS A 440 ? 0.34300 0.47402 0.31923 -0.04099 -0.13711 0.02882  440 CYS A C   
3535 O  O   . CYS A 440 ? 0.34218 0.47384 0.30698 -0.04815 -0.14665 0.02625  440 CYS A O   
3536 C  CB  . CYS A 440 ? 0.34360 0.45176 0.30718 -0.03984 -0.11579 0.01649  440 CYS A CB  
3537 S  SG  . CYS A 440 ? 0.34025 0.44266 0.29693 -0.03159 -0.10956 0.02352  440 CYS A SG  
3538 N  N   . ARG A 441 ? 0.48947 0.62366 0.47092 -0.03321 -0.13655 0.03747  441 ARG A N   
3539 C  CA  . ARG A 441 ? 0.49201 0.63076 0.46524 -0.03249 -0.14717 0.04504  441 ARG A CA  
3540 C  C   . ARG A 441 ? 0.50171 0.62672 0.44402 -0.03573 -0.14703 0.04227  441 ARG A C   
3541 O  O   . ARG A 441 ? 0.51629 0.64050 0.44682 -0.03707 -0.15401 0.04376  441 ARG A O   
3542 C  CB  . ARG A 441 ? 0.49111 0.63500 0.47853 -0.02264 -0.14590 0.05520  441 ARG A CB  
3543 C  CG  . ARG A 441 ? 0.50142 0.63992 0.47422 -0.01884 -0.14964 0.06238  441 ARG A CG  
3544 C  CD  . ARG A 441 ? 0.50602 0.63010 0.46384 -0.01592 -0.14054 0.06336  441 ARG A CD  
3545 N  NE  . ARG A 441 ? 0.51503 0.63568 0.46276 -0.01182 -0.14473 0.07303  441 ARG A NE  
3546 C  CZ  . ARG A 441 ? 0.52969 0.64783 0.46068 -0.01418 -0.15086 0.07438  441 ARG A CZ  
3547 N  NH1 . ARG A 441 ? 0.53751 0.65675 0.45804 -0.02121 -0.15545 0.06732  441 ARG A NH1 
3548 N  NH2 . ARG A 441 ? 0.54299 0.65635 0.46690 -0.00933 -0.15246 0.08301  441 ARG A NH2 
3549 N  N   . TYR A 442 ? 0.35139 0.46324 0.28182 -0.03526 -0.13557 0.03668  442 TYR A N   
3550 C  CA  . TYR A 442 ? 0.36482 0.46446 0.26657 -0.03788 -0.13347 0.03397  442 TYR A CA  
3551 C  C   . TYR A 442 ? 0.37363 0.46825 0.25987 -0.04614 -0.13689 0.02407  442 TYR A C   
3552 O  O   . TYR A 442 ? 0.37725 0.47564 0.27567 -0.05009 -0.13874 0.01852  442 TYR A O   
3553 C  CB  . TYR A 442 ? 0.36596 0.45483 0.26339 -0.03374 -0.11928 0.03242  442 TYR A CB  
3554 C  CG  . TYR A 442 ? 0.36703 0.45686 0.27442 -0.02649 -0.11629 0.04186  442 TYR A CG  
3555 C  CD1 . TYR A 442 ? 0.36578 0.45419 0.26117 -0.02461 -0.12094 0.05050  442 TYR A CD1 
3556 C  CD2 . TYR A 442 ? 0.35131 0.44199 0.27872 -0.02165 -0.10902 0.04213  442 TYR A CD2 
3557 C  CE1 . TYR A 442 ? 0.36552 0.45252 0.26942 -0.01815 -0.11842 0.05912  442 TYR A CE1 
3558 C  CE2 . TYR A 442 ? 0.34669 0.43570 0.28157 -0.01520 -0.10654 0.04999  442 TYR A CE2 
3559 C  CZ  . TYR A 442 ? 0.35987 0.44664 0.28338 -0.01350 -0.11127 0.05844  442 TYR A CZ  
3560 O  OH  . TYR A 442 ? 0.35374 0.43668 0.28416 -0.00726 -0.10902 0.06627  442 TYR A OH  
3561 N  N   . ASP A 443 ? 0.50398 0.58905 0.36205 -0.04880 -0.13751 0.02199  443 ASP A N   
3562 C  CA  . ASP A 443 ? 0.51456 0.59022 0.35416 -0.05480 -0.13847 0.01148  443 ASP A CA  
3563 C  C   . ASP A 443 ? 0.52740 0.58997 0.35020 -0.05429 -0.12569 0.00483  443 ASP A C   
3564 O  O   . ASP A 443 ? 0.53918 0.59589 0.34509 -0.05140 -0.11996 0.00790  443 ASP A O   
3565 C  CB  . ASP A 443 ? 0.53515 0.60847 0.35713 -0.05582 -0.14616 0.01285  443 ASP A CB  
3566 C  CG  . ASP A 443 ? 0.55934 0.62367 0.36500 -0.06194 -0.14902 0.00189  443 ASP A CG  
3567 O  OD1 . ASP A 443 ? 0.55763 0.61370 0.35980 -0.06469 -0.14277 -0.00716 443 ASP A OD1 
3568 O  OD2 . ASP A 443 ? 0.57081 0.63572 0.36684 -0.06387 -0.15771 0.00231  443 ASP A OD2 
3569 N  N   . VAL A 444 ? 0.46515 0.52292 0.29496 -0.05599 -0.11977 -0.00406 444 VAL A N   
3570 C  CA  . VAL A 444 ? 0.48196 0.52796 0.30172 -0.05349 -0.10587 -0.01060 444 VAL A CA  
3571 C  C   . VAL A 444 ? 0.50188 0.53537 0.28920 -0.05628 -0.10467 -0.01718 444 VAL A C   
3572 O  O   . VAL A 444 ? 0.51190 0.53666 0.28860 -0.05308 -0.09246 -0.02113 444 VAL A O   
3573 C  CB  . VAL A 444 ? 0.47973 0.52364 0.31606 -0.05430 -0.10077 -0.01775 444 VAL A CB  
3574 C  CG1 . VAL A 444 ? 0.48111 0.51574 0.30355 -0.06117 -0.10562 -0.02805 444 VAL A CG1 
3575 C  CG2 . VAL A 444 ? 0.47714 0.51536 0.31656 -0.04868 -0.08592 -0.01938 444 VAL A CG2 
3576 N  N   . LYS A 445 ? 0.51497 0.54755 0.28672 -0.06165 -0.11661 -0.01838 445 LYS A N   
3577 C  CA  . LYS A 445 ? 0.54228 0.56199 0.28492 -0.06212 -0.11409 -0.02483 445 LYS A CA  
3578 C  C   . LYS A 445 ? 0.55713 0.57768 0.28381 -0.05853 -0.11304 -0.01686 445 LYS A C   
3579 O  O   . LYS A 445 ? 0.57635 0.58758 0.27815 -0.05836 -0.11111 -0.02105 445 LYS A O   
3580 C  CB  . LYS A 445 ? 0.59335 0.61007 0.33258 -0.06722 -0.12460 -0.03133 445 LYS A CB  
3581 C  CG  . LYS A 445 ? 0.58799 0.59959 0.33767 -0.07140 -0.12433 -0.04062 445 LYS A CG  
3582 C  CD  . LYS A 445 ? 0.59835 0.61231 0.35358 -0.07741 -0.13698 -0.04355 445 LYS A CD  
3583 C  CE  . LYS A 445 ? 0.59050 0.62115 0.36087 -0.07736 -0.14798 -0.03281 445 LYS A CE  
3584 N  NZ  . LYS A 445 ? 0.56349 0.60871 0.36616 -0.07693 -0.14967 -0.02643 445 LYS A NZ  
3585 N  N   . LYS A 446 ? 0.58515 0.61594 0.32527 -0.05542 -0.11397 -0.00541 446 LYS A N   
3586 C  CA  . LYS A 446 ? 0.59585 0.62706 0.32294 -0.05208 -0.11294 0.00356  446 LYS A CA  
3587 C  C   . LYS A 446 ? 0.59192 0.62411 0.32219 -0.04859 -0.10163 0.00974  446 LYS A C   
3588 O  O   . LYS A 446 ? 0.57334 0.60981 0.32832 -0.04595 -0.09644 0.00985  446 LYS A O   
3589 C  CB  . LYS A 446 ? 0.57474 0.61641 0.31458 -0.05118 -0.12543 0.01314  446 LYS A CB  
3590 C  CG  . LYS A 446 ? 0.59779 0.64074 0.33492 -0.05499 -0.13737 0.00868  446 LYS A CG  
3591 C  CD  . LYS A 446 ? 0.59150 0.64667 0.34449 -0.05329 -0.14878 0.01885  446 LYS A CD  
3592 C  CE  . LYS A 446 ? 0.61958 0.67514 0.36159 -0.05668 -0.16005 0.01649  446 LYS A CE  
3593 N  NZ  . LYS A 446 ? 0.61966 0.68714 0.37544 -0.05411 -0.17042 0.02723  446 LYS A NZ  
3594 N  N   . ARG A 447 ? 0.57746 0.60520 0.28895 -0.04632 -0.09546 0.01451  447 ARG A N   
3595 C  CA  . ARG A 447 ? 0.56423 0.59262 0.28031 -0.04257 -0.08351 0.02102  447 ARG A CA  
3596 C  C   . ARG A 447 ? 0.56960 0.60222 0.28595 -0.04081 -0.08759 0.03491  447 ARG A C   
3597 O  O   . ARG A 447 ? 0.55947 0.59461 0.29273 -0.03733 -0.08119 0.04151  447 ARG A O   
3598 C  CB  . ARG A 447 ? 0.58595 0.60567 0.27953 -0.04185 -0.07003 0.01556  447 ARG A CB  
3599 C  CG  . ARG A 447 ? 0.58453 0.60592 0.28787 -0.03780 -0.05595 0.02114  447 ARG A CG  
3600 C  CD  . ARG A 447 ? 0.61314 0.62810 0.29259 -0.03689 -0.04316 0.01747  447 ARG A CD  
3601 N  NE  . ARG A 447 ? 0.62521 0.63293 0.29524 -0.03729 -0.03993 0.00375  447 ARG A NE  
3602 C  CZ  . ARG A 447 ? 0.64608 0.64561 0.28918 -0.03672 -0.03195 -0.00247 447 ARG A CZ  
3603 N  NH1 . ARG A 447 ? 0.65929 0.65806 0.28437 -0.03509 -0.02565 0.00390  447 ARG A NH1 
3604 N  NH2 . ARG A 447 ? 0.65617 0.64735 0.29239 -0.03668 -0.02960 -0.01537 447 ARG A NH2 
3605 N  N   . LEU A 448 ? 0.53339 0.56510 0.23811 -0.04077 -0.09638 0.03830  448 LEU A N   
3606 C  CA  . LEU A 448 ? 0.52553 0.55949 0.23152 -0.03797 -0.10027 0.05110  448 LEU A CA  
3607 C  C   . LEU A 448 ? 0.51915 0.56059 0.24130 -0.03713 -0.11481 0.05477  448 LEU A C   
3608 O  O   . LEU A 448 ? 0.52248 0.56682 0.24871 -0.03961 -0.12243 0.04735  448 LEU A O   
3609 C  CB  . LEU A 448 ? 0.55237 0.57930 0.23048 -0.03750 -0.09696 0.05341  448 LEU A CB  
3610 C  CG  . LEU A 448 ? 0.56471 0.58463 0.22391 -0.03797 -0.08232 0.04745  448 LEU A CG  
3611 C  CD1 . LEU A 448 ? 0.59379 0.60759 0.22537 -0.03694 -0.07996 0.04970  448 LEU A CD1 
3612 C  CD2 . LEU A 448 ? 0.55958 0.58156 0.23046 -0.03707 -0.07070 0.05300  448 LEU A CD2 
3613 N  N   . GLY A 449 ? 0.60003 0.64452 0.33221 -0.03349 -0.11821 0.06651  449 GLY A N   
3614 C  CA  . GLY A 449 ? 0.58152 0.63395 0.33076 -0.03120 -0.13065 0.07151  449 GLY A CA  
3615 C  C   . GLY A 449 ? 0.56526 0.62513 0.34418 -0.02876 -0.13147 0.07327  449 GLY A C   
3616 O  O   . GLY A 449 ? 0.54524 0.60450 0.33160 -0.02970 -0.12374 0.06927  449 GLY A O   
3617 N  N   . ASP A 450 ? 0.66815 0.73560 0.46431 -0.02509 -0.14091 0.07946  450 ASP A N   
3618 C  CA  . ASP A 450 ? 0.64758 0.72218 0.47220 -0.02124 -0.14145 0.08213  450 ASP A CA  
3619 C  C   . ASP A 450 ? 0.63196 0.71355 0.47031 -0.02456 -0.14237 0.07237  450 ASP A C   
3620 O  O   . ASP A 450 ? 0.61565 0.70093 0.47312 -0.02255 -0.13864 0.07205  450 ASP A O   
3621 C  CB  . ASP A 450 ? 0.64667 0.72764 0.48578 -0.01546 -0.15039 0.09120  450 ASP A CB  
3622 C  CG  . ASP A 450 ? 0.67807 0.75090 0.50785 -0.01127 -0.14866 0.10196  450 ASP A CG  
3623 O  OD1 . ASP A 450 ? 0.67409 0.73760 0.49281 -0.01234 -0.13948 0.10348  450 ASP A OD1 
3624 O  OD2 . ASP A 450 ? 0.68310 0.75893 0.51697 -0.00707 -0.15641 0.10917  450 ASP A OD2 
3625 N  N   . ASP A 451 ? 0.56924 0.65194 0.39796 -0.02968 -0.14729 0.06446  451 ASP A N   
3626 C  CA  . ASP A 451 ? 0.55247 0.64032 0.39330 -0.03368 -0.14830 0.05517  451 ASP A CA  
3627 C  C   . ASP A 451 ? 0.54421 0.62384 0.37413 -0.03747 -0.13837 0.04630  451 ASP A C   
3628 O  O   . ASP A 451 ? 0.54334 0.62580 0.38419 -0.04049 -0.13776 0.03891  451 ASP A O   
3629 C  CB  . ASP A 451 ? 0.56504 0.65627 0.40063 -0.03813 -0.15818 0.05029  451 ASP A CB  
3630 C  CG  . ASP A 451 ? 0.56391 0.66493 0.41106 -0.03461 -0.16850 0.05885  451 ASP A CG  
3631 O  OD1 . ASP A 451 ? 0.54585 0.65737 0.41935 -0.03050 -0.17043 0.06364  451 ASP A OD1 
3632 O  OD2 . ASP A 451 ? 0.60095 0.69924 0.43060 -0.03553 -0.17436 0.06078  451 ASP A OD2 
3633 N  N   . ALA A 452 ? 0.43173 0.50166 0.24115 -0.03728 -0.13018 0.04711  452 ALA A N   
3634 C  CA  . ALA A 452 ? 0.44075 0.50262 0.23941 -0.03982 -0.11930 0.03801  452 ALA A CA  
3635 C  C   . ALA A 452 ? 0.43119 0.49440 0.25482 -0.03601 -0.10973 0.03587  452 ALA A C   
3636 O  O   . ALA A 452 ? 0.41659 0.48283 0.25618 -0.03116 -0.10800 0.04344  452 ALA A O   
3637 C  CB  . ALA A 452 ? 0.45639 0.50923 0.23052 -0.03926 -0.11115 0.04060  452 ALA A CB  
3638 N  N   . CYS A 453 ? 0.39209 0.45184 0.21788 -0.03818 -0.10382 0.02545  453 CYS A N   
3639 C  CA  . CYS A 453 ? 0.38271 0.44243 0.22863 -0.03495 -0.09421 0.02287  453 CYS A CA  
3640 C  C   . CYS A 453 ? 0.38691 0.44128 0.22892 -0.03139 -0.08323 0.02702  453 CYS A C   
3641 O  O   . CYS A 453 ? 0.40536 0.45330 0.22763 -0.03266 -0.07714 0.02471  453 CYS A O   
3642 C  CB  . CYS A 453 ? 0.38259 0.43795 0.22789 -0.03806 -0.09001 0.01139  453 CYS A CB  
3643 S  SG  . CYS A 453 ? 0.38036 0.43248 0.24157 -0.03432 -0.07612 0.00760  453 CYS A SG  
3644 N  N   . PRO A 454 ? 0.36162 0.41815 0.22125 -0.02714 -0.08032 0.03322  454 PRO A N   
3645 C  CA  . PRO A 454 ? 0.36547 0.41683 0.22087 -0.02506 -0.07139 0.03831  454 PRO A CA  
3646 C  C   . PRO A 454 ? 0.38446 0.43127 0.23567 -0.02584 -0.05972 0.03154  454 PRO A C   
3647 O  O   . PRO A 454 ? 0.38729 0.43069 0.22779 -0.02584 -0.05273 0.03493  454 PRO A O   
3648 C  CB  . PRO A 454 ? 0.35650 0.40964 0.23317 -0.02081 -0.07156 0.04418  454 PRO A CB  
3649 C  CG  . PRO A 454 ? 0.34839 0.40876 0.23868 -0.01973 -0.08056 0.04378  454 PRO A CG  
3650 C  CD  . PRO A 454 ? 0.34772 0.41128 0.23013 -0.02416 -0.08583 0.03674  454 PRO A CD  
3651 N  N   . PHE A 455 ? 0.31162 0.35869 0.17113 -0.02645 -0.05737 0.02266  455 PHE A N   
3652 C  CA  . PHE A 455 ? 0.31667 0.35973 0.17367 -0.02628 -0.04649 0.01649  455 PHE A CA  
3653 C  C   . PHE A 455 ? 0.34229 0.38073 0.17484 -0.02794 -0.04241 0.01364  455 PHE A C   
3654 O  O   . PHE A 455 ? 0.35158 0.38775 0.18022 -0.02670 -0.03190 0.01200  455 PHE A O   
3655 C  CB  . PHE A 455 ? 0.30962 0.35264 0.17806 -0.02673 -0.04616 0.00775  455 PHE A CB  
3656 C  CG  . PHE A 455 ? 0.29041 0.33640 0.18165 -0.02424 -0.04453 0.00934  455 PHE A CG  
3657 C  CD1 . PHE A 455 ? 0.28815 0.33912 0.19311 -0.02358 -0.05205 0.01205  455 PHE A CD1 
3658 C  CD2 . PHE A 455 ? 0.27983 0.32399 0.17849 -0.02238 -0.03544 0.00816  455 PHE A CD2 
3659 C  CE1 . PHE A 455 ? 0.26490 0.31753 0.18840 -0.02090 -0.04982 0.01307  455 PHE A CE1 
3660 C  CE2 . PHE A 455 ? 0.26323 0.30899 0.18028 -0.02038 -0.03446 0.00930  455 PHE A CE2 
3661 C  CZ  . PHE A 455 ? 0.25547 0.30474 0.18385 -0.01954 -0.04130 0.01147  455 PHE A CZ  
3662 N  N   . ASN A 456 ? 0.41599 0.45332 0.23175 -0.03058 -0.05051 0.01316  456 ASN A N   
3663 C  CA  . ASN A 456 ? 0.44178 0.47306 0.23127 -0.03217 -0.04691 0.00882  456 ASN A CA  
3664 C  C   . ASN A 456 ? 0.45501 0.48581 0.23249 -0.03088 -0.03972 0.01667  456 ASN A C   
3665 O  O   . ASN A 456 ? 0.47261 0.50073 0.24182 -0.02955 -0.02831 0.01400  456 ASN A O   
3666 C  CB  . ASN A 456 ? 0.44926 0.47908 0.22320 -0.03608 -0.05908 0.00638  456 ASN A CB  
3667 C  CG  . ASN A 456 ? 0.44377 0.47191 0.22426 -0.03871 -0.06400 -0.00339 456 ASN A CG  
3668 O  OD1 . ASN A 456 ? 0.43901 0.46415 0.22845 -0.03737 -0.05646 -0.00999 456 ASN A OD1 
3669 N  ND2 . ASN A 456 ? 0.43862 0.46887 0.21517 -0.04278 -0.07709 -0.00379 456 ASN A ND2 
3670 N  N   . ALA A 457 ? 0.36778 0.40137 0.14472 -0.03112 -0.04599 0.02696  457 ALA A N   
3671 C  CA  . ALA A 457 ? 0.37930 0.41199 0.14504 -0.03066 -0.03949 0.03565  457 ALA A CA  
3672 C  C   . ALA A 457 ? 0.36136 0.39619 0.14496 -0.02869 -0.02914 0.03903  457 ALA A C   
3673 O  O   . ALA A 457 ? 0.37635 0.41091 0.15170 -0.02866 -0.01915 0.04232  457 ALA A O   
3674 C  CB  . ALA A 457 ? 0.38847 0.42231 0.14989 -0.03128 -0.04952 0.04645  457 ALA A CB  
3675 N  N   . LEU A 458 ? 0.34785 0.38518 0.15565 -0.02728 -0.03138 0.03848  458 LEU A N   
3676 C  CA  . LEU A 458 ? 0.34420 0.38303 0.16872 -0.02607 -0.02299 0.04114  458 LEU A CA  
3677 C  C   . LEU A 458 ? 0.35439 0.39385 0.17858 -0.02528 -0.01198 0.03369  458 LEU A C   
3678 O  O   . LEU A 458 ? 0.36708 0.40884 0.19688 -0.02503 -0.00299 0.03742  458 LEU A O   
3679 C  CB  . LEU A 458 ? 0.31959 0.35968 0.16724 -0.02454 -0.02829 0.04122  458 LEU A CB  
3680 C  CG  . LEU A 458 ? 0.31205 0.35136 0.16435 -0.02379 -0.03711 0.04997  458 LEU A CG  
3681 C  CD1 . LEU A 458 ? 0.28944 0.33014 0.16224 -0.02142 -0.04208 0.04765  458 LEU A CD1 
3682 C  CD2 . LEU A 458 ? 0.32430 0.36082 0.17622 -0.02446 -0.03294 0.05995  458 LEU A CD2 
3683 N  N   . TYR A 459 ? 0.41640 0.45377 0.23480 -0.02490 -0.01268 0.02354  459 TYR A N   
3684 C  CA  . TYR A 459 ? 0.43219 0.46888 0.24954 -0.02309 -0.00216 0.01628  459 TYR A CA  
3685 C  C   . TYR A 459 ? 0.46165 0.49788 0.25937 -0.02272 0.00718  0.01834  459 TYR A C   
3686 O  O   . TYR A 459 ? 0.47593 0.51591 0.27955 -0.02094 0.01817  0.01977  459 TYR A O   
3687 C  CB  . TYR A 459 ? 0.42926 0.46125 0.24275 -0.02302 -0.00571 0.00506  459 TYR A CB  
3688 C  CG  . TYR A 459 ? 0.45066 0.47910 0.25664 -0.02049 0.00479  -0.00298 459 TYR A CG  
3689 C  CD1 . TYR A 459 ? 0.44556 0.47687 0.26906 -0.01755 0.01271  -0.00459 459 TYR A CD1 
3690 C  CD2 . TYR A 459 ? 0.47888 0.50053 0.25959 -0.02063 0.00669  -0.00895 459 TYR A CD2 
3691 C  CE1 . TYR A 459 ? 0.46783 0.49611 0.28577 -0.01412 0.02253  -0.01145 459 TYR A CE1 
3692 C  CE2 . TYR A 459 ? 0.49619 0.51328 0.26953 -0.01719 0.01707  -0.01665 459 TYR A CE2 
3693 C  CZ  . TYR A 459 ? 0.48737 0.50820 0.28035 -0.01359 0.02513  -0.01761 459 TYR A CZ  
3694 O  OH  . TYR A 459 ? 0.50432 0.52090 0.29139 -0.00911 0.03565  -0.02477 459 TYR A OH  
3695 N  N   . TRP A 460 ? 0.47276 0.50511 0.24700 -0.02440 0.00297  0.01890  460 TRP A N   
3696 C  CA  . TRP A 460 ? 0.49647 0.52759 0.24868 -0.02383 0.01241  0.02029  460 TRP A CA  
3697 C  C   . TRP A 460 ? 0.49513 0.53185 0.25142 -0.02471 0.01799  0.03277  460 TRP A C   
3698 O  O   . TRP A 460 ? 0.51487 0.55431 0.26377 -0.02352 0.03012  0.03485  460 TRP A O   
3699 C  CB  . TRP A 460 ? 0.50066 0.52508 0.22455 -0.02585 0.00526  0.01747  460 TRP A CB  
3700 C  CG  . TRP A 460 ? 0.51365 0.53074 0.22777 -0.02533 0.00375  0.00416  460 TRP A CG  
3701 C  CD1 . TRP A 460 ? 0.50178 0.51456 0.21282 -0.02814 -0.00907 -0.00148 460 TRP A CD1 
3702 C  CD2 . TRP A 460 ? 0.52231 0.53505 0.22952 -0.02182 0.01545  -0.00500 460 TRP A CD2 
3703 N  NE1 . TRP A 460 ? 0.51060 0.51519 0.21209 -0.02742 -0.00647 -0.01379 460 TRP A NE1 
3704 C  CE2 . TRP A 460 ? 0.52807 0.53173 0.22653 -0.02300 0.00869  -0.01637 460 TRP A CE2 
3705 C  CE3 . TRP A 460 ? 0.53546 0.55139 0.24381 -0.01766 0.03104  -0.00435 460 TRP A CE3 
3706 C  CZ2 . TRP A 460 ? 0.53453 0.52994 0.22390 -0.01977 0.01703  -0.02747 460 TRP A CZ2 
3707 C  CZ3 . TRP A 460 ? 0.55473 0.56429 0.25527 -0.01364 0.03972  -0.01510 460 TRP A CZ3 
3708 C  CH2 . TRP A 460 ? 0.55087 0.54916 0.24130 -0.01453 0.03272  -0.02675 460 TRP A CH2 
3709 N  N   . ASP A 461 ? 0.46086 0.49910 0.22909 -0.02673 0.00970  0.04134  461 ASP A N   
3710 C  CA  . ASP A 461 ? 0.46332 0.50532 0.23829 -0.02825 0.01453  0.05318  461 ASP A CA  
3711 C  C   . ASP A 461 ? 0.46060 0.50853 0.25743 -0.02727 0.02390  0.05296  461 ASP A C   
3712 O  O   . ASP A 461 ? 0.47058 0.52329 0.26915 -0.02847 0.03300  0.06020  461 ASP A O   
3713 C  CB  . ASP A 461 ? 0.45283 0.49273 0.23600 -0.02994 0.00308  0.06146  461 ASP A CB  
3714 C  CG  . ASP A 461 ? 0.46136 0.50210 0.24705 -0.03235 0.00676  0.07434  461 ASP A CG  
3715 O  OD1 . ASP A 461 ? 0.47430 0.51440 0.24039 -0.03389 0.01060  0.08051  461 ASP A OD1 
3716 O  OD2 . ASP A 461 ? 0.44851 0.48975 0.25489 -0.03305 0.00579  0.07836  461 ASP A OD2 
3717 N  N   . PHE A 462 ? 0.36707 0.41536 0.18098 -0.02543 0.02157  0.04525  462 PHE A N   
3718 C  CA  . PHE A 462 ? 0.36602 0.42010 0.20039 -0.02436 0.02930  0.04463  462 PHE A CA  
3719 C  C   . PHE A 462 ? 0.38058 0.43902 0.20758 -0.02183 0.04256  0.04131  462 PHE A C   
3720 O  O   . PHE A 462 ? 0.38102 0.44706 0.21768 -0.02229 0.05155  0.04724  462 PHE A O   
3721 C  CB  . PHE A 462 ? 0.34988 0.40240 0.20075 -0.02266 0.02361  0.03685  462 PHE A CB  
3722 C  CG  . PHE A 462 ? 0.35126 0.40934 0.22240 -0.02140 0.03012  0.03581  462 PHE A CG  
3723 C  CD1 . PHE A 462 ? 0.33861 0.39924 0.22752 -0.02372 0.02825  0.04264  462 PHE A CD1 
3724 C  CD2 . PHE A 462 ? 0.35699 0.41687 0.22902 -0.01783 0.03748  0.02797  462 PHE A CD2 
3725 C  CE1 . PHE A 462 ? 0.31728 0.38343 0.22443 -0.02308 0.03294  0.04196  462 PHE A CE1 
3726 C  CE2 . PHE A 462 ? 0.34688 0.41271 0.23827 -0.01636 0.04265  0.02778  462 PHE A CE2 
3727 C  CZ  . PHE A 462 ? 0.31923 0.38882 0.22823 -0.01928 0.04001  0.03490  462 PHE A CZ  
3728 N  N   . ILE A 463 ? 0.46229 0.51589 0.27244 -0.01910 0.04398  0.03184  463 ILE A N   
3729 C  CA  . ILE A 463 ? 0.46217 0.51818 0.26298 -0.01539 0.05727  0.02774  463 ILE A CA  
3730 C  C   . ILE A 463 ? 0.47814 0.53821 0.26433 -0.01677 0.06543  0.03668  463 ILE A C   
3731 O  O   . ILE A 463 ? 0.47886 0.54663 0.26834 -0.01450 0.07851  0.03900  463 ILE A O   
3732 C  CB  . ILE A 463 ? 0.47265 0.51914 0.25490 -0.01259 0.05590  0.01523  463 ILE A CB  
3733 C  CG1 . ILE A 463 ? 0.45979 0.50202 0.25652 -0.01253 0.04643  0.00792  463 ILE A CG1 
3734 C  CG2 . ILE A 463 ? 0.49295 0.54040 0.26702 -0.00725 0.07050  0.00978  463 ILE A CG2 
3735 C  CD1 . ILE A 463 ? 0.45812 0.50218 0.27064 -0.00815 0.05360  0.00168  463 ILE A CD1 
3736 N  N   . ASP A 464 ? 0.52945 0.58511 0.29996 -0.02036 0.05802  0.04254  464 ASP A N   
3737 C  CA  . ASP A 464 ? 0.53735 0.59594 0.29221 -0.02219 0.06525  0.05210  464 ASP A CA  
3738 C  C   . ASP A 464 ? 0.53190 0.59962 0.30777 -0.02536 0.06963  0.06418  464 ASP A C   
3739 O  O   . ASP A 464 ? 0.53636 0.61140 0.30920 -0.02571 0.08164  0.07075  464 ASP A O   
3740 C  CB  . ASP A 464 ? 0.55398 0.60469 0.28640 -0.02516 0.05471  0.05566  464 ASP A CB  
3741 C  CG  . ASP A 464 ? 0.56550 0.61798 0.27876 -0.02721 0.06184  0.06605  464 ASP A CG  
3742 O  OD1 . ASP A 464 ? 0.58856 0.63844 0.27640 -0.02511 0.06918  0.06200  464 ASP A OD1 
3743 O  OD2 . ASP A 464 ? 0.56188 0.61737 0.28453 -0.03100 0.06028  0.07829  464 ASP A OD2 
3744 N  N   . ARG A 465 ? 0.63302 0.70019 0.42995 -0.02792 0.06017  0.06728  465 ARG A N   
3745 C  CA  . ARG A 465 ? 0.62154 0.69497 0.43771 -0.03195 0.06247  0.07833  465 ARG A CA  
3746 C  C   . ARG A 465 ? 0.61103 0.69595 0.44503 -0.03042 0.07442  0.07770  465 ARG A C   
3747 O  O   . ARG A 465 ? 0.60981 0.70328 0.44948 -0.03329 0.08302  0.08721  465 ARG A O   
3748 C  CB  . ARG A 465 ? 0.60752 0.67572 0.44072 -0.03412 0.04973  0.07961  465 ARG A CB  
3749 C  CG  . ARG A 465 ? 0.60003 0.67181 0.45273 -0.03887 0.05043  0.08981  465 ARG A CG  
3750 C  CD  . ARG A 465 ? 0.59672 0.65959 0.45870 -0.04064 0.03751  0.09183  465 ARG A CD  
3751 N  NE  . ARG A 465 ? 0.61319 0.66758 0.45835 -0.03896 0.02836  0.09044  465 ARG A NE  
3752 C  CZ  . ARG A 465 ? 0.61804 0.66743 0.44903 -0.04120 0.02508  0.09949  465 ARG A CZ  
3753 N  NH1 . ARG A 465 ? 0.61129 0.66220 0.44192 -0.04560 0.03055  0.11074  465 ARG A NH1 
3754 N  NH2 . ARG A 465 ? 0.61178 0.65486 0.42923 -0.03923 0.01577  0.09785  465 ARG A NH2 
3755 N  N   . HIS A 466 ? 0.41505 0.50085 0.25892 -0.02600 0.07495  0.06718  466 HIS A N   
3756 C  CA  . HIS A 466 ? 0.40242 0.49930 0.26655 -0.02381 0.08429  0.06637  466 HIS A CA  
3757 C  C   . HIS A 466 ? 0.41324 0.51345 0.26574 -0.01737 0.09669  0.05924  466 HIS A C   
3758 O  O   . HIS A 466 ? 0.40282 0.50863 0.26975 -0.01297 0.10209  0.05395  466 HIS A O   
3759 C  CB  . HIS A 466 ? 0.38442 0.47969 0.26958 -0.02305 0.07626  0.06070  466 HIS A CB  
3760 C  CG  . HIS A 466 ? 0.37438 0.46426 0.26912 -0.02820 0.06433  0.06599  466 HIS A CG  
3761 N  ND1 . HIS A 466 ? 0.36275 0.45699 0.26995 -0.03383 0.06433  0.07687  466 HIS A ND1 
3762 C  CD2 . HIS A 466 ? 0.37291 0.45296 0.26660 -0.02836 0.05238  0.06184  466 HIS A CD2 
3763 C  CE1 . HIS A 466 ? 0.35588 0.44147 0.26781 -0.03672 0.05294  0.07856  466 HIS A CE1 
3764 N  NE2 . HIS A 466 ? 0.36127 0.43905 0.26569 -0.03309 0.04596  0.06973  466 HIS A NE2 
3765 N  N   . ALA A 467 ? 0.56956 0.66561 0.39511 -0.01643 0.10133  0.05914  467 ALA A N   
3766 C  CA  . ALA A 467 ? 0.58183 0.67724 0.39139 -0.00970 0.11254  0.05063  467 ALA A CA  
3767 C  C   . ALA A 467 ? 0.57631 0.68683 0.40181 -0.00615 0.12809  0.05436  467 ALA A C   
3768 O  O   . ALA A 467 ? 0.58611 0.69812 0.41619 0.00072  0.13507  0.04598  467 ALA A O   
3769 C  CB  . ALA A 467 ? 0.60191 0.68982 0.37761 -0.01018 0.11442  0.05111  467 ALA A CB  
3770 N  N   . GLN A 468 ? 0.65851 0.78064 0.49365 -0.01079 0.13362  0.06742  468 GLN A N   
3771 C  CA  . GLN A 468 ? 0.64638 0.78560 0.49823 -0.00792 0.14878  0.07247  468 GLN A CA  
3772 C  C   . GLN A 468 ? 0.62749 0.77453 0.51087 -0.00599 0.14663  0.06994  468 GLN A C   
3773 O  O   . GLN A 468 ? 0.62550 0.78151 0.51854 0.00098  0.15754  0.06638  468 GLN A O   
3774 C  CB  . GLN A 468 ? 0.64322 0.78991 0.50171 -0.01537 0.15190  0.08643  468 GLN A CB  
3775 C  CG  . GLN A 468 ? 0.65865 0.81460 0.52246 -0.01299 0.16679  0.08821  468 GLN A CG  
3776 C  CD  . GLN A 468 ? 0.65024 0.81419 0.52646 -0.02124 0.16861  0.10192  468 GLN A CD  
3777 O  OE1 . GLN A 468 ? 0.66222 0.81801 0.52407 -0.02725 0.16323  0.10868  468 GLN A OE1 
3778 N  NE2 . GLN A 468 ? 0.63814 0.81771 0.54143 -0.02159 0.17559  0.10619  468 GLN A NE2 
3779 N  N   . ARG A 469 ? 0.67588 0.81934 0.57503 -0.01164 0.13273  0.07188  469 ARG A N   
3780 C  CA  . ARG A 469 ? 0.64946 0.79913 0.57641 -0.01030 0.12936  0.06958  469 ARG A CA  
3781 C  C   . ARG A 469 ? 0.65809 0.79942 0.58022 -0.00225 0.12864  0.05582  469 ARG A C   
3782 O  O   . ARG A 469 ? 0.64268 0.79221 0.58219 0.00303  0.13410  0.05319  469 ARG A O   
3783 C  CB  . ARG A 469 ? 0.63496 0.77984 0.57530 -0.01796 0.11455  0.07379  469 ARG A CB  
3784 C  CG  . ARG A 469 ? 0.60856 0.75980 0.57647 -0.01766 0.11033  0.07257  469 ARG A CG  
3785 C  CD  . ARG A 469 ? 0.59418 0.73572 0.56881 -0.02369 0.09504  0.07331  469 ARG A CD  
3786 N  NE  . ARG A 469 ? 0.56890 0.71973 0.56961 -0.02851 0.09178  0.07983  469 ARG A NE  
3787 C  CZ  . ARG A 469 ? 0.54724 0.70725 0.56742 -0.02533 0.09347  0.07759  469 ARG A CZ  
3788 N  NH1 . ARG A 469 ? 0.55083 0.71097 0.56846 -0.01673 0.09859  0.06874  469 ARG A NH1 
3789 N  NH2 . ARG A 469 ? 0.52598 0.69429 0.56834 -0.03108 0.08924  0.08448  469 ARG A NH2 
3790 N  N   . LEU A 470 ? 0.56835 0.69340 0.46745 -0.00140 0.12161  0.04743  470 LEU A N   
3791 C  CA  . LEU A 470 ? 0.57748 0.69260 0.47116 0.00496  0.11978  0.03450  470 LEU A CA  
3792 C  C   . LEU A 470 ? 0.58782 0.70469 0.47093 0.01357  0.13451  0.02867  470 LEU A C   
3793 O  O   . LEU A 470 ? 0.59394 0.70605 0.48057 0.01991  0.13594  0.01958  470 LEU A O   
3794 C  CB  . LEU A 470 ? 0.58659 0.68494 0.45907 0.00251  0.10796  0.02786  470 LEU A CB  
3795 C  CG  . LEU A 470 ? 0.57802 0.67276 0.46300 -0.00352 0.09317  0.03064  470 LEU A CG  
3796 C  CD1 . LEU A 470 ? 0.59425 0.67736 0.45854 -0.00727 0.08299  0.02947  470 LEU A CD1 
3797 C  CD2 . LEU A 470 ? 0.56680 0.65915 0.46865 -0.00099 0.08796  0.02392  470 LEU A CD2 
3798 N  N   . ALA A 471 ? 0.59647 0.71921 0.46600 0.01423  0.14585  0.03380  471 ALA A N   
3799 C  CA  . ALA A 471 ? 0.60919 0.73475 0.46955 0.02334  0.16185  0.02888  471 ALA A CA  
3800 C  C   . ALA A 471 ? 0.58444 0.72654 0.47531 0.02851  0.17059  0.03217  471 ALA A C   
3801 O  O   . ALA A 471 ? 0.57885 0.71816 0.47051 0.03717  0.17774  0.02377  471 ALA A O   
3802 C  CB  . ALA A 471 ? 0.61049 0.73838 0.45111 0.02164  0.17115  0.03422  471 ALA A CB  
3803 N  N   . GLY A 472 ? 0.96564 1.12343 0.88268 0.02252  0.16839  0.04395  472 GLY A N   
3804 C  CA  . GLY A 472 ? 0.94202 1.11548 0.89061 0.02593  0.17315  0.04733  472 GLY A CA  
3805 C  C   . GLY A 472 ? 0.92783 1.09545 0.88994 0.02902  0.16422  0.04026  472 GLY A C   
3806 O  O   . GLY A 472 ? 0.91077 1.08703 0.89102 0.03619  0.17037  0.03894  472 GLY A O   
3807 N  N   . ASN A 473 ? 0.90474 1.05721 0.85885 0.02362  0.14913  0.03577  473 ASN A N   
3808 C  CA  . ASN A 473 ? 0.89572 1.04031 0.86048 0.02564  0.13969  0.02868  473 ASN A CA  
3809 C  C   . ASN A 473 ? 0.89820 1.03392 0.85329 0.03607  0.14695  0.01744  473 ASN A C   
3810 O  O   . ASN A 473 ? 0.88099 1.02190 0.85445 0.04211  0.14969  0.01598  473 ASN A O   
3811 C  CB  . ASN A 473 ? 0.90429 1.03390 0.85843 0.01861  0.12408  0.02556  473 ASN A CB  
3812 C  CG  . ASN A 473 ? 0.88549 1.00683 0.84941 0.02012  0.11464  0.01876  473 ASN A CG  
3813 O  OD1 . ASN A 473 ? 0.89561 1.00367 0.84629 0.02457  0.11380  0.00858  473 ASN A OD1 
3814 N  ND2 . ASN A 473 ? 0.83844 0.96686 0.82472 0.01596  0.10734  0.02448  473 ASN A ND2 
3815 N  N   . GLY A 474 ? 0.80691 0.92825 0.73245 0.03827  0.14971  0.00948  474 GLY A N   
3816 C  CA  . GLY A 474 ? 0.82454 0.93523 0.73722 0.04808  0.15776  -0.00153 474 GLY A CA  
3817 C  C   . GLY A 474 ? 0.83306 0.92188 0.72951 0.04743  0.14710  -0.01318 474 GLY A C   
3818 O  O   . GLY A 474 ? 0.85265 0.92669 0.72376 0.05146  0.15108  -0.02277 474 GLY A O   
3819 N  N   . ARG A 475 ? 0.71272 0.79906 0.62302 0.04206  0.13359  -0.01246 475 ARG A N   
3820 C  CA  . ARG A 475 ? 0.71560 0.78350 0.61550 0.04099  0.12337  -0.02235 475 ARG A CA  
3821 C  C   . ARG A 475 ? 0.74492 0.80173 0.62141 0.03378  0.11422  -0.02500 475 ARG A C   
3822 O  O   . ARG A 475 ? 0.74197 0.78601 0.61274 0.03084  0.10377  -0.03139 475 ARG A O   
3823 C  CB  . ARG A 475 ? 0.69539 0.76590 0.61931 0.03838  0.11333  -0.01996 475 ARG A CB  
3824 C  CG  . ARG A 475 ? 0.66261 0.73673 0.60549 0.04635  0.11885  -0.02121 475 ARG A CG  
3825 C  CD  . ARG A 475 ? 0.65628 0.74952 0.61541 0.05142  0.13109  -0.01330 475 ARG A CD  
3826 N  NE  . ARG A 475 ? 0.63858 0.74837 0.61912 0.04476  0.12607  -0.00193 475 ARG A NE  
3827 C  CZ  . ARG A 475 ? 0.60670 0.72901 0.61370 0.04616  0.12521  0.00392  475 ARG A CZ  
3828 N  NH1 . ARG A 475 ? 0.58092 0.70263 0.59808 0.05470  0.12948  0.00046  475 ARG A NH1 
3829 N  NH2 . ARG A 475 ? 0.58237 0.71737 0.60556 0.03874  0.11948  0.01362  475 ARG A NH2 
3830 N  N   . MET A 476 ? 0.56520 0.62720 0.42882 0.03081  0.11774  -0.01962 476 MET A N   
3831 C  CA  . MET A 476 ? 0.58028 0.63371 0.42238 0.02414  0.10884  -0.02031 476 MET A CA  
3832 C  C   . MET A 476 ? 0.60603 0.65128 0.41741 0.02715  0.11697  -0.02563 476 MET A C   
3833 O  O   . MET A 476 ? 0.61451 0.65994 0.40893 0.02278  0.11539  -0.02144 476 MET A O   
3834 C  CB  . MET A 476 ? 0.56773 0.63255 0.41964 0.01709  0.10385  -0.00825 476 MET A CB  
3835 C  CG  . MET A 476 ? 0.53706 0.60591 0.41338 0.01288  0.09323  -0.00416 476 MET A CG  
3836 S  SD  . MET A 476 ? 0.54735 0.60124 0.41975 0.01040  0.07892  -0.01319 476 MET A SD  
3837 C  CE  . MET A 476 ? 0.54973 0.60396 0.41760 0.00217  0.06696  -0.00593 476 MET A CE  
3838 N  N   . MET A 477 ? 0.71571 0.75246 0.51837 0.03496  0.12574  -0.03502 477 MET A N   
3839 C  CA  . MET A 477 ? 0.72691 0.75626 0.50032 0.03937  0.13633  -0.04025 477 MET A CA  
3840 C  C   . MET A 477 ? 0.73913 0.75179 0.48191 0.03382  0.12605  -0.04703 477 MET A C   
3841 O  O   . MET A 477 ? 0.75752 0.76961 0.47753 0.03179  0.12865  -0.04460 477 MET A O   
3842 C  CB  . MET A 477 ? 0.76440 0.78704 0.53679 0.05000  0.14826  -0.04920 477 MET A CB  
3843 C  CG  . MET A 477 ? 0.78948 0.80108 0.53263 0.05359  0.15579  -0.05748 477 MET A CG  
3844 S  SD  . MET A 477 ? 0.78419 0.80199 0.54168 0.06476  0.17144  -0.06080 477 MET A SD  
3845 C  CE  . MET A 477 ? 0.75634 0.80130 0.55300 0.06591  0.17748  -0.04563 477 MET A CE  
3846 N  N   . MET A 478 ? 0.73412 0.73366 0.47616 0.03091  0.11398  -0.05495 478 MET A N   
3847 C  CA  . MET A 478 ? 0.76518 0.74939 0.47948 0.02526  0.10327  -0.06172 478 MET A CA  
3848 C  C   . MET A 478 ? 0.76647 0.75805 0.47761 0.01695  0.09307  -0.05247 478 MET A C   
3849 O  O   . MET A 478 ? 0.76998 0.75504 0.45284 0.01448  0.09155  -0.05378 478 MET A O   
3850 C  CB  . MET A 478 ? 0.78672 0.75718 0.50494 0.02320  0.09250  -0.07103 478 MET A CB  
3851 C  CG  . MET A 478 ? 0.79473 0.75020 0.48690 0.01638  0.07998  -0.07803 478 MET A CG  
3852 S  SD  . MET A 478 ? 0.79011 0.72548 0.48013 0.01510  0.07163  -0.09140 478 MET A SD  
3853 C  CE  . MET A 478 ? 0.77371 0.71397 0.47534 0.00382  0.05144  -0.08652 478 MET A CE  
3854 N  N   . PRO A 479 ? 0.65597 0.65964 0.39296 0.01265  0.08565  -0.04319 479 PRO A N   
3855 C  CA  . PRO A 479 ? 0.65127 0.66025 0.38375 0.00572  0.07648  -0.03432 479 PRO A CA  
3856 C  C   . PRO A 479 ? 0.65868 0.67498 0.37799 0.00643  0.08616  -0.02631 479 PRO A C   
3857 O  O   . PRO A 479 ? 0.66399 0.67735 0.36307 0.00211  0.08046  -0.02311 479 PRO A O   
3858 C  CB  . PRO A 479 ? 0.63077 0.65038 0.39536 0.00289  0.06972  -0.02668 479 PRO A CB  
3859 C  CG  . PRO A 479 ? 0.61492 0.63060 0.39534 0.00632  0.07012  -0.03407 479 PRO A CG  
3860 C  CD  . PRO A 479 ? 0.62255 0.63347 0.39175 0.01369  0.08390  -0.04084 479 PRO A CD  
3861 N  N   . LEU A 480 ? 0.59142 0.61794 0.32224 0.01168  0.10066  -0.02230 480 LEU A N   
3862 C  CA  . LEU A 480 ? 0.60162 0.63642 0.32131 0.01216  0.11131  -0.01385 480 LEU A CA  
3863 C  C   . LEU A 480 ? 0.63021 0.65318 0.31280 0.01505  0.11769  -0.02133 480 LEU A C   
3864 O  O   . LEU A 480 ? 0.64127 0.66518 0.30357 0.01234  0.11931  -0.01536 480 LEU A O   
3865 C  CB  . LEU A 480 ? 0.59347 0.64364 0.33698 0.01705  0.12543  -0.00784 480 LEU A CB  
3866 C  CG  . LEU A 480 ? 0.57032 0.63497 0.34412 0.01212  0.12097  0.00441  480 LEU A CG  
3867 C  CD1 . LEU A 480 ? 0.55462 0.63486 0.35190 0.01670  0.13434  0.00965  480 LEU A CD1 
3868 C  CD2 . LEU A 480 ? 0.57418 0.64175 0.33799 0.00531  0.11657  0.01516  480 LEU A CD2 
3869 N  N   . ARG A 481 ? 0.94470 0.95514 0.61668 0.02051  0.12126  -0.03443 481 ARG A N   
3870 C  CA  . ARG A 481 ? 0.95169 0.95270 0.59646 0.02170  0.12318  -0.04300 481 ARG A CA  
3871 C  C   . ARG A 481 ? 0.95965 0.95088 0.58132 0.01468  0.10761  -0.04446 481 ARG A C   
3872 O  O   . ARG A 481 ? 0.97449 0.96581 0.57556 0.01338  0.10772  -0.04359 481 ARG A O   
3873 C  CB  . ARG A 481 ? 0.99996 0.98983 0.64496 0.02812  0.12695  -0.05669 481 ARG A CB  
3874 C  CG  . ARG A 481 ? 1.00482 1.00174 0.65497 0.03589  0.14383  -0.05817 481 ARG A CG  
3875 C  CD  . ARG A 481 ? 1.00560 0.98862 0.65315 0.04241  0.14620  -0.07192 481 ARG A CD  
3876 N  NE  . ARG A 481 ? 1.01032 0.99857 0.65898 0.05014  0.16176  -0.07400 481 ARG A NE  
3877 C  CZ  . ARG A 481 ? 1.01860 0.99346 0.65288 0.05545  0.16531  -0.08589 481 ARG A CZ  
3878 N  NH1 . ARG A 481 ? 1.02279 0.97803 0.64124 0.05333  0.15422  -0.09683 481 ARG A NH1 
3879 N  NH2 . ARG A 481 ? 1.02238 1.00349 0.65857 0.06280  0.18016  -0.08664 481 ARG A NH2 
3880 N  N   . THR A 482 ? 0.75535 0.73904 0.38131 0.00981  0.09378  -0.04632 482 THR A N   
3881 C  CA  . THR A 482 ? 0.76390 0.74099 0.37324 0.00268  0.07741  -0.04639 482 THR A CA  
3882 C  C   . THR A 482 ? 0.76034 0.74782 0.36698 -0.00147 0.07515  -0.03238 482 THR A C   
3883 O  O   . THR A 482 ? 0.77849 0.76366 0.36573 -0.00359 0.06823  -0.03069 482 THR A O   
3884 C  CB  . THR A 482 ? 0.74864 0.72049 0.37205 -0.00237 0.06291  -0.05020 482 THR A CB  
3885 O  OG1 . THR A 482 ? 0.75545 0.71340 0.37402 0.00046  0.06385  -0.06380 482 THR A OG1 
3886 C  CG2 . THR A 482 ? 0.74942 0.71797 0.35953 -0.01022 0.04581  -0.04791 482 THR A CG2 
3887 N  N   . LEU A 483 ? 0.69161 0.69245 0.32315 -0.00200 0.07962  -0.02161 483 LEU A N   
3888 C  CA  . LEU A 483 ? 0.69571 0.70594 0.32728 -0.00604 0.07799  -0.00754 483 LEU A CA  
3889 C  C   . LEU A 483 ? 0.70506 0.71769 0.31530 -0.00265 0.09000  -0.00380 483 LEU A C   
3890 O  O   . LEU A 483 ? 0.70157 0.71433 0.29829 -0.00500 0.08486  0.00418  483 LEU A O   
3891 C  CB  . LEU A 483 ? 0.67215 0.69685 0.34010 -0.00650 0.08012  0.00248  483 LEU A CB  
3892 C  CG  . LEU A 483 ? 0.65675 0.69097 0.32784 -0.01029 0.08124  0.01776  483 LEU A CG  
3893 C  CD1 . LEU A 483 ? 0.64944 0.68048 0.31921 -0.01618 0.06415  0.02328  483 LEU A CD1 
3894 C  CD2 . LEU A 483 ? 0.64484 0.69276 0.34797 -0.00951 0.08916  0.02571  483 LEU A CD2 
3895 N  N   . GLU A 484 ? 0.83233 0.84919 0.44525 0.00284  0.10482  -0.00934 484 GLU A N   
3896 C  CA  . GLU A 484 ? 0.84532 0.86883 0.44553 0.00349  0.11605  -0.00652 484 GLU A CA  
3897 C  C   . GLU A 484 ? 0.86351 0.87786 0.43376 0.00410  0.10967  -0.01398 484 GLU A C   
3898 O  O   . GLU A 484 ? 0.86402 0.88350 0.41899 0.00289  0.11432  -0.00882 484 GLU A O   
3899 C  CB  . GLU A 484 ? 0.88662 0.91542 0.50015 0.00933  0.13335  -0.01075 484 GLU A CB  
3900 C  CG  . GLU A 484 ? 0.89823 0.91757 0.49579 0.01522  0.13744  -0.02540 484 GLU A CG  
3901 C  CD  . GLU A 484 ? 0.89422 0.91771 0.51058 0.02278  0.15169  -0.03020 484 GLU A CD  
3902 O  OE1 . GLU A 484 ? 0.90027 0.91286 0.51596 0.02767  0.15022  -0.04234 484 GLU A OE1 
3903 O  OE2 . GLU A 484 ? 0.88353 0.92111 0.51651 0.02379  0.16379  -0.02138 484 GLU A OE2 
3904 N  N   . LYS A 485 ? 0.93150 0.93185 0.49313 0.00489  0.09894  -0.02576 485 LYS A N   
3905 C  CA  . LYS A 485 ? 0.93033 0.92029 0.46441 0.00424  0.09093  -0.03329 485 LYS A CA  
3906 C  C   . LYS A 485 ? 0.94429 0.93153 0.46901 -0.00103 0.07396  -0.02633 485 LYS A C   
3907 O  O   . LYS A 485 ? 0.95723 0.93670 0.46002 -0.00245 0.06531  -0.03134 485 LYS A O   
3908 C  CB  . LYS A 485 ? 0.97992 0.95530 0.51039 0.00638  0.08746  -0.04945 485 LYS A CB  
3909 C  CG  . LYS A 485 ? 0.96832 0.93276 0.49776 0.00125  0.06841  -0.05422 485 LYS A CG  
3910 C  CD  . LYS A 485 ? 0.98194 0.93131 0.50317 0.00272  0.06598  -0.07007 485 LYS A CD  
3911 C  CE  . LYS A 485 ? 1.00881 0.95013 0.50074 0.00205  0.06246  -0.07645 485 LYS A CE  
3912 N  NZ  . LYS A 485 ? 1.01750 0.94207 0.50113 0.00125  0.05564  -0.09119 485 LYS A NZ  
3913 N  N   . MET A 486 ? 0.79296 0.78601 0.33402 -0.00400 0.06920  -0.01455 486 MET A N   
3914 C  CA  . MET A 486 ? 0.78600 0.77649 0.32325 -0.00905 0.05327  -0.00660 486 MET A CA  
3915 C  C   . MET A 486 ? 0.79639 0.79233 0.32055 -0.00840 0.05705  0.00570  486 MET A C   
3916 O  O   . MET A 486 ? 0.80730 0.81191 0.34030 -0.00640 0.06993  0.01492  486 MET A O   
3917 C  CB  . MET A 486 ? 0.77352 0.76732 0.33628 -0.01335 0.04696  -0.00024 486 MET A CB  
3918 C  CG  . MET A 486 ? 0.75967 0.74743 0.32902 -0.01781 0.03050  -0.00733 486 MET A CG  
3919 S  SD  . MET A 486 ? 0.75235 0.74905 0.35038 -0.02379 0.02062  0.00291  486 MET A SD  
3920 C  CE  . MET A 486 ? 0.71706 0.71195 0.33591 -0.02342 0.02058  -0.00900 486 MET A CE  
3921 N  N   . PRO A 487 ? 0.67945 0.67058 0.18337 -0.01011 0.04625  0.00665  487 PRO A N   
3922 C  CA  . PRO A 487 ? 0.69883 0.69384 0.18927 -0.00931 0.04943  0.01896  487 PRO A CA  
3923 C  C   . PRO A 487 ? 0.67884 0.67591 0.18610 -0.01246 0.04607  0.03392  487 PRO A C   
3924 O  O   . PRO A 487 ? 0.65177 0.64872 0.17908 -0.01647 0.03699  0.03458  487 PRO A O   
3925 C  CB  . PRO A 487 ? 0.72598 0.71417 0.19307 -0.01115 0.03557  0.01501  487 PRO A CB  
3926 C  CG  . PRO A 487 ? 0.71085 0.69261 0.18762 -0.01483 0.02094  0.00561  487 PRO A CG  
3927 C  CD  . PRO A 487 ? 0.69040 0.67239 0.18335 -0.01301 0.03051  -0.00321 487 PRO A CD  
3928 N  N   . ASP A 488 ? 0.78243 0.78181 0.28162 -0.01125 0.05361  0.04604  488 ASP A N   
3929 C  CA  . ASP A 488 ? 0.78376 0.78431 0.29985 -0.01533 0.05298  0.06034  488 ASP A CA  
3930 C  C   . ASP A 488 ? 0.77061 0.76894 0.29315 -0.02006 0.03346  0.06458  488 ASP A C   
3931 O  O   . ASP A 488 ? 0.75561 0.75782 0.30164 -0.02392 0.02886  0.07112  488 ASP A O   
3932 C  CB  . ASP A 488 ? 0.79934 0.79940 0.30255 -0.01378 0.06444  0.07211  488 ASP A CB  
3933 C  CG  . ASP A 488 ? 0.81343 0.81659 0.32250 -0.01103 0.08508  0.07201  488 ASP A CG  
3934 O  OD1 . ASP A 488 ? 0.80902 0.81585 0.33700 -0.01121 0.08989  0.06547  488 ASP A OD1 
3935 O  OD2 . ASP A 488 ? 0.82366 0.82479 0.32044 -0.00975 0.09623  0.07810  488 ASP A OD2 
3936 N  N   . ALA A 489 ? 0.81774 0.81146 0.32115 -0.01959 0.02165  0.06103  489 ALA A N   
3937 C  CA  . ALA A 489 ? 0.80490 0.79759 0.31538 -0.02313 0.00318  0.06549  489 ALA A CA  
3938 C  C   . ALA A 489 ? 0.77473 0.76969 0.30780 -0.02583 -0.00604 0.05826  489 ALA A C   
3939 O  O   . ALA A 489 ? 0.75300 0.75072 0.30357 -0.02845 -0.01718 0.06475  489 ALA A O   
3940 C  CB  . ALA A 489 ? 0.81531 0.80374 0.30097 -0.02225 -0.00718 0.06270  489 ALA A CB  
3941 N  N   . GLU A 490 ? 0.75548 0.74933 0.28884 -0.02478 -0.00136 0.04504  490 GLU A N   
3942 C  CA  . GLU A 490 ? 0.74146 0.73725 0.29646 -0.02737 -0.00858 0.03845  490 GLU A CA  
3943 C  C   . GLU A 490 ? 0.73811 0.74093 0.31828 -0.02855 -0.00088 0.04446  490 GLU A C   
3944 O  O   . GLU A 490 ? 0.70924 0.71622 0.31072 -0.03119 -0.00964 0.04581  490 GLU A O   
3945 C  CB  . GLU A 490 ? 0.74111 0.73181 0.28803 -0.02598 -0.00604 0.02248  490 GLU A CB  
3946 C  CG  . GLU A 490 ? 0.73215 0.72280 0.29696 -0.02917 -0.01678 0.01484  490 GLU A CG  
3947 C  CD  . GLU A 490 ? 0.74802 0.73204 0.30693 -0.02773 -0.01189 -0.00045 490 GLU A CD  
3948 O  OE1 . GLU A 490 ? 0.76469 0.74362 0.30224 -0.02439 -0.00415 -0.00627 490 GLU A OE1 
3949 O  OE2 . GLU A 490 ? 0.73720 0.72110 0.31302 -0.02974 -0.01558 -0.00656 490 GLU A OE2 
3950 N  N   . ARG A 491 ? 0.83959 0.84505 0.41876 -0.02656 0.01537  0.04839  491 ARG A N   
3951 C  CA  . ARG A 491 ? 0.81884 0.83294 0.42315 -0.02832 0.02246  0.05528  491 ARG A CA  
3952 C  C   . ARG A 491 ? 0.81330 0.83021 0.43059 -0.03141 0.01323  0.06880  491 ARG A C   
3953 O  O   . ARG A 491 ? 0.78964 0.81169 0.42985 -0.03354 0.00740  0.07116  491 ARG A O   
3954 C  CB  . ARG A 491 ? 0.83807 0.85553 0.43944 -0.02578 0.04138  0.05820  491 ARG A CB  
3955 C  CG  . ARG A 491 ? 0.85545 0.87160 0.45042 -0.02132 0.05305  0.04548  491 ARG A CG  
3956 C  CD  . ARG A 491 ? 0.86122 0.88539 0.46691 -0.01946 0.07131  0.05042  491 ARG A CD  
3957 N  NE  . ARG A 491 ? 0.87160 0.89557 0.47621 -0.01418 0.08325  0.03894  491 ARG A NE  
3958 C  CZ  . ARG A 491 ? 0.87685 0.91089 0.50210 -0.01281 0.09611  0.03983  491 ARG A CZ  
3959 N  NH1 . ARG A 491 ? 0.84859 0.89519 0.49849 -0.01625 0.09800  0.05148  491 ARG A NH1 
3960 N  NH2 . ARG A 491 ? 0.88377 0.91538 0.50619 -0.00770 0.10679  0.02887  491 ARG A NH2 
3961 N  N   . GLU A 492 ? 0.68602 0.69883 0.28839 -0.03111 0.01194  0.07782  492 GLU A N   
3962 C  CA  . GLU A 492 ? 0.67251 0.68585 0.28605 -0.03325 0.00360  0.09085  492 GLU A CA  
3963 C  C   . GLU A 492 ? 0.65515 0.66797 0.27808 -0.03384 -0.01398 0.08910  492 GLU A C   
3964 O  O   . GLU A 492 ? 0.63951 0.65405 0.28020 -0.03485 -0.02076 0.09762  492 GLU A O   
3965 C  CB  . GLU A 492 ? 0.68118 0.68901 0.27421 -0.03240 0.00542  0.10003  492 GLU A CB  
3966 C  CG  . GLU A 492 ? 0.70897 0.71835 0.29879 -0.03257 0.02264  0.10617  492 GLU A CG  
3967 C  CD  . GLU A 492 ? 0.75824 0.76238 0.31806 -0.02922 0.03092  0.10309  492 GLU A CD  
3968 O  OE1 . GLU A 492 ? 0.75394 0.76025 0.31036 -0.02757 0.04658  0.09987  492 GLU A OE1 
3969 O  OE2 . GLU A 492 ? 0.77537 0.77371 0.31544 -0.02777 0.02186  0.10399  492 GLU A OE2 
3970 N  N   . ALA A 493 ? 0.62655 0.63688 0.23890 -0.03301 -0.02132 0.07814  493 ALA A N   
3971 C  CA  . ALA A 493 ? 0.61005 0.62136 0.23260 -0.03361 -0.03792 0.07655  493 ALA A CA  
3972 C  C   . ALA A 493 ? 0.59149 0.60875 0.24130 -0.03483 -0.04002 0.07453  493 ALA A C   
3973 O  O   . ALA A 493 ? 0.57305 0.59295 0.24029 -0.03469 -0.04889 0.08162  493 ALA A O   
3974 C  CB  . ALA A 493 ? 0.60983 0.61741 0.21549 -0.03334 -0.04482 0.06507  493 ALA A CB  
3975 N  N   . PHE A 494 ? 0.51035 0.52950 0.16410 -0.03538 -0.03175 0.06486  494 PHE A N   
3976 C  CA  . PHE A 494 ? 0.47845 0.50258 0.16101 -0.03501 -0.03284 0.06213  494 PHE A CA  
3977 C  C   . PHE A 494 ? 0.46232 0.48945 0.16485 -0.03417 -0.02593 0.07172  494 PHE A C   
3978 O  O   . PHE A 494 ? 0.43821 0.46761 0.16630 -0.03293 -0.02953 0.07210  494 PHE A O   
3979 C  CB  . PHE A 494 ? 0.46978 0.49319 0.15628 -0.03382 -0.02584 0.04801  494 PHE A CB  
3980 C  CG  . PHE A 494 ? 0.47578 0.49949 0.15726 -0.03217 -0.00887 0.04599  494 PHE A CG  
3981 C  CD1 . PHE A 494 ? 0.46609 0.49514 0.16812 -0.03111 0.00032  0.05209  494 PHE A CD1 
3982 C  CD2 . PHE A 494 ? 0.49659 0.51528 0.15346 -0.03153 -0.00221 0.03748  494 PHE A CD2 
3983 C  CE1 . PHE A 494 ? 0.47570 0.50739 0.17560 -0.02952 0.01565  0.05089  494 PHE A CE1 
3984 C  CE2 . PHE A 494 ? 0.50662 0.52679 0.16033 -0.02893 0.01413  0.03573  494 PHE A CE2 
3985 C  CZ  . PHE A 494 ? 0.49542 0.52329 0.17182 -0.02793 0.02304  0.04288  494 PHE A CZ  
3986 N  N   . ARG A 495 ? 0.53009 0.55693 0.22104 -0.03517 -0.01609 0.07948  495 ARG A N   
3987 C  CA  . ARG A 495 ? 0.53279 0.56143 0.24120 -0.03581 -0.01139 0.09009  495 ARG A CA  
3988 C  C   . ARG A 495 ? 0.51605 0.54172 0.23185 -0.03592 -0.02397 0.09976  495 ARG A C   
3989 O  O   . ARG A 495 ? 0.50624 0.53201 0.24607 -0.03487 -0.02668 0.10161  495 ARG A O   
3990 C  CB  . ARG A 495 ? 0.54675 0.57622 0.23963 -0.03771 0.00098  0.09781  495 ARG A CB  
3991 C  CG  . ARG A 495 ? 0.55608 0.59059 0.25136 -0.03657 0.01618  0.09067  495 ARG A CG  
3992 C  CD  . ARG A 495 ? 0.57042 0.60750 0.25393 -0.03830 0.02900  0.09989  495 ARG A CD  
3993 N  NE  . ARG A 495 ? 0.58545 0.62731 0.26396 -0.03593 0.04358  0.09229  495 ARG A NE  
3994 C  CZ  . ARG A 495 ? 0.61374 0.65184 0.27077 -0.03365 0.05272  0.09112  495 ARG A CZ  
3995 N  NH1 . ARG A 495 ? 0.61309 0.64315 0.25050 -0.03387 0.04881  0.09724  495 ARG A NH1 
3996 N  NH2 . ARG A 495 ? 0.60672 0.64883 0.26177 -0.03044 0.06634  0.08374  495 ARG A NH2 
3997 N  N   . LYS A 496 ? 0.55385 0.57584 0.24967 -0.03627 -0.03170 0.10531  496 LYS A N   
3998 C  CA  . LYS A 496 ? 0.54701 0.56558 0.25115 -0.03460 -0.04369 0.11387  496 LYS A CA  
3999 C  C   . LYS A 496 ? 0.52614 0.54831 0.24914 -0.03292 -0.05414 0.10899  496 LYS A C   
4000 O  O   . LYS A 496 ? 0.51590 0.53645 0.25754 -0.03079 -0.05904 0.11489  496 LYS A O   
4001 C  CB  . LYS A 496 ? 0.59629 0.61026 0.27993 -0.03306 -0.05017 0.11653  496 LYS A CB  
4002 C  CG  . LYS A 496 ? 0.61288 0.62172 0.28130 -0.03381 -0.04210 0.12572  496 LYS A CG  
4003 C  CD  . LYS A 496 ? 0.62335 0.62774 0.27114 -0.03188 -0.04978 0.12855  496 LYS A CD  
4004 C  CE  . LYS A 496 ? 0.64355 0.64297 0.27219 -0.03264 -0.04005 0.13610  496 LYS A CE  
4005 N  NZ  . LYS A 496 ? 0.67345 0.67081 0.27428 -0.03143 -0.03997 0.13063  496 LYS A NZ  
4006 N  N   . GLN A 497 ? 0.59563 0.62115 0.31653 -0.03278 -0.05662 0.09684  497 GLN A N   
4007 C  CA  . GLN A 497 ? 0.57762 0.60680 0.31992 -0.03055 -0.06484 0.09066  497 GLN A CA  
4008 C  C   . GLN A 497 ? 0.56520 0.59506 0.33392 -0.02874 -0.05801 0.08844  497 GLN A C   
4009 O  O   . GLN A 497 ? 0.54848 0.57912 0.33685 -0.02600 -0.06404 0.09032  497 GLN A O   
4010 C  CB  . GLN A 497 ? 0.57293 0.60445 0.30685 -0.03198 -0.06760 0.07803  497 GLN A CB  
4011 C  CG  . GLN A 497 ? 0.55578 0.59216 0.31148 -0.03052 -0.07571 0.07185  497 GLN A CG  
4012 C  CD  . GLN A 497 ? 0.55533 0.59539 0.31092 -0.03010 -0.09104 0.07715  497 GLN A CD  
4013 O  OE1 . GLN A 497 ? 0.57324 0.61060 0.31263 -0.03006 -0.09542 0.08288  497 GLN A OE1 
4014 N  NE2 . GLN A 497 ? 0.54482 0.59081 0.32263 -0.02830 -0.09764 0.07418  497 GLN A NE2 
4015 N  N   . ALA A 498 ? 0.44688 0.47666 0.21615 -0.02998 -0.04541 0.08460  498 ALA A N   
4016 C  CA  . ALA A 498 ? 0.43959 0.47028 0.23274 -0.02883 -0.03957 0.08202  498 ALA A CA  
4017 C  C   . ALA A 498 ? 0.43720 0.46369 0.24148 -0.02850 -0.04028 0.09300  498 ALA A C   
4018 O  O   . ALA A 498 ? 0.43083 0.45621 0.25531 -0.02650 -0.04224 0.09201  498 ALA A O   
4019 C  CB  . ALA A 498 ? 0.44747 0.48031 0.23882 -0.03009 -0.02647 0.07625  498 ALA A CB  
4020 N  N   . ARG A 499 ? 0.50177 0.52472 0.29214 -0.03058 -0.03849 0.10350  499 ARG A N   
4021 C  CA  . ARG A 499 ? 0.49851 0.51505 0.29788 -0.03068 -0.04026 0.11450  499 ARG A CA  
4022 C  C   . ARG A 499 ? 0.48625 0.49969 0.29432 -0.02649 -0.05249 0.11723  499 ARG A C   
4023 O  O   . ARG A 499 ? 0.48250 0.49052 0.30676 -0.02458 -0.05417 0.12040  499 ARG A O   
4024 C  CB  . ARG A 499 ? 0.51324 0.52620 0.29424 -0.03401 -0.03675 0.12613  499 ARG A CB  
4025 C  CG  . ARG A 499 ? 0.53588 0.55377 0.30405 -0.03735 -0.02445 0.12394  499 ARG A CG  
4026 C  CD  . ARG A 499 ? 0.56020 0.57487 0.31981 -0.04141 -0.01803 0.13692  499 ARG A CD  
4027 N  NE  . ARG A 499 ? 0.58004 0.59031 0.31754 -0.04116 -0.02281 0.14417  499 ARG A NE  
4028 C  CZ  . ARG A 499 ? 0.59077 0.60292 0.30701 -0.04064 -0.01911 0.14013  499 ARG A CZ  
4029 N  NH1 . ARG A 499 ? 0.58745 0.60643 0.29796 -0.04116 -0.01062 0.13084  499 ARG A NH1 
4030 N  NH2 . ARG A 499 ? 0.59637 0.60249 0.29611 -0.03911 -0.02396 0.14539  499 ARG A NH2 
4031 N  N   . ALA A 500 ? 0.43201 0.44886 0.22955 -0.02490 -0.06122 0.11598  500 ALA A N   
4032 C  CA  . ALA A 500 ? 0.41965 0.43616 0.22710 -0.02034 -0.07290 0.11914  500 ALA A CA  
4033 C  C   . ALA A 500 ? 0.40253 0.42263 0.23284 -0.01715 -0.07365 0.11014  500 ALA A C   
4034 O  O   . ALA A 500 ? 0.39088 0.40787 0.23639 -0.01279 -0.07811 0.11356  500 ALA A O   
4035 C  CB  . ALA A 500 ? 0.41854 0.43979 0.20991 -0.02028 -0.08267 0.11999  500 ALA A CB  
4036 N  N   . LEU A 501 ? 0.35588 0.38175 0.18814 -0.01891 -0.06896 0.09878  501 LEU A N   
4037 C  CA  . LEU A 501 ? 0.33331 0.36245 0.18610 -0.01640 -0.06880 0.09052  501 LEU A CA  
4038 C  C   . LEU A 501 ? 0.32208 0.34504 0.18961 -0.01542 -0.06261 0.09192  501 LEU A C   
4039 O  O   . LEU A 501 ? 0.31170 0.33397 0.19592 -0.01167 -0.06491 0.08981  501 LEU A O   
4040 C  CB  . LEU A 501 ? 0.32588 0.36062 0.17591 -0.01891 -0.06458 0.07881  501 LEU A CB  
4041 C  CG  . LEU A 501 ? 0.33640 0.37645 0.17439 -0.02032 -0.07202 0.07462  501 LEU A CG  
4042 C  CD1 . LEU A 501 ? 0.33373 0.37529 0.16522 -0.02321 -0.06579 0.06341  501 LEU A CD1 
4043 C  CD2 . LEU A 501 ? 0.32820 0.37399 0.18122 -0.01728 -0.08220 0.07431  501 LEU A CD2 
4044 N  N   . ARG A 502 ? 0.45891 0.47749 0.32029 -0.01898 -0.05477 0.09554  502 ARG A N   
4045 C  CA  . ARG A 502 ? 0.46284 0.47491 0.33723 -0.01933 -0.05004 0.09746  502 ARG A CA  
4046 C  C   . ARG A 502 ? 0.46512 0.46772 0.34446 -0.01616 -0.05607 0.10633  502 ARG A C   
4047 O  O   . ARG A 502 ? 0.46497 0.46150 0.35808 -0.01409 -0.05576 0.10510  502 ARG A O   
4048 C  CB  . ARG A 502 ? 0.47722 0.48865 0.34479 -0.02464 -0.04073 0.10039  502 ARG A CB  
4049 C  CG  . ARG A 502 ? 0.48637 0.50585 0.35427 -0.02643 -0.03307 0.09086  502 ARG A CG  
4050 C  CD  . ARG A 502 ? 0.49384 0.51378 0.36475 -0.03065 -0.02346 0.09350  502 ARG A CD  
4051 N  NE  . ARG A 502 ? 0.52043 0.54831 0.38356 -0.03202 -0.01530 0.08808  502 ARG A NE  
4052 C  CZ  . ARG A 502 ? 0.52342 0.55374 0.36736 -0.03274 -0.01318 0.08933  502 ARG A CZ  
4053 N  NH1 . ARG A 502 ? 0.52366 0.54993 0.35366 -0.03293 -0.01892 0.09685  502 ARG A NH1 
4054 N  NH2 . ARG A 502 ? 0.54769 0.58397 0.38539 -0.03291 -0.00503 0.08294  502 ARG A NH2 
4055 N  N   . VAL A 503 ? 0.40355 0.40373 0.27087 -0.01543 -0.06166 0.11526  503 VAL A N   
4056 C  CA  . VAL A 503 ? 0.40434 0.39492 0.27643 -0.01114 -0.06808 0.12388  503 VAL A CA  
4057 C  C   . VAL A 503 ? 0.39887 0.39351 0.28400 -0.00423 -0.07505 0.11963  503 VAL A C   
4058 O  O   . VAL A 503 ? 0.39301 0.38011 0.29064 0.00047  -0.07649 0.12066  503 VAL A O   
4059 C  CB  . VAL A 503 ? 0.41978 0.40679 0.27486 -0.01214 -0.07234 0.13560  503 VAL A CB  
4060 C  CG1 . VAL A 503 ? 0.42013 0.39596 0.28069 -0.00685 -0.07913 0.14494  503 VAL A CG1 
4061 C  CG2 . VAL A 503 ? 0.43367 0.41767 0.27649 -0.01914 -0.06415 0.14048  503 VAL A CG2 
4062 N  N   . LYS A 504 ? 0.42022 0.42666 0.30252 -0.00365 -0.07926 0.11476  504 LYS A N   
4063 C  CA  . LYS A 504 ? 0.40855 0.42168 0.30440 0.00225  -0.08600 0.11167  504 LYS A CA  
4064 C  C   . LYS A 504 ? 0.39914 0.41172 0.31262 0.00469  -0.08126 0.10351  504 LYS A C   
4065 O  O   . LYS A 504 ? 0.39465 0.40721 0.32168 0.01112  -0.08471 0.10393  504 LYS A O   
4066 C  CB  . LYS A 504 ? 0.44455 0.47053 0.33384 0.00017  -0.09091 0.10693  504 LYS A CB  
4067 C  CG  . LYS A 504 ? 0.43396 0.46948 0.33733 0.00531  -0.09921 0.10574  504 LYS A CG  
4068 C  CD  . LYS A 504 ? 0.43315 0.47927 0.32615 0.00220  -0.10709 0.10471  504 LYS A CD  
4069 C  CE  . LYS A 504 ? 0.42585 0.48212 0.33270 0.00736  -0.11754 0.10801  504 LYS A CE  
4070 N  NZ  . LYS A 504 ? 0.43620 0.49169 0.33363 0.00958  -0.12683 0.11973  504 LYS A NZ  
4071 N  N   . MET A 505 ? 0.37316 0.38540 0.28653 0.00011  -0.07319 0.09646  505 MET A N   
4072 C  CA  . MET A 505 ? 0.36832 0.38053 0.29620 0.00170  -0.06885 0.08839  505 MET A CA  
4073 C  C   . MET A 505 ? 0.36622 0.36523 0.29878 0.00206  -0.06468 0.09072  505 MET A C   
4074 O  O   . MET A 505 ? 0.35602 0.35321 0.29861 0.00303  -0.06104 0.08436  505 MET A O   
4075 C  CB  . MET A 505 ? 0.35211 0.37173 0.27783 -0.00315 -0.06333 0.07925  505 MET A CB  
4076 C  CG  . MET A 505 ? 0.34795 0.37894 0.27203 -0.00328 -0.06802 0.07466  505 MET A CG  
4077 S  SD  . MET A 505 ? 0.34417 0.38125 0.26331 -0.00849 -0.06208 0.06397  505 MET A SD  
4078 C  CE  . MET A 505 ? 0.34189 0.38781 0.25201 -0.00967 -0.07093 0.06295  505 MET A CE  
4079 N  N   . GLY A 506 ? 0.40758 0.39664 0.33234 0.00083  -0.06551 0.09981  506 GLY A N   
4080 C  CA  . GLY A 506 ? 0.40727 0.38193 0.33558 0.00019  -0.06268 0.10247  506 GLY A CA  
4081 C  C   . GLY A 506 ? 0.41090 0.38513 0.33945 -0.00664 -0.05538 0.09829  506 GLY A C   
4082 O  O   . GLY A 506 ? 0.40989 0.37568 0.34584 -0.00691 -0.05326 0.09555  506 GLY A O   
4083 N  N   . VAL A 507 ? 0.30723 0.29038 0.22759 -0.01194 -0.05158 0.09780  507 VAL A N   
4084 C  CA  . VAL A 507 ? 0.30632 0.29198 0.22860 -0.01779 -0.04428 0.09420  507 VAL A CA  
4085 C  C   . VAL A 507 ? 0.31653 0.29505 0.23284 -0.02348 -0.04162 0.10346  507 VAL A C   
4086 O  O   . VAL A 507 ? 0.31402 0.28456 0.23691 -0.02667 -0.03979 0.10461  507 VAL A O   
4087 C  CB  . VAL A 507 ? 0.35119 0.35045 0.26895 -0.01950 -0.04039 0.08779  507 VAL A CB  
4088 C  CG1 . VAL A 507 ? 0.35570 0.35842 0.27540 -0.02490 -0.03237 0.08603  507 VAL A CG1 
4089 C  CG2 . VAL A 507 ? 0.33827 0.34370 0.26385 -0.01519 -0.04271 0.07859  507 VAL A CG2 
4090 N  N   . SER A 508 ? 0.50043 0.48160 0.40374 -0.02532 -0.04159 0.11034  508 SER A N   
4091 C  CA  . SER A 508 ? 0.51159 0.48731 0.40841 -0.03126 -0.03831 0.12025  508 SER A CA  
4092 C  C   . SER A 508 ? 0.52498 0.50108 0.40556 -0.03107 -0.04079 0.12878  508 SER A C   
4093 O  O   . SER A 508 ? 0.52836 0.50984 0.40285 -0.02672 -0.04543 0.12630  508 SER A O   
4094 C  CB  . SER A 508 ? 0.51536 0.49993 0.41460 -0.03731 -0.02932 0.11781  508 SER A CB  
4095 O  OG  . SER A 508 ? 0.52870 0.52599 0.41996 -0.03650 -0.02547 0.11266  508 SER A OG  
4172 FE FE1 . SF4 D .   ? 0.67799 0.46402 0.41760 0.02479  0.01377  -0.02307 603 SF4 A FE1 
4173 FE FE2 . SF4 D .   ? 0.37286 0.32824 0.35964 -0.00051 -0.00107 0.03616  603 SF4 A FE2 
4174 FE FE3 . SF4 D .   ? 0.36444 0.32576 0.31710 -0.04928 -0.08143 0.00227  603 SF4 A FE3 
4175 FE FE4 . SF4 D .   ? 0.37052 0.35282 0.35895 -0.00603 -0.02737 0.01205  603 SF4 A FE4 
4176 S  S1  . SF4 D .   ? 0.26236 0.31098 0.36548 0.01639  -0.01441 0.02040  603 SF4 A S1  
4177 S  S2  . SF4 D .   ? 0.41197 0.31851 0.33040 0.03708  -0.03352 -0.03702 603 SF4 A S2  
4178 S  S3  . SF4 D .   ? 0.42619 0.38780 0.34040 -0.04573 0.00037  0.01893  603 SF4 A S3  
4179 S  S4  . SF4 D .   ? 0.45605 0.33247 0.41572 -0.05029 0.04065  0.01840  603 SF4 A S4  
# 
